CNRS Nantes University US2B US2B
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***    ***

elNémo ID: 2610201159422660167

Job options:

ID        	=	 2610201159422660167
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

ATOM      1  N   MET A   1      21.750  20.914  37.968  1.00 61.42           N  
ATOM      2  CA  MET A   1      21.639  22.389  37.752  1.00 49.36           C  
ATOM      3  C   MET A   1      22.878  23.084  38.341  1.00 45.47           C  
ATOM      4  O   MET A   1      23.162  22.986  39.526  1.00 37.92           O  
ATOM      5  CB  MET A   1      20.362  22.941  38.400  1.00 54.33           C  
ATOM      6  CG  MET A   1      20.325  24.459  38.511  1.00 57.47           C  
ATOM      7  SD  MET A   1      18.755  25.104  39.161  1.00 56.63           S  
ATOM      8  CE  MET A   1      17.774  25.218  37.666  1.00 55.67           C  
ATOM      9  N   LYS A   2      23.610  23.815  37.498  1.00 39.00           N  
ATOM     10  CA  LYS A   2      24.759  24.576  37.965  1.00 33.37           C  
ATOM     11  C   LYS A   2      24.250  25.772  38.778  1.00 24.61           C  
ATOM     12  O   LYS A   2      23.117  26.198  38.618  1.00 22.18           O  
ATOM     13  CB  LYS A   2      25.629  25.026  36.786  1.00 36.04           C  
ATOM     14  CG  LYS A   2      25.952  23.916  35.794  1.00 40.91           C  
ATOM     15  CD  LYS A   2      27.317  24.005  35.168  1.00 36.34           C  
ATOM     16  CE  LYS A   2      27.810  22.662  34.671  1.00 37.80           C  
ATOM     17  NZ  LYS A   2      29.188  22.406  35.152  1.00 43.40           N  
ATOM     18  N   LYS A   3      25.108  26.267  39.668  1.00 22.95           N  
ATOM     19  CA  LYS A   3      24.836  27.443  40.452  1.00 21.87           C  
ATOM     20  C   LYS A   3      24.877  28.680  39.539  1.00 23.57           C  
ATOM     21  O   LYS A   3      23.993  29.510  39.625  1.00 25.09           O  
ATOM     22  CB  LYS A   3      25.859  27.562  41.589  1.00 22.07           C  
ATOM     23  CG  LYS A   3      25.728  26.526  42.697  1.00 23.21           C  
ATOM     24  CD  LYS A   3      26.813  26.656  43.760  1.00 23.82           C  
ATOM     25  CE  LYS A   3      26.670  25.679  44.910  1.00 25.74           C  
ATOM     26  NZ  LYS A   3      27.767  25.858  45.894  1.00 26.14           N  
ATOM     27  N   VAL A   4      25.893  28.786  38.671  1.00 23.28           N  
ATOM     28  CA  VAL A   4      26.140  30.027  37.865  1.00 25.39           C  
ATOM     29  C   VAL A   4      26.617  29.710  36.438  1.00 28.54           C  
ATOM     30  O   VAL A   4      27.633  29.054  36.280  1.00 28.49           O  
ATOM     31  CB  VAL A   4      27.192  30.935  38.527  1.00 27.69           C  
ATOM     32  CG1 VAL A   4      27.393  32.187  37.685  1.00 28.41           C  
ATOM     33  CG2 VAL A   4      26.843  31.296  39.971  1.00 29.86           C  
ATOM     34  N   SER A   5      25.925  30.268  35.430  1.00 22.85           N  
ATOM     35  CA  SER A   5      26.426  30.402  34.052  1.00 23.65           C  
ATOM     36  C   SER A   5      26.997  31.812  33.860  1.00 26.08           C  
ATOM     37  O   SER A   5      26.250  32.785  33.932  1.00 22.31           O  
ATOM     38  CB  SER A   5      25.344  30.173  33.011  1.00 25.24           C  
ATOM     39  OG  SER A   5      24.589  28.998  33.240  1.00 27.63           O  
ATOM     40  N   VAL A   6      28.309  31.912  33.627  1.00 25.77           N  
ATOM     41  CA  VAL A   6      28.931  33.142  33.182  1.00 24.84           C  
ATOM     42  C   VAL A   6      28.723  33.255  31.664  1.00 27.28           C  
ATOM     43  O   VAL A   6      29.110  32.348  30.912  1.00 25.60           O  
ATOM     44  CB  VAL A   6      30.419  33.185  33.561  1.00 25.06           C  
ATOM     45  CG1 VAL A   6      31.076  34.472  33.083  1.00 27.87           C  
ATOM     46  CG2 VAL A   6      30.612  33.016  35.061  1.00 28.78           C  
ATOM     47  N   ILE A   7      28.071  34.336  31.225  1.00 23.33           N  
ATOM     48  CA  ILE A   7      27.783  34.561  29.810  1.00 24.73           C  
ATOM     49  C   ILE A   7      28.687  35.692  29.314  1.00 29.75           C  
ATOM     50  O   ILE A   7      28.674  36.801  29.877  1.00 28.18           O  
ATOM     51  CB  ILE A   7      26.289  34.849  29.586  1.00 22.96           C  
ATOM     52  CG1 ILE A   7      25.426  33.651  29.989  1.00 26.53           C  
ATOM     53  CG2 ILE A   7      26.025  35.280  28.149  1.00 25.11           C  
ATOM     54  CD1 ILE A   7      23.943  33.921  29.985  1.00 27.30           C  
ATOM     55  N   MET A   8      29.488  35.396  28.279  1.00 27.67           N  
ATOM     56  CA  MET A   8      30.537  36.285  27.808  1.00 25.61           C  
ATOM     57  C   MET A   8      30.519  36.350  26.278  1.00 33.82           C  
ATOM     58  O   MET A   8      31.007  35.440  25.609  1.00 28.71           O  
ATOM     59  CB  MET A   8      31.920  35.828  28.282  1.00 25.42           C  
ATOM     60  CG  MET A   8      33.043  36.671  27.676  1.00 27.37           C  
ATOM     61  SD  MET A   8      34.693  36.444  28.374  1.00 31.88           S  
ATOM     62  CE  MET A   8      35.204  34.950  27.527  1.00 32.61           C  
ATOM     63  N   PRO A   9      29.937  37.412  25.671  1.00 32.97           N  
ATOM     64  CA  PRO A   9      30.098  37.663  24.239  1.00 31.66           C  
ATOM     65  C   PRO A   9      31.549  38.052  23.936  1.00 30.26           C  
ATOM     66  O   PRO A   9      32.213  38.675  24.767  1.00 32.86           O  
ATOM     67  CB  PRO A   9      29.141  38.822  23.934  1.00 30.59           C  
ATOM     68  CG  PRO A   9      28.211  38.860  25.132  1.00 35.80           C  
ATOM     69  CD  PRO A   9      29.067  38.414  26.301  1.00 32.94           C  
ATOM     70  N   THR A  10      32.040  37.654  22.758  1.00 30.60           N  
ATOM     71  CA  THR A  10      33.352  38.082  22.274  1.00 30.00           C  
ATOM     72  C   THR A  10      33.201  38.705  20.882  1.00 30.67           C  
ATOM     73  O   THR A  10      32.227  38.433  20.137  1.00 25.50           O  
ATOM     74  CB  THR A  10      34.377  36.937  22.246  1.00 30.71           C  
ATOM     75  OG1 THR A  10      33.869  35.877  21.435  1.00 30.51           O  
ATOM     76  CG2 THR A  10      34.714  36.403  23.620  1.00 29.44           C  
ATOM     77  N   PHE A  11      34.165  39.572  20.565  1.00 31.56           N  
ATOM     78  CA  PHE A  11      34.347  40.101  19.221  1.00 37.14           C  
ATOM     79  C   PHE A  11      35.735  40.739  19.129  1.00 34.22           C  
ATOM     80  O   PHE A  11      35.993  41.752  19.771  1.00 34.29           O  
ATOM     81  CB  PHE A  11      33.264  41.114  18.842  1.00 37.61           C  
ATOM     82  CG  PHE A  11      33.415  41.640  17.437  1.00 41.96           C  
ATOM     83  CD1 PHE A  11      33.100  40.842  16.350  1.00 41.25           C  
ATOM     84  CD2 PHE A  11      33.908  42.915  17.199  1.00 41.67           C  
ATOM     85  CE1 PHE A  11      33.257  41.310  15.053  1.00 47.31           C  
ATOM     86  CE2 PHE A  11      34.060  43.385  15.902  1.00 44.71           C  
ATOM     87  CZ  PHE A  11      33.734  42.583  14.830  1.00 42.87           C  
ATOM     88  N   ASN A  12      36.616  40.107  18.346  1.00 29.70           N  
ATOM     89  CA  ASN A  12      37.923  40.633  17.977  1.00 32.08           C  
ATOM     90  C   ASN A  12      38.757  40.975  19.215  1.00 36.58           C  
ATOM     91  O   ASN A  12      39.484  41.958  19.200  1.00 35.49           O  
ATOM     92  CB  ASN A  12      37.794  41.849  17.056  1.00 33.86           C  
ATOM     93  CG  ASN A  12      37.286  41.476  15.678  1.00 40.86           C  
ATOM     94  OD1 ASN A  12      37.125  40.295  15.368  1.00 38.58           O  
ATOM     95  ND2 ASN A  12      37.035  42.471  14.843  1.00 45.53           N  
ATOM     96  N   ASN A  13      38.684  40.139  20.258  1.00 34.64           N  
ATOM     97  CA  ASN A  13      39.355  40.427  21.525  1.00 33.26           C  
ATOM     98  C   ASN A  13      40.849  40.093  21.433  1.00 35.64           C  
ATOM     99  O   ASN A  13      41.671  40.788  22.017  1.00 37.55           O  
ATOM    100  CB  ASN A  13      38.659  39.727  22.701  1.00 33.70           C  
ATOM    101  CG  ASN A  13      37.219  40.173  22.860  1.00 34.79           C  
ATOM    102  OD1 ASN A  13      36.307  39.560  22.309  1.00 34.06           O  
ATOM    103  ND2 ASN A  13      37.010  41.282  23.554  1.00 40.30           N  
ATOM    104  N   GLY A  14      41.203  39.017  20.725  1.00 35.14           N  
ATOM    105  CA  GLY A  14      42.606  38.609  20.598  1.00 38.73           C  
ATOM    106  C   GLY A  14      43.183  38.141  21.928  1.00 39.54           C  
ATOM    107  O   GLY A  14      42.447  37.672  22.793  1.00 39.13           O  
ATOM    108  N   GLU A  15      44.501  38.307  22.092  1.00 40.13           N  
ATOM    109  CA  GLU A  15      45.290  37.652  23.147  1.00 50.86           C  
ATOM    110  C   GLU A  15      44.876  38.131  24.546  1.00 46.64           C  
ATOM    111  O   GLU A  15      45.052  37.396  25.515  1.00 54.16           O  
ATOM    112  CB  GLU A  15      46.791  37.872  22.928  1.00 52.30           C  
ATOM    113  CG  GLU A  15      47.398  36.928  21.900  1.00 55.87           C  
ATOM    114  N   LYS A  16      44.331  39.348  24.646  1.00 48.75           N  
ATOM    115  CA  LYS A  16      43.883  39.924  25.925  1.00 50.29           C  
ATOM    116  C   LYS A  16      42.816  39.025  26.571  1.00 52.30           C  
ATOM    117  O   LYS A  16      42.580  39.100  27.781  1.00 47.07           O  
ATOM    118  CB  LYS A  16      43.341  41.344  25.719  1.00 49.86           C  
ATOM    119  N   LEU A  17      42.174  38.184  25.753  1.00 43.59           N  
ATOM    120  CA  LEU A  17      41.079  37.331  26.175  1.00 39.54           C  
ATOM    121  C   LEU A  17      41.577  36.181  27.066  1.00 38.90           C  
ATOM    122  O   LEU A  17      40.772  35.607  27.797  1.00 40.37           O  
ATOM    123  CB  LEU A  17      40.373  36.809  24.921  1.00 35.22           C  
ATOM    124  CG  LEU A  17      39.018  36.156  25.146  1.00 36.73           C  
ATOM    125  CD1 LEU A  17      38.075  37.112  25.860  1.00 37.18           C  
ATOM    126  CD2 LEU A  17      38.422  35.690  23.827  1.00 34.85           C  
ATOM    127  N   HIS A  18      42.877  35.849  27.014  1.00 34.15           N  
ATOM    128  CA  HIS A  18      43.464  34.816  27.901  1.00 41.23           C  
ATOM    129  C   HIS A  18      43.242  35.193  29.377  1.00 34.09           C  
ATOM    130  O   HIS A  18      42.879  34.351  30.189  1.00 28.73           O  
ATOM    131  CB  HIS A  18      44.958  34.583  27.600  1.00 40.82           C  
ATOM    132  CG  HIS A  18      45.226  33.637  26.472  1.00 54.11           C  
ATOM    133  ND1 HIS A  18      45.020  32.276  26.575  1.00 61.11           N  
ATOM    134  CD2 HIS A  18      45.705  33.834  25.223  1.00 53.00           C  
ATOM    135  N   ARG A  19      43.461  36.466  29.721  1.00 44.39           N  
ANISOU  135  N   ARG A  19     6501   4813   5550    797   2034    458       N  
ATOM    136  CA  ARG A  19      43.432  36.901  31.125  1.00 42.37           C  
ANISOU  136  CA  ARG A  19     6133   4550   5414    668   1916    417       C  
ATOM    137  C   ARG A  19      42.001  36.834  31.666  1.00 35.45           C  
ANISOU  137  C   ARG A  19     5330   3706   4431    605   1781    304       C  
ATOM    138  O   ARG A  19      41.793  36.432  32.809  1.00 33.42           O  
ANISOU  138  O   ARG A  19     5038   3457   4200    530   1674    242       O  
ATOM    139  CB  ARG A  19      44.015  38.305  31.297  1.00 45.83           C  
ANISOU  139  CB  ARG A  19     6447   4949   6015    627   1954    496       C  
ATOM    140  CG  ARG A  19      44.642  38.525  32.666  1.00 50.47           C  
ANISOU  140  CG  ARG A  19     6898   5507   6770    528   1859    483       C  
ATOM    141  CD  ARG A  19      45.793  39.516  32.636  1.00 53.22           C  
ANISOU  141  CD  ARG A  19     7100   5793   7326    519   1927    593       C  
ATOM    142  NE  ARG A  19      45.309  40.842  32.312  1.00 55.05           N  
ANISOU  142  NE  ARG A  19     7324   6011   7581    502   1941    618       N  
ATOM    143  CZ  ARG A  19      45.147  41.847  33.176  1.00 50.33           C  
ANISOU  143  CZ  ARG A  19     6651   5384   7087    413   1840    592       C  
ATOM    144  NH1 ARG A  19      45.392  41.692  34.469  1.00 47.41           N  
ANISOU  144  NH1 ARG A  19     6217   4997   6799    337   1707    534       N  
ATOM    145  NH2 ARG A  19      44.751  43.017  32.723  1.00 45.95           N  
ANISOU  145  NH2 ARG A  19     6094   4815   6550    410   1872    625       N  
ATOM    146  N   THR A  20      41.033  37.218  30.826  1.00 33.27           N  
ANISOU  146  N   THR A  20     5156   3446   4039    644   1792    286       N  
ATOM    147  CA  THR A  20      39.606  37.150  31.137  1.00 31.05           C  
ANISOU  147  CA  THR A  20     4948   3189   3658    599   1677    191       C  
ATOM    148  C   THR A  20      39.188  35.703  31.396  1.00 29.40           C  
ANISOU  148  C   THR A  20     4805   2995   3367    605   1607    117       C  
ATOM    149  O   THR A  20      38.622  35.403  32.463  1.00 28.24           O  
ANISOU  149  O   THR A  20     4634   2859   3235    529   1502     55       O  
ATOM    150  CB  THR A  20      38.749  37.747  30.009  1.00 31.63           C  
ANISOU  150  CB  THR A  20     5124   3269   3623    657   1709    193       C  
ATOM    151  OG1 THR A  20      39.040  39.144  29.879  1.00 30.46           O  
ANISOU  151  OG1 THR A  20     4909   3105   3558    640   1767    260       O  
ATOM    152  CG2 THR A  20      37.269  37.567  30.246  1.00 30.51           C  
ANISOU  152  CG2 THR A  20     5056   3146   3388    617   1590    100       C  
ATOM    153  N   ILE A  21      39.440  34.818  30.422  1.00 28.69           N  
ANISOU  153  N   ILE A  21     4802   2903   3192    704   1665    126       N  
ATOM    154  CA  ILE A  21      39.017  33.419  30.515  1.00 29.15           C  
ANISOU  154  CA  ILE A  21     4933   2968   3174    721   1596     56       C  
ATOM    155  C   ILE A  21      39.681  32.792  31.745  1.00 29.31           C  
ANISOU  155  C   ILE A  21     4855   2988   3291    654   1558     48       C  
ATOM    156  O   ILE A  21      39.014  32.151  32.565  1.00 28.71           O  
ANISOU  156  O   ILE A  21     4782   2920   3204    598   1458    -17       O  
ATOM    157  CB  ILE A  21      39.313  32.608  29.241  1.00 28.87           C  
ANISOU  157  CB  ILE A  21     5013   2922   3032    852   1666     69       C  
ATOM    158  CG1 ILE A  21      38.560  33.157  28.026  1.00 30.04           C  
ANISOU  158  CG1 ILE A  21     5280   3067   3065    931   1686     66       C  
ATOM    159  CG2 ILE A  21      38.961  31.149  29.466  1.00 29.12           C  
ANISOU  159  CG2 ILE A  21     5104   2951   3010    859   1583     -4       C  
ATOM    160  CD1 ILE A  21      38.998  32.589  26.689  1.00 33.10           C  
ANISOU  160  CD1 ILE A  21     5794   3441   3341   1085   1775     94       C  
ATOM    161  N   SER A  22      40.986  33.020  31.881  1.00 30.45           N  
ANISOU  161  N   SER A  22     4908   3120   3538    663   1640    122       N  
ATOM    162  CA  SER A  22      41.761  32.520  32.999  1.00 32.21           C  
ANISOU  162  CA  SER A  22     5035   3340   3864    608   1606    123       C  
ATOM    163  C   SER A  22      41.155  32.963  34.338  1.00 29.81           C  
ANISOU  163  C   SER A  22     4675   3043   3609    502   1490     71       C  
ATOM    164  O   SER A  22      41.114  32.172  35.288  1.00 28.50           O  
ANISOU  164  O   SER A  22     4491   2884   3455    464   1419     28       O  
ATOM    165  CB  SER A  22      43.188  32.961  32.881  1.00 37.52           C  
ANISOU  165  CB  SER A  22     5606   3986   4662    630   1706    219       C  
ATOM    166  OG  SER A  22      43.948  32.454  33.965  1.00 46.60           O  
ANISOU  166  OG  SER A  22     6664   5127   5913    581   1660    215       O  
ATOM    167  N   SER A  23      40.687  34.224  34.426  1.00 29.46           N  
ANISOU  167  N   SER A  23     4608   2997   3588    462   1475     77       N  
ATOM    168  CA  SER A  23      40.106  34.737  35.700  1.00 29.60           C  
ANISOU  168  CA  SER A  23     4583   3019   3644    374   1369     31       C  
ATOM    169  C   SER A  23      38.847  33.939  36.096  1.00 29.60           C  
ANISOU  169  C   SER A  23     4657   3041   3547    356   1286    -45       C  
ATOM    170  O   SER A  23      38.539  33.830  37.280  1.00 29.52           O  
ANISOU  170  O   SER A  23     4619   3035   3560    303   1208    -81       O  
ATOM    171  CB  SER A  23      39.832  36.244  35.635  1.00 29.38           C  
ANISOU  171  CB  SER A  23     4523   2980   3656    343   1372     53       C  
ATOM    172  OG  SER A  23      38.633  36.527  34.925  1.00 29.44           O  
ANISOU  172  OG  SER A  23     4621   3006   3559    360   1369     27       O  
ATOM    173  N   VAL A  24      38.100  33.456  35.093  1.00 28.81           N  
ANISOU  173  N   VAL A  24     4653   2948   3344    405   1301    -66       N  
ATOM    174  CA  VAL A  24      36.859  32.734  35.252  1.00 29.97           C  
ANISOU  174  CA  VAL A  24     4867   3102   3418    394   1224   -129       C  
ATOM    175  C   VAL A  24      37.144  31.263  35.590  1.00 31.54           C  
ANISOU  175  C   VAL A  24     5075   3297   3609    409   1201   -153       C  
ATOM    176  O   VAL A  24      36.442  30.665  36.417  1.00 31.31           O  
ANISOU  176  O   VAL A  24     5046   3270   3578    371   1130   -193       O  
ATOM    177  CB  VAL A  24      35.976  32.833  33.994  1.00 30.11           C  
ANISOU  177  CB  VAL A  24     4982   3115   3340    445   1231   -145       C  
ATOM    178  CG1 VAL A  24      34.676  32.070  34.162  1.00 31.29           C  
ANISOU  178  CG1 VAL A  24     5187   3259   3442    430   1139   -207       C  
ATOM    179  CG2 VAL A  24      35.686  34.268  33.596  1.00 31.73           C  
ANISOU  179  CG2 VAL A  24     5182   3324   3548    436   1259   -118       C  
ATOM    180  N   LEU A  25      38.138  30.658  34.926  1.00 32.40           N  
ANISOU  180  N   LEU A  25     5195   3399   3714    470   1269   -124       N  
ATOM    181  CA  LEU A  25      38.438  29.243  35.150  1.00 33.03           C  
ANISOU  181  CA  LEU A  25     5290   3473   3784    490   1251   -146       C  
ATOM    182  C   LEU A  25      39.133  29.060  36.502  1.00 34.63           C  
ANISOU  182  C   LEU A  25     5399   3682   4075    436   1226   -138       C  
ATOM    183  O   LEU A  25      39.103  27.973  37.039  1.00 35.74           O  
ANISOU  183  O   LEU A  25     5543   3820   4213    432   1189   -164       O  
ATOM    184  CB  LEU A  25      39.291  28.698  34.000  1.00 33.99           C  
ANISOU  184  CB  LEU A  25     5461   3585   3867    584   1337   -114       C  
ATOM    185  CG  LEU A  25      38.605  28.764  32.636  1.00 37.30           C  
ANISOU  185  CG  LEU A  25     5997   3994   4179    659   1352   -130       C  
ATOM    186  CD1 LEU A  25      39.447  28.105  31.558  1.00 41.28           C  
ANISOU  186  CD1 LEU A  25     6569   4486   4630    769   1438   -100       C  
ATOM    187  CD2 LEU A  25      37.207  28.167  32.679  1.00 37.14           C  
ANISOU  187  CD2 LEU A  25     6045   3962   4102    639   1242   -205       C  
ATOM    188  N   ASN A  26      39.688  30.130  37.079  1.00 33.51           N  
ANISOU  188  N   ASN A  26     5178   3541   4013    396   1235   -105       N  
ATOM    189  CA  ASN A  26      40.414  30.005  38.346  1.00 35.88           C  
ANISOU  189  CA  ASN A  26     5397   3839   4397    355   1198   -100       C  
ATOM    190  C   ASN A  26      39.584  30.570  39.510  1.00 33.72           C  
ANISOU  190  C   ASN A  26     5110   3572   4128    296   1113   -136       C  
ATOM    191  O   ASN A  26      40.122  31.041  40.484  1.00 36.66           O  
ANISOU  191  O   ASN A  26     5421   3937   4569    265   1077   -130       O  
ATOM    192  CB  ASN A  26      41.798  30.644  38.243  1.00 35.98           C  
ANISOU  192  CB  ASN A  26     5325   3833   4513    363   1255    -38       C  
ATOM    193  CG  ASN A  26      42.699  29.828  37.343  1.00 42.70           C  
ANISOU  193  CG  ASN A  26     6184   4675   5362    431   1342      1       C  
ATOM    194  OD1 ASN A  26      42.890  28.632  37.569  1.00 46.21           O  
ANISOU  194  OD1 ASN A  26     6648   5124   5786    449   1330    -18       O  
ATOM    195  ND2 ASN A  26      43.204  30.447  36.290  1.00 48.14           N  
ANISOU  195  ND2 ASN A  26     6868   5353   6069    477   1437     62       N  
ATOM    196  N   GLN A  27      38.263  30.447  39.431  1.00 32.42           N  
ANISOU  196  N   GLN A  27     5007   3417   3892    287   1079   -172       N  
ATOM    197  CA  GLN A  27      37.382  30.801  40.543  1.00 29.16           C  
ANISOU  197  CA  GLN A  27     4591   3010   3475    245   1011   -199       C  
ATOM    198  C   GLN A  27      37.594  29.854  41.737  1.00 29.99           C  
ANISOU  198  C   GLN A  27     4679   3118   3598    239    969   -213       C  
ATOM    199  O   GLN A  27      37.889  28.678  41.554  1.00 29.78           O  
ANISOU  199  O   GLN A  27     4663   3088   3561    263    982   -216       O  
ATOM    200  CB  GLN A  27      35.933  30.742  40.064  1.00 27.85           C  
ANISOU  200  CB  GLN A  27     4489   2848   3245    243    993   -223       C  
ATOM    201  CG  GLN A  27      35.602  31.896  39.121  1.00 28.20           C  
ANISOU  201  CG  GLN A  27     4552   2893   3270    246   1021   -211       C  
ATOM    202  CD  GLN A  27      35.654  33.217  39.854  1.00 27.38           C  
ANISOU  202  CD  GLN A  27     4404   2791   3206    208   1003   -201       C  
ATOM    203  OE1 GLN A  27      34.935  33.434  40.842  1.00 26.45           O  
ANISOU  203  OE1 GLN A  27     4286   2677   3085    182    954   -219       O  
ATOM    204  NE2 GLN A  27      36.561  34.079  39.418  1.00 25.63           N  
ANISOU  204  NE2 GLN A  27     4144   2561   3032    212   1045   -167       N  
ATOM    205  N   THR A  28      37.388  30.366  42.959  1.00 27.77           N  
ANISOU  205  N   THR A  28     4379   2837   3332    215    918   -222       N  
ATOM    206  CA  THR A  28      37.326  29.523  44.185  1.00 27.48           C  
ANISOU  206  CA  THR A  28     4343   2803   3292    221    878   -235       C  
ATOM    207  C   THR A  28      36.150  28.549  44.110  1.00 27.67           C  
ANISOU  207  C   THR A  28     4411   2829   3270    229    878   -245       C  
ATOM    208  O   THR A  28      36.217  27.438  44.643  1.00 28.96           O  
ANISOU  208  O   THR A  28     4577   2989   3435    244    870   -246       O  
ATOM    209  CB  THR A  28      37.192  30.376  45.454  1.00 27.24           C  
ANISOU  209  CB  THR A  28     4307   2771   3269    212    824   -243       C  
ATOM    210  OG1 THR A  28      36.053  31.223  45.280  1.00 25.33           O  
ANISOU  210  OG1 THR A  28     4095   2534   2992    198    823   -248       O  
ATOM    211  CG2 THR A  28      38.435  31.189  45.736  1.00 26.90           C  
ANISOU  211  CG2 THR A  28     4213   2712   3295    205    797   -238       C  
ATOM    212  N   MET A  29      35.048  28.956  43.470  1.00 26.48           N  
ANISOU  212  N   MET A  29     4292   2677   3090    218    883   -250       N  
ATOM    213  CA  MET A  29      33.916  28.040  43.303  1.00 25.27           C  
ANISOU  213  CA  MET A  29     4170   2512   2919    223    873   -257       C  
ATOM    214  C   MET A  29      34.420  26.775  42.579  1.00 24.66           C  
ANISOU  214  C   MET A  29     4104   2422   2844    247    886   -265       C  
ATOM    215  O   MET A  29      35.264  26.858  41.649  1.00 23.74           O  
ANISOU  215  O   MET A  29     3992   2308   2720    264    918   -265       O  
ATOM    216  CB  MET A  29      32.778  28.695  42.505  1.00 23.32           C  
ANISOU  216  CB  MET A  29     3951   2258   2651    211    868   -262       C  
ATOM    217  CG  MET A  29      31.534  27.858  42.423  1.00 24.26           C  
ANISOU  217  CG  MET A  29     4087   2352   2778    211    843   -265       C  
ATOM    218  SD  MET A  29      30.120  28.589  41.528  1.00 25.92           S  
ANISOU  218  SD  MET A  29     4325   2544   2977    197    822   -272       S  
ATOM    219  CE  MET A  29      29.373  29.572  42.830  1.00 25.90           C  
ANISOU  219  CE  MET A  29     4298   2555   2984    178    824   -244       C  
ATOM    220  N   LYS A  30      33.897  25.607  42.982  1.00 22.64           N  
ANISOU  220  N   LYS A  30     3852   2148   2599    254    868   -266       N  
ATOM    221  CA  LYS A  30      34.148  24.348  42.274  1.00 23.58           C  
ANISOU  221  CA  LYS A  30     3991   2246   2719    278    869   -280       C  
ATOM    222  C   LYS A  30      33.608  24.423  40.837  1.00 24.51           C  
ANISOU  222  C   LYS A  30     4159   2344   2808    292    860   -302       C  
ATOM    223  O   LYS A  30      32.457  24.820  40.590  1.00 24.22           O  
ANISOU  223  O   LYS A  30     4138   2293   2771    277    830   -309       O  
ATOM    224  CB  LYS A  30      33.448  23.171  42.957  1.00 24.76           C  
ANISOU  224  CB  LYS A  30     4133   2370   2902    279    843   -274       C  
ATOM    225  CG  LYS A  30      33.960  22.826  44.347  1.00 25.94           C  
ANISOU  225  CG  LYS A  30     4250   2535   3070    283    852   -251       C  
ATOM    226  CD  LYS A  30      33.240  21.617  44.922  1.00 27.03           C  
ANISOU  226  CD  LYS A  30     4380   2643   3247    291    840   -235       C  
ATOM    227  CE  LYS A  30      33.766  21.222  46.285  1.00 27.37           C  
ANISOU  227  CE  LYS A  30     4401   2700   3295    309    853   -210       C  
ATOM    228  NZ  LYS A  30      33.194  22.079  47.342  1.00 28.01           N  
ANISOU  228  NZ  LYS A  30     4481   2796   3364    311    858   -184       N  
ATOM    229  N   SER A  31      34.431  23.960  39.893  1.00 26.56           N  
ANISOU  229  N   SER A  31     4449   2599   3043    330    883   -313       N  
ATOM    230  CA  SER A  31      34.105  24.031  38.483  1.00 29.75           C  
ANISOU  230  CA  SER A  31     4918   2983   3400    365    877   -336       C  
ATOM    231  C   SER A  31      32.895  23.138  38.158  1.00 30.80           C  
ANISOU  231  C   SER A  31     5088   3068   3545    369    805   -368       C  
ATOM    232  O   SER A  31      32.280  23.304  37.130  1.00 33.98           O  
ANISOU  232  O   SER A  31     5548   3446   3914    392    773   -393       O  
ATOM    233  CB  SER A  31      35.331  23.708  37.647  1.00 31.36           C  
ANISOU  233  CB  SER A  31     5152   3192   3571    421    931   -332       C  
ATOM    234  OG  SER A  31      35.873  22.455  38.057  1.00 32.29           O  
ANISOU  234  OG  SER A  31     5258   3298   3711    435    928   -335       O  
ATOM    235  N   THR A  32      32.512  22.220  39.065  1.00 29.79           N  
ANISOU  235  N   THR A  32     4924   2921   3474    347    775   -362       N  
ATOM    236  CA  THR A  32      31.294  21.455  38.904  1.00 29.61           C  
ANISOU  236  CA  THR A  32     4912   2841   3497    341    703   -380       C  
ATOM    237  C   THR A  32      30.048  22.355  38.887  1.00 30.39           C  
ANISOU  237  C   THR A  32     5001   2929   3614    309    671   -374       C  
ATOM    238  O   THR A  32      29.038  21.995  38.254  1.00 30.06           O  
ANISOU  238  O   THR A  32     4984   2833   3602    313    600   -398       O  
ATOM    239  CB  THR A  32      31.107  20.434  40.036  1.00 32.62           C  
ANISOU  239  CB  THR A  32     5239   3203   3950    322    694   -357       C  
ATOM    240  OG1 THR A  32      32.368  19.796  40.266  1.00 34.79           O  
ANISOU  240  OG1 THR A  32     5512   3499   4206    345    734   -355       O  
ATOM    241  CG2 THR A  32      30.051  19.409  39.692  1.00 32.16           C  
ANISOU  241  CG2 THR A  32     5189   3070   3960    323    617   -374       C  
ATOM    242  N   ASP A  33      30.124  23.487  39.603  1.00 28.79           N  
ANISOU  242  N   ASP A  33     4763   2773   3402    280    716   -344       N  
ATOM    243  CA  ASP A  33      28.976  24.326  39.976  1.00 31.55           C  
ANISOU  243  CA  ASP A  33     5088   3119   3779    247    701   -325       C  
ATOM    244  C   ASP A  33      28.822  25.552  39.060  1.00 29.66           C  
ANISOU  244  C   ASP A  33     4887   2897   3486    250    703   -340       C  
ATOM    245  O   ASP A  33      27.816  26.278  39.169  1.00 25.40           O  
ANISOU  245  O   ASP A  33     4334   2350   2966    227    685   -329       O  
ATOM    246  CB  ASP A  33      29.112  24.809  41.421  1.00 34.04           C  
ANISOU  246  CB  ASP A  33     5351   3470   4110    225    745   -284       C  
ATOM    247  CG  ASP A  33      29.102  23.670  42.427  1.00 39.51           C  
ANISOU  247  CG  ASP A  33     6010   4146   4856    229    748   -258       C  
ATOM    248  OD1 ASP A  33      28.692  22.578  42.023  1.00 32.88           O  
ANISOU  248  OD1 ASP A  33     5172   3257   4062    236    710   -268       O  
ATOM    249  OD2 ASP A  33      29.478  23.911  43.608  1.00 49.17           O  
ANISOU  249  OD2 ASP A  33     7207   5400   6074    230    785   -229       O  
ATOM    250  N   TYR A  34      29.769  25.768  38.149  1.00 27.68           N  
ANISOU  250  N   TYR A  34     4680   2664   3171    284    730   -360       N  
ATOM    251  CA  TYR A  34      29.622  26.886  37.213  1.00 29.99           C  
ANISOU  251  CA  TYR A  34     5014   2969   3412    297    739   -368       C  
ATOM    252  C   TYR A  34      30.164  26.487  35.852  1.00 28.92           C  
ANISOU  252  C   TYR A  34     4957   2818   3213    361    740   -397       C  
ATOM    253  O   TYR A  34      30.838  25.472  35.731  1.00 26.72           O  
ANISOU  253  O   TYR A  34     4695   2528   2929    392    745   -407       O  
ATOM    254  CB  TYR A  34      30.290  28.157  37.751  1.00 30.19           C  
ANISOU  254  CB  TYR A  34     5002   3044   3424    274    803   -337       C  
ATOM    255  CG  TYR A  34      31.786  28.152  37.670  1.00 29.79           C  
ANISOU  255  CG  TYR A  34     4943   3019   3356    298    864   -324       C  
ATOM    256  CD1 TYR A  34      32.429  28.574  36.524  1.00 32.12           C  
ANISOU  256  CD1 TYR A  34     5280   3319   3602    342    907   -321       C  
ATOM    257  CD2 TYR A  34      32.558  27.711  38.729  1.00 28.69           C  
ANISOU  257  CD2 TYR A  34     4752   2894   3253    283    881   -308       C  
ATOM    258  CE1 TYR A  34      33.808  28.548  36.424  1.00 33.98           C  
ANISOU  258  CE1 TYR A  34     5498   3572   3841    368    972   -296       C  
ATOM    259  CE2 TYR A  34      33.937  27.680  38.646  1.00 30.94           C  
ANISOU  259  CE2 TYR A  34     5020   3196   3540    304    932   -291       C  
ATOM    260  CZ  TYR A  34      34.567  28.126  37.499  1.00 33.42           C  
ANISOU  260  CZ  TYR A  34     5364   3512   3819    344    981   -282       C  
ATOM    261  OH  TYR A  34      35.928  28.104  37.403  1.00 40.71           O  
ANISOU  261  OH  TYR A  34     6260   4445   4762    367   1040   -253       O  
ATOM    262  N   GLU A  35      29.766  27.271  34.842  1.00 28.44           N  
ANISOU  262  N   GLU A  35     4951   2753   3101    387    732   -409       N  
ATOM    263  CA  GLU A  35      30.161  27.102  33.447  1.00 28.03           C  
ANISOU  263  CA  GLU A  35     4995   2686   2968    467    737   -433       C  
ATOM    264  C   GLU A  35      30.396  28.494  32.856  1.00 28.01           C  
ANISOU  264  C   GLU A  35     5012   2715   2913    483    798   -409       C  
ATOM    265  O   GLU A  35      29.721  29.457  33.249  1.00 28.00           O  
ANISOU  265  O   GLU A  35     4973   2728   2938    434    789   -396       O  
ATOM    266  CB  GLU A  35      29.092  26.350  32.642  1.00 28.25           C  
ANISOU  266  CB  GLU A  35     5096   2650   2988    500    628   -486       C  
ATOM    267  CG  GLU A  35      27.714  26.959  32.735  1.00 28.59           C  
ANISOU  267  CG  GLU A  35     5119   2670   3071    456    559   -493       C  
ATOM    268  CD  GLU A  35      26.650  26.360  31.832  1.00 30.29           C  
ANISOU  268  CD  GLU A  35     5405   2813   3290    492    435   -547       C  
ATOM    269  OE1 GLU A  35      26.904  25.315  31.245  1.00 33.72           O  
ANISOU  269  OE1 GLU A  35     5904   3206   3700    548    388   -586       O  
ATOM    270  OE2 GLU A  35      25.558  26.930  31.741  1.00 30.61           O  
ANISOU  270  OE2 GLU A  35     5434   2831   3363    465    378   -551       O  
ATOM    271  N   LEU A  36      31.343  28.584  31.918  1.00 26.27           N  
ANISOU  271  N   LEU A  36     4851   2505   2625    558    865   -397       N  
ATOM    272  CA  LEU A  36      31.547  29.794  31.126  1.00 25.33           C  
ANISOU  272  CA  LEU A  36     4765   2405   2452    594    927   -368       C  
ATOM    273  C   LEU A  36      30.986  29.532  29.735  1.00 25.13           C  
ANISOU  273  C   LEU A  36     4871   2344   2333    685    880   -409       C  
ATOM    274  O   LEU A  36      31.380  28.584  29.116  1.00 26.40           O  
ANISOU  274  O   LEU A  36     5104   2480   2444    760    873   -431       O  
ATOM    275  CB  LEU A  36      33.043  30.097  31.115  1.00 25.87           C  
ANISOU  275  CB  LEU A  36     4799   2504   2525    622   1047   -311       C  
ATOM    276  CG  LEU A  36      33.520  31.221  30.193  1.00 27.38           C  
ANISOU  276  CG  LEU A  36     5022   2709   2670    678   1138   -264       C  
ATOM    277  CD1 LEU A  36      32.819  32.540  30.500  1.00 26.41           C  
ANISOU  277  CD1 LEU A  36     4857   2600   2575    616   1126   -253       C  
ATOM    278  CD2 LEU A  36      35.039  31.341  30.276  1.00 27.81           C  
ANISOU  278  CD2 LEU A  36     5022   2781   2763    702   1255   -198       C  
ATOM    279  N   ILE A  37      29.977  30.302  29.335  1.00 24.40           N  
ANISOU  279  N   ILE A  37     4807   2240   2220    679    832   -424       N  
ATOM    280  CA  ILE A  37      29.402  30.238  28.006  1.00 26.12           C  
ANISOU  280  CA  ILE A  37     5157   2423   2345    770    778   -463       C  
ATOM    281  C   ILE A  37      29.967  31.393  27.170  1.00 27.39           C  
ANISOU  281  C   ILE A  37     5363   2613   2430    835    884   -415       C  
ATOM    282  O   ILE A  37      29.669  32.579  27.442  1.00 27.61           O  
ANISOU  282  O   ILE A  37     5337   2666   2486    783    913   -384       O  
ATOM    283  CB  ILE A  37      27.869  30.299  28.052  1.00 26.80           C  
ANISOU  283  CB  ILE A  37     5247   2470   2466    727    646   -510       C  
ATOM    284  CG1 ILE A  37      27.288  29.237  28.985  1.00 28.01           C  
ANISOU  284  CG1 ILE A  37     5331   2589   2720    657    556   -538       C  
ATOM    285  CG2 ILE A  37      27.316  30.166  26.648  1.00 29.96           C  
ANISOU  285  CG2 ILE A  37     5792   2824   2767    832    570   -559       C  
ATOM    286  CD1 ILE A  37      25.781  29.270  29.107  1.00 29.05           C  
ANISOU  286  CD1 ILE A  37     5445   2674   2917    610    433   -569       C  
ATOM    287  N   ILE A  38      30.749  31.058  26.140  1.00 27.61           N  
ANISOU  287  N   ILE A  38     5494   2634   2362    955    945   -406       N  
ATOM    288  CA  ILE A  38      31.379  32.067  25.294  1.00 29.49           C  
ANISOU  288  CA  ILE A  38     5777   2894   2531   1034   1066   -345       C  
ATOM    289  C   ILE A  38      30.633  32.140  23.957  1.00 31.54           C  
ANISOU  289  C   ILE A  38     6199   3120   2664   1149   1006   -387       C  
ATOM    290  O   ILE A  38      30.570  31.171  23.253  1.00 33.25           O  
ANISOU  290  O   ILE A  38     6533   3298   2802   1243    949   -437       O  
ATOM    291  CB  ILE A  38      32.869  31.754  25.094  1.00 29.86           C  
ANISOU  291  CB  ILE A  38     5821   2958   2565   1103   1203   -283       C  
ATOM    292  CG1 ILE A  38      33.622  31.794  26.418  1.00 28.55           C  
ANISOU  292  CG1 ILE A  38     5494   2823   2531    991   1251   -242       C  
ATOM    293  CG2 ILE A  38      33.494  32.707  24.074  1.00 33.10           C  
ANISOU  293  CG2 ILE A  38     6290   3382   2904   1207   1338   -210       C  
ATOM    294  CD1 ILE A  38      35.045  31.347  26.303  1.00 30.72           C  
ANISOU  294  CD1 ILE A  38     5751   3105   2814   1050   1370   -184       C  
ATOM    295  N   ILE A  39      30.084  33.311  23.621  1.00 33.58           N  
ANISOU  295  N   ILE A  39     6466   3389   2902   1145   1016   -369       N  
ATOM    296  CA  ILE A  39      29.334  33.507  22.357  1.00 34.83           C  
ANISOU  296  CA  ILE A  39     6781   3514   2937   1257    954   -408       C  
ATOM    297  C   ILE A  39      30.091  34.533  21.502  1.00 35.39           C  
ANISOU  297  C   ILE A  39     6905   3613   2929   1356   1111   -326       C  
ATOM    298  O   ILE A  39      30.055  35.718  21.796  1.00 33.89           O  
ANISOU  298  O   ILE A  39     6634   3453   2789   1296   1173   -273       O  
ATOM    299  CB  ILE A  39      27.859  33.923  22.596  1.00 34.08           C  
ANISOU  299  CB  ILE A  39     6664   3397   2884   1177    813   -461       C  
ATOM    300  CG1 ILE A  39      27.149  32.999  23.592  1.00 33.95           C  
ANISOU  300  CG1 ILE A  39     6564   3353   2979   1068    683   -517       C  
ATOM    301  CG2 ILE A  39      27.101  33.964  21.275  1.00 34.23           C  
ANISOU  301  CG2 ILE A  39     6854   3372   2777   1301    725   -512       C  
ATOM    302  CD1 ILE A  39      27.191  33.460  25.005  1.00 35.39           C  
ANISOU  302  CD1 ILE A  39     6576   3576   3295    922    724   -477       C  
ATOM    303  N   ASP A  40      30.780  34.045  20.461  1.00 36.21           N  
ANISOU  303  N   ASP A  40     7144   3701   2910   1515   1176   -312       N  
ATOM    304  CA  ASP A  40      31.545  34.903  19.592  1.00 37.05           C  
ANISOU  304  CA  ASP A  40     7308   3827   2941   1631   1341   -222       C  
ATOM    305  C   ASP A  40      30.614  35.498  18.528  1.00 38.10           C  
ANISOU  305  C   ASP A  40     7585   3938   2950   1727   1281   -253       C  
ATOM    306  O   ASP A  40      29.942  34.770  17.786  1.00 41.03           O  
ANISOU  306  O   ASP A  40     8112   4264   3212   1822   1153   -338       O  
ATOM    307  CB  ASP A  40      32.730  34.179  18.960  1.00 37.84           C  
ANISOU  307  CB  ASP A  40     7490   3921   2963   1772   1460   -177       C  
ATOM    308  CG  ASP A  40      33.593  35.132  18.152  1.00 40.39           C  
ANISOU  308  CG  ASP A  40     7848   4263   3234   1890   1658    -59       C  
ATOM    309  OD1 ASP A  40      34.330  35.947  18.767  1.00 36.23           O  
ANISOU  309  OD1 ASP A  40     7164   3767   2833   1808   1785     35       O  
ATOM    310  OD2 ASP A  40      33.476  35.090  16.906  1.00 40.45           O  
ANISOU  310  OD2 ASP A  40     8041   4248   3077   2067   1679    -61       O  
ATOM    311  N   ASP A  41      30.609  36.833  18.449  1.00 38.76           N  
ANISOU  311  N   ASP A  41     7620   4050   3056   1706   1372   -183       N  
ATOM    312  CA  ASP A  41      29.799  37.545  17.494  1.00 40.08           C  
ANISOU  312  CA  ASP A  41     7910   4201   3114   1792   1333   -199       C  
ATOM    313  C   ASP A  41      30.528  37.639  16.142  1.00 42.39           C  
ANISOU  313  C   ASP A  41     8372   4486   3245   2008   1468   -138       C  
ATOM    314  O   ASP A  41      30.674  38.726  15.582  1.00 42.33           O  
ANISOU  314  O   ASP A  41     8388   4494   3199   2069   1581    -61       O  
ATOM    315  CB  ASP A  41      29.430  38.925  18.028  1.00 40.68           C  
ANISOU  315  CB  ASP A  41     7861   4308   3287   1675   1368   -152       C  
ATOM    316  CG  ASP A  41      28.064  39.400  17.563  1.00 42.95           C  
ANISOU  316  CG  ASP A  41     8228   4574   3517   1683   1232   -216       C  
ATOM    317  OD1 ASP A  41      27.468  38.736  16.665  1.00 41.86           O  
ANISOU  317  OD1 ASP A  41     8260   4393   3252   1800   1117   -292       O  
ATOM    318  OD2 ASP A  41      27.599  40.433  18.106  1.00 44.92           O  
ANISOU  318  OD2 ASP A  41     8371   4844   3851   1574   1234   -193       O  
ATOM    319  N   HIS A  42      30.939  36.481  15.619  1.00 44.50           N  
ANISOU  319  N   HIS A  42     8764   4726   3415   2129   1454   -172       N  
ATOM    320  CA  HIS A  42      31.544  36.333  14.280  1.00 46.69           C  
ANISOU  320  CA  HIS A  42     9239   4987   3512   2364   1563   -129       C  
ATOM    321  C   HIS A  42      32.732  37.300  14.143  1.00 47.35           C  
ANISOU  321  C   HIS A  42     9246   5109   3635   2406   1820     31       C  
ATOM    322  O   HIS A  42      32.700  38.242  13.334  1.00 49.38           O  
ANISOU  322  O   HIS A  42     9580   5370   3812   2511   1915     96       O  
ATOM    323  CB  HIS A  42      30.454  36.495  13.201  1.00 49.88           C  
ANISOU  323  CB  HIS A  42     9846   5353   3752   2491   1432   -205       C  
ATOM    324  CG  HIS A  42      30.717  35.691  11.970  1.00 52.70           C  
ANISOU  324  CG  HIS A  42    10449   5668   3903   2730   1431   -234       C  
ATOM    325  ND1 HIS A  42      30.525  34.313  11.924  1.00 55.14           N  
ANISOU  325  ND1 HIS A  42    10850   5930   4168   2767   1280   -341       N  
ATOM    326  CD2 HIS A  42      31.184  36.052  10.756  1.00 55.13           C  
ANISOU  326  CD2 HIS A  42    10937   5971   4037   2952   1565   -167       C  
ATOM    327  CE1 HIS A  42      30.883  33.859  10.737  1.00 54.47           C  
ANISOU  327  CE1 HIS A  42    10997   5814   3885   3004   1317   -345       C  
ATOM    328  NE2 HIS A  42      31.277  34.910   9.992  1.00 57.68           N  
ANISOU  328  NE2 HIS A  42    11466   6246   4202   3128   1494   -237       N  
ATOM    329  N   SER A  43      33.762  37.067  14.970  1.00 43.90           N  
ANISOU  329  N   SER A  43     8649   4694   3335   2319   1926     97       N  
ATOM    330  CA  SER A  43      35.017  37.815  14.948  1.00 43.54           C  
ANISOU  330  CA  SER A  43     8503   4671   3367   2349   2163    254       C  
ATOM    331  C   SER A  43      35.610  37.727  13.539  1.00 46.10           C  
ANISOU  331  C   SER A  43     9023   4977   3513   2604   2314    328       C  
ATOM    332  O   SER A  43      35.393  36.747  12.877  1.00 43.65           O  
ANISOU  332  O   SER A  43     8895   4640   3047   2738   2239    254       O  
ATOM    333  CB  SER A  43      36.010  37.271  15.940  1.00 41.41           C  
ANISOU  333  CB  SER A  43     8066   4414   3252   2245   2221    292       C  
ATOM    334  OG  SER A  43      35.661  37.633  17.263  1.00 39.56           O  
ANISOU  334  OG  SER A  43     7638   4199   3192   2022   2129    259       O  
ATOM    335  N   ASN A  44      36.402  38.729  13.154  1.00 49.75           N  
ANISOU  335  N   ASN A  44     9437   5450   4012   2670   2528    479       N  
ATOM    336  CA  ASN A  44      36.963  38.856  11.796  1.00 52.40           C  
ANISOU  336  CA  ASN A  44     9954   5770   4183   2926   2704    577       C  
ATOM    337  C   ASN A  44      38.434  39.296  11.882  1.00 58.32           C  
ANISOU  337  C   ASN A  44    10563   6525   5068   2955   2967    763       C  
ATOM    338  O   ASN A  44      38.907  40.031  11.001  1.00 61.81           O  
ANISOU  338  O   ASN A  44    11065   6960   5458   3111   3158    895       O  
ATOM    339  CB  ASN A  44      36.146  39.826  10.929  1.00 52.04           C  
ANISOU  339  CB  ASN A  44    10037   5721   4014   3019   2696    581       C  
ATOM    340  CG  ASN A  44      36.120  41.244  11.469  1.00 54.82           C  
ANISOU  340  CG  ASN A  44    10199   6093   4534   2875   2767    665       C  
ATOM    341  OD1 ASN A  44      37.095  41.699  12.060  1.00 60.90           O  
ANISOU  341  OD1 ASN A  44    10778   6872   5488   2794   2914    782       O  
ATOM    342  ND2 ASN A  44      35.007  41.948  11.314  1.00 53.08           N  
ANISOU  342  ND2 ASN A  44    10023   5876   4267   2838   2651    603       N  
ATOM    343  N   ASP A  45      39.161  38.827  12.907  1.00 54.61           N  
ANISOU  343  N   ASP A  45     9910   6063   4775   2817   2976    778       N  
ATOM    344  CA  ASP A  45      40.533  39.289  13.189  1.00 53.72           C  
ANISOU  344  CA  ASP A  45     9619   5946   4843   2805   3197    949       C  
ATOM    345  C   ASP A  45      41.518  38.198  12.778  1.00 55.68           C  
ANISOU  345  C   ASP A  45     9941   6180   5034   2954   3311    998       C  
ATOM    346  O   ASP A  45      42.432  37.834  13.530  1.00 53.21           O  
ANISOU  346  O   ASP A  45     9464   5866   4887   2868   3366   1049       O  
ATOM    347  CB  ASP A  45      40.684  39.744  14.644  1.00 52.67           C  
ANISOU  347  CB  ASP A  45     9219   5826   4967   2546   3131    944       C  
ATOM    348  CG  ASP A  45      40.344  38.696  15.696  1.00 51.05           C  
ANISOU  348  CG  ASP A  45     8959   5634   4804   2395   2936    803       C  
ATOM    349  OD1 ASP A  45      39.795  37.640  15.326  1.00 49.07           O  
ANISOU  349  OD1 ASP A  45     8873   5379   4389   2469   2822    692       O  
ATOM    350  OD2 ASP A  45      40.660  38.934  16.875  1.00 47.57           O  
ANISOU  350  OD2 ASP A  45     8311   5199   4563   2212   2901    809       O  
ATOM    351  N   ASN A  46      41.319  37.721  11.544  1.00 59.92           N  
ANISOU  351  N   ASN A  46    10734   6703   5328   3189   3345    985       N  
ATOM    352  CA  ASN A  46      42.025  36.619  10.933  1.00 59.87           C  
ANISOU  352  CA  ASN A  46    10867   6680   5201   3373   3432   1008       C  
ATOM    353  C   ASN A  46      42.351  35.558  11.991  1.00 57.62           C  
ANISOU  353  C   ASN A  46    10459   6400   5034   3225   3326    933       C  
ATOM    354  O   ASN A  46      43.510  35.138  12.146  1.00 55.88           O  
ANISOU  354  O   ASN A  46    10155   6171   4903   3260   3475   1033       O  
ATOM    355  CB  ASN A  46      43.251  37.098  10.158  1.00 62.92           C  
ANISOU  355  CB  ASN A  46    11251   7049   5603   3560   3739   1222       C  
ATOM    356  CG  ASN A  46      43.423  36.331   8.860  1.00 67.38           C  
ANISOU  356  CG  ASN A  46    12104   7594   5903   3859   3825   1233       C  
ATOM    357  OD1 ASN A  46      42.669  36.529   7.906  1.00 64.91           O  
ANISOU  357  OD1 ASN A  46    12014   7273   5374   4014   3784   1187       O  
ATOM    358  ND2 ASN A  46      44.378  35.416   8.832  1.00 68.23           N  
ANISOU  358  ND2 ASN A  46    12216   7689   6018   3944   3929   1285       N  
ATOM    359  N   GLY A  47      41.307  35.120  12.705  1.00 55.62           N  
ANISOU  359  N   GLY A  47    10196   6156   4781   3065   3073    761       N  
ATOM    360  CA  GLY A  47      41.342  33.866  13.450  1.00 54.02           C  
ANISOU  360  CA  GLY A  47     9959   5951   4613   2975   2938    656       C  
ATOM    361  C   GLY A  47      41.869  34.003  14.874  1.00 52.39           C  
ANISOU  361  C   GLY A  47     9476   5764   4664   2743   2929    683       C  
ATOM    362  O   GLY A  47      41.838  33.040  15.620  1.00 50.09           O  
ANISOU  362  O   GLY A  47     9139   5474   4416   2648   2811    597       O  
ATOM    363  N   GLU A  48      42.334  35.193  15.260  1.00 49.90           N  
ANISOU  363  N   GLU A  48     8982   5459   4519   2656   3045    799       N  
ATOM    364  CA  GLU A  48      43.128  35.344  16.465  1.00 51.70           C  
ANISOU  364  CA  GLU A  48     8958   5692   4991   2481   3073    854       C  
ATOM    365  C   GLU A  48      42.271  35.145  17.728  1.00 48.84           C  
ANISOU  365  C   GLU A  48     8494   5349   4712   2256   2844    711       C  
ATOM    366  O   GLU A  48      42.742  34.550  18.680  1.00 49.02           O  
ANISOU  366  O   GLU A  48     8392   5376   4856   2147   2801    692       O  
ATOM    367  CB  GLU A  48      43.785  36.721  16.535  1.00 57.71           C  
ANISOU  367  CB  GLU A  48     9557   6446   5923   2447   3236   1009       C  
ATOM    368  CG  GLU A  48      44.773  36.835  17.685  1.00 59.26           C  
ANISOU  368  CG  GLU A  48     9502   6635   6380   2294   3271   1075       C  
ATOM    369  CD  GLU A  48      45.962  35.896  17.543  1.00 62.28           C  
ANISOU  369  CD  GLU A  48     9870   7000   6792   2390   3397   1153       C  
ATOM    370  N   THR A  49      41.036  35.664  17.725  1.00 45.42           N  
ANISOU  370  N   THR A  49     8114   4927   4216   2197   2706    621       N  
ATOM    371  CA  THR A  49      40.108  35.510  18.865  1.00 45.67           C  
ANISOU  371  CA  THR A  49     8061   4973   4315   2000   2497    493       C  
ATOM    372  C   THR A  49      39.704  34.035  18.996  1.00 45.72           C  
ANISOU  372  C   THR A  49     8167   4973   4231   2011   2355    370       C  
ATOM    373  O   THR A  49      39.754  33.470  20.109  1.00 40.69           O  
ANISOU  373  O   THR A  49     7412   4344   3702   1872   2264    319       O  
ATOM    374  CB  THR A  49      38.886  36.436  18.761  1.00 44.73           C  
ANISOU  374  CB  THR A  49     7977   4863   4155   1947   2397    438       C  
ATOM    375  OG1 THR A  49      39.311  37.795  18.850  1.00 44.13           O  
ANISOU  375  OG1 THR A  49     7779   4791   4197   1908   2518    551       O  
ATOM    376  CG2 THR A  49      37.868  36.209  19.860  1.00 45.05           C  
ANISOU  376  CG2 THR A  49     7948   4915   4253   1767   2192    313       C  
ATOM    377  N   LEU A  50      39.344  33.415  17.858  1.00 45.66           N  
ANISOU  377  N   LEU A  50     8377   4945   4025   2185   2338    326       N  
ATOM    378  CA  LEU A  50      38.802  32.045  17.847  1.00 45.31           C  
ANISOU  378  CA  LEU A  50     8447   4880   3885   2208   2180    198       C  
ATOM    379  C   LEU A  50      39.916  31.085  18.258  1.00 45.66           C  
ANISOU  379  C   LEU A  50     8430   4924   3994   2217   2253    234       C  
ATOM    380  O   LEU A  50      39.639  30.059  18.903  1.00 46.48           O  
ANISOU  380  O   LEU A  50     8518   5020   4121   2141   2120    142       O  
ATOM    381  CB  LEU A  50      38.215  31.724  16.468  1.00 45.86           C  
ANISOU  381  CB  LEU A  50     8775   4920   3730   2408   2142    146       C  
ATOM    382  CG  LEU A  50      37.628  30.320  16.308  1.00 49.49           C  
ANISOU  382  CG  LEU A  50     9372   5342   4087   2452   1966      9       C  
ATOM    383  N   ASN A  51      41.163  31.462  17.929  1.00 45.15           N  
ANISOU  383  N   ASN A  51     8317   4864   3974   2302   2467    378       N  
ATOM    384  CA  ASN A  51      42.352  30.684  18.271  1.00 46.93           C  
ANISOU  384  CA  ASN A  51     8468   5085   4276   2319   2564    437       C  
ATOM    385  C   ASN A  51      42.653  30.698  19.771  1.00 43.23           C  
ANISOU  385  C   ASN A  51     7768   4635   4019   2105   2507    432       C  
ATOM    386  O   ASN A  51      43.143  29.700  20.281  1.00 44.94           O  
ANISOU  386  O   ASN A  51     7948   4848   4278   2080   2484    409       O  
ATOM    387  CB  ASN A  51      43.593  31.144  17.509  1.00 50.03           C  
ANISOU  387  CB  ASN A  51     8857   5470   4680   2471   2817    607       C  
ATOM    388  CG  ASN A  51      43.766  30.381  16.215  1.00 55.08           C  
ANISOU  388  CG  ASN A  51     9734   6086   5105   2716   2888    611       C  
ATOM    389  OD1 ASN A  51      43.398  29.209  16.132  1.00 60.07           O  
ANISOU  389  OD1 ASN A  51    10489   6705   5631   2754   2765    499       O  
ATOM    390  ND2 ASN A  51      44.358  31.018  15.219  1.00 56.41           N  
ANISOU  390  ND2 ASN A  51     9970   6245   5215   2888   3091    744       N  
ATOM    391  N   VAL A  52      42.426  31.833  20.439  1.00 42.58           N  
ANISOU  391  N   VAL A  52     7540   4568   4067   1965   2493    458       N  
ATOM    392  CA  VAL A  52      42.551  31.922  21.901  1.00 42.44           C  
ANISOU  392  CA  VAL A  52     7325   4565   4234   1766   2412    436       C  
ATOM    393  C   VAL A  52      41.498  31.008  22.544  1.00 40.72           C  
ANISOU  393  C   VAL A  52     7149   4353   3969   1675   2205    285       C  
ATOM    394  O   VAL A  52      41.803  30.236  23.446  1.00 44.56           O  
ANISOU  394  O   VAL A  52     7553   4842   4535   1593   2149    254       O  
ATOM    395  CB  VAL A  52      42.393  33.367  22.418  1.00 41.43           C  
ANISOU  395  CB  VAL A  52     7060   4447   4235   1650   2422    482       C  
ATOM    396  CG1 VAL A  52      42.419  33.424  23.941  1.00 39.86           C  
ANISOU  396  CG1 VAL A  52     6683   4258   4201   1459   2316    444       C  
ATOM    397  CG2 VAL A  52      43.454  34.292  21.859  1.00 42.97           C  
ANISOU  397  CG2 VAL A  52     7187   4626   4511   1728   2625    641       C  
ATOM    398  N   ILE A  53      40.254  31.127  22.076  1.00 39.86           N  
ANISOU  398  N   ILE A  53     7163   4241   3742   1692   2092    200       N  
ATOM    399  CA  ILE A  53      39.115  30.410  22.633  1.00 39.80           C  
ANISOU  399  CA  ILE A  53     7185   4228   3709   1604   1895     68       C  
ATOM    400  C   ILE A  53      39.354  28.897  22.523  1.00 41.58           C  
ANISOU  400  C   ILE A  53     7490   4432   3875   1667   1851     13       C  
ATOM    401  O   ILE A  53      38.994  28.169  23.452  1.00 41.22           O  
ANISOU  401  O   ILE A  53     7383   4384   3892   1560   1732    -55       O  
ATOM    402  CB  ILE A  53      37.792  30.858  21.968  1.00 39.40           C  
ANISOU  402  CB  ILE A  53     7256   4166   3547   1633   1793      0       C  
ATOM    403  CG1 ILE A  53      37.500  32.339  22.241  1.00 37.83           C  
ANISOU  403  CG1 ILE A  53     6963   3989   3421   1550   1824     47       C  
ATOM    404  CG2 ILE A  53      36.622  29.985  22.415  1.00 39.77           C  
ANISOU  404  CG2 ILE A  53     7339   4193   3577   1561   1591   -129       C  
ATOM    405  CD1 ILE A  53      36.337  32.903  21.439  1.00 38.60           C  
ANISOU  405  CD1 ILE A  53     7184   4076   3405   1599   1752      0       C  
ATOM    406  N   LYS A  54      39.954  28.449  21.403  1.00 43.69           N  
ANISOU  406  N   LYS A  54     7896   4680   4022   1847   1950     50       N  
ATOM    407  CA  LYS A  54      40.150  27.025  21.084  1.00 44.99           C  
ANISOU  407  CA  LYS A  54     8173   4818   4104   1938   1909     -5       C  
ATOM    408  C   LYS A  54      41.111  26.376  22.089  1.00 43.56           C  
ANISOU  408  C   LYS A  54     7845   4649   4056   1856   1950     28       C  
ATOM    409  O   LYS A  54      40.941  25.200  22.440  1.00 41.49           O  
ANISOU  409  O   LYS A  54     7609   4369   3786   1837   1850    -46       O  
ATOM    410  CB  LYS A  54      40.634  26.830  19.640  1.00 50.70           C  
ANISOU  410  CB  LYS A  54     9085   5518   4659   2167   2025     38       C  
ATOM    411  CG  LYS A  54      39.615  26.150  18.731  1.00 57.29           C  
ANISOU  411  CG  LYS A  54    10142   6310   5315   2282   1878    -80       C  
ATOM    412  CD  LYS A  54      39.736  26.460  17.251  1.00 60.91           C  
ANISOU  412  CD  LYS A  54    10805   6749   5587   2506   1973    -42       C  
ATOM    413  CE  LYS A  54      38.595  27.311  16.716  1.00 65.79           C  
ANISOU  413  CE  LYS A  54    11509   7360   6127   2518   1882    -89       C  
ATOM    414  NZ  LYS A  54      37.539  26.506  16.043  1.00 64.83           N  
ANISOU  414  NZ  LYS A  54    11589   7183   5860   2605   1684   -229       N  
ATOM    415  N   LYS A  55      42.059  27.148  22.626  1.00 41.33           N  
ANISOU  415  N   LYS A  55     7400   4391   3910   1796   2079    137       N  
ATOM    416  CA  LYS A  55      42.962  26.636  23.679  1.00 43.77           C  
ANISOU  416  CA  LYS A  55     7556   4709   4362   1706   2103    168       C  
ATOM    417  C   LYS A  55      42.180  26.190  24.929  1.00 41.30           C  
ANISOU  417  C   LYS A  55     7162   4405   4123   1540   1928     69       C  
ATOM    418  O   LYS A  55      42.748  25.503  25.747  1.00 43.34           O  
ANISOU  418  O   LYS A  55     7332   4666   4466   1482   1917     69       O  
ATOM    419  CB  LYS A  55      44.007  27.678  24.098  1.00 45.15           C  
ANISOU  419  CB  LYS A  55     7559   4898   4694   1657   2243    295       C  
ATOM    420  CG  LYS A  55      44.909  28.218  22.983  1.00 46.58           C  
ANISOU  420  CG  LYS A  55     7783   5068   4845   1814   2445    424       C  
ATOM    421  CD  LYS A  55      46.052  27.334  22.564  1.00 48.51           C  
ANISOU  421  CD  LYS A  55     8055   5296   5078   1937   2572    492       C  
ATOM    422  N   TYR A  56      40.912  26.606  25.105  1.00 41.00           N  
ANISOU  422  N   TYR A  56     7147   4369   4060   1467   1800     -6       N  
ATOM    423  CA  TYR A  56      40.110  26.221  26.304  1.00 41.83           C  
ANISOU  423  CA  TYR A  56     7174   4478   4239   1318   1647    -87       C  
ATOM    424  C   TYR A  56      38.990  25.233  25.949  1.00 40.47           C  
ANISOU  424  C   TYR A  56     7131   4272   3971   1347   1498   -197       C  
ATOM    425  O   TYR A  56      38.086  25.044  26.739  1.00 36.57           O  
ANISOU  425  O   TYR A  56     6590   3775   3529   1240   1373   -260       O  
ATOM    426  CB  TYR A  56      39.498  27.443  27.011  1.00 39.89           C  
ANISOU  426  CB  TYR A  56     6825   4255   4073   1194   1608    -81       C  
ATOM    427  CG  TYR A  56      40.531  28.442  27.445  1.00 38.44           C  
ANISOU  427  CG  TYR A  56     6505   4092   4005   1154   1726     17       C  
ATOM    428  CD1 TYR A  56      41.243  28.274  28.621  1.00 37.45           C  
ANISOU  428  CD1 TYR A  56     6240   3977   4011   1061   1726     40       C  
ATOM    429  CD2 TYR A  56      40.897  29.476  26.600  1.00 38.96           C  
ANISOU  429  CD2 TYR A  56     6589   4159   4053   1224   1843     95       C  
ATOM    430  CE1 TYR A  56      42.234  29.169  28.989  1.00 39.06           C  
ANISOU  430  CE1 TYR A  56     6316   4187   4338   1029   1819    130       C  
ATOM    431  CE2 TYR A  56      41.876  30.384  26.956  1.00 39.91           C  
ANISOU  431  CE2 TYR A  56     6576   4286   4303   1189   1949    194       C  
ATOM    432  CZ  TYR A  56      42.539  30.236  28.161  1.00 40.69           C  
ANISOU  432  CZ  TYR A  56     6529   4389   4543   1088   1928    208       C  
ATOM    433  OH  TYR A  56      43.508  31.133  28.502  1.00 46.61           O  
ANISOU  433  OH  TYR A  56     7142   5131   5435   1054   2014    301       O  
ATOM    434  N   LYS A  57      39.059  24.600  24.777  1.00 42.80           N  
ANISOU  434  N   LYS A  57     7589   4537   4135   1498   1511   -218       N  
ATOM    435  CA  LYS A  57      38.091  23.583  24.410  1.00 44.42           C  
ANISOU  435  CA  LYS A  57     7918   4695   4263   1534   1357   -326       C  
ATOM    436  C   LYS A  57      38.025  22.517  25.508  1.00 39.83           C  
ANISOU  436  C   LYS A  57     7250   4105   3779   1433   1270   -370       C  
ATOM    437  O   LYS A  57      39.053  22.070  26.029  1.00 38.08           O  
ANISOU  437  O   LYS A  57     6952   3900   3614   1421   1350   -324       O  
ATOM    438  CB  LYS A  57      38.445  22.896  23.090  1.00 47.35           C  
ANISOU  438  CB  LYS A  57     8479   5030   4481   1726   1391   -340       C  
ATOM    439  CG  LYS A  57      37.345  21.982  22.573  1.00 51.84           C  
ANISOU  439  CG  LYS A  57     9192   5536   4968   1774   1207   -461       C  
ATOM    440  CD  LYS A  57      37.492  21.613  21.121  1.00 59.53           C  
ANISOU  440  CD  LYS A  57    10385   6469   5762   1982   1223   -483       C  
ATOM    441  CE  LYS A  57      36.788  20.318  20.765  1.00 65.15           C  
ANISOU  441  CE  LYS A  57    11229   7106   6418   2036   1042   -602       C  
ATOM    442  NZ  LYS A  57      35.429  20.578  20.241  1.00 69.58           N  
ANISOU  442  NZ  LYS A  57    11885   7620   6932   2045    872   -689       N  
ATOM    443  N   GLY A  58      36.800  22.127  25.852  1.00 38.41           N  
ANISOU  443  N   GLY A  58     7076   3893   3624   1362   1108   -454       N  
ATOM    444  CA  GLY A  58      36.557  21.178  26.929  1.00 38.28           C  
ANISOU  444  CA  GLY A  58     6973   3862   3708   1262   1022   -491       C  
ATOM    445  C   GLY A  58      36.394  21.833  28.289  1.00 39.14           C  
ANISOU  445  C   GLY A  58     6911   4012   3945   1108   1026   -457       C  
ATOM    446  O   GLY A  58      35.931  21.160  29.229  1.00 40.82           O  
ANISOU  446  O   GLY A  58     7055   4212   4241   1022    944   -488       O  
ATOM    447  N   LEU A  59      36.768  23.122  28.424  1.00 35.70           N  
ANISOU  447  N   LEU A  59     6410   3623   3530   1078   1121   -393       N  
ATOM    448  CA  LEU A  59      36.643  23.842  29.685  1.00 34.42           C  
ANISOU  448  CA  LEU A  59     6101   3497   3478    946   1121   -364       C  
ATOM    449  C   LEU A  59      35.546  24.904  29.599  1.00 32.33           C  
ANISOU  449  C   LEU A  59     5837   3236   3209    900   1070   -378       C  
ATOM    450  O   LEU A  59      35.227  25.498  30.588  1.00 31.71           O  
ANISOU  450  O   LEU A  59     5657   3179   3208    800   1054   -365       O  
ATOM    451  CB  LEU A  59      37.977  24.482  30.069  1.00 35.70           C  
ANISOU  451  CB  LEU A  59     6169   3700   3695    935   1254   -279       C  
ATOM    452  CG  LEU A  59      39.175  23.537  30.084  1.00 38.56           C  
ANISOU  452  CG  LEU A  59     6523   4060   4067    988   1321   -252       C  
ATOM    453  CD1 LEU A  59      40.459  24.337  30.247  1.00 38.88           C  
ANISOU  453  CD1 LEU A  59     6471   4128   4172    989   1454   -159       C  
ATOM    454  CD2 LEU A  59      39.041  22.469  31.186  1.00 37.74           C  
ANISOU  454  CD2 LEU A  59     6360   3948   4030    916   1243   -289       C  
ATOM    455  N   VAL A  60      34.987  25.125  28.411  1.00 31.29           N  
ANISOU  455  N   VAL A  60     5828   3079   2980    984   1043   -406       N  
ATOM    456  CA  VAL A  60      33.993  26.160  28.210  1.00 32.57           C  
ANISOU  456  CA  VAL A  60     5998   3244   3132    952   1001   -417       C  
ATOM    457  C   VAL A  60      32.883  25.590  27.324  1.00 31.60           C  
ANISOU  457  C   VAL A  60     6004   3064   2939   1013    872   -496       C  
ATOM    458  O   VAL A  60      33.081  24.551  26.678  1.00 31.18           O  
ANISOU  458  O   VAL A  60     6050   2972   2825   1102    838   -534       O  
ATOM    459  CB  VAL A  60      34.640  27.420  27.590  1.00 33.98           C  
ANISOU  459  CB  VAL A  60     6186   3456   3269   1001   1126   -349       C  
ATOM    460  CG1 VAL A  60      35.756  27.950  28.480  1.00 34.62           C  
ANISOU  460  CG1 VAL A  60     6130   3578   3444    938   1234   -273       C  
ATOM    461  CG2 VAL A  60      35.164  27.174  26.170  1.00 36.33           C  
ANISOU  461  CG2 VAL A  60     6628   3734   3439   1160   1190   -339       C  
ATOM    462  N   ARG A  61      31.732  26.263  27.302  1.00 30.00           N  
ANISOU  462  N   ARG A  61     5798   2849   2749    968    794   -520       N  
ATOM    463  CA  ARG A  61      30.780  26.070  26.209  1.00 31.17           C  
ANISOU  463  CA  ARG A  61     6081   2942   2818   1046    682   -585       C  
ATOM    464  C   ARG A  61      30.920  27.238  25.242  1.00 31.69           C  
ANISOU  464  C   ARG A  61     6223   3031   2785   1123    757   -553       C  
ATOM    465  O   ARG A  61      31.189  28.365  25.636  1.00 31.51           O  
ANISOU  465  O   ARG A  61     6117   3058   2796   1069    849   -492       O  
ATOM    466  CB  ARG A  61      29.352  25.906  26.728  1.00 32.38           C  
ANISOU  466  CB  ARG A  61     6187   3054   3062    956    534   -633       C  
ATOM    467  CG  ARG A  61      29.165  24.676  27.609  1.00 32.76           C  
ANISOU  467  CG  ARG A  61     6166   3068   3211    894    462   -658       C  
ATOM    468  CD  ARG A  61      27.829  24.723  28.329  1.00 33.57           C  
ANISOU  468  CD  ARG A  61     6185   3138   3432    793    354   -674       C  
ATOM    469  NE  ARG A  61      26.716  24.675  27.386  1.00 35.23           N  
ANISOU  469  NE  ARG A  61     6486   3278   3619    839    215   -735       N  
ATOM    470  CZ  ARG A  61      25.472  24.992  27.701  1.00 35.25           C  
ANISOU  470  CZ  ARG A  61     6432   3248   3712    771    124   -744       C  
ATOM    471  NH1 ARG A  61      25.194  25.377  28.941  1.00 32.07           N  
ANISOU  471  NH1 ARG A  61     5890   2879   3416    661    168   -692       N  
ATOM    472  NH2 ARG A  61      24.525  24.920  26.773  1.00 34.91           N  
ANISOU  472  NH2 ARG A  61     6477   3134   3651    821    -12   -802       N  
ATOM    473  N   PHE A  62      30.780  26.948  23.954  1.00 32.27           N  
ANISOU  473  N   PHE A  62     6461   3065   2733   1260    718   -593       N  
ATOM    474  CA  PHE A  62      31.057  27.936  22.960  1.00 33.91           C  
ANISOU  474  CA  PHE A  62     6757   3292   2832   1359    808   -554       C  
ATOM    475  C   PHE A  62      30.016  27.848  21.851  1.00 35.86           C  
ANISOU  475  C   PHE A  62     7165   3480   2977   1455    672   -630       C  
ATOM    476  O   PHE A  62      29.646  26.772  21.451  1.00 37.23           O  
ANISOU  476  O   PHE A  62     7433   3593   3119   1512    548   -706       O  
ATOM    477  CB  PHE A  62      32.470  27.750  22.413  1.00 35.38           C  
ANISOU  477  CB  PHE A  62     6999   3502   2941   1475    965   -493       C  
ATOM    478  CG  PHE A  62      32.808  28.638  21.250  1.00 36.70           C  
ANISOU  478  CG  PHE A  62     7278   3680   2983   1609   1072   -443       C  
ATOM    479  CD1 PHE A  62      33.201  29.953  21.452  1.00 36.82           C  
ANISOU  479  CD1 PHE A  62     7202   3745   3041   1567   1201   -355       C  
ATOM    480  CD2 PHE A  62      32.668  28.175  19.951  1.00 39.68           C  
ANISOU  480  CD2 PHE A  62     7859   4014   3202   1784   1034   -487       C  
ATOM    481  CE1 PHE A  62      33.515  30.767  20.377  1.00 39.85           C  
ANISOU  481  CE1 PHE A  62     7685   4136   3317   1695   1310   -298       C  
ATOM    482  CE2 PHE A  62      32.979  28.993  18.873  1.00 40.74           C  
ANISOU  482  CE2 PHE A  62     8106   4159   3212   1922   1143   -433       C  
ATOM    483  CZ  PHE A  62      33.405  30.285  19.086  1.00 40.38           C  
ANISOU  483  CZ  PHE A  62     7959   4165   3218   1876   1288   -334       C  
ATOM    484  N   LYS A  63      29.583  29.018  21.379  1.00 36.96           N  
ANISOU  484  N   LYS A  63     7331   3637   3074   1472    695   -608       N  
ATOM    485  CA  LYS A  63      28.793  29.147  20.178  1.00 40.72           C  
ANISOU  485  CA  LYS A  63     7975   4064   3430   1589    594   -665       C  
ATOM    486  C   LYS A  63      29.279  30.371  19.389  1.00 40.91           C  
ANISOU  486  C   LYS A  63     8061   4130   3350   1682    741   -591       C  
ATOM    487  O   LYS A  63      29.557  31.406  19.955  1.00 36.74           O  
ANISOU  487  O   LYS A  63     7410   3657   2893   1596    852   -517       O  
ATOM    488  CB  LYS A  63      27.308  29.292  20.499  1.00 42.01           C  
ANISOU  488  CB  LYS A  63     8096   4187   3678   1492    417   -728       C  
ATOM    489  CG  LYS A  63      26.402  29.017  19.313  1.00 47.13           C  
ANISOU  489  CG  LYS A  63     8924   4758   4222   1613    253   -815       C  
ATOM    490  CD  LYS A  63      24.980  29.459  19.525  1.00 52.77           C  
ANISOU  490  CD  LYS A  63     9587   5436   5024   1525    103   -857       C  
ATOM    491  CE  LYS A  63      24.023  28.829  18.533  1.00 59.43           C  
ANISOU  491  CE  LYS A  63    10590   6180   5808   1626   -109   -961       C  
ATOM    492  NZ  LYS A  63      24.516  28.926  17.135  1.00 60.83           N  
ANISOU  492  NZ  LYS A  63    10989   6347   5777   1831    -78   -977       N  
ATOM    493  N   GLN A  64      29.399  30.222  18.074  1.00 45.86           N  
ANISOU  493  N   GLN A  64     8887   4725   3810   1867    741   -611       N  
ATOM    494  CA  GLN A  64      29.669  31.354  17.213  1.00 49.64           C  
ANISOU  494  CA  GLN A  64     9445   5233   4182   1972    865   -545       C  
ATOM    495  C   GLN A  64      28.420  31.647  16.380  1.00 49.97           C  
ANISOU  495  C   GLN A  64     9622   5225   4137   2036    706   -622       C  
ATOM    496  O   GLN A  64      27.845  30.739  15.763  1.00 50.42           O  
ANISOU  496  O   GLN A  64     9823   5213   4120   2125    542   -720       O  
ATOM    497  CB  GLN A  64      30.862  31.101  16.295  1.00 54.12           C  
ANISOU  497  CB  GLN A  64    10145   5807   4610   2160   1022   -486       C  
ATOM    498  CG  GLN A  64      31.340  32.384  15.625  1.00 55.88           C  
ANISOU  498  CG  GLN A  64    10401   6068   4761   2248   1200   -382       C  
ATOM    499  CD  GLN A  64      32.474  32.162  14.662  1.00 58.30           C  
ANISOU  499  CD  GLN A  64    10844   6376   4930   2451   1370   -310       C  
ATOM    500  OE1 GLN A  64      32.408  31.297  13.792  1.00 64.67           O  
ANISOU  500  OE1 GLN A  64    11846   7135   5588   2614   1303   -372       O  
ATOM    501  NE2 GLN A  64      33.503  32.983  14.786  1.00 54.37           N  
ANISOU  501  NE2 GLN A  64    10248   5926   4484   2451   1590   -174       N  
ATOM    502  N   LEU A  65      28.027  32.922  16.361  1.00 51.06           N  
ANISOU  502  N   LEU A  65     9713   5395   4290   1995    752   -577       N  
ATOM    503  CA  LEU A  65      26.936  33.381  15.528  1.00 52.33           C  
ANISOU  503  CA  LEU A  65     9999   5516   4366   2063    625   -634       C  
ATOM    504  C   LEU A  65      27.436  33.481  14.083  1.00 53.24           C  
ANISOU  504  C   LEU A  65    10341   5618   4268   2301    701   -615       C  
ATOM    505  O   LEU A  65      28.648  33.639  13.850  1.00 50.76           O  
ANISOU  505  O   LEU A  65    10041   5344   3901   2385    904   -521       O  
ATOM    506  CB  LEU A  65      26.431  34.727  16.050  1.00 51.90           C  
ANISOU  506  CB  LEU A  65     9811   5505   4403   1938    665   -583       C  
ATOM    507  CG  LEU A  65      25.940  34.746  17.497  1.00 52.64           C  
ANISOU  507  CG  LEU A  65     9689   5615   4695   1719    608   -590       C  
ATOM    508  CD1 LEU A  65      25.479  36.139  17.856  1.00 51.19           C  
ANISOU  508  CD1 LEU A  65     9404   5470   4573   1626    655   -540       C  
ATOM    509  CD2 LEU A  65      24.825  33.730  17.740  1.00 53.83           C  
ANISOU  509  CD2 LEU A  65     9846   5695   4910   1666    379   -700       C  
ATOM    510  N   LYS A  66      26.495  33.363  13.135  1.00 56.64           N  
ANISOU  510  N   LYS A  66    10949   5986   4583   2415    534   -702       N  
ATOM    511  CA  LYS A  66      26.795  33.252  11.689  1.00 61.73           C  
ANISOU  511  CA  LYS A  66    11854   6601   5000   2669    561   -711       C  
ATOM    512  C   LYS A  66      27.169  34.626  11.126  1.00 62.60           C  
ANISOU  512  C   LYS A  66    11993   6764   5028   2748    750   -601       C  
ATOM    513  O   LYS A  66      28.072  34.740  10.313  1.00 71.53           O  
ANISOU  513  O   LYS A  66    13252   7908   6015   2928    916   -529       O  
ATOM    514  CB  LYS A  66      25.590  32.692  10.923  1.00 62.54           C  
ANISOU  514  CB  LYS A  66    12134   6609   5017   2759    291   -851       C  
ATOM    515  N   LYS A  67      26.423  35.640  11.564  1.00 60.46           N  
ANISOU  515  N   LYS A  67    11603   6515   4854   2616    721   -587       N  
ATOM    516  CA  LYS A  67      26.522  37.018  11.136  1.00 62.19           C  
ANISOU  516  CA  LYS A  67    11827   6776   5025   2659    864   -494       C  
ATOM    517  C   LYS A  67      26.769  37.876  12.378  1.00 61.10           C  
ANISOU  517  C   LYS A  67    11425   6702   5087   2442    978   -411       C  
ATOM    518  O   LYS A  67      26.148  37.651  13.426  1.00 57.68           O  
ANISOU  518  O   LYS A  67    10838   6266   4810   2255    858   -462       O  
ATOM    519  CB  LYS A  67      25.212  37.427  10.451  1.00 67.68           C  
ANISOU  519  CB  LYS A  67    12644   7424   5644   2710    681   -576       C  
ATOM    520  CG  LYS A  67      25.043  38.908  10.152  1.00 72.83           C  
ANISOU  520  CG  LYS A  67    13279   8116   6275   2719    792   -494       C  
ATOM    521  CD  LYS A  67      25.374  39.263   8.717  1.00 79.27           C  
ANISOU  521  CD  LYS A  67    14335   8920   6861   2978    883   -455       C  
ATOM    522  CE  LYS A  67      24.652  40.504   8.245  1.00 85.19           C  
ANISOU  522  CE  LYS A  67    15120   9678   7569   3001    878   -431       C  
ATOM    523  NZ  LYS A  67      23.183  40.350   8.359  1.00 88.55           N  
ANISOU  523  NZ  LYS A  67    15553  10051   8041   2919    604   -560       N  
ATOM    524  N   ASN A  68      27.641  38.880  12.252  1.00 58.27           N  
ANISOU  524  N   ASN A  68    11018   6394   4727   2473   1204   -280       N  
ATOM    525  CA  ASN A  68      27.926  39.769  13.359  1.00 54.92           C  
ANISOU  525  CA  ASN A  68    10359   6022   4486   2284   1306   -202       C  
ATOM    526  C   ASN A  68      26.682  40.636  13.589  1.00 55.95           C  
ANISOU  526  C   ASN A  68    10441   6150   4667   2181   1186   -243       C  
ATOM    527  O   ASN A  68      26.173  41.249  12.637  1.00 56.68           O  
ANISOU  527  O   ASN A  68    10668   6228   4640   2297   1171   -244       O  
ATOM    528  CB  ASN A  68      29.205  40.567  13.113  1.00 54.48           C  
ANISOU  528  CB  ASN A  68    10262   6005   4432   2351   1569    -50       C  
ATOM    529  CG  ASN A  68      29.429  41.672  14.121  1.00 55.30           C  
ANISOU  529  CG  ASN A  68    10141   6149   4719   2173   1660     27       C  
ATOM    530  OD1 ASN A  68      29.162  41.516  15.307  1.00 56.75           O  
ANISOU  530  OD1 ASN A  68    10165   6345   5052   1988   1577    -12       O  
ATOM    531  ND2 ASN A  68      29.905  42.808  13.652  1.00 62.64           N  
ANISOU  531  ND2 ASN A  68    11063   7097   5640   2234   1829    141       N  
ATOM    532  N   SER A  69      26.192  40.651  14.838  1.00 49.65           N  
ANISOU  532  N   SER A  69     9459   5363   4040   1975   1103   -275       N  
ATOM    533  CA  SER A  69      24.983  41.382  15.234  1.00 49.65           C  
ANISOU  533  CA  SER A  69     9390   5360   4112   1860    986   -313       C  
ATOM    534  C   SER A  69      25.291  42.871  15.439  1.00 52.30           C  
ANISOU  534  C   SER A  69     9626   5742   4502   1810   1141   -209       C  
ATOM    535  O   SER A  69      24.415  43.716  15.236  1.00 49.08           O  
ANISOU  535  O   SER A  69     9230   5331   4087   1792   1087   -219       O  
ATOM    536  CB  SER A  69      24.363  40.773  16.485  1.00 50.42           C  
ANISOU  536  CB  SER A  69     9340   5449   4366   1678    852   -377       C  
ATOM    537  OG  SER A  69      25.096  41.095  17.666  1.00 43.50           O  
ANISOU  537  OG  SER A  69     8275   4620   3631   1539    968   -311       O  
ATOM    538  N   GLY A  70      26.505  43.163  15.930  1.00 55.37           N  
ANISOU  538  N   GLY A  70     9902   6167   4966   1774   1319   -113       N  
ATOM    539  CA  GLY A  70      27.015  44.522  16.101  1.00 55.08           C  
ANISOU  539  CA  GLY A  70     9764   6164   4997   1736   1479     -3       C  
ATOM    540  C   GLY A  70      26.748  45.108  17.477  1.00 57.17           C  
ANISOU  540  C   GLY A  70     9828   6451   5442   1530   1450     -2       C  
ATOM    541  O   GLY A  70      26.897  46.314  17.658  1.00 58.18           O  
ANISOU  541  O   GLY A  70     9875   6597   5632   1486   1540     68       O  
ATOM    542  N   ASN A  71      26.347  44.271  18.445  1.00 57.22           N  
ANISOU  542  N   ASN A  71     9757   6453   5528   1413   1326    -77       N  
ATOM    543  CA  ASN A  71      26.157  44.693  19.862  1.00 57.13           C  
ANISOU  543  CA  ASN A  71     9563   6462   5680   1230   1301    -76       C  
ATOM    544  C   ASN A  71      25.911  43.444  20.712  1.00 49.27           C  
ANISOU  544  C   ASN A  71     8522   5457   4742   1151   1184   -151       C  
ATOM    545  O   ASN A  71      25.527  42.423  20.175  1.00 50.17           O  
ANISOU  545  O   ASN A  71     8743   5540   4778   1221   1088   -217       O  
ATOM    546  CB  ASN A  71      24.995  45.675  20.052  1.00 56.06           C  
ANISOU  546  CB  ASN A  71     9398   6327   5574   1160   1227    -95       C  
ATOM    547  CG  ASN A  71      23.642  45.043  19.800  1.00 60.97           C  
ANISOU  547  CG  ASN A  71    10100   6916   6150   1166   1043   -194       C  
ATOM    548  OD1 ASN A  71      22.910  44.777  20.743  1.00 60.66           O  
ANISOU  548  OD1 ASN A  71     9972   6871   6205   1049    941   -240       O  
ATOM    549  ND2 ASN A  71      23.305  44.777  18.544  1.00 61.80           N  
ANISOU  549  ND2 ASN A  71    10372   6992   6116   1308    996   -225       N  
ATOM    550  N   ALA A  72      26.090  43.556  22.032  1.00 45.36           N  
ANISOU  550  N   ALA A  72     7872   4981   4382   1010   1188   -141       N  
ATOM    551  CA  ALA A  72      26.082  42.370  22.930  1.00 44.42           C  
ANISOU  551  CA  ALA A  72     7697   4855   4325    940   1109   -193       C  
ATOM    552  C   ALA A  72      24.677  41.750  23.110  1.00 40.75           C  
ANISOU  552  C   ALA A  72     7256   4359   3867    900    935   -279       C  
ATOM    553  O   ALA A  72      24.574  40.704  23.731  1.00 36.06           O  
ANISOU  553  O   ALA A  72     6628   3751   3322    855    866   -321       O  
ATOM    554  CB  ALA A  72      26.698  42.715  24.273  1.00 39.53           C  
ANISOU  554  CB  ALA A  72     6918   4263   3838    818   1164   -154       C  
ATOM    555  N   SER A  73      23.606  42.331  22.547  1.00 39.97           N  
ANISOU  555  N   SER A  73     7214   4242   3729    920    863   -303       N  
ATOM    556  CA  SER A  73      22.238  41.855  22.861  1.00 40.25           C  
ANISOU  556  CA  SER A  73     7239   4240   3811    865    700   -372       C  
ATOM    557  C   SER A  73      22.013  40.435  22.319  1.00 38.14           C  
ANISOU  557  C   SER A  73     7067   3923   3499    933    585   -443       C  
ATOM    558  O   SER A  73      21.610  39.567  23.050  1.00 37.49           O  
ANISOU  558  O   SER A  73     6924   3818   3503    865    500   -479       O  
ATOM    559  CB  SER A  73      21.167  42.823  22.403  1.00 38.92           C  
ANISOU  559  CB  SER A  73     7101   4060   3625    869    646   -378       C  
ATOM    560  OG  SER A  73      21.025  43.911  23.327  1.00 39.05           O  
ANISOU  560  OG  SER A  73     6997   4111   3729    765    705   -332       O  
ATOM    561  N   VAL A  74      22.276  40.202  21.029  1.00 40.46           N  
ANISOU  561  N   VAL A  74     7517   4197   3659   1077    582   -461       N  
ATOM    562  CA  VAL A  74      21.978  38.920  20.435  1.00 41.72           C  
ANISOU  562  CA  VAL A  74     7784   4298   3769   1153    452   -537       C  
ATOM    563  C   VAL A  74      22.860  37.843  21.068  1.00 39.31           C  
ANISOU  563  C   VAL A  74     7429   4000   3505   1127    490   -537       C  
ATOM    564  O   VAL A  74      22.347  36.808  21.474  1.00 37.02           O  
ANISOU  564  O   VAL A  74     7115   3668   3283   1085    369   -592       O  
ATOM    565  CB  VAL A  74      22.109  38.957  18.904  1.00 44.14           C  
ANISOU  565  CB  VAL A  74     8288   4579   3902   1332    445   -557       C  
ATOM    566  CG1 VAL A  74      22.047  37.565  18.301  1.00 46.37           C  
ANISOU  566  CG1 VAL A  74     8695   4800   4122   1428    321   -637       C  
ATOM    567  CG2 VAL A  74      21.044  39.860  18.301  1.00 46.45           C  
ANISOU  567  CG2 VAL A  74     8634   4852   4160   1356    369   -573       C  
ATOM    568  N   PRO A  75      24.196  38.024  21.195  1.00 38.21           N  
ANISOU  568  N   PRO A  75     7264   3909   3342   1149    656   -470       N  
ATOM    569  CA  PRO A  75      25.016  37.039  21.903  1.00 38.01           C  
ANISOU  569  CA  PRO A  75     7177   3893   3372   1112    689   -467       C  
ATOM    570  C   PRO A  75      24.568  36.814  23.358  1.00 33.05           C  
ANISOU  570  C   PRO A  75     6389   3271   2896    954    639   -474       C  
ATOM    571  O   PRO A  75      24.667  35.702  23.852  1.00 33.65           O  
ANISOU  571  O   PRO A  75     6437   3326   3019    927    588   -505       O  
ATOM    572  CB  PRO A  75      26.461  37.568  21.874  1.00 37.40           C  
ANISOU  572  CB  PRO A  75     7072   3865   3271   1147    882   -379       C  
ATOM    573  CG  PRO A  75      26.431  38.841  21.043  1.00 37.18           C  
ANISOU  573  CG  PRO A  75     7102   3853   3171   1214    960   -330       C  
ATOM    574  CD  PRO A  75      25.003  39.097  20.600  1.00 37.55           C  
ANISOU  574  CD  PRO A  75     7213   3865   3186   1219    815   -392       C  
ATOM    575  N   ARG A  76      24.072  37.848  24.034  1.00 30.75           N  
ANISOU  575  N   ARG A  76     5999   3004   2677    860    657   -444       N  
ATOM    576  CA  ARG A  76      23.648  37.676  25.441  1.00 30.74           C  
ANISOU  576  CA  ARG A  76     5859   3011   2811    727    622   -443       C  
ATOM    577  C   ARG A  76      22.362  36.847  25.485  1.00 29.84           C  
ANISOU  577  C   ARG A  76     5754   2836   2748    704    458   -506       C  
ATOM    578  O   ARG A  76      22.226  36.019  26.348  1.00 31.80           O  
ANISOU  578  O   ARG A  76     5929   3070   3084    642    418   -517       O  
ATOM    579  CB  ARG A  76      23.464  39.013  26.165  1.00 32.46           C  
ANISOU  579  CB  ARG A  76     5979   3266   3085    644    684   -393       C  
ATOM    580  CG  ARG A  76      24.757  39.595  26.709  1.00 32.72           C  
ANISOU  580  CG  ARG A  76     5943   3349   3139    619    825   -330       C  
ATOM    581  CD  ARG A  76      24.548  40.998  27.214  1.00 33.85           C  
ANISOU  581  CD  ARG A  76     6015   3519   3326    557    873   -289       C  
ATOM    582  NE  ARG A  76      25.785  41.622  27.680  1.00 35.48           N  
ANISOU  582  NE  ARG A  76     6152   3757   3568    536    992   -230       N  
ATOM    583  CZ  ARG A  76      25.932  42.940  27.819  1.00 35.10           C  
ANISOU  583  CZ  ARG A  76     6061   3727   3546    508   1054   -186       C  
ATOM    584  NH1 ARG A  76      24.983  43.751  27.379  1.00 32.39           N  
ANISOU  584  NH1 ARG A  76     5751   3378   3175    513   1022   -191       N  
ATOM    585  NH2 ARG A  76      27.022  43.431  28.382  1.00 35.58           N  
ANISOU  585  NH2 ARG A  76     6044   3805   3667    478   1139   -137       N  
ATOM    586  N   ASN A  77      21.444  37.069  24.540  1.00 29.63           N  
ANISOU  586  N   ASN A  77     5816   2768   2674    760    362   -544       N  
ATOM    587  CA  ASN A  77      20.212  36.308  24.476  1.00 31.16           C  
ANISOU  587  CA  ASN A  77     6015   2889   2933    744    192   -603       C  
ATOM    588  C   ASN A  77      20.525  34.836  24.158  1.00 32.68           C  
ANISOU  588  C   ASN A  77     6270   3033   3112    799    117   -655       C  
ATOM    589  O   ASN A  77      19.897  33.917  24.703  1.00 32.90           O  
ANISOU  589  O   ASN A  77     6240   3010   3250    746     15   -683       O  
ATOM    590  CB  ASN A  77      19.219  36.919  23.486  1.00 31.33           C  
ANISOU  590  CB  ASN A  77     6122   2872   2908    798     97   -633       C  
ATOM    591  CG  ASN A  77      18.571  38.200  23.975  1.00 32.84           C  
ANISOU  591  CG  ASN A  77     6230   3095   3153    723    134   -589       C  
ATOM    592  OD1 ASN A  77      18.548  38.513  25.179  1.00 31.33           O  
ANISOU  592  OD1 ASN A  77     5907   2937   3058    619    196   -545       O  
ATOM    593  ND2 ASN A  77      18.083  38.983  23.024  1.00 31.88           N  
ANISOU  593  ND2 ASN A  77     6193   2961   2956    786    102   -600       N  
ATOM    594  N   THR A  78      21.478  34.613  23.244  1.00 32.46           N  
ANISOU  594  N   THR A  78     6365   3016   2951    914    171   -665       N  
ATOM    595  CA  THR A  78      21.907  33.287  22.890  1.00 33.16           C  
ANISOU  595  CA  THR A  78     6527   3063   3007    980    116   -712       C  
ATOM    596  C   THR A  78      22.419  32.569  24.147  1.00 32.28           C  
ANISOU  596  C   THR A  78     6287   2973   3004    884    164   -687       C  
ATOM    597  O   THR A  78      22.063  31.434  24.387  1.00 30.78           O  
ANISOU  597  O   THR A  78     6083   2727   2882    867     60   -729       O  
ATOM    598  CB  THR A  78      22.941  33.339  21.757  1.00 34.41           C  
ANISOU  598  CB  THR A  78     6837   3241   2996   1128    202   -707       C  
ATOM    599  OG1 THR A  78      22.371  33.951  20.597  1.00 34.86           O  
ANISOU  599  OG1 THR A  78     7025   3271   2947   1228    145   -734       O  
ATOM    600  CG2 THR A  78      23.433  31.964  21.384  1.00 34.04           C  
ANISOU  600  CG2 THR A  78     6876   3150   2905   1207    151   -757       C  
ATOM    601  N   GLY A  79      23.237  33.264  24.955  1.00 32.02           N  
ANISOU  601  N   GLY A  79     6158   3015   2993    823    317   -617       N  
ATOM    602  CA  GLY A  79      23.783  32.718  26.190  1.00 32.19           C  
ANISOU  602  CA  GLY A  79     6061   3062   3107    738    369   -588       C  
ATOM    603  C   GLY A  79      22.690  32.370  27.193  1.00 32.95           C  
ANISOU  603  C   GLY A  79     6049   3125   3344    634    278   -597       C  
ATOM    604  O   GLY A  79      22.754  31.326  27.878  1.00 29.85           O  
ANISOU  604  O   GLY A  79     5603   2710   3026    598    247   -605       O  
ATOM    605  N   LEU A  80      21.678  33.240  27.270  1.00 32.24           N  
ANISOU  605  N   LEU A  80     5926   3029   3293    593    240   -588       N  
ATOM    606  CA  LEU A  80      20.511  33.012  28.138  1.00 33.65           C  
ANISOU  606  CA  LEU A  80     6003   3170   3612    506    160   -583       C  
ATOM    607  C   LEU A  80      19.775  31.711  27.758  1.00 33.56           C  
ANISOU  607  C   LEU A  80     6020   3064   3664    528      4   -640       C  
ATOM    608  O   LEU A  80      19.421  30.925  28.641  1.00 31.59           O  
ANISOU  608  O   LEU A  80     5679   2784   3536    468    -27   -628       O  
ATOM    609  CB  LEU A  80      19.586  34.234  28.081  1.00 33.68           C  
ANISOU  609  CB  LEU A  80     5984   3180   3634    476    149   -563       C  
ATOM    610  CG  LEU A  80      19.988  35.411  28.973  1.00 32.41           C  
ANISOU  610  CG  LEU A  80     5743   3094   3476    416    281   -500       C  
ATOM    611  CD1 LEU A  80      19.035  36.570  28.763  1.00 32.97           C  
ANISOU  611  CD1 LEU A  80     5806   3164   3555    398    261   -487       C  
ATOM    612  CD2 LEU A  80      20.020  35.029  30.448  1.00 32.10           C  
ANISOU  612  CD2 LEU A  80     5585   3070   3540    335    320   -463       C  
ATOM    613  N   LYS A  81      19.560  31.475  26.462  1.00 34.42           N  
ANISOU  613  N   LYS A  81     6259   3123   3694    621    -94   -701       N  
ATOM    614  CA  LYS A  81      18.866  30.270  25.988  1.00 37.05           C  
ANISOU  614  CA  LYS A  81     6633   3354   4089    653   -267   -765       C  
ATOM    615  C   LYS A  81      19.696  29.005  26.269  1.00 34.90           C  
ANISOU  615  C   LYS A  81     6365   3071   3822    667   -254   -781       C  
ATOM    616  O   LYS A  81      19.142  27.939  26.481  1.00 35.11           O  
ANISOU  616  O   LYS A  81     6358   3020   3962    646   -368   -809       O  
ATOM    617  CB  LYS A  81      18.533  30.384  24.498  1.00 42.00           C  
ANISOU  617  CB  LYS A  81     7421   3930   4607    766   -380   -833       C  
ATOM    618  CG  LYS A  81      17.461  31.416  24.190  1.00 46.35           C  
ANISOU  618  CG  LYS A  81     7964   4465   5180    750   -437   -829       C  
ATOM    619  CD  LYS A  81      17.235  31.665  22.717  1.00 56.33           C  
ANISOU  619  CD  LYS A  81     9400   5688   6312    875   -535   -892       C  
ATOM    620  CE  LYS A  81      18.369  32.440  22.073  1.00 61.98           C  
ANISOU  620  CE  LYS A  81    10224   6488   6837    964   -382   -868       C  
ATOM    621  NZ  LYS A  81      17.886  33.615  21.312  1.00 60.91           N  
ANISOU  621  NZ  LYS A  81    10157   6364   6621   1012   -388   -865       N  
ATOM    622  N   MET A  82      21.021  29.135  26.316  1.00 34.27           N  
ANISOU  622  N   MET A  82     6316   3066   3637    700   -112   -755       N  
ATOM    623  CA  MET A  82      21.914  28.018  26.535  1.00 35.44           C  
ANISOU  623  CA  MET A  82     6474   3213   3778    721    -86   -766       C  
ATOM    624  C   MET A  82      22.061  27.682  28.029  1.00 36.13           C  
ANISOU  624  C   MET A  82     6408   3328   3990    613    -20   -713       C  
ATOM    625  O   MET A  82      22.450  26.571  28.356  1.00 35.22           O  
ANISOU  625  O   MET A  82     6279   3190   3914    613    -36   -724       O  
ATOM    626  CB  MET A  82      23.299  28.316  25.954  1.00 37.87           C  
ANISOU  626  CB  MET A  82     6872   3586   3931    807     46   -751       C  
ATOM    627  CG  MET A  82      23.319  28.258  24.446  1.00 38.34           C  
ANISOU  627  CG  MET A  82     7110   3606   3850    946    -16   -807       C  
ATOM    628  SD  MET A  82      24.845  28.936  23.743  1.00 40.43           S  
ANISOU  628  SD  MET A  82     7468   3951   3942   1053    173   -759       S  
ATOM    629  CE  MET A  82      26.082  27.813  24.400  1.00 42.55           C  
ANISOU  629  CE  MET A  82     7691   4239   4234   1045    255   -740       C  
ATOM    630  N   SER A  83      21.771  28.626  28.928  1.00 32.38           N  
ANISOU  630  N   SER A  83     5828   2903   3571    531     52   -655       N  
ATOM    631  CA  SER A  83      21.984  28.419  30.351  1.00 33.95           C  
ANISOU  631  CA  SER A  83     5900   3134   3863    447    125   -601       C  
ATOM    632  C   SER A  83      20.764  27.753  31.005  1.00 37.58           C  
ANISOU  632  C   SER A  83     6270   3522   4484    388     28   -594       C  
ATOM    633  O   SER A  83      19.624  28.124  30.724  1.00 38.93           O  
ANISOU  633  O   SER A  83     6429   3646   4714    373    -54   -599       O  
ATOM    634  CB  SER A  83      22.288  29.705  31.045  1.00 33.64           C  
ANISOU  634  CB  SER A  83     5802   3175   3804    400    245   -545       C  
ATOM    635  OG  SER A  83      22.375  29.483  32.440  1.00 32.94           O  
ANISOU  635  OG  SER A  83     5604   3109   3801    331    299   -498       O  
ATOM    636  N   LYS A  84      21.025  26.808  31.915  1.00 39.03           N  
ANISOU  636  N   LYS A  84     6385   3697   4746    354     48   -571       N  
ATOM    637  CA  LYS A  84      19.984  26.194  32.752  1.00 40.87           C  
ANISOU  637  CA  LYS A  84     6511   3867   5148    295     -6   -538       C  
ATOM    638  C   LYS A  84      20.399  26.300  34.226  1.00 38.42           C  
ANISOU  638  C   LYS A  84     6104   3618   4875    242    117   -468       C  
ATOM    639  O   LYS A  84      19.923  25.538  35.079  1.00 34.80           O  
ANISOU  639  O   LYS A  84     5561   3119   4541    208    107   -429       O  
ATOM    640  CB  LYS A  84      19.726  24.742  32.316  1.00 45.93           C  
ANISOU  640  CB  LYS A  84     7174   4412   5866    321   -131   -584       C  
ATOM    641  CG  LYS A  84      19.151  24.569  30.915  1.00 48.69           C  
ANISOU  641  CG  LYS A  84     7625   4682   6193    381   -284   -661       C  
ATOM    642  CD  LYS A  84      17.839  25.293  30.684  1.00 53.36           C  
ANISOU  642  CD  LYS A  84     8183   5228   6864    355   -363   -652       C  
ATOM    643  N   ALA A  85      21.234  27.295  34.541  1.00 34.23           N  
ANISOU  643  N   ALA A  85     5583   3178   4243    240    230   -446       N  
ATOM    644  CA  ALA A  85      21.762  27.435  35.890  1.00 31.81           C  
ANISOU  644  CA  ALA A  85     5205   2927   3951    204    336   -391       C  
ATOM    645  C   ALA A  85      20.769  28.224  36.756  1.00 30.60           C  
ANISOU  645  C   ALA A  85     4978   2779   3869    160    363   -334       C  
ATOM    646  O   ALA A  85      19.767  28.761  36.274  1.00 29.57           O  
ANISOU  646  O   ALA A  85     4845   2615   3772    153    310   -336       O  
ATOM    647  CB  ALA A  85      23.137  28.055  35.862  1.00 31.36           C  
ANISOU  647  CB  ALA A  85     5189   2951   3775    223    428   -396       C  
ATOM    648  N   GLU A  86      21.021  28.202  38.066  1.00 29.32           N  
ANISOU  648  N   GLU A  86     4756   2651   3733    139    442   -282       N  
ATOM    649  CA  GLU A  86      20.218  28.930  39.050  1.00 28.63           C  
ANISOU  649  CA  GLU A  86     4607   2574   3697    113    489   -220       C  
ATOM    650  C   GLU A  86      20.341  30.446  38.802  1.00 26.00           C  
ANISOU  650  C   GLU A  86     4307   2295   3275    110    526   -227       C  
ATOM    651  O   GLU A  86      19.374  31.196  38.939  1.00 26.23           O  
ANISOU  651  O   GLU A  86     4310   2313   3341     95    524   -198       O  
ATOM    652  CB  GLU A  86      20.697  28.571  40.462  1.00 29.69           C  
ANISOU  652  CB  GLU A  86     4698   2738   3843    113    569   -171       C  
ATOM    653  CG  GLU A  86      19.743  28.979  41.573  1.00 32.45           C  
ANISOU  653  CG  GLU A  86     4987   3081   4260    106    619    -96       C  
ATOM    654  CD  GLU A  86      20.108  28.546  42.995  1.00 36.19           C  
ANISOU  654  CD  GLU A  86     5431   3576   4742    124    696    -43       C  
ATOM    655  OE1 GLU A  86      21.098  27.796  43.173  1.00 35.40           O  
ANISOU  655  OE1 GLU A  86     5346   3492   4609    135    704    -64       O  
ATOM    656  OE2 GLU A  86      19.396  28.986  43.931  1.00 37.52           O  
ANISOU  656  OE2 GLU A  86     5566   3745   4945    135    750     21       O  
ATOM    657  N   TYR A  87      21.557  30.883  38.498  1.00 23.94           N  
ANISOU  657  N   TYR A  87     4096   2090   2910    124    564   -258       N  
ATOM    658  CA  TYR A  87      21.882  32.302  38.299  1.00 23.48           C  
ANISOU  658  CA  TYR A  87     4065   2082   2775    122    606   -261       C  
ATOM    659  C   TYR A  87      22.731  32.446  37.036  1.00 24.41           C  
ANISOU  659  C   TYR A  87     4253   2214   2809    152    597   -308       C  
ATOM    660  O   TYR A  87      23.432  31.517  36.655  1.00 22.58           O  
ANISOU  660  O   TYR A  87     4047   1972   2559    177    586   -332       O  
ATOM    661  CB  TYR A  87      22.709  32.862  39.459  1.00 22.49           C  
ANISOU  661  CB  TYR A  87     3917   2010   2616    115    683   -235       C  
ATOM    662  CG  TYR A  87      21.966  33.083  40.749  1.00 22.37           C  
ANISOU  662  CG  TYR A  87     3855   1993   2649    104    712   -184       C  
ATOM    663  CD1 TYR A  87      21.322  34.278  41.004  1.00 23.38           C  
ANISOU  663  CD1 TYR A  87     3979   2134   2769     95    731   -162       C  
ATOM    664  CD2 TYR A  87      21.938  32.113  41.733  1.00 24.22           C  
ANISOU  664  CD2 TYR A  87     4054   2214   2932    112    729   -153       C  
ATOM    665  CE1 TYR A  87      20.658  34.511  42.199  1.00 23.97           C  
ANISOU  665  CE1 TYR A  87     4022   2208   2877    101    768   -111       C  
ATOM    666  CE2 TYR A  87      21.261  32.317  42.923  1.00 24.33           C  
ANISOU  666  CE2 TYR A  87     4036   2226   2982    120    769    -97       C  
ATOM    667  CZ  TYR A  87      20.633  33.522  43.168  1.00 25.04           C  
ANISOU  667  CZ  TYR A  87     4128   2330   3056    118    791    -76       C  
ATOM    668  OH  TYR A  87      19.976  33.742  44.351  1.00 25.74           O  
ANISOU  668  OH  TYR A  87     4195   2415   3169    140    840    -16       O  
ATOM    669  N   VAL A  88      22.678  33.637  36.424  1.00 24.53           N  
ANISOU  669  N   VAL A  88     4299   2251   2771    156    612   -313       N  
ATOM    670  CA  VAL A  88      23.559  33.985  35.334  1.00 23.23           C  
ANISOU  670  CA  VAL A  88     4197   2105   2522    194    632   -338       C  
ATOM    671  C   VAL A  88      24.338  35.227  35.763  1.00 23.56           C  
ANISOU  671  C   VAL A  88     4221   2199   2531    179    710   -312       C  
ATOM    672  O   VAL A  88      23.890  35.982  36.637  1.00 25.23           O  
ANISOU  672  O   VAL A  88     4391   2425   2771    145    726   -287       O  
ATOM    673  CB  VAL A  88      22.811  34.188  34.002  1.00 24.71           C  
ANISOU  673  CB  VAL A  88     4451   2258   2677    228    569   -368       C  
ATOM    674  CG1 VAL A  88      22.149  32.906  33.512  1.00 25.57           C  
ANISOU  674  CG1 VAL A  88     4583   2302   2827    248    471   -403       C  
ATOM    675  CG2 VAL A  88      21.812  35.331  34.041  1.00 25.82           C  
ANISOU  675  CG2 VAL A  88     4574   2400   2834    202    559   -351       C  
ATOM    676  N   PHE A  89      25.543  35.370  35.208  1.00 23.97           N  
ANISOU  676  N   PHE A  89     4301   2274   2532    210    759   -315       N  
ATOM    677  CA  PHE A  89      26.421  36.461  35.452  1.00 23.50           C  
ANISOU  677  CA  PHE A  89     4218   2249   2459    200    826   -289       C  
ATOM    678  C   PHE A  89      27.021  36.892  34.107  1.00 24.67           C  
ANISOU  678  C   PHE A  89     4423   2401   2547    252    865   -287       C  
ATOM    679  O   PHE A  89      27.657  36.075  33.415  1.00 23.46           O  
ANISOU  679  O   PHE A  89     4312   2240   2361    300    877   -298       O  
ATOM    680  CB  PHE A  89      27.541  36.062  36.413  1.00 25.38           C  
ANISOU  680  CB  PHE A  89     4410   2506   2728    187    861   -276       C  
ATOM    681  CG  PHE A  89      28.315  37.248  36.911  1.00 26.09           C  
ANISOU  681  CG  PHE A  89     4460   2618   2833    166    906   -251       C  
ATOM    682  CD1 PHE A  89      29.197  37.932  36.068  1.00 29.12           C  
ANISOU  682  CD1 PHE A  89     4853   3009   3202    191    960   -231       C  
ATOM    683  CD2 PHE A  89      28.037  37.788  38.156  1.00 27.82           C  
ANISOU  683  CD2 PHE A  89     4640   2845   3085    130    893   -243       C  
ATOM    684  CE1 PHE A  89      29.840  39.081  36.501  1.00 27.05           C  
ANISOU  684  CE1 PHE A  89     4545   2754   2976    168    992   -206       C  
ATOM    685  CE2 PHE A  89      28.697  38.926  38.591  1.00 27.86           C  
ANISOU  685  CE2 PHE A  89     4614   2859   3110    114    915   -227       C  
ATOM    686  CZ  PHE A  89      29.583  39.574  37.766  1.00 27.39           C  
ANISOU  686  CZ  PHE A  89     4550   2801   3055    127    960   -209       C  
ATOM    687  N   PHE A  90      26.782  38.154  33.732  1.00 25.65           N  
ANISOU  687  N   PHE A  90     4555   2535   2654    249    889   -270       N  
ATOM    688  CA  PHE A  90      27.242  38.679  32.439  1.00 25.42           C  
ANISOU  688  CA  PHE A  90     4584   2508   2566    307    937   -257       C  
ATOM    689  C   PHE A  90      28.637  39.268  32.653  1.00 26.16           C  
ANISOU  689  C   PHE A  90     4630   2621   2687    307   1025   -214       C  
ATOM    690  O   PHE A  90      28.792  40.119  33.554  1.00 27.47           O  
ANISOU  690  O   PHE A  90     4730   2797   2908    254   1035   -195       O  
ATOM    691  CB  PHE A  90      26.266  39.710  31.859  1.00 25.49           C  
ANISOU  691  CB  PHE A  90     4625   2512   2547    310    919   -257       C  
ATOM    692  CG  PHE A  90      24.924  39.136  31.498  1.00 24.92           C  
ANISOU  692  CG  PHE A  90     4596   2408   2461    317    824   -297       C  
ATOM    693  CD1 PHE A  90      24.768  38.341  30.375  1.00 27.19           C  
ANISOU  693  CD1 PHE A  90     4971   2668   2689    386    782   -330       C  
ATOM    694  CD2 PHE A  90      23.836  39.317  32.332  1.00 25.48           C  
ANISOU  694  CD2 PHE A  90     4619   2471   2588    260    772   -301       C  
ATOM    695  CE1 PHE A  90      23.541  37.774  30.067  1.00 27.02           C  
ANISOU  695  CE1 PHE A  90     4984   2605   2677    391    675   -370       C  
ATOM    696  CE2 PHE A  90      22.614  38.731  32.030  1.00 26.35           C  
ANISOU  696  CE2 PHE A  90     4754   2542   2715    263    681   -330       C  
ATOM    697  CZ  PHE A  90      22.465  37.973  30.898  1.00 25.90           C  
ANISOU  697  CZ  PHE A  90     4777   2451   2611    325    625   -367       C  
ATOM    698  N   LEU A  91      29.616  38.760  31.888  1.00 24.57           N  
ANISOU  698  N   LEU A  91     4460   2417   2456    368   1080   -197       N  
ATOM    699  CA  LEU A  91      30.992  39.198  31.885  1.00 26.35           C  
ANISOU  699  CA  LEU A  91     4638   2651   2723    380   1170   -145       C  
ATOM    700  C   LEU A  91      31.300  39.789  30.501  1.00 27.38           C  
ANISOU  700  C   LEU A  91     4829   2776   2796    460   1247   -106       C  
ATOM    701  O   LEU A  91      31.071  39.117  29.458  1.00 27.92           O  
ANISOU  701  O   LEU A  91     4995   2835   2776    539   1245   -124       O  
ATOM    702  CB  LEU A  91      31.910  38.022  32.211  1.00 27.49           C  
ANISOU  702  CB  LEU A  91     4762   2793   2887    394   1182   -146       C  
ATOM    703  CG  LEU A  91      33.412  38.273  32.077  1.00 29.77           C  
ANISOU  703  CG  LEU A  91     5000   3081   3230    419   1278    -86       C  
ATOM    704  CD1 LEU A  91      33.903  39.283  33.094  1.00 30.71           C  
ANISOU  704  CD1 LEU A  91     5015   3199   3452    349   1281    -58       C  
ATOM    705  CD2 LEU A  91      34.208  36.983  32.213  1.00 32.13           C  
ANISOU  705  CD2 LEU A  91     5295   3377   3533    445   1289    -90       C  
ATOM    706  N   ASP A  92      31.811  41.029  30.484  1.00 26.58           N  
ANISOU  706  N   ASP A  92     4676   2676   2746    447   1313    -51       N  
ATOM    707  CA  ASP A  92      32.360  41.638  29.236  1.00 30.24           C  
ANISOU  707  CA  ASP A  92     5182   3133   3174    530   1417      9       C  
ATOM    708  C   ASP A  92      33.776  41.118  28.998  1.00 29.37           C  
ANISOU  708  C   ASP A  92     5042   3015   3100    580   1510     63       C  
ATOM    709  O   ASP A  92      34.590  41.013  29.918  1.00 28.20           O  
ANISOU  709  O   ASP A  92     4797   2863   3053    527   1514     80       O  
ATOM    710  CB  ASP A  92      32.335  43.164  29.294  1.00 34.30           C  
ANISOU  710  CB  ASP A  92     5643   3643   3744    497   1454     53       C  
ATOM    711  CG  ASP A  92      30.937  43.747  29.196  1.00 40.10           C  
ANISOU  711  CG  ASP A  92     6425   4384   4425    474   1384     12       C  
ATOM    712  OD1 ASP A  92      29.987  42.971  28.910  1.00 47.81           O  
ANISOU  712  OD1 ASP A  92     7479   5362   5321    494   1310    -45       O  
ATOM    713  OD2 ASP A  92      30.803  44.982  29.385  1.00 51.33           O  
ANISOU  713  OD2 ASP A  92     7803   5803   5895    437   1401     40       O  
ATOM    714  N   SER A  93      34.080  40.829  27.726  1.00 31.68           N  
ANISOU  714  N   SER A  93     5426   3303   3308    694   1587     95       N  
ATOM    715  CA  SER A  93      35.252  40.092  27.345  1.00 36.58           C  
ANISOU  715  CA  SER A  93     6048   3915   3935    764   1675    141       C  
ATOM    716  C   SER A  93      36.570  40.820  27.667  1.00 37.00           C  
ANISOU  716  C   SER A  93     5973   3953   4130    744   1780    236       C  
ATOM    717  O   SER A  93      37.593  40.172  27.753  1.00 45.63           O  
ANISOU  717  O   SER A  93     7028   5037   5270    770   1834    273       O  
ATOM    718  CB  SER A  93      35.171  39.687  25.872  1.00 39.73           C  
ANISOU  718  CB  SER A  93     6593   4308   4194    907   1734    153       C  
ATOM    719  OG  SER A  93      34.521  40.697  25.123  1.00 42.90           O  
ANISOU  719  OG  SER A  93     7052   4709   4538    944   1753    170       O  
ATOM    720  N   ASP A  94      36.595  42.135  27.865  1.00 37.90           N  
ANISOU  720  N   ASP A  94     6016   4057   4327    697   1804    280       N  
ATOM    721  CA  ASP A  94      37.897  42.739  28.281  1.00 42.15           C  
ANISOU  721  CA  ASP A  94     6416   4567   5032    669   1882    368       C  
ATOM    722  C   ASP A  94      38.192  42.521  29.789  1.00 40.40           C  
ANISOU  722  C   ASP A  94     6085   4340   4926    557   1783    325       C  
ATOM    723  O   ASP A  94      39.344  42.611  30.246  1.00 38.26           O  
ANISOU  723  O   ASP A  94     5703   4040   4793    536   1819    380       O  
ATOM    724  CB  ASP A  94      37.927  44.210  27.858  1.00 48.52           C  
ANISOU  724  CB  ASP A  94     7182   5352   5898    672   1950    439       C  
ATOM    725  CG  ASP A  94      37.916  44.393  26.340  1.00 51.68           C  
ANISOU  725  CG  ASP A  94     7687   5753   6195    805   2075    504       C  
ATOM    726  OD1 ASP A  94      38.449  43.497  25.637  1.00 53.37           O  
ANISOU  726  OD1 ASP A  94     7964   5968   6343    905   2151    532       O  
ATOM    727  OD2 ASP A  94      37.341  45.407  25.872  1.00 56.26           O  
ANISOU  727  OD2 ASP A  94     8294   6331   6750    815   2094    523       O  
ATOM    728  N   ASP A  95      37.171  42.168  30.566  1.00 34.67           N  
ANISOU  728  N   ASP A  95     5391   3637   4143    493   1657    230       N  
ATOM    729  CA  ASP A  95      37.156  42.401  32.029  1.00 31.48           C  
ANISOU  729  CA  ASP A  95     4900   3228   3833    390   1556    189       C  
ATOM    730  C   ASP A  95      37.666  41.164  32.783  1.00 32.28           C  
ANISOU  730  C   ASP A  95     4978   3334   3953    374   1514    156       C  
ATOM    731  O   ASP A  95      38.015  40.142  32.171  1.00 30.31           O  
ANISOU  731  O   ASP A  95     4775   3091   3647    438   1561    164       O  
ATOM    732  CB  ASP A  95      35.765  42.872  32.426  1.00 29.68           C  
ANISOU  732  CB  ASP A  95     4718   3018   3541    341   1466    123       C  
ATOM    733  CG  ASP A  95      35.347  44.203  31.808  1.00 29.21           C  
ANISOU  733  CG  ASP A  95     4666   2949   3481    348   1504    158       C  
ATOM    734  OD1 ASP A  95      36.225  44.939  31.339  1.00 32.28           O  
ANISOU  734  OD1 ASP A  95     4999   3311   3952    371   1592    237       O  
ATOM    735  OD2 ASP A  95      34.151  44.480  31.779  1.00 28.34           O  
ANISOU  735  OD2 ASP A  95     4614   2856   3295    332   1450    112       O  
ATOM    736  N   LEU A  96      37.752  41.275  34.115  1.00 29.37           N  
ANISOU  736  N   LEU A  96     4541   2958   3659    298   1425    121       N  
ATOM    737  CA  LEU A  96      38.332  40.240  34.943  1.00 30.31           C  
ANISOU  737  CA  LEU A  96     4627   3078   3811    282   1383     97       C  
ATOM    738  C   LEU A  96      37.397  39.984  36.121  1.00 30.54           C  
ANISOU  738  C   LEU A  96     4678   3125   3801    225   1268     18       C  
ATOM    739  O   LEU A  96      36.790  40.927  36.623  1.00 29.58           O  
ANISOU  739  O   LEU A  96     4548   2999   3689    184   1219      0       O  
ATOM    740  CB  LEU A  96      39.709  40.689  35.438  1.00 32.26           C  
ANISOU  740  CB  LEU A  96     4754   3283   4219    260   1400    152       C  
ATOM    741  CG  LEU A  96      40.741  41.054  34.375  1.00 33.97           C  
ANISOU  741  CG  LEU A  96     4923   3470   4511    316   1528    251       C  
ATOM    742  CD1 LEU A  96      41.938  41.723  35.027  1.00 37.24           C  
ANISOU  742  CD1 LEU A  96     5199   3829   5119    276   1517    303       C  
ATOM    743  CD2 LEU A  96      41.192  39.826  33.594  1.00 34.59           C  
ANISOU  743  CD2 LEU A  96     5051   3565   4525    393   1609    274       C  
ATOM    744  N   LEU A  97      37.275  38.710  36.532  1.00 28.74           N  
ANISOU  744  N   LEU A  97     4479   2914   3526    231   1232    -20       N  
ATOM    745  CA  LEU A  97      36.685  38.380  37.800  1.00 27.13           C  
ANISOU  745  CA  LEU A  97     4277   2720   3310    187   1139    -76       C  
ATOM    746  C   LEU A  97      37.786  38.146  38.840  1.00 26.79           C  
ANISOU  746  C   LEU A  97     4160   2658   3361    167   1104    -71       C  
ATOM    747  O   LEU A  97      38.738  37.447  38.588  1.00 26.38           O  
ANISOU  747  O   LEU A  97     4078   2598   3345    192   1143    -45       O  
ATOM    748  CB  LEU A  97      35.828  37.127  37.674  1.00 28.08           C  
ANISOU  748  CB  LEU A  97     4469   2862   3335    206   1117   -117       C  
ATOM    749  CG  LEU A  97      34.599  37.211  36.776  1.00 28.56           C  
ANISOU  749  CG  LEU A  97     4608   2934   3309    225   1120   -135       C  
ATOM    750  CD1 LEU A  97      33.825  35.899  36.874  1.00 30.59           C  
ANISOU  750  CD1 LEU A  97     4916   3197   3507    236   1077   -177       C  
ATOM    751  CD2 LEU A  97      33.720  38.399  37.129  1.00 29.66           C  
ANISOU  751  CD2 LEU A  97     4746   3075   3448    188   1087   -143       C  
ATOM    752  N   HIS A  98      37.587  38.711  40.039  1.00 25.62           N  
ANISOU  752  N   HIS A  98     3989   2500   3244    128   1023   -100       N  
ATOM    753  CA  HIS A  98      38.316  38.321  41.230  1.00 25.84           C  
ANISOU  753  CA  HIS A  98     3975   2512   3330    115    959   -117       C  
ATOM    754  C   HIS A  98      38.096  36.817  41.441  1.00 25.65           C  
ANISOU  754  C   HIS A  98     3991   2514   3239    136    957   -141       C  
ATOM    755  O   HIS A  98      37.013  36.308  41.099  1.00 24.86           O  
ANISOU  755  O   HIS A  98     3957   2440   3049    145    968   -162       O  
ATOM    756  CB  HIS A  98      37.800  39.107  42.447  1.00 25.73           C  
ANISOU  756  CB  HIS A  98     3970   2488   3316     89    867   -156       C  
ATOM    757  CG  HIS A  98      38.663  39.010  43.662  1.00 26.80           C  
ANISOU  757  CG  HIS A  98     4066   2595   3520     85    786   -174       C  
ATOM    758  ND1 HIS A  98      38.636  37.905  44.506  1.00 25.97           N  
ANISOU  758  ND1 HIS A  98     3989   2506   3372    103    750   -203       N  
ATOM    759  CD2 HIS A  98      39.539  39.879  44.206  1.00 27.72           C  
ANISOU  759  CD2 HIS A  98     4122   2662   3748     70    724   -171       C  
ATOM    760  CE1 HIS A  98      39.470  38.105  45.507  1.00 27.51           C  
ANISOU  760  CE1 HIS A  98     4149   2667   3637    103    670   -218       C  
ATOM    761  NE2 HIS A  98      40.047  39.300  45.342  1.00 27.76           N  
ANISOU  761  NE2 HIS A  98     4124   2654   3769     82    646   -201       N  
ATOM    762  N   GLU A  99      39.085  36.120  42.014  1.00 26.76           N  
ANISOU  762  N   GLU A  99     4090   2643   3433    142    938   -138       N  
ATOM    763  CA  GLU A  99      38.978  34.653  42.200  1.00 29.80           C  
ANISOU  763  CA  GLU A  99     4508   3049   3765    164    941   -156       C  
ATOM    764  C   GLU A  99      37.806  34.278  43.128  1.00 28.16           C  
ANISOU  764  C   GLU A  99     4357   2860   3481    158    885   -199       C  
ATOM    765  O   GLU A  99      37.275  33.154  43.003  1.00 25.00           O  
ANISOU  765  O   GLU A  99     3995   2476   3025    174    898   -210       O  
ATOM    766  CB  GLU A  99      40.299  34.040  42.687  1.00 34.45           C  
ANISOU  766  CB  GLU A  99     5038   3619   4431    173    929   -142       C  
ATOM    767  CG  GLU A  99      40.690  34.436  44.095  1.00 38.88           C  
ANISOU  767  CG  GLU A  99     5568   4158   5044    156    833   -166       C  
ATOM    768  CD  GLU A  99      42.062  33.940  44.546  1.00 48.48           C  
ANISOU  768  CD  GLU A  99     6717   5347   6355    164    809   -151       C  
ATOM    769  OE1 GLU A  99      42.637  33.056  43.867  1.00 58.67           O  
ANISOU  769  OE1 GLU A  99     7990   6644   7657    185    875   -122       O  
ATOM    770  OE2 GLU A  99      42.566  34.435  45.582  1.00 53.89           O  
ANISOU  770  OE2 GLU A  99     7371   6001   7103    155    719   -169       O  
ATOM    771  N   ARG A 100      37.379  35.186  44.020  1.00 25.21           N  
ANISOU  771  N   ARG A 100     3989   2479   3108    142    828   -217       N  
ATOM    772  CA  ARG A 100      36.324  34.886  45.004  1.00 26.27           C  
ANISOU  772  CA  ARG A 100     4176   2629   3177    150    787   -244       C  
ATOM    773  C   ARG A 100      34.923  35.270  44.500  1.00 26.11           C  
ANISOU  773  C   ARG A 100     4200   2623   3096    142    810   -245       C  
ATOM    774  O   ARG A 100      33.952  35.041  45.183  1.00 25.31           O  
ANISOU  774  O   ARG A 100     4136   2530   2950    151    793   -254       O  
ATOM    775  CB  ARG A 100      36.623  35.560  46.340  1.00 27.58           C  
ANISOU  775  CB  ARG A 100     4340   2776   3362    155    710   -264       C  
ATOM    776  CG  ARG A 100      37.880  35.036  47.010  1.00 31.14           C  
ANISOU  776  CG  ARG A 100     4753   3208   3869    169    668   -268       C  
ATOM    777  CD  ARG A 100      38.201  35.676  48.348  1.00 32.67           C  
ANISOU  777  CD  ARG A 100     4960   3375   4078    187    572   -297       C  
ATOM    778  NE  ARG A 100      37.114  35.499  49.296  1.00 37.45           N  
ANISOU  778  NE  ARG A 100     5641   3997   4588    221    554   -314       N  
ATOM    779  CZ  ARG A 100      36.956  34.437  50.082  1.00 40.73           C  
ANISOU  779  CZ  ARG A 100     6092   4426   4955    260    550   -317       C  
ATOM    780  NH1 ARG A 100      37.912  33.527  50.173  1.00 44.05           N  
ANISOU  780  NH1 ARG A 100     6480   4842   5413    266    543   -314       N  
ATOM    781  NH2 ARG A 100      35.818  34.257  50.724  1.00 38.65           N  
ANISOU  781  NH2 ARG A 100     5892   4179   4611    294    564   -314       N  
ATOM    782  N   ALA A 101      34.814  35.803  43.276  1.00 25.08           N  
ANISOU  782  N   ALA A 101     4066   2492   2968    131    853   -231       N  
ATOM    783  CA  ALA A 101      33.586  36.458  42.830  1.00 23.72           C  
ANISOU  783  CA  ALA A 101     3930   2328   2752    121    862   -233       C  
ATOM    784  C   ALA A 101      32.388  35.513  42.803  1.00 23.55           C  
ANISOU  784  C   ALA A 101     3950   2317   2680    130    862   -241       C  
ATOM    785  O   ALA A 101      31.379  35.833  43.384  1.00 22.54           O  
ANISOU  785  O   ALA A 101     3842   2190   2529    127    843   -244       O  
ATOM    786  CB  ALA A 101      33.772  37.087  41.471  1.00 24.39           C  
ANISOU  786  CB  ALA A 101     4010   2410   2844    120    911   -214       C  
ATOM    787  N   LEU A 102      32.453  34.392  42.069  1.00 22.81           N  
ANISOU  787  N   LEU A 102     3868   2223   2575    145    883   -242       N  
ATOM    788  CA  LEU A 102      31.247  33.589  41.906  1.00 22.86           C  
ANISOU  788  CA  LEU A 102     3906   2225   2555    150    872   -249       C  
ATOM    789  C   LEU A 102      30.816  33.005  43.260  1.00 22.84           C  
ANISOU  789  C   LEU A 102     3896   2221   2559    154    849   -245       C  
ATOM    790  O   LEU A 102      29.629  33.050  43.598  1.00 20.73           O  
ANISOU  790  O   LEU A 102     3642   1947   2287    151    840   -236       O  
ATOM    791  CB  LEU A 102      31.446  32.488  40.868  1.00 23.72           C  
ANISOU  791  CB  LEU A 102     4034   2324   2652    171    885   -258       C  
ATOM    792  CG  LEU A 102      31.782  32.973  39.452  1.00 23.82           C  
ANISOU  792  CG  LEU A 102     4072   2335   2641    189    918   -257       C  
ATOM    793  CD1 LEU A 102      31.786  31.810  38.474  1.00 25.06           C  
ANISOU  793  CD1 LEU A 102     4272   2477   2771    226    919   -272       C  
ATOM    794  CD2 LEU A 102      30.801  34.037  38.999  1.00 23.40           C  
ANISOU  794  CD2 LEU A 102     4040   2282   2567    177    910   -257       C  
ATOM    795  N   GLU A 103      31.781  32.493  44.016  1.00 25.19           N  
ANISOU  795  N   GLU A 103     4175   2522   2872    165    844   -246       N  
ATOM    796  CA  GLU A 103      31.494  31.839  45.310  1.00 27.86           C  
ANISOU  796  CA  GLU A 103     4517   2859   3208    184    829   -237       C  
ATOM    797  C   GLU A 103      30.879  32.853  46.291  1.00 26.65           C  
ANISOU  797  C   GLU A 103     4380   2708   3035    192    814   -230       C  
ATOM    798  O   GLU A 103      29.869  32.578  46.936  1.00 27.13           O  
ANISOU  798  O   GLU A 103     4457   2765   3085    210    822   -209       O  
ATOM    799  CB  GLU A 103      32.768  31.204  45.875  1.00 32.22           C  
ANISOU  799  CB  GLU A 103     5050   3414   3777    200    820   -242       C  
ATOM    800  CG  GLU A 103      32.569  30.365  47.151  1.00 33.65           C  
ANISOU  800  CG  GLU A 103     5241   3593   3949    231    810   -231       C  
ATOM    801  CD  GLU A 103      31.904  28.985  47.072  1.00 38.96           C  
ANISOU  801  CD  GLU A 103     5915   4254   4632    241    829   -214       C  
ATOM    802  OE1 GLU A 103      31.671  28.408  48.159  1.00 46.55           O  
ANISOU  802  OE1 GLU A 103     6885   5212   5588    272    832   -194       O  
ATOM    803  OE2 GLU A 103      31.568  28.481  45.958  1.00 37.72           O  
ANISOU  803  OE2 GLU A 103     5755   4085   4489    224    839   -220       O  
ATOM    804  N   ASP A 104      31.517  34.013  46.449  1.00 24.73           N  
ANISOU  804  N   ASP A 104     4133   2468   2794    185    794   -243       N  
ATOM    805  CA  ASP A 104      31.067  35.014  47.437  1.00 25.45           C  
ANISOU  805  CA  ASP A 104     4252   2557   2859    202    770   -244       C  
ATOM    806  C   ASP A 104      29.683  35.582  47.059  1.00 24.69           C  
ANISOU  806  C   ASP A 104     4174   2462   2745    193    793   -228       C  
ATOM    807  O   ASP A 104      28.811  35.769  47.939  1.00 24.15           O  
ANISOU  807  O   ASP A 104     4135   2392   2649    223    798   -210       O  
ATOM    808  CB  ASP A 104      32.105  36.116  47.653  1.00 24.24           C  
ANISOU  808  CB  ASP A 104     4086   2393   2728    195    727   -265       C  
ATOM    809  CG  ASP A 104      33.309  35.682  48.479  1.00 27.90           C  
ANISOU  809  CG  ASP A 104     4538   2846   3213    217    684   -280       C  
ATOM    810  OD1 ASP A 104      33.405  34.478  48.779  1.00 28.45           O  
ANISOU  810  OD1 ASP A 104     4610   2923   3274    237    697   -272       O  
ATOM    811  OD2 ASP A 104      34.157  36.557  48.804  1.00 27.38           O  
ANISOU  811  OD2 ASP A 104     4458   2760   3183    215    631   -299       O  
ATOM    812  N   LEU A 105      29.474  35.900  45.775  1.00 22.74           N  
ANISOU  812  N   LEU A 105     3912   2215   2510    159    809   -231       N  
ATOM    813  CA  LEU A 105      28.208  36.493  45.359  1.00 22.52           C  
ANISOU  813  CA  LEU A 105     3899   2185   2471    149    822   -218       C  
ATOM    814  C   LEU A 105      27.077  35.459  45.456  1.00 21.11           C  
ANISOU  814  C   LEU A 105     3721   1996   2303    160    837   -193       C  
ATOM    815  O   LEU A 105      26.021  35.789  45.962  1.00 19.84           O  
ANISOU  815  O   LEU A 105     3569   1828   2138    172    848   -168       O  
ATOM    816  CB  LEU A 105      28.329  37.097  43.956  1.00 22.62           C  
ANISOU  816  CB  LEU A 105     3904   2198   2489    121    831   -228       C  
ATOM    817  CG  LEU A 105      28.780  38.558  43.888  1.00 27.38           C  
ANISOU  817  CG  LEU A 105     4505   2803   3095    108    824   -234       C  
ATOM    818  CD1 LEU A 105      29.966  38.860  44.801  1.00 28.72           C  
ANISOU  818  CD1 LEU A 105     4659   2967   3285    116    795   -246       C  
ATOM    819  CD2 LEU A 105      29.105  38.948  42.453  1.00 25.64           C  
ANISOU  819  CD2 LEU A 105     4277   2583   2883     92    849   -234       C  
ATOM    820  N   TYR A 106      27.308  34.226  44.979  1.00 22.73           N  
ANISOU  820  N   TYR A 106     3912   2193   2530    157    838   -196       N  
ATOM    821  CA  TYR A 106      26.304  33.174  45.047  1.00 22.61           C  
ANISOU  821  CA  TYR A 106     3886   2154   2548    164    843   -171       C  
ATOM    822  C   TYR A 106      25.893  32.920  46.506  1.00 22.01           C  
ANISOU  822  C   TYR A 106     3812   2077   2473    201    864   -133       C  
ATOM    823  O   TYR A 106      24.729  32.841  46.815  1.00 21.43           O  
ANISOU  823  O   TYR A 106     3730   1985   2427    212    883    -93       O  
ATOM    824  CB  TYR A 106      26.803  31.875  44.403  1.00 23.52           C  
ANISOU  824  CB  TYR A 106     3992   2257   2685    162    832   -186       C  
ATOM    825  CG  TYR A 106      25.818  30.753  44.533  1.00 24.44           C  
ANISOU  825  CG  TYR A 106     4089   2338   2857    167    827   -159       C  
ATOM    826  CD1 TYR A 106      24.769  30.649  43.632  1.00 26.14           C  
ANISOU  826  CD1 TYR A 106     4298   2519   3111    151    800   -158       C  
ATOM    827  CD2 TYR A 106      25.848  29.865  45.608  1.00 25.04           C  
ANISOU  827  CD2 TYR A 106     4149   2407   2956    192    847   -128       C  
ATOM    828  CE1 TYR A 106      23.834  29.632  43.718  1.00 25.19           C  
ANISOU  828  CE1 TYR A 106     4148   2352   3068    153    785   -130       C  
ATOM    829  CE2 TYR A 106      24.880  28.886  45.748  1.00 25.20           C  
ANISOU  829  CE2 TYR A 106     4141   2385   3048    197    848    -91       C  
ATOM    830  CZ  TYR A 106      23.865  28.773  44.804  1.00 26.68           C  
ANISOU  830  CZ  TYR A 106     4312   2533   3292    174    814    -91       C  
ATOM    831  OH  TYR A 106      22.926  27.781  44.868  1.00 27.41           O  
ANISOU  831  OH  TYR A 106     4363   2569   3480    174    802    -53       O  
ATOM    832  N   ASN A 107      26.882  32.784  47.387  1.00 23.02           N  
ANISOU  832  N   ASN A 107     3952   2220   2573    226    862   -141       N  
ATOM    833  CA  ASN A 107      26.669  32.435  48.787  1.00 24.01           C  
ANISOU  833  CA  ASN A 107     4096   2344   2683    279    884   -107       C  
ATOM    834  C   ASN A 107      25.844  33.538  49.467  1.00 22.87           C  
ANISOU  834  C   ASN A 107     3981   2200   2505    308    900    -83       C  
ATOM    835  O   ASN A 107      24.845  33.265  50.187  1.00 22.35           O  
ANISOU  835  O   ASN A 107     3920   2120   2449    349    943    -28       O  
ATOM    836  CB  ASN A 107      28.007  32.157  49.496  1.00 24.01           C  
ANISOU  836  CB  ASN A 107     4111   2358   2654    304    861   -132       C  
ATOM    837  CG  ASN A 107      28.632  30.823  49.142  1.00 25.59           C  
ANISOU  837  CG  ASN A 107     4282   2552   2886    293    861   -137       C  
ATOM    838  OD1 ASN A 107      27.991  30.008  48.485  1.00 25.31           O  
ANISOU  838  OD1 ASN A 107     4223   2499   2894    275    875   -121       O  
ATOM    839  ND2 ASN A 107      29.874  30.591  49.563  1.00 22.55           N  
ANISOU  839  ND2 ASN A 107     3902   2178   2487    307    837   -161       N  
ATOM    840  N   TYR A 108      26.229  34.798  49.227  1.00 22.68           N  
ANISOU  840  N   TYR A 108     3976   2189   2451    292    872   -118       N  
ATOM    841  CA  TYR A 108      25.503  35.969  49.764  1.00 23.06           C  
ANISOU  841  CA  TYR A 108     4059   2237   2464    318    881   -104       C  
ATOM    842  C   TYR A 108      24.062  35.996  49.254  1.00 22.69           C  
ANISOU  842  C   TYR A 108     3989   2176   2456    304    919    -61       C  
ATOM    843  O   TYR A 108      23.125  36.216  50.049  1.00 25.08           O  
ANISOU  843  O   TYR A 108     4311   2470   2748    351    959    -13       O  
ATOM    844  CB  TYR A 108      26.218  37.279  49.408  1.00 23.86           C  
ANISOU  844  CB  TYR A 108     4173   2347   2545    292    838   -151       C  
ATOM    845  CG  TYR A 108      25.893  38.411  50.340  1.00 26.51           C  
ANISOU  845  CG  TYR A 108     4562   2678   2830    339    828   -151       C  
ATOM    846  CD1 TYR A 108      26.116  38.295  51.709  1.00 25.73           C  
ANISOU  846  CD1 TYR A 108     4519   2575   2679    415    819   -146       C  
ATOM    847  CD2 TYR A 108      25.355  39.591  49.855  1.00 24.18           C  
ANISOU  847  CD2 TYR A 108     4271   2381   2532    316    826   -156       C  
ATOM    848  CE1 TYR A 108      25.800  39.329  52.574  1.00 27.13           C  
ANISOU  848  CE1 TYR A 108     4763   2745   2799    472    805   -149       C  
ATOM    849  CE2 TYR A 108      25.048  40.638  50.705  1.00 25.76           C  
ANISOU  849  CE2 TYR A 108     4528   2575   2684    364    815   -158       C  
ATOM    850  CZ  TYR A 108      25.283  40.511  52.065  1.00 26.92           C  
ANISOU  850  CZ  TYR A 108     4737   2715   2775    445    802   -157       C  
ATOM    851  OH  TYR A 108      24.981  41.558  52.887  1.00 27.96           O  
ANISOU  851  OH  TYR A 108     4939   2836   2848    504    785   -164       O  
ATOM    852  N   GLY A 109      23.889  35.718  47.954  1.00 23.08           N  
ANISOU  852  N   GLY A 109     3999   2218   2550    248    906    -75       N  
ATOM    853  CA  GLY A 109      22.565  35.582  47.334  1.00 23.08           C  
ANISOU  853  CA  GLY A 109     3969   2193   2605    229    920    -41       C  
ATOM    854  C   GLY A 109      21.741  34.456  47.960  1.00 23.95           C  
ANISOU  854  C   GLY A 109     4050   2274   2774    259    957     20       C  
ATOM    855  O   GLY A 109      20.557  34.647  48.311  1.00 24.80           O  
ANISOU  855  O   GLY A 109     4143   2361   2919    280    994     78       O  
ATOM    856  N   LYS A 110      22.370  33.289  48.123  1.00 24.81           N  
ANISOU  856  N   LYS A 110     4148   2379   2900    265    953     16       N  
ATOM    857  CA  LYS A 110      21.690  32.125  48.735  1.00 30.01           C  
ANISOU  857  CA  LYS A 110     4772   3004   3624    295    991     80       C  
ATOM    858  C   LYS A 110      21.229  32.467  50.164  1.00 30.12           C  
ANISOU  858  C   LYS A 110     4815   3022   3606    369   1056    143       C  
ATOM    859  O   LYS A 110      20.038  32.295  50.508  1.00 30.49           O  
ANISOU  859  O   LYS A 110     4830   3036   3716    395   1107    219       O  
ATOM    860  CB  LYS A 110      22.597  30.893  48.725  1.00 33.33           C  
ANISOU  860  CB  LYS A 110     5183   3424   4057    292    975     60       C  
ATOM    861  CG  LYS A 110      21.868  29.586  48.470  1.00 42.53           C  
ANISOU  861  CG  LYS A 110     6291   4537   5329    283    978    102       C  
ATOM    862  CD  LYS A 110      21.043  29.586  47.191  1.00 44.61           C  
ANISOU  862  CD  LYS A 110     6519   4762   5667    232    930     88       C  
ATOM    863  CE  LYS A 110      20.371  28.251  46.958  1.00 47.53           C  
ANISOU  863  CE  LYS A 110     6830   5067   6161    224    914    125       C  
ATOM    864  NZ  LYS A 110      19.012  28.407  46.389  1.00 50.33           N  
ANISOU  864  NZ  LYS A 110     7136   5366   6619    201    889    158       N  
ATOM    865  N   GLU A 111      22.165  32.964  50.985  1.00 30.86           N  
ANISOU  865  N   GLU A 111     4970   3150   3605    411   1053    114       N  
ATOM    866  CA  GLU A 111      21.850  33.401  52.335  1.00 33.11           C  
ANISOU  866  CA  GLU A 111     5309   3440   3831    498   1104    160       C  
ATOM    867  C   GLU A 111      20.648  34.353  52.359  1.00 32.48           C  
ANISOU  867  C   GLU A 111     5232   3349   3760    513   1142    203       C  
ATOM    868  O   GLU A 111      19.878  34.274  53.263  1.00 29.64           O  
ANISOU  868  O   GLU A 111     4886   2974   3401    586   1213    279       O  
ATOM    869  CB  GLU A 111      22.999  34.166  52.984  1.00 40.63           C  
ANISOU  869  CB  GLU A 111     6336   4423   4677    533   1061    100       C  
ATOM    870  CG  GLU A 111      24.189  33.306  53.349  1.00 52.33           C  
ANISOU  870  CG  GLU A 111     7829   5915   6139    545   1031     69       C  
ATOM    871  CD  GLU A 111      25.403  34.102  53.809  1.00 63.51           C  
ANISOU  871  CD  GLU A 111     9304   7349   7477    564    963      1       C  
ATOM    872  OE1 GLU A 111      25.232  35.303  54.176  1.00 69.18           O  
ANISOU  872  OE1 GLU A 111    10072   8069   8142    593    946    -13       O  
ATOM    873  OE2 GLU A 111      26.516  33.521  53.817  1.00 72.02           O  
ANISOU  873  OE2 GLU A 111    10375   8434   8556    553    922    -35       O  
ATOM    874  N   ASN A 112      20.542  35.303  51.412  1.00 27.72           N  
ANISOU  874  N   ASN A 112     4620   2754   3158    453   1100    159       N  
ATOM    875  CA  ASN A 112      19.609  36.421  51.539  1.00 28.51           C  
ANISOU  875  CA  ASN A 112     4737   2850   3245    474   1129    188       C  
ATOM    876  C   ASN A 112      18.439  36.291  50.555  1.00 29.55           C  
ANISOU  876  C   ASN A 112     4795   2950   3482    420   1136    224       C  
ATOM    877  O   ASN A 112      17.710  37.272  50.320  1.00 29.21           O  
ANISOU  877  O   ASN A 112     4754   2904   3439    415   1145    236       O  
ATOM    878  CB  ASN A 112      20.324  37.759  51.374  1.00 28.46           C  
ANISOU  878  CB  ASN A 112     4784   2871   3157    459   1075    115       C  
ATOM    879  CG  ASN A 112      21.330  37.997  52.483  1.00 31.46           C  
ANISOU  879  CG  ASN A 112     5240   3267   3444    523   1055     83       C  
ATOM    880  OD1 ASN A 112      20.945  38.112  53.630  1.00 32.96           O  
ANISOU  880  OD1 ASN A 112     5486   3452   3583    614   1100    127       O  
ATOM    881  ND2 ASN A 112      22.618  38.008  52.176  1.00 31.49           N  
ANISOU  881  ND2 ASN A 112     5247   3285   3429    486    988     13       N  
ATOM    882  N   ASN A 113      18.277  35.093  49.998  1.00 27.30           N  
ANISOU  882  N   ASN A 113     4447   2637   3288    384   1124    239       N  
ATOM    883  CA  ASN A 113      17.250  34.767  49.031  1.00 30.64           C  
ANISOU  883  CA  ASN A 113     4797   3016   3826    334   1106    264       C  
ATOM    884  C   ASN A 113      17.197  35.793  47.880  1.00 27.05           C  
ANISOU  884  C   ASN A 113     4352   2574   3351    277   1048    205       C  
ATOM    885  O   ASN A 113      16.136  36.251  47.486  1.00 26.81           O  
ANISOU  885  O   ASN A 113     4290   2518   3378    264   1050    237       O  
ATOM    886  CB  ASN A 113      15.891  34.643  49.717  1.00 37.20           C  
ANISOU  886  CB  ASN A 113     5585   3805   4743    381   1183    374       C  
ATOM    887  CG  ASN A 113      14.896  33.941  48.818  1.00 45.11           C  
ANISOU  887  CG  ASN A 113     6494   4743   5900    331   1150    407       C  
ATOM    888  OD1 ASN A 113      15.290  33.137  47.963  1.00 44.70           O  
ANISOU  888  OD1 ASN A 113     6418   4674   5891    280   1079    357       O  
ATOM    889  ND2 ASN A 113      13.619  34.270  48.972  1.00 48.26           N  
ANISOU  889  ND2 ASN A 113     6844   5102   6388    348   1194    488       N  
ATOM    890  N   SER A 114      18.359  36.136  47.325  1.00 26.31           N  
ANISOU  890  N   SER A 114     4297   2517   3181    246    999    123       N  
ATOM    891  CA  SER A 114      18.484  37.301  46.430  1.00 24.54           C  
ANISOU  891  CA  SER A 114     4096   2312   2916    209    961     72       C  
ATOM    892  C   SER A 114      18.094  36.922  44.990  1.00 24.28           C  
ANISOU  892  C   SER A 114     4030   2252   2943    158    905     47       C  
ATOM    893  O   SER A 114      18.463  35.851  44.481  1.00 22.05           O  
ANISOU  893  O   SER A 114     3731   1952   2693    142    871     25       O  
ATOM    894  CB  SER A 114      19.869  37.863  46.455  1.00 25.33           C  
ANISOU  894  CB  SER A 114     4243   2454   2927    204    940     10       C  
ATOM    895  OG  SER A 114      20.291  38.156  47.773  1.00 24.38           O  
ANISOU  895  OG  SER A 114     4162   2350   2750    258    970     22       O  
ATOM    896  N   ASP A 115      17.330  37.818  44.353  1.00 24.20           N  
ANISOU  896  N   ASP A 115     4016   2233   2943    140    890     48       N  
ATOM    897  CA  ASP A 115      17.065  37.768  42.930  1.00 25.18           C  
ANISOU  897  CA  ASP A 115     4134   2336   3095    102    826     11       C  
ATOM    898  C   ASP A 115      18.231  38.383  42.136  1.00 24.70           C  
ANISOU  898  C   ASP A 115     4124   2316   2944     87    804    -56       C  
ATOM    899  O   ASP A 115      18.441  38.017  40.983  1.00 22.86           O  
ANISOU  899  O   ASP A 115     3904   2071   2710     72    756    -95       O  
ATOM    900  CB  ASP A 115      15.754  38.473  42.594  1.00 26.72           C  
ANISOU  900  CB  ASP A 115     4305   2503   3342     95    817     44       C  
ATOM    901  CG  ASP A 115      14.566  37.854  43.307  1.00 27.90           C  
ANISOU  901  CG  ASP A 115     4391   2603   3606    112    846    125       C  
ATOM    902  OD1 ASP A 115      14.414  36.637  43.178  1.00 30.65           O  
ANISOU  902  OD1 ASP A 115     4699   2910   4036    106    817    136       O  
ATOM    903  OD2 ASP A 115      13.848  38.595  44.044  1.00 30.31           O  
ANISOU  903  OD2 ASP A 115     4685   2909   3919    137    903    181       O  
ATOM    904  N   LEU A 116      18.978  39.306  42.757  1.00 23.87           N  
ANISOU  904  N   LEU A 116     4049   2251   2769     97    839    -65       N  
ATOM    905  CA  LEU A 116      20.072  40.036  42.108  1.00 23.71           C  
ANISOU  905  CA  LEU A 116     4062   2261   2686     83    830   -113       C  
ATOM    906  C   LEU A 116      21.181  40.291  43.136  1.00 22.86           C  
ANISOU  906  C   LEU A 116     3969   2180   2536     99    853   -122       C  
ATOM    907  O   LEU A 116      20.902  40.753  44.233  1.00 23.07           O  
ANISOU  907  O   LEU A 116     4004   2210   2550    125    875    -98       O  
ATOM    908  CB  LEU A 116      19.507  41.357  41.567  1.00 23.74           C  
ANISOU  908  CB  LEU A 116     4079   2268   2671     73    828   -113       C  
ATOM    909  CG  LEU A 116      20.506  42.295  40.900  1.00 24.23           C  
ANISOU  909  CG  LEU A 116     4168   2354   2682     62    830   -147       C  
ATOM    910  CD1 LEU A 116      21.043  41.690  39.610  1.00 26.00           C  
ANISOU  910  CD1 LEU A 116     4406   2574   2896     58    809   -176       C  
ATOM    911  CD2 LEU A 116      19.863  43.636  40.612  1.00 25.90           C  
ANISOU  911  CD2 LEU A 116     4391   2568   2881     55    836   -139       C  
ATOM    912  N   ILE A 117      22.426  39.979  42.776  1.00 21.52           N  
ANISOU  912  N   ILE A 117     3804   2024   2346     92    844   -155       N  
ATOM    913  CA  ILE A 117      23.597  40.265  43.612  1.00 21.33           C  
ANISOU  913  CA  ILE A 117     3788   2017   2297    104    848   -169       C  
ATOM    914  C   ILE A 117      24.572  41.126  42.796  1.00 21.40           C  
ANISOU  914  C   ILE A 117     3799   2035   2294     84    843   -195       C  
ATOM    915  O   ILE A 117      24.958  40.801  41.698  1.00 21.35           O  
ANISOU  915  O   ILE A 117     3790   2029   2290     74    846   -205       O  
ATOM    916  CB  ILE A 117      24.253  39.000  44.188  1.00 21.58           C  
ANISOU  916  CB  ILE A 117     3810   2048   2338    119    847   -171       C  
ATOM    917  CG1 ILE A 117      23.202  38.014  44.725  1.00 23.41           C  
ANISOU  917  CG1 ILE A 117     4029   2262   2601    138    860   -134       C  
ATOM    918  CG2 ILE A 117      25.245  39.410  45.272  1.00 21.75           C  
ANISOU  918  CG2 ILE A 117     3845   2081   2338    139    838   -183       C  
ATOM    919  CD1 ILE A 117      22.866  36.854  43.799  1.00 23.62           C  
ANISOU  919  CD1 ILE A 117     4035   2268   2672    122    844   -135       C  
ATOM    920  N   ILE A 118      24.896  42.281  43.353  1.00 21.87           N  
ANISOU  920  N   ILE A 118     3867   2097   2344     85    838   -200       N  
ATOM    921  CA  ILE A 118      25.812  43.209  42.768  1.00 22.37           C  
ANISOU  921  CA  ILE A 118     3920   2159   2417     67    836   -212       C  
ATOM    922  C   ILE A 118      27.111  43.154  43.556  1.00 21.79           C  
ANISOU  922  C   ILE A 118     3833   2081   2366     74    814   -227       C  
ATOM    923  O   ILE A 118      27.135  43.506  44.753  1.00 22.00           O  
ANISOU  923  O   ILE A 118     3876   2100   2382     95    784   -236       O  
ATOM    924  CB  ILE A 118      25.211  44.628  42.754  1.00 23.41           C  
ANISOU  924  CB  ILE A 118     4066   2287   2542     61    835   -208       C  
ATOM    925  CG1 ILE A 118      23.799  44.589  42.171  1.00 25.23           C  
ANISOU  925  CG1 ILE A 118     4309   2519   2757     59    849   -191       C  
ATOM    926  CG2 ILE A 118      26.133  45.563  41.983  1.00 23.93           C  
ANISOU  926  CG2 ILE A 118     4112   2345   2634     41    841   -211       C  
ATOM    927  CD1 ILE A 118      22.958  45.783  42.470  1.00 26.34           C  
ANISOU  927  CD1 ILE A 118     4466   2655   2886     61    850   -180       C  
ATOM    928  N   GLY A 119      28.181  42.815  42.833  1.00 21.47           N  
ANISOU  928  N   GLY A 119     3763   2039   2354     63    825   -229       N  
ATOM    929  CA  GLY A 119      29.541  42.815  43.366  1.00 23.52           C  
ANISOU  929  CA  GLY A 119     3993   2286   2657     64    802   -238       C  
ATOM    930  C   GLY A 119      30.230  44.147  43.091  1.00 25.06           C  
ANISOU  930  C   GLY A 119     4159   2457   2904     46    793   -234       C  
ATOM    931  O   GLY A 119      30.079  44.727  42.004  1.00 24.09           O  
ANISOU  931  O   GLY A 119     4029   2336   2789     33    832   -215       O  
ATOM    932  N   LYS A 120      31.072  44.584  44.026  1.00 24.52           N  
ANISOU  932  N   LYS A 120     4072   2361   2881     48    738   -250       N  
ATOM    933  CA  LYS A 120      31.790  45.840  43.883  1.00 25.68           C  
ANISOU  933  CA  LYS A 120     4181   2472   3104     29    715   -245       C  
ATOM    934  C   LYS A 120      32.723  45.784  42.662  1.00 26.96           C  
ANISOU  934  C   LYS A 120     4283   2626   3334     13    773   -207       C  
ATOM    935  O   LYS A 120      33.423  44.815  42.438  1.00 25.24           O  
ANISOU  935  O   LYS A 120     4041   2414   3132     20    795   -197       O  
ATOM    936  CB  LYS A 120      32.641  46.150  45.114  1.00 27.02           C  
ANISOU  936  CB  LYS A 120     4339   2602   3325     39    625   -274       C  
ATOM    937  CG  LYS A 120      33.028  47.609  45.227  1.00 31.78           C  
ANISOU  937  CG  LYS A 120     4915   3154   4002     23    576   -279       C  
ATOM    938  CD  LYS A 120      34.349  47.864  45.887  1.00 37.12           C  
ANISOU  938  CD  LYS A 120     5542   3773   4787     20    490   -295       C  
ATOM    939  CE  LYS A 120      34.366  47.684  47.383  1.00 37.91           C  
ANISOU  939  CE  LYS A 120     5700   3856   4847     61    388   -347       C  
ATOM    940  NZ  LYS A 120      35.568  46.903  47.807  1.00 40.93           N  
ANISOU  940  NZ  LYS A 120     6040   4216   5296     67    341   -355       N  
ATOM    941  N   TYR A 121      32.763  46.891  41.917  1.00 26.98           N  
ANISOU  941  N   TYR A 121     4262   2610   3378     -1    801   -181       N  
ATOM    942  CA  TYR A 121      33.578  47.012  40.718  1.00 27.97           C  
ANISOU  942  CA  TYR A 121     4336   2724   3567     -3    873   -131       C  
ATOM    943  C   TYR A 121      34.920  47.662  41.060  1.00 29.34           C  
ANISOU  943  C   TYR A 121     4426   2839   3883    -20    839   -111       C  
ATOM    944  O   TYR A 121      34.993  48.597  41.850  1.00 27.69           O  
ANISOU  944  O   TYR A 121     4203   2590   3726    -36    763   -133       O  
ATOM    945  CB  TYR A 121      32.872  47.867  39.667  1.00 27.31           C  
ANISOU  945  CB  TYR A 121     4273   2648   3455     -3    930   -104       C  
ATOM    946  CG  TYR A 121      31.537  47.316  39.259  1.00 25.90           C  
ANISOU  946  CG  TYR A 121     4169   2515   3156     11    950   -122       C  
ATOM    947  CD1 TYR A 121      31.433  46.132  38.531  1.00 26.52           C  
ANISOU  947  CD1 TYR A 121     4276   2622   3179     36    993   -118       C  
ATOM    948  CD2 TYR A 121      30.380  47.996  39.547  1.00 25.45           C  
ANISOU  948  CD2 TYR A 121     4151   2465   3050      2    923   -142       C  
ATOM    949  CE1 TYR A 121      30.201  45.633  38.137  1.00 26.37           C  
ANISOU  949  CE1 TYR A 121     4319   2631   3070     49    994   -136       C  
ATOM    950  CE2 TYR A 121      29.140  47.499  39.180  1.00 27.32           C  
ANISOU  950  CE2 TYR A 121     4445   2734   3200     14    934   -153       C  
ATOM    951  CZ  TYR A 121      29.044  46.294  38.503  1.00 26.28           C  
ANISOU  951  CZ  TYR A 121     4335   2623   3024     35    963   -153       C  
ATOM    952  OH  TYR A 121      27.810  45.826  38.150  1.00 26.31           O  
ANISOU  952  OH  TYR A 121     4387   2645   2962     45    957   -166       O  
ATOM    953  N   GLY A 122      35.971  47.135  40.454  1.00 30.11           N  
ANISOU  953  N   GLY A 122     4466   2924   4048    -11    893    -68       N  
ATOM    954  CA  GLY A 122      37.278  47.758  40.371  1.00 32.82           C  
ANISOU  954  CA  GLY A 122     4709   3205   4554    -24    892    -22       C  
ATOM    955  C   GLY A 122      37.620  48.128  38.927  1.00 32.51           C  
ANISOU  955  C   GLY A 122     4635   3161   4556     -6   1016     57       C  
ATOM    956  O   GLY A 122      36.794  47.981  38.020  1.00 28.52           O  
ANISOU  956  O   GLY A 122     4194   2699   3940     18   1088     67       O  
ATOM    957  N   VAL A 123      38.836  48.650  38.741  1.00 36.24           N  
ANISOU  957  N   VAL A 123     5002   3571   5196    -14   1036    118       N  
ATOM    958  CA  VAL A 123      39.290  49.178  37.455  1.00 38.68           C  
ANISOU  958  CA  VAL A 123     5265   3860   5571     10   1162    212       C  
ATOM    959  C   VAL A 123      40.788  48.893  37.269  1.00 38.22           C  
ANISOU  959  C   VAL A 123     5094   3750   5677     21   1208    286       C  
ATOM    960  O   VAL A 123      41.589  48.956  38.212  1.00 36.95           O  
ANISOU  960  O   VAL A 123     4855   3535   5647    -11   1114    271       O  
ATOM    961  CB  VAL A 123      38.985  50.680  37.316  1.00 41.12           C  
ANISOU  961  CB  VAL A 123     5548   4130   5946    -13   1152    232       C  
ATOM    962  CG1 VAL A 123      39.720  51.271  36.138  1.00 47.34           C  
ANISOU  962  CG1 VAL A 123     6262   4878   6844     14   1281    345       C  
ATOM    963  CG2 VAL A 123      37.491  50.959  37.188  1.00 43.70           C  
ANISOU  963  CG2 VAL A 123     5984   4510   6108    -12   1141    180       C  
ATOM    964  N   GLU A 124      41.131  48.577  36.009  1.00 38.00           N  
ANISOU  964  N   GLU A 124     5063   3736   5636     76   1355    368       N  
ATOM    965  CA  GLU A 124      42.480  48.616  35.477  1.00 38.90           C  
ANISOU  965  CA  GLU A 124     5064   3794   5919    101   1447    474       C  
ATOM    966  C   GLU A 124      42.511  49.640  34.347  1.00 38.07           C  
ANISOU  966  C   GLU A 124     4934   3664   5865    134   1571    571       C  
ATOM    967  O   GLU A 124      41.683  49.595  33.436  1.00 36.55           O  
ANISOU  967  O   GLU A 124     4844   3525   5517    183   1650    575       O  
ATOM    968  CB  GLU A 124      42.917  47.248  34.958  1.00 38.83           C  
ANISOU  968  CB  GLU A 124     5086   3824   5841    160   1532    498       C  
ATOM    969  CG  GLU A 124      43.630  46.419  36.002  1.00 41.21           C  
ANISOU  969  CG  GLU A 124     5336   4109   6210    130   1440    458       C  
ATOM    970  CD  GLU A 124      44.149  45.075  35.500  1.00 47.79           C  
ANISOU  970  CD  GLU A 124     6192   4975   6989    188   1526    486       C  
ATOM    971  OE1 GLU A 124      44.475  44.206  36.354  1.00 46.16           O  
ANISOU  971  OE1 GLU A 124     5976   4775   6789    168   1446    436       O  
ATOM    972  OE2 GLU A 124      44.242  44.900  34.254  1.00 45.31           O  
ANISOU  972  OE2 GLU A 124     5911   4677   6624    261   1673    560       O  
ATOM    973  N   GLY A 125      43.466  50.566  34.453  1.00 42.90           N  
ANISOU  973  N   GLY A 125     5407   4187   6704    109   1576    649       N  
ATOM    974  CA  GLY A 125      43.627  51.700  33.545  1.00 43.03           C  
ANISOU  974  CA  GLY A 125     5372   4160   6817    133   1686    752       C  
ATOM    975  C   GLY A 125      43.412  53.026  34.271  1.00 45.82           C  
ANISOU  975  C   GLY A 125     5667   4450   7289     60   1568    723       C  
ATOM    976  O   GLY A 125      43.447  53.092  35.512  1.00 43.71           O  
ANISOU  976  O   GLY A 125     5377   4156   7075     -1   1402    637       O  
ATOM    977  N   LYS A 126      43.170  54.078  33.483  1.00 50.96           N  
ANISOU  977  N   LYS A 126     6306   5079   7976     78   1654    793       N  
ATOM    978  CA  LYS A 126      42.888  55.438  33.976  1.00 56.86           C  
ANISOU  978  CA  LYS A 126     7006   5766   8829     18   1561    774       C  
ATOM    979  C   LYS A 126      41.379  55.618  34.188  1.00 59.98           C  
ANISOU  979  C   LYS A 126     7548   6236   9003      5   1494    666       C  
ATOM    980  O   LYS A 126      40.614  54.647  34.148  1.00 63.93           O  
ANISOU  980  O   LYS A 126     8169   6825   9295     29   1493    597       O  
ATOM    981  CB  LYS A 126      43.410  56.478  32.980  1.00 58.17           C  
ANISOU  981  CB  LYS A 126     7078   5865   9155     48   1700    917       C  
ATOM    982  CG  LYS A 126      44.927  56.592  32.880  1.00 61.09           C  
ANISOU  982  CG  LYS A 126     7270   6133   9806     51   1756   1040       C  
ATOM    983  CD  LYS A 126      45.571  55.943  31.657  1.00 62.39           C  
ANISOU  983  CD  LYS A 126     7421   6317   9964    147   1971   1173       C  
ATOM    984  CE  LYS A 126      47.087  55.917  31.754  1.00 64.29           C  
ANISOU  984  CE  LYS A 126     7475   6455  10495    144   2010   1289       C  
ATOM    985  NZ  LYS A 126      47.757  55.456  30.512  1.00 64.94           N  
ANISOU  985  NZ  LYS A 126     7537   6544  10592    251   2242   1442       N  
ATOM    986  N   VAL A 130      32.885  53.480  36.677  1.00 53.47           N  
ANISOU  986  N   VAL A 130     7476   5841   6997    -28   1102     79       N  
ATOM    987  CA  VAL A 130      32.075  52.496  37.425  1.00 56.72           C  
ANISOU  987  CA  VAL A 130     7956   6299   7295    -29   1041      9       C  
ATOM    988  C   VAL A 130      31.379  53.203  38.592  1.00 54.84           C  
ANISOU  988  C   VAL A 130     7742   6048   7045    -54    946    -43       C  
ATOM    989  O   VAL A 130      31.938  54.118  39.204  1.00 48.64           O  
ANISOU  989  O   VAL A 130     6910   5208   6361    -76    891    -46       O  
ATOM    990  CB  VAL A 130      32.906  51.288  37.916  1.00 53.57           C  
ANISOU  990  CB  VAL A 130     7532   5903   6917    -24   1022     -3       C  
ATOM    991  CG2 VAL A 130      33.795  51.621  39.111  1.00 50.91           C  
ANISOU  991  CG2 VAL A 130     7134   5513   6694    -51    933    -23       C  
ATOM    992  N   PRO A 131      30.133  52.800  38.937  1.00 49.83           N  
ANISOU  992  N   PRO A 131     7182   5457   6293    -46    923    -85       N  
ATOM    993  CA  PRO A 131      29.438  53.364  40.092  1.00 46.43           C  
ANISOU  993  CA  PRO A 131     6786   5017   5838    -54    845   -130       C  
ATOM    994  C   PRO A 131      30.195  53.163  41.416  1.00 46.31           C  
ANISOU  994  C   PRO A 131     6753   4969   5871    -55    758   -168       C  
ATOM    995  O   PRO A 131      31.030  52.234  41.542  1.00 49.40           O  
ANISOU  995  O   PRO A 131     7116   5362   6292    -52    756   -166       O  
ATOM    996  CB  PRO A 131      28.081  52.656  40.134  1.00 48.59           C  
ANISOU  996  CB  PRO A 131     7129   5342   5990    -37    856   -151       C  
ATOM    997  CG  PRO A 131      27.936  51.967  38.793  1.00 52.44           C  
ANISOU  997  CG  PRO A 131     7624   5861   6440    -25    930   -121       C  
ATOM    998  CD  PRO A 131      29.327  51.808  38.217  1.00 52.35           C  
ANISOU  998  CD  PRO A 131     7555   5828   6507    -23    970    -86       C  
ATOM    999  N   LYS A 132      29.905  54.059  42.370  1.00 39.83           N  
ANISOU  999  N   LYS A 132     5958   4117   5056    -53    683   -202       N  
ATOM   1000  CA  LYS A 132      30.538  54.096  43.665  1.00 39.18           C  
ANISOU 1000  CA  LYS A 132     5879   3993   5013    -42    581   -245       C  
ATOM   1001  C   LYS A 132      29.486  54.219  44.793  1.00 37.23           C  
ANISOU 1001  C   LYS A 132     5724   3759   4661     -4    530   -290       C  
ATOM   1002  O   LYS A 132      29.648  53.577  45.834  1.00 37.55           O  
ANISOU 1002  O   LYS A 132     5801   3800   4666     28    475   -324       O  
ATOM   1003  CB  LYS A 132      31.577  55.221  43.713  1.00 43.65           C  
ANISOU 1003  CB  LYS A 132     6378   4480   5725    -65    523   -239       C  
ATOM   1004  CG  LYS A 132      32.781  54.931  44.599  1.00 47.06           C  
ANISOU 1004  CG  LYS A 132     6773   4859   6248    -62    426   -267       C  
ATOM   1005  N   ALA A 133      28.418  55.010  44.616  1.00 31.84           N  
ANISOU 1005  N   ALA A 133     5082   3088   3927      0    553   -286       N  
ATOM   1006  CA  ALA A 133      27.468  55.297  45.736  1.00 33.83           C  
ANISOU 1006  CA  ALA A 133     5421   3343   4090     47    510   -320       C  
ATOM   1007  C   ALA A 133      26.795  54.005  46.232  1.00 31.27           C  
ANISOU 1007  C   ALA A 133     5143   3069   3668     83    543   -320       C  
ATOM   1008  O   ALA A 133      26.631  53.802  47.418  1.00 30.40           O  
ANISOU 1008  O   ALA A 133     5094   2952   3503    135    496   -348       O  
ATOM   1009  CB  ALA A 133      26.430  56.305  45.328  1.00 33.76           C  
ANISOU 1009  CB  ALA A 133     5437   3338   4049     44    543   -305       C  
ATOM   1010  N   ILE A 134      26.441  53.122  45.293  1.00 29.02           N  
ANISOU 1010  N   ILE A 134     4830   2830   3365     60    622   -286       N  
ATOM   1011  CA  ILE A 134      25.861  51.823  45.611  1.00 26.93           C  
ANISOU 1011  CA  ILE A 134     4591   2605   3035     85    654   -278       C  
ATOM   1012  C   ILE A 134      26.699  51.014  46.613  1.00 24.87           C  
ANISOU 1012  C   ILE A 134     4340   2334   2774    114    604   -304       C  
ATOM   1013  O   ILE A 134      26.130  50.180  47.302  1.00 25.93           O  
ANISOU 1013  O   ILE A 134     4514   2490   2846    153    619   -300       O  
ATOM   1014  CB  ILE A 134      25.544  51.040  44.329  1.00 26.51           C  
ANISOU 1014  CB  ILE A 134     4502   2587   2981     54    725   -246       C  
ATOM   1015  CG1 ILE A 134      24.706  49.801  44.632  1.00 27.46           C  
ANISOU 1015  CG1 ILE A 134     4646   2738   3047     78    754   -234       C  
ATOM   1016  CG2 ILE A 134      26.800  50.697  43.525  1.00 26.64           C  
ANISOU 1016  CG2 ILE A 134     4460   2596   3063     24    735   -239       C  
ATOM   1017  CD1 ILE A 134      24.133  49.171  43.380  1.00 27.69           C  
ANISOU 1017  CD1 ILE A 134     4654   2792   3074     55    804   -209       C  
ATOM   1018  N   PHE A 135      28.000  51.266  46.723  1.00 24.88           N  
ANISOU 1018  N   PHE A 135     4303   2297   2850     98    547   -325       N  
ATOM   1019  CA  PHE A 135      28.926  50.457  47.522  1.00 27.17           C  
ANISOU 1019  CA  PHE A 135     4591   2574   3154    120    495   -348       C  
ATOM   1020  C   PHE A 135      29.385  51.177  48.796  1.00 28.73           C  
ANISOU 1020  C   PHE A 135     4838   2720   3357    163    384   -396       C  
ATOM   1021  O   PHE A 135      30.157  50.620  49.588  1.00 34.16           O  
ANISOU 1021  O   PHE A 135     5536   3390   4053    191    322   -423       O  
ATOM   1022  CB  PHE A 135      30.129  50.051  46.666  1.00 27.65           C  
ANISOU 1022  CB  PHE A 135     4566   2626   3311     74    508   -332       C  
ATOM   1023  CG  PHE A 135      29.770  49.327  45.391  1.00 25.86           C  
ANISOU 1023  CG  PHE A 135     4309   2445   3070     46    607   -291       C  
ATOM   1024  CD1 PHE A 135      29.010  48.167  45.416  1.00 25.44           C  
ANISOU 1024  CD1 PHE A 135     4287   2435   2943     64    650   -283       C  
ATOM   1025  CD2 PHE A 135      30.188  49.799  44.158  1.00 26.50           C  
ANISOU 1025  CD2 PHE A 135     4334   2518   3214     10    653   -260       C  
ATOM   1026  CE1 PHE A 135      28.665  47.501  44.248  1.00 25.47           C  
ANISOU 1026  CE1 PHE A 135     4271   2470   2934     45    720   -255       C  
ATOM   1027  CE2 PHE A 135      29.874  49.109  42.994  1.00 25.32           C  
ANISOU 1027  CE2 PHE A 135     4176   2406   3037      0    734   -229       C  
ATOM   1028  CZ  PHE A 135      29.103  47.974  43.034  1.00 25.75           C  
ANISOU 1028  CZ  PHE A 135     4267   2500   3016     17    759   -232       C  
ATOM   1029  N   GLU A 136      28.889  52.393  49.004  1.00 31.48           N  
ANISOU 1029  N   GLU A 136     5223   3042   3695    176    354   -410       N  
ATOM   1030  CA  GLU A 136      29.362  53.328  50.051  1.00 33.12           C  
ANISOU 1030  CA  GLU A 136     5479   3184   3919    217    233   -462       C  
ATOM   1031  C   GLU A 136      28.955  52.843  51.457  1.00 31.64           C  
ANISOU 1031  C   GLU A 136     5402   3002   3617    311    193   -492       C  
ATOM   1032  O   GLU A 136      29.607  53.195  52.427  1.00 38.16           O  
ANISOU 1032  O   GLU A 136     6276   3773   4449    359     76   -544       O  
ATOM   1033  CB  GLU A 136      28.838  54.741  49.756  1.00 32.32           C  
ANISOU 1033  CB  GLU A 136     5389   3055   3835    204    224   -464       C  
ATOM   1034  N   LYS A 137      27.923  52.005  51.555  1.00 30.61           N  
ANISOU 1034  N   LYS A 137     5310   2930   3389    342    286   -457       N  
ATOM   1035  CA  LYS A 137      27.418  51.487  52.842  1.00 31.09           C  
ANISOU 1035  CA  LYS A 137     5476   3000   3336    443    279   -466       C  
ATOM   1036  C   LYS A 137      27.892  50.056  53.144  1.00 30.21           C  
ANISOU 1036  C   LYS A 137     5352   2914   3212    458    294   -456       C  
ATOM   1037  O   LYS A 137      27.420  49.451  54.096  1.00 30.01           O  
ANISOU 1037  O   LYS A 137     5405   2903   3094    542    313   -448       O  
ATOM   1038  CB  LYS A 137      25.892  51.534  52.827  1.00 31.30           C  
ANISOU 1038  CB  LYS A 137     5546   3066   3279    477    381   -418       C  
ATOM   1039  CG  LYS A 137      25.337  52.940  52.885  1.00 33.52           C  
ANISOU 1039  CG  LYS A 137     5872   3319   3544    493    358   -432       C  
ATOM   1040  CD  LYS A 137      23.856  52.995  52.699  1.00 35.37           C  
ANISOU 1040  CD  LYS A 137     6129   3591   3720    514    465   -376       C  
ATOM   1041  CE  LYS A 137      23.356  54.421  52.664  1.00 38.60           C  
ANISOU 1041  CE  LYS A 137     6574   3971   4119    525    444   -389       C  
ATOM   1042  NZ  LYS A 137      21.913  54.444  52.352  1.00 41.87           N  
ANISOU 1042  NZ  LYS A 137     6992   4421   4493    536    554   -328       N  
ATOM   1043  N   GLY A 138      28.839  49.542  52.363  1.00 26.78           N  
ANISOU 1043  N   GLY A 138     4821   2481   2870    384    291   -454       N  
ATOM   1044  CA  GLY A 138      29.336  48.191  52.510  1.00 25.85           C  
ANISOU 1044  CA  GLY A 138     4681   2387   2751    389    308   -444       C  
ATOM   1045  C   GLY A 138      28.297  47.191  52.039  1.00 23.93           C  
ANISOU 1045  C   GLY A 138     4426   2202   2462    381    430   -388       C  
ATOM   1046  O   GLY A 138      27.461  47.490  51.175  1.00 23.46           O  
ANISOU 1046  O   GLY A 138     4340   2164   2410    341    498   -357       O  
ATOM   1047  N   ASN A 139      28.291  46.014  52.660  1.00 24.09           N  
ANISOU 1047  N   ASN A 139     4470   2241   2439    425    451   -375       N  
ATOM   1048  CA  ASN A 139      27.332  44.981  52.320  1.00 23.32           C  
ANISOU 1048  CA  ASN A 139     4358   2186   2316    423    555   -321       C  
ATOM   1049  C   ASN A 139      25.902  45.386  52.718  1.00 24.39           C  
ANISOU 1049  C   ASN A 139     4550   2331   2386    475    614   -284       C  
ATOM   1050  O   ASN A 139      25.627  45.899  53.817  1.00 24.55           O  
ANISOU 1050  O   ASN A 139     4659   2332   2333    561    590   -293       O  
ATOM   1051  CB  ASN A 139      27.742  43.634  52.916  1.00 23.73           C  
ANISOU 1051  CB  ASN A 139     4416   2249   2350    458    562   -312       C  
ATOM   1052  CG  ASN A 139      29.084  43.147  52.422  1.00 25.73           C  
ANISOU 1052  CG  ASN A 139     4602   2495   2676    405    518   -339       C  
ATOM   1053  OD1 ASN A 139      29.595  43.628  51.405  1.00 26.98           O  
ANISOU 1053  OD1 ASN A 139     4696   2647   2906    334    509   -348       O  
ATOM   1054  ND2 ASN A 139      29.646  42.176  53.119  1.00 25.93           N  
ANISOU 1054  ND2 ASN A 139     4644   2522   2685    444    499   -344       N  
ATOM   1055  N   VAL A 140      24.971  45.130  51.795  1.00 26.30           N  
ANISOU 1055  N   VAL A 140     4743   2596   2654    428    692   -239       N  
ATOM   1056  CA  VAL A 140      23.536  45.322  52.007  1.00 25.33           C  
ANISOU 1056  CA  VAL A 140     4648   2480   2495    467    762   -188       C  
ATOM   1057  C   VAL A 140      22.785  44.040  51.573  1.00 25.05           C  
ANISOU 1057  C   VAL A 140     4560   2462   2494    449    839   -131       C  
ATOM   1058  O   VAL A 140      22.758  43.677  50.387  1.00 22.12           O  
ANISOU 1058  O   VAL A 140     4120   2101   2182    373    850   -129       O  
ATOM   1059  CB  VAL A 140      23.033  46.543  51.228  1.00 24.63           C  
ANISOU 1059  CB  VAL A 140     4544   2386   2426    423    763   -193       C  
ATOM   1060  CG1 VAL A 140      21.598  46.895  51.623  1.00 23.86           C  
ANISOU 1060  CG1 VAL A 140     4483   2289   2291    475    828   -141       C  
ATOM   1061  CG2 VAL A 140      23.959  47.750  51.405  1.00 25.85           C  
ANISOU 1061  CG2 VAL A 140     4726   2514   2581    418    675   -253       C  
ATOM   1062  N   ALA A 141      22.131  43.391  52.542  1.00 24.66           N  
ANISOU 1062  N   ALA A 141     4547   2412   2409    527    892    -81       N  
ATOM   1063  CA  ALA A 141      21.481  42.087  52.367  1.00 25.78           C  
ANISOU 1063  CA  ALA A 141     4639   2559   2597    522    959    -21       C  
ATOM   1064  C   ALA A 141      20.184  42.235  51.551  1.00 25.21           C  
ANISOU 1064  C   ALA A 141     4514   2481   2583    483   1010     27       C  
ATOM   1065  O   ALA A 141      19.873  41.389  50.725  1.00 24.88           O  
ANISOU 1065  O   ALA A 141     4404   2436   2613    430   1024     46       O  
ATOM   1066  CB  ALA A 141      21.206  41.484  53.725  1.00 28.69           C  
ANISOU 1066  CB  ALA A 141     5066   2921   2914    628   1006     25       C  
ATOM   1067  N   LYS A 142      19.448  43.306  51.811  1.00 25.48           N  
ANISOU 1067  N   LYS A 142     4584   2509   2587    516   1030     44       N  
ATOM   1068  CA  LYS A 142      18.151  43.614  51.190  1.00 28.85           C  
ANISOU 1068  CA  LYS A 142     4967   2925   3066    492   1076     95       C  
ATOM   1069  C   LYS A 142      18.121  45.100  50.821  1.00 27.41           C  
ANISOU 1069  C   LYS A 142     4813   2746   2854    472   1044     57       C  
ATOM   1070  O   LYS A 142      17.605  45.929  51.569  1.00 23.51           O  
ANISOU 1070  O   LYS A 142     4377   2245   2308    538   1069     77       O  
ATOM   1071  CB  LYS A 142      16.981  43.349  52.145  1.00 33.24           C  
ANISOU 1071  CB  LYS A 142     5540   3465   3624    580   1167    187       C  
ATOM   1072  CG  LYS A 142      16.993  41.989  52.813  1.00 42.23           C  
ANISOU 1072  CG  LYS A 142     6665   4596   4784    626   1213    238       C  
ATOM   1073  CD  LYS A 142      16.290  40.919  52.024  1.00 47.09           C  
ANISOU 1073  CD  LYS A 142     7178   5190   5524    568   1238    288       C  
ATOM   1074  CE  LYS A 142      16.138  39.633  52.806  1.00 49.41           C  
ANISOU 1074  CE  LYS A 142     7455   5466   5850    624   1298    356       C  
ATOM   1075  NZ  LYS A 142      15.367  38.647  52.022  1.00 53.60           N  
ANISOU 1075  NZ  LYS A 142     7879   5962   6522    567   1311    406       N  
ATOM   1076  N   ALA A 143      18.686  45.425  49.660  1.00 25.12           N  
ANISOU 1076  N   ALA A 143     4485   2464   2593    388    991      5       N  
ATOM   1077  CA  ALA A 143      18.872  46.787  49.262  1.00 25.86           C  
ANISOU 1077  CA  ALA A 143     4600   2559   2667    364    956    -32       C  
ATOM   1078  C   ALA A 143      17.560  47.342  48.690  1.00 27.85           C  
ANISOU 1078  C   ALA A 143     4828   2804   2949    350    995      9       C  
ATOM   1079  O   ALA A 143      16.660  46.591  48.355  1.00 31.89           O  
ANISOU 1079  O   ALA A 143     5290   3307   3516    340   1033     60       O  
ATOM   1080  CB  ALA A 143      19.983  46.851  48.229  1.00 27.53           C  
ANISOU 1080  CB  ALA A 143     4776   2778   2905    289    902    -88       C  
ATOM   1081  N   ASP A 144      17.520  48.671  48.538  1.00 28.03           N  
ANISOU 1081  N   ASP A 144     4880   2824   2946    345    975    -13       N  
ATOM   1082  CA  ASP A 144      16.411  49.474  48.024  1.00 31.52           C  
ANISOU 1082  CA  ASP A 144     5308   3260   3408    333   1003     17       C  
ATOM   1083  C   ASP A 144      16.940  50.228  46.796  1.00 28.20           C  
ANISOU 1083  C   ASP A 144     4864   2845   3005    260    957    -29       C  
ATOM   1084  O   ASP A 144      18.071  50.697  46.825  1.00 26.79           O  
ANISOU 1084  O   ASP A 144     4705   2667   2807    247    912    -80       O  
ATOM   1085  CB  ASP A 144      15.929  50.483  49.090  1.00 36.64           C  
ANISOU 1085  CB  ASP A 144     6029   3898   3995    411   1026     33       C  
ATOM   1086  CG  ASP A 144      14.884  51.497  48.618  1.00 48.88           C  
ANISOU 1086  CG  ASP A 144     7571   5440   5560    403   1051     61       C  
ATOM   1087  OD1 ASP A 144      13.739  51.070  48.329  1.00 55.76           O  
ANISOU 1087  OD1 ASP A 144     8395   6305   6486    401   1102    124       O  
ATOM   1088  OD2 ASP A 144      15.201  52.724  48.555  1.00 49.78           O  
ANISOU 1088  OD2 ASP A 144     7723   5549   5640    399   1016     21       O  
ATOM   1089  N   ILE A 145      16.113  50.369  45.760  1.00 24.83           N  
ANISOU 1089  N   ILE A 145     4397   2417   2620    221    969     -7       N  
ATOM   1090  CA  ILE A 145      16.551  50.986  44.520  1.00 27.24           C  
ANISOU 1090  CA  ILE A 145     4685   2727   2937    163    937    -42       C  
ATOM   1091  C   ILE A 145      17.014  52.424  44.795  1.00 26.81           C  
ANISOU 1091  C   ILE A 145     4670   2668   2849    170    918    -70       C  
ATOM   1092  O   ILE A 145      18.054  52.837  44.314  1.00 27.32           O  
ANISOU 1092  O   ILE A 145     4729   2732   2919    138    887   -108       O  
ATOM   1093  CB  ILE A 145      15.443  50.928  43.446  1.00 28.76           C  
ANISOU 1093  CB  ILE A 145     4840   2914   3172    135    946    -13       C  
ATOM   1094  CG1 ILE A 145      15.195  49.495  42.983  1.00 29.15           C  
ANISOU 1094  CG1 ILE A 145     4848   2957   3268    119    939      0       C  
ATOM   1095  CG2 ILE A 145      15.748  51.872  42.278  1.00 30.46           C  
ANISOU 1095  CG2 ILE A 145     5057   3134   3381     96    924    -41       C  
ATOM   1096  CD1 ILE A 145      13.896  49.300  42.223  1.00 30.74           C  
ANISOU 1096  CD1 ILE A 145     5012   3137   3528    106    934     35       C  
ATOM   1097  N   ILE A 146      16.247  53.181  45.584  1.00 27.05           N  
ANISOU 1097  N   ILE A 146     4737   2687   2851    217    939    -48       N  
ATOM   1098  CA  ILE A 146      16.516  54.578  45.747  1.00 30.75           C  
ANISOU 1098  CA  ILE A 146     5244   3143   3296    223    915    -75       C  
ATOM   1099  C   ILE A 146      17.605  54.827  46.801  1.00 32.74           C  
ANISOU 1099  C   ILE A 146     5545   3380   3514    259    868   -119       C  
ATOM   1100  O   ILE A 146      18.585  55.530  46.502  1.00 33.60           O  
ANISOU 1100  O   ILE A 146     5649   3473   3642    228    818   -161       O  
ATOM   1101  CB  ILE A 146      15.216  55.346  46.021  1.00 30.44           C  
ANISOU 1101  CB  ILE A 146     5227   3096   3241    260    954    -35       C  
ATOM   1102  CG1 ILE A 146      14.351  55.339  44.760  1.00 33.42           C  
ANISOU 1102  CG1 ILE A 146     5551   3480   3666    211    974     -5       C  
ATOM   1103  CG2 ILE A 146      15.525  56.757  46.483  1.00 31.58           C  
ANISOU 1103  CG2 ILE A 146     5427   3220   3351    284    924    -67       C  
ATOM   1104  CD1 ILE A 146      12.898  55.608  45.028  1.00 36.37           C  
ANISOU 1104  CD1 ILE A 146     5924   3844   4049    247   1023     52       C  
ATOM   1105  N   ASP A 147      17.473  54.228  47.984  1.00 28.76           N  
ANISOU 1105  N   ASP A 147     5085   2874   2968    327    880   -108       N  
ATOM   1106  CA  ASP A 147      18.435  54.436  49.073  1.00 31.70           C  
ANISOU 1106  CA  ASP A 147     5519   3226   3298    377    822   -154       C  
ATOM   1107  C   ASP A 147      19.851  53.948  48.750  1.00 28.68           C  
ANISOU 1107  C   ASP A 147     5099   2841   2956    328    765   -198       C  
ATOM   1108  O   ASP A 147      20.786  54.448  49.383  1.00 26.44           O  
ANISOU 1108  O   ASP A 147     4851   2528   2665    350    692   -246       O  
ATOM   1109  CB  ASP A 147      18.023  53.739  50.371  1.00 33.32           C  
ANISOU 1109  CB  ASP A 147     5786   3431   3441    472    854   -127       C  
ATOM   1110  CG  ASP A 147      17.050  54.581  51.159  1.00 43.26           C  
ANISOU 1110  CG  ASP A 147     7121   4677   4640    557    888   -100       C  
ATOM   1111  OD1 ASP A 147      17.210  55.819  51.132  1.00 49.34           O  
ANISOU 1111  OD1 ASP A 147     7925   5424   5398    556    842   -136       O  
ATOM   1112  OD2 ASP A 147      16.113  54.005  51.727  1.00 48.83           O  
ANISOU 1112  OD2 ASP A 147     7843   5390   5320    621    965    -36       O  
ATOM   1113  N   ASN A 148      19.999  52.954  47.862  1.00 25.58           N  
ANISOU 1113  N   ASN A 148     4638   2472   2606    273    792   -182       N  
ATOM   1114  CA  ASN A 148      21.322  52.366  47.560  1.00 26.16           C  
ANISOU 1114  CA  ASN A 148     4674   2545   2718    235    752   -214       C  
ATOM   1115  C   ASN A 148      21.763  52.688  46.127  1.00 26.10           C  
ANISOU 1115  C   ASN A 148     4604   2541   2770    160    756   -216       C  
ATOM   1116  O   ASN A 148      22.689  52.051  45.609  1.00 24.40           O  
ANISOU 1116  O   ASN A 148     4346   2330   2592    127    748   -226       O  
ATOM   1117  CB  ASN A 148      21.345  50.863  47.825  1.00 27.76           C  
ANISOU 1117  CB  ASN A 148     4864   2769   2914    249    779   -196       C  
ATOM   1118  CG  ASN A 148      21.053  50.534  49.281  1.00 27.01           C  
ANISOU 1118  CG  ASN A 148     4837   2668   2758    335    781   -187       C  
ATOM   1119  OD1 ASN A 148      19.999  49.984  49.606  1.00 28.58           O  
ANISOU 1119  OD1 ASN A 148     5045   2878   2936    373    843   -137       O  
ATOM   1120  ND2 ASN A 148      21.965  50.882  50.169  1.00 27.87           N  
ANISOU 1120  ND2 ASN A 148     4994   2753   2841    374    714   -232       N  
ATOM   1121  N   SER A 149      21.130  53.707  45.523  1.00 25.60           N  
ANISOU 1121  N   SER A 149     4540   2474   2713    143    773   -204       N  
ATOM   1122  CA  SER A 149      21.562  54.367  44.254  1.00 26.58           C  
ANISOU 1122  CA  SER A 149     4620   2594   2885     88    778   -203       C  
ATOM   1123  C   SER A 149      21.697  53.377  43.105  1.00 25.91           C  
ANISOU 1123  C   SER A 149     4492   2534   2818     55    813   -186       C  
ATOM   1124  O   SER A 149      22.653  53.468  42.281  1.00 26.02           O  
ANISOU 1124  O   SER A 149     4470   2543   2874     25    815   -189       O  
ATOM   1125  CB  SER A 149      22.842  55.083  44.485  1.00 29.56           C  
ANISOU 1125  CB  SER A 149     4984   2935   3312     76    723   -234       C  
ATOM   1126  OG  SER A 149      22.650  56.045  45.502  1.00 29.62           O  
ANISOU 1126  OG  SER A 149     5042   2911   3298    113    677   -257       O  
ATOM   1127  N   ILE A 150      20.753  52.430  43.045  1.00 24.82           N  
ANISOU 1127  N   ILE A 150     4357   2416   2654     67    841   -165       N  
ATOM   1128  CA  ILE A 150      20.842  51.362  42.076  1.00 25.22           C  
ANISOU 1128  CA  ILE A 150     4380   2483   2716     46    859   -158       C  
ATOM   1129  C   ILE A 150      20.622  51.903  40.659  1.00 23.92           C  
ANISOU 1129  C   ILE A 150     4206   2322   2559     23    877   -147       C  
ATOM   1130  O   ILE A 150      21.207  51.366  39.722  1.00 22.52           O  
ANISOU 1130  O   ILE A 150     4015   2151   2389     12    887   -149       O  
ATOM   1131  CB  ILE A 150      19.886  50.210  42.431  1.00 27.31           C  
ANISOU 1131  CB  ILE A 150     4646   2757   2972     65    871   -137       C  
ATOM   1132  CG1 ILE A 150      20.261  49.627  43.792  1.00 28.32           C  
ANISOU 1132  CG1 ILE A 150     4789   2882   3086     99    862   -143       C  
ATOM   1133  CG2 ILE A 150      19.901  49.146  41.352  1.00 26.52           C  
ANISOU 1133  CG2 ILE A 150     4524   2663   2886     47    874   -136       C  
ATOM   1134  CD1 ILE A 150      19.450  48.417  44.149  1.00 29.86           C  
ANISOU 1134  CD1 ILE A 150     4976   3081   3288    119    884   -113       C  
ATOM   1135  N   PHE A 151      19.814  52.958  40.505  1.00 23.60           N  
ANISOU 1135  N   PHE A 151     4179   2275   2510     23    883   -135       N  
ATOM   1136  CA  PHE A 151      19.606  53.581  39.179  1.00 25.19           C  
ANISOU 1136  CA  PHE A 151     4379   2478   2713      8    900   -124       C  
ATOM   1137  C   PHE A 151      20.910  54.124  38.580  1.00 23.77           C  
ANISOU 1137  C   PHE A 151     4182   2290   2559     -4    913   -127       C  
ATOM   1138  O   PHE A 151      20.947  54.386  37.399  1.00 24.20           O  
ANISOU 1138  O   PHE A 151     4239   2347   2609     -4    939   -112       O  
ATOM   1139  CB  PHE A 151      18.586  54.721  39.265  1.00 26.92           C  
ANISOU 1139  CB  PHE A 151     4613   2689   2923     12    904   -110       C  
ATOM   1140  CG  PHE A 151      17.135  54.317  39.276  1.00 25.40           C  
ANISOU 1140  CG  PHE A 151     4427   2500   2723     23    905    -89       C  
ATOM   1141  CD1 PHE A 151      16.695  53.165  38.658  1.00 27.63           C  
ANISOU 1141  CD1 PHE A 151     4699   2786   3012     23    895    -85       C  
ATOM   1142  CD2 PHE A 151      16.194  55.137  39.872  1.00 26.68           C  
ANISOU 1142  CD2 PHE A 151     4600   2654   2880     37    913    -72       C  
ATOM   1143  CE1 PHE A 151      15.350  52.823  38.666  1.00 28.42           C  
ANISOU 1143  CE1 PHE A 151     4789   2875   3131     30    887    -61       C  
ATOM   1144  CE2 PHE A 151      14.855  54.788  39.889  1.00 27.55           C  
ANISOU 1144  CE2 PHE A 151     4703   2760   3003     49    918    -42       C  
ATOM   1145  CZ  PHE A 151      14.429  53.641  39.269  1.00 28.27           C  
ANISOU 1145  CZ  PHE A 151     4772   2849   3119     42    903    -35       C  
ATOM   1146  N   TYR A 152      21.953  54.312  39.412  1.00 24.57           N  
ANISOU 1146  N   TYR A 152     4265   2375   2693     -9    894   -141       N  
ATOM   1147  CA  TYR A 152      23.284  54.791  39.001  1.00 25.91           C  
ANISOU 1147  CA  TYR A 152     4400   2524   2919    -22    904   -134       C  
ATOM   1148  C   TYR A 152      24.264  53.621  38.738  1.00 26.26           C  
ANISOU 1148  C   TYR A 152     4420   2576   2978    -20    916   -135       C  
ATOM   1149  O   TYR A 152      25.457  53.837  38.496  1.00 24.81           O  
ANISOU 1149  O   TYR A 152     4198   2373   2855    -28    928   -122       O  
ATOM   1150  CB  TYR A 152      23.804  55.770  40.059  1.00 26.03           C  
ANISOU 1150  CB  TYR A 152     4406   2503   2980    -28    858   -152       C  
ATOM   1151  CG  TYR A 152      22.943  57.018  40.162  1.00 26.14           C  
ANISOU 1151  CG  TYR A 152     4445   2505   2982    -27    852   -149       C  
ATOM   1152  CD1 TYR A 152      21.818  57.059  40.976  1.00 25.31           C  
ANISOU 1152  CD1 TYR A 152     4384   2410   2822     -4    836   -161       C  
ATOM   1153  CD2 TYR A 152      23.218  58.140  39.398  1.00 27.63           C  
ANISOU 1153  CD2 TYR A 152     4610   2670   3215    -42    873   -126       C  
ATOM   1154  CE1 TYR A 152      21.017  58.184  41.051  1.00 25.71           C  
ANISOU 1154  CE1 TYR A 152     4458   2448   2859      1    836   -155       C  
ATOM   1155  CE2 TYR A 152      22.421  59.272  39.446  1.00 27.15           C  
ANISOU 1155  CE2 TYR A 152     4573   2598   3144    -41    869   -123       C  
ATOM   1156  CZ  TYR A 152      21.314  59.297  40.273  1.00 26.87           C  
ANISOU 1156  CZ  TYR A 152     4584   2574   3049    -19    849   -140       C  
ATOM   1157  OH  TYR A 152      20.517  60.407  40.279  1.00 25.93           O  
ANISOU 1157  OH  TYR A 152     4489   2444   2919    -14    850   -133       O  
ATOM   1158  N   ALA A 153      23.779  52.376  38.822  1.00 27.54           N  
ANISOU 1158  N   ALA A 153     4602   2763   3097     -9    913   -145       N  
ATOM   1159  CA  ALA A 153      24.612  51.200  38.545  1.00 27.31           C  
ANISOU 1159  CA  ALA A 153     4558   2743   3076     -2    924   -147       C  
ATOM   1160  C   ALA A 153      23.777  50.154  37.796  1.00 25.93           C  
ANISOU 1160  C   ALA A 153     4413   2589   2850     12    934   -148       C  
ATOM   1161  O   ALA A 153      23.572  49.029  38.296  1.00 24.61           O  
ANISOU 1161  O   ALA A 153     4249   2430   2672     17    914   -161       O  
ATOM   1162  CB  ALA A 153      25.133  50.667  39.860  1.00 28.40           C  
ANISOU 1162  CB  ALA A 153     4683   2874   3231     -3    885   -169       C  
ATOM   1163  N   LEU A 154      23.280  50.518  36.604  1.00 24.07           N  
ANISOU 1163  N   LEU A 154     4201   2356   2587     23    957   -134       N  
ATOM   1164  CA  LEU A 154      22.346  49.651  35.878  1.00 25.54           C  
ANISOU 1164  CA  LEU A 154     4422   2550   2732     42    942   -142       C  
ATOM   1165  C   LEU A 154      23.018  48.735  34.834  1.00 24.28           C  
ANISOU 1165  C   LEU A 154     4285   2393   2547     73    961   -143       C  
ATOM   1166  O   LEU A 154      22.306  48.153  34.027  1.00 24.36           O  
ANISOU 1166  O   LEU A 154     4334   2399   2519     97    939   -154       O  
ATOM   1167  CB  LEU A 154      21.284  50.519  35.216  1.00 25.07           C  
ANISOU 1167  CB  LEU A 154     4389   2487   2649     46    939   -132       C  
ATOM   1168  CG  LEU A 154      20.305  51.194  36.174  1.00 26.08           C  
ANISOU 1168  CG  LEU A 154     4505   2611   2792     26    918   -129       C  
ATOM   1169  CD1 LEU A 154      19.386  52.143  35.412  1.00 27.04           C  
ANISOU 1169  CD1 LEU A 154     4649   2728   2896     31    919   -116       C  
ATOM   1170  CD2 LEU A 154      19.499  50.158  36.926  1.00 26.31           C  
ANISOU 1170  CD2 LEU A 154     4527   2638   2831     25    886   -136       C  
ATOM   1171  N   SER A 155      24.348  48.600  34.835  1.00 25.49           N  
ANISOU 1171  N   SER A 155     4413   2546   2724     78    997   -132       N  
ATOM   1172  CA  SER A 155      25.010  47.592  33.927  1.00 26.21           C  
ANISOU 1172  CA  SER A 155     4530   2639   2787    118   1022   -131       C  
ATOM   1173  C   SER A 155      24.478  46.189  34.272  1.00 25.65           C  
ANISOU 1173  C   SER A 155     4474   2570   2700    119    971   -164       C  
ATOM   1174  O   SER A 155      23.940  45.956  35.393  1.00 25.13           O  
ANISOU 1174  O   SER A 155     4382   2505   2661     87    933   -176       O  
ATOM   1175  CB  SER A 155      26.519  47.643  34.020  1.00 25.48           C  
ANISOU 1175  CB  SER A 155     4396   2543   2741    122   1073   -105       C  
ATOM   1176  OG  SER A 155      26.997  46.883  35.134  1.00 26.78           O  
ANISOU 1176  OG  SER A 155     4523   2709   2943     97   1043   -123       O  
ATOM   1177  N   VAL A 156      24.605  45.259  33.329  1.00 25.74           N  
ANISOU 1177  N   VAL A 156     4530   2578   2670    162    971   -174       N  
ATOM   1178  CA  VAL A 156      24.230  43.854  33.625  1.00 24.86           C  
ANISOU 1178  CA  VAL A 156     4427   2458   2558    163    919   -204       C  
ATOM   1179  C   VAL A 156      25.434  43.079  34.158  1.00 24.01           C  
ANISOU 1179  C   VAL A 156     4288   2358   2475    162    945   -202       C  
ATOM   1180  O   VAL A 156      25.388  41.847  34.161  1.00 27.01           O  
ANISOU 1180  O   VAL A 156     4682   2730   2849    175    915   -223       O  
ATOM   1181  CB  VAL A 156      23.584  43.146  32.424  1.00 25.52           C  
ANISOU 1181  CB  VAL A 156     4582   2523   2589    212    878   -229       C  
ATOM   1182  CG1 VAL A 156      22.293  43.826  32.037  1.00 26.07           C  
ANISOU 1182  CG1 VAL A 156     4675   2581   2649    208    836   -234       C  
ATOM   1183  CG2 VAL A 156      24.523  43.017  31.218  1.00 27.41           C  
ANISOU 1183  CG2 VAL A 156     4879   2764   2769    280    929   -220       C  
ATOM   1184  N   LEU A 157      26.479  43.759  34.641  1.00 24.34           N  
ANISOU 1184  N   LEU A 157     4283   2407   2554    146    990   -177       N  
ATOM   1185  CA  LEU A 157      27.678  43.087  35.144  1.00 24.41           C  
ANISOU 1185  CA  LEU A 157     4257   2419   2598    145   1010   -172       C  
ATOM   1186  C   LEU A 157      27.434  42.670  36.603  1.00 23.05           C  
ANISOU 1186  C   LEU A 157     4049   2249   2460    107    964   -191       C  
ATOM   1187  O   LEU A 157      28.142  43.094  37.522  1.00 23.59           O  
ANISOU 1187  O   LEU A 157     4072   2316   2573     85    964   -184       O  
ATOM   1188  CB  LEU A 157      28.891  43.995  34.957  1.00 26.98           C  
ANISOU 1188  CB  LEU A 157     4541   2739   2968    148   1071   -133       C  
ATOM   1189  CG  LEU A 157      29.111  44.453  33.516  1.00 29.18           C  
ANISOU 1189  CG  LEU A 157     4860   3014   3211    199   1135   -100       C  
ATOM   1190  CD1 LEU A 157      30.325  45.363  33.393  1.00 33.74           C  
ANISOU 1190  CD1 LEU A 157     5379   3578   3861    200   1205    -45       C  
ATOM   1191  CD2 LEU A 157      29.262  43.263  32.581  1.00 32.99           C  
ANISOU 1191  CD2 LEU A 157     5403   3498   3630    260   1151   -109       C  
ATOM   1192  N   LYS A 158      26.470  41.752  36.738  1.00 21.21           N  
ANISOU 1192  N   LYS A 158     3838   2013   2208    109    922   -212       N  
ATOM   1193  CA  LYS A 158      25.799  41.395  37.987  1.00 21.97           C  
ANISOU 1193  CA  LYS A 158     3912   2107   2325     86    886   -219       C  
ATOM   1194  C   LYS A 158      25.305  39.942  37.902  1.00 22.39           C  
ANISOU 1194  C   LYS A 158     3979   2148   2379     98    855   -233       C  
ATOM   1195  O   LYS A 158      25.245  39.329  36.812  1.00 22.72           O  
ANISOU 1195  O   LYS A 158     4056   2178   2397    123    845   -247       O  
ATOM   1196  CB  LYS A 158      24.581  42.286  38.242  1.00 22.07           C  
ANISOU 1196  CB  LYS A 158     3930   2116   2337     70    869   -212       C  
ATOM   1197  CG  LYS A 158      24.881  43.771  38.492  1.00 21.99           C  
ANISOU 1197  CG  LYS A 158     3908   2112   2333     56    889   -200       C  
ATOM   1198  CD  LYS A 158      23.661  44.623  38.455  1.00 22.15           C  
ANISOU 1198  CD  LYS A 158     3941   2128   2344     48    878   -193       C  
ATOM   1199  CE  LYS A 158      23.938  46.088  38.736  1.00 24.33           C  
ANISOU 1199  CE  LYS A 158     4209   2405   2628     36    892   -184       C  
ATOM   1200  NZ  LYS A 158      24.762  46.740  37.682  1.00 26.06           N  
ANISOU 1200  NZ  LYS A 158     4427   2622   2849     40    926   -173       N  
ATOM   1201  N   MET A 159      24.896  39.413  39.058  1.00 22.76           N  
ANISOU 1201  N   MET A 159     4000   2191   2453     86    838   -228       N  
ATOM   1202  CA  MET A 159      24.419  38.013  39.163  1.00 23.00           C  
ANISOU 1202  CA  MET A 159     4029   2203   2507     94    810   -233       C  
ATOM   1203  C   MET A 159      22.890  38.017  39.261  1.00 20.86           C  
ANISOU 1203  C   MET A 159     3751   1907   2267     85    780   -219       C  
ATOM   1204  O   MET A 159      22.338  38.534  40.214  1.00 22.93           O  
ANISOU 1204  O   MET A 159     3993   2172   2545     78    793   -194       O  
ATOM   1205  CB  MET A 159      25.027  37.315  40.382  1.00 24.80           C  
ANISOU 1205  CB  MET A 159     4230   2438   2755     95    820   -225       C  
ATOM   1206  CG  MET A 159      24.770  35.781  40.411  1.00 27.50           C  
ANISOU 1206  CG  MET A 159     4564   2756   3125    104    797   -228       C  
ATOM   1207  SD  MET A 159      25.649  34.951  41.762  1.00 24.84           S  
ANISOU 1207  SD  MET A 159     4203   2432   2802    114    815   -218       S  
ATOM   1208  CE  MET A 159      27.328  34.968  41.148  1.00 28.77           C  
ANISOU 1208  CE  MET A 159     4708   2949   3274    121    833   -241       C  
ATOM   1209  N   PHE A 160      22.228  37.509  38.221  1.00 21.74           N  
ANISOU 1209  N   PHE A 160     3884   1989   2388     93    737   -234       N  
ATOM   1210  CA  PHE A 160      20.786  37.541  38.070  1.00 22.56           C  
ANISOU 1210  CA  PHE A 160     3974   2057   2538     85    696   -221       C  
ATOM   1211  C   PHE A 160      20.207  36.141  38.234  1.00 22.57           C  
ANISOU 1211  C   PHE A 160     3949   2013   2611     87    652   -216       C  
ATOM   1212  O   PHE A 160      20.687  35.234  37.586  1.00 22.77           O  
ANISOU 1212  O   PHE A 160     4000   2023   2627    103    621   -248       O  
ATOM   1213  CB  PHE A 160      20.392  37.979  36.660  1.00 23.32           C  
ANISOU 1213  CB  PHE A 160     4117   2138   2603     99    656   -247       C  
ATOM   1214  CG  PHE A 160      20.719  39.409  36.323  1.00 23.52           C  
ANISOU 1214  CG  PHE A 160     4166   2198   2572     99    696   -244       C  
ATOM   1215  CD1 PHE A 160      21.986  39.766  35.897  1.00 22.97           C  
ANISOU 1215  CD1 PHE A 160     4123   2157   2446    115    741   -254       C  
ATOM   1216  CD2 PHE A 160      19.759  40.393  36.457  1.00 24.89           C  
ANISOU 1216  CD2 PHE A 160     4327   2368   2761     84    694   -224       C  
ATOM   1217  CE1 PHE A 160      22.275  41.082  35.578  1.00 24.59           C  
ANISOU 1217  CE1 PHE A 160     4340   2385   2617    115    779   -244       C  
ATOM   1218  CE2 PHE A 160      20.050  41.716  36.157  1.00 24.23           C  
ANISOU 1218  CE2 PHE A 160     4262   2310   2631     83    730   -220       C  
ATOM   1219  CZ  PHE A 160      21.307  42.049  35.708  1.00 25.56           C  
ANISOU 1219  CZ  PHE A 160     4455   2504   2750     98    771   -230       C  
ATOM   1220  N   LYS A 161      19.137  36.014  39.034  1.00 24.92           N  
ANISOU 1220  N   LYS A 161     4197   2284   2985     75    651   -173       N  
ATOM   1221  CA  LYS A 161      18.391  34.751  39.209  1.00 25.56           C  
ANISOU 1221  CA  LYS A 161     4235   2308   3166     73    609   -154       C  
ATOM   1222  C   LYS A 161      17.590  34.422  37.934  1.00 26.79           C  
ANISOU 1222  C   LYS A 161     4407   2406   3366     74    513   -185       C  
ATOM   1223  O   LYS A 161      16.698  35.171  37.493  1.00 25.74           O  
ANISOU 1223  O   LYS A 161     4272   2255   3252     68    485   -178       O  
ATOM   1224  CB  LYS A 161      17.476  34.810  40.440  1.00 28.22           C  
ANISOU 1224  CB  LYS A 161     4510   2629   3581     70    652    -83       C  
ATOM   1225  CG  LYS A 161      16.675  33.543  40.688  1.00 30.90           C  
ANISOU 1225  CG  LYS A 161     4790   2901   4049     69    620    -45       C  
ATOM   1226  CD  LYS A 161      15.925  33.549  41.986  1.00 36.76           C  
ANISOU 1226  CD  LYS A 161     5472   3631   4863     80    689     39       C  
ATOM   1227  CE  LYS A 161      16.811  33.118  43.134  1.00 43.34           C  
ANISOU 1227  CE  LYS A 161     6313   4503   5651    106    760     58       C  
ATOM   1228  NZ  LYS A 161      16.064  33.148  44.415  1.00 52.29           N  
ANISOU 1228  NZ  LYS A 161     7403   5623   6839    137    837    148       N  
ATOM   1229  N   LYS A 162      17.901  33.255  37.370  1.00 25.24           N  
ANISOU 1229  N   LYS A 162     4228   2174   3186     87    456   -220       N  
ATOM   1230  CA  LYS A 162      17.476  32.865  36.041  1.00 26.08           C  
ANISOU 1230  CA  LYS A 162     4379   2225   3302    105    351   -271       C  
ATOM   1231  C   LYS A 162      15.962  32.652  35.991  1.00 27.34           C  
ANISOU 1231  C   LYS A 162     4480   2306   3600     87    273   -243       C  
ATOM   1232  O   LYS A 162      15.345  32.946  34.983  1.00 28.06           O  
ANISOU 1232  O   LYS A 162     4605   2359   3694     98    189   -276       O  
ATOM   1233  CB  LYS A 162      18.278  31.637  35.597  1.00 28.88           C  
ANISOU 1233  CB  LYS A 162     4774   2562   3637    131    314   -315       C  
ATOM   1234  CG  LYS A 162      17.949  31.153  34.198  1.00 30.83           C  
ANISOU 1234  CG  LYS A 162     5089   2747   3876    168    195   -377       C  
ATOM   1235  CD  LYS A 162      18.218  32.187  33.151  1.00 31.98           C  
ANISOU 1235  CD  LYS A 162     5321   2926   3902    202    197   -412       C  
ATOM   1236  CE  LYS A 162      18.628  31.578  31.826  1.00 34.30           C  
ANISOU 1236  CE  LYS A 162     5724   3188   4121    269    120   -481       C  
ATOM   1237  NZ  LYS A 162      17.572  30.701  31.284  1.00 34.97           N  
ANISOU 1237  NZ  LYS A 162     5812   3171   4303    279    -30   -516       N  
ATOM   1238  N   SER A 163      15.360  32.168  37.085  1.00 28.05           N  
ANISOU 1238  N   SER A 163     4480   2367   3808     65    304   -178       N  
ATOM   1239  CA  SER A 163      13.904  31.905  37.109  1.00 30.82           C  
ANISOU 1239  CA  SER A 163     4754   2633   4322     47    238   -135       C  
ATOM   1240  C   SER A 163      13.086  33.186  36.846  1.00 29.92           C  
ANISOU 1240  C   SER A 163     4636   2526   4203     39    238   -118       C  
ATOM   1241  O   SER A 163      12.006  33.152  36.211  1.00 30.10           O  
ANISOU 1241  O   SER A 163     4632   2475   4328     33    141   -118       O  
ATOM   1242  CB  SER A 163      13.511  31.232  38.418  1.00 30.36           C  
ANISOU 1242  CB  SER A 163     4599   2550   4386     36    303    -49       C  
ATOM   1243  OG  SER A 163      13.827  32.074  39.521  1.00 30.40           O  
ANISOU 1243  OG  SER A 163     4597   2630   4321     40    432      0       O  
ATOM   1244  N   VAL A 164      13.595  34.325  37.326  1.00 28.44           N  
ANISOU 1244  N   VAL A 164     4476   2423   3905     40    339   -104       N  
ATOM   1245  CA  VAL A 164      12.962  35.618  37.130  1.00 29.50           C  
ANISOU 1245  CA  VAL A 164     4615   2574   4017     35    352    -89       C  
ATOM   1246  C   VAL A 164      12.994  35.988  35.641  1.00 30.40           C  
ANISOU 1246  C   VAL A 164     4807   2677   4064     50    260   -162       C  
ATOM   1247  O   VAL A 164      11.985  36.463  35.097  1.00 29.79           O  
ANISOU 1247  O   VAL A 164     4719   2559   4041     46    197   -158       O  
ATOM   1248  CB  VAL A 164      13.631  36.717  37.973  1.00 30.13           C  
ANISOU 1248  CB  VAL A 164     4715   2741   3990     37    471    -67       C  
ATOM   1249  CG1 VAL A 164      13.081  38.093  37.615  1.00 31.47           C  
ANISOU 1249  CG1 VAL A 164     4902   2929   4125     33    478    -62       C  
ATOM   1250  CG2 VAL A 164      13.468  36.448  39.470  1.00 29.80           C  
ANISOU 1250  CG2 VAL A 164     4612   2706   4004     40    559      7       C  
ATOM   1251  N   ILE A 165      14.146  35.758  35.001  1.00 28.37           N  
ANISOU 1251  N   ILE A 165     4633   2456   3691     75    256   -223       N  
ATOM   1252  CA  ILE A 165      14.316  36.017  33.558  1.00 32.10           C  
ANISOU 1252  CA  ILE A 165     5198   2918   4077    110    180   -290       C  
ATOM   1253  C   ILE A 165      13.349  35.124  32.762  1.00 32.87           C  
ANISOU 1253  C   ILE A 165     5294   2915   4278    122     30   -322       C  
ATOM   1254  O   ILE A 165      12.602  35.637  31.913  1.00 32.47           O  
ANISOU 1254  O   ILE A 165     5275   2830   4232    137    -50   -344       O  
ATOM   1255  CB  ILE A 165      15.792  35.837  33.156  1.00 33.50           C  
ANISOU 1255  CB  ILE A 165     5456   3150   4121    144    226   -333       C  
ATOM   1256  CG1 ILE A 165      16.644  36.940  33.790  1.00 31.76           C  
ANISOU 1256  CG1 ILE A 165     5234   3016   3816    131    352   -305       C  
ATOM   1257  CG2 ILE A 165      15.970  35.759  31.636  1.00 33.99           C  
ANISOU 1257  CG2 ILE A 165     5626   3188   4097    203    145   -399       C  
ATOM   1258  CD1 ILE A 165      18.113  36.636  33.892  1.00 32.24           C  
ANISOU 1258  CD1 ILE A 165     5327   3124   3795    148    418   -320       C  
ATOM   1259  N   ASP A 166      13.319  33.820  33.092  1.00 32.90           N  
ANISOU 1259  N   ASP A 166     5257   2866   4375    115    -13   -320       N  
ATOM   1260  CA  ASP A 166      12.486  32.835  32.404  1.00 34.84           C  
ANISOU 1260  CA  ASP A 166     5495   3001   4739    126   -170   -353       C  
ATOM   1261  C   ASP A 166      10.993  33.145  32.581  1.00 35.02           C  
ANISOU 1261  C   ASP A 166     5425   2954   4925     94   -229   -304       C  
ATOM   1262  O   ASP A 166      10.262  33.231  31.615  1.00 32.76           O  
ANISOU 1262  O   ASP A 166     5170   2602   4674    112   -359   -344       O  
ATOM   1263  CB  ASP A 166      12.789  31.421  32.887  1.00 37.02           C  
ANISOU 1263  CB  ASP A 166     5730   3235   5098    119   -188   -350       C  
ATOM   1264  CG  ASP A 166      14.164  30.905  32.494  1.00 41.24           C  
ANISOU 1264  CG  ASP A 166     6361   3816   5491    160   -162   -408       C  
ATOM   1265  OD1 ASP A 166      14.861  31.607  31.725  1.00 44.88           O  
ANISOU 1265  OD1 ASP A 166     6924   4334   5795    200   -137   -451       O  
ATOM   1266  OD2 ASP A 166      14.536  29.801  32.967  1.00 48.25           O  
ANISOU 1266  OD2 ASP A 166     7218   4682   6433    154   -160   -403       O  
ATOM   1267  N   LYS A 167      10.539  33.316  33.823  1.00 33.21           N  
ANISOU 1267  N   LYS A 167     5086   2736   4796     53   -132   -213       N  
ATOM   1268  CA  LYS A 167       9.108  33.500  34.092  1.00 36.06           C  
ANISOU 1268  CA  LYS A 167     5342   3023   5337     26   -173   -148       C  
ATOM   1269  C   LYS A 167       8.553  34.748  33.382  1.00 37.33           C  
ANISOU 1269  C   LYS A 167     5541   3196   5445     33   -205   -164       C  
ATOM   1270  O   LYS A 167       7.410  34.746  32.973  1.00 39.74           O  
ANISOU 1270  O   LYS A 167     5796   3416   5886     25   -310   -152       O  
ATOM   1271  CB  LYS A 167       8.867  33.611  35.598  1.00 38.34           C  
ANISOU 1271  CB  LYS A 167     5525   3338   5703      0    -30    -39       C  
ATOM   1272  CG  LYS A 167       7.499  34.152  35.999  1.00 41.61           C  
ANISOU 1272  CG  LYS A 167     5837   3701   6271    -18    -21     46       C  
ATOM   1273  N   ASN A 168       9.359  35.811  33.263  1.00 36.80           N  
ANISOU 1273  N   ASN A 168     5557   3231   5194     48   -114   -188       N  
ATOM   1274  CA  ASN A 168       8.926  37.110  32.754  1.00 35.21           C  
ANISOU 1274  CA  ASN A 168     5389   3056   4933     54   -114   -192       C  
ATOM   1275  C   ASN A 168       9.418  37.333  31.316  1.00 36.88           C  
ANISOU 1275  C   ASN A 168     5734   3275   5004    103   -200   -285       C  
ATOM   1276  O   ASN A 168       9.206  38.410  30.760  1.00 36.70           O  
ANISOU 1276  O   ASN A 168     5757   3278   4909    118   -199   -295       O  
ATOM   1277  CB  ASN A 168       9.425  38.230  33.671  1.00 34.91           C  
ANISOU 1277  CB  ASN A 168     5345   3117   4799     41     48   -144       C  
ATOM   1278  CG  ASN A 168       8.820  38.114  35.049  1.00 35.45           C  
ANISOU 1278  CG  ASN A 168     5300   3176   4993     13    133    -48       C  
ATOM   1279  OD1 ASN A 168       7.614  38.300  35.190  1.00 39.77           O  
ANISOU 1279  OD1 ASN A 168     5770   3665   5675      0    105      5       O  
ATOM   1280  ND2 ASN A 168       9.618  37.729  36.036  1.00 32.16           N  
ANISOU 1280  ND2 ASN A 168     4872   2805   4541     12    232    -24       N  
ATOM   1281  N   LYS A 169      10.104  36.335  30.746  1.00 35.83           N  
ANISOU 1281  N   LYS A 169     5667   3120   4826    136   -263   -347       N  
ATOM   1282  CA  LYS A 169      10.583  36.361  29.382  1.00 39.13           C  
ANISOU 1282  CA  LYS A 169     6223   3535   5108    202   -343   -432       C  
ATOM   1283  C   LYS A 169      11.364  37.661  29.142  1.00 37.38           C  
ANISOU 1283  C   LYS A 169     6074   3414   4712    224   -226   -431       C  
ATOM   1284  O   LYS A 169      11.139  38.353  28.157  1.00 38.86           O  
ANISOU 1284  O   LYS A 169     6341   3599   4823    267   -274   -463       O  
ATOM   1285  CB  LYS A 169       9.406  36.219  28.409  1.00 42.59           C  
ANISOU 1285  CB  LYS A 169     6679   3869   5631    226   -526   -471       C  
ATOM   1286  CG  LYS A 169       8.684  34.874  28.429  1.00 46.86           C  
ANISOU 1286  CG  LYS A 169     7157   4290   6356    213   -673   -483       C  
ATOM   1287  CD  LYS A 169       7.314  34.964  27.796  1.00 53.59           C  
ANISOU 1287  CD  LYS A 169     7981   5035   7345    215   -842   -496       C  
ATOM   1288  CE  LYS A 169       6.476  33.714  27.951  1.00 57.83           C  
ANISOU 1288  CE  LYS A 169     8422   5438   8111    190   -987   -490       C  
ATOM   1289  NZ  LYS A 169       6.198  33.090  26.639  1.00 65.58           N  
ANISOU 1289  NZ  LYS A 169     9508   6316   9091    255  -1209   -593       N  
ATOM   1290  N   ILE A 170      12.307  37.955  30.042  1.00 32.48           N  
ANISOU 1290  N   ILE A 170     5427   2877   4036    198    -77   -393       N  
ATOM   1291  CA  ILE A 170      13.152  39.100  29.918  1.00 32.17           C  
ANISOU 1291  CA  ILE A 170     5440   2924   3858    213     34   -387       C  
ATOM   1292  C   ILE A 170      14.275  38.776  28.927  1.00 32.88           C  
ANISOU 1292  C   ILE A 170     5649   3035   3809    283     35   -441       C  
ATOM   1293  O   ILE A 170      14.992  37.782  29.058  1.00 33.95           O  
ANISOU 1293  O   ILE A 170     5796   3168   3936    295     39   -460       O  
ATOM   1294  CB  ILE A 170      13.689  39.541  31.292  1.00 29.82           C  
ANISOU 1294  CB  ILE A 170     5067   2693   3569    163    173   -328       C  
ATOM   1295  CG1 ILE A 170      12.554  39.807  32.287  1.00 29.88           C  
ANISOU 1295  CG1 ILE A 170     4968   2677   3707    113    183   -267       C  
ATOM   1296  CG2 ILE A 170      14.588  40.760  31.124  1.00 31.18           C  
ANISOU 1296  CG2 ILE A 170     5287   2942   3616    176    276   -323       C  
ATOM   1297  CD1 ILE A 170      13.011  40.277  33.673  1.00 28.96           C  
ANISOU 1297  CD1 ILE A 170     4795   2621   3587     80    312   -212       C  
ATOM   1298  N   LYS A 171      14.430  39.643  27.926  1.00 34.06           N  
ANISOU 1298  N   LYS A 171     5888   3204   3847    335     40   -461       N  
ATOM   1299  CA  LYS A 171      15.422  39.484  26.875  1.00 34.69           C  
ANISOU 1299  CA  LYS A 171     6092   3302   3787    420     55   -500       C  
ATOM   1300  C   LYS A 171      16.014  40.855  26.588  1.00 32.60           C  
ANISOU 1300  C   LYS A 171     5862   3104   3420    440    170   -468       C  
ATOM   1301  O   LYS A 171      15.383  41.859  26.858  1.00 34.57           O  
ANISOU 1301  O   LYS A 171     6067   3366   3699    402    189   -438       O  
ATOM   1302  CB  LYS A 171      14.811  38.931  25.583  1.00 34.91           C  
ANISOU 1302  CB  LYS A 171     6227   3254   3781    500    -98   -566       C  
ATOM   1303  CG  LYS A 171      14.336  37.491  25.659  1.00 39.92           C  
ANISOU 1303  CG  LYS A 171     6844   3807   4516    495   -231   -607       C  
ATOM   1304  N   PHE A 172      17.224  40.863  26.024  1.00 33.08           N  
ANISOU 1304  N   PHE A 172     5999   3201   3368    503    249   -471       N  
ATOM   1305  CA  PHE A 172      17.856  42.066  25.546  1.00 32.37           C  
ANISOU 1305  CA  PHE A 172     5951   3162   3186    538    356   -437       C  
ATOM   1306  C   PHE A 172      17.133  42.454  24.250  1.00 36.28           C  
ANISOU 1306  C   PHE A 172     6557   3622   3605    620    275   -468       C  
ATOM   1307  O   PHE A 172      16.916  41.597  23.372  1.00 38.01           O  
ANISOU 1307  O   PHE A 172     6875   3790   3777    697    171   -524       O  
ATOM   1308  CB  PHE A 172      19.367  41.866  25.405  1.00 30.28           C  
ANISOU 1308  CB  PHE A 172     5717   2937   2849    582    471   -417       C  
ATOM   1309  CG  PHE A 172      20.110  41.654  26.704  1.00 31.68           C  
ANISOU 1309  CG  PHE A 172     5784   3150   3101    502    549   -385       C  
ATOM   1310  CD1 PHE A 172      20.264  40.379  27.251  1.00 30.69           C  
ANISOU 1310  CD1 PHE A 172     5629   3005   3025    481    507   -408       C  
ATOM   1311  CD2 PHE A 172      20.642  42.730  27.405  1.00 28.77           C  
ANISOU 1311  CD2 PHE A 172     5344   2828   2757    451    655   -332       C  
ATOM   1312  CE1 PHE A 172      20.929  40.195  28.454  1.00 27.89           C  
ANISOU 1312  CE1 PHE A 172     5182   2682   2733    416    573   -380       C  
ATOM   1313  CE2 PHE A 172      21.339  42.534  28.589  1.00 28.58           C  
ANISOU 1313  CE2 PHE A 172     5231   2831   2797    389    710   -309       C  
ATOM   1314  CZ  PHE A 172      21.461  41.267  29.123  1.00 28.45           C  
ANISOU 1314  CZ  PHE A 172     5190   2798   2820    372    670   -333       C  
ATOM   1315  N   LYS A 173      16.680  43.715  24.184  1.00 39.88           N  
ANISOU 1315  N   LYS A 173     6998   4098   4056    603    309   -437       N  
ATOM   1316  CA  LYS A 173      16.012  44.250  23.001  1.00 43.74           C  
ANISOU 1316  CA  LYS A 173     7589   4559   4468    680    242   -460       C  
ATOM   1317  C   LYS A 173      17.094  44.645  21.984  1.00 42.68           C  
ANISOU 1317  C   LYS A 173     7572   4456   4188    790    344   -441       C  
ATOM   1318  O   LYS A 173      18.247  44.903  22.338  1.00 38.77           O  
ANISOU 1318  O   LYS A 173     7041   4009   3677    781    483   -393       O  
ATOM   1319  CB  LYS A 173      15.094  45.426  23.361  1.00 46.79           C  
ANISOU 1319  CB  LYS A 173     7909   4953   4912    619    243   -429       C  
ATOM   1320  CG  LYS A 173      13.984  45.144  24.371  1.00 50.65           C  
ANISOU 1320  CG  LYS A 173     8281   5410   5552    521    164   -429       C  
ATOM   1321  CD  LYS A 173      12.920  44.170  23.915  1.00 49.82           C  
ANISOU 1321  CD  LYS A 173     8201   5222   5506    542    -13   -484       C  
ATOM   1322  N   THR A 174      16.719  44.653  20.705  1.00 50.08           N  
ANISOU 1322  N   THR A 174     8648   5358   5020    903    271   -477       N  
ATOM   1323  CA  THR A 174      17.686  44.882  19.627  1.00 56.70           C  
ANISOU 1323  CA  THR A 174     9618   6217   5706   1035    366   -457       C  
ATOM   1324  C   THR A 174      17.363  46.183  18.871  1.00 65.64           C  
ANISOU 1324  C   THR A 174    10810   7362   6766   1090    406   -425       C  
ATOM   1325  O   THR A 174      18.218  46.682  18.130  1.00 74.16           O  
ANISOU 1325  O   THR A 174    11972   8468   7737   1189    528   -379       O  
ATOM   1326  CB  THR A 174      17.772  43.654  18.707  1.00 56.19           C  
ANISOU 1326  CB  THR A 174     9697   6101   5549   1155    264   -525       C  
ATOM   1327  OG1 THR A 174      16.539  43.502  18.005  1.00 58.20           O  
ANISOU 1327  OG1 THR A 174    10034   6289   5786   1201     83   -592       O  
ATOM   1328  CG2 THR A 174      18.083  42.374  19.457  1.00 51.49           C  
ANISOU 1328  CG2 THR A 174     9039   5490   5032   1098    225   -554       C  
ATOM   1329  N   PHE A 175      16.162  46.750  19.089  1.00 69.98           N  
ANISOU 1329  N   PHE A 175    11313   7893   7383   1029    315   -439       N  
ATOM   1330  CA  PHE A 175      15.667  47.953  18.356  1.00 64.98           C  
ANISOU 1330  CA  PHE A 175    10739   7264   6685   1080    329   -416       C  
ATOM   1331  C   PHE A 175      16.667  49.119  18.462  1.00 63.83           C  
ANISOU 1331  C   PHE A 175    10557   7181   6512   1078    529   -326       C  
ATOM   1332  O   PHE A 175      16.747  49.914  17.528  1.00 59.33           O  
ANISOU 1332  O   PHE A 175    10082   6618   5843   1173    582   -296       O  
ATOM   1333  CB  PHE A 175      14.283  48.390  18.862  1.00 68.22           C  
ANISOU 1333  CB  PHE A 175    11064   7648   7206    987    218   -433       C  
ATOM   1334  CG  PHE A 175      13.585  49.451  18.035  1.00 67.01           C  
ANISOU 1334  CG  PHE A 175    10983   7487   6991   1045    193   -425       C  
ATOM   1335  CD1 PHE A 175      12.815  49.110  16.926  1.00 67.71           C  
ANISOU 1335  CD1 PHE A 175    11208   7516   7003   1151     39   -488       C  
ATOM   1336  CD2 PHE A 175      13.700  50.800  18.363  1.00 63.22           C  
ANISOU 1336  CD2 PHE A 175    10437   7054   6529    998    316   -357       C  
ATOM   1337  CE1 PHE A 175      12.176  50.086  16.170  1.00 65.40           C  
ANISOU 1337  CE1 PHE A 175    10984   7214   6648   1209     14   -480       C  
ATOM   1338  CE2 PHE A 175      13.056  51.775  17.610  1.00 62.05           C  
ANISOU 1338  CE2 PHE A 175    10353   6897   6323   1052    296   -347       C  
ATOM   1339  CZ  PHE A 175      12.297  51.415  16.515  1.00 66.74           C  
ANISOU 1339  CZ  PHE A 175    11083   7437   6838   1158    147   -407       C  
ATOM   1340  N   SER A 176      17.387  49.236  19.594  1.00 54.60           N  
ANISOU 1340  N   SER A 176     9253   6050   5439    973    632   -282       N  
ATOM   1341  CA  SER A 176      18.443  50.258  19.777  1.00 58.26           C  
ANISOU 1341  CA  SER A 176     9666   6561   5907    964    811   -197       C  
ATOM   1342  C   SER A 176      19.815  49.603  19.988  1.00 58.65           C  
ANISOU 1342  C   SER A 176     9698   6629   5956    981    913   -168       C  
ATOM   1343  O   SER A 176      19.908  48.489  20.493  1.00 54.11           O  
ANISOU 1343  O   SER A 176     9097   6044   5417    948    854   -211       O  
ATOM   1344  CB  SER A 176      18.124  51.184  20.920  1.00 55.40           C  
ANISOU 1344  CB  SER A 176     9161   6220   5666    831    839   -167       C  
ATOM   1345  OG  SER A 176      18.652  50.689  22.139  1.00 58.96           O  
ANISOU 1345  OG  SER A 176     9498   6687   6216    734    863   -164       O  
ATOM   1346  N   LYS A 177      20.870  50.345  19.628  1.00 63.47           N  
ANISOU 1346  N   LYS A 177    10312   7264   6540   1031   1071    -89       N  
ATOM   1347  CA  LYS A 177      22.261  49.922  19.740  1.00 62.45           C  
ANISOU 1347  CA  LYS A 177    10157   7149   6420   1056   1191    -41       C  
ATOM   1348  C   LYS A 177      22.792  50.253  21.141  1.00 62.72           C  
ANISOU 1348  C   LYS A 177    10020   7204   6604    915   1239    -11       C  
ATOM   1349  O   LYS A 177      23.829  49.743  21.542  1.00 69.62           O  
ANISOU 1349  O   LYS A 177    10845   8087   7520    903   1304     12       O  
ATOM   1350  CB  LYS A 177      23.101  50.604  18.653  1.00 64.09           C  
ANISOU 1350  CB  LYS A 177    10443   7362   6545   1185   1342     42       C  
ATOM   1351  N   THR A 178      22.071  51.099  21.884  1.00 62.96           N  
ANISOU 1351  N   THR A 178     9968   7241   6712    815   1202    -15       N  
ATOM   1352  CA  THR A 178      22.523  51.587  23.187  1.00 55.65           C  
ANISOU 1352  CA  THR A 178     8897   6330   5916    695   1241     11       C  
ATOM   1353  C   THR A 178      21.365  51.556  24.207  1.00 54.78           C  
ANISOU 1353  C   THR A 178     8726   6218   5869    591   1125    -43       C  
ATOM   1354  O   THR A 178      20.179  51.511  23.815  1.00 43.72           O  
ANISOU 1354  O   THR A 178     7379   4803   4428    605   1032    -83       O  
ATOM   1355  CB  THR A 178      23.119  52.990  23.020  1.00 65.00           C  
ANISOU 1355  CB  THR A 178    10038   7518   7138    698   1360     92       C  
ATOM   1356  OG1 THR A 178      23.668  53.390  24.276  1.00 67.57           O  
ANISOU 1356  OG1 THR A 178    10231   7848   7592    592   1383    111       O  
ATOM   1357  CG2 THR A 178      22.101  53.996  22.522  1.00 61.11           C  
ANISOU 1357  CG2 THR A 178     9588   7022   6608    712   1333     94       C  
ATOM   1358  N   ALA A 179      21.744  51.587  25.504  1.00 43.39           N  
ANISOU 1358  N   ALA A 179     7172   4786   4528    495   1134    -38       N  
ATOM   1359  CA  ALA A 179      20.864  51.567  26.730  1.00 43.79           C  
ANISOU 1359  CA  ALA A 179     7150   4836   4650    398   1053    -74       C  
ATOM   1360  C   ALA A 179      20.054  50.266  26.920  1.00 37.07           C  
ANISOU 1360  C   ALA A 179     6321   3971   3793    391    945   -133       C  
ATOM   1361  O   ALA A 179      19.201  50.189  27.834  1.00 31.63           O  
ANISOU 1361  O   ALA A 179     5578   3277   3163    325    884   -153       O  
ATOM   1362  CB  ALA A 179      19.938  52.751  26.730  1.00 37.18           C  
ANISOU 1362  CB  ALA A 179     6305   3996   3822    374   1039    -63       C  
ATOM   1363  N   GLU A 180      20.290  49.241  26.099  1.00 40.02           N  
ANISOU 1363  N   GLU A 180     6769   4332   4101    461    921   -158       N  
ATOM   1364  CA  GLU A 180      19.517  47.983  26.203  1.00 41.56           C  
ANISOU 1364  CA  GLU A 180     6984   4502   4304    457    807   -215       C  
ATOM   1365  C   GLU A 180      19.871  47.235  27.500  1.00 35.34           C  
ANISOU 1365  C   GLU A 180     6107   3721   3597    384    804   -221       C  
ATOM   1366  O   GLU A 180      19.033  46.519  28.027  1.00 36.18           O  
ANISOU 1366  O   GLU A 180     6187   3807   3753    348    721   -251       O  
ATOM   1367  CB  GLU A 180      19.736  47.085  24.979  1.00 46.08           C  
ANISOU 1367  CB  GLU A 180     7673   5053   4782    561    774   -245       C  
ATOM   1368  CG  GLU A 180      19.269  47.705  23.666  1.00 54.30           C  
ANISOU 1368  CG  GLU A 180     8822   6079   5728    650    759   -247       C  
ATOM   1369  CD  GLU A 180      17.767  47.836  23.423  1.00 58.95           C  
ANISOU 1369  CD  GLU A 180     9433   6634   6329    641    631   -286       C  
ATOM   1370  OE1 GLU A 180      16.981  47.797  24.406  1.00 66.49           O  
ANISOU 1370  OE1 GLU A 180    10295   7581   7386    549    577   -294       O  
ATOM   1371  OE2 GLU A 180      17.371  47.982  22.237  1.00 57.84           O  
ANISOU 1371  OE2 GLU A 180     9406   6470   6098    734    586   -305       O  
ATOM   1372  N   ASP A 181      21.087  47.424  28.018  1.00 34.21           N  
ANISOU 1372  N   ASP A 181     5917   3604   3477    366    894   -188       N  
ATOM   1373  CA  ASP A 181      21.503  46.766  29.239  1.00 38.75           C  
ANISOU 1373  CA  ASP A 181     6416   4186   4119    307    893   -194       C  
ATOM   1374  C   ASP A 181      20.702  47.357  30.398  1.00 37.95           C  
ANISOU 1374  C   ASP A 181     6245   4089   4086    232    866   -189       C  
ATOM   1375  O   ASP A 181      20.112  46.610  31.186  1.00 31.66           O  
ANISOU 1375  O   ASP A 181     5413   3280   3333    197    813   -208       O  
ATOM   1376  CB  ASP A 181      23.020  46.816  29.453  1.00 42.04           C  
ANISOU 1376  CB  ASP A 181     6800   4621   4549    312    983   -161       C  
ATOM   1377  CG  ASP A 181      23.602  48.193  29.232  1.00 52.97           C  
ANISOU 1377  CG  ASP A 181     8165   6015   5945    314   1066   -111       C  
ATOM   1378  OD1 ASP A 181      22.985  48.961  28.438  1.00 51.98           O  
ANISOU 1378  OD1 ASP A 181     8086   5885   5777    345   1068   -101       O  
ATOM   1379  OD2 ASP A 181      24.633  48.504  29.885  1.00 62.08           O  
ANISOU 1379  OD2 ASP A 181     9252   7175   7160    284   1121    -81       O  
ATOM   1380  N   GLN A 182      20.679  48.701  30.468  1.00 33.32           N  
ANISOU 1380  N   GLN A 182     5640   3513   3507    216    909   -160       N  
ATOM   1381  CA  GLN A 182      19.927  49.435  31.419  1.00 30.71           C  
ANISOU 1381  CA  GLN A 182     5259   3182   3224    162    893   -153       C  
ATOM   1382  C   GLN A 182      18.483  48.941  31.469  1.00 27.66           C  
ANISOU 1382  C   GLN A 182     4880   2776   2854    154    812   -174       C  
ATOM   1383  O   GLN A 182      17.905  48.758  32.572  1.00 28.75           O  
ANISOU 1383  O   GLN A 182     4966   2909   3045    113    791   -171       O  
ATOM   1384  CB  GLN A 182      19.825  50.904  31.018  1.00 35.38           C  
ANISOU 1384  CB  GLN A 182     5858   3778   3804    165    933   -125       C  
ATOM   1385  CG  GLN A 182      20.736  51.829  31.788  1.00 39.58           C  
ANISOU 1385  CG  GLN A 182     6337   4319   4382    132    990    -98       C  
ATOM   1386  CD  GLN A 182      20.400  53.252  31.414  1.00 38.95           C  
ANISOU 1386  CD  GLN A 182     6262   4235   4300    132   1017    -73       C  
ATOM   1387  OE1 GLN A 182      19.734  53.950  32.173  1.00 40.54           O  
ANISOU 1387  OE1 GLN A 182     6497   4436   4470    173   1064    -47       O  
ATOM   1388  NE2 GLN A 182      20.873  53.688  30.257  1.00 33.98           N  
ANISOU 1388  NE2 GLN A 182     5604   3603   3701     93    993    -75       N  
ATOM   1389  N   LEU A 183      17.870  48.821  30.287  1.00 24.87           N  
ANISOU 1389  N   LEU A 183     4589   2404   2457    198    768   -189       N  
ATOM   1390  CA  LEU A 183      16.490  48.367  30.208  1.00 25.82           C  
ANISOU 1390  CA  LEU A 183     4708   2491   2611    192    677   -207       C  
ATOM   1391  C   LEU A 183      16.379  46.941  30.789  1.00 25.50           C  
ANISOU 1391  C   LEU A 183     4637   2430   2622    176    628   -227       C  
ATOM   1392  O   LEU A 183      15.427  46.631  31.504  1.00 24.86           O  
ANISOU 1392  O   LEU A 183     4503   2325   2615    142    587   -218       O  
ATOM   1393  CB  LEU A 183      16.030  48.389  28.750  1.00 25.41           C  
ANISOU 1393  CB  LEU A 183     4742   2415   2497    255    623   -230       C  
ATOM   1394  CG  LEU A 183      14.623  47.849  28.493  1.00 26.53           C  
ANISOU 1394  CG  LEU A 183     4885   2507   2686    255    505   -254       C  
ATOM   1395  CD1 LEU A 183      13.602  48.513  29.393  1.00 26.25           C  
ANISOU 1395  CD1 LEU A 183     4772   2466   2733    198    503   -223       C  
ATOM   1396  CD2 LEU A 183      14.214  48.023  27.038  1.00 27.60           C  
ANISOU 1396  CD2 LEU A 183     5119   2617   2750    328    442   -282       C  
ATOM   1397  N   PHE A 184      17.325  46.058  30.433  1.00 24.46           N  
ANISOU 1397  N   PHE A 184     4538   2301   2453    207    636   -247       N  
ATOM   1398  CA  PHE A 184      17.304  44.678  30.972  1.00 25.25           C  
ANISOU 1398  CA  PHE A 184     4610   2381   2603    193    593   -265       C  
ATOM   1399  C   PHE A 184      17.286  44.758  32.503  1.00 23.77           C  
ANISOU 1399  C   PHE A 184     4337   2209   2483    136    633   -234       C  
ATOM   1400  O   PHE A 184      16.421  44.138  33.143  1.00 25.20           O  
ANISOU 1400  O   PHE A 184     4472   2362   2738    112    591   -226       O  
ATOM   1401  CB  PHE A 184      18.450  43.843  30.396  1.00 26.48           C  
ANISOU 1401  CB  PHE A 184     4815   2542   2701    238    610   -287       C  
ATOM   1402  CG  PHE A 184      18.468  42.403  30.845  1.00 25.69           C  
ANISOU 1402  CG  PHE A 184     4693   2417   2648    229    563   -308       C  
ATOM   1403  CD1 PHE A 184      18.989  42.049  32.082  1.00 24.53           C  
ANISOU 1403  CD1 PHE A 184     4479   2291   2549    186    608   -288       C  
ATOM   1404  CD2 PHE A 184      17.955  41.404  30.038  1.00 26.93           C  
ANISOU 1404  CD2 PHE A 184     4901   2525   2804    268    466   -348       C  
ATOM   1405  CE1 PHE A 184      19.031  40.715  32.481  1.00 26.68           C  
ANISOU 1405  CE1 PHE A 184     4731   2541   2865    181    571   -303       C  
ATOM   1406  CE2 PHE A 184      17.989  40.073  30.447  1.00 27.81           C  
ANISOU 1406  CE2 PHE A 184     4988   2608   2968    259    421   -365       C  
ATOM   1407  CZ  PHE A 184      18.528  39.730  31.665  1.00 26.36           C  
ANISOU 1407  CZ  PHE A 184     4733   2451   2832    214    480   -339       C  
ATOM   1408  N   THR A 185      18.197  45.546  33.082  1.00 23.37           N  
ANISOU 1408  N   THR A 185     4268   2198   2413    120    712   -214       N  
ATOM   1409  CA  THR A 185      18.333  45.585  34.510  1.00 24.84           C  
ANISOU 1409  CA  THR A 185     4395   2397   2643     83    743   -194       C  
ATOM   1410  C   THR A 185      17.072  46.192  35.141  1.00 26.48           C  
ANISOU 1410  C   THR A 185     4570   2593   2897     61    731   -168       C  
ATOM   1411  O   THR A 185      16.600  45.706  36.156  1.00 25.77           O  
ANISOU 1411  O   THR A 185     4439   2494   2859     47    730   -149       O  
ATOM   1412  CB  THR A 185      19.608  46.319  34.933  1.00 23.96           C  
ANISOU 1412  CB  THR A 185     4275   2318   2509     76    810   -185       C  
ATOM   1413  OG1 THR A 185      20.747  45.728  34.320  1.00 24.93           O  
ANISOU 1413  OG1 THR A 185     4421   2448   2603    101    830   -197       O  
ATOM   1414  CG2 THR A 185      19.798  46.314  36.429  1.00 22.82           C  
ANISOU 1414  CG2 THR A 185     4086   2182   2399     51    827   -172       C  
ATOM   1415  N   ILE A 186      16.508  47.230  34.512  1.00 24.12           N  
ANISOU 1415  N   ILE A 186     4291   2292   2579     66    728   -162       N  
ATOM   1416  CA  ILE A 186      15.286  47.849  34.992  1.00 26.78           C  
ANISOU 1416  CA  ILE A 186     4599   2615   2959     51    719   -134       C  
ATOM   1417  C   ILE A 186      14.122  46.842  34.981  1.00 25.61           C  
ANISOU 1417  C   ILE A 186     4421   2422   2886     49    655   -126       C  
ATOM   1418  O   ILE A 186      13.342  46.742  35.973  1.00 24.57           O  
ANISOU 1418  O   ILE A 186     4237   2275   2820     36    667    -88       O  
ATOM   1419  CB  ILE A 186      14.966  49.133  34.183  1.00 26.90           C  
ANISOU 1419  CB  ILE A 186     4645   2635   2937     58    724   -131       C  
ATOM   1420  CG1 ILE A 186      15.886  50.297  34.569  1.00 29.54           C  
ANISOU 1420  CG1 ILE A 186     4984   3002   3236     50    791   -123       C  
ATOM   1421  CG2 ILE A 186      13.498  49.515  34.297  1.00 27.92           C  
ANISOU 1421  CG2 ILE A 186     4749   2739   3119     51    693   -106       C  
ATOM   1422  CD1 ILE A 186      15.621  50.888  35.927  1.00 29.15           C  
ANISOU 1422  CD1 ILE A 186     4901   2959   3215     32    820    -99       C  
ATOM   1423  N   GLU A 187      13.937  46.148  33.864  1.00 25.17           N  
ANISOU 1423  N   GLU A 187     4397   2337   2827     69    585   -158       N  
ATOM   1424  CA  GLU A 187      12.857  45.139  33.742  1.00 27.87           C  
ANISOU 1424  CA  GLU A 187     4706   2621   3262     66    503   -155       C  
ATOM   1425  C   GLU A 187      13.025  44.048  34.828  1.00 26.39           C  
ANISOU 1425  C   GLU A 187     4463   2424   3137     51    522   -134       C  
ATOM   1426  O   GLU A 187      12.050  43.659  35.509  1.00 26.63           O  
ANISOU 1426  O   GLU A 187     4427   2417   3271     37    511    -92       O  
ATOM   1427  CB  GLU A 187      12.815  44.563  32.321  1.00 29.74           C  
ANISOU 1427  CB  GLU A 187     5006   2824   3470    101    411   -205       C  
ATOM   1428  CG  GLU A 187      12.361  45.576  31.276  1.00 32.76           C  
ANISOU 1428  CG  GLU A 187     5441   3202   3801    126    381   -218       C  
ATOM   1429  CD  GLU A 187      12.122  45.036  29.866  1.00 36.60           C  
ANISOU 1429  CD  GLU A 187     6004   3644   4255    177    273   -270       C  
ATOM   1430  OE1 GLU A 187      12.598  43.934  29.566  1.00 38.78           O  
ANISOU 1430  OE1 GLU A 187     6310   3901   4521    200    232   -304       O  
ATOM   1431  OE2 GLU A 187      11.444  45.724  29.071  1.00 42.63           O  
ANISOU 1431  OE2 GLU A 187     6805   4391   5001    199    226   -277       O  
ATOM   1432  N   PHE A 188      14.273  43.628  35.049  1.00 25.26           N  
ANISOU 1432  N   PHE A 188     4344   2316   2938     56    561   -155       N  
ATOM   1433  CA  PHE A 188      14.615  42.695  36.120  1.00 25.21           C  
ANISOU 1433  CA  PHE A 188     4295   2310   2973     47    589   -137       C  
ATOM   1434  C   PHE A 188      14.223  43.287  37.499  1.00 23.88           C  
ANISOU 1434  C   PHE A 188     4080   2157   2835     37    658    -83       C  
ATOM   1435  O   PHE A 188      13.556  42.616  38.294  1.00 22.54           O  
ANISOU 1435  O   PHE A 188     3857   1958   2747     36    664    -40       O  
ATOM   1436  CB  PHE A 188      16.086  42.254  36.037  1.00 23.37           C  
ANISOU 1436  CB  PHE A 188     4098   2111   2670     58    617   -170       C  
ATOM   1437  CG  PHE A 188      16.355  41.041  36.900  1.00 23.40           C  
ANISOU 1437  CG  PHE A 188     4064   2104   2720     54    624   -159       C  
ATOM   1438  CD1 PHE A 188      16.550  41.177  38.265  1.00 22.86           C  
ANISOU 1438  CD1 PHE A 188     3962   2059   2664     48    686   -123       C  
ATOM   1439  CD2 PHE A 188      16.275  39.768  36.370  1.00 24.58           C  
ANISOU 1439  CD2 PHE A 188     4216   2213   2908     63    562   -182       C  
ATOM   1440  CE1 PHE A 188      16.749  40.077  39.072  1.00 23.42           C  
ANISOU 1440  CE1 PHE A 188     4003   2119   2776     51    697   -107       C  
ATOM   1441  CE2 PHE A 188      16.453  38.660  37.186  1.00 25.10           C  
ANISOU 1441  CE2 PHE A 188     4242   2265   3026     59    570   -166       C  
ATOM   1442  CZ  PHE A 188      16.682  38.816  38.533  1.00 23.71           C  
ANISOU 1442  CZ  PHE A 188     4032   2118   2857     53    642   -125       C  
ATOM   1443  N   LEU A 189      14.623  44.526  37.801  1.00 22.62           N  
ANISOU 1443  N   LEU A 189     3944   2038   2613     36    710    -80       N  
ATOM   1444  CA  LEU A 189      14.344  45.140  39.127  1.00 24.08           C  
ANISOU 1444  CA  LEU A 189     4105   2236   2805     42    771    -36       C  
ATOM   1445  C   LEU A 189      12.835  45.280  39.382  1.00 24.35           C  
ANISOU 1445  C   LEU A 189     4096   2234   2922     45    769     17       C  
ATOM   1446  O   LEU A 189      12.340  45.061  40.522  1.00 23.95           O  
ANISOU 1446  O   LEU A 189     4011   2173   2915     63    816     71       O  
ATOM   1447  CB  LEU A 189      14.994  46.514  39.224  1.00 24.59           C  
ANISOU 1447  CB  LEU A 189     4208   2339   2796     42    807    -51       C  
ATOM   1448  CG  LEU A 189      16.507  46.532  39.376  1.00 24.66           C  
ANISOU 1448  CG  LEU A 189     4242   2379   2747     41    825    -86       C  
ATOM   1449  CD1 LEU A 189      17.027  47.914  39.057  1.00 25.59           C  
ANISOU 1449  CD1 LEU A 189     4386   2517   2819     35    842   -100       C  
ATOM   1450  CD2 LEU A 189      16.894  46.123  40.793  1.00 24.97           C  
ANISOU 1450  CD2 LEU A 189     4272   2427   2789     57    855    -71       C  
ATOM   1451  N   MET A 190      12.106  45.621  38.321  1.00 23.07           N  
ANISOU 1451  N   MET A 190     3934   2047   2783     35    717      8       N  
ATOM   1452  CA  MET A 190      10.691  45.861  38.412  1.00 24.47           C  
ANISOU 1452  CA  MET A 190     4063   2183   3048     36    708     59       C  
ATOM   1453  C   MET A 190       9.907  44.549  38.522  1.00 25.81           C  
ANISOU 1453  C   MET A 190     4167   2293   3345     33    667     93       C  
ATOM   1454  O   MET A 190       8.703  44.602  38.764  1.00 26.33           O  
ANISOU 1454  O   MET A 190     4173   2314   3514     35    667    153       O  
ATOM   1455  CB  MET A 190      10.197  46.654  37.193  1.00 24.64           C  
ANISOU 1455  CB  MET A 190     4110   2195   3055     28    653     34       C  
ATOM   1456  CG  MET A 190      10.659  48.110  37.182  1.00 24.25           C  
ANISOU 1456  CG  MET A 190     4108   2193   2911     31    702     22       C  
ATOM   1457  SD  MET A 190      10.247  49.032  38.705  1.00 25.18           S  
ANISOU 1457  SD  MET A 190     4206   2329   3032     47    794     82       S  
ATOM   1458  CE  MET A 190      11.834  49.042  39.538  1.00 25.01           C  
ANISOU 1458  CE  MET A 190     4227   2356   2919     55    842     49       C  
ATOM   1459  N   ASN A 191      10.553  43.393  38.293  1.00 25.15           N  
ANISOU 1459  N   ASN A 191     4089   2199   3266     29    630     60       N  
ATOM   1460  CA  ASN A 191       9.853  42.122  38.340  1.00 26.81           C  
ANISOU 1460  CA  ASN A 191     4234   2343   3610     25    582     90       C  
ATOM   1461  C   ASN A 191      10.480  41.204  39.398  1.00 26.39           C  
ANISOU 1461  C   ASN A 191     4161   2301   3563     35    639    113       C  
ATOM   1462  O   ASN A 191      10.260  40.033  39.353  1.00 26.87           O  
ANISOU 1462  O   ASN A 191     4180   2313   3716     31    598    123       O  
ATOM   1463  CB  ASN A 191       9.777  41.502  36.939  1.00 28.29           C  
ANISOU 1463  CB  ASN A 191     4444   2485   3817     17    458     27       C  
ATOM   1464  CG  ASN A 191       8.760  42.208  36.074  1.00 28.97           C  
ANISOU 1464  CG  ASN A 191     4528   2536   3943     13    391     25       C  
ATOM   1465  OD1 ASN A 191       7.575  41.921  36.180  1.00 33.42           O  
ANISOU 1465  OD1 ASN A 191     5015   3031   4651      5    351     75       O  
ATOM   1466  ND2 ASN A 191       9.194  43.180  35.279  1.00 28.77           N  
ANISOU 1466  ND2 ASN A 191     4578   2552   3800     22    385    -21       N  
ATOM   1467  N   SER A 192      11.279  41.758  40.312  1.00 26.02           N  
ANISOU 1467  N   SER A 192     4150   2316   3421     52    726    118       N  
ATOM   1468  CA  SER A 192      11.901  40.995  41.402  1.00 26.85           C  
ANISOU 1468  CA  SER A 192     4246   2435   3517     72    782    141       C  
ATOM   1469  C   SER A 192      11.942  41.836  42.678  1.00 25.66           C  
ANISOU 1469  C   SER A 192     4115   2322   3312    108    878    185       C  
ATOM   1470  O   SER A 192      11.722  43.023  42.638  1.00 24.92           O  
ANISOU 1470  O   SER A 192     4047   2249   3172    112    895    184       O  
ATOM   1471  CB  SER A 192      13.263  40.536  41.020  1.00 26.84           C  
ANISOU 1471  CB  SER A 192     4295   2469   3433     64    758     71       C  
ATOM   1472  OG  SER A 192      14.100  41.629  40.728  1.00 25.69           O  
ANISOU 1472  OG  SER A 192     4210   2376   3175     61    771     24       O  
ATOM   1473  N   LYS A 193      12.224  41.197  43.812  1.00 28.84           N  
ANISOU 1473  N   LYS A 193     4510   2729   3717    143    935    223       N  
ATOM   1474  CA  LYS A 193      11.997  41.812  45.152  1.00 29.12           C  
ANISOU 1474  CA  LYS A 193     4566   2783   3714    200   1027    281       C  
ATOM   1475  C   LYS A 193      13.307  42.045  45.910  1.00 27.07           C  
ANISOU 1475  C   LYS A 193     4378   2575   3331    227   1049    237       C  
ATOM   1476  O   LYS A 193      13.451  43.014  46.645  1.00 27.51           O  
ANISOU 1476  O   LYS A 193     4485   2656   3309    267   1087    240       O  
ATOM   1477  CB  LYS A 193      11.108  40.873  45.985  1.00 35.80           C  
ANISOU 1477  CB  LYS A 193     5348   3582   4672    239   1086    380       C  
ATOM   1478  CG  LYS A 193       9.632  41.228  45.920  1.00 46.18           C  
ANISOU 1478  CG  LYS A 193     6599   4849   6099    247   1113    461       C  
ATOM   1479  CD  LYS A 193       8.634  40.095  46.163  1.00 54.77           C  
ANISOU 1479  CD  LYS A 193     7585   5863   7361    257   1136    557       C  
ATOM   1480  CE  LYS A 193       7.193  40.533  45.922  1.00 55.96           C  
ANISOU 1480  CE  LYS A 193     7661   5958   7640    256   1148    634       C  
ATOM   1481  NZ  LYS A 193       6.394  39.464  45.270  1.00 59.66           N  
ANISOU 1481  NZ  LYS A 193     8022   6341   8304    216   1081    670       N  
ATOM   1482  N   ASN A 194      14.230  41.098  45.803  1.00 25.79           N  
ANISOU 1482  N   ASN A 194     4218   2421   3158    213   1021    199       N  
ATOM   1483  CA  ASN A 194      15.352  40.968  46.742  1.00 26.37           C  
ANISOU 1483  CA  ASN A 194     4343   2529   3146    248   1043    177       C  
ATOM   1484  C   ASN A 194      16.671  41.240  46.005  1.00 24.66           C  
ANISOU 1484  C   ASN A 194     4160   2345   2864    207    985     89       C  
ATOM   1485  O   ASN A 194      17.122  40.452  45.153  1.00 25.28           O  
ANISOU 1485  O   ASN A 194     4218   2418   2968    169    943     55       O  
ATOM   1486  CB  ASN A 194      15.404  39.577  47.374  1.00 25.79           C  
ANISOU 1486  CB  ASN A 194     4240   2436   3122    274   1070    217       C  
ATOM   1487  CG  ASN A 194      14.299  39.280  48.368  1.00 29.46           C  
ANISOU 1487  CG  ASN A 194     4675   2868   3648    335   1151    320       C  
ATOM   1488  OD1 ASN A 194      13.593  40.173  48.828  1.00 29.19           O  
ANISOU 1488  OD1 ASN A 194     4658   2833   3598    374   1198    362       O  
ATOM   1489  ND2 ASN A 194      14.174  38.010  48.746  1.00 32.79           N  
ANISOU 1489  ND2 ASN A 194     5055   3262   4142    352   1175    367       N  
ATOM   1490  N   TYR A 195      17.328  42.332  46.378  1.00 25.80           N  
ANISOU 1490  N   TYR A 195     4356   2518   2927    220    985     56       N  
ATOM   1491  CA  TYR A 195      18.600  42.702  45.786  1.00 25.58           C  
ANISOU 1491  CA  TYR A 195     4349   2514   2853    187    941    -12       C  
ATOM   1492  C   TYR A 195      19.627  42.809  46.923  1.00 25.08           C  
ANISOU 1492  C   TYR A 195     4329   2466   2732    226    941    -32       C  
ATOM   1493  O   TYR A 195      19.311  43.227  47.990  1.00 25.82           O  
ANISOU 1493  O   TYR A 195     4460   2558   2791    281    967     -8       O  
ATOM   1494  CB  TYR A 195      18.470  44.008  44.996  1.00 25.85           C  
ANISOU 1494  CB  TYR A 195     4397   2555   2870    158    924    -35       C  
ATOM   1495  CG  TYR A 195      17.096  44.361  44.477  1.00 23.71           C  
ANISOU 1495  CG  TYR A 195     4103   2265   2641    149    934      0       C  
ATOM   1496  CD1 TYR A 195      16.432  43.567  43.557  1.00 22.38           C  
ANISOU 1496  CD1 TYR A 195     3893   2072   2538    123    912     11       C  
ATOM   1497  CD2 TYR A 195      16.461  45.513  44.902  1.00 23.15           C  
ANISOU 1497  CD2 TYR A 195     4053   2194   2549    171    958     21       C  
ATOM   1498  CE1 TYR A 195      15.178  43.909  43.084  1.00 22.95           C  
ANISOU 1498  CE1 TYR A 195     3939   2119   2660    115    908     44       C  
ATOM   1499  CE2 TYR A 195      15.210  45.877  44.431  1.00 22.23           C  
ANISOU 1499  CE2 TYR A 195     3911   2058   2477    163    967     58       C  
ATOM   1500  CZ  TYR A 195      14.567  45.084  43.501  1.00 24.09           C  
ANISOU 1500  CZ  TYR A 195     4099   2268   2785    133    939     69       C  
ATOM   1501  OH  TYR A 195      13.307  45.437  43.071  1.00 24.74           O  
ANISOU 1501  OH  TYR A 195     4150   2322   2925    127    938    107       O  
ATOM   1502  N   SER A 196      20.849  42.371  46.666  1.00 23.98           N  
ANISOU 1502  N   SER A 196     4187   2338   2584    205    910    -75       N  
ATOM   1503  CA  SER A 196      21.941  42.362  47.629  1.00 24.07           C  
ANISOU 1503  CA  SER A 196     4231   2358   2555    237    891   -100       C  
ATOM   1504  C   SER A 196      23.178  42.994  46.985  1.00 21.80           C  
ANISOU 1504  C   SER A 196     3939   2077   2267    197    847   -152       C  
ATOM   1505  O   SER A 196      23.414  42.849  45.778  1.00 20.78           O  
ANISOU 1505  O   SER A 196     3777   1952   2167    152    844   -164       O  
ATOM   1506  CB  SER A 196      22.249  40.927  48.045  1.00 26.53           C  
ANISOU 1506  CB  SER A 196     4528   2668   2882    255    901    -87       C  
ATOM   1507  OG  SER A 196      21.072  40.328  48.573  1.00 36.97           O  
ANISOU 1507  OG  SER A 196     5843   3977   4227    291    951    -25       O  
ATOM   1508  N   ILE A 197      24.015  43.580  47.832  1.00 22.26           N  
ANISOU 1508  N   ILE A 197     4028   2130   2297    224    812   -180       N  
ATOM   1509  CA  ILE A 197      25.204  44.288  47.440  1.00 23.10           C  
ANISOU 1509  CA  ILE A 197     4121   2230   2425    193    768   -220       C  
ATOM   1510  C   ILE A 197      26.352  43.738  48.287  1.00 24.09           C  
ANISOU 1510  C   ILE A 197     4254   2348   2550    218    727   -244       C  
ATOM   1511  O   ILE A 197      26.273  43.707  49.512  1.00 24.77           O  
ANISOU 1511  O   ILE A 197     4391   2427   2593    277    708   -247       O  
ATOM   1512  CB  ILE A 197      25.031  45.810  47.636  1.00 22.31           C  
ANISOU 1512  CB  ILE A 197     4048   2114   2312    198    743   -233       C  
ATOM   1513  CG1 ILE A 197      23.867  46.363  46.800  1.00 22.22           C  
ANISOU 1513  CG1 ILE A 197     4029   2110   2302    175    783   -207       C  
ATOM   1514  CG2 ILE A 197      26.346  46.547  47.414  1.00 22.60           C  
ANISOU 1514  CG2 ILE A 197     4062   2130   2394    170    689   -269       C  
ATOM   1515  CD1 ILE A 197      23.367  47.720  47.246  1.00 23.37           C  
ANISOU 1515  CD1 ILE A 197     4214   2241   2422    196    770   -211       C  
ATOM   1516  N   LYS A 198      27.411  43.304  47.610  1.00 23.78           N  
ANISOU 1516  N   LYS A 198     4168   2309   2556    181    716   -258       N  
ATOM   1517  CA  LYS A 198      28.525  42.650  48.251  1.00 27.95           C  
ANISOU 1517  CA  LYS A 198     4690   2829   3097    198    678   -277       C  
ATOM   1518  C   LYS A 198      29.830  43.349  47.860  1.00 28.03           C  
ANISOU 1518  C   LYS A 198     4659   2816   3174    166    633   -301       C  
ATOM   1519  O   LYS A 198      30.053  43.583  46.643  1.00 26.72           O  
ANISOU 1519  O   LYS A 198     4447   2652   3050    122    666   -288       O  
ATOM   1520  CB  LYS A 198      28.461  41.176  47.852  1.00 29.44           C  
ANISOU 1520  CB  LYS A 198     4855   3037   3291    191    720   -258       C  
ATOM   1521  CG  LYS A 198      29.532  40.311  48.462  1.00 33.90           C  
ANISOU 1521  CG  LYS A 198     5412   3598   3868    210    691   -272       C  
ATOM   1522  CD  LYS A 198      29.215  39.851  49.828  1.00 34.61           C  
ANISOU 1522  CD  LYS A 198     5555   3688   3908    274    679   -267       C  
ATOM   1523  CE  LYS A 198      30.074  38.662  50.194  1.00 32.04           C  
ANISOU 1523  CE  LYS A 198     5215   3365   3594    289    668   -272       C  
ATOM   1524  NZ  LYS A 198      30.547  38.796  51.589  1.00 35.39           N  
ANISOU 1524  NZ  LYS A 198     5693   3773   3980    354    609   -292       N  
ATOM   1525  N   THR A 199      30.667  43.663  48.870  1.00 24.33           N  
ANISOU 1525  N   THR A 199     4206   2318   2719    194    558   -331       N  
ATOM   1526  CA  THR A 199      31.708  44.702  48.772  1.00 25.32           C  
ANISOU 1526  CA  THR A 199     4294   2401   2924    170    494   -353       C  
ATOM   1527  C   THR A 199      33.071  44.302  49.375  1.00 25.64           C  
ANISOU 1527  C   THR A 199     4307   2410   3023    180    421   -376       C  
ATOM   1528  O   THR A 199      34.006  45.101  49.340  1.00 24.84           O  
ANISOU 1528  O   THR A 199     4162   2262   3013    160    358   -390       O  
ATOM   1529  CB  THR A 199      31.239  46.018  49.433  1.00 27.21           C  
ANISOU 1529  CB  THR A 199     4586   2612   3139    195    439   -376       C  
ATOM   1530  OG1 THR A 199      31.294  45.913  50.860  1.00 26.71           O  
ANISOU 1530  OG1 THR A 199     4597   2531   3021    265    367   -409       O  
ATOM   1531  CG2 THR A 199      29.848  46.412  48.991  1.00 26.93           C  
ANISOU 1531  CG2 THR A 199     4580   2604   3044    193    506   -352       C  
ATOM   1532  N   ASP A 200      33.228  43.077  49.887  1.00 24.74           N  
ANISOU 1532  N   ASP A 200     4209   2316   2873    210    427   -376       N  
ATOM   1533  CA  ASP A 200      34.437  42.678  50.663  1.00 26.36           C  
ANISOU 1533  CA  ASP A 200     4401   2490   3123    232    346   -402       C  
ATOM   1534  C   ASP A 200      35.740  42.786  49.837  1.00 26.53           C  
ANISOU 1534  C   ASP A 200     4321   2482   3277    178    337   -389       C  
ATOM   1535  O   ASP A 200      36.840  42.989  50.390  1.00 27.20           O  
ANISOU 1535  O   ASP A 200     4376   2518   3441    185    245   -412       O  
ATOM   1536  CB  ASP A 200      34.254  41.252  51.153  1.00 26.52           C  
ANISOU 1536  CB  ASP A 200     4451   2544   3079    269    379   -392       C  
ATOM   1537  CG  ASP A 200      33.079  41.149  52.113  1.00 29.53           C  
ANISOU 1537  CG  ASP A 200     4928   2943   3347    336    392   -392       C  
ATOM   1538  OD1 ASP A 200      31.920  41.176  51.651  1.00 30.20           O  
ANISOU 1538  OD1 ASP A 200     5027   3057   3390    326    468   -363       O  
ATOM   1539  OD2 ASP A 200      33.336  41.181  53.307  1.00 36.94           O  
ANISOU 1539  OD2 ASP A 200     5930   3861   4245    401    321   -420       O  
ATOM   1540  N   TYR A 201      35.613  42.574  48.530  1.00 24.70           N  
ANISOU 1540  N   TYR A 201     4038   2276   3067    135    433   -349       N  
ATOM   1541  CA  TYR A 201      36.693  42.719  47.563  1.00 25.80           C  
ANISOU 1541  CA  TYR A 201     4085   2392   3324     94    458   -319       C  
ATOM   1542  C   TYR A 201      36.136  43.458  46.357  1.00 26.14           C  
ANISOU 1542  C   TYR A 201     4111   2447   3371     63    535   -287       C  
ATOM   1543  O   TYR A 201      34.908  43.584  46.212  1.00 25.14           O  
ANISOU 1543  O   TYR A 201     4043   2354   3153     69    570   -290       O  
ATOM   1544  CB  TYR A 201      37.201  41.344  47.103  1.00 26.46           C  
ANISOU 1544  CB  TYR A 201     4139   2504   3411     95    517   -296       C  
ATOM   1545  CG  TYR A 201      37.638  40.451  48.232  1.00 27.97           C  
ANISOU 1545  CG  TYR A 201     4351   2690   3583    130    455   -323       C  
ATOM   1546  CD1 TYR A 201      38.936  40.482  48.708  1.00 30.02           C  
ANISOU 1546  CD1 TYR A 201     4557   2903   3945    131    380   -331       C  
ATOM   1547  CD2 TYR A 201      36.730  39.612  48.865  1.00 29.77           C  
ANISOU 1547  CD2 TYR A 201     4655   2958   3699    166    468   -337       C  
ATOM   1548  CE1 TYR A 201      39.333  39.692  49.776  1.00 32.01           C  
ANISOU 1548  CE1 TYR A 201     4837   3151   4174    169    315   -359       C  
ATOM   1549  CE2 TYR A 201      37.102  38.830  49.947  1.00 31.40           C  
ANISOU 1549  CE2 TYR A 201     4889   3160   3881    208    415   -358       C  
ATOM   1550  CZ  TYR A 201      38.410  38.866  50.397  1.00 34.72           C  
ANISOU 1550  CZ  TYR A 201     5263   3537   4389    210    336   -372       C  
ATOM   1551  OH  TYR A 201      38.784  38.054  51.426  1.00 37.47           O  
ANISOU 1551  OH  TYR A 201     5645   3883   4709    256    283   -394       O  
ATOM   1552  N   GLU A 202      37.039  43.885  45.468  1.00 28.38           N  
ANISOU 1552  N   GLU A 202     4315   2703   3765     35    567   -249       N  
ATOM   1553  CA  GLU A 202      36.649  44.355  44.151  1.00 29.89           C  
ANISOU 1553  CA  GLU A 202     4492   2909   3954     18    660   -207       C  
ATOM   1554  C   GLU A 202      36.463  43.118  43.262  1.00 28.66           C  
ANISOU 1554  C   GLU A 202     4352   2801   3736     32    751   -184       C  
ATOM   1555  O   GLU A 202      37.403  42.591  42.742  1.00 31.32           O  
ANISOU 1555  O   GLU A 202     4639   3129   4131     36    793   -152       O  
ATOM   1556  CB  GLU A 202      37.694  45.336  43.598  1.00 31.29           C  
ANISOU 1556  CB  GLU A 202     4578   3030   4279     -4    667   -165       C  
ATOM   1557  CG  GLU A 202      37.704  46.652  44.356  1.00 34.56           C  
ANISOU 1557  CG  GLU A 202     4985   3391   4755    -19    570   -192       C  
ATOM   1558  CD  GLU A 202      38.674  47.731  43.888  1.00 37.94           C  
ANISOU 1558  CD  GLU A 202     5312   3748   5353    -46    565   -147       C  
ATOM   1559  OE1 GLU A 202      39.473  47.453  42.967  1.00 40.60           O  
ANISOU 1559  OE1 GLU A 202     5576   4076   5772    -49    649    -83       O  
ATOM   1560  OE2 GLU A 202      38.631  48.851  44.461  1.00 39.89           O  
ANISOU 1560  OE2 GLU A 202     5556   3945   5656    -58    478   -172       O  
ATOM   1561  N   TYR A 203      35.217  42.685  43.106  1.00 27.43           N  
ANISOU 1561  N   TYR A 203     4266   2688   3466     42    777   -200       N  
ATOM   1562  CA  TYR A 203      34.919  41.359  42.610  1.00 27.46           C  
ANISOU 1562  CA  TYR A 203     4298   2727   3405     60    827   -197       C  
ATOM   1563  C   TYR A 203      34.994  41.319  41.074  1.00 27.89           C  
ANISOU 1563  C   TYR A 203     4348   2791   3456     68    914   -159       C  
ATOM   1564  O   TYR A 203      35.261  40.275  40.494  1.00 26.67           O  
ANISOU 1564  O   TYR A 203     4202   2651   3279     90    957   -149       O  
ATOM   1565  CB  TYR A 203      33.545  40.954  43.132  1.00 26.20           C  
ANISOU 1565  CB  TYR A 203     4206   2597   3152     68    808   -224       C  
ATOM   1566  CG  TYR A 203      33.513  40.497  44.575  1.00 24.44           C  
ANISOU 1566  CG  TYR A 203     4003   2371   2910     85    746   -252       C  
ATOM   1567  CD1 TYR A 203      34.100  39.297  44.958  1.00 23.81           C  
ANISOU 1567  CD1 TYR A 203     3914   2296   2834    101    741   -256       C  
ATOM   1568  CD2 TYR A 203      32.820  41.204  45.546  1.00 25.31           C  
ANISOU 1568  CD2 TYR A 203     4152   2475   2987     95    699   -272       C  
ATOM   1569  CE1 TYR A 203      34.050  38.826  46.263  1.00 23.95           C  
ANISOU 1569  CE1 TYR A 203     3960   2314   2826    127    691   -277       C  
ATOM   1570  CE2 TYR A 203      32.757  40.748  46.855  1.00 24.39           C  
ANISOU 1570  CE2 TYR A 203     4069   2357   2838    129    652   -292       C  
ATOM   1571  CZ  TYR A 203      33.361  39.550  47.220  1.00 25.82           C  
ANISOU 1571  CZ  TYR A 203     4241   2544   3023    146    648   -294       C  
ATOM   1572  OH  TYR A 203      33.294  39.078  48.514  1.00 27.21           O  
ANISOU 1572  OH  TYR A 203     4459   2719   3160    189    605   -310       O  
ATOM   1573  N   TYR A 204      34.663  42.449  40.451  1.00 25.82           N  
ANISOU 1573  N   TYR A 204     4085   2520   3202     59    939   -140       N  
ATOM   1574  CA  TYR A 204      34.593  42.583  39.025  1.00 26.70           C  
ANISOU 1574  CA  TYR A 204     4210   2640   3292     80   1020   -104       C  
ATOM   1575  C   TYR A 204      35.499  43.746  38.619  1.00 25.65           C  
ANISOU 1575  C   TYR A 204     4012   2471   3263     72   1054    -55       C  
ATOM   1576  O   TYR A 204      35.250  44.893  39.015  1.00 27.76           O  
ANISOU 1576  O   TYR A 204     4262   2717   3566     46   1018    -60       O  
ATOM   1577  CB  TYR A 204      33.139  42.794  38.598  1.00 23.77           C  
ANISOU 1577  CB  TYR A 204     3909   2294   2829     82   1019   -124       C  
ATOM   1578  CG  TYR A 204      32.945  42.798  37.110  1.00 26.48           C  
ANISOU 1578  CG  TYR A 204     4289   2645   3127    118   1091    -96       C  
ATOM   1579  CD1 TYR A 204      33.482  43.805  36.319  1.00 25.85           C  
ANISOU 1579  CD1 TYR A 204     4182   2548   3092    129   1151    -47       C  
ATOM   1580  CD2 TYR A 204      32.280  41.758  36.474  1.00 27.25           C  
ANISOU 1580  CD2 TYR A 204     4451   2762   3141    149   1097   -116       C  
ATOM   1581  CE1 TYR A 204      33.373  43.766  34.940  1.00 26.87           C  
ANISOU 1581  CE1 TYR A 204     4358   2683   3167    180   1224    -17       C  
ATOM   1582  CE2 TYR A 204      32.131  41.730  35.091  1.00 27.10           C  
ANISOU 1582  CE2 TYR A 204     4483   2745   3067    197   1152    -96       C  
ATOM   1583  CZ  TYR A 204      32.667  42.752  34.322  1.00 28.77           C  
ANISOU 1583  CZ  TYR A 204     4678   2945   3308    218   1220    -46       C  
ATOM   1584  OH  TYR A 204      32.579  42.740  32.952  1.00 30.48           O  
ANISOU 1584  OH  TYR A 204     4957   3163   3460    282   1282    -22       O  
ATOM   1585  N   ILE A 205      36.498  43.473  37.789  1.00 27.66           N  
ANISOU 1585  N   ILE A 205     4229   2713   3568    100   1130     -2       N  
ATOM   1586  CA  ILE A 205      37.449  44.517  37.384  1.00 29.79           C  
ANISOU 1586  CA  ILE A 205     4418   2937   3962     97   1176     61       C  
ATOM   1587  C   ILE A 205      37.232  44.877  35.914  1.00 30.13           C  
ANISOU 1587  C   ILE A 205     4495   2989   3962    142   1285    114       C  
ATOM   1588  O   ILE A 205      37.407  44.068  35.026  1.00 30.36           O  
ANISOU 1588  O   ILE A 205     4563   3037   3933    196   1358    138       O  
ATOM   1589  CB  ILE A 205      38.885  44.079  37.693  1.00 31.14           C  
ANISOU 1589  CB  ILE A 205     4502   3073   4256     99   1183     96       C  
ATOM   1590  CG1 ILE A 205      39.056  43.919  39.206  1.00 34.74           C  
ANISOU 1590  CG1 ILE A 205     4933   3514   4752     59   1059     38       C  
ATOM   1591  CG2 ILE A 205      39.887  45.066  37.130  1.00 33.24           C  
ANISOU 1591  CG2 ILE A 205     4673   3284   4671    102   1246    180       C  
ATOM   1592  CD1 ILE A 205      39.863  42.737  39.591  1.00 37.50           C  
ANISOU 1592  CD1 ILE A 205     5258   3864   5125     72   1050     35       C  
ATOM   1593  N   VAL A 206      36.846  46.129  35.694  1.00 32.84           N  
ANISOU 1593  N   VAL A 206     4829   3316   4330    126   1290    132       N  
ATOM   1594  CA  VAL A 206      36.687  46.706  34.358  1.00 35.17           C  
ANISOU 1594  CA  VAL A 206     5153   3613   4596    173   1393    191       C  
ATOM   1595  C   VAL A 206      38.071  47.110  33.835  1.00 34.76           C  
ANISOU 1595  C   VAL A 206     5006   3513   4686    198   1486    288       C  
ATOM   1596  O   VAL A 206      38.796  47.865  34.482  1.00 36.72           O  
ANISOU 1596  O   VAL A 206     5153   3710   5088    153   1451    312       O  
ATOM   1597  CB  VAL A 206      35.702  47.890  34.390  1.00 35.40           C  
ANISOU 1597  CB  VAL A 206     5207   3642   4600    145   1360    173       C  
ATOM   1598  CG1 VAL A 206      35.491  48.481  33.012  1.00 39.04           C  
ANISOU 1598  CG1 VAL A 206     5705   4105   5021    199   1464    233       C  
ATOM   1599  CG2 VAL A 206      34.375  47.480  35.008  1.00 36.47           C  
ANISOU 1599  CG2 VAL A 206     5419   3817   4618    121   1272     88       C  
ATOM   1600  N   VAL A 207      38.442  46.571  32.671  1.00 35.77           N  
ANISOU 1600  N   VAL A 207     5168   3653   4768    275   1603    345       N  
ATOM   1601  CA  VAL A 207      39.708  46.881  32.026  1.00 39.29           C  
ANISOU 1601  CA  VAL A 207     5530   4054   5342    318   1720    456       C  
ATOM   1602  C   VAL A 207      39.427  47.875  30.888  1.00 39.91           C  
ANISOU 1602  C   VAL A 207     5638   4125   5401    368   1824    525       C  
ATOM   1603  O   VAL A 207      38.747  47.521  29.908  1.00 38.25           O  
ANISOU 1603  O   VAL A 207     5546   3954   5033    441   1878    519       O  
ATOM   1604  CB  VAL A 207      40.405  45.601  31.532  1.00 39.20           C  
ANISOU 1604  CB  VAL A 207     5541   4057   5294    386   1794    484       C  
ATOM   1605  CG1 VAL A 207      41.734  45.906  30.889  1.00 41.14           C  
ANISOU 1605  CG1 VAL A 207     5693   4252   5683    437   1929    611       C  
ATOM   1606  CG2 VAL A 207      40.608  44.606  32.665  1.00 40.30           C  
ANISOU 1606  CG2 VAL A 207     5660   4207   5446    336   1690    412       C  
ATOM   1607  N   ASN A 208      39.895  49.119  31.056  1.00 40.65           N  
ANISOU 1607  N   ASN A 208     5627   4163   5652    332   1837    585       N  
ATOM   1608  CA  ASN A 208      39.654  50.199  30.075  1.00 48.86           C  
ANISOU 1608  CA  ASN A 208     6682   5189   6694    374   1934    658       C  
ATOM   1609  C   ASN A 208      40.779  50.244  29.034  1.00 48.17           C  
ANISOU 1609  C   ASN A 208     6542   5064   6693    463   2108    797       C  
ATOM   1610  O   ASN A 208      41.919  50.052  29.409  1.00 47.93           O  
ANISOU 1610  O   ASN A 208     6397   4989   6825    448   2128    851       O  
ATOM   1611  CB  ASN A 208      39.539  51.564  30.747  1.00 53.28           C  
ANISOU 1611  CB  ASN A 208     7156   5700   7385    294   1863    657       C  
ATOM   1612  CG  ASN A 208      38.332  51.648  31.651  1.00 59.46           C  
ANISOU 1612  CG  ASN A 208     8005   6519   8068    227   1714    533       C  
ATOM   1613  OD1 ASN A 208      38.456  52.047  32.805  1.00 72.69           O  
ANISOU 1613  OD1 ASN A 208     9616   8162   9840    152   1599    487       O  
ATOM   1614  ND2 ASN A 208      37.173  51.251  31.144  1.00 58.44           N  
ANISOU 1614  ND2 ASN A 208     8004   6451   7746    261   1714    480       N  
ATOM   1615  N   SER A 221      23.718  59.401  16.436  1.00 90.40           N  
ANISOU 1615  N   SER A 221    13637  10689  10019   1299   1999    567       N  
ATOM   1616  CA  SER A 221      22.348  58.939  16.656  1.00 85.50           C  
ANISOU 1616  CA  SER A 221    13071  10078   9334   1254   1813    446       C  
ATOM   1617  C   SER A 221      21.382  60.134  16.698  1.00 79.25           C  
ANISOU 1617  C   SER A 221    12263   9285   8562   1209   1775    446       C  
ATOM   1618  O   SER A 221      21.726  61.195  17.225  1.00 73.64           O  
ANISOU 1618  O   SER A 221    11439   8569   7971   1134   1848    507       O  
ATOM   1619  CB  SER A 221      22.253  58.113  17.913  1.00 81.69           C  
ANISOU 1619  CB  SER A 221    12490   9603   8941   1119   1706    369       C  
ATOM   1620  OG  SER A 221      20.950  57.563  18.049  1.00 84.76           O  
ANISOU 1620  OG  SER A 221    12931   9994   9278   1089   1535    265       O  
ATOM   1621  N   THR A 222      20.180  59.946  16.128  1.00 72.29           N  
ANISOU 1621  N   THR A 222    11495   8402   7567   1257   1654    376       N  
ATOM   1622  CA  THR A 222      19.100  60.957  16.134  1.00 65.02           C  
ANISOU 1622  CA  THR A 222    10569   7479   6654   1219   1597    365       C  
ATOM   1623  C   THR A 222      18.354  60.895  17.477  1.00 59.63           C  
ANISOU 1623  C   THR A 222     9765   6801   6087   1053   1476    295       C  
ATOM   1624  O   THR A 222      17.714  61.886  17.855  1.00 47.42           O  
ANISOU 1624  O   THR A 222     8164   5254   4597    987   1459    303       O  
ATOM   1625  CB  THR A 222      18.137  60.783  14.945  1.00 67.79           C  
ANISOU 1625  CB  THR A 222    11092   7819   6843   1348   1510    322       C  
ATOM   1626  OG1 THR A 222      17.441  62.016  14.726  1.00 67.75           O  
ANISOU 1626  OG1 THR A 222    11085   7813   6844   1341   1517    350       O  
ATOM   1627  CG2 THR A 222      17.121  59.673  15.135  1.00 62.40           C  
ANISOU 1627  CG2 THR A 222    10453   7127   6129   1321   1314    204       C  
ATOM   1628  N   GLY A 223      18.429  59.723  18.145  1.00 47.61           N  
ANISOU 1628  N   GLY A 223     8212   5283   4594    999   1399    233       N  
ATOM   1629  CA  GLY A 223      17.830  59.460  19.425  1.00 43.62           C  
ANISOU 1629  CA  GLY A 223     7600   4780   4190    861   1299    174       C  
ATOM   1630  C   GLY A 223      16.533  58.676  19.323  1.00 39.82           C  
ANISOU 1630  C   GLY A 223     7177   4287   3666    861   1133     87       C  
ATOM   1631  O   GLY A 223      15.965  58.325  20.345  1.00 34.79           O  
ANISOU 1631  O   GLY A 223     6458   3648   3112    759   1051     43       O  
ATOM   1632  N   ASN A 224      16.071  58.383  18.103  1.00 39.98           N  
ANISOU 1632  N   ASN A 224     7336   4290   3562    981   1081     63       N  
ATOM   1633  CA  ASN A 224      14.827  57.632  17.891  1.00 40.51           C  
ANISOU 1633  CA  ASN A 224     7460   4330   3601    990    905    -20       C  
ATOM   1634  C   ASN A 224      14.938  56.278  18.621  1.00 38.58           C  
ANISOU 1634  C   ASN A 224     7169   4077   3410    933    830    -75       C  
ATOM   1635  O   ASN A 224      14.069  55.915  19.406  1.00 38.45           O  
ANISOU 1635  O   ASN A 224     7080   4046   3480    844    725   -118       O  
ATOM   1636  CB  ASN A 224      14.495  57.443  16.401  1.00 45.76           C  
ANISOU 1636  CB  ASN A 224     8301   4970   4113   1148    852    -42       C  
ATOM   1637  CG  ASN A 224      13.348  56.470  16.186  1.00 50.41           C  
ANISOU 1637  CG  ASN A 224     8946   5515   4691   1160    650   -136       C  
ATOM   1638  OD1 ASN A 224      13.463  55.512  15.421  1.00 60.20           O  
ANISOU 1638  OD1 ASN A 224    10306   6730   5837   1264    582   -182       O  
ATOM   1639  ND2 ASN A 224      12.245  56.675  16.888  1.00 53.36           N  
ANISOU 1639  ND2 ASN A 224     9228   5874   5169   1057    551   -163       N  
ATOM   1640  N   GLN A 225      16.051  55.570  18.429  1.00 33.79           N  
ANISOU 1640  N   GLN A 225     6594   3480   2763    983    899    -63       N  
ATOM   1641  CA  GLN A 225      16.259  54.251  19.098  1.00 34.92           C  
ANISOU 1641  CA  GLN A 225     6697   3616   2954    935    837   -112       C  
ATOM   1642  C   GLN A 225      16.487  54.442  20.599  1.00 31.57           C  
ANISOU 1642  C   GLN A 225     6111   3214   2669    790    875    -94       C  
ATOM   1643  O   GLN A 225      15.929  53.688  21.409  1.00 31.12           O  
ANISOU 1643  O   GLN A 225     5993   3145   2685    716    782   -140       O  
ATOM   1644  CB  GLN A 225      17.428  53.473  18.477  1.00 35.56           C  
ANISOU 1644  CB  GLN A 225     6858   3701   2951   1034    909   -100       C  
ATOM   1645  N   TYR A 226      17.333  55.415  20.965  1.00 29.41           N  
ANISOU 1645  N   TYR A 226     5771   2967   2436    759   1009    -26       N  
ATOM   1646  CA  TYR A 226      17.752  55.574  22.376  1.00 29.99           C  
ANISOU 1646  CA  TYR A 226     5706   3056   2631    639   1045    -11       C  
ATOM   1647  C   TYR A 226      16.524  55.929  23.231  1.00 28.65           C  
ANISOU 1647  C   TYR A 226     5470   2881   2534    548    958    -39       C  
ATOM   1648  O   TYR A 226      16.306  55.308  24.284  1.00 28.26           O  
ANISOU 1648  O   TYR A 226     5348   2830   2556    473    910    -67       O  
ATOM   1649  CB  TYR A 226      18.875  56.608  22.506  1.00 30.45           C  
ANISOU 1649  CB  TYR A 226     5710   3129   2729    630   1188     65       C  
ATOM   1650  CG  TYR A 226      19.156  57.082  23.912  1.00 29.01           C  
ANISOU 1650  CG  TYR A 226     5398   2953   2669    514   1206     76       C  
ATOM   1651  CD1 TYR A 226      19.759  56.247  24.842  1.00 30.14           C  
ANISOU 1651  CD1 TYR A 226     5478   3101   2869    461   1196     56       C  
ATOM   1652  CD2 TYR A 226      18.827  58.365  24.324  1.00 28.40           C  
ANISOU 1652  CD2 TYR A 226     5268   2874   2646    465   1228    103       C  
ATOM   1653  CE1 TYR A 226      20.046  56.668  26.132  1.00 27.86           C  
ANISOU 1653  CE1 TYR A 226     5087   2816   2682    370   1204     62       C  
ATOM   1654  CE2 TYR A 226      19.079  58.790  25.617  1.00 29.38           C  
ANISOU 1654  CE2 TYR A 226     5290   2998   2872    372   1232    106       C  
ATOM   1655  CZ  TYR A 226      19.687  57.944  26.526  1.00 29.04           C  
ANISOU 1655  CZ  TYR A 226     5195   2960   2879    327   1217     84       C  
ATOM   1656  OH  TYR A 226      19.963  58.368  27.796  1.00 29.71           O  
ANISOU 1656  OH  TYR A 226     5193   3040   3052    250   1213     82       O  
ATOM   1657  N   PHE A 227      15.702  56.881  22.756  1.00 28.17           N  
ANISOU 1657  N   PHE A 227     5438   2813   2452    565    942    -28       N  
ATOM   1658  CA  PHE A 227      14.512  57.321  23.503  1.00 29.79           C  
ANISOU 1658  CA  PHE A 227     5581   3010   2725    489    872    -43       C  
ATOM   1659  C   PHE A 227      13.388  56.266  23.445  1.00 30.34           C  
ANISOU 1659  C   PHE A 227     5671   3050   2806    489    731   -102       C  
ATOM   1660  O   PHE A 227      12.586  56.200  24.367  1.00 29.23           O  
ANISOU 1660  O   PHE A 227     5454   2900   2751    416    681   -111       O  
ATOM   1661  CB  PHE A 227      14.110  58.751  23.102  1.00 29.16           C  
ANISOU 1661  CB  PHE A 227     5513   2933   2633    501    913     -5       C  
ATOM   1662  CG  PHE A 227      15.055  59.764  23.702  1.00 28.65           C  
ANISOU 1662  CG  PHE A 227     5379   2886   2620    458   1030     48       C  
ATOM   1663  CD1 PHE A 227      15.199  59.861  25.085  1.00 28.04           C  
ANISOU 1663  CD1 PHE A 227     5201   2814   2636    365   1035     46       C  
ATOM   1664  CD2 PHE A 227      15.896  60.528  22.897  1.00 29.48           C  
ANISOU 1664  CD2 PHE A 227     5519   2995   2686    519   1135    104       C  
ATOM   1665  CE1 PHE A 227      16.122  60.731  25.653  1.00 27.33           C  
ANISOU 1665  CE1 PHE A 227     5051   2729   2604    329   1122     87       C  
ATOM   1666  CE2 PHE A 227      16.799  61.410  23.467  1.00 28.10           C  
ANISOU 1666  CE2 PHE A 227     5267   2822   2584    475   1231    155       C  
ATOM   1667  CZ  PHE A 227      16.911  61.515  24.840  1.00 28.68           C  
ANISOU 1667  CZ  PHE A 227     5245   2897   2755    379   1215    141       C  
ATOM   1668  N   ALA A 228      13.340  55.431  22.405  1.00 30.27           N  
ANISOU 1668  N   ALA A 228     5761   3019   2719    574    667   -138       N  
ATOM   1669  CA  ALA A 228      12.428  54.256  22.422  1.00 32.02           C  
ANISOU 1669  CA  ALA A 228     5991   3200   2975    569    521   -196       C  
ATOM   1670  C   ALA A 228      12.748  53.346  23.628  1.00 30.61           C  
ANISOU 1670  C   ALA A 228     5718   3026   2885    490    523   -205       C  
ATOM   1671  O   ALA A 228      11.849  52.812  24.305  1.00 27.92           O  
ANISOU 1671  O   ALA A 228     5312   2658   2636    434    440   -222       O  
ATOM   1672  CB  ALA A 228      12.493  53.514  21.116  1.00 31.22           C  
ANISOU 1672  CB  ALA A 228     6024   3069   2768    683    450   -239       C  
ATOM   1673  N   THR A 229      14.042  53.216  23.921  1.00 30.75           N  
ANISOU 1673  N   THR A 229     5724   3077   2882    489    625   -184       N  
ATOM   1674  CA  THR A 229      14.537  52.402  25.011  1.00 29.09           C  
ANISOU 1674  CA  THR A 229     5436   2875   2739    426    640   -189       C  
ATOM   1675  C   THR A 229      14.237  53.071  26.353  1.00 27.21           C  
ANISOU 1675  C   THR A 229     5088   2653   2594    333    675   -160       C  
ATOM   1676  O   THR A 229      13.867  52.395  27.295  1.00 25.84           O  
ANISOU 1676  O   THR A 229     4851   2470   2494    280    637   -170       O  
ATOM   1677  CB  THR A 229      16.022  52.071  24.799  1.00 30.86           C  
ANISOU 1677  CB  THR A 229     5687   3125   2913    463    732   -174       C  
ATOM   1678  OG1 THR A 229      16.083  51.291  23.604  1.00 31.77           O  
ANISOU 1678  OG1 THR A 229     5914   3217   2938    561    682   -207       O  
ATOM   1679  CG2 THR A 229      16.677  51.325  25.935  1.00 30.59           C  
ANISOU 1679  CG2 THR A 229     5574   3103   2945    402    755   -176       C  
ATOM   1680  N   ILE A 230      14.417  54.391  26.444  1.00 27.18           N  
ANISOU 1680  N   ILE A 230     5068   2670   2586    320    749   -122       N  
ATOM   1681  CA  ILE A 230      14.110  55.118  27.681  1.00 26.34           C  
ANISOU 1681  CA  ILE A 230     4876   2575   2555    245    777    -99       C  
ATOM   1682  C   ILE A 230      12.604  55.032  27.924  1.00 24.09           C  
ANISOU 1682  C   ILE A 230     4566   2263   2322    222    692   -108       C  
ATOM   1683  O   ILE A 230      12.174  54.878  29.031  1.00 24.05           O  
ANISOU 1683  O   ILE A 230     4494   2255   2387    172    687    -99       O  
ATOM   1684  CB  ILE A 230      14.617  56.570  27.629  1.00 27.52           C  
ANISOU 1684  CB  ILE A 230     5019   2743   2694    242    864    -59       C  
ATOM   1685  CG1 ILE A 230      16.145  56.648  27.490  1.00 28.60           C  
ANISOU 1685  CG1 ILE A 230     5157   2895   2813    259    952    -37       C  
ATOM   1686  CG2 ILE A 230      14.108  57.364  28.827  1.00 27.32           C  
ANISOU 1686  CG2 ILE A 230     4925   2720   2736    179    874    -43       C  
ATOM   1687  CD1 ILE A 230      16.913  55.703  28.378  1.00 29.43           C  
ANISOU 1687  CD1 ILE A 230     5216   3007   2956    226    957    -51       C  
ATOM   1688  N   ASN A 231      11.812  55.121  26.859  1.00 24.16           N  
ANISOU 1688  N   ASN A 231     4633   2247   2297    268    626   -122       N  
ATOM   1689  CA  ASN A 231      10.395  55.006  26.981  1.00 25.04           C  
ANISOU 1689  CA  ASN A 231     4715   2323   2474    250    537   -127       C  
ATOM   1690  C   ASN A 231      10.029  53.674  27.649  1.00 26.17           C  
ANISOU 1690  C   ASN A 231     4806   2438   2697    220    474   -144       C  
ATOM   1691  O   ASN A 231       9.105  53.623  28.483  1.00 24.16           O  
ANISOU 1691  O   ASN A 231     4477   2164   2538    177    452   -122       O  
ATOM   1692  CB  ASN A 231       9.718  55.113  25.616  1.00 27.33           C  
ANISOU 1692  CB  ASN A 231     5087   2583   2713    315    454   -149       C  
ATOM   1693  CG  ASN A 231       8.212  55.041  25.711  1.00 29.77           C  
ANISOU 1693  CG  ASN A 231     5353   2845   3111    294    352   -150       C  
ATOM   1694  OD1 ASN A 231       7.603  54.228  25.035  1.00 37.37           O  
ANISOU 1694  OD1 ASN A 231     6349   3758   4089    327    233   -187       O  
ATOM   1695  ND2 ASN A 231       7.603  55.841  26.575  1.00 26.63           N  
ANISOU 1695  ND2 ASN A 231     4880   2455   2781    242    393   -110       N  
ATOM   1696  N   GLU A 232      10.727  52.603  27.261  1.00 25.89           N  
ANISOU 1696  N   GLU A 232     4810   2398   2627    249    449   -177       N  
ATOM   1697  CA  GLU A 232      10.523  51.263  27.807  1.00 26.23           C  
ANISOU 1697  CA  GLU A 232     4810   2412   2744    226    391   -194       C  
ATOM   1698  C   GLU A 232      10.872  51.212  29.295  1.00 24.35           C  
ANISOU 1698  C   GLU A 232     4485   2200   2564    166    469   -161       C  
ATOM   1699  O   GLU A 232      10.231  50.415  30.016  1.00 23.12           O  
ANISOU 1699  O   GLU A 232     4265   2014   2502    136    430   -152       O  
ATOM   1700  CB  GLU A 232      11.370  50.208  27.086  1.00 29.71           C  
ANISOU 1700  CB  GLU A 232     5320   2846   3120    276    362   -237       C  
ATOM   1701  CG  GLU A 232      10.979  50.009  25.644  1.00 34.80           C  
ANISOU 1701  CG  GLU A 232     6068   3453   3701    353    264   -279       C  
ATOM   1702  CD  GLU A 232       9.536  49.602  25.486  1.00 42.05           C  
ANISOU 1702  CD  GLU A 232     6958   4303   4715    344    124   -296       C  
ATOM   1703  OE1 GLU A 232       9.075  48.780  26.293  1.00 54.95           O  
ANISOU 1703  OE1 GLU A 232     8509   5906   6464    294     84   -289       O  
ATOM   1704  OE2 GLU A 232       8.877  50.110  24.582  1.00 49.88           O  
ANISOU 1704  OE2 GLU A 232     8007   5269   5675    387     57   -310       O  
ATOM   1705  N   ILE A 233      11.897  51.964  29.721  1.00 22.16           N  
ANISOU 1705  N   ILE A 233     4208   1971   2238    155    571   -144       N  
ATOM   1706  CA  ILE A 233      12.270  52.007  31.141  1.00 22.33           C  
ANISOU 1706  CA  ILE A 233     4164   2015   2303    109    635   -120       C  
ATOM   1707  C   ILE A 233      11.077  52.545  31.961  1.00 22.44           C  
ANISOU 1707  C   ILE A 233     4121   2015   2390     81    633    -84       C  
ATOM   1708  O   ILE A 233      10.696  51.939  32.994  1.00 20.96           O  
ANISOU 1708  O   ILE A 233     3876   1815   2270     59    636    -64       O  
ATOM   1709  CB  ILE A 233      13.582  52.780  31.374  1.00 20.58           C  
ANISOU 1709  CB  ILE A 233     3954   1835   2030    106    724   -112       C  
ATOM   1710  CG1 ILE A 233      14.791  51.996  30.876  1.00 22.87           C  
ANISOU 1710  CG1 ILE A 233     4278   2135   2274    132    740   -134       C  
ATOM   1711  CG2 ILE A 233      13.778  53.177  32.817  1.00 21.35           C  
ANISOU 1711  CG2 ILE A 233     3997   1948   2166     68    774    -90       C  
ATOM   1712  CD1 ILE A 233      16.107  52.775  30.824  1.00 23.01           C  
ANISOU 1712  CD1 ILE A 233     4303   2181   2257    137    824   -118       C  
ATOM   1713  N   TYR A 234      10.475  53.666  31.518  1.00 23.19           N  
ANISOU 1713  N   TYR A 234     4230   2108   2471     87    635    -70       N  
ATOM   1714  CA  TYR A 234       9.382  54.263  32.257  1.00 23.15           C  
ANISOU 1714  CA  TYR A 234     4175   2090   2531     67    643    -31       C  
ATOM   1715  C   TYR A 234       8.175  53.315  32.263  1.00 24.19           C  
ANISOU 1715  C   TYR A 234     4259   2170   2760     64    566    -18       C  
ATOM   1716  O   TYR A 234       7.501  53.182  33.297  1.00 23.93           O  
ANISOU 1716  O   TYR A 234     4163   2123   2807     48    590     24       O  
ATOM   1717  CB  TYR A 234       9.006  55.654  31.732  1.00 22.84           C  
ANISOU 1717  CB  TYR A 234     4161   2058   2457     76    660    -18       C  
ATOM   1718  CG  TYR A 234       9.990  56.744  32.060  1.00 22.94           C  
ANISOU 1718  CG  TYR A 234     4193   2109   2414     70    742    -13       C  
ATOM   1719  CD1 TYR A 234      10.152  57.203  33.354  1.00 24.31           C  
ANISOU 1719  CD1 TYR A 234     4334   2295   2607     50    797      6       C  
ATOM   1720  CD2 TYR A 234      10.796  57.295  31.076  1.00 22.19           C  
ANISOU 1720  CD2 TYR A 234     4152   2030   2250     92    763    -27       C  
ATOM   1721  CE1 TYR A 234      11.042  58.229  33.640  1.00 22.93           C  
ANISOU 1721  CE1 TYR A 234     4175   2141   2396     45    852      6       C  
ATOM   1722  CE2 TYR A 234      11.714  58.293  31.354  1.00 23.11           C  
ANISOU 1722  CE2 TYR A 234     4272   2168   2339     84    833    -17       C  
ATOM   1723  CZ  TYR A 234      11.833  58.774  32.641  1.00 23.14           C  
ANISOU 1723  CZ  TYR A 234     4239   2178   2375     56    869     -4       C  
ATOM   1724  OH  TYR A 234      12.709  59.792  32.918  1.00 24.10           O  
ANISOU 1724  OH  TYR A 234     4362   2308   2486     48    919      1       O  
ATOM   1725  N   LYS A 235       7.893  52.691  31.119  1.00 25.02           N  
ANISOU 1725  N   LYS A 235     4397   2241   2866     86    473    -52       N  
ATOM   1726  CA  LYS A 235       6.831  51.703  31.013  1.00 28.01           C  
ANISOU 1726  CA  LYS A 235     4728   2556   3356     83    377    -47       C  
ATOM   1727  C   LYS A 235       7.028  50.562  32.015  1.00 26.92           C  
ANISOU 1727  C   LYS A 235     4532   2408   3288     61    395    -30       C  
ATOM   1728  O   LYS A 235       6.050  50.121  32.632  1.00 26.70           O  
ANISOU 1728  O   LYS A 235     4424   2335   3384     45    377     14       O  
ATOM   1729  CB  LYS A 235       6.731  51.144  29.595  1.00 30.32           C  
ANISOU 1729  CB  LYS A 235     5087   2810   3620    121    260   -102       C  
ATOM   1730  CG  LYS A 235       5.922  52.015  28.642  1.00 34.92           C  
ANISOU 1730  CG  LYS A 235     5705   3371   4188    146    202   -107       C  
ATOM   1731  CD  LYS A 235       5.797  51.426  27.239  1.00 40.64           C  
ANISOU 1731  CD  LYS A 235     6513   4051   4874    201     71   -167       C  
ATOM   1732  N   ALA A 236       8.271  50.087  32.164  1.00 26.19           N  
ANISOU 1732  N   ALA A 236     4475   2352   3124     65    434    -60       N  
ATOM   1733  CA  ALA A 236       8.585  48.962  33.051  1.00 26.91           C  
ANISOU 1733  CA  ALA A 236     4520   2436   3267     50    451    -49       C  
ATOM   1734  C   ALA A 236       8.253  49.339  34.504  1.00 25.89           C  
ANISOU 1734  C   ALA A 236     4327   2321   3188     33    539     13       C  
ATOM   1735  O   ALA A 236       7.845  48.511  35.274  1.00 25.14           O  
ANISOU 1735  O   ALA A 236     4171   2198   3181     26    545     49       O  
ATOM   1736  CB  ALA A 236      10.045  48.571  32.928  1.00 27.75           C  
ANISOU 1736  CB  ALA A 236     4679   2585   3279     60    484    -90       C  
ATOM   1737  N   ILE A 237       8.518  50.595  34.865  1.00 24.57           N  
ANISOU 1737  N   ILE A 237     4182   2197   2956     33    611     25       N  
ATOM   1738  CA  ILE A 237       8.262  51.115  36.216  1.00 24.29           C  
ANISOU 1738  CA  ILE A 237     4111   2176   2941     33    694     77       C  
ATOM   1739  C   ILE A 237       6.756  51.195  36.472  1.00 24.16           C  
ANISOU 1739  C   ILE A 237     4030   2113   3036     36    684    139       C  
ATOM   1740  O   ILE A 237       6.265  50.681  37.473  1.00 25.19           O  
ANISOU 1740  O   ILE A 237     4105   2222   3241     45    725    195       O  
ATOM   1741  CB  ILE A 237       8.934  52.474  36.411  1.00 23.66           C  
ANISOU 1741  CB  ILE A 237     4080   2143   2767     37    753     65       C  
ATOM   1742  CG1 ILE A 237      10.459  52.342  36.434  1.00 24.11           C  
ANISOU 1742  CG1 ILE A 237     4178   2238   2744     34    775     21       C  
ATOM   1743  CG2 ILE A 237       8.408  53.137  37.657  1.00 24.33           C  
ANISOU 1743  CG2 ILE A 237     4142   2231   2870     51    821    117       C  
ATOM   1744  CD1 ILE A 237      11.175  53.656  36.341  1.00 24.56           C  
ANISOU 1744  CD1 ILE A 237     4275   2325   2730     33    813      5       C  
ATOM   1745  N   TYR A 238       6.028  51.819  35.549  1.00 24.94           N  
ANISOU 1745  N   TYR A 238     4134   2191   3150     34    633    135       N  
ATOM   1746  CA  TYR A 238       4.617  52.098  35.751  1.00 25.68           C  
ANISOU 1746  CA  TYR A 238     4163   2239   3354     37    627    198       C  
ATOM   1747  C   TYR A 238       3.764  50.833  35.671  1.00 27.70           C  
ANISOU 1747  C   TYR A 238     4341   2423   3760     30    558    229       C  
ATOM   1748  O   TYR A 238       2.634  50.861  36.143  1.00 29.59           O  
ANISOU 1748  O   TYR A 238     4504   2618   4121     34    574    302       O  
ATOM   1749  CB  TYR A 238       4.137  53.180  34.787  1.00 24.87           C  
ANISOU 1749  CB  TYR A 238     4091   2135   3222     39    589    183       C  
ATOM   1750  CG  TYR A 238       4.371  54.556  35.357  1.00 24.29           C  
ANISOU 1750  CG  TYR A 238     4050   2108   3069     47    680    199       C  
ATOM   1751  CD1 TYR A 238       3.597  55.024  36.398  1.00 25.42           C  
ANISOU 1751  CD1 TYR A 238     4149   2243   3265     62    751    269       C  
ATOM   1752  CD2 TYR A 238       5.428  55.342  34.935  1.00 24.95           C  
ANISOU 1752  CD2 TYR A 238     4208   2241   3030     47    700    149       C  
ATOM   1753  CE1 TYR A 238       3.832  56.263  36.969  1.00 27.23           C  
ANISOU 1753  CE1 TYR A 238     4417   2509   3418     77    826    277       C  
ATOM   1754  CE2 TYR A 238       5.661  56.596  35.474  1.00 25.29           C  
ANISOU 1754  CE2 TYR A 238     4278   2317   3015     54    771    160       C  
ATOM   1755  CZ  TYR A 238       4.862  57.054  36.507  1.00 24.64           C  
ANISOU 1755  CZ  TYR A 238     4161   2224   2977     69    829    220       C  
ATOM   1756  OH  TYR A 238       5.061  58.271  37.075  1.00 25.34           O  
ANISOU 1756  OH  TYR A 238     4283   2337   3007     83    890    227       O  
ATOM   1757  N   LYS A 239       4.300  49.745  35.096  1.00 27.55           N  
ANISOU 1757  N   LYS A 239     4338   2388   3741     23    485    178       N  
ATOM   1758  CA  LYS A 239       3.577  48.458  35.018  1.00 29.49           C  
ANISOU 1758  CA  LYS A 239     4509   2556   4141     14    406    201       C  
ATOM   1759  C   LYS A 239       4.167  47.405  35.969  1.00 27.17           C  
ANISOU 1759  C   LYS A 239     4187   2268   3869     14    460    220       C  
ATOM   1760  O   LYS A 239       3.812  46.205  35.868  1.00 28.52           O  
ANISOU 1760  O   LYS A 239     4301   2375   4159      5    393    230       O  
ATOM   1761  CB  LYS A 239       3.604  47.956  33.575  1.00 33.34           C  
ANISOU 1761  CB  LYS A 239     5041   3003   4622     16    261    125       C  
ATOM   1762  CG  LYS A 239       2.942  48.884  32.575  1.00 36.57           C  
ANISOU 1762  CG  LYS A 239     5480   3396   5016     25    193    106       C  
ATOM   1763  CD  LYS A 239       2.644  48.215  31.258  1.00 42.84           C  
ANISOU 1763  CD  LYS A 239     6309   4125   5842     40     28     43       C  
ATOM   1764  CE  LYS A 239       1.747  49.067  30.385  1.00 47.42           C  
ANISOU 1764  CE  LYS A 239     6904   4674   6439     54    -48     37       C  
ATOM   1765  NZ  LYS A 239       0.725  48.231  29.714  1.00 54.44           N  
ANISOU 1765  NZ  LYS A 239     7746   5452   7484     56   -217     26       N  
ATOM   1766  N   SER A 240       5.011  47.827  36.917  1.00 23.89           N  
ANISOU 1766  N   SER A 240     3805   1920   3350     25    572    228       N  
ATOM   1767  CA  SER A 240       5.639  46.919  37.862  1.00 24.51           C  
ANISOU 1767  CA  SER A 240     3869   2010   3431     32    627    245       C  
ATOM   1768  C   SER A 240       4.592  46.146  38.659  1.00 26.50           C  
ANISOU 1768  C   SER A 240     4017   2198   3851     40    653    339       C  
ATOM   1769  O   SER A 240       3.720  46.750  39.288  1.00 27.35           O  
ANISOU 1769  O   SER A 240     4080   2293   4017     59    719    416       O  
ATOM   1770  CB  SER A 240       6.572  47.628  38.791  1.00 23.14           C  
ANISOU 1770  CB  SER A 240     3751   1910   3131     50    731    241       C  
ATOM   1771  OG  SER A 240       7.231  46.684  39.621  1.00 22.84           O  
ANISOU 1771  OG  SER A 240     3706   1882   3090     61    770    249       O  
ATOM   1772  N   PRO A 241       4.630  44.787  38.654  1.00 30.28           N  
ANISOU 1772  N   PRO A 241     4450   2630   4422     31    607    342       N  
ATOM   1773  CA  PRO A 241       3.795  44.004  39.563  1.00 29.95           C  
ANISOU 1773  CA  PRO A 241     4305   2529   4543     45    655    444       C  
ATOM   1774  C   PRO A 241       4.409  43.877  40.966  1.00 31.84           C  
ANISOU 1774  C   PRO A 241     4562   2817   4717     83    789    490       C  
ATOM   1775  O   PRO A 241       3.735  43.342  41.837  1.00 33.33           O  
ANISOU 1775  O   PRO A 241     4673   2963   5026    109    856    589       O  
ATOM   1776  CB  PRO A 241       3.700  42.626  38.885  1.00 31.72           C  
ANISOU 1776  CB  PRO A 241     4484   2680   4886     19    537    417       C  
ATOM   1777  CG  PRO A 241       4.983  42.509  38.074  1.00 31.79           C  
ANISOU 1777  CG  PRO A 241     4600   2743   4735      8    477    299       C  
ATOM   1778  CD  PRO A 241       5.426  43.935  37.751  1.00 29.35           C  
ANISOU 1778  CD  PRO A 241     4377   2508   4265     13    510    255       C  
ATOM   1779  N   ILE A 242       5.655  44.336  41.151  1.00 29.69           N  
ANISOU 1779  N   ILE A 242     4387   2626   4267     90    822    422       N  
ATOM   1780  CA  ILE A 242       6.318  44.420  42.458  1.00 29.25           C  
ANISOU 1780  CA  ILE A 242     4369   2620   4124    133    933    449       C  
ATOM   1781  C   ILE A 242       5.975  45.746  43.159  1.00 28.25           C  
ANISOU 1781  C   ILE A 242     4276   2525   3931    174   1020    489       C  
ATOM   1782  O   ILE A 242       5.552  45.754  44.324  1.00 28.19           O  
ANISOU 1782  O   ILE A 242     4253   2511   3946    231   1121    574       O  
ATOM   1783  CB  ILE A 242       7.844  44.246  42.312  1.00 30.57           C  
ANISOU 1783  CB  ILE A 242     4616   2846   4150    121    911    356       C  
ATOM   1784  CG1 ILE A 242       8.221  42.938  41.602  1.00 33.76           C  
ANISOU 1784  CG1 ILE A 242     4998   3219   4608     89    828    314       C  
ATOM   1785  CG2 ILE A 242       8.527  44.372  43.673  1.00 29.74           C  
ANISOU 1785  CG2 ILE A 242     4556   2785   3957    171   1008    378       C  
ATOM   1786  CD1 ILE A 242       7.770  41.680  42.305  1.00 34.23           C  
ANISOU 1786  CD1 ILE A 242     4982   3227   4795    104    854    386       C  
ATOM   1787  N   TYR A 243       6.204  46.870  42.472  1.00 25.23           N  
ANISOU 1787  N   TYR A 243     3948   2177   3461    153    985    429       N  
ATOM   1788  CA  TYR A 243       5.890  48.219  42.980  1.00 26.70           C  
ANISOU 1788  CA  TYR A 243     4171   2389   3583    186   1051    455       C  
ATOM   1789  C   TYR A 243       4.553  48.651  42.370  1.00 25.98           C  
ANISOU 1789  C   TYR A 243     4017   2250   3603    174   1027    503       C  
ATOM   1790  O   TYR A 243       4.515  49.265  41.278  1.00 27.81           O  
ANISOU 1790  O   TYR A 243     4268   2486   3811    136    954    449       O  
ATOM   1791  CB  TYR A 243       7.033  49.190  42.657  1.00 26.14           C  
ANISOU 1791  CB  TYR A 243     4193   2379   3358    172   1030    364       C  
ATOM   1792  CG  TYR A 243       8.376  48.711  43.131  1.00 27.79           C  
ANISOU 1792  CG  TYR A 243     4452   2625   3480    177   1035    313       C  
ATOM   1793  CD1 TYR A 243       8.803  48.959  44.427  1.00 27.73           C  
ANISOU 1793  CD1 TYR A 243     4491   2642   3403    233   1106    332       C  
ATOM   1794  CD2 TYR A 243       9.190  47.930  42.317  1.00 27.69           C  
ANISOU 1794  CD2 TYR A 243     4442   2618   3459    136    967    250       C  
ATOM   1795  CE1 TYR A 243      10.029  48.503  44.881  1.00 28.05           C  
ANISOU 1795  CE1 TYR A 243     4575   2711   3372    240   1101    285       C  
ATOM   1796  CE2 TYR A 243      10.407  47.448  42.766  1.00 26.87           C  
ANISOU 1796  CE2 TYR A 243     4374   2545   3288    141    974    211       C  
ATOM   1797  CZ  TYR A 243      10.814  47.705  44.064  1.00 28.20           C  
ANISOU 1797  CZ  TYR A 243     4581   2735   3396    191   1038    229       C  
ATOM   1798  OH  TYR A 243      12.006  47.223  44.508  1.00 26.55           O  
ANISOU 1798  OH  TYR A 243     4407   2552   3129    197   1034    189       O  
ATOM   1799  N   LYS A 244       3.462  48.323  43.062  1.00 27.25           N  
ANISOU 1799  N   LYS A 244     4101   2361   3888    209   1091    611       N  
ATOM   1800  CA  LYS A 244       2.134  48.428  42.500  1.00 29.78           C  
ANISOU 1800  CA  LYS A 244     4335   2618   4360    194   1058    670       C  
ATOM   1801  C   LYS A 244       1.468  49.747  42.894  1.00 30.42           C  
ANISOU 1801  C   LYS A 244     4434   2713   4411    232   1132    719       C  
ATOM   1802  O   LYS A 244       0.547  50.162  42.209  1.00 30.69           O  
ANISOU 1802  O   LYS A 244     4417   2708   4534    211   1089    741       O  
ATOM   1803  CB  LYS A 244       1.289  47.238  42.925  1.00 34.64           C  
ANISOU 1803  CB  LYS A 244     4836   3158   5166    207   1081    771       C  
ATOM   1804  CG  LYS A 244       1.674  45.926  42.253  1.00 38.24           C  
ANISOU 1804  CG  LYS A 244     5257   3577   5692    159    976    722       C  
ATOM   1805  CD  LYS A 244       0.886  44.757  42.798  1.00 43.83           C  
ANISOU 1805  CD  LYS A 244     5847   4204   6599    174   1007    830       C  
ATOM   1806  CE  LYS A 244       1.377  44.330  44.164  1.00 45.69           C  
ANISOU 1806  CE  LYS A 244     6105   4471   6782    236   1139    888       C  
ATOM   1807  NZ  LYS A 244       0.288  43.710  44.947  1.00 54.61           N  
ANISOU 1807  NZ  LYS A 244     7117   5524   8105    279   1229   1039       N  
ATOM   1808  N   ASN A 245       1.948  50.385  43.968  1.00 29.29           N  
ANISOU 1808  N   ASN A 245     4367   2619   4142    291   1233    730       N  
ATOM   1809  CA  ASN A 245       1.399  51.677  44.441  1.00 30.47           C  
ANISOU 1809  CA  ASN A 245     4550   2783   4243    340   1307    772       C  
ATOM   1810  C   ASN A 245       1.722  52.778  43.420  1.00 28.33           C  
ANISOU 1810  C   ASN A 245     4333   2544   3887    291   1230    681       C  
ATOM   1811  O   ASN A 245       2.858  52.916  43.056  1.00 26.14           O  
ANISOU 1811  O   ASN A 245     4124   2311   3497    261   1180    586       O  
ATOM   1812  CB  ASN A 245       1.984  52.053  45.799  1.00 30.36           C  
ANISOU 1812  CB  ASN A 245     4626   2809   4096    423   1411    786       C  
ATOM   1813  CG  ASN A 245       1.392  53.331  46.343  1.00 34.07           C  
ANISOU 1813  CG  ASN A 245     5140   3287   4515    485   1488    830       C  
ATOM   1814  OD1 ASN A 245       1.904  54.413  46.065  1.00 35.77           O  
ANISOU 1814  OD1 ASN A 245     5432   3540   4617    472   1454    754       O  
ATOM   1815  ND2 ASN A 245       0.296  53.221  47.088  1.00 33.14           N  
ANISOU 1815  ND2 ASN A 245     4971   3128   4490    557   1593    956       N  
ATOM   1816  N   GLN A 246       0.732  53.571  43.007  1.00 29.02           N  
ANISOU 1816  N   GLN A 246     4386   2606   4031    290   1229    719       N  
ATOM   1817  CA  GLN A 246       0.957  54.602  41.973  1.00 30.37           C  
ANISOU 1817  CA  GLN A 246     4604   2803   4131    247   1157    642       C  
ATOM   1818  C   GLN A 246       1.929  55.682  42.471  1.00 29.61           C  
ANISOU 1818  C   GLN A 246     4618   2767   3862    272   1197    584       C  
ATOM   1819  O   GLN A 246       2.725  56.137  41.692  1.00 27.35           O  
ANISOU 1819  O   GLN A 246     4382   2513   3497    230   1134    499       O  
ATOM   1820  CB  GLN A 246      -0.340  55.251  41.475  1.00 30.07           C  
ANISOU 1820  CB  GLN A 246     4507   2724   4194    244   1148    698       C  
ATOM   1821  CG  GLN A 246      -0.219  55.750  40.030  1.00 31.94           C  
ANISOU 1821  CG  GLN A 246     4763   2966   4404    187   1035    618       C  
ATOM   1822  CD  GLN A 246      -0.203  54.667  38.962  1.00 33.89           C  
ANISOU 1822  CD  GLN A 246     4967   3177   4732    137    914    577       C  
ATOM   1823  OE1 GLN A 246      -0.342  53.470  39.235  1.00 30.82           O  
ANISOU 1823  OE1 GLN A 246     4518   2751   4441    134    904    608       O  
ATOM   1824  NE2 GLN A 246      -0.091  55.089  37.710  1.00 35.06           N  
ANISOU 1824  NE2 GLN A 246     5149   3330   4843    105    819    509       N  
ATOM   1825  N   GLU A 247       1.871  56.081  43.753  1.00 27.73           N  
ANISOU 1825  N   GLU A 247     4422   2540   3573    346   1297    632       N  
ATOM   1826  CA  GLU A 247       2.782  57.105  44.233  1.00 26.99           C  
ANISOU 1826  CA  GLU A 247     4435   2491   3328    372   1313    571       C  
ATOM   1827  C   GLU A 247       4.221  56.578  44.230  1.00 26.89           C  
ANISOU 1827  C   GLU A 247     4469   2511   3235    344   1265    486       C  
ATOM   1828  O   GLU A 247       5.154  57.363  43.972  1.00 26.38           O  
ANISOU 1828  O   GLU A 247     4469   2477   3078    323   1227    408       O  
ATOM   1829  CB  GLU A 247       2.391  57.618  45.629  1.00 30.21           C  
ANISOU 1829  CB  GLU A 247     4894   2896   3689    473   1420    636       C  
ATOM   1830  CG  GLU A 247       2.981  58.981  45.968  1.00 30.69           C  
ANISOU 1830  CG  GLU A 247     5059   2983   3616    502   1420    577       C  
ATOM   1831  CD  GLU A 247       2.702  60.103  44.975  1.00 32.79           C  
ANISOU 1831  CD  GLU A 247     5322   3252   3885    453   1375    546       C  
ATOM   1832  OE1 GLU A 247       1.616  60.115  44.356  1.00 37.96           O  
ANISOU 1832  OE1 GLU A 247     5902   3881   4639    434   1378    602       O  
ATOM   1833  OE2 GLU A 247       3.573  60.963  44.806  1.00 35.22           O  
ANISOU 1833  OE2 GLU A 247     5696   3581   4102    436   1334    469       O  
ATOM   1834  N   LYS A 248       4.404  55.277  44.513  1.00 25.15           N  
ANISOU 1834  N   LYS A 248     4212   2281   3061    345   1269    504       N  
ATOM   1835  CA  LYS A 248       5.722  54.653  44.470  1.00 24.64           C  
ANISOU 1835  CA  LYS A 248     4182   2244   2935    317   1224    430       C  
ATOM   1836  C   LYS A 248       6.250  54.621  43.024  1.00 23.83           C  
ANISOU 1836  C   LYS A 248     4066   2152   2836    236   1130    356       C  
ATOM   1837  O   LYS A 248       7.439  54.817  42.798  1.00 21.21           O  
ANISOU 1837  O   LYS A 248     3782   1850   2426    213   1096    283       O  
ATOM   1838  CB  LYS A 248       5.688  53.247  45.061  1.00 25.20           C  
ANISOU 1838  CB  LYS A 248     4211   2298   3064    338   1252    474       C  
ATOM   1839  CG  LYS A 248       7.033  52.541  45.149  1.00 24.45           C  
ANISOU 1839  CG  LYS A 248     4151   2231   2907    319   1213    405       C  
ATOM   1840  CD  LYS A 248       8.047  53.222  46.032  1.00 25.40           C  
ANISOU 1840  CD  LYS A 248     4367   2383   2900    362   1228    358       C  
ATOM   1841  CE  LYS A 248       9.387  52.540  45.994  1.00 26.66           C  
ANISOU 1841  CE  LYS A 248     4547   2564   3015    335   1181    290       C  
ATOM   1842  NZ  LYS A 248      10.386  53.214  46.835  1.00 27.18           N  
ANISOU 1842  NZ  LYS A 248     4700   2651   2976    375   1176    241       N  
ATOM   1843  N   ARG A 249       5.354  54.412  42.057  1.00 22.83           N  
ANISOU 1843  N   ARG A 249     3877   1996   2802    202   1090    378       N  
ATOM   1844  CA  ARG A 249       5.753  54.445  40.673  1.00 23.61           C  
ANISOU 1844  CA  ARG A 249     3980   2101   2890    145   1005    313       C  
ATOM   1845  C   ARG A 249       6.184  55.875  40.290  1.00 23.84           C  
ANISOU 1845  C   ARG A 249     4068   2158   2829    138   1003    270       C  
ATOM   1846  O   ARG A 249       7.186  56.055  39.607  1.00 21.60           O  
ANISOU 1846  O   ARG A 249     3821   1899   2484    110    966    207       O  
ATOM   1847  CB  ARG A 249       4.626  53.886  39.796  1.00 24.41           C  
ANISOU 1847  CB  ARG A 249     4008   2153   3113    122    948    345       C  
ATOM   1848  CG  ARG A 249       4.419  52.386  39.964  1.00 25.42           C  
ANISOU 1848  CG  ARG A 249     4074   2244   3339    118    927    372       C  
ATOM   1849  CD  ARG A 249       3.059  51.938  39.464  1.00 25.59           C  
ANISOU 1849  CD  ARG A 249     4007   2198   3517    107    881    428       C  
ATOM   1850  NE  ARG A 249       2.871  50.493  39.394  1.00 25.26           N  
ANISOU 1850  NE  ARG A 249     3902   2108   3588     94    835    446       N  
ATOM   1851  CZ  ARG A 249       1.718  49.926  39.032  1.00 26.85           C  
ANISOU 1851  CZ  ARG A 249     4011   2234   3955     84    782    498       C  
ATOM   1852  NH1 ARG A 249       0.689  50.698  38.699  1.00 26.97           N  
ANISOU 1852  NH1 ARG A 249     3992   2220   4035     85    770    537       N  
ATOM   1853  NH2 ARG A 249       1.613  48.607  38.979  1.00 26.06           N  
ANISOU 1853  NH2 ARG A 249     3852   2083   3964     71    734    510       N  
ATOM   1854  N   HIS A 250       5.443  56.888  40.736  1.00 24.02           N  
ANISOU 1854  N   HIS A 250     4098   2176   2851    168   1049    311       N  
ATOM   1855  CA  HIS A 250       5.822  58.276  40.477  1.00 23.37           C  
ANISOU 1855  CA  HIS A 250     4070   2114   2693    164   1050    275       C  
ATOM   1856  C   HIS A 250       7.208  58.535  41.063  1.00 23.40           C  
ANISOU 1856  C   HIS A 250     4135   2146   2607    170   1057    221       C  
ATOM   1857  O   HIS A 250       7.996  59.192  40.472  1.00 21.52           O  
ANISOU 1857  O   HIS A 250     3928   1924   2324    144   1030    172       O  
ATOM   1858  CB  HIS A 250       4.790  59.258  41.041  1.00 23.89           C  
ANISOU 1858  CB  HIS A 250     4138   2165   2771    205   1104    332       C  
ATOM   1859  CG  HIS A 250       3.453  59.176  40.389  1.00 23.86           C  
ANISOU 1859  CG  HIS A 250     4068   2128   2867    195   1090    385       C  
ATOM   1860  ND1 HIS A 250       3.312  59.051  39.028  1.00 24.35           N  
ANISOU 1860  ND1 HIS A 250     4109   2182   2961    149   1013    355       N  
ATOM   1861  CD2 HIS A 250       2.208  59.244  40.909  1.00 24.00           C  
ANISOU 1861  CD2 HIS A 250     4039   2114   2963    232   1140    469       C  
ATOM   1862  CE1 HIS A 250       2.021  59.025  38.730  1.00 25.39           C  
ANISOU 1862  CE1 HIS A 250     4179   2274   3191    153   1002    412       C  
ATOM   1863  NE2 HIS A 250       1.315  59.131  39.884  1.00 24.79           N  
ANISOU 1863  NE2 HIS A 250     4079   2183   3156    200   1085    488       N  
ATOM   1864  N   GLN A 251       7.454  58.024  42.269  1.00 23.08           N  
ANISOU 1864  N   GLN A 251     4110   2107   2550    212   1095    237       N  
ATOM   1865  CA  GLN A 251       8.704  58.266  42.941  1.00 24.66           C  
ANISOU 1865  CA  GLN A 251     4368   2325   2674    225   1089    186       C  
ATOM   1866  C   GLN A 251       9.854  57.620  42.148  1.00 24.09           C  
ANISOU 1866  C   GLN A 251     4285   2268   2597    172   1038    130       C  
ATOM   1867  O   GLN A 251      10.887  58.263  41.894  1.00 23.48           O  
ANISOU 1867  O   GLN A 251     4238   2202   2481    152   1013     80       O  
ATOM   1868  CB  GLN A 251       8.639  57.748  44.366  1.00 25.26           C  
ANISOU 1868  CB  GLN A 251     4470   2396   2730    292   1137    217       C  
ATOM   1869  CG  GLN A 251       9.862  58.096  45.212  1.00 28.25           C  
ANISOU 1869  CG  GLN A 251     4920   2784   3028    320   1118    162       C  
ATOM   1870  CD  GLN A 251      10.138  56.988  46.198  1.00 33.05           C  
ANISOU 1870  CD  GLN A 251     5539   3393   3623    366   1140    178       C  
ATOM   1871  OE1 GLN A 251      10.343  55.842  45.804  1.00 36.28           O  
ANISOU 1871  OE1 GLN A 251     5900   3809   4076    331   1129    180       O  
ATOM   1872  NE2 GLN A 251      10.137  57.305  47.483  1.00 34.07           N  
ANISOU 1872  NE2 GLN A 251     5740   3515   3690    451   1172    189       N  
ATOM   1873  N   LEU A 252       9.690  56.347  41.767  1.00 24.12           N  
ANISOU 1873  N   LEU A 252     4244   2269   2649    154   1024    141       N  
ATOM   1874  CA  LEU A 252      10.747  55.683  41.010  1.00 24.94           C  
ANISOU 1874  CA  LEU A 252     4344   2386   2743    115    981     92       C  
ATOM   1875  C   LEU A 252      11.009  56.454  39.702  1.00 22.58           C  
ANISOU 1875  C   LEU A 252     4054   2094   2429     80    952     62       C  
ATOM   1876  O   LEU A 252      12.142  56.688  39.341  1.00 23.90           O  
ANISOU 1876  O   LEU A 252     4242   2275   2564     63    940     23       O  
ATOM   1877  CB  LEU A 252      10.384  54.214  40.776  1.00 25.29           C  
ANISOU 1877  CB  LEU A 252     4343   2419   2847    106    965    110       C  
ATOM   1878  CG  LEU A 252      10.441  53.341  42.037  1.00 26.69           C  
ANISOU 1878  CG  LEU A 252     4513   2592   3033    142   1000    138       C  
ATOM   1879  CD1 LEU A 252       9.747  52.026  41.817  1.00 25.44           C  
ANISOU 1879  CD1 LEU A 252     4296   2408   2961    135    988    174       C  
ATOM   1880  CD2 LEU A 252      11.888  53.093  42.449  1.00 27.79           C  
ANISOU 1880  CD2 LEU A 252     4688   2754   3115    141    990     88       C  
ATOM   1881  N   ALA A 253       9.940  56.811  38.991  1.00 22.23           N  
ANISOU 1881  N   ALA A 253     3993   2037   2416     75    942     87       N  
ATOM   1882  CA  ALA A 253      10.025  57.462  37.715  1.00 22.92           C  
ANISOU 1882  CA  ALA A 253     4095   2127   2486     55    916     67       C  
ATOM   1883  C   ALA A 253      10.767  58.801  37.856  1.00 22.91           C  
ANISOU 1883  C   ALA A 253     4128   2137   2438     53    940     49       C  
ATOM   1884  O   ALA A 253      11.644  59.112  37.037  1.00 24.14           O  
ANISOU 1884  O   ALA A 253     4300   2302   2569     38    932     23       O  
ATOM   1885  CB  ALA A 253       8.640  57.618  37.115  1.00 23.41           C  
ANISOU 1885  CB  ALA A 253     4132   2166   2595     57    896    100       C  
ATOM   1886  N   GLY A 254      10.457  59.551  38.916  1.00 22.27           N  
ANISOU 1886  N   GLY A 254     4060   2050   2349     76    969     65       N  
ATOM   1887  CA  GLY A 254      11.079  60.810  39.195  1.00 23.24           C  
ANISOU 1887  CA  GLY A 254     4215   2171   2441     78    978     46       C  
ATOM   1888  C   GLY A 254      12.551  60.656  39.509  1.00 22.49           C  
ANISOU 1888  C   GLY A 254     4132   2080   2331     68    965      7       C  
ATOM   1889  O   GLY A 254      13.369  61.424  39.053  1.00 21.61           O  
ANISOU 1889  O   GLY A 254     4026   1964   2219     50    958    -11       O  
ATOM   1890  N   LYS A 255      12.901  59.618  40.258  1.00 23.69           N  
ANISOU 1890  N   LYS A 255     4281   2238   2482     80    961      0       N  
ATOM   1891  CA  LYS A 255      14.318  59.368  40.603  1.00 25.28           C  
ANISOU 1891  CA  LYS A 255     4487   2439   2677     71    941    -37       C  
ATOM   1892  C   LYS A 255      15.080  58.906  39.360  1.00 24.51           C  
ANISOU 1892  C   LYS A 255     4365   2353   2594     36    935    -48       C  
ATOM   1893  O   LYS A 255      16.246  59.232  39.202  1.00 23.77           O  
ANISOU 1893  O   LYS A 255     4266   2252   2512     21    927    -68       O  
ATOM   1894  CB  LYS A 255      14.458  58.332  41.722  1.00 27.24           C  
ANISOU 1894  CB  LYS A 255     4743   2691   2916     99    940    -39       C  
ATOM   1895  CG  LYS A 255      13.937  58.795  43.074  1.00 29.42           C  
ANISOU 1895  CG  LYS A 255     5061   2954   3162    155    953    -28       C  
ATOM   1896  CD  LYS A 255      14.716  59.947  43.656  1.00 34.34           C  
ANISOU 1896  CD  LYS A 255     5726   3554   3765    168    920    -65       C  
ATOM   1897  CE  LYS A 255      14.235  60.374  45.030  1.00 36.14           C  
ANISOU 1897  CE  LYS A 255     6018   3765   3945    242    927    -60       C  
ATOM   1898  NZ  LYS A 255      14.700  61.742  45.333  1.00 38.10           N  
ANISOU 1898  NZ  LYS A 255     6309   3982   4183    253    885    -96       N  
ATOM   1899  N   TYR A 256      14.414  58.147  38.482  1.00 25.08           N  
ANISOU 1899  N   TYR A 256     4422   2435   2670     30    935    -34       N  
ATOM   1900  CA  TYR A 256      15.072  57.734  37.228  1.00 23.74           C  
ANISOU 1900  CA  TYR A 256     4248   2274   2498     15    931    -44       C  
ATOM   1901  C   TYR A 256      15.316  58.973  36.337  1.00 23.04           C  
ANISOU 1901  C   TYR A 256     4170   2179   2402     10    948    -37       C  
ATOM   1902  O   TYR A 256      16.401  59.111  35.754  1.00 23.46           O  
ANISOU 1902  O   TYR A 256     4220   2233   2460      4    964    -41       O  
ATOM   1903  CB  TYR A 256      14.333  56.614  36.485  1.00 23.04           C  
ANISOU 1903  CB  TYR A 256     4154   2187   2411     20    909    -39       C  
ATOM   1904  CG  TYR A 256      15.126  56.266  35.256  1.00 24.61           C  
ANISOU 1904  CG  TYR A 256     4367   2392   2588     22    908    -53       C  
ATOM   1905  CD1 TYR A 256      16.264  55.468  35.329  1.00 25.61           C  
ANISOU 1905  CD1 TYR A 256     4490   2528   2713     21    914    -70       C  
ATOM   1906  CD2 TYR A 256      14.837  56.889  34.050  1.00 25.52           C  
ANISOU 1906  CD2 TYR A 256     4509   2506   2680     34    910    -46       C  
ATOM   1907  CE1 TYR A 256      17.060  55.249  34.209  1.00 26.92           C  
ANISOU 1907  CE1 TYR A 256     4674   2698   2855     35    928    -74       C  
ATOM   1908  CE2 TYR A 256      15.613  56.666  32.927  1.00 26.50           C  
ANISOU 1908  CE2 TYR A 256     4660   2635   2773     54    923    -51       C  
ATOM   1909  CZ  TYR A 256      16.725  55.847  33.004  1.00 26.01           C  
ANISOU 1909  CZ  TYR A 256     4591   2580   2710     57    936    -63       C  
ATOM   1910  OH  TYR A 256      17.487  55.695  31.876  1.00 29.23           O  
ANISOU 1910  OH  TYR A 256     5030   2991   3083     88    962    -59       O  
ATOM   1911  N   THR A 257      14.304  59.857  36.202  1.00 24.02           N  
ANISOU 1911  N   THR A 257     4304   2297   2523     15    951    -19       N  
ATOM   1912  CA  THR A 257      14.492  61.176  35.506  1.00 23.65           C  
ANISOU 1912  CA  THR A 257     4267   2242   2475     11    972     -8       C  
ATOM   1913  C   THR A 257      15.732  61.905  36.039  1.00 22.50           C  
ANISOU 1913  C   THR A 257     4110   2080   2357      0    982    -17       C  
ATOM   1914  O   THR A 257      16.567  62.449  35.272  1.00 22.19           O  
ANISOU 1914  O   THR A 257     4063   2032   2337     -5   1006     -6       O  
ATOM   1915  CB  THR A 257      13.254  62.072  35.630  1.00 22.06           C  
ANISOU 1915  CB  THR A 257     4075   2033   2271     19    972     11       C  
ATOM   1916  OG1 THR A 257      12.131  61.426  35.029  1.00 23.23           O  
ANISOU 1916  OG1 THR A 257     4225   2186   2415     28    953     23       O  
ATOM   1917  CG2 THR A 257      13.431  63.419  34.963  1.00 23.82           C  
ANISOU 1917  CG2 THR A 257     4309   2245   2496     16    994     24       C  
ATOM   1918  N   THR A 258      15.847  61.979  37.360  1.00 23.21           N  
ANISOU 1918  N   THR A 258     4201   2158   2456      1    962    -35       N  
ATOM   1919  CA  THR A 258      17.006  62.639  37.956  1.00 23.87           C  
ANISOU 1919  CA  THR A 258     4275   2214   2580     -7    947    -52       C  
ATOM   1920  C   THR A 258      18.289  61.992  37.455  1.00 24.02           C  
ANISOU 1920  C   THR A 258     4263   2234   2629    -22    955    -54       C  
ATOM   1921  O   THR A 258      19.210  62.700  37.082  1.00 23.49           O  
ANISOU 1921  O   THR A 258     4171   2141   2614    -35    965    -43       O  
ATOM   1922  CB  THR A 258      16.972  62.633  39.488  1.00 26.34           C  
ANISOU 1922  CB  THR A 258     4611   2512   2884     11    910    -79       C  
ATOM   1923  OG1 THR A 258      15.857  63.428  39.894  1.00 24.81           O  
ANISOU 1923  OG1 THR A 258     4449   2313   2665     34    915    -69       O  
ATOM   1924  CG2 THR A 258      18.241  63.178  40.110  1.00 26.26           C  
ANISOU 1924  CG2 THR A 258     4591   2463   2923      4    870   -106       C  
ATOM   1925  N   ARG A 259      18.345  60.644  37.466  1.00 24.10           N  
ANISOU 1925  N   ARG A 259     4272   2268   2616    -17    952    -62       N  
ATOM   1926  CA  ARG A 259      19.528  59.928  37.018  1.00 23.23           C  
ANISOU 1926  CA  ARG A 259     4135   2159   2529    -24    964    -62       C  
ATOM   1927  C   ARG A 259      19.791  60.226  35.539  1.00 22.78           C  
ANISOU 1927  C   ARG A 259     4074   2105   2473    -19   1013    -30       C  
ATOM   1928  O   ARG A 259      20.930  60.405  35.165  1.00 22.71           O  
ANISOU 1928  O   ARG A 259     4035   2081   2512    -23   1039    -12       O  
ATOM   1929  CB  ARG A 259      19.416  58.421  37.270  1.00 24.62           C  
ANISOU 1929  CB  ARG A 259     4316   2360   2676    -16    952    -78       C  
ATOM   1930  CG  ARG A 259      20.548  57.601  36.656  1.00 26.17           C  
ANISOU 1930  CG  ARG A 259     4492   2562   2889    -17    971    -75       C  
ATOM   1931  CD  ARG A 259      20.181  56.987  35.321  1.00 30.44           C  
ANISOU 1931  CD  ARG A 259     5054   3122   3388      1    998    -60       C  
ATOM   1932  NE  ARG A 259      21.384  56.622  34.579  1.00 32.80           N  
ANISOU 1932  NE  ARG A 259     5339   3420   3703     13   1035    -45       N  
ATOM   1933  CZ  ARG A 259      21.519  56.674  33.268  1.00 33.86           C  
ANISOU 1933  CZ  ARG A 259     5497   3558   3809     43   1079    -20       C  
ATOM   1934  NH1 ARG A 259      22.703  56.399  32.756  1.00 37.59           N  
ANISOU 1934  NH1 ARG A 259     5952   4024   4304     60   1125      3       N  
ATOM   1935  NH2 ARG A 259      20.493  56.977  32.479  1.00 32.40           N  
ANISOU 1935  NH2 ARG A 259     5354   3381   3574     63   1077    -14       N  
ATOM   1936  N   LEU A 260      18.737  60.223  34.717  1.00 21.41           N  
ANISOU 1936  N   LEU A 260     3933   1951   2251     -3   1024    -19       N  
ATOM   1937  CA  LEU A 260      18.839  60.492  33.282  1.00 22.29           C  
ANISOU 1937  CA  LEU A 260     4061   2066   2342     19   1067     10       C  
ATOM   1938  C   LEU A 260      19.430  61.889  33.011  1.00 25.45           C  
ANISOU 1938  C   LEU A 260     4438   2437   2791     13   1106     43       C  
ATOM   1939  O   LEU A 260      20.285  62.056  32.129  1.00 25.64           O  
ANISOU 1939  O   LEU A 260     4453   2453   2835     32   1160     79       O  
ATOM   1940  CB  LEU A 260      17.452  60.311  32.665  1.00 22.42           C  
ANISOU 1940  CB  LEU A 260     4119   2097   2300     38   1047      8       C  
ATOM   1941  CG  LEU A 260      17.340  60.567  31.171  1.00 24.98           C  
ANISOU 1941  CG  LEU A 260     4484   2426   2582     78   1079     32       C  
ATOM   1942  CD1 LEU A 260      18.114  59.499  30.382  1.00 27.00           C  
ANISOU 1942  CD1 LEU A 260     4761   2691   2806    113   1098     32       C  
ATOM   1943  CD2 LEU A 260      15.868  60.578  30.767  1.00 24.00           C  
ANISOU 1943  CD2 LEU A 260     4394   2306   2418     92   1037     24       C  
ATOM   1944  N   LEU A 261      19.047  62.890  33.805  1.00 25.49           N  
ANISOU 1944  N   LEU A 261     4435   2423   2826     -7   1081     36       N  
ATOM   1945  CA  LEU A 261      19.553  64.251  33.614  1.00 28.16           C  
ANISOU 1945  CA  LEU A 261     4747   2725   3226    -16   1108     65       C  
ATOM   1946  C   LEU A 261      21.006  64.339  34.084  1.00 29.10           C  
ANISOU 1946  C   LEU A 261     4810   2807   3438    -35   1106     71       C  
ATOM   1947  O   LEU A 261      21.764  65.127  33.534  1.00 28.75           O  
ANISOU 1947  O   LEU A 261     4728   2729   3465    -37   1148    114       O  
ATOM   1948  CB  LEU A 261      18.667  65.264  34.360  1.00 26.20           C  
ANISOU 1948  CB  LEU A 261     4512   2461   2978    -27   1073     50       C  
ATOM   1949  CG  LEU A 261      17.264  65.443  33.769  1.00 27.57           C  
ANISOU 1949  CG  LEU A 261     4729   2661   3085     -9   1081     59       C  
ATOM   1950  CD1 LEU A 261      16.402  66.345  34.630  1.00 29.81           C  
ANISOU 1950  CD1 LEU A 261     5025   2930   3370    -15   1051     46       C  
ATOM   1951  CD2 LEU A 261      17.296  65.978  32.348  1.00 27.73           C  
ANISOU 1951  CD2 LEU A 261     4759   2682   3092     12   1135    102       C  
ATOM   1952  N   ARG A 262      21.392  63.562  35.099  1.00 27.17           N  
ANISOU 1952  N   ARG A 262     4555   2563   3204    -48   1057     32       N  
ATOM   1953  CA  ARG A 262      22.760  63.668  35.643  1.00 28.54           C  
ANISOU 1953  CA  ARG A 262     4672   2693   3478    -67   1037     32       C  
ATOM   1954  C   ARG A 262      23.748  62.870  34.782  1.00 30.07           C  
ANISOU 1954  C   ARG A 262     4834   2895   3696    -55   1096     69       C  
ATOM   1955  O   ARG A 262      24.877  63.276  34.670  1.00 32.73           O  
ANISOU 1955  O   ARG A 262     5109   3187   4137    -65   1114    102       O  
ATOM   1956  CB  ARG A 262      22.876  63.146  37.082  1.00 31.94           C  
ANISOU 1956  CB  ARG A 262     5111   3117   3908    -76    958    -22       C  
ATOM   1957  CG  ARG A 262      22.293  64.019  38.178  1.00 35.18           C  
ANISOU 1957  CG  ARG A 262     5551   3500   4313    -75    894    -59       C  
ATOM   1958  CD  ARG A 262      22.492  63.354  39.543  1.00 37.82           C  
ANISOU 1958  CD  ARG A 262     5907   3830   4630    -64    824   -110       C  
ATOM   1959  NE  ARG A 262      21.963  64.140  40.659  1.00 42.94           N  
ANISOU 1959  NE  ARG A 262     6603   4450   5259    -45    762   -146       N  
ATOM   1960  CZ  ARG A 262      21.402  63.642  41.780  1.00 47.62           C  
ANISOU 1960  CZ  ARG A 262     7254   5058   5780     -9    726   -181       C  
ATOM   1961  NH1 ARG A 262      21.326  62.336  41.977  1.00 45.23           N  
ANISOU 1961  NH1 ARG A 262     6958   4795   5430      1    741   -184       N  
ATOM   1962  NH2 ARG A 262      20.924  64.454  42.713  1.00 43.37           N  
ANISOU 1962  NH2 ARG A 262     6770   4491   5217     21    678   -209       N  
ATOM   1963  N   HIS A 263      23.333  61.723  34.220  1.00 29.20           N  
ANISOU 1963  N   HIS A 263     4762   2833   3497    -31   1120     64       N  
ATOM   1964  CA  HIS A 263      24.267  60.727  33.576  1.00 32.79           C  
ANISOU 1964  CA  HIS A 263     5201   3299   3959    -10   1168     88       C  
ATOM   1965  C   HIS A 263      23.774  60.207  32.213  1.00 32.14           C  
ANISOU 1965  C   HIS A 263     5174   3252   3784     38   1226    112       C  
ATOM   1966  O   HIS A 263      24.412  59.329  31.605  1.00 32.23           O  
ANISOU 1966  O   HIS A 263     5191   3275   3778     70   1267    129       O  
ATOM   1967  CB  HIS A 263      24.568  59.565  34.547  1.00 33.37           C  
ANISOU 1967  CB  HIS A 263     5268   3385   4025    -23   1114     43       C  
ATOM   1968  CG  HIS A 263      25.397  60.018  35.706  1.00 40.43           C  
ANISOU 1968  CG  HIS A 263     6109   4233   5017    -55   1059     25       C  
ATOM   1969  ND1 HIS A 263      26.592  60.693  35.542  1.00 47.30           N  
ANISOU 1969  ND1 HIS A 263     6909   5051   6010    -67   1079     65       N  
ATOM   1970  CD2 HIS A 263      25.157  60.023  37.032  1.00 48.33           C  
ANISOU 1970  CD2 HIS A 263     7122   5225   6017    -71    978    -25       C  
ATOM   1971  CE1 HIS A 263      27.071  61.037  36.725  1.00 48.38           C  
ANISOU 1971  CE1 HIS A 263     7015   5145   6220    -93    997     31       C  
ATOM   1972  NE2 HIS A 263      26.208  60.638  37.653  1.00 43.74           N  
ANISOU 1972  NE2 HIS A 263     6485   4585   5548    -90    936    -26       N  
ATOM   1973  N   GLY A 264      22.681  60.758  31.688  1.00 30.81           N  
ANISOU 1973  N   GLY A 264     5053   3098   3555     53   1228    114       N  
ATOM   1974  CA  GLY A 264      22.158  60.304  30.390  1.00 31.43           C  
ANISOU 1974  CA  GLY A 264     5197   3202   3541    108   1264    128       C  
ATOM   1975  C   GLY A 264      23.157  60.528  29.277  1.00 31.17           C  
ANISOU 1975  C   GLY A 264     5161   3156   3524    158   1359    194       C  
ATOM   1976  O   GLY A 264      24.041  61.379  29.385  1.00 35.34           O  
ANISOU 1976  O   GLY A 264     5626   3649   4151    144   1405    241       O  
ATOM   1977  N   GLN A 265      22.991  59.772  28.192  1.00 31.65           N  
ANISOU 1977  N   GLN A 265     5293   3240   3493    225   1388    201       N  
ATOM   1978  CA  GLN A 265      23.752  59.956  26.979  1.00 34.48           C  
ANISOU 1978  CA  GLN A 265     5674   3589   3837    299   1492    270       C  
ATOM   1979  C   GLN A 265      23.508  61.374  26.427  1.00 33.88           C  
ANISOU 1979  C   GLN A 265     5597   3494   3780    314   1543    322       C  
ATOM   1980  O   GLN A 265      22.348  61.813  26.334  1.00 31.31           O  
ANISOU 1980  O   GLN A 265     5315   3179   3399    309   1496    294       O  
ATOM   1981  CB  GLN A 265      23.316  58.882  25.989  1.00 38.77           C  
ANISOU 1981  CB  GLN A 265     6321   4159   4251    377   1485    248       C  
ATOM   1982  CG  GLN A 265      24.124  58.875  24.709  1.00 51.81           C  
ANISOU 1982  CG  GLN A 265     8018   5803   5861    478   1598    319       C  
ATOM   1983  CD  GLN A 265      23.986  57.571  23.959  1.00 56.88           C  
ANISOU 1983  CD  GLN A 265     8761   6464   6385    557   1580    286       C  
ATOM   1984  OE1 GLN A 265      23.758  56.514  24.550  1.00 67.57           O  
ANISOU 1984  OE1 GLN A 265    10114   7830   7727    523   1499    222       O  
ATOM   1985  NE2 GLN A 265      24.114  57.648  22.642  1.00 64.73           N  
ANISOU 1985  NE2 GLN A 265     9847   7457   7287    672   1653    331       N  
ATOM   1986  N   LYS A 266      24.602  62.055  26.061  1.00 33.55           N  
ANISOU 1986  N   LYS A 266     5502   3419   3825    334   1643    404       N  
ATOM   1987  CA  LYS A 266      24.611  63.378  25.436  1.00 35.03           C  
ANISOU 1987  CA  LYS A 266     5679   3580   4049    358   1716    474       C  
ATOM   1988  C   LYS A 266      23.848  64.360  26.329  1.00 34.95           C  
ANISOU 1988  C   LYS A 266     5632   3557   4089    280   1639    436       C  
ATOM   1989  O   LYS A 266      23.035  65.168  25.837  1.00 32.71           O  
ANISOU 1989  O   LYS A 266     5390   3277   3761    299   1646    447       O  
ATOM   1990  CB  LYS A 266      23.944  63.375  24.059  1.00 38.06           C  
ANISOU 1990  CB  LYS A 266     6178   3988   4294    459   1763    496       C  
ATOM   1991  CG  LYS A 266      24.646  62.539  23.010  1.00 42.34           C  
ANISOU 1991  CG  LYS A 266     6783   4539   4765    564   1850    541       C  
ATOM   1992  CD  LYS A 266      24.050  62.636  21.622  1.00 44.20           C  
ANISOU 1992  CD  LYS A 266     7147   4790   4856    681   1895    566       C  
ATOM   1993  CE  LYS A 266      24.504  61.452  20.792  1.00 48.33           C  
ANISOU 1993  CE  LYS A 266     7759   5328   5274    787   1936    572       C  
ATOM   1994  NZ  LYS A 266      23.797  61.394  19.493  1.00 55.84           N  
ANISOU 1994  NZ  LYS A 266     8861   6293   6060    912   1946    572       N  
ATOM   1995  N   LYS A 267      24.091  64.279  27.636  1.00 32.61           N  
ANISOU 1995  N   LYS A 267     5267   3245   3876    200   1564    390       N  
ATOM   1996  CA  LYS A 267      23.295  65.050  28.577  1.00 35.10           C  
ANISOU 1996  CA  LYS A 267     5568   3551   4217    138   1483    343       C  
ATOM   1997  C   LYS A 267      23.479  66.555  28.312  1.00 36.46           C  
ANISOU 1997  C   LYS A 267     5699   3678   4476    133   1531    403       C  
ATOM   1998  O   LYS A 267      22.531  67.311  28.524  1.00 33.97           O  
ANISOU 1998  O   LYS A 267     5407   3364   4136    114   1492    380       O  
ATOM   1999  CB  LYS A 267      23.619  64.687  30.026  1.00 35.00           C  
ANISOU 1999  CB  LYS A 267     5503   3525   4269     73   1398    286       C  
ATOM   2000  CG  LYS A 267      24.989  65.101  30.538  1.00 39.63           C  
ANISOU 2000  CG  LYS A 267     5993   4053   5011     42   1409    320       C  
ATOM   2001  CD  LYS A 267      24.888  65.676  31.948  1.00 45.57           C  
ANISOU 2001  CD  LYS A 267     6710   4771   5833    -18   1307    265       C  
ATOM   2002  CE  LYS A 267      26.199  65.746  32.692  1.00 49.94           C  
ANISOU 2002  CE  LYS A 267     7175   5264   6534    -51   1275    272       C  
ATOM   2003  NZ  LYS A 267      26.679  64.387  33.027  1.00 52.94           N  
ANISOU 2003  NZ  LYS A 267     7556   5672   6886    -48   1258    244       N  
ATOM   2004  N   ASN A 268      24.675  66.952  27.834  1.00 37.77           N  
ANISOU 2004  N   ASN A 268     5801   3800   4749    152   1619    484       N  
ATOM   2005  CA  ASN A 268      25.018  68.354  27.533  1.00 35.57           C  
ANISOU 2005  CA  ASN A 268     5466   3465   4581    149   1675    557       C  
ATOM   2006  C   ASN A 268      24.967  68.608  26.020  1.00 32.41           C  
ANISOU 2006  C   ASN A 268     5118   3078   4116    239   1800    642       C  
ATOM   2007  O   ASN A 268      25.688  69.440  25.519  1.00 30.24           O  
ANISOU 2007  O   ASN A 268     4786   2754   3949    261   1892    734       O  
ATOM   2008  CB  ASN A 268      26.366  68.740  28.147  1.00 38.46           C  
ANISOU 2008  CB  ASN A 268     5710   3757   5144    106   1679    597       C  
ATOM   2009  CG  ASN A 268      26.357  68.719  29.666  1.00 40.26           C  
ANISOU 2009  CG  ASN A 268     5901   3963   5431     27   1542    510       C  
ATOM   2010  OD1 ASN A 268      25.383  69.128  30.279  1.00 45.35           O  
ANISOU 2010  OD1 ASN A 268     6480   4575   6176      0   1512    505       O  
ATOM   2011  ND2 ASN A 268      27.430  68.266  30.293  1.00 40.02           N  
ANISOU 2011  ND2 ASN A 268     5918   3947   5337      0   1460    442       N  
ATOM   2012  N   PHE A 269      24.018  67.980  25.316  1.00 28.95           N  
ANISOU 2012  N   PHE A 269     4792   2699   3505    296   1796    610       N  
ATOM   2013  CA  PHE A 269      23.889  68.165  23.853  1.00 29.20           C  
ANISOU 2013  CA  PHE A 269     4900   2745   3449    400   1904    681       C  
ATOM   2014  C   PHE A 269      23.604  69.633  23.489  1.00 29.16           C  
ANISOU 2014  C   PHE A 269     4877   2706   3494    405   1951    739       C  
ATOM   2015  O   PHE A 269      24.086  70.119  22.447  1.00 28.31           O  
ANISOU 2015  O   PHE A 269     4779   2579   3397    483   2076    839       O  
ATOM   2016  CB  PHE A 269      22.796  67.270  23.260  1.00 29.12           C  
ANISOU 2016  CB  PHE A 269     5019   2795   3249    456   1854    618       C  
ATOM   2017  CG  PHE A 269      21.391  67.715  23.560  1.00 28.79           C  
ANISOU 2017  CG  PHE A 269     5019   2773   3147    420   1759    554       C  
ATOM   2018  CD1 PHE A 269      20.831  67.516  24.812  1.00 27.79           C  
ANISOU 2018  CD1 PHE A 269     4856   2653   3048    330   1646    472       C  
ATOM   2019  CD2 PHE A 269      20.637  68.367  22.591  1.00 31.32           C  
ANISOU 2019  CD2 PHE A 269     5413   3101   3386    483   1790    582       C  
ATOM   2020  CE1 PHE A 269      19.547  67.954  25.094  1.00 28.91           C  
ANISOU 2020  CE1 PHE A 269     5029   2809   3146    303   1573    426       C  
ATOM   2021  CE2 PHE A 269      19.350  68.804  22.880  1.00 30.15           C  
ANISOU 2021  CE2 PHE A 269     5293   2965   3195    449   1704    528       C  
ATOM   2022  CZ  PHE A 269      18.808  68.608  24.128  1.00 30.22           C  
ANISOU 2022  CZ  PHE A 269     5259   2981   3242    359   1600    454       C  
ATOM   2023  N   ALA A 270      22.847  70.342  24.335  1.00 28.00           N  
ANISOU 2023  N   ALA A 270     4707   2550   3378    329   1859    684       N  
ATOM   2024  CA  ALA A 270      22.252  71.647  23.967  1.00 28.38           C  
ANISOU 2024  CA  ALA A 270     4764   2579   3439    336   1884    720       C  
ATOM   2025  C   ALA A 270      23.325  72.673  23.567  1.00 27.60           C  
ANISOU 2025  C   ALA A 270     4578   2411   3494    351   1998    835       C  
ATOM   2026  O   ALA A 270      23.142  73.388  22.589  1.00 27.91           O  
ANISOU 2026  O   ALA A 270     4651   2443   3507    416   2088    908       O  
ATOM   2027  CB  ALA A 270      21.371  72.166  25.098  1.00 26.80           C  
ANISOU 2027  CB  ALA A 270     4548   2375   3259    252   1765    639       C  
ATOM   2028  N   ASN A 271      24.424  72.764  24.333  1.00 28.37           N  
ANISOU 2028  N   ASN A 271     4561   2453   3763    293   1991    854       N  
ATOM   2029  CA  ASN A 271      25.460  73.737  24.056  1.00 32.04           C  
ANISOU 2029  CA  ASN A 271     4921   2837   4412    297   2087    967       C  
ATOM   2030  C   ASN A 271      26.637  73.081  23.302  1.00 34.07           C  
ANISOU 2030  C   ASN A 271     5149   3084   4710    367   2216   1063       C  
ATOM   2031  O   ASN A 271      27.667  73.698  23.130  1.00 35.10           O  
ANISOU 2031  O   ASN A 271     5173   3141   5021    370   2302   1168       O  
ATOM   2032  CB  ASN A 271      25.916  74.430  25.343  1.00 33.24           C  
ANISOU 2032  CB  ASN A 271     4959   2916   4753    192   1988    934       C  
ATOM   2033  CG  ASN A 271      24.866  75.371  25.903  1.00 31.75           C  
ANISOU 2033  CG  ASN A 271     4798   2722   4543    145   1897    871       C  
ATOM   2034  OD1 ASN A 271      24.475  76.342  25.251  1.00 32.21           O  
ANISOU 2034  OD1 ASN A 271     4870   2765   4604    174   1957    926       O  
ATOM   2035  ND2 ASN A 271      24.399  75.090  27.104  1.00 28.90           N  
ANISOU 2035  ND2 ASN A 271     4450   2374   4157     80   1758    759       N  
ATOM   2036  N   SER A 272      26.470  71.849  22.812  1.00 35.56           N  
ANISOU 2036  N   SER A 272     5432   3340   4739    429   2233   1034       N  
ATOM   2037  CA  SER A 272      27.571  71.086  22.169  1.00 35.66           C  
ANISOU 2037  CA  SER A 272     5428   3346   4774    503   2350   1117       C  
ATOM   2038  C   SER A 272      27.798  71.568  20.731  1.00 37.57           C  
ANISOU 2038  C   SER A 272     5715   3579   4980    630   2526   1249       C  
ATOM   2039  O   SER A 272      27.112  72.476  20.220  1.00 37.11           O  
ANISOU 2039  O   SER A 272     5701   3520   4879    658   2553   1275       O  
ATOM   2040  CB  SER A 272      27.273  69.600  22.188  1.00 35.23           C  
ANISOU 2040  CB  SER A 272     5466   3362   4555    528   2295   1032       C  
ATOM   2041  OG  SER A 272      26.288  69.286  21.209  1.00 35.57           O  
ANISOU 2041  OG  SER A 272     5659   3465   4388    620   2311   1011       O  
ATOM   2042  N   LYS A 273      28.771  70.933  20.072  1.00 39.49           N  
ANISOU 2042  N   LYS A 273     5953   3815   5236    715   2652   1337       N  
ATOM   2043  CA  LYS A 273      29.120  71.226  18.709  1.00 41.20           C  
ANISOU 2043  CA  LYS A 273     6221   4022   5410    857   2837   1474       C  
ATOM   2044  C   LYS A 273      28.229  70.431  17.735  1.00 41.01           C  
ANISOU 2044  C   LYS A 273     6396   4079   5106    978   2841   1425       C  
ATOM   2045  O   LYS A 273      28.477  70.476  16.528  1.00 40.34           O  
ANISOU 2045  O   LYS A 273     6392   3995   4939   1125   2991   1528       O  
ATOM   2046  CB  LYS A 273      30.620  70.972  18.505  1.00 44.13           C  
ANISOU 2046  CB  LYS A 273     6485   4338   5943    898   2977   1602       C  
ATOM   2047  CG  LYS A 273      31.518  72.145  18.882  1.00 44.99           C  
ANISOU 2047  CG  LYS A 273     6408   4344   6343    835   3036   1714       C  
ATOM   2048  N   MET A 274      27.218  69.707  18.244  1.00 38.00           N  
ANISOU 2048  N   MET A 274     6096   3757   4585    926   2676   1274       N  
ATOM   2049  CA  MET A 274      26.211  69.023  17.399  1.00 38.33           C  
ANISOU 2049  CA  MET A 274     6322   3863   4378   1026   2640   1211       C  
ATOM   2050  C   MET A 274      25.591  70.012  16.406  1.00 38.47           C  
ANISOU 2050  C   MET A 274     6422   3878   4315   1116   2710   1272       C  
ATOM   2051  O   MET A 274      25.305  71.121  16.753  1.00 37.21           O  
ANISOU 2051  O   MET A 274     6192   3690   4254   1049   2697   1288       O  
ATOM   2052  CB  MET A 274      25.071  68.449  18.248  1.00 38.53           C  
ANISOU 2052  CB  MET A 274     6383   3932   4321    929   2442   1050       C  
ATOM   2053  CG  MET A 274      25.140  66.977  18.491  1.00 42.06           C  
ANISOU 2053  CG  MET A 274     6877   4416   4686    932   2370    970       C  
ATOM   2054  SD  MET A 274      23.934  66.445  19.751  1.00 42.06           S  
ANISOU 2054  SD  MET A 274     6872   4451   4656    796   2152    804       S  
ATOM   2055  CE  MET A 274      22.429  66.523  18.774  1.00 38.91           C  
ANISOU 2055  CE  MET A 274     6635   4087   4059    880   2091    756       C  
ATOM   2056  N   LYS A 275      25.353  69.554  15.174  1.00 40.00           N  
ANISOU 2056  N   LYS A 275     6775   4101   4319   1276   2775   1297       N  
ATOM   2057  CA  LYS A 275      24.577  70.272  14.148  1.00 41.29           C  
ANISOU 2057  CA  LYS A 275     7059   4274   4355   1383   2816   1331       C  
ATOM   2058  C   LYS A 275      23.168  70.599  14.674  1.00 38.41           C  
ANISOU 2058  C   LYS A 275     6718   3934   3939   1288   2640   1208       C  
ATOM   2059  O   LYS A 275      22.565  69.795  15.401  1.00 35.71           O  
ANISOU 2059  O   LYS A 275     6384   3624   3560   1205   2484   1082       O  
ATOM   2060  CB  LYS A 275      24.510  69.381  12.905  1.00 47.12           C  
ANISOU 2060  CB  LYS A 275     7987   5043   4871   1570   2866   1340       C  
ATOM   2061  CG  LYS A 275      23.508  69.774  11.832  1.00 52.12           C  
ANISOU 2061  CG  LYS A 275     8790   5696   5317   1695   2856   1333       C  
ATOM   2062  CD  LYS A 275      23.586  68.862  10.603  1.00 59.75           C  
ANISOU 2062  CD  LYS A 275     9955   6681   6064   1899   2906   1344       C  
ATOM   2063  CE  LYS A 275      23.033  69.493   9.336  1.00 66.60           C  
ANISOU 2063  CE  LYS A 275    10984   7549   6769   2069   2969   1398       C  
ATOM   2064  NZ  LYS A 275      21.670  70.052   9.538  1.00 68.10           N  
ANISOU 2064  NZ  LYS A 275    11200   7754   6919   1996   2812   1302       N  
ATOM   2065  N   TYR A 276      22.621  71.742  14.235  1.00 37.48           N  
ANISOU 2065  N   TYR A 276     6620   3804   3813   1313   2674   1253       N  
ATOM   2066  CA  TYR A 276      21.365  72.280  14.760  1.00 37.02           C  
ANISOU 2066  CA  TYR A 276     6563   3761   3741   1221   2531   1161       C  
ATOM   2067  C   TYR A 276      20.228  71.267  14.578  1.00 37.03           C  
ANISOU 2067  C   TYR A 276     6699   3811   3559   1247   2376   1032       C  
ATOM   2068  O   TYR A 276      19.516  70.964  15.548  1.00 35.36           O  
ANISOU 2068  O   TYR A 276     6443   3615   3376   1127   2227    925       O  
ATOM   2069  CB  TYR A 276      20.983  73.607  14.099  1.00 35.43           C  
ANISOU 2069  CB  TYR A 276     6383   3538   3537   1273   2608   1240       C  
ATOM   2070  CG  TYR A 276      19.594  74.094  14.441  1.00 33.49           C  
ANISOU 2070  CG  TYR A 276     6165   3312   3247   1206   2466   1148       C  
ATOM   2071  CD1 TYR A 276      19.306  74.670  15.673  1.00 32.82           C  
ANISOU 2071  CD1 TYR A 276     5954   3210   3303   1048   2380   1098       C  
ATOM   2072  CD2 TYR A 276      18.564  74.010  13.510  1.00 34.20           C  
ANISOU 2072  CD2 TYR A 276     6411   3430   3153   1310   2418   1114       C  
ATOM   2073  CE1 TYR A 276      18.031  75.122  15.979  1.00 31.48           C  
ANISOU 2073  CE1 TYR A 276     5809   3057   3094    994   2263   1023       C  
ATOM   2074  CE2 TYR A 276      17.284  74.466  13.795  1.00 33.62           C  
ANISOU 2074  CE2 TYR A 276     6354   3370   3050   1251   2292   1038       C  
ATOM   2075  CZ  TYR A 276      17.020  75.028  15.034  1.00 32.22           C  
ANISOU 2075  CZ  TYR A 276     6044   3179   3017   1093   2222    997       C  
ATOM   2076  OH  TYR A 276      15.759  75.466  15.331  1.00 34.13           O  
ANISOU 2076  OH  TYR A 276     6301   3433   3233   1041   2108    930       O  
ATOM   2077  N   GLU A 277      20.059  70.770  13.347  1.00 39.37           N  
ANISOU 2077  N   GLU A 277     7158   4124   3675   1410   2409   1046       N  
ATOM   2078  CA  GLU A 277      18.967  69.858  13.034  1.00 41.56           C  
ANISOU 2078  CA  GLU A 277     7571   4434   3786   1450   2252    928       C  
ATOM   2079  C   GLU A 277      19.082  68.596  13.902  1.00 37.32           C  
ANISOU 2079  C   GLU A 277     6989   3911   3276   1363   2144    832       C  
ATOM   2080  O   GLU A 277      18.066  68.027  14.277  1.00 37.48           O  
ANISOU 2080  O   GLU A 277     7037   3948   3252   1309   1980    721       O  
ATOM   2081  CB  GLU A 277      18.927  69.493  11.553  1.00 45.44           C  
ANISOU 2081  CB  GLU A 277     8255   4930   4078   1657   2305    959       C  
ATOM   2082  CG  GLU A 277      17.564  68.979  11.107  1.00 49.67           C  
ANISOU 2082  CG  GLU A 277     8933   5482   4457   1703   2125    843       C  
ATOM   2083  N   ASP A 278      20.308  68.186  14.253  1.00 37.10           N  
ANISOU 2083  N   ASP A 278     6883   3875   3337   1345   2236    881       N  
ATOM   2084  CA  ASP A 278      20.489  66.994  15.122  1.00 36.62           C  
ANISOU 2084  CA  ASP A 278     6775   3829   3310   1261   2140    796       C  
ATOM   2085  C   ASP A 278      20.012  67.305  16.541  1.00 33.32           C  
ANISOU 2085  C   ASP A 278     6221   3410   3027   1081   2032    730       C  
ATOM   2086  O   ASP A 278      19.377  66.448  17.163  1.00 31.25           O  
ANISOU 2086  O   ASP A 278     5962   3166   2744   1017   1895    627       O  
ATOM   2087  CB  ASP A 278      21.922  66.460  15.160  1.00 36.96           C  
ANISOU 2087  CB  ASP A 278     6766   3859   3415   1289   2262    865       C  
ATOM   2088  CG  ASP A 278      22.347  65.857  13.831  1.00 43.24           C  
ANISOU 2088  CG  ASP A 278     7716   4660   4054   1480   2356    915       C  
ATOM   2089  OD1 ASP A 278      21.444  65.558  13.004  1.00 43.91           O  
ANISOU 2089  OD1 ASP A 278     7959   4758   3965   1580   2280    861       O  
ATOM   2090  OD2 ASP A 278      23.567  65.762  13.606  1.00 43.52           O  
ANISOU 2090  OD2 ASP A 278     7712   4677   4143   1535   2505   1013       O  
ATOM   2091  N   LYS A 279      20.348  68.497  17.054  1.00 32.46           N  
ANISOU 2091  N   LYS A 279     5997   3276   3060   1007   2096    791       N  
ATOM   2092  CA  LYS A 279      19.925  68.924  18.399  1.00 30.44           C  
ANISOU 2092  CA  LYS A 279     5625   3013   2926    852   2000    733       C  
ATOM   2093  C   LYS A 279      18.396  68.946  18.479  1.00 29.49           C  
ANISOU 2093  C   LYS A 279     5567   2916   2721    829   1864    646       C  
ATOM   2094  O   LYS A 279      17.829  68.525  19.454  1.00 28.75           O  
ANISOU 2094  O   LYS A 279     5430   2833   2659    735   1751    566       O  
ATOM   2095  CB  LYS A 279      20.478  70.312  18.733  1.00 32.76           C  
ANISOU 2095  CB  LYS A 279     5807   3265   3372    801   2087    816       C  
ATOM   2096  CG  LYS A 279      21.953  70.364  19.105  1.00 33.06           C  
ANISOU 2096  CG  LYS A 279     5732   3266   3563    775   2185    891       C  
ATOM   2097  CD  LYS A 279      22.464  71.771  19.299  1.00 33.94           C  
ANISOU 2097  CD  LYS A 279     5736   3321   3836    736   2263    978       C  
ATOM   2098  CE  LYS A 279      23.902  71.790  19.774  1.00 35.34           C  
ANISOU 2098  CE  LYS A 279     5784   3449   4194    698   2336   1047       C  
ATOM   2099  NZ  LYS A 279      24.363  73.166  20.058  1.00 37.05           N  
ANISOU 2099  NZ  LYS A 279     5884   3597   4595    648   2388   1124       N  
ATOM   2100  N   ILE A 280      17.745  69.474  17.440  1.00 30.98           N  
ANISOU 2100  N   ILE A 280     5854   3107   2808    921   1882    671       N  
ATOM   2101  CA  ILE A 280      16.290  69.567  17.367  1.00 30.21           C  
ANISOU 2101  CA  ILE A 280     5816   3023   2637    911   1757    600       C  
ATOM   2102  C   ILE A 280      15.672  68.165  17.412  1.00 29.52           C  
ANISOU 2102  C   ILE A 280     5793   2955   2468    918   1624    503       C  
ATOM   2103  O   ILE A 280      14.649  67.966  18.087  1.00 26.56           O  
ANISOU 2103  O   ILE A 280     5390   2585   2114    841   1500    430       O  
ATOM   2104  CB  ILE A 280      15.871  70.344  16.102  1.00 33.37           C  
ANISOU 2104  CB  ILE A 280     6322   3418   2937   1030   1809    654       C  
ATOM   2105  CG1 ILE A 280      16.205  71.830  16.237  1.00 34.25           C  
ANISOU 2105  CG1 ILE A 280     6354   3506   3154    998   1915    740       C  
ATOM   2106  CG2 ILE A 280      14.404  70.150  15.747  1.00 33.80           C  
ANISOU 2106  CG2 ILE A 280     6467   3483   2890   1053   1667    576       C  
ATOM   2107  CD1 ILE A 280      15.655  72.468  17.464  1.00 32.15           C  
ANISOU 2107  CD1 ILE A 280     5976   3232   3005    856   1842    699       C  
ATOM   2108  N   GLU A 281      16.247  67.232  16.636  1.00 31.41           N  
ANISOU 2108  N   GLU A 281     6119   3199   2613   1020   1653    507       N  
ATOM   2109  CA  GLU A 281      15.692  65.872  16.516  1.00 31.29           C  
ANISOU 2109  CA  GLU A 281     6180   3193   2516   1044   1523    416       C  
ATOM   2110  C   GLU A 281      15.903  65.117  17.834  1.00 29.35           C  
ANISOU 2110  C   GLU A 281     5821   2954   2375    918   1466    364       C  
ATOM   2111  O   GLU A 281      15.011  64.447  18.303  1.00 29.03           O  
ANISOU 2111  O   GLU A 281     5777   2915   2337    867   1334    286       O  
ATOM   2112  CB  GLU A 281      16.301  65.145  15.323  1.00 36.21           C  
ANISOU 2112  CB  GLU A 281     6937   3814   3004   1200   1575    437       C  
ATOM   2113  CG  GLU A 281      15.629  65.528  14.014  1.00 41.60           C  
ANISOU 2113  CG  GLU A 281     7772   4490   3543   1340   1560    446       C  
ATOM   2114  CD  GLU A 281      16.126  64.749  12.808  1.00 45.53           C  
ANISOU 2114  CD  GLU A 281     8431   4982   3883   1515   1595    457       C  
ATOM   2115  OE1 GLU A 281      16.154  65.339  11.725  1.00 53.54           O  
ANISOU 2115  OE1 GLU A 281     9558   5991   4792   1652   1670    514       O  
ATOM   2116  OE2 GLU A 281      16.473  63.545  12.972  1.00 49.13           O  
ANISOU 2116  OE2 GLU A 281     8906   5440   4319   1520   1549    407       O  
ATOM   2117  N   TRP A 282      17.063  65.296  18.455  1.00 27.66           N  
ANISOU 2117  N   TRP A 282     5510   2738   2258    868   1566    414       N  
ATOM   2118  CA  TRP A 282      17.359  64.736  19.735  1.00 26.62           C  
ANISOU 2118  CA  TRP A 282     5273   2611   2227    754   1523    374       C  
ATOM   2119  C   TRP A 282      16.366  65.204  20.815  1.00 26.70           C  
ANISOU 2119  C   TRP A 282     5210   2622   2313    641   1431    327       C  
ATOM   2120  O   TRP A 282      15.777  64.385  21.539  1.00 24.04           O  
ANISOU 2120  O   TRP A 282     4852   2292   1991    584   1329    259       O  
ATOM   2121  CB  TRP A 282      18.800  65.078  20.105  1.00 27.50           C  
ANISOU 2121  CB  TRP A 282     5296   2711   2441    731   1648    446       C  
ATOM   2122  CG  TRP A 282      19.206  64.451  21.393  1.00 27.97           C  
ANISOU 2122  CG  TRP A 282     5258   2772   2596    627   1600    403       C  
ATOM   2123  CD1 TRP A 282      19.101  65.000  22.630  1.00 27.06           C  
ANISOU 2123  CD1 TRP A 282     5040   2648   2592    516   1564    385       C  
ATOM   2124  CD2 TRP A 282      19.742  63.128  21.569  1.00 28.05           C  
ANISOU 2124  CD2 TRP A 282     5276   2793   2587    635   1579    369       C  
ATOM   2125  NE1 TRP A 282      19.590  64.137  23.563  1.00 27.78           N  
ANISOU 2125  NE1 TRP A 282     5075   2743   2735    458   1527    347       N  
ATOM   2126  CE2 TRP A 282      19.981  62.974  22.947  1.00 28.02           C  
ANISOU 2126  CE2 TRP A 282     5166   2786   2691    523   1536    337       C  
ATOM   2127  CE3 TRP A 282      20.095  62.086  20.693  1.00 29.61           C  
ANISOU 2127  CE3 TRP A 282     5565   2998   2685    733   1596    366       C  
ATOM   2128  CZ2 TRP A 282      20.523  61.802  23.484  1.00 28.39           C  
ANISOU 2128  CZ2 TRP A 282     5190   2842   2754    501   1508    303       C  
ATOM   2129  CZ3 TRP A 282      20.632  60.932  21.222  1.00 29.22           C  
ANISOU 2129  CZ3 TRP A 282     5490   2956   2654    707   1569    331       C  
ATOM   2130  CH2 TRP A 282      20.828  60.790  22.600  1.00 29.14           C  
ANISOU 2130  CH2 TRP A 282     5368   2946   2756    590   1525    300       C  
ATOM   2131  N   LEU A 283      16.201  66.532  20.948  1.00 24.99           N  
ANISOU 2131  N   LEU A 283     4952   2394   2149    612   1475    370       N  
ATOM   2132  CA  LEU A 283      15.304  67.107  21.896  1.00 24.43           C  
ANISOU 2132  CA  LEU A 283     4820   2320   2140    522   1406    336       C  
ATOM   2133  C   LEU A 283      13.857  66.697  21.583  1.00 23.99           C  
ANISOU 2133  C   LEU A 283     4829   2272   2013    541   1291    280       C  
ATOM   2134  O   LEU A 283      13.090  66.481  22.533  1.00 24.89           O  
ANISOU 2134  O   LEU A 283     4893   2387   2176    467   1210    234       O  
ATOM   2135  CB  LEU A 283      15.453  68.640  21.886  1.00 25.12           C  
ANISOU 2135  CB  LEU A 283     4867   2388   2287    508   1481    398       C  
ATOM   2136  CG  LEU A 283      14.538  69.392  22.853  1.00 25.06           C  
ANISOU 2136  CG  LEU A 283     4805   2374   2340    425   1420    370       C  
ATOM   2137  CD1 LEU A 283      14.799  68.967  24.279  1.00 25.41           C  
ANISOU 2137  CD1 LEU A 283     4769   2418   2468    335   1376    328       C  
ATOM   2138  CD2 LEU A 283      14.715  70.893  22.718  1.00 26.93           C  
ANISOU 2138  CD2 LEU A 283     5012   2587   2632    421   1492    431       C  
ATOM   2139  N   ASN A 284      13.466  66.645  20.302  1.00 23.81           N  
ANISOU 2139  N   ASN A 284     4914   2248   1884    642   1281    286       N  
ATOM   2140  CA  ASN A 284      12.107  66.228  19.953  1.00 26.12           C  
ANISOU 2140  CA  ASN A 284     5264   2534   2123    663   1154    230       C  
ATOM   2141  C   ASN A 284      11.819  64.820  20.517  1.00 26.56           C  
ANISOU 2141  C   ASN A 284     5303   2590   2196    625   1051    162       C  
ATOM   2142  O   ASN A 284      10.737  64.579  21.122  1.00 24.37           O  
ANISOU 2142  O   ASN A 284     4987   2303   1968    568    951    122       O  
ATOM   2143  CB  ASN A 284      11.875  66.198  18.448  1.00 30.69           C  
ANISOU 2143  CB  ASN A 284     5979   3106   2573    794   1145    238       C  
ATOM   2144  CG  ASN A 284      10.412  66.126  18.067  1.00 36.35           C  
ANISOU 2144  CG  ASN A 284     6747   3807   3257    813   1008    189       C  
ATOM   2145  OD1 ASN A 284       9.570  66.745  18.716  1.00 43.61           O  
ANISOU 2145  OD1 ASN A 284     7778   4712   4080    907    929    153       O  
ATOM   2146  ND2 ASN A 284      10.081  65.336  17.058  1.00 34.18           N  
ANISOU 2146  ND2 ASN A 284     6396   3528   3060    733    977    189       N  
ATOM   2147  N   ASN A 285      12.793  63.918  20.346  1.00 25.64           N  
ANISOU 2147  N   ASN A 285     5210   2480   2051    658   1083    158       N  
ATOM   2148  CA  ASN A 285      12.699  62.544  20.872  1.00 27.82           C  
ANISOU 2148  CA  ASN A 285     5469   2753   2346    626    999     99       C  
ATOM   2149  C   ASN A 285      12.652  62.561  22.411  1.00 26.41           C  
ANISOU 2149  C   ASN A 285     5166   2582   2285    505    994     91       C  
ATOM   2150  O   ASN A 285      11.800  61.839  22.998  1.00 25.88           O  
ANISOU 2150  O   ASN A 285     5068   2505   2259    460    896     46       O  
ATOM   2151  CB  ASN A 285      13.796  61.646  20.278  1.00 28.93           C  
ANISOU 2151  CB  ASN A 285     5670   2899   2421    698   1045    102       C  
ATOM   2152  CG  ASN A 285      13.432  61.209  18.879  1.00 30.47           C  
ANISOU 2152  CG  ASN A 285     6009   3078   2488    826    991     80       C  
ATOM   2153  OD1 ASN A 285      12.323  60.759  18.650  1.00 33.79           O  
ANISOU 2153  OD1 ASN A 285     6469   3476   2891    836    857     24       O  
ATOM   2154  ND2 ASN A 285      14.336  61.343  17.931  1.00 31.97           N  
ANISOU 2154  ND2 ASN A 285     6282   3273   2589    932   1091    125       N  
ATOM   2155  N   PHE A 286      13.547  63.336  23.047  1.00 23.51           N  
ANISOU 2155  N   PHE A 286     4731   2224   1976    460   1093    134       N  
ATOM   2156  CA  PHE A 286      13.612  63.429  24.516  1.00 24.86           C  
ANISOU 2156  CA  PHE A 286     4801   2398   2245    361   1089    124       C  
ATOM   2157  C   PHE A 286      12.288  63.989  25.055  1.00 25.48           C  
ANISOU 2157  C   PHE A 286     4850   2469   2359    318   1028    112       C  
ATOM   2158  O   PHE A 286      11.715  63.442  25.968  1.00 23.93           O  
ANISOU 2158  O   PHE A 286     4610   2271   2210    269    972     83       O  
ATOM   2159  CB  PHE A 286      14.807  64.282  24.919  1.00 24.42           C  
ANISOU 2159  CB  PHE A 286     4691   2341   2246    336   1190    172       C  
ATOM   2160  CG  PHE A 286      15.327  64.143  26.316  1.00 23.60           C  
ANISOU 2160  CG  PHE A 286     4502   2236   2228    258   1189    157       C  
ATOM   2161  CD1 PHE A 286      14.634  63.473  27.299  1.00 25.35           C  
ANISOU 2161  CD1 PHE A 286     4696   2463   2473    211   1115    113       C  
ATOM   2162  CD2 PHE A 286      16.532  64.736  26.642  1.00 24.39           C  
ANISOU 2162  CD2 PHE A 286     4551   2324   2392    239   1262    194       C  
ATOM   2163  CE1 PHE A 286      15.164  63.349  28.577  1.00 26.75           C  
ANISOU 2163  CE1 PHE A 286     4810   2638   2716    155   1115    101       C  
ATOM   2164  CE2 PHE A 286      17.051  64.636  27.920  1.00 26.25           C  
ANISOU 2164  CE2 PHE A 286     4718   2551   2703    176   1246    176       C  
ATOM   2165  CZ  PHE A 286      16.376  63.923  28.883  1.00 25.48           C  
ANISOU 2165  CZ  PHE A 286     4608   2464   2607    138   1173    127       C  
ATOM   2166  N   SER A 287      11.751  65.018  24.383  1.00 27.38           N  
ANISOU 2166  N   SER A 287     5124   2704   2574    348   1042    138       N  
ATOM   2167  CA  SER A 287      10.491  65.674  24.762  1.00 26.38           C  
ANISOU 2167  CA  SER A 287     4974   2568   2480    317    994    135       C  
ATOM   2168  C   SER A 287       9.287  64.711  24.654  1.00 26.44           C  
ANISOU 2168  C   SER A 287     4995   2562   2487    322    879     94       C  
ATOM   2169  O   SER A 287       8.478  64.614  25.572  1.00 26.22           O  
ANISOU 2169  O   SER A 287     4909   2526   2526    271    839     87       O  
ATOM   2170  CB  SER A 287      10.301  66.900  23.910  1.00 26.78           C  
ANISOU 2170  CB  SER A 287     5065   2614   2495    359   1036    173       C  
ATOM   2171  OG  SER A 287       9.294  67.717  24.440  1.00 30.93           O  
ANISOU 2171  OG  SER A 287     5555   3131   3065    320   1012    179       O  
ATOM   2172  N   LYS A 288       9.141  64.026  23.524  1.00 27.42           N  
ANISOU 2172  N   LYS A 288     5198   2677   2543    391    825     72       N  
ATOM   2173  CA  LYS A 288       8.026  63.104  23.313  1.00 30.36           C  
ANISOU 2173  CA  LYS A 288     5582   3021   2930    401    698     32       C  
ATOM   2174  C   LYS A 288       8.061  61.980  24.365  1.00 29.67           C  
ANISOU 2174  C   LYS A 288     5427   2931   2915    343    665      8       C  
ATOM   2175  O   LYS A 288       7.012  61.566  24.845  1.00 30.31           O  
ANISOU 2175  O   LYS A 288     5460   2987   3070    310    589      0       O  
ATOM   2176  CB  LYS A 288       8.044  62.513  21.897  1.00 31.77           C  
ANISOU 2176  CB  LYS A 288     5875   3184   3012    498    636      3       C  
ATOM   2177  CG  LYS A 288       7.533  63.454  20.813  1.00 36.41           C  
ANISOU 2177  CG  LYS A 288     6538   3762   3531    567    626     20       C  
ATOM   2178  CD  LYS A 288       7.529  62.830  19.399  1.00 39.80           C  
ANISOU 2178  CD  LYS A 288     7102   4171   3848    683    554    -13       C  
ATOM   2179  N   THR A 289       9.263  61.528  24.752  1.00 28.52           N  
ANISOU 2179  N   THR A 289     5271   2807   2758    331    728      7       N  
ATOM   2180  CA  THR A 289       9.402  60.454  25.712  1.00 28.47           C  
ANISOU 2180  CA  THR A 289     5207   2799   2810    284    705    -12       C  
ATOM   2181  C   THR A 289       8.989  60.954  27.100  1.00 26.16           C  
ANISOU 2181  C   THR A 289     4826   2511   2601    214    734      9       C  
ATOM   2182  O   THR A 289       8.233  60.281  27.808  1.00 25.76           O  
ANISOU 2182  O   THR A 289     4726   2443   2619    184    684      4       O  
ATOM   2183  CB  THR A 289      10.823  59.886  25.672  1.00 30.79           C  
ANISOU 2183  CB  THR A 289     5519   3113   3065    299    764    -18       C  
ATOM   2184  OG1 THR A 289      11.009  59.328  24.369  1.00 32.12           O  
ANISOU 2184  OG1 THR A 289     5782   3272   3150    379    728    -39       O  
ATOM   2185  CG2 THR A 289      11.102  58.839  26.726  1.00 28.88           C  
ANISOU 2185  CG2 THR A 289     5219   2874   2880    251    750    -36       C  
ATOM   2186  N   ILE A 290       9.500  62.114  27.504  1.00 25.14           N  
ANISOU 2186  N   ILE A 290     4681   2399   2470    195    816     38       N  
ATOM   2187  CA  ILE A 290       9.268  62.608  28.863  1.00 28.87           C  
ANISOU 2187  CA  ILE A 290     5088   2874   3004    143    846     54       C  
ATOM   2188  C   ILE A 290       7.798  63.035  29.004  1.00 27.09           C  
ANISOU 2188  C   ILE A 290     4842   2630   2821    138    805     71       C  
ATOM   2189  O   ILE A 290       7.237  62.888  30.071  1.00 24.34           O  
ANISOU 2189  O   ILE A 290     4441   2274   2530    110    804     83       O  
ATOM   2190  CB  ILE A 290      10.289  63.695  29.258  1.00 33.92           C  
ANISOU 2190  CB  ILE A 290     5719   3528   3640    128    929     73       C  
ATOM   2191  CG1 ILE A 290      11.680  63.087  29.449  1.00 38.78           C  
ANISOU 2191  CG1 ILE A 290     6329   4155   4249    123    963     61       C  
ATOM   2192  CG2 ILE A 290       9.858  64.430  30.519  1.00 35.96           C  
ANISOU 2192  CG2 ILE A 290     5934   3781   3946     93    946     86       C  
ATOM   2193  CD1 ILE A 290      11.856  62.343  30.772  1.00 39.15           C  
ANISOU 2193  CD1 ILE A 290     6332   4205   4339     87    951     44       C  
ATOM   2194  N   ASN A 291       7.147  63.448  27.901  1.00 26.35           N  
ANISOU 2194  N   ASN A 291     4788   2524   2698    172    768     74       N  
ATOM   2195  CA  ASN A 291       5.740  63.880  27.963  1.00 28.71           C  
ANISOU 2195  CA  ASN A 291     5061   2798   3046    168    724     93       C  
ATOM   2196  C   ASN A 291       4.774  62.676  28.067  1.00 28.71           C  
ANISOU 2196  C   ASN A 291     5025   2765   3118    163    633     83       C  
ATOM   2197  O   ASN A 291       3.586  62.860  28.284  1.00 29.43           O  
ANISOU 2197  O   ASN A 291     5073   2828   3278    155    597    108       O  
ATOM   2198  CB  ASN A 291       5.399  64.851  26.826  1.00 29.44           C  
ANISOU 2198  CB  ASN A 291     5208   2888   3090    208    716    103       C  
ATOM   2199  CG  ASN A 291       5.905  66.249  27.120  1.00 30.65           C  
ANISOU 2199  CG  ASN A 291     5361   3059   3223    196    808    131       C  
ATOM   2200  OD1 ASN A 291       5.984  66.638  28.282  1.00 29.97           O  
ANISOU 2200  OD1 ASN A 291     5228   2979   3180    158    853    145       O  
ATOM   2201  ND2 ASN A 291       6.308  66.984  26.098  1.00 26.91           N  
ANISOU 2201  ND2 ASN A 291     4944   2592   2686    236    837    141       N  
ATOM   2202  N   LYS A 292       5.271  61.446  27.977  1.00 28.44           N  
ANISOU 2202  N   LYS A 292     4997   2727   3080    167    597     53       N  
ATOM   2203  CA  LYS A 292       4.468  60.264  28.310  1.00 29.93           C  
ANISOU 2203  CA  LYS A 292     5135   2878   3360    153    519     50       C  
ATOM   2204  C   LYS A 292       4.610  59.893  29.798  1.00 30.52           C  
ANISOU 2204  C   LYS A 292     5138   2961   3494    113    580     76       C  
ATOM   2205  O   LYS A 292       3.986  58.943  30.230  1.00 31.25           O  
ANISOU 2205  O   LYS A 292     5176   3021   3674    101    536     87       O  
ATOM   2206  CB  LYS A 292       4.922  59.085  27.445  1.00 32.94           C  
ANISOU 2206  CB  LYS A 292     5566   3243   3705    184    444      2       C  
ATOM   2207  CG  LYS A 292       4.672  59.248  25.960  1.00 34.25           C  
ANISOU 2207  CG  LYS A 292     5818   3390   3806    243    366    -27       C  
ATOM   2208  CD  LYS A 292       5.284  58.148  25.156  1.00 37.34           C  
ANISOU 2208  CD  LYS A 292     6277   3768   4140    288    304    -77       C  
ATOM   2209  CE  LYS A 292       5.351  58.487  23.686  1.00 41.23           C  
ANISOU 2209  CE  LYS A 292     6885   4254   4526    369    258   -104       C  
ATOM   2210  NZ  LYS A 292       5.964  57.385  22.919  1.00 45.42           N  
ANISOU 2210  NZ  LYS A 292     7496   4769   4990    426    200   -154       N  
ATOM   2211  N   VAL A 293       5.468  60.599  30.548  1.00 27.89           N  
ANISOU 2211  N   VAL A 293     4810   2667   3118     99    674     85       N  
ATOM   2212  CA  VAL A 293       5.720  60.348  31.959  1.00 26.29           C  
ANISOU 2212  CA  VAL A 293     4563   2476   2949     76    730    103       C  
ATOM   2213  C   VAL A 293       4.876  61.347  32.738  1.00 26.92           C  
ANISOU 2213  C   VAL A 293     4612   2550   3065     74    774    148       C  
ATOM   2214  O   VAL A 293       5.007  62.563  32.517  1.00 24.24           O  
ANISOU 2214  O   VAL A 293     4303   2225   2683     78    807    151       O  
ATOM   2215  CB  VAL A 293       7.208  60.497  32.327  1.00 26.15           C  
ANISOU 2215  CB  VAL A 293     4574   2495   2867     69    789     79       C  
ATOM   2216  CG1 VAL A 293       7.455  60.208  33.792  1.00 25.09           C  
ANISOU 2216  CG1 VAL A 293     4406   2367   2759     56    833     93       C  
ATOM   2217  CG2 VAL A 293       8.117  59.638  31.433  1.00 27.49           C  
ANISOU 2217  CG2 VAL A 293     4781   2671   2991     80    760     41       C  
ATOM   2218  N   PRO A 294       3.987  60.870  33.642  1.00 24.97           N  
ANISOU 2218  N   PRO A 294     4307   2280   2901     73    781    190       N  
ATOM   2219  CA  PRO A 294       3.121  61.754  34.420  1.00 25.24           C  
ANISOU 2219  CA  PRO A 294     4315   2305   2970     84    832    241       C  
ATOM   2220  C   PRO A 294       3.905  62.875  35.119  1.00 26.55           C  
ANISOU 2220  C   PRO A 294     4524   2502   3060     90    904    232       C  
ATOM   2221  O   PRO A 294       5.003  62.619  35.664  1.00 25.57           O  
ANISOU 2221  O   PRO A 294     4424   2400   2891     86    928    203       O  
ATOM   2222  CB  PRO A 294       2.511  60.826  35.488  1.00 27.48           C  
ANISOU 2222  CB  PRO A 294     4536   2564   3338     92    855    289       C  
ATOM   2223  CG  PRO A 294       2.574  59.429  34.889  1.00 26.16           C  
ANISOU 2223  CG  PRO A 294     4343   2375   3220     77    779    267       C  
ATOM   2224  CD  PRO A 294       3.776  59.442  33.966  1.00 26.69           C  
ANISOU 2224  CD  PRO A 294     4478   2473   3188     68    748    197       C  
ATOM   2225  N   ARG A 295       3.332  64.094  35.121  1.00 25.79           N  
ANISOU 2225  N   ARG A 295     4438   2402   2958    101    930    256       N  
ATOM   2226  CA  ARG A 295       3.948  65.244  35.793  1.00 25.11           C  
ANISOU 2226  CA  ARG A 295     4394   2333   2813    111    985    247       C  
ATOM   2227  C   ARG A 295       4.012  65.001  37.302  1.00 27.09           C  
ANISOU 2227  C   ARG A 295     4643   2583   3065    137   1035    265       C  
ATOM   2228  O   ARG A 295       4.860  65.550  37.930  1.00 26.77           O  
ANISOU 2228  O   ARG A 295     4645   2553   2973    145   1058    238       O  
ATOM   2229  CB  ARG A 295       3.203  66.543  35.471  1.00 26.42           C  
ANISOU 2229  CB  ARG A 295     4570   2490   2979    121    999    271       C  
ATOM   2230  CG  ARG A 295       3.475  67.055  34.067  1.00 26.40           C  
ANISOU 2230  CG  ARG A 295     4592   2493   2944    106    964    246       C  
ATOM   2231  CD  ARG A 295       2.816  68.414  33.873  1.00 29.42           C  
ANISOU 2231  CD  ARG A 295     4987   2867   3324    118    985    271       C  
ATOM   2232  NE  ARG A 295       3.241  69.063  32.651  1.00 28.77           N  
ANISOU 2232  NE  ARG A 295     4939   2792   3200    113    968    252       N  
ATOM   2233  CZ  ARG A 295       4.298  69.843  32.550  1.00 27.33           C  
ANISOU 2233  CZ  ARG A 295     4790   2620   2973    106    999    231       C  
ATOM   2234  NH1 ARG A 295       5.034  70.084  33.619  1.00 27.31           N  
ANISOU 2234  NH1 ARG A 295     4793   2618   2964    101   1031    218       N  
ATOM   2235  NH2 ARG A 295       4.616  70.381  31.386  1.00 25.49           N  
ANISOU 2235  NH2 ARG A 295     4585   2390   2708    111    995    227       N  
ATOM   2236  N   ASP A 296       3.208  64.073  37.827  1.00 27.60           N  
ANISOU 2236  N   ASP A 296     4662   2631   3193    154   1045    310       N  
ATOM   2237  CA  ASP A 296       3.265  63.685  39.267  1.00 30.73           C  
ANISOU 2237  CA  ASP A 296     5063   3025   3585    194   1101    336       C  
ATOM   2238  C   ASP A 296       4.661  63.186  39.664  1.00 30.82           C  
ANISOU 2238  C   ASP A 296     5112   3059   3539    185   1091    280       C  
ATOM   2239  O   ASP A 296       5.028  63.262  40.866  1.00 28.38           O  
ANISOU 2239  O   ASP A 296     4839   2753   3190    225   1129    281       O  
ATOM   2240  CB  ASP A 296       2.278  62.564  39.597  1.00 34.66           C  
ANISOU 2240  CB  ASP A 296     5492   3496   4177    210   1115    400       C  
ATOM   2241  CG  ASP A 296       0.887  62.867  39.088  1.00 40.44           C  
ANISOU 2241  CG  ASP A 296     6169   4196   4998    212   1110    458       C  
ATOM   2242  OD1 ASP A 296       0.711  62.859  37.839  1.00 44.99           O  
ANISOU 2242  OD1 ASP A 296     6729   4766   5600    173   1037    433       O  
ATOM   2243  OD2 ASP A 296       0.023  63.174  39.926  1.00 42.34           O  
ANISOU 2243  OD2 ASP A 296     6392   4418   5275    260   1178    528       O  
ATOM   2244  N   SER A 297       5.441  62.678  38.687  1.00 24.54           N  
ANISOU 2244  N   SER A 297     4311   2276   2734    141   1039    234       N  
ATOM   2245  CA  SER A 297       6.807  62.190  39.008  1.00 25.31           C  
ANISOU 2245  CA  SER A 297     4435   2392   2787    130   1030    185       C  
ATOM   2246  C   SER A 297       7.773  63.359  39.218  1.00 25.31           C  
ANISOU 2246  C   SER A 297     4486   2400   2731    129   1035    147       C  
ATOM   2247  O   SER A 297       8.817  63.192  39.882  1.00 24.67           O  
ANISOU 2247  O   SER A 297     4428   2323   2621    133   1031    114       O  
ATOM   2248  CB  SER A 297       7.322  61.264  37.937  1.00 24.57           C  
ANISOU 2248  CB  SER A 297     4324   2307   2704     94    982    156       C  
ATOM   2249  OG  SER A 297       7.409  61.985  36.718  1.00 24.35           O  
ANISOU 2249  OG  SER A 297     4311   2283   2658     75    959    139       O  
ATOM   2250  N   ASP A 298       7.439  64.530  38.648  1.00 26.77           N  
ANISOU 2250  N   ASP A 298     4682   2579   2910    124   1037    152       N  
ATOM   2251  CA  ASP A 298       8.347  65.675  38.607  1.00 28.11           C  
ANISOU 2251  CA  ASP A 298     4887   2745   3048    115   1034    119       C  
ATOM   2252  C   ASP A 298       8.704  66.167  40.015  1.00 28.85           C  
ANISOU 2252  C   ASP A 298     5023   2824   3114    152   1045    105       C  
ATOM   2253  O   ASP A 298       9.810  66.632  40.218  1.00 27.37           O  
ANISOU 2253  O   ASP A 298     4857   2627   2916    142   1022     65       O  
ATOM   2254  CB  ASP A 298       7.797  66.831  37.769  1.00 29.02           C  
ANISOU 2254  CB  ASP A 298     5006   2853   3167    107   1039    134       C  
ATOM   2255  CG  ASP A 298       7.743  66.557  36.269  1.00 28.97           C  
ANISOU 2255  CG  ASP A 298     4981   2857   3169     81   1019    136       C  
ATOM   2256  OD1 ASP A 298       8.134  65.411  35.820  1.00 24.97           O  
ANISOU 2256  OD1 ASP A 298     4460   2362   2665     68    997    122       O  
ATOM   2257  OD2 ASP A 298       7.300  67.480  35.550  1.00 29.49           O  
ANISOU 2257  OD2 ASP A 298     5054   2917   3232     80   1023    150       O  
ATOM   2258  N   LYS A 299       7.808  66.042  40.996  1.00 26.22           N  
ANISOU 2258  N   LYS A 299     4704   2484   2774    203   1076    138       N  
ATOM   2259  CA  LYS A 299       8.155  66.573  42.298  1.00 28.96           C  
ANISOU 2259  CA  LYS A 299     5112   2814   3076    255   1081    120       C  
ATOM   2260  C   LYS A 299       9.295  65.786  42.969  1.00 28.94           C  
ANISOU 2260  C   LYS A 299     5126   2813   3053    260   1052     79       C  
ATOM   2261  O   LYS A 299       9.827  66.238  43.973  1.00 28.53           O  
ANISOU 2261  O   LYS A 299     5133   2741   2962    303   1032     48       O  
ATOM   2262  CB  LYS A 299       6.917  66.624  43.192  1.00 32.32           C  
ANISOU 2262  CB  LYS A 299     5558   3231   3490    326   1137    176       C  
ATOM   2263  CG  LYS A 299       6.300  65.278  43.511  1.00 33.12           C  
ANISOU 2263  CG  LYS A 299     5619   3341   3621    345   1173    225       C  
ATOM   2264  CD  LYS A 299       5.073  65.384  44.374  1.00 38.46           C  
ANISOU 2264  CD  LYS A 299     6309   4004   4300    423   1245    297       C  
ATOM   2265  CE  LYS A 299       4.466  64.032  44.668  1.00 40.90           C  
ANISOU 2265  CE  LYS A 299     6563   4313   4661    441   1286    358       C  
ATOM   2266  NZ  LYS A 299       3.676  63.529  43.521  1.00 43.82           N  
ANISOU 2266  NZ  LYS A 299     6841   4679   5127    382   1272    394       N  
ATOM   2267  N   TYR A 300       9.617  64.586  42.467  1.00 26.96           N  
ANISOU 2267  N   TYR A 300     4830   2584   2828    224   1044     79       N  
ATOM   2268  CA  TYR A 300      10.677  63.716  43.017  1.00 26.12           C  
ANISOU 2268  CA  TYR A 300     4731   2482   2709    225   1019     45       C  
ATOM   2269  C   TYR A 300      12.024  63.983  42.353  1.00 26.97           C  
ANISOU 2269  C   TYR A 300     4825   2586   2834    172    973     -3       C  
ATOM   2270  O   TYR A 300      13.031  63.438  42.769  1.00 30.05           O  
ANISOU 2270  O   TYR A 300     5220   2975   3222    170    945    -34       O  
ATOM   2271  CB  TYR A 300      10.292  62.251  42.819  1.00 25.23           C  
ANISOU 2271  CB  TYR A 300     4573   2389   2623    216   1038     74       C  
ATOM   2272  CG  TYR A 300       9.074  61.874  43.613  1.00 26.24           C  
ANISOU 2272  CG  TYR A 300     4702   2511   2755    273   1091    134       C  
ATOM   2273  CD1 TYR A 300       9.162  61.753  44.985  1.00 28.47           C  
ANISOU 2273  CD1 TYR A 300     5038   2785   2991    345   1114    140       C  
ATOM   2274  CD2 TYR A 300       7.825  61.739  43.028  1.00 27.94           C  
ANISOU 2274  CD2 TYR A 300     4869   2723   3022    265   1118    190       C  
ATOM   2275  CE1 TYR A 300       8.057  61.444  45.763  1.00 30.67           C  
ANISOU 2275  CE1 TYR A 300     5321   3056   3275    412   1181    210       C  
ATOM   2276  CE2 TYR A 300       6.710  61.397  43.787  1.00 29.39           C  
ANISOU 2276  CE2 TYR A 300     5041   2894   3231    322   1177    259       C  
ATOM   2277  CZ  TYR A 300       6.825  61.261  45.164  1.00 30.51           C  
ANISOU 2277  CZ  TYR A 300     5236   3030   3324    398   1218    274       C  
ATOM   2278  OH  TYR A 300       5.752  60.955  45.960  1.00 32.34           O  
ANISOU 2278  OH  TYR A 300     5461   3246   3578    468   1294    356       O  
ATOM   2279  N   VAL A 301      12.030  64.820  41.308  1.00 26.96           N  
ANISOU 2279  N   VAL A 301     4806   2582   2856    135    972     -1       N  
ATOM   2280  CA  VAL A 301      13.262  65.222  40.652  1.00 26.00           C  
ANISOU 2280  CA  VAL A 301     4666   2449   2763     94    945    -29       C  
ATOM   2281  C   VAL A 301      13.936  66.301  41.494  1.00 28.62           C  
ANISOU 2281  C   VAL A 301     5033   2740   3101    111    907    -63       C  
ATOM   2282  O   VAL A 301      13.278  67.222  41.944  1.00 27.65           O  
ANISOU 2282  O   VAL A 301     4947   2598   2958    141    909    -58       O  
ATOM   2283  CB  VAL A 301      12.993  65.762  39.243  1.00 26.16           C  
ANISOU 2283  CB  VAL A 301     4660   2476   2803     62    966     -7       C  
ATOM   2284  CG1 VAL A 301      14.285  66.239  38.582  1.00 26.61           C  
ANISOU 2284  CG1 VAL A 301     4695   2516   2899     29    956    -20       C  
ATOM   2285  CG2 VAL A 301      12.263  64.728  38.398  1.00 26.06           C  
ANISOU 2285  CG2 VAL A 301     4624   2494   2784     54    982     17       C  
ATOM   2286  N   THR A 302      15.253  66.199  41.652  1.00 28.79           N  
ANISOU 2286  N   THR A 302     5041   2741   3157     91    866    -96       N  
ATOM   2287  CA  THR A 302      16.068  67.171  42.405  1.00 30.01           C  
ANISOU 2287  CA  THR A 302     5221   2841   3341    103    805   -135       C  
ATOM   2288  C   THR A 302      15.822  68.589  41.856  1.00 29.50           C  
ANISOU 2288  C   THR A 302     5152   2747   3308     88    809   -123       C  
ATOM   2289  O   THR A 302      15.819  68.795  40.650  1.00 29.97           O  
ANISOU 2289  O   THR A 302     5167   2819   3399     50    848    -91       O  
ATOM   2290  CB  THR A 302      17.547  66.761  42.331  1.00 30.49           C  
ANISOU 2290  CB  THR A 302     5239   2880   3463     70    764   -159       C  
ATOM   2291  OG1 THR A 302      17.656  65.418  42.821  1.00 34.86           O  
ANISOU 2291  OG1 THR A 302     5799   3466   3980     86    765   -168       O  
ATOM   2292  CG2 THR A 302      18.467  67.637  43.137  1.00 31.30           C  
ANISOU 2292  CG2 THR A 302     5358   2914   3618     80    679   -204       C  
ATOM   2293  N   GLN A 303      15.663  69.552  42.767  1.00 30.00           N  
ANISOU 2293  N   GLN A 303     5271   2767   3359    127    765   -150       N  
ATOM   2294  CA  GLN A 303      15.132  70.910  42.489  1.00 34.26           C  
ANISOU 2294  CA  GLN A 303     5825   3279   3913    129    770   -140       C  
ATOM   2295  C   GLN A 303      16.002  71.636  41.438  1.00 30.40           C  
ANISOU 2295  C   GLN A 303     5270   2759   3521     70    767   -126       C  
ATOM   2296  O   GLN A 303      15.475  72.319  40.572  1.00 28.36           O  
ANISOU 2296  O   GLN A 303     4995   2506   3274     54    811    -91       O  
ATOM   2297  CB  GLN A 303      14.995  71.633  43.836  1.00 38.18           C  
ANISOU 2297  CB  GLN A 303     6406   3727   4373    195    709   -183       C  
ATOM   2298  CG  GLN A 303      14.717  73.135  43.780  1.00 47.61           C  
ANISOU 2298  CG  GLN A 303     7624   4873   5592    202    688   -188       C  
ATOM   2299  CD  GLN A 303      13.458  73.532  43.040  1.00 57.14           C  
ANISOU 2299  CD  GLN A 303     8825   6117   6769    200    768   -135       C  
ATOM   2300  OE1 GLN A 303      13.411  74.551  42.334  1.00 66.95           O  
ANISOU 2300  OE1 GLN A 303    10043   7335   8058    171    776   -120       O  
ATOM   2301  NE2 GLN A 303      12.413  72.741  43.217  1.00 58.34           N  
ANISOU 2301  NE2 GLN A 303     8995   6321   6850    233    827   -104       N  
ATOM   2302  N   ILE A 304      17.327  71.471  41.486  1.00 30.91           N  
ANISOU 2302  N   ILE A 304     5293   2787   3662     42    721   -147       N  
ATOM   2303  CA  ILE A 304      18.221  72.221  40.562  1.00 33.37           C  
ANISOU 2303  CA  ILE A 304     5533   3056   4087     -5    726   -121       C  
ATOM   2304  C   ILE A 304      17.899  71.936  39.089  1.00 29.73           C  
ANISOU 2304  C   ILE A 304     5030   2647   3618    -31    823    -60       C  
ATOM   2305  O   ILE A 304      18.324  72.721  38.229  1.00 28.49           O  
ANISOU 2305  O   ILE A 304     4827   2461   3536    -56    851    -23       O  
ATOM   2306  CB  ILE A 304      19.714  71.952  40.826  1.00 36.10           C  
ANISOU 2306  CB  ILE A 304     5827   3353   4535    -30    667   -141       C  
ATOM   2307  CG1 ILE A 304      20.034  70.459  40.824  1.00 36.69           C  
ANISOU 2307  CG1 ILE A 304     5888   3480   4570    -32    689   -142       C  
ATOM   2308  CG2 ILE A 304      20.163  72.660  42.092  1.00 41.15           C  
ANISOU 2308  CG2 ILE A 304     6506   3913   5214     -4    549   -203       C  
ATOM   2309  CD1 ILE A 304      21.482  70.146  40.583  1.00 39.17           C  
ANISOU 2309  CD1 ILE A 304     6127   3757   4997    -66    668   -135       C  
ATOM   2310  N   PHE A 305      17.229  70.812  38.807  1.00 25.64           N  
ANISOU 2310  N   PHE A 305     4527   2197   3017    -21    867    -49       N  
ATOM   2311  CA  PHE A 305      16.930  70.394  37.481  1.00 27.12           C  
ANISOU 2311  CA  PHE A 305     4690   2429   3183    -33    938     -3       C  
ATOM   2312  C   PHE A 305      15.526  70.814  37.045  1.00 28.10           C  
ANISOU 2312  C   PHE A 305     4848   2582   3246    -16    972     18       C  
ATOM   2313  O   PHE A 305      15.103  70.404  35.963  1.00 29.25           O  
ANISOU 2313  O   PHE A 305     4987   2764   3360    -16   1018     49       O  
ATOM   2314  CB  PHE A 305      17.038  68.874  37.342  1.00 27.59           C  
ANISOU 2314  CB  PHE A 305     4745   2536   3200    -31    952     -7       C  
ATOM   2315  CG  PHE A 305      18.444  68.338  37.424  1.00 29.92           C  
ANISOU 2315  CG  PHE A 305     4996   2811   3557    -49    937    -15       C  
ATOM   2316  CD1 PHE A 305      19.380  68.657  36.452  1.00 30.65           C  
ANISOU 2316  CD1 PHE A 305     5038   2883   3723    -68    976     23       C  
ATOM   2317  CD2 PHE A 305      18.843  67.537  38.488  1.00 31.26           C  
ANISOU 2317  CD2 PHE A 305     5176   2981   3719    -43    887    -55       C  
ATOM   2318  CE1 PHE A 305      20.680  68.171  36.528  1.00 33.54           C  
ANISOU 2318  CE1 PHE A 305     5355   3225   4160    -82    967     24       C  
ATOM   2319  CE2 PHE A 305      20.146  67.066  38.573  1.00 32.89           C  
ANISOU 2319  CE2 PHE A 305     5339   3166   3992    -60    868    -62       C  
ATOM   2320  CZ  PHE A 305      21.060  67.370  37.585  1.00 33.15           C  
ANISOU 2320  CZ  PHE A 305     5312   3176   4105    -82    909    -20       C  
ATOM   2321  N   ASN A 306      14.840  71.647  37.840  1.00 27.99           N  
ANISOU 2321  N   ASN A 306     4871   2545   3216      4    946      2       N  
ATOM   2322  CA  ASN A 306      13.443  72.029  37.583  1.00 30.10           C  
ANISOU 2322  CA  ASN A 306     5168   2837   3431     24    976     25       C  
ATOM   2323  C   ASN A 306      13.301  72.649  36.177  1.00 28.88           C  
ANISOU 2323  C   ASN A 306     4991   2687   3294      8   1023     68       C  
ATOM   2324  O   ASN A 306      12.411  72.293  35.388  1.00 25.42           O  
ANISOU 2324  O   ASN A 306     4559   2286   2811     17   1053     94       O  
ATOM   2325  CB  ASN A 306      12.914  72.973  38.676  1.00 33.84           C  
ANISOU 2325  CB  ASN A 306     5690   3276   3892     55    946      4       C  
ATOM   2326  CG  ASN A 306      13.443  74.410  38.660  1.00 38.05           C  
ANISOU 2326  CG  ASN A 306     6220   3749   4488     45    921     -1       C  
ATOM   2327  OD1 ASN A 306      14.652  74.678  38.484  1.00 32.78           O  
ANISOU 2327  OD1 ASN A 306     5513   3041   3900     16    895     -9       O  
ATOM   2328  ND2 ASN A 306      12.546  75.365  38.903  1.00 41.28           N  
ANISOU 2328  ND2 ASN A 306     6666   4143   4874     71    925      3       N  
ATOM   2329  N   LEU A 307      14.163  73.621  35.887  1.00 27.82           N  
ANISOU 2329  N   LEU A 307     4831   2507   3230     -9   1023     78       N  
ATOM   2330  CA  LEU A 307      14.083  74.357  34.639  1.00 26.68           C  
ANISOU 2330  CA  LEU A 307     4671   2360   3106    -13   1075    126       C  
ATOM   2331  C   LEU A 307      14.474  73.441  33.468  1.00 25.98           C  
ANISOU 2331  C   LEU A 307     4564   2308   2997    -11   1122    156       C  
ATOM   2332  O   LEU A 307      13.764  73.395  32.439  1.00 25.88           O  
ANISOU 2332  O   LEU A 307     4571   2326   2934      7   1158    185       O  
ATOM   2333  CB  LEU A 307      14.951  75.613  34.747  1.00 26.25           C  
ANISOU 2333  CB  LEU A 307     4586   2237   3151    -30   1064    135       C  
ATOM   2334  CG  LEU A 307      15.249  76.331  33.435  1.00 26.68           C  
ANISOU 2334  CG  LEU A 307     4609   2277   3249    -33   1131    197       C  
ATOM   2335  CD1 LEU A 307      13.981  76.869  32.802  1.00 26.69           C  
ANISOU 2335  CD1 LEU A 307     4649   2307   3184    -11   1163    221       C  
ATOM   2336  CD2 LEU A 307      16.280  77.422  33.652  1.00 28.18           C  
ANISOU 2336  CD2 LEU A 307     4749   2386   3569    -55   1115    210       C  
ATOM   2337  N   LYS A 308      15.562  72.682  33.603  1.00 25.99           N  
ANISOU 2337  N   LYS A 308     4535   2305   3032    -24   1117    147       N  
ATOM   2338  CA  LYS A 308      15.964  71.797  32.495  1.00 25.47           C  
ANISOU 2338  CA  LYS A 308     4463   2272   2941    -11   1165    175       C  
ATOM   2339  C   LYS A 308      14.851  70.813  32.105  1.00 23.68           C  
ANISOU 2339  C   LYS A 308     4279   2099   2616     11   1159    164       C  
ATOM   2340  O   LYS A 308      14.598  70.597  30.931  1.00 23.94           O  
ANISOU 2340  O   LYS A 308     4335   2155   2606     38   1193    191       O  
ATOM   2341  CB  LYS A 308      17.257  71.042  32.789  1.00 27.69           C  
ANISOU 2341  CB  LYS A 308     4705   2541   3274    -25   1160    167       C  
ATOM   2342  CG  LYS A 308      17.734  70.195  31.620  1.00 28.90           C  
ANISOU 2342  CG  LYS A 308     4859   2724   3398     -1   1218    201       C  
ATOM   2343  CD  LYS A 308      19.214  70.016  31.596  1.00 32.08           C  
ANISOU 2343  CD  LYS A 308     5204   3094   3889    -11   1243    224       C  
ATOM   2344  CE  LYS A 308      19.663  69.103  30.473  1.00 34.21           C  
ANISOU 2344  CE  LYS A 308     5486   3394   4116     26   1307    260       C  
ATOM   2345  NZ  LYS A 308      21.118  68.844  30.563  1.00 35.60           N  
ANISOU 2345  NZ  LYS A 308     5599   3537   4388     17   1335    286       N  
ATOM   2346  N   LEU A 309      14.211  70.187  33.093  1.00 24.76           N  
ANISOU 2346  N   LEU A 309     4429   2253   2725      5   1112    125       N  
ATOM   2347  CA  LEU A 309      13.154  69.226  32.858  1.00 23.88           C  
ANISOU 2347  CA  LEU A 309     4343   2179   2551     21   1096    118       C  
ATOM   2348  C   LEU A 309      11.956  69.910  32.179  1.00 24.40           C  
ANISOU 2348  C   LEU A 309     4432   2250   2587     39   1104    142       C  
ATOM   2349  O   LEU A 309      11.364  69.363  31.238  1.00 22.41           O  
ANISOU 2349  O   LEU A 309     4201   2019   2293     60   1100    151       O  
ATOM   2350  CB  LEU A 309      12.765  68.593  34.203  1.00 25.57           C  
ANISOU 2350  CB  LEU A 309     4556   2397   2760     16   1058     86       C  
ATOM   2351  CG  LEU A 309      11.615  67.582  34.186  1.00 27.50           C  
ANISOU 2351  CG  LEU A 309     4810   2669   2969     29   1039     86       C  
ATOM   2352  CD1 LEU A 309      11.926  66.388  33.318  1.00 28.67           C  
ANISOU 2352  CD1 LEU A 309     4957   2837   3096     33   1034     82       C  
ATOM   2353  CD2 LEU A 309      11.264  67.131  35.595  1.00 28.16           C  
ANISOU 2353  CD2 LEU A 309     4892   2750   3055     35   1020     70       C  
ATOM   2354  N   GLU A 310      11.593  71.111  32.653  1.00 24.92           N  
ANISOU 2354  N   GLU A 310     4499   2292   2675     35   1107    149       N  
ATOM   2355  CA  GLU A 310      10.452  71.795  32.075  1.00 25.63           C  
ANISOU 2355  CA  GLU A 310     4609   2385   2741     51   1114    172       C  
ATOM   2356  C   GLU A 310      10.783  72.203  30.638  1.00 24.49           C  
ANISOU 2356  C   GLU A 310     4478   2243   2584     70   1152    205       C  
ATOM   2357  O   GLU A 310       9.920  72.081  29.760  1.00 24.17           O  
ANISOU 2357  O   GLU A 310     4463   2218   2500     95   1145    219       O  
ATOM   2358  CB  GLU A 310       9.995  72.986  32.926  1.00 26.73           C  
ANISOU 2358  CB  GLU A 310     4752   2497   2904     49   1112    173       C  
ATOM   2359  CG  GLU A 310       8.641  73.523  32.492  1.00 28.85           C  
ANISOU 2359  CG  GLU A 310     5038   2773   3151     67   1115    198       C  
ATOM   2360  CD  GLU A 310       7.519  72.499  32.416  1.00 29.75           C  
ANISOU 2360  CD  GLU A 310     5150   2911   3240     80   1089    200       C  
ATOM   2361  OE1 GLU A 310       7.381  71.733  33.391  1.00 31.76           O  
ANISOU 2361  OE1 GLU A 310     5395   3171   3501     78   1074    185       O  
ATOM   2362  OE2 GLU A 310       6.805  72.433  31.364  1.00 29.45           O  
ANISOU 2362  OE2 GLU A 310     5122   2883   3184     95   1080    219       O  
ATOM   2363  N   ALA A 311      12.023  72.667  30.410  1.00 23.87           N  
ANISOU 2363  N   ALA A 311     4380   2142   2546     62   1190    222       N  
ATOM   2364  CA  ALA A 311      12.502  73.005  29.058  1.00 24.43           C  
ANISOU 2364  CA  ALA A 311     4462   2211   2606     93   1245    266       C  
ATOM   2365  C   ALA A 311      12.325  71.819  28.106  1.00 25.12           C  
ANISOU 2365  C   ALA A 311     4590   2334   2621    131   1241    263       C  
ATOM   2366  O   ALA A 311      11.857  71.975  26.976  1.00 25.04           O  
ANISOU 2366  O   ALA A 311     4624   2334   2556    176   1256    287       O  
ATOM   2367  CB  ALA A 311      13.941  73.458  29.109  1.00 25.26           C  
ANISOU 2367  CB  ALA A 311     4524   2281   2789     78   1290    292       C  
ATOM   2368  N   ILE A 312      12.702  70.631  28.585  1.00 24.33           N  
ANISOU 2368  N   ILE A 312     4479   2249   2517    118   1213    231       N  
ATOM   2369  CA  ILE A 312      12.572  69.407  27.811  1.00 24.45           C  
ANISOU 2369  CA  ILE A 312     4531   2289   2467    153   1195    218       C  
ATOM   2370  C   ILE A 312      11.083  69.107  27.556  1.00 23.27           C  
ANISOU 2370  C   ILE A 312     4414   2151   2274    168   1133    200       C  
ATOM   2371  O   ILE A 312      10.694  68.841  26.414  1.00 23.42           O  
ANISOU 2371  O   ILE A 312     4486   2178   2235    218   1120    206       O  
ATOM   2372  CB  ILE A 312      13.344  68.260  28.492  1.00 24.11           C  
ANISOU 2372  CB  ILE A 312     4462   2254   2443    131   1179    189       C  
ATOM   2373  CG1 ILE A 312      14.849  68.541  28.488  1.00 26.17           C  
ANISOU 2373  CG1 ILE A 312     4689   2497   2757    125   1239    216       C  
ATOM   2374  CG2 ILE A 312      13.017  66.929  27.848  1.00 25.49           C  
ANISOU 2374  CG2 ILE A 312     4677   2451   2557    164   1141    166       C  
ATOM   2375  CD1 ILE A 312      15.644  67.706  29.479  1.00 27.99           C  
ANISOU 2375  CD1 ILE A 312     4880   2727   3028     91   1217    185       C  
ATOM   2376  N   ARG A 313      10.237  69.179  28.594  1.00 22.62           N  
ANISOU 2376  N   ARG A 313     4303   2066   2224    134   1094    183       N  
ATOM   2377  CA  ARG A 313       8.789  68.998  28.405  1.00 23.37           C  
ANISOU 2377  CA  ARG A 313     4410   2161   2306    145   1039    178       C  
ATOM   2378  C   ARG A 313       8.237  69.967  27.351  1.00 23.84           C  
ANISOU 2378  C   ARG A 313     4508   2215   2335    180   1049    206       C  
ATOM   2379  O   ARG A 313       7.376  69.594  26.609  1.00 23.56           O  
ANISOU 2379  O   ARG A 313     4503   2179   2270    210    998    201       O  
ATOM   2380  CB  ARG A 313       8.022  69.156  29.716  1.00 23.72           C  
ANISOU 2380  CB  ARG A 313     4415   2199   2398    113   1022    174       C  
ATOM   2381  CG  ARG A 313       8.134  67.955  30.647  1.00 23.70           C  
ANISOU 2381  CG  ARG A 313     4385   2202   2417     94    997    150       C  
ATOM   2382  CD  ARG A 313       7.135  67.991  31.784  1.00 24.41           C  
ANISOU 2382  CD  ARG A 313     4444   2283   2545     83    986    159       C  
ATOM   2383  NE  ARG A 313       7.251  66.866  32.714  1.00 25.46           N  
ANISOU 2383  NE  ARG A 313     4553   2420   2699     74    973    146       N  
ATOM   2384  CZ  ARG A 313       6.808  65.627  32.488  1.00 26.68           C  
ANISOU 2384  CZ  ARG A 313     4692   2574   2870     76    931    141       C  
ATOM   2385  NH1 ARG A 313       6.167  65.323  31.366  1.00 23.34           N  
ANISOU 2385  NH1 ARG A 313     4279   2142   2444     91    884    142       N  
ATOM   2386  NH2 ARG A 313       6.978  64.709  33.429  1.00 26.29           N  
ANISOU 2386  NH2 ARG A 313     4618   2526   2842     69    931    134       N  
ATOM   2387  N   GLN A 314       8.701  71.225  27.339  1.00 25.58           N  
ANISOU 2387  N   GLN A 314     4723   2425   2570    176   1108    234       N  
ATOM   2388  CA  GLN A 314       8.205  72.252  26.406  1.00 26.71           C  
ANISOU 2388  CA  GLN A 314     4901   2561   2686    210   1128    267       C  
ATOM   2389  C   GLN A 314       8.891  72.132  25.032  1.00 28.51           C  
ANISOU 2389  C   GLN A 314     5183   2794   2853    270   1164    289       C  
ATOM   2390  O   GLN A 314       8.547  72.842  24.109  1.00 27.91           O  
ANISOU 2390  O   GLN A 314     5148   2714   2739    314   1183    317       O  
ATOM   2391  CB  GLN A 314       8.482  73.645  26.966  1.00 28.52           C  
ANISOU 2391  CB  GLN A 314     5100   2770   2965    184   1178    292       C  
ATOM   2392  CG  GLN A 314       7.755  73.999  28.268  1.00 28.43           C  
ANISOU 2392  CG  GLN A 314     5055   2749   2998    145   1151    276       C  
ATOM   2393  CD  GLN A 314       6.256  73.910  28.143  1.00 30.75           C  
ANISOU 2393  CD  GLN A 314     5357   3047   3278    159   1105    278       C  
ATOM   2394  OE1 GLN A 314       5.692  74.134  27.078  1.00 30.92           O  
ANISOU 2394  OE1 GLN A 314     5412   3071   3266    193   1093    294       O  
ATOM   2395  NE2 GLN A 314       5.597  73.546  29.233  1.00 30.90           N  
ANISOU 2395  NE2 GLN A 314     5347   3065   3329    138   1078    265       N  
ATOM   2396  N   ASN A 315       9.918  71.284  24.916  1.00 26.06           N  
ANISOU 2396  N   ASN A 315     4875   2492   2531    279   1185    281       N  
ATOM   2397  CA  ASN A 315      10.604  71.028  23.633  1.00 26.45           C  
ANISOU 2397  CA  ASN A 315     4987   2548   2515    352   1229    306       C  
ATOM   2398  C   ASN A 315      11.225  72.343  23.143  1.00 27.87           C  
ANISOU 2398  C   ASN A 315     5164   2711   2713    374   1326    370       C  
ATOM   2399  O   ASN A 315      11.112  72.699  21.966  1.00 27.11           O  
ANISOU 2399  O   ASN A 315     5133   2614   2551    448   1359    405       O  
ATOM   2400  CB  ASN A 315       9.676  70.391  22.587  1.00 26.07           C  
ANISOU 2400  CB  ASN A 315     5020   2506   2378    418   1158    284       C  
ATOM   2401  CG  ASN A 315      10.388  69.832  21.366  1.00 29.52           C  
ANISOU 2401  CG  ASN A 315     5540   2948   2728    509   1192    297       C  
ATOM   2402  OD1 ASN A 315      11.587  69.563  21.416  1.00 32.98           O  
ANISOU 2402  OD1 ASN A 315     6064   3383   3081    585   1146    288       O  
ATOM   2403  ND2 ASN A 315       9.685  69.664  20.258  1.00 28.45           N  
ANISOU 2403  ND2 ASN A 315     5383   2816   2608    510   1267    319       N  
ATOM   2404  N   ASP A 316      11.914  73.026  24.059  1.00 27.18           N  
ANISOU 2404  N   ASP A 316     5003   2603   2719    314   1366    386       N  
ATOM   2405  CA  ASP A 316      12.390  74.408  23.857  1.00 28.06           C  
ANISOU 2405  CA  ASP A 316     5090   2686   2886    316   1444    445       C  
ATOM   2406  C   ASP A 316      13.922  74.420  23.946  1.00 27.55           C  
ANISOU 2406  C   ASP A 316     4974   2597   2895    309   1520    485       C  
ATOM   2407  O   ASP A 316      14.484  74.456  25.065  1.00 28.06           O  
ANISOU 2407  O   ASP A 316     4970   2641   3049    243   1500    464       O  
ATOM   2408  CB  ASP A 316      11.750  75.369  24.874  1.00 27.88           C  
ANISOU 2408  CB  ASP A 316     5022   2643   2926    255   1410    429       C  
ATOM   2409  CG  ASP A 316      12.057  76.849  24.642  1.00 29.53           C  
ANISOU 2409  CG  ASP A 316     5208   2815   3196    256   1475    486       C  
ATOM   2410  OD1 ASP A 316      13.172  77.178  24.209  1.00 29.59           O  
ANISOU 2410  OD1 ASP A 316     5191   2797   3253    273   1553    540       O  
ATOM   2411  OD2 ASP A 316      11.175  77.661  24.910  1.00 35.34           O  
ANISOU 2411  OD2 ASP A 316     5947   3543   3937    242   1450    481       O  
ATOM   2412  N   LEU A 317      14.587  74.423  22.785  1.00 25.88           N  
ANISOU 2412  N   LEU A 317     4797   2383   2650    383   1606    546       N  
ATOM   2413  CA  LEU A 317      16.032  74.232  22.767  1.00 26.50           C  
ANISOU 2413  CA  LEU A 317     4826   2440   2803    386   1683    593       C  
ATOM   2414  C   LEU A 317      16.781  75.380  23.471  1.00 26.56           C  
ANISOU 2414  C   LEU A 317     4734   2391   2965    326   1719    633       C  
ATOM   2415  O   LEU A 317      17.764  75.136  24.203  1.00 24.69           O  
ANISOU 2415  O   LEU A 317     4423   2127   2828    279   1718    630       O  
ATOM   2416  CB  LEU A 317      16.507  74.094  21.323  1.00 28.37           C  
ANISOU 2416  CB  LEU A 317     5128   2682   2967    495   1784    664       C  
ATOM   2417  CG  LEU A 317      18.022  73.981  21.159  1.00 29.49           C  
ANISOU 2417  CG  LEU A 317     5213   2795   3195    514   1889    736       C  
ATOM   2418  CD1 LEU A 317      18.571  72.786  21.903  1.00 28.84           C  
ANISOU 2418  CD1 LEU A 317     5098   2726   3133    471   1840    683       C  
ATOM   2419  CD2 LEU A 317      18.402  73.919  19.688  1.00 31.59           C  
ANISOU 2419  CD2 LEU A 317     5558   3066   3377    643   2005    818       C  
ATOM   2420  N   LEU A 318      16.353  76.632  23.239  1.00 25.70           N  
ANISOU 2420  N   LEU A 318     4622   2258   2885    329   1745    669       N  
ATOM   2421  CA  LEU A 318      16.994  77.768  23.898  1.00 26.54           C  
ANISOU 2421  CA  LEU A 318     4636   2299   3146    272   1763    702       C  
ATOM   2422  C   LEU A 318      16.942  77.611  25.421  1.00 24.91           C  
ANISOU 2422  C   LEU A 318     4382   2080   3002    185   1656    620       C  
ATOM   2423  O   LEU A 318      17.933  77.915  26.124  1.00 24.87           O  
ANISOU 2423  O   LEU A 318     4295   2019   3132    139   1650    629       O  
ATOM   2424  CB  LEU A 318      16.304  79.070  23.482  1.00 27.67           C  
ANISOU 2424  CB  LEU A 318     4795   2423   3293    288   1789    739       C  
ATOM   2425  CG  LEU A 318      16.646  79.559  22.079  1.00 29.23           C  
ANISOU 2425  CG  LEU A 318     5022   2611   3470    376   1915    843       C  
ATOM   2426  CD1 LEU A 318      15.712  80.672  21.676  1.00 29.61           C  
ANISOU 2426  CD1 LEU A 318     5105   2654   3490    395   1922    863       C  
ATOM   2427  CD2 LEU A 318      18.103  79.986  21.964  1.00 30.72           C  
ANISOU 2427  CD2 LEU A 318     5119   2737   3816    375   2013    933       C  
ATOM   2428  N   ALA A 319      15.786  77.183  25.925  1.00 23.79           N  
ANISOU 2428  N   ALA A 319     4289   1980   2769    170   1572    547       N  
ATOM   2429  CA  ALA A 319      15.609  77.036  27.378  1.00 24.65           C  
ANISOU 2429  CA  ALA A 319     4370   2079   2915    106   1479    474       C  
ATOM   2430  C   ALA A 319      16.515  75.916  27.905  1.00 24.10           C  
ANISOU 2430  C   ALA A 319     4270   2014   2871     86   1458    446       C  
ATOM   2431  O   ALA A 319      17.082  76.053  29.002  1.00 23.85           O  
ANISOU 2431  O   ALA A 319     4189   1944   2925     39   1407    414       O  
ATOM   2432  CB  ALA A 319      14.156  76.816  27.720  1.00 24.50           C  
ANISOU 2432  CB  ALA A 319     4406   2101   2801    105   1415    420       C  
ATOM   2433  N   VAL A 320      16.734  74.864  27.100  1.00 23.57           N  
ANISOU 2433  N   VAL A 320     4234   1987   2733    128   1495    459       N  
ATOM   2434  CA  VAL A 320      17.661  73.811  27.530  1.00 25.06           C  
ANISOU 2434  CA  VAL A 320     4392   2179   2950    112   1483    439       C  
ATOM   2435  C   VAL A 320      19.084  74.365  27.590  1.00 24.45           C  
ANISOU 2435  C   VAL A 320     4231   2040   3018     96   1534    495       C  
ATOM   2436  O   VAL A 320      19.785  74.113  28.575  1.00 23.78           O  
ANISOU 2436  O   VAL A 320     4092   1926   3014     50   1484    463       O  
ATOM   2437  CB  VAL A 320      17.612  72.531  26.661  1.00 25.30           C  
ANISOU 2437  CB  VAL A 320     4478   2260   2873    166   1507    439       C  
ATOM   2438  CG1 VAL A 320      18.584  71.502  27.190  1.00 25.66           C  
ANISOU 2438  CG1 VAL A 320     4486   2306   2956    146   1495    419       C  
ATOM   2439  CG2 VAL A 320      16.210  71.939  26.605  1.00 25.73           C  
ANISOU 2439  CG2 VAL A 320     4603   2362   2810    179   1441    385       C  
ATOM   2440  N   MET A 321      19.476  75.122  26.554  1.00 25.98           N  
ANISOU 2440  N   MET A 321     4413   2208   3250    137   1631    581       N  
ATOM   2441  CA  MET A 321      20.794  75.763  26.479  1.00 27.02           C  
ANISOU 2441  CA  MET A 321     4451   2268   3545    127   1694    656       C  
ATOM   2442  C   MET A 321      21.042  76.622  27.722  1.00 27.49           C  
ANISOU 2442  C   MET A 321     4441   2261   3743     52   1609    620       C  
ATOM   2443  O   MET A 321      22.113  76.548  28.320  1.00 27.97           O  
ANISOU 2443  O   MET A 321     4422   2268   3936     16   1585    624       O  
ATOM   2444  CB  MET A 321      20.931  76.639  25.234  1.00 28.24           C  
ANISOU 2444  CB  MET A 321     4609   2402   3719    187   1815    760       C  
ATOM   2445  CG  MET A 321      20.939  75.834  23.954  1.00 29.90           C  
ANISOU 2445  CG  MET A 321     4893   2663   3802    280   1907    806       C  
ATOM   2446  SD  MET A 321      20.978  76.817  22.440  1.00 31.21           S  
ANISOU 2446  SD  MET A 321     5090   2812   3956    376   2056    932       S  
ATOM   2447  CE  MET A 321      22.641  77.474  22.540  1.00 32.29           C  
ANISOU 2447  CE  MET A 321     5079   2852   4335    357   2153   1044       C  
ATOM   2448  N   ILE A 322      20.046  77.440  28.076  1.00 26.66           N  
ANISOU 2448  N   ILE A 322     4369   2154   3606     35   1559    585       N  
ATOM   2449  CA  ILE A 322      20.127  78.357  29.201  1.00 27.29           C  
ANISOU 2449  CA  ILE A 322     4406   2167   3794    -18   1472    545       C  
ATOM   2450  C   ILE A 322      20.205  77.561  30.503  1.00 25.92           C  
ANISOU 2450  C   ILE A 322     4238   2001   3606    -55   1363    453       C  
ATOM   2451  O   ILE A 322      21.039  77.865  31.373  1.00 26.58           O  
ANISOU 2451  O   ILE A 322     4262   2015   3820    -92   1297    432       O  
ATOM   2452  CB  ILE A 322      18.938  79.332  29.172  1.00 27.96           C  
ANISOU 2452  CB  ILE A 322     4541   2257   3823    -13   1456    532       C  
ATOM   2453  CG1 ILE A 322      19.079  80.331  28.024  1.00 28.02           C  
ANISOU 2453  CG1 ILE A 322     4528   2235   3883     18   1559    630       C  
ATOM   2454  CG2 ILE A 322      18.761  80.039  30.517  1.00 28.76           C  
ANISOU 2454  CG2 ILE A 322     4633   2306   3987    -58   1345    464       C  
ATOM   2455  CD1 ILE A 322      17.786  80.951  27.593  1.00 28.64           C  
ANISOU 2455  CD1 ILE A 322     4675   2348   3857     44   1570    628       C  
ATOM   2456  N   ALA A 323      19.374  76.515  30.610  1.00 25.62           N  
ANISOU 2456  N   ALA A 323     4271   2042   3419    -39   1341    402       N  
ATOM   2457  CA  ALA A 323      19.347  75.678  31.797  1.00 25.89           C  
ANISOU 2457  CA  ALA A 323     4320   2092   3424    -62   1252    323       C  
ATOM   2458  C   ALA A 323      20.738  75.071  32.053  1.00 28.10           C  
ANISOU 2458  C   ALA A 323     4534   2339   3804    -80   1245    331       C  
ATOM   2459  O   ALA A 323      21.189  75.051  33.191  1.00 28.76           O  
ANISOU 2459  O   ALA A 323     4595   2381   3948   -109   1157    279       O  
ATOM   2460  CB  ALA A 323      18.301  74.616  31.650  1.00 25.80           C  
ANISOU 2460  CB  ALA A 323     4380   2164   3258    -38   1250    289       C  
ATOM   2461  N   ASP A 324      21.435  74.636  30.987  1.00 27.93           N  
ANISOU 2461  N   ASP A 324     4481   2327   3800    -56   1338    399       N  
ATOM   2462  CA  ASP A 324      22.767  74.051  31.118  1.00 29.13           C  
ANISOU 2462  CA  ASP A 324     4564   2448   4056    -68   1347    420       C  
ATOM   2463  C   ASP A 324      23.786  75.111  31.536  1.00 29.10           C  
ANISOU 2463  C   ASP A 324     4463   2339   4254   -104   1319    452       C  
ATOM   2464  O   ASP A 324      24.658  74.834  32.322  1.00 31.27           O  
ANISOU 2464  O   ASP A 324     4684   2568   4629   -133   1253    426       O  
ATOM   2465  CB  ASP A 324      23.189  73.347  29.829  1.00 31.91           C  
ANISOU 2465  CB  ASP A 324     4919   2838   4368    -18   1465    493       C  
ATOM   2466  CG  ASP A 324      22.552  71.975  29.654  1.00 37.27           C  
ANISOU 2466  CG  ASP A 324     5676   3602   4882      9   1458    446       C  
ATOM   2467  OD1 ASP A 324      21.976  71.463  30.641  1.00 39.28           O  
ANISOU 2467  OD1 ASP A 324     5962   3881   5078    -17   1366    365       O  
ATOM   2468  OD2 ASP A 324      22.651  71.409  28.542  1.00 41.41           O  
ANISOU 2468  OD2 ASP A 324     6232   4162   5338     64   1544    494       O  
ATOM   2469  N   LYS A 325      23.677  76.323  30.992  1.00 30.45           N  
ANISOU 2469  N   LYS A 325     4610   2466   4494    -99   1365    510       N  
ATOM   2470  CA  LYS A 325      24.550  77.439  31.396  1.00 31.46           C  
ANISOU 2470  CA  LYS A 325     4641   2479   4832   -136   1326    539       C  
ATOM   2471  C   LYS A 325      24.386  77.750  32.897  1.00 32.41           C  
ANISOU 2471  C   LYS A 325     4777   2554   4981   -176   1165    435       C  
ATOM   2472  O   LYS A 325      25.364  78.113  33.522  1.00 35.38           O  
ANISOU 2472  O   LYS A 325     5075   2838   5529   -208   1091    430       O  
ATOM   2473  CB  LYS A 325      24.338  78.652  30.483  1.00 33.28           C  
ANISOU 2473  CB  LYS A 325     4851   2675   5118   -118   1413    624       C  
ATOM   2474  CG  LYS A 325      25.238  78.626  29.247  1.00 36.80           C  
ANISOU 2474  CG  LYS A 325     5228   3102   5652    -81   1562    753       C  
ATOM   2475  CD  LYS A 325      24.890  79.572  28.159  1.00 39.71           C  
ANISOU 2475  CD  LYS A 325     5601   3462   6024    -41   1674    844       C  
ATOM   2476  CE  LYS A 325      25.530  79.187  26.839  1.00 44.12           C  
ANISOU 2476  CE  LYS A 325     6139   4037   6587     27   1841    965       C  
ATOM   2477  NZ  LYS A 325      27.011  79.191  26.907  1.00 46.53           N  
ANISOU 2477  NZ  LYS A 325     6310   4253   7114     10   1877   1043       N  
ATOM   2478  N   LEU A 326      23.183  77.612  33.467  1.00 29.60           N  
ANISOU 2478  N   LEU A 326     4522   2257   4466   -166   1110    356       N  
ATOM   2479  CA  LEU A 326      22.938  77.935  34.892  1.00 33.64           C  
ANISOU 2479  CA  LEU A 326     5071   2729   4981   -183    967    260       C  
ATOM   2480  C   LEU A 326      23.265  76.756  35.816  1.00 38.80           C  
ANISOU 2480  C   LEU A 326     5745   3407   5587   -185    893    192       C  
ATOM   2481  O   LEU A 326      23.455  76.971  37.005  1.00 40.98           O  
ANISOU 2481  O   LEU A 326     6039   3631   5898   -191    771    120       O  
ATOM   2482  CB  LEU A 326      21.482  78.346  35.087  1.00 33.11           C  
ANISOU 2482  CB  LEU A 326     5100   2711   4769   -161    958    221       C  
ATOM   2483  CG  LEU A 326      21.083  79.611  34.342  1.00 33.05           C  
ANISOU 2483  CG  LEU A 326     5080   2673   4805   -158   1013    277       C  
ATOM   2484  CD1 LEU A 326      19.590  79.838  34.425  1.00 33.56           C  
ANISOU 2484  CD1 LEU A 326     5239   2797   4714   -132   1017    245       C  
ATOM   2485  CD2 LEU A 326      21.843  80.787  34.895  1.00 37.22           C  
ANISOU 2485  CD2 LEU A 326     5547   3077   5517   -186    932    273       C  
ATOM   2486  N   LEU A 327      23.297  75.526  35.286  1.00 40.89           N  
ANISOU 2486  N   LEU A 327     6019   3751   5766   -171    963    211       N  
ATOM   2487  CA  LEU A 327      23.728  74.366  36.084  1.00 44.67           C  
ANISOU 2487  CA  LEU A 327     6508   4251   6215   -174    903    156       C  
ATOM   2488  C   LEU A 327      25.256  74.369  36.204  1.00 50.38           C  
ANISOU 2488  C   LEU A 327     7125   4891   7123   -201    874    183       C  
ATOM   2489  O   LEU A 327      25.969  75.181  35.620  1.00 56.83           O  
ANISOU 2489  O   LEU A 327     7858   5638   8097   -217    910    252       O  
ATOM   2490  CB  LEU A 327      23.251  73.068  35.433  1.00 43.05           C  
ANISOU 2490  CB  LEU A 327     6342   4147   5865   -150    984    169       C  
ATOM   2491  CG  LEU A 327      21.775  72.748  35.622  1.00 42.68           C  
ANISOU 2491  CG  LEU A 327     6393   4177   5647   -126    982    127       C  
ATOM   2492  CD1 LEU A 327      21.298  71.800  34.535  1.00 39.89           C  
ANISOU 2492  CD1 LEU A 327     6064   3904   5187   -103   1073    162       C  
ATOM   2493  CD2 LEU A 327      21.526  72.167  37.004  1.00 40.54           C  
ANISOU 2493  CD2 LEU A 327     6171   3914   5319   -120    887     47       C  
ATOM   2494  OXT LEU A 327      25.826  73.534  36.897  1.00 57.18           O  
ANISOU 2494  OXT LEU A 327     7980   5751   7994   -206    813    142       O  
TER    2495      LEU A 327                                                      
ATOM   2496  N   MET B   1      48.172 109.330 -16.993  1.00 63.01           N  
ATOM   2497  CA  MET B   1      47.514 108.553 -15.894  1.00 51.66           C  
ATOM   2498  C   MET B   1      48.270 108.798 -14.579  1.00 41.45           C  
ATOM   2499  O   MET B   1      49.435 108.408 -14.411  1.00 40.14           O  
ATOM   2500  CB  MET B   1      47.489 107.051 -16.206  1.00 53.83           C  
ATOM   2501  CG  MET B   1      46.405 106.285 -15.453  1.00 60.15           C  
ATOM   2502  SD  MET B   1      46.846 104.549 -15.138  1.00 71.73           S  
ATOM   2503  CE  MET B   1      45.264 103.863 -14.650  1.00 76.12           C  
ATOM   2504  N   LYS B   2      47.578 109.432 -13.634  1.00 32.50           N  
ATOM   2505  CA  LYS B   2      48.101 109.696 -12.301  1.00 28.08           C  
ATOM   2506  C   LYS B   2      48.329 108.368 -11.560  1.00 26.86           C  
ATOM   2507  O   LYS B   2      47.665 107.371 -11.814  1.00 26.82           O  
ATOM   2508  CB  LYS B   2      47.116 110.576 -11.527  1.00 32.14           C  
ATOM   2509  CG  LYS B   2      46.808 111.939 -12.143  1.00 35.75           C  
ATOM   2510  CD  LYS B   2      47.867 112.963 -11.858  1.00 40.79           C  
ATOM   2511  CE  LYS B   2      47.630 114.268 -12.584  1.00 48.48           C  
ATOM   2512  NZ  LYS B   2      48.801 115.162 -12.441  1.00 55.49           N  
ATOM   2513  N   LYS B   3      49.294 108.367 -10.643  1.00 23.06           N  
ATOM   2514  CA  LYS B   3      49.476 107.269  -9.718  1.00 21.69           C  
ATOM   2515  C   LYS B   3      48.282 107.182  -8.753  1.00 24.16           C  
ATOM   2516  O   LYS B   3      47.735 106.082  -8.540  1.00 19.53           O  
ATOM   2517  CB  LYS B   3      50.786 107.455  -8.952  1.00 24.33           C  
ATOM   2518  CG  LYS B   3      52.031 107.317  -9.809  1.00 28.85           C  
ATOM   2519  CD  LYS B   3      53.307 107.422  -9.025  1.00 28.66           C  
ATOM   2520  CE  LYS B   3      54.526 107.247  -9.907  1.00 31.10           C  
ATOM   2521  NZ  LYS B   3      55.769 107.352  -9.113  1.00 34.71           N  
ATOM   2522  N   VAL B   4      47.859 108.328  -8.192  1.00 19.26           N  
ATOM   2523  CA  VAL B   4      46.824 108.347  -7.117  1.00 20.10           C  
ATOM   2524  C   VAL B   4      45.889 109.539  -7.281  1.00 22.76           C  
ATOM   2525  O   VAL B   4      46.342 110.670  -7.507  1.00 24.58           O  
ATOM   2526  CB  VAL B   4      47.463 108.380  -5.718  1.00 21.02           C  
ATOM   2527  CG1 VAL B   4      46.409 108.314  -4.613  1.00 22.40           C  
ATOM   2528  CG2 VAL B   4      48.482 107.269  -5.555  1.00 19.95           C  
ATOM   2529  N   SER B   5      44.582 109.275  -7.147  1.00 22.52           N  
ATOM   2530  CA  SER B   5      43.571 110.308  -6.908  1.00 23.86           C  
ATOM   2531  C   SER B   5      43.141 110.233  -5.442  1.00 26.63           C  
ATOM   2532  O   SER B   5      42.607 109.196  -5.027  1.00 21.46           O  
ATOM   2533  CB  SER B   5      42.373 110.146  -7.804  1.00 25.50           C  
ATOM   2534  OG  SER B   5      42.749 110.161  -9.170  1.00 30.63           O  
ATOM   2535  N   VAL B   6      43.383 111.307  -4.679  1.00 19.68           N  
ATOM   2536  CA  VAL B   6      42.791 111.459  -3.366  1.00 22.25           C  
ATOM   2537  C   VAL B   6      41.407 112.084  -3.545  1.00 26.94           C  
ATOM   2538  O   VAL B   6      41.268 113.134  -4.171  1.00 23.83           O  
ATOM   2539  CB  VAL B   6      43.667 112.287  -2.413  1.00 22.46           C  
ATOM   2540  CG1 VAL B   6      43.051 112.377  -1.020  1.00 21.15           C  
ATOM   2541  CG2 VAL B   6      45.086 111.756  -2.358  1.00 22.64           C  
ATOM   2542  N   ILE B   7      40.385 111.425  -2.989  1.00 22.04           N  
ATOM   2543  CA  ILE B   7      39.004 111.859  -3.120  1.00 23.64           C  
ATOM   2544  C   ILE B   7      38.505 112.311  -1.739  1.00 25.26           C  
ATOM   2545  O   ILE B   7      38.490 111.526  -0.792  1.00 23.03           O  
ATOM   2546  CB  ILE B   7      38.134 110.743  -3.727  1.00 23.40           C  
ATOM   2547  CG1 ILE B   7      38.588 110.402  -5.149  1.00 24.89           C  
ATOM   2548  CG2 ILE B   7      36.657 111.116  -3.675  1.00 24.36           C  
ATOM   2549  CD1 ILE B   7      37.961 109.153  -5.715  1.00 23.93           C  
ATOM   2550  N   MET B   8      38.107 113.588  -1.629  1.00 22.89           N  
ATOM   2551  CA  MET B   8      37.730 114.161  -0.342  1.00 27.26           C  
ATOM   2552  C   MET B   8      36.377 114.860  -0.447  1.00 29.91           C  
ATOM   2553  O   MET B   8      36.259 115.902  -1.091  1.00 29.75           O  
ATOM   2554  CB  MET B   8      38.779 115.149   0.166  1.00 26.75           C  
ATOM   2555  CG  MET B   8      38.462 115.673   1.563  1.00 29.57           C  
ATOM   2556  SD  MET B   8      39.732 116.762   2.215  1.00 33.56           S  
ATOM   2557  CE  MET B   8      39.556 118.130   1.073  1.00 32.82           C  
ATOM   2558  N   PRO B   9      35.320 114.296   0.180  1.00 28.53           N  
ATOM   2559  CA  PRO B   9      34.054 115.007   0.372  1.00 28.44           C  
ATOM   2560  C   PRO B   9      34.182 116.129   1.408  1.00 24.14           C  
ATOM   2561  O   PRO B   9      34.930 115.995   2.398  1.00 24.32           O  
ATOM   2562  CB  PRO B   9      33.088 113.930   0.910  1.00 29.20           C  
ATOM   2563  CG  PRO B   9      33.774 112.624   0.603  1.00 28.58           C  
ATOM   2564  CD  PRO B   9      35.254 112.924   0.711  1.00 28.83           C  
ATOM   2565  N   THR B  10      33.467 117.233   1.178  1.00 26.94           N  
ATOM   2566  CA  THR B  10      33.415 118.334   2.170  1.00 27.59           C  
ATOM   2567  C   THR B  10      31.963 118.740   2.432  1.00 24.23           C  
ATOM   2568  O   THR B  10      31.095 118.584   1.568  1.00 24.08           O  
ATOM   2569  CB  THR B  10      34.240 119.552   1.721  1.00 27.92           C  
ATOM   2570  OG1 THR B  10      33.720 120.022   0.478  1.00 28.48           O  
ATOM   2571  CG2 THR B  10      35.710 119.234   1.571  1.00 28.16           C  
ATOM   2572  N   PHE B  11      31.743 119.306   3.620  1.00 29.82           N  
ATOM   2573  CA  PHE B  11      30.487 119.947   3.984  1.00 32.95           C  
ATOM   2574  C   PHE B  11      30.713 120.752   5.262  1.00 32.98           C  
ATOM   2575  O   PHE B  11      31.011 120.171   6.305  1.00 31.21           O  
ATOM   2576  CB  PHE B  11      29.363 118.930   4.195  1.00 37.86           C  
ATOM   2577  CG  PHE B  11      28.073 119.534   4.685  1.00 40.48           C  
ATOM   2578  CD1 PHE B  11      27.149 120.049   3.789  1.00 44.29           C  
ATOM   2579  CD2 PHE B  11      27.789 119.606   6.041  1.00 42.56           C  
ATOM   2580  CE1 PHE B  11      25.962 120.611   4.238  1.00 47.51           C  
ATOM   2581  CE2 PHE B  11      26.603 120.171   6.489  1.00 44.86           C  
ATOM   2582  CZ  PHE B  11      25.691 120.672   5.587  1.00 44.62           C  
ATOM   2583  N   ASN B  12      30.609 122.084   5.134  1.00 31.44           N  
ATOM   2584  CA  ASN B  12      30.617 123.054   6.236  1.00 33.34           C  
ATOM   2585  C   ASN B  12      31.827 122.833   7.142  1.00 32.23           C  
ATOM   2586  O   ASN B  12      31.719 122.973   8.356  1.00 38.92           O  
ATOM   2587  CB  ASN B  12      29.324 123.017   7.055  1.00 40.44           C  
ATOM   2588  CG  ASN B  12      28.124 123.543   6.296  1.00 41.99           C  
ATOM   2589  OD1 ASN B  12      28.215 123.857   5.111  1.00 39.33           O  
ATOM   2590  ND2 ASN B  12      26.988 123.636   6.972  1.00 40.89           N  
ATOM   2591  N   ASN B  13      32.981 122.536   6.534  1.00 30.65           N  
ATOM   2592  CA  ASN B  13      34.214 122.284   7.268  1.00 31.46           C  
ATOM   2593  C   ASN B  13      34.882 123.598   7.677  1.00 30.24           C  
ATOM   2594  O   ASN B  13      35.561 123.651   8.699  1.00 33.30           O  
ATOM   2595  CB  ASN B  13      35.198 121.456   6.438  1.00 36.44           C  
ATOM   2596  CG  ASN B  13      34.602 120.142   5.985  1.00 35.86           C  
ATOM   2597  OD1 ASN B  13      33.856 120.081   5.004  1.00 33.41           O  
ATOM   2598  ND2 ASN B  13      34.911 119.089   6.721  1.00 43.84           N  
ATOM   2599  N   GLY B  14      34.744 124.621   6.826  1.00 35.67           N  
ATOM   2600  CA  GLY B  14      35.308 125.944   7.063  1.00 36.14           C  
ATOM   2601  C   GLY B  14      36.826 125.935   7.095  1.00 34.32           C  
ATOM   2602  O   GLY B  14      37.467 125.145   6.396  1.00 38.73           O  
ATOM   2603  N   GLU B  15      37.383 126.805   7.943  1.00 36.73           N  
ATOM   2604  CA  GLU B  15      38.823 127.131   8.020  1.00 42.90           C  
ATOM   2605  C   GLU B  15      39.673 125.883   8.319  1.00 43.58           C  
ATOM   2606  O   GLU B  15      40.817 125.816   7.888  1.00 41.15           O  
ATOM   2607  CB  GLU B  15      39.039 128.236   9.064  1.00 50.37           C  
ATOM   2608  CG  GLU B  15      40.396 128.219   9.754  1.00 56.36           C  
ATOM   2609  CD  GLU B  15      40.572 127.155  10.829  1.00 67.76           C  
ATOM   2610  OE1 GLU B  15      41.710 126.654  10.985  1.00 65.01           O  
ATOM   2611  OE2 GLU B  15      39.573 126.834  11.517  1.00 77.60           O  
ATOM   2612  N   LYS B  16      39.127 124.929   9.084  1.00 40.92           N  
ATOM   2613  CA  LYS B  16      39.799 123.665   9.438  1.00 42.54           C  
ATOM   2614  C   LYS B  16      40.427 123.001   8.201  1.00 34.54           C  
ATOM   2615  O   LYS B  16      41.493 122.410   8.282  1.00 32.82           O  
ATOM   2616  CB  LYS B  16      38.794 122.671  10.036  1.00 42.41           C  
ATOM   2617  CG  LYS B  16      38.477 122.837  11.516  1.00 47.88           C  
ATOM   2618  CD  LYS B  16      37.482 121.818  12.044  1.00 45.36           C  
ATOM   2619  CE  LYS B  16      36.158 121.834  11.304  1.00 51.01           C  
ATOM   2620  NZ  LYS B  16      35.128 121.016  11.985  1.00 65.23           N  
ATOM   2621  N   LEU B  17      39.714 123.085   7.075  1.00 31.08           N  
ATOM   2622  CA  LEU B  17      40.007 122.373   5.844  1.00 32.53           C  
ATOM   2623  C   LEU B  17      41.400 122.724   5.283  1.00 37.04           C  
ATOM   2624  O   LEU B  17      41.991 121.892   4.577  1.00 31.93           O  
ATOM   2625  CB  LEU B  17      38.897 122.728   4.853  1.00 30.58           C  
ATOM   2626  CG  LEU B  17      38.652 121.741   3.727  1.00 30.99           C  
ATOM   2627  CD1 LEU B  17      38.268 120.371   4.282  1.00 32.16           C  
ATOM   2628  CD2 LEU B  17      37.569 122.272   2.808  1.00 29.10           C  
ATOM   2629  N   HIS B  18      41.916 123.933   5.575  1.00 30.21           N  
ATOM   2630  CA  HIS B  18      43.285 124.337   5.170  1.00 37.57           C  
ATOM   2631  C   HIS B  18      44.284 123.230   5.527  1.00 31.65           C  
ATOM   2632  O   HIS B  18      45.107 122.835   4.689  1.00 25.96           O  
ATOM   2633  CB  HIS B  18      43.751 125.654   5.834  1.00 36.38           C  
ATOM   2634  CG  HIS B  18      43.140 126.886   5.258  1.00 54.81           C  
ATOM   2635  ND1 HIS B  18      43.595 127.458   4.082  1.00 65.85           N  
ATOM   2636  CD2 HIS B  18      42.119 127.663   5.690  1.00 55.47           C  
ATOM   2637  CE1 HIS B  18      42.871 128.529   3.810  1.00 66.93           C  
ATOM   2638  NE2 HIS B  18      41.956 128.676   4.783  1.00 58.68           N  
ATOM   2639  N   ARG B  19      44.246 122.791   6.787  1.00 35.44           N  
ANISOU 2639  N   ARG B  19     5339   2696   5429   -203   1770   -585       N  
ATOM   2640  CA  ARG B  19      45.262 121.880   7.305  1.00 37.75           C  
ANISOU 2640  CA  ARG B  19     5688   3108   5544   -271   1641   -644       C  
ATOM   2641  C   ARG B  19      45.164 120.499   6.619  1.00 31.74           C  
ANISOU 2641  C   ARG B  19     4894   2462   4702   -205   1492   -548       C  
ATOM   2642  O   ARG B  19      46.171 119.855   6.337  1.00 28.38           O  
ANISOU 2642  O   ARG B  19     4470   2124   4189   -218   1376   -535       O  
ATOM   2643  CB  ARG B  19      45.131 121.772   8.828  1.00 43.67           C  
ANISOU 2643  CB  ARG B  19     6529   3859   6202   -376   1694   -773       C  
ATOM   2644  CG  ARG B  19      46.386 121.248   9.517  1.00 49.90           C  
ANISOU 2644  CG  ARG B  19     7375   4752   6831   -479   1584   -840       C  
ATOM   2645  CD  ARG B  19      46.475 121.643  10.985  1.00 56.70           C  
ANISOU 2645  CD  ARG B  19     8335   5595   7614   -620   1663   -980       C  
ATOM   2646  NE  ARG B  19      45.514 120.933  11.815  1.00 55.59           N  
ANISOU 2646  NE  ARG B  19     8238   5476   7406   -635   1684  -1008       N  
ATOM   2647  CZ  ARG B  19      45.810 119.910  12.614  1.00 62.81           C  
ANISOU 2647  CZ  ARG B  19     9198   6504   8161   -703   1579  -1029       C  
ATOM   2648  NH1 ARG B  19      44.873 119.379  13.386  1.00 51.80           N  
ANISOU 2648  NH1 ARG B  19     7847   5118   6716   -718   1618  -1059       N  
ATOM   2649  NH2 ARG B  19      47.041 119.427  12.637  1.00 59.13           N  
ANISOU 2649  NH2 ARG B  19     8727   6141   7597   -753   1438  -1012       N  
ATOM   2650  N   THR B  20      43.944 120.065   6.300  1.00 28.51           N  
ANISOU 2650  N   THR B  20     4451   2046   4335   -136   1502   -474       N  
ATOM   2651  CA  THR B  20      43.748 118.816   5.598  1.00 27.45           C  
ANISOU 2651  CA  THR B  20     4288   2010   4132    -81   1377   -387       C  
ATOM   2652  C   THR B  20      44.262 118.933   4.154  1.00 26.24           C  
ANISOU 2652  C   THR B  20     4078   1875   4017    -30   1318   -289       C  
ATOM   2653  O   THR B  20      44.991 118.049   3.695  1.00 23.90           O  
ANISOU 2653  O   THR B  20     3785   1665   3629    -29   1211   -268       O  
ATOM   2654  CB  THR B  20      42.281 118.384   5.602  1.00 29.67           C  
ANISOU 2654  CB  THR B  20     4544   2276   4452    -30   1405   -329       C  
ATOM   2655  OG1 THR B  20      41.878 118.117   6.952  1.00 32.52           O  
ANISOU 2655  OG1 THR B  20     4967   2631   4758    -82   1454   -423       O  
ATOM   2656  CG2 THR B  20      42.017 117.179   4.729  1.00 29.78           C  
ANISOU 2656  CG2 THR B  20     4527   2384   4403     20   1284   -233       C  
ATOM   2657  N   ILE B  21      43.827 119.973   3.435  1.00 25.25           N  
ANISOU 2657  N   ILE B  21     3896   1667   4028      9   1393   -223       N  
ATOM   2658  CA  ILE B  21      44.278 120.169   2.032  1.00 25.42           C  
ANISOU 2658  CA  ILE B  21     3866   1708   4084     49   1342   -123       C  
ATOM   2659  C   ILE B  21      45.805 120.284   2.025  1.00 24.28           C  
ANISOU 2659  C   ILE B  21     3752   1590   3882      6   1302   -186       C  
ATOM   2660  O   ILE B  21      46.476 119.674   1.193  1.00 22.62           O  
ANISOU 2660  O   ILE B  21     3533   1447   3612     18   1215   -141       O  
ATOM   2661  CB  ILE B  21      43.592 121.389   1.400  1.00 27.56           C  
ANISOU 2661  CB  ILE B  21     4067   1879   4526     90   1438    -37       C  
ATOM   2662  CG1 ILE B  21      42.086 121.163   1.252  1.00 26.49           C  
ANISOU 2662  CG1 ILE B  21     3882   1726   4456    136   1459     57       C  
ATOM   2663  CG2 ILE B  21      44.259 121.766   0.077  1.00 27.33           C  
ANISOU 2663  CG2 ILE B  21     3993   1865   4523    112   1394     50       C  
ATOM   2664  CD1 ILE B  21      41.339 122.377   0.811  1.00 28.48           C  
ANISOU 2664  CD1 ILE B  21     4051   1867   4900    175   1566    153       C  
ATOM   2665  N   SER B  22      46.354 121.047   2.974  1.00 25.67           N  
ANISOU 2665  N   SER B  22     3964   1711   4075    -52   1371   -290       N  
ATOM   2666  CA  SER B  22      47.817 121.243   3.049  1.00 26.69           C  
ANISOU 2666  CA  SER B  22     4114   1863   4160   -103   1333   -345       C  
ATOM   2667  C   SER B  22      48.565 119.902   3.217  1.00 25.19           C  
ANISOU 2667  C   SER B  22     3951   1787   3833   -124   1208   -356       C  
ATOM   2668  O   SER B  22      49.610 119.672   2.574  1.00 23.04           O  
ANISOU 2668  O   SER B  22     3662   1551   3539   -122   1146   -329       O  
ATOM   2669  CB  SER B  22      48.188 122.248   4.093  1.00 29.79           C  
ANISOU 2669  CB  SER B  22     4548   2185   4584   -180   1425   -457       C  
ATOM   2670  OG  SER B  22      49.601 122.314   4.211  1.00 36.48           O  
ANISOU 2670  OG  SER B  22     5412   3068   5379   -237   1370   -501       O  
ATOM   2671  N   SER B  23      48.017 118.978   4.025  1.00 24.64           N  
ANISOU 2671  N   SER B  23     3915   1766   3681   -140   1176   -385       N  
ATOM   2672  CA  SER B  23      48.636 117.697   4.257  1.00 22.52           C  
ANISOU 2672  CA  SER B  23     3661   1594   3299   -158   1068   -386       C  
ATOM   2673  C   SER B  23      48.680 116.895   2.958  1.00 22.00           C  
ANISOU 2673  C   SER B  23     3559   1573   3227    -92   1005   -291       C  
ATOM   2674  O   SER B  23      49.603 116.121   2.773  1.00 25.25           O  
ANISOU 2674  O   SER B  23     3967   2040   3586   -101    935   -281       O  
ATOM   2675  CB  SER B  23      47.986 116.910   5.399  1.00 22.33           C  
ANISOU 2675  CB  SER B  23     3679   1611   3195   -190   1053   -431       C  
ATOM   2676  OG  SER B  23      46.770 116.283   5.005  1.00 22.86           O  
ANISOU 2676  OG  SER B  23     3731   1687   3267   -126   1053   -374       O  
ATOM   2677  N   VAL B  24      47.681 117.068   2.083  1.00 21.13           N  
ANISOU 2677  N   VAL B  24     3420   1438   3169    -34   1033   -220       N  
ATOM   2678  CA  VAL B  24      47.633 116.354   0.808  1.00 21.28           C  
ANISOU 2678  CA  VAL B  24     3416   1502   3167      8    979   -133       C  
ATOM   2679  C   VAL B  24      48.632 116.974  -0.197  1.00 22.28           C  
ANISOU 2679  C   VAL B  24     3520   1609   3336     12    983   -101       C  
ATOM   2680  O   VAL B  24      49.311 116.254  -0.922  1.00 21.61           O  
ANISOU 2680  O   VAL B  24     3436   1568   3206     16    935    -73       O  
ATOM   2681  CB  VAL B  24      46.195 116.310   0.248  1.00 21.85           C  
ANISOU 2681  CB  VAL B  24     3464   1567   3272     50    994    -56       C  
ATOM   2682  CG1 VAL B  24      46.135 115.654  -1.126  1.00 22.05           C  
ANISOU 2682  CG1 VAL B  24     3475   1643   3260     71    940     31       C  
ATOM   2683  CG2 VAL B  24      45.267 115.570   1.180  1.00 22.17           C  
ANISOU 2683  CG2 VAL B  24     3525   1629   3268     48    987    -84       C  
ATOM   2684  N   LEU B  25      48.703 118.308  -0.242  1.00 21.96           N  
ANISOU 2684  N   LEU B  25     3459   1496   3390     10   1051   -105       N  
ATOM   2685  CA  LEU B  25      49.594 119.016  -1.157  1.00 25.03           C  
ANISOU 2685  CA  LEU B  25     3823   1858   3829     15   1064    -72       C  
ATOM   2686  C   LEU B  25      51.056 118.862  -0.723  1.00 25.33           C  
ANISOU 2686  C   LEU B  25     3876   1912   3833    -25   1034   -136       C  
ATOM   2687  O   LEU B  25      51.924 118.887  -1.582  1.00 26.30           O  
ANISOU 2687  O   LEU B  25     3984   2040   3965    -18   1019   -102       O  
ATOM   2688  CB  LEU B  25      49.173 120.481  -1.238  1.00 24.96           C  
ANISOU 2688  CB  LEU B  25     3781   1758   3942     26   1154    -56       C  
ATOM   2689  CG  LEU B  25      47.781 120.700  -1.819  1.00 27.53           C  
ANISOU 2689  CG  LEU B  25     4067   2063   4328     70   1181     39       C  
ATOM   2690  CD1 LEU B  25      47.482 122.176  -1.942  1.00 29.66           C  
ANISOU 2690  CD1 LEU B  25     4292   2231   4746     85   1280     70       C  
ATOM   2691  CD2 LEU B  25      47.611 120.009  -3.159  1.00 29.18           C  
ANISOU 2691  CD2 LEU B  25     4261   2340   4486     92   1112    144       C  
ATOM   2692  N   ASN B  26      51.312 118.625   0.567  1.00 24.37           N  
ANISOU 2692  N   ASN B  26     3784   1805   3668    -73   1021   -216       N  
ATOM   2693  CA  ASN B  26      52.661 118.432   1.099  1.00 27.47           C  
ANISOU 2693  CA  ASN B  26     4183   2224   4031   -125    978   -260       C  
ATOM   2694  C   ASN B  26      53.016 116.933   1.132  1.00 27.07           C  
ANISOU 2694  C   ASN B  26     4133   2250   3900   -121    898   -237       C  
ATOM   2695  O   ASN B  26      53.066 116.326   2.187  1.00 33.19           O  
ANISOU 2695  O   ASN B  26     4927   3066   4617   -161    859   -274       O  
ATOM   2696  CB  ASN B  26      52.778 119.048   2.499  1.00 32.07           C  
ANISOU 2696  CB  ASN B  26     4796   2785   4603   -201   1004   -351       C  
ATOM   2697  CG  ASN B  26      54.173 118.951   3.093  1.00 38.28           C  
ANISOU 2697  CG  ASN B  26     5580   3604   5359   -272    950   -383       C  
ATOM   2698  OD1 ASN B  26      55.167 119.092   2.383  1.00 42.69           O  
ANISOU 2698  OD1 ASN B  26     6104   4156   5956   -261    933   -348       O  
ATOM   2699  ND2 ASN B  26      54.265 118.757   4.399  1.00 39.35           N  
ANISOU 2699  ND2 ASN B  26     5750   3774   5427   -352    924   -445       N  
ATOM   2700  N   GLN B  27      53.241 116.319  -0.028  1.00 26.53           N  
ANISOU 2700  N   GLN B  27     4049   2200   3832    -78    881   -175       N  
ATOM   2701  CA  GLN B  27      53.590 114.877  -0.102  1.00 26.53           C  
ANISOU 2701  CA  GLN B  27     4048   2256   3775    -71    827   -152       C  
ATOM   2702  C   GLN B  27      55.003 114.726  -0.672  1.00 27.81           C  
ANISOU 2702  C   GLN B  27     4180   2411   3972    -76    820   -127       C  
ATOM   2703  O   GLN B  27      55.419 115.534  -1.516  1.00 26.17           O  
ANISOU 2703  O   GLN B  27     3960   2164   3818    -64    857   -108       O  
ATOM   2704  CB  GLN B  27      52.590 114.139  -0.994  1.00 25.56           C  
ANISOU 2704  CB  GLN B  27     3939   2155   3617    -27    830   -106       C  
ATOM   2705  CG  GLN B  27      51.227 113.920  -0.341  1.00 25.40           C  
ANISOU 2705  CG  GLN B  27     3939   2150   3560    -21    826   -120       C  
ATOM   2706  CD  GLN B  27      51.270 112.980   0.843  1.00 26.17           C  
ANISOU 2706  CD  GLN B  27     4050   2292   3602    -46    782   -156       C  
ATOM   2707  OE1 GLN B  27      51.646 111.810   0.695  1.00 22.65           O  
ANISOU 2707  OE1 GLN B  27     3599   1882   3122    -40    748   -136       O  
ATOM   2708  NE2 GLN B  27      50.856 113.481   2.010  1.00 22.11           N  
ANISOU 2708  NE2 GLN B  27     3552   1770   3079    -78    792   -208       N  
ATOM   2709  N   THR B  28      55.727 113.691  -0.237  1.00 27.33           N  
ANISOU 2709  N   THR B  28     4102   2385   3894    -91    776   -118       N  
ATOM   2710  CA  THR B  28      57.010 113.304  -0.849  1.00 27.23           C  
ANISOU 2710  CA  THR B  28     4053   2360   3931    -86    780    -80       C  
ATOM   2711  C   THR B  28      56.813 112.879  -2.310  1.00 28.81           C  
ANISOU 2711  C   THR B  28     4269   2544   4131    -43    828    -43       C  
ATOM   2712  O   THR B  28      57.731 113.039  -3.126  1.00 29.07           O  
ANISOU 2712  O   THR B  28     4284   2545   4216    -37    863    -19       O  
ATOM   2713  CB  THR B  28      57.721 112.210  -0.060  1.00 28.05           C  
ANISOU 2713  CB  THR B  28     4123   2499   4034   -108    729    -59       C  
ATOM   2714  OG1 THR B  28      56.829 111.096   0.081  1.00 27.28           O  
ANISOU 2714  OG1 THR B  28     4049   2437   3878    -87    717    -55       O  
ATOM   2715  CG2 THR B  28      58.203 112.704   1.284  1.00 29.66           C  
ANISOU 2715  CG2 THR B  28     4307   2726   4233   -175    674    -83       C  
ATOM   2716  N   MET B  29      55.637 112.322  -2.644  1.00 26.15           N  
ANISOU 2716  N   MET B  29     3969   2231   3733    -23    832    -40       N  
ATOM   2717  CA  MET B  29      55.301 112.012  -4.039  1.00 26.04           C  
ANISOU 2717  CA  MET B  29     3983   2212   3696     -5    873     -8       C  
ATOM   2718  C   MET B  29      55.341 113.316  -4.865  1.00 25.87           C  
ANISOU 2718  C   MET B  29     3961   2157   3710     -3    908     10       C  
ATOM   2719  O   MET B  29      54.830 114.329  -4.462  1.00 25.70           O  
ANISOU 2719  O   MET B  29     3932   2122   3708     -2    903      1       O  
ATOM   2720  CB  MET B  29      53.926 111.344  -4.153  1.00 23.41           C  
ANISOU 2720  CB  MET B  29     3687   1918   3287      1    859     -3       C  
ATOM   2721  CG  MET B  29      53.566 110.901  -5.538  1.00 23.89           C  
ANISOU 2721  CG  MET B  29     3785   1987   3304     -3    893     29       C  
ATOM   2722  SD  MET B  29      51.996 110.018  -5.736  1.00 25.50           S  
ANISOU 2722  SD  MET B  29     4029   2243   3415    -10    868     43       S  
ATOM   2723  CE  MET B  29      52.466 108.369  -5.232  1.00 24.13           C  
ANISOU 2723  CE  MET B  29     3862   2079   3225    -11    872     13       C  
ATOM   2724  N   LYS B  30      55.894 113.233  -6.074  1.00 28.47           N  
ANISOU 2724  N   LYS B  30     4300   2468   4046     -4    952     40       N  
ATOM   2725  CA  LYS B  30      55.940 114.325  -7.010  1.00 29.50           C  
ANISOU 2725  CA  LYS B  30     4430   2572   4203     -4    985     71       C  
ATOM   2726  C   LYS B  30      54.517 114.848  -7.248  1.00 28.59           C  
ANISOU 2726  C   LYS B  30     4330   2480   4054      0    970    103       C  
ATOM   2727  O   LYS B  30      53.618 114.072  -7.527  1.00 25.36           O  
ANISOU 2727  O   LYS B  30     3949   2111   3573     -7    952    119       O  
ATOM   2728  CB  LYS B  30      56.568 113.796  -8.306  1.00 37.86           C  
ANISOU 2728  CB  LYS B  30     5516   3623   5245    -18   1038     96       C  
ATOM   2729  CG  LYS B  30      56.928 114.833  -9.365  1.00 43.61           C  
ANISOU 2729  CG  LYS B  30     6243   4323   6002    -25   1079    134       C  
ATOM   2730  CD  LYS B  30      57.510 114.203 -10.633  1.00 44.60           C  
ANISOU 2730  CD  LYS B  30     6410   4442   6095    -52   1142    150       C  
ATOM   2731  CE  LYS B  30      58.589 113.178 -10.345  1.00 47.04           C  
ANISOU 2731  CE  LYS B  30     6708   4720   6442    -48   1179    117       C  
ATOM   2732  N   SER B  31      54.333 116.177  -7.208  1.00 27.08           N  
ANISOU 2732  N   SER B  31     4111   2255   3923      8    982    120       N  
ATOM   2733  CA  SER B  31      53.001 116.767  -7.213  1.00 27.94           C  
ANISOU 2733  CA  SER B  31     4211   2368   4034     18    974    160       C  
ATOM   2734  C   SER B  31      52.247 116.375  -8.486  1.00 27.77           C  
ANISOU 2734  C   SER B  31     4213   2390   3946      2    965    236       C  
ATOM   2735  O   SER B  31      51.036 116.308  -8.497  1.00 30.45           O  
ANISOU 2735  O   SER B  31     4549   2757   4262      3    940    278       O  
ATOM   2736  CB  SER B  31      53.059 118.288  -7.040  1.00 30.38           C  
ANISOU 2736  CB  SER B  31     4481   2618   4443     30   1009    171       C  
ATOM   2737  OG  SER B  31      53.901 118.835  -8.037  1.00 40.39           O  
ANISOU 2737  OG  SER B  31     5740   3864   5742     25   1039    206       O  
ATOM   2738  N   THR B  32      52.968 116.161  -9.584  1.00 27.95           N  
ANISOU 2738  N   THR B  32     4260   2421   3939    -21    989    259       N  
ATOM   2739  CA  THR B  32      52.328 115.865 -10.881  1.00 30.88           C  
ANISOU 2739  CA  THR B  32     4663   2840   4229    -61    982    332       C  
ATOM   2740  C   THR B  32      51.892 114.391 -10.968  1.00 28.34           C  
ANISOU 2740  C   THR B  32     4393   2570   3802    -91    962    308       C  
ATOM   2741  O   THR B  32      51.159 114.001 -11.865  1.00 27.39           O  
ANISOU 2741  O   THR B  32     4307   2501   3596   -139    945    361       O  
ATOM   2742  CB  THR B  32      53.280 116.226 -12.039  1.00 33.95           C  
ANISOU 2742  CB  THR B  32     5069   3213   4616    -89   1028    359       C  
ATOM   2743  OG1 THR B  32      54.563 115.645 -11.801  1.00 38.05           O  
ANISOU 2743  OG1 THR B  32     5603   3700   5153    -83   1068    287       O  
ATOM   2744  CG2 THR B  32      53.449 117.723 -12.189  1.00 35.40           C  
ANISOU 2744  CG2 THR B  32     5200   3353   4897    -67   1045    408       C  
ATOM   2745  N   ASP B  33      52.335 113.564 -10.023  1.00 27.54           N  
ANISOU 2745  N   ASP B  33     4298   2458   3707    -70    962    232       N  
ATOM   2746  CA  ASP B  33      52.000 112.137 -10.037  1.00 27.11           C  
ANISOU 2746  CA  ASP B  33     4287   2441   3569    -94    955    204       C  
ATOM   2747  C   ASP B  33      50.646 111.850  -9.352  1.00 24.82           C  
ANISOU 2747  C   ASP B  33     3989   2189   3249    -83    899    215       C  
ATOM   2748  O   ASP B  33      50.147 110.741  -9.417  1.00 23.40           O  
ANISOU 2748  O   ASP B  33     3846   2046   2998   -106    887    202       O  
ATOM   2749  CB  ASP B  33      53.084 111.342  -9.312  1.00 33.27           C  
ANISOU 2749  CB  ASP B  33     5064   3191   4386    -74    981    135       C  
ATOM   2750  CG  ASP B  33      54.307 111.003 -10.142  1.00 36.92           C  
ANISOU 2750  CG  ASP B  33     5547   3618   4859    -95   1052    123       C  
ATOM   2751  OD1 ASP B  33      54.230 111.172 -11.355  1.00 37.30           O  
ANISOU 2751  OD1 ASP B  33     5635   3677   4857   -138   1084    155       O  
ATOM   2752  OD2 ASP B  33      55.331 110.606  -9.544  1.00 42.11           O  
ANISOU 2752  OD2 ASP B  33     6178   4239   5583    -73   1075     88       O  
ATOM   2753  N   TYR B  34      50.067 112.819  -8.650  1.00 21.78           N  
ANISOU 2753  N   TYR B  34     3557   1787   2927    -49    876    234       N  
ATOM   2754  CA  TYR B  34      48.775 112.612  -7.972  1.00 23.94           C  
ANISOU 2754  CA  TYR B  34     3819   2086   3189    -36    836    248       C  
ATOM   2755  C   TYR B  34      47.885 113.854  -8.053  1.00 23.46           C  
ANISOU 2755  C   TYR B  34     3709   2008   3194    -20    831    322       C  
ATOM   2756  O   TYR B  34      48.305 114.919  -8.475  1.00 24.25           O  
ANISOU 2756  O   TYR B  34     3782   2073   3356    -14    857    356       O  
ATOM   2757  CB  TYR B  34      49.008 112.195  -6.517  1.00 24.13           C  
ANISOU 2757  CB  TYR B  34     3834   2093   3237     -5    829    169       C  
ATOM   2758  CG  TYR B  34      49.515 113.284  -5.613  1.00 23.67           C  
ANISOU 2758  CG  TYR B  34     3741   1983   3267     19    848    134       C  
ATOM   2759  CD1 TYR B  34      50.864 113.576  -5.531  1.00 24.59           C  
ANISOU 2759  CD1 TYR B  34     3851   2069   3423     17    871     98       C  
ATOM   2760  CD2 TYR B  34      48.651 113.984  -4.793  1.00 24.56           C  
ANISOU 2760  CD2 TYR B  34     3828   2074   3427     38    851    134       C  
ATOM   2761  CE1 TYR B  34      51.343 114.552  -4.671  1.00 23.83           C  
ANISOU 2761  CE1 TYR B  34     3727   1929   3397     24    886     61       C  
ATOM   2762  CE2 TYR B  34      49.102 114.989  -3.953  1.00 24.02           C  
ANISOU 2762  CE2 TYR B  34     3739   1953   3433     45    882     89       C  
ATOM   2763  CZ  TYR B  34      50.451 115.258  -3.876  1.00 24.07           C  
ANISOU 2763  CZ  TYR B  34     3744   1938   3463     34    894     50       C  
ATOM   2764  OH  TYR B  34      50.884 116.215  -3.011  1.00 23.33           O  
ANISOU 2764  OH  TYR B  34     3635   1796   3431     25    921      1       O  
ATOM   2765  N   GLU B  35      46.622 113.679  -7.691  1.00 23.03           N  
ANISOU 2765  N   GLU B  35     3638   1974   3135    -13    801    357       N  
ATOM   2766  CA  GLU B  35      45.638 114.750  -7.712  1.00 24.71           C  
ANISOU 2766  CA  GLU B  35     3793   2163   3432      5    805    442       C  
ATOM   2767  C   GLU B  35      44.727 114.639  -6.465  1.00 23.08           C  
ANISOU 2767  C   GLU B  35     3566   1936   3265     39    807    411       C  
ATOM   2768  O   GLU B  35      44.478 113.559  -5.963  1.00 22.86           O  
ANISOU 2768  O   GLU B  35     3571   1944   3170     34    780    364       O  
ATOM   2769  CB  GLU B  35      44.812 114.674  -8.995  1.00 25.33           C  
ANISOU 2769  CB  GLU B  35     3863   2299   3463    -39    763    566       C  
ATOM   2770  CG  GLU B  35      44.000 113.387  -9.117  1.00 27.12           C  
ANISOU 2770  CG  GLU B  35     4125   2595   3584    -75    712    573       C  
ATOM   2771  CD  GLU B  35      43.123 113.305 -10.365  1.00 31.98           C  
ANISOU 2771  CD  GLU B  35     4733   3278   4139   -141    659    703       C  
ATOM   2772  OE1 GLU B  35      43.114 114.283 -11.125  1.00 37.81           O  
ANISOU 2772  OE1 GLU B  35     5431   4011   4922   -154    659    799       O  
ATOM   2773  OE2 GLU B  35      42.466 112.267 -10.589  1.00 30.99           O  
ANISOU 2773  OE2 GLU B  35     4641   3214   3918   -186    615    712       O  
ATOM   2774  N   LEU B  36      44.265 115.780  -5.968  1.00 21.13           N  
ANISOU 2774  N   LEU B  36     3267   1626   3136     71    850    437       N  
ATOM   2775  CA  LEU B  36      43.265 115.874  -4.922  1.00 22.53           C  
ANISOU 2775  CA  LEU B  36     3420   1771   3369     99    873    425       C  
ATOM   2776  C   LEU B  36      41.960 116.306  -5.601  1.00 24.00           C  
ANISOU 2776  C   LEU B  36     3541   1959   3619    104    862    569       C  
ATOM   2777  O   LEU B  36      41.914 117.380  -6.200  1.00 24.14           O  
ANISOU 2777  O   LEU B  36     3505   1937   3730    112    890    654       O  
ATOM   2778  CB  LEU B  36      43.702 116.926  -3.888  1.00 23.15           C  
ANISOU 2778  CB  LEU B  36     3487   1761   3547    121    952    349       C  
ATOM   2779  CG  LEU B  36      42.706 117.226  -2.767  1.00 23.00           C  
ANISOU 2779  CG  LEU B  36     3448   1687   3602    143   1006    326       C  
ATOM   2780  CD1 LEU B  36      42.206 115.960  -2.080  1.00 23.84           C  
ANISOU 2780  CD1 LEU B  36     3593   1848   3615    137    963    279       C  
ATOM   2781  CD2 LEU B  36      43.316 118.170  -1.735  1.00 24.51           C  
ANISOU 2781  CD2 LEU B  36     3652   1796   3865    140   1091    225       C  
ATOM   2782  N   ILE B  37      40.927 115.467  -5.507  1.00 23.19           N  
ANISOU 2782  N   ILE B  37     3436   1900   3472     97    819    606       N  
ATOM   2783  CA  ILE B  37      39.579 115.776  -6.014  1.00 25.53           C  
ANISOU 2783  CA  ILE B  37     3658   2202   3837     99    800    755       C  
ATOM   2784  C   ILE B  37      38.712 116.101  -4.803  1.00 25.93           C  
ANISOU 2784  C   ILE B  37     3673   2181   3998    145    864    733       C  
ATOM   2785  O   ILE B  37      38.522 115.230  -3.959  1.00 24.76           O  
ANISOU 2785  O   ILE B  37     3568   2051   3788    148    857    647       O  
ATOM   2786  CB  ILE B  37      38.976 114.610  -6.830  1.00 26.37           C  
ANISOU 2786  CB  ILE B  37     3787   2413   3819     46    706    821       C  
ATOM   2787  CG1 ILE B  37      39.938 114.106  -7.915  1.00 26.93           C  
ANISOU 2787  CG1 ILE B  37     3920   2551   3759    -12    662    807       C  
ATOM   2788  CG2 ILE B  37      37.636 115.026  -7.419  1.00 28.08           C  
ANISOU 2788  CG2 ILE B  37     3914   2641   4113     36    674    999       C  
ATOM   2789  CD1 ILE B  37      39.464 112.885  -8.673  1.00 28.47           C  
ANISOU 2789  CD1 ILE B  37     4158   2843   3814    -81    586    842       C  
ATOM   2790  N   ILE B  38      38.256 117.360  -4.705  1.00 25.76           N  
ANISOU 2790  N   ILE B  38     3573   2070   4142    178    939    804       N  
ATOM   2791  CA  ILE B  38      37.388 117.802  -3.614  1.00 26.69           C  
ANISOU 2791  CA  ILE B  38     3653   2099   4388    219   1028    789       C  
ATOM   2792  C   ILE B  38      35.961 117.878  -4.159  1.00 29.17           C  
ANISOU 2792  C   ILE B  38     3871   2418   4795    229   1004    969       C  
ATOM   2793  O   ILE B  38      35.729 118.538  -5.148  1.00 33.29           O  
ANISOU 2793  O   ILE B  38     4317   2939   5389    223    985   1117       O  
ATOM   2794  CB  ILE B  38      37.839 119.141  -3.027  1.00 27.10           C  
ANISOU 2794  CB  ILE B  38     3686   2030   4581    246   1153    736       C  
ATOM   2795  CG1 ILE B  38      39.311 119.111  -2.621  1.00 26.79           C  
ANISOU 2795  CG1 ILE B  38     3732   1996   4448    224   1160    580       C  
ATOM   2796  CG2 ILE B  38      36.927 119.560  -1.871  1.00 29.09           C  
ANISOU 2796  CG2 ILE B  38     3910   2179   4962    278   1268    706       C  
ATOM   2797  CD1 ILE B  38      39.864 120.444  -2.201  1.00 27.64           C  
ANISOU 2797  CD1 ILE B  38     3826   1994   4681    234   1274    529       C  
ATOM   2798  N   ILE B  39      35.020 117.206  -3.481  1.00 29.90           N  
ANISOU 2798  N   ILE B  39     3960   2514   4886    240   1004    961       N  
ATOM   2799  CA  ILE B  39      33.601 117.283  -3.809  1.00 33.76           C  
ANISOU 2799  CA  ILE B  39     4346   2995   5483    252    990   1133       C  
ATOM   2800  C   ILE B  39      32.848 117.856  -2.605  1.00 34.70           C  
ANISOU 2800  C   ILE B  39     4426   2988   5769    305   1126   1101       C  
ATOM   2801  O   ILE B  39      32.744 117.227  -1.570  1.00 31.21           O  
ANISOU 2801  O   ILE B  39     4046   2539   5271    311   1156    977       O  
ATOM   2802  CB  ILE B  39      33.022 115.915  -4.223  1.00 35.95           C  
ANISOU 2802  CB  ILE B  39     4647   3393   5617    210    866   1173       C  
ATOM   2803  CG1 ILE B  39      33.825 115.285  -5.366  1.00 35.30           C  
ANISOU 2803  CG1 ILE B  39     4625   3427   5359    145    754   1178       C  
ATOM   2804  CG2 ILE B  39      31.554 116.067  -4.596  1.00 36.97           C  
ANISOU 2804  CG2 ILE B  39     4659   3517   5870    216    844   1369       C  
ATOM   2805  CD1 ILE B  39      34.833 114.278  -4.913  1.00 39.76           C  
ANISOU 2805  CD1 ILE B  39     5311   4038   5755    128    734    996       C  
ATOM   2806  N   ASP B  40      32.319 119.071  -2.776  1.00 35.67           N  
ANISOU 2806  N   ASP B  40     4441   3007   6103    340   1217   1222       N  
ATOM   2807  CA  ASP B  40      31.594 119.734  -1.744  1.00 35.41           C  
ANISOU 2807  CA  ASP B  40     4364   2834   6254    387   1372   1203       C  
ATOM   2808  C   ASP B  40      30.122 119.354  -1.898  1.00 37.48           C  
ANISOU 2808  C   ASP B  40     4528   3103   6610    404   1344   1366       C  
ATOM   2809  O   ASP B  40      29.535 119.525  -2.997  1.00 35.69           O  
ANISOU 2809  O   ASP B  40     4194   2918   6448    395   1264   1576       O  
ATOM   2810  CB  ASP B  40      31.762 121.251  -1.801  1.00 37.07           C  
ANISOU 2810  CB  ASP B  40     4503   2908   6673    419   1508   1249       C  
ATOM   2811  CG  ASP B  40      31.062 121.945  -0.643  1.00 38.62           C  
ANISOU 2811  CG  ASP B  40     4668   2941   7063    460   1701   1203       C  
ATOM   2812  OD1 ASP B  40      31.530 121.788   0.511  1.00 37.10           O  
ANISOU 2812  OD1 ASP B  40     4585   2712   6798    445   1781    999       O  
ATOM   2813  OD2 ASP B  40      30.030 122.609  -0.898  1.00 40.29           O  
ANISOU 2813  OD2 ASP B  40     4744   3063   7498    500   1772   1376       O  
ATOM   2814  N   ASP B  41      29.547 118.882  -0.780  1.00 37.06           N  
ANISOU 2814  N   ASP B  41     4508   3007   6565    422   1413   1274       N  
ATOM   2815  CA  ASP B  41      28.169 118.425  -0.714  1.00 41.72           C  
ANISOU 2815  CA  ASP B  41     5016   3596   7240    439   1399   1402       C  
ATOM   2816  C   ASP B  41      27.236 119.624  -0.457  1.00 44.93           C  
ANISOU 2816  C   ASP B  41     5288   3836   7947    495   1563   1528       C  
ATOM   2817  O   ASP B  41      26.448 119.628   0.499  1.00 44.37           O  
ANISOU 2817  O   ASP B  41     5201   3669   7986    527   1683   1496       O  
ATOM   2818  CB  ASP B  41      28.041 117.335   0.353  1.00 41.61           C  
ANISOU 2818  CB  ASP B  41     5102   3613   7092    432   1400   1244       C  
ATOM   2819  CG  ASP B  41      26.926 116.329   0.104  1.00 43.63           C  
ANISOU 2819  CG  ASP B  41     5309   3945   7321    425   1301   1359       C  
ATOM   2820  OD1 ASP B  41      26.107 116.567  -0.802  1.00 42.70           O  
ANISOU 2820  OD1 ASP B  41     5066   3841   7315    426   1246   1573       O  
ATOM   2821  OD2 ASP B  41      26.926 115.289   0.801  1.00 46.09           O  
ANISOU 2821  OD2 ASP B  41     5709   4308   7495    412   1273   1237       O  
ATOM   2822  N   HIS B  42      27.311 120.611  -1.356  1.00 48.96           N  
ANISOU 2822  N   HIS B  42     5697   4310   8595    506   1569   1681       N  
ATOM   2823  CA  HIS B  42      26.557 121.875  -1.305  1.00 51.09           C  
ANISOU 2823  CA  HIS B  42     5821   4414   9177    560   1727   1827       C  
ATOM   2824  C   HIS B  42      26.548 122.456   0.116  1.00 51.94           C  
ANISOU 2824  C   HIS B  42     5980   4349   9403    594   1958   1650       C  
ATOM   2825  O   HIS B  42      25.499 122.509   0.762  1.00 52.42           O  
ANISOU 2825  O   HIS B  42     5980   4310   9625    630   2073   1692       O  
ATOM   2826  CB  HIS B  42      25.138 121.668  -1.839  1.00 54.66           C  
ANISOU 2826  CB  HIS B  42     6114   4878   9773    575   1671   2082       C  
ATOM   2827  CG  HIS B  42      24.508 122.932  -2.303  1.00 57.66           C  
ANISOU 2827  CG  HIS B  42     6314   5130  10464    620   1772   2306       C  
ATOM   2828  ND1 HIS B  42      24.793 123.477  -3.538  1.00 58.48           N  
ANISOU 2828  ND1 HIS B  42     6333   5288  10596    599   1675   2484       N  
ATOM   2829  CD2 HIS B  42      23.627 123.760  -1.702  1.00 60.38           C  
ANISOU 2829  CD2 HIS B  42     6543   5288  11110    683   1969   2386       C  
ATOM   2830  CE1 HIS B  42      24.122 124.601  -3.681  1.00 62.82           C  
ANISOU 2830  CE1 HIS B  42     6715   5693  11460    651   1801   2674       C  
ATOM   2831  NE2 HIS B  42      23.393 124.795  -2.566  1.00 65.60           N  
ANISOU 2831  NE2 HIS B  42     7043   5889  11992    705   1989   2617       N  
ATOM   2832  N   SER B  43      27.731 122.895   0.579  1.00 48.45           N  
ANISOU 2832  N   SER B  43     5653   3874   8880    575   2028   1454       N  
ATOM   2833  CA  SER B  43      27.903 123.593   1.861  1.00 47.00           C  
ANISOU 2833  CA  SER B  43     5535   3529   8792    582   2252   1273       C  
ATOM   2834  C   SER B  43      27.011 124.842   1.881  1.00 48.38           C  
ANISOU 2834  C   SER B  43     5560   3508   9313    638   2451   1419       C  
ATOM   2835  O   SER B  43      26.680 125.401   0.836  1.00 45.15           O  
ANISOU 2835  O   SER B  43     5007   3089   9058    668   2411   1641       O  
ATOM   2836  CB  SER B  43      29.346 123.980   2.099  1.00 43.84           C  
ANISOU 2836  CB  SER B  43     5257   3136   8261    540   2271   1083       C  
ATOM   2837  OG  SER B  43      30.152 122.845   2.325  1.00 42.08           O  
ANISOU 2837  OG  SER B  43     5172   3067   7748    491   2124    934       O  
ATOM   2838  N   ASN B  44      26.628 125.272   3.080  1.00 51.15           N  
ANISOU 2838  N   ASN B  44     5946   3700   9789    647   2672   1295       N  
ATOM   2839  CA  ASN B  44      25.727 126.405   3.222  1.00 54.51           C  
ANISOU 2839  CA  ASN B  44     6231   3915  10564    702   2895   1421       C  
ATOM   2840  C   ASN B  44      26.170 127.257   4.412  1.00 53.66           C  
ANISOU 2840  C   ASN B  44     6227   3633  10527    676   3154   1194       C  
ATOM   2841  O   ASN B  44      25.336 127.833   5.077  1.00 62.30           O  
ANISOU 2841  O   ASN B  44     7269   4546  11857    704   3380   1203       O  
ATOM   2842  CB  ASN B  44      24.279 125.931   3.357  1.00 56.91           C  
ANISOU 2842  CB  ASN B  44     6425   4187  11011    746   2915   1574       C  
ATOM   2843  CG  ASN B  44      24.100 124.923   4.474  1.00 60.20           C  
ANISOU 2843  CG  ASN B  44     6978   4644  11250    714   2926   1385       C  
ATOM   2844  OD1 ASN B  44      24.809 124.954   5.479  1.00 61.07           O  
ANISOU 2844  OD1 ASN B  44     7248   4723  11232    666   3024   1135       O  
ATOM   2845  ND2 ASN B  44      23.172 124.001   4.293  1.00 65.11           N  
ANISOU 2845  ND2 ASN B  44     7540   5345  11853    733   2815   1508       N  
ATOM   2846  N   ASP B  45      27.484 127.330   4.646  1.00 48.44           N  
ANISOU 2846  N   ASP B  45     5711   3029   9665    615   3120    996       N  
ATOM   2847  CA  ASP B  45      28.099 128.055   5.758  1.00 48.66           C  
ANISOU 2847  CA  ASP B  45     5864   2925   9698    560   3333    757       C  
ATOM   2848  C   ASP B  45      28.528 129.460   5.276  1.00 50.78           C  
ANISOU 2848  C   ASP B  45     6059   3056  10177    578   3465    809       C  
ATOM   2849  O   ASP B  45      29.572 129.987   5.688  1.00 47.55           O  
ANISOU 2849  O   ASP B  45     5762   2617   9686    517   3532    627       O  
ATOM   2850  CB  ASP B  45      29.248 127.245   6.379  1.00 47.27           C  
ANISOU 2850  CB  ASP B  45     5884   2898   9177    473   3211    520       C  
ATOM   2851  CG  ASP B  45      30.419 126.949   5.450  1.00 48.08           C  
ANISOU 2851  CG  ASP B  45     6013   3165   9087    456   2988    534       C  
ATOM   2852  OD1 ASP B  45      30.239 127.091   4.220  1.00 44.46           O  
ANISOU 2852  OD1 ASP B  45     5427   2749   8714    509   2879    741       O  
ATOM   2853  OD2 ASP B  45      31.505 126.567   5.962  1.00 47.25           O  
ANISOU 2853  OD2 ASP B  45     6054   3148   8748    383   2923    343       O  
ATOM   2854  N   ASN B  46      27.716 130.034   4.376  1.00 51.57           N  
ANISOU 2854  N   ASN B  46     5965   3081  10547    657   3490   1070       N  
ATOM   2855  CA  ASN B  46      27.821 131.405   3.886  1.00 54.11           C  
ANISOU 2855  CA  ASN B  46     6175   3245  11139    692   3640   1173       C  
ATOM   2856  C   ASN B  46      29.133 131.578   3.110  1.00 52.94           C  
ANISOU 2856  C   ASN B  46     6074   3215  10826    661   3484   1144       C  
ATOM   2857  O   ASN B  46      29.857 132.544   3.307  1.00 50.09           O  
ANISOU 2857  O   ASN B  46     5750   2746  10535    637   3622   1041       O  
ATOM   2858  CB  ASN B  46      27.626 132.412   5.023  1.00 58.10           C  
ANISOU 2858  CB  ASN B  46     6722   3502  11851    673   3979   1018       C  
ATOM   2859  CG  ASN B  46      26.226 132.345   5.604  1.00 60.42           C  
ANISOU 2859  CG  ASN B  46     6935   3659  12362    718   4149   1094       C  
ATOM   2860  OD1 ASN B  46      25.350 133.123   5.226  1.00 65.06           O  
ANISOU 2860  OD1 ASN B  46     7341   4085  13293    791   4294   1301       O  
ATOM   2861  ND2 ASN B  46      25.992 131.392   6.492  1.00 63.57           N  
ANISOU 2861  ND2 ASN B  46     7456   4123  12573    677   4126    945       N  
ATOM   2862  N   GLY B  47      29.415 130.604   2.240  1.00 50.74           N  
ANISOU 2862  N   GLY B  47     5795   3154  10327    658   3204   1232       N  
ATOM   2863  CA  GLY B  47      30.552 130.631   1.325  1.00 47.91           C  
ANISOU 2863  CA  GLY B  47     5464   2924   9815    635   3034   1243       C  
ATOM   2864  C   GLY B  47      31.882 130.249   1.954  1.00 45.22           C  
ANISOU 2864  C   GLY B  47     5318   2666   9194    558   2985    972       C  
ATOM   2865  O   GLY B  47      32.877 130.205   1.241  1.00 44.94           O  
ANISOU 2865  O   GLY B  47     5312   2737   9024    538   2847    969       O  
ATOM   2866  N   GLU B  48      31.929 129.944   3.255  1.00 43.49           N  
ANISOU 2866  N   GLU B  48     5231   2409   8883    509   3088    754       N  
ATOM   2867  CA  GLU B  48      33.223 129.787   3.941  1.00 44.32           C  
ANISOU 2867  CA  GLU B  48     5509   2571   8757    423   3066    505       C  
ATOM   2868  C   GLU B  48      33.986 128.525   3.473  1.00 40.20           C  
ANISOU 2868  C   GLU B  48     5062   2282   7931    397   2794    483       C  
ATOM   2869  O   GLU B  48      35.209 128.572   3.293  1.00 37.56           O  
ANISOU 2869  O   GLU B  48     4799   2017   7454    353   2715    391       O  
ATOM   2870  CB  GLU B  48      33.067 129.776   5.459  1.00 47.27           C  
ANISOU 2870  CB  GLU B  48     6007   2854   9097    359   3240    287       C  
ATOM   2871  CG  GLU B  48      34.403 129.773   6.196  1.00 52.17           C  
ANISOU 2871  CG  GLU B  48     6796   3524   9500    255   3228     46       C  
ATOM   2872  CD  GLU B  48      34.316 129.710   7.715  1.00 62.19           C  
ANISOU 2872  CD  GLU B  48     8205   4727  10696    165   3383   -173       C  
ATOM   2873  OE1 GLU B  48      33.541 130.511   8.297  1.00 72.56           O  
ANISOU 2873  OE1 GLU B  48     9496   5851  12224    167   3632   -197       O  
ATOM   2874  OE2 GLU B  48      35.013 128.852   8.321  1.00 58.23           O  
ANISOU 2874  OE2 GLU B  48     7833   4362   9927     88   3261   -317       O  
ATOM   2875  N   THR B  49      33.313 127.383   3.312  1.00 38.09           N  
ANISOU 2875  N   THR B  49     4778   2128   7563    418   2657    558       N  
ATOM   2876  CA  THR B  49      34.056 126.186   2.904  1.00 36.48           C  
ANISOU 2876  CA  THR B  49     4648   2127   7083    389   2424    525       C  
ATOM   2877  C   THR B  49      34.562 126.407   1.465  1.00 34.59           C  
ANISOU 2877  C   THR B  49     4334   1961   6847    413   2292    677       C  
ATOM   2878  O   THR B  49      35.732 126.098   1.135  1.00 33.01           O  
ANISOU 2878  O   THR B  49     4205   1863   6471    377   2177    604       O  
ATOM   2879  CB  THR B  49      33.238 124.906   3.132  1.00 36.81           C  
ANISOU 2879  CB  THR B  49     4701   2265   7016    398   2323    554       C  
ATOM   2880  OG1 THR B  49      33.002 124.729   4.533  1.00 36.08           O  
ANISOU 2880  OG1 THR B  49     4703   2112   6891    361   2446    385       O  
ATOM   2881  CG2 THR B  49      33.932 123.669   2.601  1.00 34.26           C  
ANISOU 2881  CG2 THR B  49     4441   2138   6436    373   2096    539       C  
ATOM   2882  N   LEU B  50      33.687 126.956   0.622  1.00 33.94           N  
ANISOU 2882  N   LEU B  50     4102   1823   6968    470   2315    896       N  
ATOM   2883  CA  LEU B  50      34.024 127.270  -0.746  1.00 37.43           C  
ANISOU 2883  CA  LEU B  50     4462   2326   7433    486   2206   1062       C  
ATOM   2884  C   LEU B  50      35.233 128.215  -0.816  1.00 35.92           C  
ANISOU 2884  C   LEU B  50     4310   2078   7258    465   2270    968       C  
ATOM   2885  O   LEU B  50      36.107 128.025  -1.646  1.00 32.75           O  
ANISOU 2885  O   LEU B  50     3930   1782   6729    446   2139    988       O  
ATOM   2886  CB  LEU B  50      32.820 127.913  -1.426  1.00 42.71           C  
ANISOU 2886  CB  LEU B  50     4952   2913   8361    543   2256   1316       C  
ATOM   2887  CG  LEU B  50      32.914 127.946  -2.949  1.00 47.46           C  
ANISOU 2887  CG  LEU B  50     5461   3619   8950    546   2097   1531       C  
ATOM   2888  CD2 LEU B  50      32.114 126.794  -3.544  1.00 51.90           C  
ANISOU 2888  CD2 LEU B  50     5990   4329   9399    535   1919   1668       C  
ATOM   2889  N   ASN B  51      35.240 129.252   0.030  1.00 36.16           N  
ANISOU 2889  N   ASN B  51     4348   1936   7455    465   2483    871       N  
ATOM   2890  CA  ASN B  51      36.324 130.242   0.087  1.00 36.45           C  
ANISOU 2890  CA  ASN B  51     4421   1899   7529    439   2570    772       C  
ATOM   2891  C   ASN B  51      37.659 129.566   0.390  1.00 34.40           C  
ANISOU 2891  C   ASN B  51     4309   1764   6996    372   2453    583       C  
ATOM   2892  O   ASN B  51      38.669 129.909  -0.218  1.00 33.73           O  
ANISOU 2892  O   ASN B  51     4234   1713   6866    358   2398    579       O  
ATOM   2893  CB  ASN B  51      36.031 131.360   1.102  1.00 39.23           C  
ANISOU 2893  CB  ASN B  51     4775   2038   8092    432   2836    671       C  
ATOM   2894  CG  ASN B  51      34.923 132.276   0.637  1.00 42.88           C  
ANISOU 2894  CG  ASN B  51     5066   2350   8874    506   2973    881       C  
ATOM   2895  OD1 ASN B  51      34.623 132.298  -0.549  1.00 44.12           O  
ANISOU 2895  OD1 ASN B  51     5101   2565   9095    552   2861   1104       O  
ATOM   2896  ND2 ASN B  51      34.304 133.024   1.550  1.00 45.02           N  
ANISOU 2896  ND2 ASN B  51     5325   2428   9351    510   3218    818       N  
ATOM   2897  N   VAL B  52      37.658 128.582   1.296  1.00 32.67           N  
ANISOU 2897  N   VAL B  52     4196   1615   6602    332   2409    443       N  
ATOM   2898  CA  VAL B  52      38.878 127.888   1.625  1.00 32.54           C  
ANISOU 2898  CA  VAL B  52     4304   1715   6341    268   2296    286       C  
ATOM   2899  C   VAL B  52      39.325 127.086   0.400  1.00 31.29           C  
ANISOU 2899  C   VAL B  52     4124   1717   6047    286   2087    397       C  
ATOM   2900  O   VAL B  52      40.489 127.078   0.049  1.00 30.15           O  
ANISOU 2900  O   VAL B  52     4023   1631   5801    258   2016    346       O  
ATOM   2901  CB  VAL B  52      38.712 126.962   2.843  1.00 34.20           C  
ANISOU 2901  CB  VAL B  52     4622   1972   6401    221   2289    135       C  
ATOM   2902  CG1 VAL B  52      39.933 126.056   2.990  1.00 34.77           C  
ANISOU 2902  CG1 VAL B  52     4797   2190   6224    164   2134     23       C  
ATOM   2903  CG2 VAL B  52      38.445 127.750   4.115  1.00 38.69           C  
ANISOU 2903  CG2 VAL B  52     5241   2389   7069    176   2502     -5       C  
ATOM   2904  N   ILE B  53      38.382 126.370  -0.215  1.00 30.79           N  
ANISOU 2904  N   ILE B  53     3997   1722   5978    325   1996    543       N  
ATOM   2905  CA  ILE B  53      38.682 125.510  -1.340  1.00 31.28           C  
ANISOU 2905  CA  ILE B  53     4051   1935   5896    326   1809    640       C  
ATOM   2906  C   ILE B  53      39.225 126.356  -2.501  1.00 31.04           C  
ANISOU 2906  C   ILE B  53     3956   1894   5944    339   1794    753       C  
ATOM   2907  O   ILE B  53      40.212 125.949  -3.159  1.00 30.93           O  
ANISOU 2907  O   ILE B  53     3986   1978   5787    314   1683    736       O  
ATOM   2908  CB  ILE B  53      37.458 124.652  -1.730  1.00 32.62           C  
ANISOU 2908  CB  ILE B  53     4166   2172   6054    351   1726    777       C  
ATOM   2909  CG1 ILE B  53      37.131 123.625  -0.635  1.00 32.96           C  
ANISOU 2909  CG1 ILE B  53     4291   2253   5978    333   1715    650       C  
ATOM   2910  CG2 ILE B  53      37.678 123.971  -3.073  1.00 32.36           C  
ANISOU 2910  CG2 ILE B  53     4115   2281   5899    339   1554    899       C  
ATOM   2911  CD1 ILE B  53      35.749 123.024  -0.749  1.00 33.46           C  
ANISOU 2911  CD1 ILE B  53     4289   2337   6084    361   1684    775       C  
ATOM   2912  N   LYS B  54      38.615 127.519  -2.730  1.00 32.42           N  
ANISOU 2912  N   LYS B  54     4024   1942   6350    378   1914    869       N  
ATOM   2913  CA  LYS B  54      39.021 128.419  -3.816  1.00 34.29           C  
ANISOU 2913  CA  LYS B  54     4183   2156   6687    393   1912    998       C  
ATOM   2914  C   LYS B  54      40.459 128.934  -3.626  1.00 31.99           C  
ANISOU 2914  C   LYS B  54     3968   1842   6342    361   1946    849       C  
ATOM   2915  O   LYS B  54      41.130 129.208  -4.619  1.00 32.05           O  
ANISOU 2915  O   LYS B  54     3953   1893   6331    358   1883    922       O  
ATOM   2916  CB  LYS B  54      37.972 129.524  -3.979  1.00 39.22           C  
ANISOU 2916  CB  LYS B  54     4666   2638   7596    444   2047   1162       C  
ATOM   2917  CG  LYS B  54      36.688 128.983  -4.588  1.00 44.73           C  
ANISOU 2917  CG  LYS B  54     5265   3395   8334    469   1962   1368       C  
ATOM   2918  CD  LYS B  54      35.659 129.976  -5.040  1.00 50.83           C  
ANISOU 2918  CD  LYS B  54     5868   4053   9389    519   2055   1593       C  
ATOM   2919  CE  LYS B  54      34.546 129.246  -5.773  1.00 55.96           C  
ANISOU 2919  CE  LYS B  54     6430   4807  10026    522   1920   1804       C  
ATOM   2920  NZ  LYS B  54      33.503 130.158  -6.304  1.00 59.00           N  
ANISOU 2920  NZ  LYS B  54     6627   5094  10695    568   1989   2064       N  
ATOM   2921  N   LYS B  55      40.979 128.966  -2.397  1.00 30.57           N  
ANISOU 2921  N   LYS B  55     3885   1612   6116    325   2027    643       N  
ATOM   2922  CA  LYS B  55      42.380 129.352  -2.145  1.00 31.19           C  
ANISOU 2922  CA  LYS B  55     4039   1683   6126    281   2042    498       C  
ATOM   2923  C   LYS B  55      43.376 128.373  -2.776  1.00 29.25           C  
ANISOU 2923  C   LYS B  55     3852   1594   5665    256   1866    479       C  
ATOM   2924  O   LYS B  55      44.566 128.720  -2.860  1.00 29.08           O  
ANISOU 2924  O   LYS B  55     3869   1573   5603    227   1862    404       O  
ATOM   2925  CB  LYS B  55      42.691 129.531  -0.652  1.00 33.82           C  
ANISOU 2925  CB  LYS B  55     4468   1945   6436    227   2154    288       C  
ATOM   2926  CG  LYS B  55      42.177 130.844  -0.032  1.00 37.18           C  
ANISOU 2926  CG  LYS B  55     4856   2180   7090    231   2374    261       C  
ATOM   2927  CD  LYS B  55      42.786 132.105  -0.608  1.00 40.98           C  
ANISOU 2927  CD  LYS B  55     5283   2567   7721    240   2457    300       C  
ATOM   2928  CE  LYS B  55      42.023 133.375  -0.320  1.00 46.72           C  
ANISOU 2928  CE  LYS B  55     5934   3097   8720    267   2678    338       C  
ATOM   2929  NZ  LYS B  55      42.447 133.996   0.959  1.00 49.05           N  
ANISOU 2929  NZ  LYS B  55     6325   3278   9033    191   2844    123       N  
ATOM   2930  N   TYR B  56      42.923 127.178  -3.191  1.00 27.30           N  
ANISOU 2930  N   TYR B  56     3613   1469   5288    262   1735    542       N  
ATOM   2931  CA  TYR B  56      43.784 126.149  -3.751  1.00 26.94           C  
ANISOU 2931  CA  TYR B  56     3627   1560   5046    236   1589    519       C  
ATOM   2932  C   TYR B  56      43.432 125.867  -5.214  1.00 26.15           C  
ANISOU 2932  C   TYR B  56     3468   1541   4925    252   1490    700       C  
ATOM   2933  O   TYR B  56      43.832 124.844  -5.760  1.00 24.55           O  
ANISOU 2933  O   TYR B  56     3313   1454   4560    229   1375    699       O  
ATOM   2934  CB  TYR B  56      43.670 124.879  -2.893  1.00 26.57           C  
ANISOU 2934  CB  TYR B  56     3661   1590   4844    212   1528    411       C  
ATOM   2935  CG  TYR B  56      44.181 125.097  -1.500  1.00 27.67           C  
ANISOU 2935  CG  TYR B  56     3870   1674   4969    173   1605    234       C  
ATOM   2936  CD1 TYR B  56      45.548 125.156  -1.245  1.00 27.22           C  
ANISOU 2936  CD1 TYR B  56     3871   1635   4834    129   1584    124       C  
ATOM   2937  CD2 TYR B  56      43.296 125.367  -0.464  1.00 29.20           C  
ANISOU 2937  CD2 TYR B  56     4067   1786   5239    172   1711    184       C  
ATOM   2938  CE1 TYR B  56      46.028 125.467   0.017  1.00 29.02           C  
ANISOU 2938  CE1 TYR B  56     4162   1816   5048     74   1653    -28       C  
ATOM   2939  CE2 TYR B  56      43.759 125.638   0.813  1.00 30.12           C  
ANISOU 2939  CE2 TYR B  56     4258   1852   5331    116   1790     18       C  
ATOM   2940  CZ  TYR B  56      45.123 125.666   1.055  1.00 30.73           C  
ANISOU 2940  CZ  TYR B  56     4395   1963   5316     62   1752    -86       C  
ATOM   2941  OH  TYR B  56      45.574 125.954   2.304  1.00 32.77           O  
ANISOU 2941  OH  TYR B  56     4728   2183   5540    -11   1821   -240       O  
ATOM   2942  N   LYS B  57      42.646 126.748  -5.819  1.00 28.74           N  
ANISOU 2942  N   LYS B  57     3692   1806   5419    285   1540    858       N  
ATOM   2943  CA  LYS B  57      42.231 126.626  -7.183  1.00 29.80           C  
ANISOU 2943  CA  LYS B  57     3762   2015   5544    285   1449   1049       C  
ATOM   2944  C   LYS B  57      43.507 126.544  -8.030  1.00 27.78           C  
ANISOU 2944  C   LYS B  57     3553   1825   5175    253   1386   1028       C  
ATOM   2945  O   LYS B  57      44.497 127.269  -7.809  1.00 27.38           O  
ANISOU 2945  O   LYS B  57     3521   1710   5169    254   1451    943       O  
ATOM   2946  CB  LYS B  57      41.318 127.789  -7.579  1.00 33.14           C  
ANISOU 2946  CB  LYS B  57     4051   2341   6197    323   1530   1228       C  
ATOM   2947  CG  LYS B  57      41.003 127.862  -9.062  1.00 34.47           C  
ANISOU 2947  CG  LYS B  57     4144   2589   6364    309   1433   1447       C  
ATOM   2948  CD  LYS B  57      39.813 128.711  -9.439  1.00 36.60           C  
ANISOU 2948  CD  LYS B  57     4263   2787   6853    343   1482   1666       C  
ATOM   2949  CE  LYS B  57      39.768 128.926 -10.935  1.00 37.90           C  
ANISOU 2949  CE  LYS B  57     4360   3037   7004    312   1383   1879       C  
ATOM   2950  NZ  LYS B  57      38.460 129.459 -11.381  1.00 42.37           N  
ANISOU 2950  NZ  LYS B  57     4769   3570   7757    332   1388   2129       N  
ATOM   2951  N   GLY B  58      43.494 125.589  -8.952  1.00 26.93           N  
ANISOU 2951  N   GLY B  58     3473   1845   4913    219   1263   1093       N  
ATOM   2952  CA  GLY B  58      44.633 125.287  -9.772  1.00 26.99           C  
ANISOU 2952  CA  GLY B  58     3537   1922   4795    182   1205   1068       C  
ATOM   2953  C   GLY B  58      45.505 124.209  -9.177  1.00 27.06           C  
ANISOU 2953  C   GLY B  58     3653   1982   4644    160   1170    893       C  
ATOM   2954  O   GLY B  58      46.356 123.700  -9.901  1.00 27.69           O  
ANISOU 2954  O   GLY B  58     3784   2128   4608    127   1118    876       O  
ATOM   2955  N   LEU B  59      45.307 123.847  -7.889  1.00 24.81           N  
ANISOU 2955  N   LEU B  59     3401   1666   4357    175   1201    771       N  
ATOM   2956  CA  LEU B  59      46.122 122.817  -7.252  1.00 24.48           C  
ANISOU 2956  CA  LEU B  59     3450   1674   4178    152   1163    621       C  
ATOM   2957  C   LEU B  59      45.291 121.570  -6.937  1.00 23.76           C  
ANISOU 2957  C   LEU B  59     3389   1653   3985    144   1101    613       C  
ATOM   2958  O   LEU B  59      45.862 120.559  -6.560  1.00 22.54           O  
ANISOU 2958  O   LEU B  59     3301   1550   3712    125   1060    515       O  
ATOM   2959  CB  LEU B  59      46.775 123.348  -5.974  1.00 24.92           C  
ANISOU 2959  CB  LEU B  59     3530   1648   4288    156   1240    476       C  
ATOM   2960  CG  LEU B  59      47.652 124.587  -6.135  1.00 25.28           C  
ANISOU 2960  CG  LEU B  59     3552   1615   4437    158   1310    463       C  
ATOM   2961  CD1 LEU B  59      48.230 125.017  -4.785  1.00 26.12           C  
ANISOU 2961  CD1 LEU B  59     3694   1653   4577    140   1379    311       C  
ATOM   2962  CD2 LEU B  59      48.778 124.353  -7.122  1.00 25.82           C  
ANISOU 2962  CD2 LEU B  59     3642   1737   4431    140   1258    479       C  
ATOM   2963  N   VAL B  60      43.970 121.663  -7.108  1.00 24.25           N  
ANISOU 2963  N   VAL B  60     3394   1714   4106    159   1096    725       N  
ATOM   2964  CA  VAL B  60      43.040 120.622  -6.815  1.00 25.62           C  
ANISOU 2964  CA  VAL B  60     3582   1944   4207    154   1044    733       C  
ATOM   2965  C   VAL B  60      42.011 120.598  -7.943  1.00 27.64           C  
ANISOU 2965  C   VAL B  60     3775   2251   4473    139    986    917       C  
ATOM   2966  O   VAL B  60      41.804 121.587  -8.650  1.00 25.52           O  
ANISOU 2966  O   VAL B  60     3434   1949   4312    145   1007   1043       O  
ATOM   2967  CB  VAL B  60      42.346 120.859  -5.458  1.00 26.87           C  
ANISOU 2967  CB  VAL B  60     3728   2026   4453    185   1118    668       C  
ATOM   2968  CG1 VAL B  60      43.358 120.984  -4.325  1.00 27.07           C  
ANISOU 2968  CG1 VAL B  60     3816   2008   4461    179   1171    495       C  
ATOM   2969  CG2 VAL B  60      41.432 122.077  -5.513  1.00 28.86           C  
ANISOU 2969  CG2 VAL B  60     3882   2183   4900    220   1200    782       C  
ATOM   2970  N   ARG B  61      41.338 119.464  -8.096  1.00 27.22           N  
ANISOU 2970  N   ARG B  61     3748   2282   4313    112    910    940       N  
ATOM   2971  CA  ARG B  61      40.139 119.450  -8.900  1.00 30.48           C  
ANISOU 2971  CA  ARG B  61     4091   2739   4749     91    855   1118       C  
ATOM   2972  C   ARG B  61      38.948 119.563  -7.953  1.00 31.51           C  
ANISOU 2972  C   ARG B  61     4165   2812   4995    135    897   1141       C  
ATOM   2973  O   ARG B  61      38.953 119.005  -6.866  1.00 33.57           O  
ANISOU 2973  O   ARG B  61     4474   3054   5224    155    924   1011       O  
ATOM   2974  CB  ARG B  61      40.121 118.183  -9.747  1.00 31.83           C  
ANISOU 2974  CB  ARG B  61     4326   3037   4731     20    751   1135       C  
ATOM   2975  CG  ARG B  61      41.313 118.102 -10.688  1.00 31.81           C  
ANISOU 2975  CG  ARG B  61     4384   3077   4624    -26    732   1107       C  
ATOM   2976  CD  ARG B  61      41.299 116.772 -11.395  1.00 33.34           C  
ANISOU 2976  CD  ARG B  61     4656   3380   4631   -103    655   1096       C  
ATOM   2977  NE  ARG B  61      40.029 116.580 -12.085  1.00 34.05           N  
ANISOU 2977  NE  ARG B  61     4698   3539   4700   -155    580   1256       N  
ATOM   2978  CZ  ARG B  61      39.605 115.407 -12.503  1.00 33.30           C  
ANISOU 2978  CZ  ARG B  61     4658   3535   4459   -226    512   1258       C  
ATOM   2979  NH1 ARG B  61      40.347 114.336 -12.251  1.00 34.17           N  
ANISOU 2979  NH1 ARG B  61     4868   3664   4448   -241    524   1105       N  
ATOM   2980  NH2 ARG B  61      38.475 115.315 -13.187  1.00 30.58           N  
ANISOU 2980  NH2 ARG B  61     4265   3260   4094   -287    435   1418       N  
ATOM   2981  N   PHE B  62      37.934 120.298  -8.370  1.00 33.14           N  
ANISOU 2981  N   PHE B  62     4261   2987   5341    148    905   1316       N  
ATOM   2982  CA  PHE B  62      36.850 120.624  -7.483  1.00 37.55           C  
ANISOU 2982  CA  PHE B  62     4751   3464   6052    198    975   1348       C  
ATOM   2983  C   PHE B  62      35.515 120.547  -8.230  1.00 38.55           C  
ANISOU 2983  C   PHE B  62     4775   3636   6236    179    906   1567       C  
ATOM   2984  O   PHE B  62      35.401 121.028  -9.337  1.00 35.11           O  
ANISOU 2984  O   PHE B  62     4274   3236   5828    148    855   1732       O  
ATOM   2985  CB  PHE B  62      37.083 122.010  -6.875  1.00 41.17           C  
ANISOU 2985  CB  PHE B  62     5158   3775   6708    253   1118   1323       C  
ATOM   2986  CG  PHE B  62      35.881 122.572  -6.177  1.00 43.35           C  
ANISOU 2986  CG  PHE B  62     5342   3945   7184    303   1215   1394       C  
ATOM   2987  CD1 PHE B  62      35.430 122.009  -4.987  1.00 44.09           C  
ANISOU 2987  CD1 PHE B  62     5480   4008   7265    320   1263   1276       C  
ATOM   2988  CD2 PHE B  62      35.166 123.620  -6.733  1.00 46.44           C  
ANISOU 2988  CD2 PHE B  62     5597   4267   7781    329   1261   1590       C  
ATOM   2989  CE1 PHE B  62      34.312 122.524  -4.339  1.00 44.74           C  
ANISOU 2989  CE1 PHE B  62     5478   3981   7539    365   1369   1338       C  
ATOM   2990  CE2 PHE B  62      34.033 124.117  -6.096  1.00 48.68           C  
ANISOU 2990  CE2 PHE B  62     5786   4439   8271    377   1365   1664       C  
ATOM   2991  CZ  PHE B  62      33.606 123.564  -4.903  1.00 47.44           C  
ANISOU 2991  CZ  PHE B  62     5681   4244   8099    395   1424   1533       C  
ATOM   2992  N   LYS B  63      34.510 119.957  -7.571  1.00 41.05           N  
ANISOU 2992  N   LYS B  63     5073   3949   6574    195    905   1572       N  
ATOM   2993  CA  LYS B  63      33.130 119.972  -8.044  1.00 43.08           C  
ANISOU 2993  CA  LYS B  63     5214   4227   6926    186    856   1785       C  
ATOM   2994  C   LYS B  63      32.199 120.235  -6.850  1.00 45.70           C  
ANISOU 2994  C   LYS B  63     5488   4441   7432    254    969   1769       C  
ATOM   2995  O   LYS B  63      32.359 119.652  -5.780  1.00 41.60           O  
ANISOU 2995  O   LYS B  63     5053   3899   6851    274   1014   1592       O  
ATOM   2996  CB  LYS B  63      32.846 118.660  -8.778  1.00 44.43           C  
ANISOU 2996  CB  LYS B  63     5436   4554   6891    104    703   1822       C  
ATOM   2997  CG  LYS B  63      31.382 118.419  -9.107  1.00 50.62           C  
ANISOU 2997  CG  LYS B  63     6114   5376   7743     81    636   2022       C  
ATOM   2998  CD  LYS B  63      31.160 117.317 -10.109  1.00 53.65           C  
ANISOU 2998  CD  LYS B  63     6542   5921   7920    -25    479   2087       C  
ATOM   2999  CE  LYS B  63      31.272 117.788 -11.541  1.00 58.29           C  
ANISOU 2999  CE  LYS B  63     7084   6589   8474   -106    391   2268       C  
ATOM   3000  NZ  LYS B  63      31.199 116.655 -12.490  1.00 64.67           N  
ANISOU 3000  NZ  LYS B  63     7968   7557   9047   -232    251   2294       N  
ATOM   3001  N   GLN B  64      31.244 121.159  -7.019  1.00 45.01           N  
ANISOU 3001  N   GLN B  64     5254   4271   7575    289   1024   1959       N  
ATOM   3002  CA  GLN B  64      30.222 121.422  -6.015  1.00 47.53           C  
ANISOU 3002  CA  GLN B  64     5503   4472   8082    350   1141   1975       C  
ATOM   3003  C   GLN B  64      28.923 120.750  -6.463  1.00 48.86           C  
ANISOU 3003  C   GLN B  64     5585   4716   8263    324   1036   2161       C  
ATOM   3004  O   GLN B  64      28.439 121.020  -7.555  1.00 51.91           O  
ANISOU 3004  O   GLN B  64     5865   5159   8699    288    946   2388       O  
ATOM   3005  CB  GLN B  64      29.976 122.924  -5.834  1.00 49.97           C  
ANISOU 3005  CB  GLN B  64     5693   4614   8677    412   1300   2068       C  
ATOM   3006  N   LEU B  65      28.359 119.896  -5.605  1.00 51.18           N  
ANISOU 3006  N   LEU B  65     5921   5012   8513    336   1047   2072       N  
ATOM   3007  CA  LEU B  65      27.045 119.346  -5.879  1.00 51.96           C  
ANISOU 3007  CA  LEU B  65     5925   5160   8658    319    969   2248       C  
ATOM   3008  C   LEU B  65      25.991 120.454  -5.694  1.00 53.30           C  
ANISOU 3008  C   LEU B  65     5917   5183   9150    383   1089   2440       C  
ATOM   3009  O   LEU B  65      26.111 121.302  -4.818  1.00 50.89           O  
ANISOU 3009  O   LEU B  65     5601   4719   9015    451   1271   2354       O  
ATOM   3010  CB  LEU B  65      26.821 118.128  -4.982  1.00 49.72           C  
ANISOU 3010  CB  LEU B  65     5741   4912   8237    317    955   2088       C  
ATOM   3011  CG  LEU B  65      27.861 117.018  -5.137  1.00 49.23           C  
ANISOU 3011  CG  LEU B  65     5843   4979   7881    259    852   1908       C  
ATOM   3012  CD1 LEU B  65      27.525 115.830  -4.256  1.00 47.73           C  
ANISOU 3012  CD1 LEU B  65     5732   4820   7583    261    841   1778       C  
ATOM   3013  CD2 LEU B  65      27.989 116.575  -6.584  1.00 47.67           C  
ANISOU 3013  CD2 LEU B  65     5642   4930   7536    168    683   2036       C  
ATOM   3014  N   LYS B  66      24.981 120.441  -6.569  1.00 53.79           N  
ANISOU 3014  N   LYS B  66     5838   5302   9297    351    986   2707       N  
ATOM   3015  CA  LYS B  66      23.999 121.518  -6.713  1.00 57.59           C  
ANISOU 3015  CA  LYS B  66     6118   5663  10100    401   1071   2953       C  
ATOM   3016  C   LYS B  66      22.979 121.488  -5.555  1.00 60.28           C  
ANISOU 3016  C   LYS B  66     6403   5870  10631    472   1215   2936       C  
ATOM   3017  O   LYS B  66      22.435 122.517  -5.191  1.00 64.98           O  
ANISOU 3017  O   LYS B  66     6870   6297  11521    542   1377   3038       O  
ATOM   3018  CB  LYS B  66      23.355 121.428  -8.106  1.00 56.99           C  
ANISOU 3018  CB  LYS B  66     5914   5719  10019    322    885   3255       C  
ATOM   3019  CG  LYS B  66      24.334 121.410  -9.281  1.00 53.85           C  
ANISOU 3019  CG  LYS B  66     5584   5460   9417    236    748   3270       C  
ATOM   3020  CD  LYS B  66      25.370 122.530  -9.237  1.00 56.83           C  
ANISOU 3020  CD  LYS B  66     5980   5734   9876    285    870   3189       C  
ATOM   3021  CE  LYS B  66      26.449 122.443 -10.302  1.00 58.88           C  
ANISOU 3021  CE  LYS B  66     6327   6125   9917    204    749   3168       C  
ATOM   3022  N   LYS B  67      22.732 120.318  -4.965  1.00 57.45           N  
ANISOU 3022  N   LYS B  67     6140   5575  10112    455   1168   2805       N  
ATOM   3023  CA  LYS B  67      21.924 120.199  -3.740  1.00 64.06           C  
ANISOU 3023  CA  LYS B  67     6960   6287  11092    520   1316   2739       C  
ATOM   3024  C   LYS B  67      22.603 119.182  -2.817  1.00 59.37           C  
ANISOU 3024  C   LYS B  67     6567   5742  10249    507   1318   2440       C  
ATOM   3025  O   LYS B  67      23.227 118.244  -3.301  1.00 56.70           O  
ANISOU 3025  O   LYS B  67     6336   5561   9643    442   1159   2362       O  
ATOM   3026  CB  LYS B  67      20.479 119.788  -4.059  1.00 65.54           C  
ANISOU 3026  CB  LYS B  67     6996   6504  11401    510   1239   2983       C  
ATOM   3027  N   ASN B  68      22.468 119.383  -1.500  1.00 58.27           N  
ANISOU 3027  N   ASN B  68     6472   5464  10205    564   1504   2282       N  
ATOM   3028  CA  ASN B  68      23.086 118.521  -0.489  1.00 59.02           C  
ANISOU 3028  CA  ASN B  68     6747   5591  10087    552   1522   2009       C  
ATOM   3029  C   ASN B  68      22.447 117.131  -0.552  1.00 62.94           C  
ANISOU 3029  C   ASN B  68     7266   6215  10433    517   1379   2032       C  
ATOM   3030  O   ASN B  68      21.254 117.011  -0.808  1.00 74.79           O  
ANISOU 3030  O   ASN B  68     8637   7708  12070    527   1353   2224       O  
ATOM   3031  CB  ASN B  68      22.961 119.102   0.924  1.00 59.89           C  
ANISOU 3031  CB  ASN B  68     6893   5523  10339    604   1759   1855       C  
ATOM   3032  CG  ASN B  68      23.713 118.303   1.970  1.00 59.75           C  
ANISOU 3032  CG  ASN B  68     7062   5546  10092    578   1773   1579       C  
ATOM   3033  OD1 ASN B  68      24.772 117.743   1.700  1.00 64.99           O  
ANISOU 3033  OD1 ASN B  68     7838   6331  10522    534   1652   1464       O  
ATOM   3034  ND2 ASN B  68      23.179 118.235   3.175  1.00 61.91           N  
ANISOU 3034  ND2 ASN B  68     7368   5719  10435    602   1922   1478       N  
ATOM   3035  N   SER B  69      23.257 116.093  -0.329  1.00 58.44           N  
ANISOU 3035  N   SER B  69     6852   5759   9592    476   1288   1843       N  
ATOM   3036  CA  SER B  69      22.787 114.710  -0.267  1.00 55.42           C  
ANISOU 3036  CA  SER B  69     6513   5490   9052    442   1169   1827       C  
ATOM   3037  C   SER B  69      22.745 114.204   1.188  1.00 56.18           C  
ANISOU 3037  C   SER B  69     6708   5528   9109    471   1280   1628       C  
ATOM   3038  O   SER B  69      22.004 113.289   1.495  1.00 63.47           O  
ANISOU 3038  O   SER B  69     7631   6491   9993    467   1239   1640       O  
ATOM   3039  CB  SER B  69      23.649 113.834  -1.141  1.00 55.61           C  
ANISOU 3039  CB  SER B  69     6631   5682   8813    369    990   1780       C  
ATOM   3040  OG  SER B  69      24.875 113.510  -0.495  1.00 50.43           O  
ANISOU 3040  OG  SER B  69     6129   5041   7991    365   1020   1541       O  
ATOM   3041  N   GLY B  70      23.600 114.746   2.067  1.00 61.69           N  
ANISOU 3041  N   GLY B  70     7499   6143   9795    489   1411   1440       N  
ATOM   3042  CA  GLY B  70      23.555 114.477   3.523  1.00 59.08           C  
ANISOU 3042  CA  GLY B  70     7260   5744   9444    506   1540   1257       C  
ATOM   3043  C   GLY B  70      24.437 113.321   3.978  1.00 61.39           C  
ANISOU 3043  C   GLY B  70     7706   6152   9466    464   1449   1070       C  
ATOM   3044  O   GLY B  70      24.432 112.971   5.166  1.00 55.70           O  
ANISOU 3044  O   GLY B  70     7067   5397   8699    464   1532    925       O  
ATOM   3045  N   ASN B  71      25.217 112.747   3.054  1.00 57.43           N  
ANISOU 3045  N   ASN B  71     7244   5782   8793    423   1288   1075       N  
ATOM   3046  CA  ASN B  71      26.049 111.551   3.305  1.00 56.61           C  
ANISOU 3046  CA  ASN B  71     7266   5792   8448    384   1191    928       C  
ATOM   3047  C   ASN B  71      27.306 111.624   2.419  1.00 49.00           C  
ANISOU 3047  C   ASN B  71     6349   4905   7361    349   1100    900       C  
ATOM   3048  O   ASN B  71      27.342 112.361   1.429  1.00 46.19           O  
ANISOU 3048  O   ASN B  71     5922   4544   7082    347   1075   1020       O  
ATOM   3049  CB  ASN B  71      25.260 110.265   3.027  1.00 58.09           C  
ANISOU 3049  CB  ASN B  71     7441   6075   8555    367   1076    993       C  
ATOM   3050  CG  ASN B  71      24.797 110.213   1.584  1.00 64.18           C  
ANISOU 3050  CG  ASN B  71     8122   6919   9344    339    952   1185       C  
ATOM   3051  OD1 ASN B  71      25.620 110.186   0.668  1.00 57.71           O  
ANISOU 3051  OD1 ASN B  71     7331   6174   8421    299    864   1190       O  
ATOM   3052  ND2 ASN B  71      23.493 110.262   1.361  1.00 60.72           N  
ANISOU 3052  ND2 ASN B  71     7569   6457   9043    352    947   1350       N  
ATOM   3053  N   ALA B  72      28.320 110.829   2.760  1.00 43.75           N  
ANISOU 3053  N   ALA B  72     5797   4312   6513    320   1050    751       N  
ATOM   3054  CA  ALA B  72      29.558 110.814   2.026  1.00 43.06           C  
ANISOU 3054  CA  ALA B  72     5759   4288   6313    289    977    712       C  
ATOM   3055  C   ALA B  72      29.429 109.985   0.734  1.00 40.20           C  
ANISOU 3055  C   ALA B  72     5381   4040   5852    248    834    813       C  
ATOM   3056  O   ALA B  72      30.304 110.046  -0.100  1.00 35.39           O  
ANISOU 3056  O   ALA B  72     4798   3479   5168    218    778    812       O  
ATOM   3057  CB  ALA B  72      30.677 110.310   2.900  1.00 42.96           C  
ANISOU 3057  CB  ALA B  72     5857   4298   6164    272    986    532       C  
ATOM   3058  N   SER B  73      28.324 109.257   0.541  1.00 38.72           N  
ANISOU 3058  N   SER B  73     5152   3892   5668    240    780    904       N  
ATOM   3059  CA  SER B  73      28.252 108.243  -0.535  1.00 39.96           C  
ANISOU 3059  CA  SER B  73     5323   4167   5694    180    646    965       C  
ATOM   3060  C   SER B  73      28.179 108.889  -1.927  1.00 35.73           C  
ANISOU 3060  C   SER B  73     4722   3665   5190    141    584   1119       C  
ATOM   3061  O   SER B  73      28.925 108.527  -2.841  1.00 34.23           O  
ANISOU 3061  O   SER B  73     4581   3551   4871     84    510   1108       O  
ATOM   3062  CB  SER B  73      27.121 107.253  -0.264  1.00 41.40           C  
ANISOU 3062  CB  SER B  73     5485   4382   5863    173    607   1007       C  
ATOM   3063  OG  SER B  73      27.482 106.378   0.809  1.00 37.48           O  
ANISOU 3063  OG  SER B  73     5073   3888   5279    189    636    853       O  
ATOM   3064  N   VAL B  74      27.317 109.882  -2.097  1.00 36.03           N  
ANISOU 3064  N   VAL B  74     4645   3639   5405    167    621   1267       N  
ATOM   3065  CA  VAL B  74      27.109 110.482  -3.427  1.00 40.60           C  
ANISOU 3065  CA  VAL B  74     5144   4258   6021    123    550   1446       C  
ATOM   3066  C   VAL B  74      28.367 111.260  -3.851  1.00 38.53           C  
ANISOU 3066  C   VAL B  74     4921   3981   5735    121    575   1391       C  
ATOM   3067  O   VAL B  74      28.822 111.139  -4.989  1.00 36.29           O  
ANISOU 3067  O   VAL B  74     4657   3780   5350     56    488   1444       O  
ATOM   3068  CB  VAL B  74      25.819 111.329  -3.448  1.00 43.33           C  
ANISOU 3068  CB  VAL B  74     5338   4532   6590    158    587   1640       C  
ATOM   3069  CG1 VAL B  74      25.616 112.092  -4.749  1.00 45.23           C  
ANISOU 3069  CG1 VAL B  74     5481   4808   6894    114    518   1846       C  
ATOM   3070  CG2 VAL B  74      24.611 110.462  -3.137  1.00 42.88           C  
ANISOU 3070  CG2 VAL B  74     5243   4502   6546    150    548   1701       C  
ATOM   3071  N   PRO B  75      28.965 112.101  -2.976  1.00 37.46           N  
ANISOU 3071  N   PRO B  75     4802   3741   5690    184    697   1286       N  
ATOM   3072  CA  PRO B  75      30.216 112.793  -3.304  1.00 37.96           C  
ANISOU 3072  CA  PRO B  75     4906   3788   5727    181    722   1222       C  
ATOM   3073  C   PRO B  75      31.375 111.842  -3.654  1.00 32.44           C  
ANISOU 3073  C   PRO B  75     4326   3182   4817    132    651   1097       C  
ATOM   3074  O   PRO B  75      32.111 112.084  -4.603  1.00 31.33           O  
ANISOU 3074  O   PRO B  75     4203   3083   4619     94    610   1122       O  
ATOM   3075  CB  PRO B  75      30.576 113.541  -2.013  1.00 39.19           C  
ANISOU 3075  CB  PRO B  75     5081   3821   5985    243    866   1093       C  
ATOM   3076  CG  PRO B  75      29.269 113.692  -1.277  1.00 40.23           C  
ANISOU 3076  CG  PRO B  75     5140   3879   6266    285    937   1155       C  
ATOM   3077  CD  PRO B  75      28.438 112.490  -1.661  1.00 37.34           C  
ANISOU 3077  CD  PRO B  75     4764   3612   5811    250    824   1228       C  
ATOM   3078  N   ARG B  76      31.523 110.781  -2.859  1.00 31.12           N  
ANISOU 3078  N   ARG B  76     4235   3039   4548    134    646    967       N  
ATOM   3079  CA  ARG B  76      32.563 109.799  -3.073  1.00 28.45           C  
ANISOU 3079  CA  ARG B  76     3999   2774   4036     95    596    853       C  
ATOM   3080  C   ARG B  76      32.380 109.152  -4.445  1.00 29.09           C  
ANISOU 3080  C   ARG B  76     4087   2956   4009     16    492    946       C  
ATOM   3081  O   ARG B  76      33.368 108.960  -5.194  1.00 28.18           O  
ANISOU 3081  O   ARG B  76     4030   2884   3793    -26    465    907       O  
ATOM   3082  CB  ARG B  76      32.570 108.765  -1.955  1.00 29.10           C  
ANISOU 3082  CB  ARG B  76     4142   2861   4052    112    610    727       C  
ATOM   3083  CG  ARG B  76      33.325 109.200  -0.709  1.00 30.02           C  
ANISOU 3083  CG  ARG B  76     4297   2907   4200    155    698    592       C  
ATOM   3084  CD  ARG B  76      33.038 108.207   0.410  1.00 33.16           C  
ANISOU 3084  CD  ARG B  76     4737   3315   4545    166    706    504       C  
ATOM   3085  NE  ARG B  76      33.991 108.329   1.499  1.00 36.21           N  
ANISOU 3085  NE  ARG B  76     5180   3668   4907    178    760    368       N  
ATOM   3086  CZ  ARG B  76      33.844 107.784   2.693  1.00 39.83           C  
ANISOU 3086  CZ  ARG B  76     5675   4121   5337    186    787    286       C  
ATOM   3087  NH1 ARG B  76      32.744 107.102   2.969  1.00 40.86           N  
ANISOU 3087  NH1 ARG B  76     5787   4265   5472    196    775    323       N  
ATOM   3088  NH2 ARG B  76      34.804 107.919   3.594  1.00 43.45           N  
ANISOU 3088  NH2 ARG B  76     6185   4564   5760    178    821    175       N  
ATOM   3089  N   ASN B  77      31.129 108.838  -4.798  1.00 28.59           N  
ANISOU 3089  N   ASN B  77     3965   2929   3966    -10    436   1072       N  
ATOM   3090  CA  ASN B  77      30.869 108.231  -6.106  1.00 29.58           C  
ANISOU 3090  CA  ASN B  77     4101   3159   3976   -108    333   1166       C  
ATOM   3091  C   ASN B  77      31.198 109.225  -7.212  1.00 31.16           C  
ANISOU 3091  C   ASN B  77     4263   3373   4202   -144    310   1277       C  
ATOM   3092  O   ASN B  77      31.721 108.819  -8.247  1.00 31.72           O  
ANISOU 3092  O   ASN B  77     4392   3521   4138   -228    255   1281       O  
ATOM   3093  CB  ASN B  77      29.436 107.736  -6.272  1.00 30.03           C  
ANISOU 3093  CB  ASN B  77     4096   3260   4052   -142    267   1293       C  
ATOM   3094  CG  ASN B  77      29.155 106.501  -5.439  1.00 28.25           C  
ANISOU 3094  CG  ASN B  77     3925   3047   3760   -130    270   1185       C  
ATOM   3095  OD1 ASN B  77      30.062 105.741  -5.067  1.00 26.32           O  
ANISOU 3095  OD1 ASN B  77     3777   2809   3411   -127    294   1030       O  
ATOM   3096  ND2 ASN B  77      27.891 106.328  -5.107  1.00 29.29           N  
ANISOU 3096  ND2 ASN B  77     3986   3174   3968   -119    252   1277       N  
ATOM   3097  N   THR B  78      30.869 110.503  -6.970  1.00 32.23           N  
ANISOU 3097  N   THR B  78     4301   3429   4515    -84    363   1367       N  
ATOM   3098  CA  THR B  78      31.196 111.600  -7.878  1.00 36.11           C  
ANISOU 3098  CA  THR B  78     4741   3914   5063   -102    358   1479       C  
ATOM   3099  C   THR B  78      32.708 111.626  -8.110  1.00 34.03           C  
ANISOU 3099  C   THR B  78     4575   3655   4699   -111    385   1342       C  
ATOM   3100  O   THR B  78      33.181 111.655  -9.264  1.00 37.09           O  
ANISOU 3100  O   THR B  78     4990   4108   4994   -186    333   1392       O  
ATOM   3101  CB  THR B  78      30.649 112.926  -7.335  1.00 37.07           C  
ANISOU 3101  CB  THR B  78     4745   3922   5417    -19    442   1570       C  
ATOM   3102  OG1 THR B  78      29.242 112.752  -7.185  1.00 41.02           O  
ANISOU 3102  OG1 THR B  78     5152   4423   6008    -17    414   1705       O  
ATOM   3103  CG2 THR B  78      30.935 114.101  -8.242  1.00 39.02           C  
ANISOU 3103  CG2 THR B  78     4924   4155   5745    -32    442   1700       C  
ATOM   3104  N   GLY B  79      33.461 111.605  -7.005  1.00 34.28           N  
ANISOU 3104  N   GLY B  79     4659   3616   4748    -43    468   1173       N  
ATOM   3105  CA  GLY B  79      34.926 111.560  -7.031  1.00 31.70           C  
ANISOU 3105  CA  GLY B  79     4417   3284   4341    -44    499   1037       C  
ATOM   3106  C   GLY B  79      35.461 110.421  -7.886  1.00 33.65           C  
ANISOU 3106  C   GLY B  79     4755   3626   4405   -127    436    994       C  
ATOM   3107  O   GLY B  79      36.379 110.648  -8.717  1.00 32.43           O  
ANISOU 3107  O   GLY B  79     4637   3491   4191   -165    434    986       O  
ATOM   3108  N   LEU B  80      34.898 109.207  -7.701  1.00 30.88           N  
ANISOU 3108  N   LEU B  80     4440   3325   3966   -157    395    965       N  
ATOM   3109  CA  LEU B  80      35.321 107.997  -8.464  1.00 31.84           C  
ANISOU 3109  CA  LEU B  80     4654   3527   3916   -243    353    913       C  
ATOM   3110  C   LEU B  80      35.147 108.200  -9.975  1.00 34.09           C  
ANISOU 3110  C   LEU B  80     4939   3888   4126   -348    290   1037       C  
ATOM   3111  O   LEU B  80      36.025 107.795 -10.747  1.00 32.39           O  
ANISOU 3111  O   LEU B  80     4804   3706   3796   -413    296    981       O  
ATOM   3112  CB  LEU B  80      34.517 106.768  -8.018  1.00 30.80           C  
ANISOU 3112  CB  LEU B  80     4545   3431   3726   -261    322    885       C  
ATOM   3113  CG  LEU B  80      34.934 106.189  -6.675  1.00 29.60           C  
ANISOU 3113  CG  LEU B  80     4426   3228   3592   -186    377    741       C  
ATOM   3114  CD1 LEU B  80      33.957 105.112  -6.228  1.00 29.12           C  
ANISOU 3114  CD1 LEU B  80     4369   3199   3496   -197    346    738       C  
ATOM   3115  CD2 LEU B  80      36.349 105.658  -6.750  1.00 30.25           C  
ANISOU 3115  CD2 LEU B  80     4590   3304   3597   -195    416    614       C  
ATOM   3116  N   LYS B  81      34.004 108.769 -10.378  1.00 35.80           N  
ANISOU 3116  N   LYS B  81     5066   4130   4406   -372    233   1208       N  
ATOM   3117  CA  LYS B  81      33.696 109.041 -11.788  1.00 37.61           C  
ANISOU 3117  CA  LYS B  81     5280   4443   4567   -484    156   1358       C  
ATOM   3118  C   LYS B  81      34.727 110.003 -12.389  1.00 37.72           C  
ANISOU 3118  C   LYS B  81     5300   4433   4598   -482    192   1364       C  
ATOM   3119  O   LYS B  81      35.050 109.878 -13.546  1.00 38.00           O  
ANISOU 3119  O   LYS B  81     5385   4540   4513   -587    154   1405       O  
ATOM   3120  CB  LYS B  81      32.295 109.638 -11.955  1.00 41.43           C  
ANISOU 3120  CB  LYS B  81     5635   4945   5158   -493     91   1564       C  
ATOM   3121  CG  LYS B  81      31.153 108.670 -11.691  1.00 46.34           C  
ANISOU 3121  CG  LYS B  81     6246   5615   5745   -528     32   1597       C  
ATOM   3122  CD  LYS B  81      29.803 109.330 -11.549  1.00 50.40           C  
ANISOU 3122  CD  LYS B  81     6614   6117   6418   -504     -8   1794       C  
ATOM   3123  CE  LYS B  81      28.754 108.348 -11.068  1.00 51.94           C  
ANISOU 3123  CE  LYS B  81     6798   6340   6594   -518    -49   1801       C  
ATOM   3124  NZ  LYS B  81      27.399 108.940 -11.142  1.00 59.00           N  
ANISOU 3124  NZ  LYS B  81     7541   7234   7640   -515   -101   2023       N  
ATOM   3125  N   MET B  82      35.252 110.930 -11.580  1.00 37.58           N  
ANISOU 3125  N   MET B  82     5239   4314   4723   -369    270   1317       N  
ATOM   3126  CA  MET B  82      36.180 111.967 -12.042  1.00 35.82           C  
ANISOU 3126  CA  MET B  82     5007   4055   4545   -355    310   1329       C  
ATOM   3127  C   MET B  82      37.614 111.437 -12.121  1.00 33.73           C  
ANISOU 3127  C   MET B  82     4855   3784   4174   -365    360   1161       C  
ATOM   3128  O   MET B  82      38.425 111.974 -12.870  1.00 35.20           O  
ANISOU 3128  O   MET B  82     5062   3972   4339   -393    377   1174       O  
ATOM   3129  CB  MET B  82      36.157 113.184 -11.111  1.00 36.34           C  
ANISOU 3129  CB  MET B  82     4984   4008   4813   -238    384   1339       C  
ATOM   3130  CG  MET B  82      34.853 113.958 -11.158  1.00 37.72           C  
ANISOU 3130  CG  MET B  82     5028   4166   5135   -221    359   1529       C  
ATOM   3131  SD  MET B  82      34.761 115.201  -9.826  1.00 40.47           S  
ANISOU 3131  SD  MET B  82     5290   4357   5728    -85    484   1499       S  
ATOM   3132  CE  MET B  82      35.884 116.441 -10.473  1.00 38.12           C  
ANISOU 3132  CE  MET B  82     4980   4016   5484    -77    530   1518       C  
ATOM   3133  N   SER B  83      37.943 110.404 -11.346  1.00 31.00           N  
ANISOU 3133  N   SER B  83     4577   3427   3775   -340    388   1014       N  
ATOM   3134  CA  SER B  83      39.316 109.896 -11.298  1.00 32.86           C  
ANISOU 3134  CA  SER B  83     4901   3641   3943   -337    445    865       C  
ATOM   3135  C   SER B  83      39.660 109.006 -12.500  1.00 35.95           C  
ANISOU 3135  C   SER B  83     5385   4107   4168   -456    427    852       C  
ATOM   3136  O   SER B  83      38.914 108.088 -12.827  1.00 38.50           O  
ANISOU 3136  O   SER B  83     5739   4493   4393   -529    381    872       O  
ATOM   3137  CB  SER B  83      39.583 109.110 -10.063  1.00 30.95           C  
ANISOU 3137  CB  SER B  83     4686   3359   3712   -274    482    729       C  
ATOM   3138  OG  SER B  83      40.871 108.523 -10.197  1.00 31.76           O  
ANISOU 3138  OG  SER B  83     4865   3449   3751   -286    530    614       O  
ATOM   3139  N   LYS B  84      40.884 109.170 -13.017  1.00 38.75           N  
ANISOU 3139  N   LYS B  84     5790   4441   4490   -472    480    793       N  
ATOM   3140  CA  LYS B  84      41.415 108.324 -14.113  1.00 43.08           C  
ANISOU 3140  CA  LYS B  84     6442   5040   4887   -584    497    753       C  
ATOM   3141  C   LYS B  84      42.743 107.656 -13.709  1.00 40.14           C  
ANISOU 3141  C   LYS B  84     6133   4606   4512   -547    589    596       C  
ATOM   3142  O   LYS B  84      43.448 107.121 -14.577  1.00 42.41           O  
ANISOU 3142  O   LYS B  84     6504   4905   4704   -626    638    549       O  
ATOM   3143  CB  LYS B  84      41.603 109.173 -15.377  1.00 47.30           C  
ANISOU 3143  CB  LYS B  84     6978   5613   5380   -662    480    857       C  
ATOM   3144  CG  LYS B  84      41.332 108.440 -16.679  1.00 52.81           C  
ANISOU 3144  CG  LYS B  84     7765   6404   5897   -825    453    890       C  
ATOM   3145  N   ALA B  85      43.035 107.625 -12.399  1.00 33.18           N  
ANISOU 3145  N   ALA B  85     5213   3660   3731   -438    614    522       N  
ATOM   3146  CA  ALA B  85      44.328 107.226 -11.816  1.00 30.29           C  
ANISOU 3146  CA  ALA B  85     4873   3230   3404   -385    689    401       C  
ATOM   3147  C   ALA B  85      44.386 105.705 -11.595  1.00 26.68           C  
ANISOU 3147  C   ALA B  85     4476   2778   2881   -411    718    316       C  
ATOM   3148  O   ALA B  85      43.400 105.015 -11.675  1.00 26.43           O  
ANISOU 3148  O   ALA B  85     4463   2795   2785   -456    678    336       O  
ATOM   3149  CB  ALA B  85      44.538 107.941 -10.495  1.00 28.54           C  
ANISOU 3149  CB  ALA B  85     4580   2950   3312   -276    690    377       C  
ATOM   3150  N   GLU B  86      45.572 105.226 -11.231  1.00 25.24           N  
ANISOU 3150  N   GLU B  86     4314   2540   2736   -377    789    226       N  
ATOM   3151  CA  GLU B  86      45.822 103.843 -10.971  1.00 26.39           C  
ANISOU 3151  CA  GLU B  86     4504   2670   2853   -389    836    148       C  
ATOM   3152  C   GLU B  86      45.182 103.423  -9.637  1.00 23.43           C  
ANISOU 3152  C   GLU B  86     4082   2294   2523   -321    792    132       C  
ATOM   3153  O   GLU B  86      44.586 102.368  -9.536  1.00 24.01           O  
ANISOU 3153  O   GLU B  86     4186   2390   2546   -350    789    111       O  
ATOM   3154  CB  GLU B  86      47.328 103.627 -10.917  1.00 30.82           C  
ANISOU 3154  CB  GLU B  86     5074   3161   3474   -362    926     82       C  
ATOM   3155  CG  GLU B  86      47.709 102.166 -10.926  1.00 35.62           C  
ANISOU 3155  CG  GLU B  86     5729   3739   4063   -387   1001     12       C  
ATOM   3156  CD  GLU B  86      49.183 101.914 -11.185  1.00 39.81           C  
ANISOU 3156  CD  GLU B  86     6271   4196   4659   -379   1108    -35       C  
ATOM   3157  OE1 GLU B  86      49.550 100.719 -11.245  1.00 43.83           O  
ANISOU 3157  OE1 GLU B  86     6815   4666   5173   -399   1190    -87       O  
ATOM   3158  OE2 GLU B  86      49.952 102.909 -11.287  1.00 39.11           O  
ANISOU 3158  OE2 GLU B  86     6150   4081   4626   -348   1114    -15       O  
ATOM   3159  N   TYR B  87      45.379 104.253  -8.616  1.00 22.72           N  
ANISOU 3159  N   TYR B  87     3927   2176   2528   -238    768    137       N  
ATOM   3160  CA  TYR B  87      44.848 104.045  -7.263  1.00 20.73           C  
ANISOU 3160  CA  TYR B  87     3633   1921   2321   -177    732    121       C  
ATOM   3161  C   TYR B  87      44.002 105.240  -6.840  1.00 22.05           C  
ANISOU 3161  C   TYR B  87     3747   2096   2535   -143    682    179       C  
ATOM   3162  O   TYR B  87      44.219 106.361  -7.286  1.00 19.66           O  
ANISOU 3162  O   TYR B  87     3421   1779   2266   -141    684    220       O  
ATOM   3163  CB  TYR B  87      46.000 103.847  -6.276  1.00 21.00           C  
ANISOU 3163  CB  TYR B  87     3643   1907   2427   -122    764     62       C  
ATOM   3164  CG  TYR B  87      46.704 102.513  -6.409  1.00 22.69           C  
ANISOU 3164  CG  TYR B  87     3890   2102   2630   -140    820     14       C  
ATOM   3165  CD1 TYR B  87      46.195 101.374  -5.809  1.00 21.67           C  
ANISOU 3165  CD1 TYR B  87     3766   1984   2482   -135    814     -7       C  
ATOM   3166  CD2 TYR B  87      47.865 102.379  -7.165  1.00 21.51           C  
ANISOU 3166  CD2 TYR B  87     3762   1912   2496   -162    891     -6       C  
ATOM   3167  CE1 TYR B  87      46.818 100.134  -5.932  1.00 21.55           C  
ANISOU 3167  CE1 TYR B  87     3773   1938   2474   -149    879    -45       C  
ATOM   3168  CE2 TYR B  87      48.522 101.161  -7.266  1.00 24.05           C  
ANISOU 3168  CE2 TYR B  87     4106   2199   2833   -174    963    -45       C  
ATOM   3169  CZ  TYR B  87      47.998 100.033  -6.643  1.00 23.60           C  
ANISOU 3169  CZ  TYR B  87     4050   2150   2766   -167    958    -64       C  
ATOM   3170  OH  TYR B  87      48.616  98.815  -6.742  1.00 24.20           O  
ANISOU 3170  OH  TYR B  87     4140   2181   2873   -178   1041    -97       O  
ATOM   3171  N   VAL B  88      43.032 105.001  -5.949  1.00 20.72           N  
ANISOU 3171  N   VAL B  88     3554   1940   2378   -114    647    185       N  
ATOM   3172  CA  VAL B  88      42.309 106.085  -5.333  1.00 21.33           C  
ANISOU 3172  CA  VAL B  88     3577   2002   2524    -73    625    227       C  
ATOM   3173  C   VAL B  88      42.504 105.919  -3.825  1.00 20.66           C  
ANISOU 3173  C   VAL B  88     3476   1889   2483    -20    635    161       C  
ATOM   3174  O   VAL B  88      42.711 104.800  -3.328  1.00 20.35           O  
ANISOU 3174  O   VAL B  88     3459   1862   2410    -19    635    113       O  
ATOM   3175  CB  VAL B  88      40.811 106.112  -5.698  1.00 24.34           C  
ANISOU 3175  CB  VAL B  88     3937   2422   2888    -96    581    312       C  
ATOM   3176  CG1 VAL B  88      40.587 106.344  -7.189  1.00 25.96           C  
ANISOU 3176  CG1 VAL B  88     4155   2668   3038   -167    558    394       C  
ATOM   3177  CG2 VAL B  88      40.081 104.856  -5.229  1.00 23.64           C  
ANISOU 3177  CG2 VAL B  88     3869   2365   2749   -104    559    288       C  
ATOM   3178  N   PHE B  89      42.429 107.037  -3.107  1.00 20.00           N  
ANISOU 3178  N   PHE B  89     3355   1767   2474     14    648    161       N  
ATOM   3179  CA  PHE B  89      42.555 107.079  -1.673  1.00 20.80           C  
ANISOU 3179  CA  PHE B  89     3448   1846   2607     45    659    101       C  
ATOM   3180  C   PHE B  89      41.465 108.008  -1.148  1.00 21.80           C  
ANISOU 3180  C   PHE B  89     3539   1943   2798     68    674    132       C  
ATOM   3181  O   PHE B  89      41.402 109.162  -1.539  1.00 21.49           O  
ANISOU 3181  O   PHE B  89     3472   1869   2824     75    698    172       O  
ATOM   3182  CB  PHE B  89      43.971 107.508  -1.258  1.00 21.65           C  
ANISOU 3182  CB  PHE B  89     3558   1925   2743     48    680     46       C  
ATOM   3183  CG  PHE B  89      44.261 107.301   0.204  1.00 22.86           C  
ANISOU 3183  CG  PHE B  89     3712   2073   2899     55    679    -14       C  
ATOM   3184  CD1 PHE B  89      43.674 108.100   1.166  1.00 26.27           C  
ANISOU 3184  CD1 PHE B  89     4134   2478   3367     63    700    -35       C  
ATOM   3185  CD2 PHE B  89      45.083 106.276   0.635  1.00 27.32           C  
ANISOU 3185  CD2 PHE B  89     4287   2660   3432     47    661    -46       C  
ATOM   3186  CE1 PHE B  89      43.916 107.885   2.521  1.00 25.52           C  
ANISOU 3186  CE1 PHE B  89     4052   2388   3255     50    697    -93       C  
ATOM   3187  CE2 PHE B  89      45.345 106.074   1.988  1.00 25.88           C  
ANISOU 3187  CE2 PHE B  89     4103   2486   3243     40    647    -87       C  
ATOM   3188  CZ  PHE B  89      44.730 106.852   2.929  1.00 25.61           C  
ANISOU 3188  CZ  PHE B  89     4072   2436   3223     36    662   -114       C  
ATOM   3189  N   PHE B  90      40.570 107.490  -0.302  1.00 22.93           N  
ANISOU 3189  N   PHE B  90     3682   2095   2934     81    668    121       N  
ATOM   3190  CA  PHE B  90      39.513 108.314   0.244  1.00 22.20           C  
ANISOU 3190  CA  PHE B  90     3555   1962   2916    104    702    149       C  
ATOM   3191  C   PHE B  90      40.029 108.966   1.527  1.00 23.99           C  
ANISOU 3191  C   PHE B  90     3793   2141   3178    110    752     66       C  
ATOM   3192  O   PHE B  90      40.630 108.292   2.387  1.00 21.93           O  
ANISOU 3192  O   PHE B  90     3566   1904   2862     97    738     -3       O  
ATOM   3193  CB  PHE B  90      38.260 107.486   0.494  1.00 23.93           C  
ANISOU 3193  CB  PHE B  90     3767   2207   3115    109    679    180       C  
ATOM   3194  CG  PHE B  90      37.678 106.900  -0.763  1.00 21.63           C  
ANISOU 3194  CG  PHE B  90     3467   1966   2782     84    627    264       C  
ATOM   3195  CD1 PHE B  90      36.877 107.666  -1.583  1.00 22.30           C  
ANISOU 3195  CD1 PHE B  90     3502   2044   2926     80    621    372       C  
ATOM   3196  CD2 PHE B  90      37.878 105.569  -1.080  1.00 20.95           C  
ANISOU 3196  CD2 PHE B  90     3422   1934   2601     56    588    241       C  
ATOM   3197  CE1 PHE B  90      36.339 107.125  -2.741  1.00 23.35           C  
ANISOU 3197  CE1 PHE B  90     3631   2235   3003     35    562    455       C  
ATOM   3198  CE2 PHE B  90      37.331 105.022  -2.230  1.00 21.18           C  
ANISOU 3198  CE2 PHE B  90     3455   2012   2577     13    545    309       C  
ATOM   3199  CZ  PHE B  90      36.594 105.808  -3.077  1.00 22.51           C  
ANISOU 3199  CZ  PHE B  90     3580   2186   2785     -3    525    415       C  
ATOM   3200  N   LEU B  91      39.776 110.276   1.651  1.00 23.50           N  
ANISOU 3200  N   LEU B  91     3703   2014   3210    121    812     79       N  
ATOM   3201  CA  LEU B  91      40.216 111.072   2.766  1.00 27.23           C  
ANISOU 3201  CA  LEU B  91     4193   2434   3718    110    875     -2       C  
ATOM   3202  C   LEU B  91      38.988 111.779   3.348  1.00 29.52           C  
ANISOU 3202  C   LEU B  91     4458   2657   4100    129    953     13       C  
ATOM   3203  O   LEU B  91      38.205 112.391   2.628  1.00 30.01           O  
ANISOU 3203  O   LEU B  91     4465   2683   4254    156    978    103       O  
ATOM   3204  CB  LEU B  91      41.275 112.075   2.288  1.00 27.73           C  
ANISOU 3204  CB  LEU B  91     4249   2464   3821    100    896    -12       C  
ATOM   3205  CG  LEU B  91      41.707 113.138   3.303  1.00 31.64           C  
ANISOU 3205  CG  LEU B  91     4761   2893   4364     76    973    -93       C  
ATOM   3206  CD1 LEU B  91      42.449 112.509   4.486  1.00 32.74           C  
ANISOU 3206  CD1 LEU B  91     4954   3073   4412     30    947   -188       C  
ATOM   3207  CD2 LEU B  91      42.594 114.174   2.625  1.00 31.92           C  
ANISOU 3207  CD2 LEU B  91     4779   2892   4457     72    995    -84       C  
ATOM   3208  N   ASP B  92      38.805 111.651   4.662  1.00 31.81           N  
ANISOU 3208  N   ASP B  92     4785   2931   4369    110    995    -67       N  
ATOM   3209  CA  ASP B  92      37.771 112.428   5.341  1.00 34.14           C  
ANISOU 3209  CA  ASP B  92     5066   3143   4762    121   1100    -73       C  
ATOM   3210  C   ASP B  92      38.317 113.841   5.584  1.00 28.73           C  
ANISOU 3210  C   ASP B  92     4383   2372   4158    101   1194   -121       C  
ATOM   3211  O   ASP B  92      39.450 114.002   5.995  1.00 26.12           O  
ANISOU 3211  O   ASP B  92     4098   2058   3768     56   1183   -202       O  
ATOM   3212  CB  ASP B  92      37.340 111.726   6.629  1.00 37.78           C  
ANISOU 3212  CB  ASP B  92     5575   3620   5159     98   1117   -145       C  
ATOM   3213  CG  ASP B  92      36.551 110.451   6.403  1.00 44.45           C  
ANISOU 3213  CG  ASP B  92     6406   4528   5955    124   1046    -88       C  
ATOM   3214  OD1 ASP B  92      35.980 110.288   5.297  1.00 51.45           O  
ANISOU 3214  OD1 ASP B  92     7238   5428   6880    159   1005     15       O  
ATOM   3215  OD2 ASP B  92      36.480 109.638   7.348  1.00 51.94           O  
ANISOU 3215  OD2 ASP B  92     7398   5513   6823    103   1032   -144       O  
ATOM   3216  N   SER B  93      37.470 114.854   5.413  1.00 30.98           N  
ANISOU 3216  N   SER B  93     4618   2563   4590    130   1293    -70       N  
ATOM   3217  CA  SER B  93      37.887 116.234   5.523  1.00 32.32           C  
ANISOU 3217  CA  SER B  93     4782   2637   4860    116   1397   -105       C  
ATOM   3218  C   SER B  93      38.359 116.644   6.934  1.00 34.08           C  
ANISOU 3218  C   SER B  93     5085   2817   5044     47   1485   -256       C  
ATOM   3219  O   SER B  93      39.052 117.635   7.036  1.00 34.20           O  
ANISOU 3219  O   SER B  93     5115   2776   5103     16   1548   -308       O  
ATOM   3220  CB  SER B  93      36.838 117.176   4.999  1.00 38.29           C  
ANISOU 3220  CB  SER B  93     5453   3294   5801    166   1490      0       C  
ATOM   3221  OG  SER B  93      35.528 116.801   5.359  1.00 39.93           O  
ANISOU 3221  OG  SER B  93     5631   3476   6061    195   1529     44       O  
ATOM   3222  N   ASP B  94      38.062 115.901   8.002  1.00 33.22           N  
ANISOU 3222  N   ASP B  94     5034   2741   4845     12   1485   -327       N  
ATOM   3223  CA  ASP B  94      38.687 116.232   9.331  1.00 40.69           C  
ANISOU 3223  CA  ASP B  94     6071   3671   5718    -80   1549   -472       C  
ATOM   3224  C   ASP B  94      40.185 115.848   9.377  1.00 41.02           C  
ANISOU 3224  C   ASP B  94     6151   3806   5626   -136   1435   -519       C  
ATOM   3225  O   ASP B  94      40.962 116.461  10.118  1.00 42.17           O  
ANISOU 3225  O   ASP B  94     6354   3934   5735   -219   1477   -617       O  
ATOM   3226  CB  ASP B  94      37.903 115.612  10.503  1.00 42.80           C  
ANISOU 3226  CB  ASP B  94     6391   3945   5925   -112   1590   -530       C  
ATOM   3227  N   ASP B  95      40.615 114.879   8.555  1.00 36.52           N  
ANISOU 3227  N   ASP B  95     5550   3329   4995    -96   1298   -447       N  
ATOM   3228  CA  ASP B  95      41.834 114.081   8.797  1.00 33.03           C  
ANISOU 3228  CA  ASP B  95     5139   2986   4423   -143   1184   -477       C  
ATOM   3229  C   ASP B  95      43.081 114.672   8.107  1.00 32.34           C  
ANISOU 3229  C   ASP B  95     5034   2899   4354   -154   1152   -471       C  
ATOM   3230  O   ASP B  95      43.018 115.690   7.417  1.00 32.10           O  
ANISOU 3230  O   ASP B  95     4969   2796   4429   -125   1214   -446       O  
ATOM   3231  CB  ASP B  95      41.523 112.636   8.418  1.00 30.22           C  
ANISOU 3231  CB  ASP B  95     4763   2715   4002    -98   1081   -412       C  
ATOM   3232  CG  ASP B  95      40.390 112.051   9.250  1.00 34.39           C  
ANISOU 3232  CG  ASP B  95     5314   3246   4505    -97   1112   -427       C  
ATOM   3233  OD1 ASP B  95      40.056 112.651  10.308  1.00 36.32           O  
ANISOU 3233  OD1 ASP B  95     5605   3440   4753   -150   1206   -504       O  
ATOM   3234  OD2 ASP B  95      39.834 111.030   8.830  1.00 31.40           O  
ANISOU 3234  OD2 ASP B  95     4911   2915   4104    -50   1051   -365       O  
ATOM   3235  N   LEU B  96      44.234 114.042   8.365  1.00 27.95           N  
ANISOU 3235  N   LEU B  96     4495   2420   3702   -199   1060   -491       N  
ATOM   3236  CA  LEU B  96      45.571 114.492   7.913  1.00 27.19           C  
ANISOU 3236  CA  LEU B  96     4385   2332   3613   -224   1023   -492       C  
ATOM   3237  C   LEU B  96      46.363 113.313   7.339  1.00 25.87           C  
ANISOU 3237  C   LEU B  96     4189   2248   3390   -200    907   -432       C  
ATOM   3238  O   LEU B  96      46.312 112.221   7.904  1.00 24.24           O  
ANISOU 3238  O   LEU B  96     3995   2106   3107   -214    848   -429       O  
ATOM   3239  CB  LEU B  96      46.354 115.049   9.099  1.00 29.36           C  
ANISOU 3239  CB  LEU B  96     4713   2609   3834   -335   1041   -586       C  
ATOM   3240  CG  LEU B  96      45.707 116.190   9.869  1.00 32.31           C  
ANISOU 3240  CG  LEU B  96     5133   2893   4249   -385   1176   -672       C  
ATOM   3241  CD1 LEU B  96      46.574 116.533  11.066  1.00 34.05           C  
ANISOU 3241  CD1 LEU B  96     5417   3139   4379   -521   1174   -767       C  
ATOM   3242  CD2 LEU B  96      45.477 117.415   8.989  1.00 34.16           C  
ANISOU 3242  CD2 LEU B  96     5329   3022   4625   -334   1272   -652       C  
ATOM   3243  N   LEU B  97      47.067 113.531   6.212  1.00 23.40           N  
ANISOU 3243  N   LEU B  97     3837   1927   3124   -164    886   -384       N  
ATOM   3244  CA  LEU B  97      48.045 112.565   5.720  1.00 23.64           C  
ANISOU 3244  CA  LEU B  97     3844   2018   3118   -155    800   -340       C  
ATOM   3245  C   LEU B  97      49.441 112.968   6.210  1.00 24.58           C  
ANISOU 3245  C   LEU B  97     3962   2149   3228   -222    773   -371       C  
ATOM   3246  O   LEU B  97      49.805 114.154   6.170  1.00 23.42           O  
ANISOU 3246  O   LEU B  97     3819   1950   3129   -249    821   -405       O  
ATOM   3247  CB  LEU B  97      48.052 112.539   4.194  1.00 23.84           C  
ANISOU 3247  CB  LEU B  97     3835   2028   3195    -89    801   -271       C  
ATOM   3248  CG  LEU B  97      46.785 112.116   3.466  1.00 23.79           C  
ANISOU 3248  CG  LEU B  97     3820   2021   3195    -33    811   -218       C  
ATOM   3249  CD1 LEU B  97      47.062 112.093   1.966  1.00 22.22           C  
ANISOU 3249  CD1 LEU B  97     3596   1821   3024      2    802   -152       C  
ATOM   3250  CD2 LEU B  97      46.299 110.745   3.952  1.00 25.99           C  
ANISOU 3250  CD2 LEU B  97     4113   2357   3402    -29    764   -214       C  
ATOM   3251  N   HIS B  98      50.214 111.957   6.620  1.00 23.24           N  
ANISOU 3251  N   HIS B  98     3779   2045   3006   -250    695   -350       N  
ATOM   3252  CA  HIS B  98      51.665 112.001   6.773  1.00 22.79           C  
ANISOU 3252  CA  HIS B  98     3693   2010   2953   -299    644   -337       C  
ATOM   3253  C   HIS B  98      52.241 112.353   5.396  1.00 22.84           C  
ANISOU 3253  C   HIS B  98     3663   1974   3038   -242    665   -295       C  
ATOM   3254  O   HIS B  98      51.718 111.881   4.362  1.00 22.05           O  
ANISOU 3254  O   HIS B  98     3554   1865   2958   -171    682   -254       O  
ATOM   3255  CB  HIS B  98      52.188 110.614   7.228  1.00 22.07           C  
ANISOU 3255  CB  HIS B  98     3574   1991   2819   -312    561   -286       C  
ATOM   3256  CG  HIS B  98      53.599 110.600   7.714  1.00 23.68           C  
ANISOU 3256  CG  HIS B  98     3741   2229   3027   -381    499   -259       C  
ATOM   3257  ND1 HIS B  98      54.681 110.608   6.851  1.00 25.00           N  
ANISOU 3257  ND1 HIS B  98     3854   2375   3268   -354    490   -208       N  
ATOM   3258  CD2 HIS B  98      54.117 110.640   8.967  1.00 25.29           C  
ANISOU 3258  CD2 HIS B  98     3951   2486   3172   -484    442   -271       C  
ATOM   3259  CE1 HIS B  98      55.809 110.677   7.552  1.00 25.13           C  
ANISOU 3259  CE1 HIS B  98     3836   2426   3284   -432    428   -184       C  
ATOM   3260  NE2 HIS B  98      55.488 110.683   8.864  1.00 26.00           N  
ANISOU 3260  NE2 HIS B  98     3983   2590   3307   -519    391   -218       N  
ATOM   3261  N   GLU B  99      53.327 113.109   5.387  1.00 23.53           N  
ANISOU 3261  N   GLU B  99     3733   2045   3163   -283    662   -304       N  
ATOM   3262  CA  GLU B  99      53.936 113.546   4.108  1.00 26.66           C  
ANISOU 3262  CA  GLU B  99     4097   2397   3634   -236    690   -267       C  
ATOM   3263  C   GLU B  99      54.407 112.359   3.249  1.00 25.59           C  
ANISOU 3263  C   GLU B  99     3926   2284   3513   -185    662   -198       C  
ATOM   3264  O   GLU B  99      54.538 112.519   2.016  1.00 24.76           O  
ANISOU 3264  O   GLU B  99     3810   2145   3452   -137    698   -168       O  
ATOM   3265  CB  GLU B  99      55.048 114.557   4.365  1.00 30.03           C  
ANISOU 3265  CB  GLU B  99     4509   2801   4100   -296    691   -290       C  
ATOM   3266  CG  GLU B  99      56.343 113.971   4.878  1.00 36.37           C  
ANISOU 3266  CG  GLU B  99     5269   3650   4897   -349    615   -255       C  
ATOM   3267  CD  GLU B  99      57.444 115.030   4.988  1.00 45.31           C  
ANISOU 3267  CD  GLU B  99     6381   4757   6075   -409    615   -270       C  
ATOM   3268  OE1 GLU B  99      57.315 116.108   4.353  1.00 48.29           O  
ANISOU 3268  OE1 GLU B  99     6771   5072   6505   -387    682   -299       O  
ATOM   3269  OE2 GLU B  99      58.441 114.781   5.702  1.00 57.65           O  
ANISOU 3269  OE2 GLU B  99     7912   6364   7628   -481    545   -246       O  
ATOM   3270  N   ARG B 100      54.619 111.184   3.851  1.00 25.37           N  
ANISOU 3270  N   ARG B 100     3882   2307   3449   -198    607   -172       N  
ATOM   3271  CA  ARG B 100      55.133 110.022   3.071  1.00 25.84           C  
ANISOU 3271  CA  ARG B 100     3906   2373   3539   -155    600   -111       C  
ATOM   3272  C   ARG B 100      54.025 109.005   2.764  1.00 24.65           C  
ANISOU 3272  C   ARG B 100     3783   2236   3348   -107    615   -102       C  
ATOM   3273  O   ARG B 100      54.358 107.916   2.266  1.00 24.10           O  
ANISOU 3273  O   ARG B 100     3692   2164   3298    -78    624    -62       O  
ATOM   3274  CB  ARG B 100      56.263 109.333   3.842  1.00 27.87           C  
ANISOU 3274  CB  ARG B 100     4109   2666   3812   -197    538    -65       C  
ATOM   3275  CG  ARG B 100      57.403 110.258   4.239  1.00 32.07           C  
ANISOU 3275  CG  ARG B 100     4608   3190   4386   -255    515    -63       C  
ATOM   3276  CD  ARG B 100      58.591 109.492   4.784  1.00 35.66           C  
ANISOU 3276  CD  ARG B 100     4988   3675   4884   -291    453     12       C  
ATOM   3277  NE  ARG B 100      58.648 108.134   4.266  1.00 38.62           N  
ANISOU 3277  NE  ARG B 100     5323   4045   5303   -236    464     78       N  
ATOM   3278  CZ  ARG B 100      59.428 107.741   3.266  1.00 48.66           C  
ANISOU 3278  CZ  ARG B 100     6556   5265   6666   -187    518    122       C  
ATOM   3279  NH1 ARG B 100      59.325 108.316   2.080  1.00 44.40           N  
ANISOU 3279  NH1 ARG B 100     6050   4673   6146   -148    589     88       N  
ATOM   3280  NH2 ARG B 100      60.307 106.773   3.456  1.00 49.03           N  
ANISOU 3280  NH2 ARG B 100     6529   5310   6790   -179    506    206       N  
ATOM   3281  N   ALA B 101      52.764 109.365   3.008  1.00 23.93           N  
ANISOU 3281  N   ALA B 101     3733   2150   3207   -102    626   -139       N  
ATOM   3282  CA  ALA B 101      51.629 108.451   2.818  1.00 23.04           C  
ANISOU 3282  CA  ALA B 101     3644   2058   3051    -67    629   -131       C  
ATOM   3283  C   ALA B 101      51.496 107.981   1.363  1.00 23.30           C  
ANISOU 3283  C   ALA B 101     3682   2073   3099    -25    665    -97       C  
ATOM   3284  O   ALA B 101      51.445 106.763   1.097  1.00 20.85           O  
ANISOU 3284  O   ALA B 101     3369   1778   2772    -10    663    -75       O  
ATOM   3285  CB  ALA B 101      50.333 109.070   3.289  1.00 22.17           C  
ANISOU 3285  CB  ALA B 101     3570   1944   2910    -68    647   -168       C  
ATOM   3286  N   LEU B 102      51.358 108.909   0.418  1.00 21.92           N  
ANISOU 3286  N   LEU B 102     3515   1864   2947    -12    702    -92       N  
ATOM   3287  CA  LEU B 102      51.039 108.490  -0.966  1.00 23.31           C  
ANISOU 3287  CA  LEU B 102     3709   2034   3110      8    732    -60       C  
ATOM   3288  C   LEU B 102      52.202 107.704  -1.595  1.00 22.60           C  
ANISOU 3288  C   LEU B 102     3606   1932   3048      6    755    -42       C  
ATOM   3289  O   LEU B 102      52.010 106.619  -2.155  1.00 20.54           O  
ANISOU 3289  O   LEU B 102     3363   1678   2760     10    774    -31       O  
ATOM   3290  CB  LEU B 102      50.669 109.715  -1.804  1.00 24.02           C  
ANISOU 3290  CB  LEU B 102     3805   2098   3222     13    760    -44       C  
ATOM   3291  CG  LEU B 102      49.406 110.473  -1.392  1.00 24.36           C  
ANISOU 3291  CG  LEU B 102     3852   2137   3264     21    760    -45       C  
ATOM   3292  CD1 LEU B 102      48.992 111.475  -2.457  1.00 23.75           C  
ANISOU 3292  CD1 LEU B 102     3768   2034   3219     30    788      0       C  
ATOM   3293  CD2 LEU B 102      48.246 109.543  -1.070  1.00 23.74           C  
ANISOU 3293  CD2 LEU B 102     3791   2096   3132     29    737    -40       C  
ATOM   3294  N   GLU B 103      53.419 108.219  -1.439  1.00 22.70           N  
ANISOU 3294  N   GLU B 103     3584   1918   3120     -2    759    -40       N  
ATOM   3295  CA  GLU B 103      54.604 107.582  -1.997  1.00 26.25           C  
ANISOU 3295  CA  GLU B 103     4010   2341   3622      0    793    -16       C  
ATOM   3296  C   GLU B 103      54.813 106.177  -1.395  1.00 24.75           C  
ANISOU 3296  C   GLU B 103     3797   2166   3439      2    781      0       C  
ATOM   3297  O   GLU B 103      55.039 105.188  -2.140  1.00 23.17           O  
ANISOU 3297  O   GLU B 103     3604   1944   3255     10    835     13       O  
ATOM   3298  CB  GLU B 103      55.836 108.451  -1.755  1.00 28.39           C  
ANISOU 3298  CB  GLU B 103     4236   2584   3965    -14    789     -9       C  
ATOM   3299  CG  GLU B 103      57.109 107.704  -2.057  1.00 33.00           C  
ANISOU 3299  CG  GLU B 103     4776   3136   4625    -10    822     27       C  
ATOM   3300  CD  GLU B 103      58.283 108.564  -2.415  1.00 40.95           C  
ANISOU 3300  CD  GLU B 103     5747   4102   5709    -18    844     43       C  
ATOM   3301  OE1 GLU B 103      58.574 109.506  -1.636  1.00 48.70           O  
ANISOU 3301  OE1 GLU B 103     6705   5094   6704    -42    796     33       O  
ATOM   3302  OE2 GLU B 103      58.856 108.311  -3.488  1.00 47.90           O  
ANISOU 3302  OE2 GLU B 103     6629   4938   6630     -5    915     60       O  
ATOM   3303  N   ASP B 104      54.829 106.087  -0.063  1.00 23.03           N  
ANISOU 3303  N   ASP B 104     3550   1982   3217    -12    718      0       N  
ATOM   3304  CA  ASP B 104      55.139 104.820   0.608  1.00 24.82           C  
ANISOU 3304  CA  ASP B 104     3739   2224   3465    -11    699     32       C  
ATOM   3305  C   ASP B 104      54.049 103.785   0.315  1.00 24.53           C  
ANISOU 3305  C   ASP B 104     3744   2202   3373      7    720     21       C  
ATOM   3306  O   ASP B 104      54.357 102.606   0.092  1.00 24.75           O  
ANISOU 3306  O   ASP B 104     3753   2211   3438     19    756     47       O  
ATOM   3307  CB  ASP B 104      55.353 104.998   2.108  1.00 25.72           C  
ANISOU 3307  CB  ASP B 104     3818   2384   3569    -47    619     43       C  
ATOM   3308  CG  ASP B 104      56.685 105.619   2.472  1.00 27.62           C  
ANISOU 3308  CG  ASP B 104     4001   2615   3876    -81    591     74       C  
ATOM   3309  OD1 ASP B 104      57.457 105.935   1.549  1.00 28.26           O  
ANISOU 3309  OD1 ASP B 104     4065   2648   4024    -65    640     88       O  
ATOM   3310  OD2 ASP B 104      56.945 105.778   3.675  1.00 30.68           O  
ANISOU 3310  OD2 ASP B 104     4362   3047   4246   -130    520     87       O  
ATOM   3311  N   LEU B 105      52.773 104.201   0.347  1.00 24.70           N  
ANISOU 3311  N   LEU B 105     3816   2251   3318      8    703    -13       N  
ATOM   3312  CA  LEU B 105      51.688 103.243   0.136  1.00 23.39           C  
ANISOU 3312  CA  LEU B 105     3685   2103   3098     20    713    -20       C  
ATOM   3313  C   LEU B 105      51.679 102.812  -1.330  1.00 22.32           C  
ANISOU 3313  C   LEU B 105     3585   1937   2958     20    783    -20       C  
ATOM   3314  O   LEU B 105      51.562 101.611  -1.619  1.00 19.49           O  
ANISOU 3314  O   LEU B 105     3238   1570   2597     21    819    -17       O  
ATOM   3315  CB  LEU B 105      50.332 103.802   0.563  1.00 24.03           C  
ANISOU 3315  CB  LEU B 105     3800   2217   3113     20    678    -45       C  
ATOM   3316  CG  LEU B 105      49.958 103.599   2.040  1.00 29.38           C  
ANISOU 3316  CG  LEU B 105     4465   2932   3766     11    625    -54       C  
ATOM   3317  CD1 LEU B 105      51.113 103.901   2.978  1.00 32.56           C  
ANISOU 3317  CD1 LEU B 105     4824   3341   4206    -15    591    -43       C  
ATOM   3318  CD2 LEU B 105      48.736 104.420   2.432  1.00 28.76           C  
ANISOU 3318  CD2 LEU B 105     4417   2865   3643     10    614    -83       C  
ATOM   3319  N   TYR B 106      51.788 103.774  -2.247  1.00 21.20           N  
ANISOU 3319  N   TYR B 106     3464   1777   2812     13    807    -24       N  
ATOM   3320  CA  TYR B 106      51.845 103.437  -3.686  1.00 23.04           C  
ANISOU 3320  CA  TYR B 106     3740   1986   3025     -5    876    -24       C  
ATOM   3321  C   TYR B 106      53.023 102.514  -4.016  1.00 22.27           C  
ANISOU 3321  C   TYR B 106     3623   1838   2998     -5    948    -18       C  
ATOM   3322  O   TYR B 106      52.842 101.502  -4.722  1.00 23.70           O  
ANISOU 3322  O   TYR B 106     3843   2002   3157    -24   1012    -30       O  
ATOM   3323  CB  TYR B 106      51.958 104.682  -4.565  1.00 22.86           C  
ANISOU 3323  CB  TYR B 106     3733   1953   2997    -17    888    -17       C  
ATOM   3324  CG  TYR B 106      52.052 104.352  -6.035  1.00 23.46           C  
ANISOU 3324  CG  TYR B 106     3863   2013   3037    -53    958    -16       C  
ATOM   3325  CD1 TYR B 106      50.908 104.154  -6.788  1.00 23.12           C  
ANISOU 3325  CD1 TYR B 106     3875   2008   2902    -89    952    -11       C  
ATOM   3326  CD2 TYR B 106      53.277 104.319  -6.695  1.00 25.14           C  
ANISOU 3326  CD2 TYR B 106     4071   2174   3306    -60   1031    -17       C  
ATOM   3327  CE1 TYR B 106      50.978 103.861  -8.147  1.00 25.60           C  
ANISOU 3327  CE1 TYR B 106     4248   2316   3160   -144   1014    -13       C  
ATOM   3328  CE2 TYR B 106      53.366 104.002  -8.042  1.00 25.94           C  
ANISOU 3328  CE2 TYR B 106     4234   2259   3363   -107   1108    -25       C  
ATOM   3329  CZ  TYR B 106      52.207 103.796  -8.774  1.00 27.50           C  
ANISOU 3329  CZ  TYR B 106     4496   2503   3450   -155   1097    -25       C  
ATOM   3330  OH  TYR B 106      52.257 103.559 -10.122  1.00 29.46           O  
ANISOU 3330  OH  TYR B 106     4814   2745   3632   -223   1168    -33       O  
ATOM   3331  N   ASN B 107      54.212 102.818  -3.481  1.00 24.57           N  
ANISOU 3331  N   ASN B 107     3852   2101   3379      9    944      3       N  
ATOM   3332  CA  ASN B 107      55.443 102.020  -3.802  1.00 26.15           C  
ANISOU 3332  CA  ASN B 107     4015   2239   3679     14   1024     26       C  
ATOM   3333  C   ASN B 107      55.328 100.586  -3.276  1.00 23.79           C  
ANISOU 3333  C   ASN B 107     3694   1933   3410     24   1042     40       C  
ATOM   3334  O   ASN B 107      55.645  99.652  -4.005  1.00 25.13           O  
ANISOU 3334  O   ASN B 107     3879   2048   3619     18   1142     36       O  
ATOM   3335  CB  ASN B 107      56.729 102.683  -3.304  1.00 28.74           C  
ANISOU 3335  CB  ASN B 107     4268   2543   4108     24   1004     64       C  
ATOM   3336  CG  ASN B 107      57.120 103.887  -4.152  1.00 31.10           C  
ANISOU 3336  CG  ASN B 107     4587   2821   4406     15   1028     52       C  
ATOM   3337  OD1 ASN B 107      56.551 104.110  -5.223  1.00 27.66           O  
ANISOU 3337  OD1 ASN B 107     4221   2385   3903      0   1070     24       O  
ATOM   3338  ND2 ASN B 107      58.030 104.702  -3.643  1.00 28.30           N  
ANISOU 3338  ND2 ASN B 107     4174   2457   4119     17    993     77       N  
ATOM   3339  N   TYR B 108      54.811 100.417  -2.055  1.00 21.96           N  
ANISOU 3339  N   TYR B 108     3433   1752   3156     35    955     54       N  
ATOM   3340  CA  TYR B 108      54.583  99.120  -1.457  1.00 21.63           C  
ANISOU 3340  CA  TYR B 108     3367   1712   3136     45    960     74       C  
ATOM   3341  C   TYR B 108      53.586  98.354  -2.321  1.00 21.38           C  
ANISOU 3341  C   TYR B 108     3414   1674   3032     31   1021     29       C  
ATOM   3342  O   TYR B 108      53.756  97.162  -2.585  1.00 23.98           O  
ANISOU 3342  O   TYR B 108     3741   1959   3409     31   1100     33       O  
ATOM   3343  CB  TYR B 108      54.068  99.254  -0.018  1.00 23.24           C  
ANISOU 3343  CB  TYR B 108     3542   1984   3304     48    850     91       C  
ATOM   3344  CG  TYR B 108      54.319  98.044   0.846  1.00 22.72           C  
ANISOU 3344  CG  TYR B 108     3414   1918   3299     60    841    144       C  
ATOM   3345  CD1 TYR B 108      55.593  97.511   0.990  1.00 24.12           C  
ANISOU 3345  CD1 TYR B 108     3505   2047   3610     69    876    215       C  
ATOM   3346  CD2 TYR B 108      53.286  97.447   1.531  1.00 22.91           C  
ANISOU 3346  CD2 TYR B 108     3456   1987   3259     62    799    136       C  
ATOM   3347  CE1 TYR B 108      55.826  96.403   1.781  1.00 25.80           C  
ANISOU 3347  CE1 TYR B 108     3648   2258   3894     79    867    284       C  
ATOM   3348  CE2 TYR B 108      53.498  96.341   2.322  1.00 24.21           C  
ANISOU 3348  CE2 TYR B 108     3561   2154   3483     72    790    193       C  
ATOM   3349  CZ  TYR B 108      54.774  95.827   2.473  1.00 25.72           C  
ANISOU 3349  CZ  TYR B 108     3661   2299   3810     80    820    272       C  
ATOM   3350  OH  TYR B 108      54.976  94.743   3.268  1.00 24.08           O  
ANISOU 3350  OH  TYR B 108     3382   2092   3673     90    809    347       O  
ATOM   3351  N   GLY B 109      52.559  99.056  -2.777  1.00 20.27           N  
ANISOU 3351  N   GLY B 109     3340   1577   2784     13    988     -8       N  
ATOM   3352  CA  GLY B 109      51.511  98.469  -3.551  1.00 20.38           C  
ANISOU 3352  CA  GLY B 109     3427   1603   2712    -15   1021    -42       C  
ATOM   3353  C   GLY B 109      52.023  97.975  -4.884  1.00 22.35           C  
ANISOU 3353  C   GLY B 109     3723   1794   2971    -52   1140    -65       C  
ATOM   3354  O   GLY B 109      51.707  96.889  -5.302  1.00 21.87           O  
ANISOU 3354  O   GLY B 109     3702   1712   2894    -78   1207    -89       O  
ATOM   3355  N   LYS B 110      52.872  98.780  -5.522  1.00 24.83           N  
ANISOU 3355  N   LYS B 110     4037   2079   3319    -58   1174    -61       N  
ATOM   3356  CA  LYS B 110      53.490  98.419  -6.791  1.00 28.01           C  
ANISOU 3356  CA  LYS B 110     4487   2418   3734    -99   1301    -86       C  
ATOM   3357  C   LYS B 110      54.426  97.225  -6.640  1.00 28.33           C  
ANISOU 3357  C   LYS B 110     4487   2376   3901    -82   1408    -78       C  
ATOM   3358  O   LYS B 110      54.343  96.283  -7.431  1.00 32.14           O  
ANISOU 3358  O   LYS B 110     5028   2811   4370   -125   1522   -117       O  
ATOM   3359  CB  LYS B 110      54.243  99.629  -7.345  1.00 32.14           C  
ANISOU 3359  CB  LYS B 110     5006   2928   4278   -101   1306    -75       C  
ATOM   3360  CG  LYS B 110      53.318 100.686  -7.902  1.00 35.68           C  
ANISOU 3360  CG  LYS B 110     5506   3441   4608   -132   1240    -79       C  
ATOM   3361  CD  LYS B 110      52.457 100.212  -9.052  1.00 40.85           C  
ANISOU 3361  CD  LYS B 110     6258   4118   5141   -209   1283   -109       C  
ATOM   3362  CE  LYS B 110      53.273  99.999 -10.311  1.00 42.22           C  
ANISOU 3362  CE  LYS B 110     6489   4234   5317   -264   1413   -135       C  
ATOM   3363  NZ  LYS B 110      52.415  99.995 -11.518  1.00 44.53           N  
ANISOU 3363  NZ  LYS B 110     6883   4572   5461   -361   1428   -153       N  
ATOM   3364  N   GLU B 111      55.321  97.275  -5.653  1.00 29.14           N  
ANISOU 3364  N   GLU B 111     4488   2457   4127    -29   1377    -23       N  
ATOM   3365  CA  GLU B 111      56.239  96.173  -5.331  1.00 33.77           C  
ANISOU 3365  CA  GLU B 111     5004   2963   4864     -3   1465     15       C  
ATOM   3366  C   GLU B 111      55.506  94.830  -5.201  1.00 33.30           C  
ANISOU 3366  C   GLU B 111     4970   2892   4790    -13   1511     -5       C  
ATOM   3367  O   GLU B 111      56.015  93.803  -5.640  1.00 31.37           O  
ANISOU 3367  O   GLU B 111     4721   2557   4638    -20   1650     -9       O  
ATOM   3368  CB  GLU B 111      56.993  96.459  -4.032  1.00 38.26           C  
ANISOU 3368  CB  GLU B 111     5452   3547   5538     43   1373     97       C  
ATOM   3369  CG  GLU B 111      58.155  97.405  -4.227  1.00 49.48           C  
ANISOU 3369  CG  GLU B 111     6824   4937   7037     51   1378    130       C  
ATOM   3370  CD  GLU B 111      58.641  98.129  -2.980  1.00 57.68           C  
ANISOU 3370  CD  GLU B 111     7770   6026   8117     71   1246    196       C  
ATOM   3371  OE1 GLU B 111      59.268  99.206  -3.135  1.00 65.25           O  
ANISOU 3371  OE1 GLU B 111     8713   6986   9092     67   1220    203       O  
ATOM   3372  OE2 GLU B 111      58.403  97.625  -1.863  1.00 62.77           O  
ANISOU 3372  OE2 GLU B 111     8362   6712   8773     82   1170    239       O  
ATOM   3373  N   ASN B 112      54.318  94.838  -4.586  1.00 26.09           N  
ANISOU 3373  N   ASN B 112     4080   2063   3770    -13   1403    -17       N  
ATOM   3374  CA  ASN B 112      53.618  93.645  -4.173  1.00 25.65           C  
ANISOU 3374  CA  ASN B 112     4028   2007   3708    -11   1418    -23       C  
ATOM   3375  C   ASN B 112      52.368  93.377  -5.023  1.00 25.49           C  
ANISOU 3375  C   ASN B 112     4123   2019   3540    -71   1438    -96       C  
ATOM   3376  O   ASN B 112      51.505  92.590  -4.608  1.00 25.65           O  
ANISOU 3376  O   ASN B 112     4156   2065   3525    -73   1418   -106       O  
ATOM   3377  CB  ASN B 112      53.304  93.809  -2.691  1.00 24.80           C  
ANISOU 3377  CB  ASN B 112     3848   1969   3604     31   1279     30       C  
ATOM   3378  CG  ASN B 112      54.565  93.746  -1.858  1.00 26.18           C  
ANISOU 3378  CG  ASN B 112     3905   2111   3929     70   1268    115       C  
ATOM   3379  OD1 ASN B 112      55.273  92.738  -1.875  1.00 26.79           O  
ANISOU 3379  OD1 ASN B 112     3927   2111   4141     85   1364    157       O  
ATOM   3380  ND2 ASN B 112      54.865  94.799  -1.129  1.00 26.15           N  
ANISOU 3380  ND2 ASN B 112     3858   2162   3914     80   1156    149       N  
ATOM   3381  N   ASN B 113      52.223  94.073  -6.157  1.00 23.33           N  
ANISOU 3381  N   ASN B 113     3930   1757   3178   -124   1464   -139       N  
ATOM   3382  CA  ASN B 113      51.052  93.918  -7.057  1.00 25.51           C  
ANISOU 3382  CA  ASN B 113     4314   2077   3302   -200   1469   -193       C  
ATOM   3383  C   ASN B 113      49.752  94.011  -6.249  1.00 24.09           C  
ANISOU 3383  C   ASN B 113     4126   1984   3040   -183   1336   -179       C  
ATOM   3384  O   ASN B 113      48.852  93.199  -6.435  1.00 24.69           O  
ANISOU 3384  O   ASN B 113     4251   2078   3051   -224   1350   -207       O  
ATOM   3385  CB  ASN B 113      51.147  92.622  -7.890  1.00 29.98           C  
ANISOU 3385  CB  ASN B 113     4946   2567   3875   -263   1628   -249       C  
ATOM   3386  CG  ASN B 113      50.115  92.502  -9.009  1.00 34.88           C  
ANISOU 3386  CG  ASN B 113     5690   3234   4329   -371   1644   -307       C  
ATOM   3387  OD1 ASN B 113      49.634  93.500  -9.549  1.00 39.57           O  
ANISOU 3387  OD1 ASN B 113     6324   3898   4812   -410   1567   -299       O  
ATOM   3388  ND2 ASN B 113      49.753  91.273  -9.373  1.00 39.08           N  
ANISOU 3388  ND2 ASN B 113     6280   3727   4840   -430   1744   -359       N  
ATOM   3389  N   SER B 114      49.647  95.013  -5.352  1.00 25.73           N  
ANISOU 3389  N   SER B 114     4275   2244   3254   -130   1216   -137       N  
ATOM   3390  CA  SER B 114      48.521  95.070  -4.373  1.00 25.04           C  
ANISOU 3390  CA  SER B 114     4170   2227   3117   -104   1104   -121       C  
ATOM   3391  C   SER B 114      47.277  95.706  -5.000  1.00 24.42           C  
ANISOU 3391  C   SER B 114     4151   2213   2912   -149   1045   -129       C  
ATOM   3392  O   SER B 114      47.377  96.723  -5.657  1.00 23.16           O  
ANISOU 3392  O   SER B 114     4010   2068   2720   -169   1030   -121       O  
ATOM   3393  CB  SER B 114      48.886  95.805  -3.124  1.00 23.96           C  
ANISOU 3393  CB  SER B 114     3954   2111   3035    -43   1018    -81       C  
ATOM   3394  OG  SER B 114      50.041  95.269  -2.546  1.00 26.46           O  
ANISOU 3394  OG  SER B 114     4204   2378   3470    -10   1057    -52       O  
ATOM   3395  N   ASP B 115      46.109  95.114  -4.714  1.00 23.48           N  
ANISOU 3395  N   ASP B 115     4050   2134   2735   -162   1006   -132       N  
ATOM   3396  CA  ASP B 115      44.803  95.702  -5.060  1.00 23.01           C  
ANISOU 3396  CA  ASP B 115     4023   2142   2577   -196    930   -115       C  
ATOM   3397  C   ASP B 115      44.425  96.727  -3.985  1.00 22.19           C  
ANISOU 3397  C   ASP B 115     3860   2071   2499   -133    836    -80       C  
ATOM   3398  O   ASP B 115      43.710  97.714  -4.250  1.00 20.56           O  
ANISOU 3398  O   ASP B 115     3655   1902   2253   -143    781    -50       O  
ATOM   3399  CB  ASP B 115      43.742  94.621  -5.262  1.00 24.39           C  
ANISOU 3399  CB  ASP B 115     4240   2340   2686   -243    934   -131       C  
ATOM   3400  CG  ASP B 115      44.145  93.596  -6.309  1.00 29.34           C  
ANISOU 3400  CG  ASP B 115     4936   2925   3286   -319   1047   -180       C  
ATOM   3401  OD1 ASP B 115      44.384  94.049  -7.465  1.00 28.50           O  
ANISOU 3401  OD1 ASP B 115     4883   2821   3121   -387   1080   -189       O  
ATOM   3402  OD2 ASP B 115      44.252  92.346  -5.953  1.00 27.63           O  
ANISOU 3402  OD2 ASP B 115     4719   2667   3111   -313   1111   -210       O  
ATOM   3403  N   LEU B 116      44.928  96.509  -2.769  1.00 20.78           N  
ANISOU 3403  N   LEU B 116     3628   1876   2391    -75    824    -79       N  
ATOM   3404  CA  LEU B 116      44.522  97.296  -1.627  1.00 21.62           C  
ANISOU 3404  CA  LEU B 116     3691   2010   2510    -30    749    -60       C  
ATOM   3405  C   LEU B 116      45.727  97.483  -0.712  1.00 20.35           C  
ANISOU 3405  C   LEU B 116     3478   1825   2427      5    749    -56       C  
ATOM   3406  O   LEU B 116      46.400  96.526  -0.419  1.00 19.61           O  
ANISOU 3406  O   LEU B 116     3361   1706   2382     14    783    -53       O  
ATOM   3407  CB  LEU B 116      43.402  96.551  -0.894  1.00 21.59           C  
ANISOU 3407  CB  LEU B 116     3686   2038   2479    -21    715    -57       C  
ATOM   3408  CG  LEU B 116      42.856  97.237   0.360  1.00 22.43           C  
ANISOU 3408  CG  LEU B 116     3758   2169   2593     16    655    -46       C  
ATOM   3409  CD1 LEU B 116      42.239  98.589   0.023  1.00 22.96           C  
ANISOU 3409  CD1 LEU B 116     3829   2248   2645     12    627    -28       C  
ATOM   3410  CD2 LEU B 116      41.862  96.339   1.083  1.00 23.06           C  
ANISOU 3410  CD2 LEU B 116     3837   2272   2650     25    634    -44       C  
ATOM   3411  N   ILE B 117      45.998  98.724  -0.311  1.00 19.27           N  
ANISOU 3411  N   ILE B 117     3319   1695   2306     20    712    -49       N  
ATOM   3412  CA  ILE B 117      47.090  99.022   0.627  1.00 19.52           C  
ANISOU 3412  CA  ILE B 117     3302   1715   2399     38    696    -41       C  
ATOM   3413  C   ILE B 117      46.493  99.816   1.795  1.00 19.62           C  
ANISOU 3413  C   ILE B 117     3303   1760   2389     46    637    -47       C  
ATOM   3414  O   ILE B 117      45.814 100.841   1.593  1.00 18.62           O  
ANISOU 3414  O   ILE B 117     3195   1638   2240     44    626    -55       O  
ATOM   3415  CB  ILE B 117      48.259  99.796  -0.032  1.00 20.46           C  
ANISOU 3415  CB  ILE B 117     3409   1799   2564     32    726    -38       C  
ATOM   3416  CG1 ILE B 117      48.638  99.232  -1.400  1.00 20.66           C  
ANISOU 3416  CG1 ILE B 117     3466   1788   2594     12    802    -43       C  
ATOM   3417  CG2 ILE B 117      49.461  99.845   0.902  1.00 20.97           C  
ANISOU 3417  CG2 ILE B 117     3415   1854   2697     40    707    -17       C  
ATOM   3418  CD1 ILE B 117      47.942  99.884  -2.564  1.00 21.54           C  
ANISOU 3418  CD1 ILE B 117     3630   1911   2642    -16    811    -51       C  
ATOM   3419  N   ILE B 118      46.846  99.392   3.009  1.00 19.36           N  
ANISOU 3419  N   ILE B 118     3238   1746   2372     48    605    -38       N  
ATOM   3420  CA  ILE B 118      46.298  99.920   4.230  1.00 19.81           C  
ANISOU 3420  CA  ILE B 118     3295   1834   2396     41    561    -51       C  
ATOM   3421  C   ILE B 118      47.459 100.428   5.094  1.00 20.33           C  
ANISOU 3421  C   ILE B 118     3326   1907   2489     16    530    -43       C  
ATOM   3422  O   ILE B 118      48.327  99.657   5.491  1.00 20.27           O  
ANISOU 3422  O   ILE B 118     3276   1906   2517      9    515     -4       O  
ATOM   3423  CB  ILE B 118      45.499  98.833   4.981  1.00 20.13           C  
ANISOU 3423  CB  ILE B 118     3337   1904   2406     48    543    -43       C  
ATOM   3424  CG1 ILE B 118      44.416  98.195   4.108  1.00 20.78           C  
ANISOU 3424  CG1 ILE B 118     3450   1982   2463     62    569    -47       C  
ATOM   3425  CG2 ILE B 118      44.934  99.421   6.257  1.00 19.13           C  
ANISOU 3425  CG2 ILE B 118     3220   1807   2240     31    509    -64       C  
ATOM   3426  CD1 ILE B 118      43.898  96.892   4.643  1.00 25.12           C  
ANISOU 3426  CD1 ILE B 118     3994   2549   2999     70    563    -34       C  
ATOM   3427  N   GLY B 119      47.468 101.728   5.378  1.00 18.32           N  
ANISOU 3427  N   GLY B 119     3086   1649   2224     -3    523    -72       N  
ATOM   3428  CA  GLY B 119      48.492 102.310   6.214  1.00 19.03           C  
ANISOU 3428  CA  GLY B 119     3152   1752   2326    -45    491    -71       C  
ATOM   3429  C   GLY B 119      48.005 102.520   7.629  1.00 19.15           C  
ANISOU 3429  C   GLY B 119     3186   1808   2282    -88    457    -96       C  
ATOM   3430  O   GLY B 119      46.827 102.828   7.834  1.00 18.95           O  
ANISOU 3430  O   GLY B 119     3200   1778   2220    -80    479   -133       O  
ATOM   3431  N   LYS B 120      48.928 102.397   8.580  1.00 19.02           N  
ANISOU 3431  N   LYS B 120     3140   1827   2258   -141    406    -70       N  
ATOM   3432  CA  LYS B 120      48.646 102.527   9.979  1.00 20.63           C  
ANISOU 3432  CA  LYS B 120     3367   2080   2390   -205    369    -90       C  
ATOM   3433  C   LYS B 120      48.015 103.905  10.234  1.00 23.20           C  
ANISOU 3433  C   LYS B 120     3752   2380   2682   -235    412   -171       C  
ATOM   3434  O   LYS B 120      48.479 104.907   9.681  1.00 19.59           O  
ANISOU 3434  O   LYS B 120     3296   1884   2261   -237    438   -194       O  
ATOM   3435  CB  LYS B 120      49.924 102.345  10.806  1.00 21.38           C  
ANISOU 3435  CB  LYS B 120     3415   2224   2485   -276    298    -36       C  
ATOM   3436  CG  LYS B 120      49.675 102.385  12.301  1.00 24.39           C  
ANISOU 3436  CG  LYS B 120     3825   2669   2770   -364    252    -49       C  
ATOM   3437  CD  LYS B 120      50.812 101.964  13.179  1.00 25.54           C  
ANISOU 3437  CD  LYS B 120     3915   2882   2906   -444    163     30       C  
ATOM   3438  CE  LYS B 120      52.052 102.768  12.940  1.00 27.42           C  
ANISOU 3438  CE  LYS B 120     4118   3111   3186   -487    140     47       C  
ATOM   3439  NZ  LYS B 120      53.104 102.452  13.941  1.00 29.46           N  
ANISOU 3439  NZ  LYS B 120     4320   3447   3426   -586     39    136       N  
ATOM   3440  N   TYR B 121      46.985 103.908  11.097  1.00 25.28           N  
ANISOU 3440  N   TYR B 121     4062   2660   2883   -258    427   -211       N  
ATOM   3441  CA  TYR B 121      46.215 105.076  11.532  1.00 26.62           C  
ANISOU 3441  CA  TYR B 121     4289   2795   3028   -289    490   -289       C  
ATOM   3442  C   TYR B 121      46.782 105.574  12.857  1.00 29.78           C  
ANISOU 3442  C   TYR B 121     4722   3236   3354   -405    465   -327       C  
ATOM   3443  O   TYR B 121      47.077 104.791  13.760  1.00 25.57           O  
ANISOU 3443  O   TYR B 121     4184   2772   2759   -459    402   -294       O  
ATOM   3444  CB  TYR B 121      44.727 104.746  11.743  1.00 27.90           C  
ANISOU 3444  CB  TYR B 121     4483   2944   3172   -252    534   -309       C  
ATOM   3445  CG  TYR B 121      44.038 104.161  10.538  1.00 28.58           C  
ANISOU 3445  CG  TYR B 121     4542   3004   3312   -157    548   -268       C  
ATOM   3446  CD1 TYR B 121      44.043 104.846   9.336  1.00 33.70           C  
ANISOU 3446  CD1 TYR B 121     5176   3602   4025   -113    582   -261       C  
ATOM   3447  CD2 TYR B 121      43.384 102.947  10.572  1.00 32.59           C  
ANISOU 3447  CD2 TYR B 121     5040   3540   3802   -122    527   -234       C  
ATOM   3448  CE1 TYR B 121      43.464 104.319   8.194  1.00 34.02           C  
ANISOU 3448  CE1 TYR B 121     5197   3629   4098    -49    587   -219       C  
ATOM   3449  CE2 TYR B 121      42.819 102.382   9.425  1.00 31.66           C  
ANISOU 3449  CE2 TYR B 121     4902   3403   3722    -54    537   -198       C  
ATOM   3450  CZ  TYR B 121      42.852 103.082   8.234  1.00 31.87           C  
ANISOU 3450  CZ  TYR B 121     4920   3388   3801    -23    564   -191       C  
ATOM   3451  OH  TYR B 121      42.264 102.632   7.099  1.00 30.51           O  
ANISOU 3451  OH  TYR B 121     4736   3203   3650     21    571   -156       O  
ATOM   3452  N   GLY B 122      46.840 106.898  12.966  1.00 26.89           N  
ANISOU 3452  N   GLY B 122     4395   2826   2995   -449    522   -395       N  
ATOM   3453  CA  GLY B 122      47.007 107.579  14.177  1.00 30.45           C  
ANISOU 3453  CA  GLY B 122     4904   3297   3368   -568    534   -461       C  
ATOM   3454  C   GLY B 122      45.725 108.306  14.542  1.00 31.30           C  
ANISOU 3454  C   GLY B 122     5077   3341   3472   -571    648   -545       C  
ATOM   3455  O   GLY B 122      44.748 108.279  13.813  1.00 30.38           O  
ANISOU 3455  O   GLY B 122     4948   3169   3424   -475    704   -536       O  
ATOM   3456  N   VAL B 123      45.727 108.941  15.708  1.00 33.87           N  
ANISOU 3456  N   VAL B 123     5474   3675   3718   -692    685   -624       N  
ATOM   3457  CA  VAL B 123      44.532 109.546  16.183  1.00 38.08           C  
ANISOU 3457  CA  VAL B 123     6073   4142   4254   -703    809   -705       C  
ATOM   3458  C   VAL B 123      44.936 110.775  16.986  1.00 41.39           C  
ANISOU 3458  C   VAL B 123     6567   4532   4627   -837    879   -807       C  
ATOM   3459  O   VAL B 123      45.929 110.747  17.693  1.00 40.46           O  
ANISOU 3459  O   VAL B 123     6470   4489   4414   -957    805   -814       O  
ATOM   3460  CB  VAL B 123      43.682 108.564  17.008  1.00 46.70           C  
ANISOU 3460  CB  VAL B 123     7192   5280   5269   -713    800   -698       C  
ATOM   3461  CG1 VAL B 123      44.119 108.517  18.468  1.00 49.77           C  
ANISOU 3461  CG1 VAL B 123     7652   5744   5512   -875    771   -745       C  
ATOM   3462  CG2 VAL B 123      42.202 108.898  16.897  1.00 48.70           C  
ANISOU 3462  CG2 VAL B 123     7469   5443   5589   -647    928   -737       C  
ATOM   3463  N   GLU B 124      44.175 111.853  16.805  1.00 41.49           N  
ANISOU 3463  N   GLU B 124     6611   4432   4720   -817   1024   -878       N  
ATOM   3464  CA  GLU B 124      44.386 113.083  17.525  1.00 49.99           C  
ANISOU 3464  CA  GLU B 124     7766   5455   5770   -941   1128   -992       C  
ATOM   3465  C   GLU B 124      43.161 113.287  18.420  1.00 54.63           C  
ANISOU 3465  C   GLU B 124     8434   5987   6336   -982   1266  -1075       C  
ATOM   3466  O   GLU B 124      42.015 113.133  17.948  1.00 45.96           O  
ANISOU 3466  O   GLU B 124     7304   4821   5335   -866   1337  -1046       O  
ATOM   3467  CB  GLU B 124      44.564 114.229  16.533  1.00 54.04           C  
ANISOU 3467  CB  GLU B 124     8244   5865   6422   -881   1204  -1002       C  
ATOM   3468  CG  GLU B 124      45.830 115.017  16.740  1.00 57.71           C  
ANISOU 3468  CG  GLU B 124     8731   6344   6850   -992   1179  -1047       C  
ATOM   3469  CD  GLU B 124      45.914 116.275  15.892  1.00 65.55           C  
ANISOU 3469  CD  GLU B 124     9700   7221   7984   -944   1280  -1071       C  
ATOM   3470  OE1 GLU B 124      45.054 117.154  16.054  1.00 65.88           O  
ANISOU 3470  OE1 GLU B 124     9779   7149   8101   -944   1444  -1141       O  
ATOM   3471  OE2 GLU B 124      46.835 116.370  15.063  1.00 71.48           O  
ANISOU 3471  OE2 GLU B 124    10389   7990   8778   -905   1202  -1013       O  
ATOM   3472  N   GLY B 125      43.405 113.550  19.710  1.00 55.83           N  
ANISOU 3472  N   GLY B 125     8686   6172   6353  -1152   1298  -1169       N  
ATOM   3473  CA  GLY B 125      42.331 113.786  20.692  1.00 62.23           C  
ANISOU 3473  CA  GLY B 125     9590   6928   7126  -1218   1447  -1265       C  
ATOM   3474  C   GLY B 125      41.468 112.561  20.984  1.00 62.85           C  
ANISOU 3474  C   GLY B 125     9656   7058   7164  -1160   1405  -1208       C  
ATOM   3475  O   GLY B 125      41.228 111.721  20.137  1.00 63.72           O  
ANISOU 3475  O   GLY B 125     9675   7194   7341  -1018   1319  -1101       O  
ATOM   3476  N   LYS B 126      40.973 112.475  22.225  1.00 76.57           N  
ANISOU 3476  N   LYS B 126    11495   8811   8787  -1280   1477  -1289       N  
ATOM   3477  CA  LYS B 126      40.035 111.421  22.645  1.00 76.10           C  
ANISOU 3477  CA  LYS B 126    11438   8788   8690  -1238   1467  -1252       C  
ATOM   3478  C   LYS B 126      38.725 111.572  21.851  1.00 76.65           C  
ANISOU 3478  C   LYS B 126    11449   8729   8942  -1070   1586  -1225       C  
ATOM   3479  O   LYS B 126      38.332 112.697  21.515  1.00 78.59           O  
ANISOU 3479  O   LYS B 126    11702   8844   9316  -1046   1738  -1280       O  
ATOM   3480  CB  LYS B 126      39.811 111.511  24.159  1.00 74.13           C  
ANISOU 3480  CB  LYS B 126    11322   8567   8277  -1422   1544  -1359       C  
ATOM   3481  N   GLY B 127      38.062 110.447  21.539  1.00 75.13           N  
ANISOU 3481  N   GLY B 127    11197   8577   8772   -959   1517  -1133       N  
ATOM   3482  CA  GLY B 127      36.781 110.450  20.806  1.00 70.04           C  
ANISOU 3482  CA  GLY B 127    10489   7829   8293   -809   1607  -1088       C  
ATOM   3483  C   GLY B 127      36.597 109.222  19.927  1.00 68.58           C  
ANISOU 3483  C   GLY B 127    10204   7712   8140   -676   1463   -956       C  
ATOM   3484  O   GLY B 127      37.133 108.152  20.196  1.00 78.33           O  
ANISOU 3484  O   GLY B 127    11433   9065   9263   -699   1324   -911       O  
ATOM   3485  N   SER B 129      39.230 106.169  19.259  1.00 75.46           N  
ANISOU 3485  N   SER B 129    10944   8924   8803   -652    964   -727       N  
ATOM   3486  CA  SER B 129      40.322 105.268  18.846  1.00 69.70           C  
ANISOU 3486  CA  SER B 129    10151   8286   8045   -636    811   -638       C  
ATOM   3487  C   SER B 129      40.112 104.783  17.405  1.00 69.25           C  
ANISOU 3487  C   SER B 129    10007   8200   8104   -490    777   -559       C  
ATOM   3488  O   SER B 129      39.056 104.991  16.797  1.00 77.81           O  
ANISOU 3488  O   SER B 129    11075   9212   9274   -406    850   -558       O  
ATOM   3489  CB  SER B 129      40.476 104.092  19.795  1.00 70.01           C  
ANISOU 3489  CB  SER B 129    10198   8429   7972   -694    724   -595       C  
ATOM   3490  N   VAL B 130      41.150 104.112  16.893  1.00 59.38           N  
ANISOU 3490  N   VAL B 130     8699   7008   6852   -471    667   -487       N  
ATOM   3491  CA  VAL B 130      41.246 103.548  15.553  1.00 49.17           C  
ANISOU 3491  CA  VAL B 130     7333   5702   5646   -360    626   -415       C  
ATOM   3492  C   VAL B 130      41.611 102.080  15.720  1.00 42.01           C  
ANISOU 3492  C   VAL B 130     6385   4870   4704   -348    532   -339       C  
ATOM   3493  O   VAL B 130      42.111 101.713  16.771  1.00 31.96           O  
ANISOU 3493  O   VAL B 130     5127   3664   3349   -431    482   -329       O  
ATOM   3494  CB  VAL B 130      42.332 104.281  14.748  1.00 49.82           C  
ANISOU 3494  CB  VAL B 130     7387   5764   5777   -359    607   -409       C  
ATOM   3495  CG1 VAL B 130      41.867 105.666  14.347  1.00 53.06           C  
ANISOU 3495  CG1 VAL B 130     7823   6087   6251   -348    707   -469       C  
ATOM   3496  CG2 VAL B 130      43.646 104.338  15.526  1.00 47.29           C  
ANISOU 3496  CG2 VAL B 130     7072   5509   5387   -463    537   -406       C  
ATOM   3497  N   PRO B 131      41.431 101.205  14.707  1.00 42.79           N  
ANISOU 3497  N   PRO B 131     6431   4962   4865   -255    507   -278       N  
ATOM   3498  CA  PRO B 131      41.808  99.799  14.851  1.00 37.19           C  
ANISOU 3498  CA  PRO B 131     5678   4310   4142   -242    435   -206       C  
ATOM   3499  C   PRO B 131      43.317  99.649  15.045  1.00 35.76           C  
ANISOU 3499  C   PRO B 131     5457   4175   3954   -294    362   -158       C  
ATOM   3500  O   PRO B 131      44.122 100.524  14.631  1.00 35.82           O  
ANISOU 3500  O   PRO B 131     5459   4161   3987   -313    363   -174       O  
ATOM   3501  CB  PRO B 131      41.336  99.174  13.558  1.00 36.26           C  
ANISOU 3501  CB  PRO B 131     5523   4154   4097   -145    449   -172       C  
ATOM   3502  CG  PRO B 131      41.408 100.324  12.601  1.00 42.15           C  
ANISOU 3502  CG  PRO B 131     6276   4844   4895   -122    491   -203       C  
ATOM   3503  CD  PRO B 131      40.872 101.492  13.384  1.00 40.65           C  
ANISOU 3503  CD  PRO B 131     6138   4628   4677   -170    549   -272       C  
ATOM   3504  N   LYS B 132      43.657  98.579  15.749  1.00 29.24           N  
ANISOU 3504  N   LYS B 132     4599   3410   3097   -320    300    -92       N  
ATOM   3505  CA  LYS B 132      44.973  98.308  16.172  1.00 32.86           C  
ANISOU 3505  CA  LYS B 132     5009   3923   3552   -379    222    -23       C  
ATOM   3506  C   LYS B 132      45.404  96.925  15.658  1.00 29.27           C  
ANISOU 3506  C   LYS B 132     4471   3472   3177   -315    189     75       C  
ATOM   3507  O   LYS B 132      46.525  96.800  15.235  1.00 29.10           O  
ANISOU 3507  O   LYS B 132     4389   3447   3220   -312    159    133       O  
ATOM   3508  CB  LYS B 132      45.052  98.421  17.694  1.00 40.28           C  
ANISOU 3508  CB  LYS B 132     5986   4940   4377   -500    178    -25       C  
ATOM   3509  CG  LYS B 132      45.149  99.849  18.228  1.00 44.69           C  
ANISOU 3509  CG  LYS B 132     6619   5495   4863   -596    207   -116       C  
ATOM   3510  CD  LYS B 132      45.956  99.936  19.502  1.00 50.74           C  
ANISOU 3510  CD  LYS B 132     7397   6356   5526   -744    128    -85       C  
ATOM   3511  CE  LYS B 132      46.199 101.356  19.959  1.00 58.85           C  
ANISOU 3511  CE  LYS B 132     8500   7375   6482   -854    162   -181       C  
ATOM   3512  NZ  LYS B 132      44.924 102.053  20.246  1.00 63.47           N  
ANISOU 3512  NZ  LYS B 132     9183   7904   7026   -857    278   -302       N  
ATOM   3513  N   ALA B 133      44.534  95.912  15.729  1.00 26.43           N  
ANISOU 3513  N   ALA B 133     4109   3113   2819   -267    204     93       N  
ATOM   3514  CA  ALA B 133      44.968  94.521  15.536  1.00 25.85           C  
ANISOU 3514  CA  ALA B 133     3957   3046   2817   -225    178    191       C  
ATOM   3515  C   ALA B 133      45.590  94.342  14.133  1.00 23.57           C  
ANISOU 3515  C   ALA B 133     3624   2691   2640   -156    215    208       C  
ATOM   3516  O   ALA B 133      46.627  93.762  14.011  1.00 24.29           O  
ANISOU 3516  O   ALA B 133     3641   2781   2806   -154    191    290       O  
ATOM   3517  CB  ALA B 133      43.818  93.579  15.760  1.00 25.64           C  
ANISOU 3517  CB  ALA B 133     3945   3020   2774   -185    202    191       C  
ATOM   3518  N   ILE B 134      44.937  94.875  13.101  1.00 21.38           N  
ANISOU 3518  N   ILE B 134     3391   2357   2372   -106    276    133       N  
ATOM   3519  CA  ILE B 134      45.444  94.838  11.708  1.00 21.58           C  
ANISOU 3519  CA  ILE B 134     3395   2322   2482    -55    320    134       C  
ATOM   3520  C   ILE B 134      46.895  95.332  11.626  1.00 21.49           C  
ANISOU 3520  C   ILE B 134     3336   2308   2518    -86    293    174       C  
ATOM   3521  O   ILE B 134      47.626  94.904  10.730  1.00 21.84           O  
ANISOU 3521  O   ILE B 134     3337   2308   2652    -50    324    208       O  
ATOM   3522  CB  ILE B 134      44.526  95.624  10.742  1.00 20.57           C  
ANISOU 3522  CB  ILE B 134     3327   2151   2337    -22    373     56       C  
ATOM   3523  CG1 ILE B 134      44.984  95.478   9.297  1.00 20.74           C  
ANISOU 3523  CG1 ILE B 134     3334   2118   2426     17    418     58       C  
ATOM   3524  CG2 ILE B 134      44.426  97.102  11.131  1.00 20.93           C  
ANISOU 3524  CG2 ILE B 134     3415   2203   2333    -62    369      0       C  
ATOM   3525  CD1 ILE B 134      43.994  96.013   8.274  1.00 21.77           C  
ANISOU 3525  CD1 ILE B 134     3516   2218   2538     43    461      5       C  
ATOM   3526  N   PHE B 135      47.309  96.242  12.512  1.00 21.48           N  
ANISOU 3526  N   PHE B 135     3347   2352   2462   -156    243    165       N  
ATOM   3527  CA  PHE B 135      48.651  96.828  12.431  1.00 21.71           C  
ANISOU 3527  CA  PHE B 135     3332   2382   2533   -194    212    200       C  
ATOM   3528  C   PHE B 135      49.627  96.151  13.401  1.00 22.91           C  
ANISOU 3528  C   PHE B 135     3406   2592   2706   -249    134    312       C  
ATOM   3529  O   PHE B 135      50.775  96.635  13.543  1.00 24.66           O  
ANISOU 3529  O   PHE B 135     3582   2828   2958   -298     91    358       O  
ATOM   3530  CB  PHE B 135      48.583  98.345  12.669  1.00 21.56           C  
ANISOU 3530  CB  PHE B 135     3374   2368   2447   -247    211    119       C  
ATOM   3531  CG  PHE B 135      47.620  99.041  11.740  1.00 19.99           C  
ANISOU 3531  CG  PHE B 135     3237   2112   2244   -194    285     32       C  
ATOM   3532  CD1 PHE B 135      47.790  98.953  10.374  1.00 19.51           C  
ANISOU 3532  CD1 PHE B 135     3161   1994   2257   -128    332     34       C  
ATOM   3533  CD2 PHE B 135      46.564  99.790  12.230  1.00 19.82           C  
ANISOU 3533  CD2 PHE B 135     3285   2092   2151   -215    311    -42       C  
ATOM   3534  CE1 PHE B 135      46.879  99.530   9.504  1.00 20.63           C  
ANISOU 3534  CE1 PHE B 135     3351   2093   2393    -87    388    -24       C  
ATOM   3535  CE2 PHE B 135      45.684 100.413  11.360  1.00 20.00           C  
ANISOU 3535  CE2 PHE B 135     3346   2061   2191   -164    376    -98       C  
ATOM   3536  CZ  PHE B 135      45.839 100.279  10.000  1.00 19.55           C  
ANISOU 3536  CZ  PHE B 135     3269   1960   2200   -103    405    -83       C  
ATOM   3537  N   GLU B 136      49.244  95.044  14.052  1.00 22.32           N  
ANISOU 3537  N   GLU B 136     3304   2551   2624   -246    111    371       N  
ATOM   3538  CA  GLU B 136      50.130  94.499  15.077  1.00 24.85           C  
ANISOU 3538  CA  GLU B 136     3544   2938   2957   -312     24    494       C  
ATOM   3539  C   GLU B 136      50.922  93.298  14.556  1.00 25.92           C  
ANISOU 3539  C   GLU B 136     3568   3031   3248   -253     42    612       C  
ATOM   3540  O   GLU B 136      51.458  92.515  15.355  1.00 27.72           O  
ANISOU 3540  O   GLU B 136     3712   3305   3514   -288    -19    739       O  
ATOM   3541  CB  GLU B 136      49.338  94.208  16.353  1.00 29.14           C  
ANISOU 3541  CB  GLU B 136     4127   3560   3385   -372    -22    496       C  
ATOM   3542  CG  GLU B 136      49.096  95.502  17.108  1.00 30.36           C  
ANISOU 3542  CG  GLU B 136     4370   3763   3402   -471    -49    408       C  
ATOM   3543  CD  GLU B 136      48.188  95.438  18.325  1.00 34.37           C  
ANISOU 3543  CD  GLU B 136     4944   4337   3776   -541    -71    377       C  
ATOM   3544  OE1 GLU B 136      48.154  96.464  19.059  1.00 37.30           O  
ANISOU 3544  OE1 GLU B 136     5387   4749   4035   -644    -88    311       O  
ATOM   3545  OE2 GLU B 136      47.517  94.387  18.519  1.00 34.83           O  
ANISOU 3545  OE2 GLU B 136     4987   4401   3843   -496    -62    413       O  
ATOM   3546  N   LYS B 137      50.995  93.163  13.231  1.00 25.01           N  
ANISOU 3546  N   LYS B 137     3452   2825   3226   -171    132    576       N  
ATOM   3547  CA  LYS B 137      51.869  92.182  12.611  1.00 25.91           C  
ANISOU 3547  CA  LYS B 137     3466   2875   3503   -120    178    673       C  
ATOM   3548  C   LYS B 137      52.904  92.852  11.704  1.00 24.06           C  
ANISOU 3548  C   LYS B 137     3205   2584   3351   -109    213    671       C  
ATOM   3549  O   LYS B 137      53.559  92.156  10.915  1.00 23.22           O  
ANISOU 3549  O   LYS B 137     3034   2400   3389    -58    286    724       O  
ATOM   3550  CB  LYS B 137      51.008  91.162  11.875  1.00 26.61           C  
ANISOU 3550  CB  LYS B 137     3579   2900   3630    -43    273    635       C  
ATOM   3551  CG  LYS B 137      50.315  90.228  12.836  1.00 30.33           C  
ANISOU 3551  CG  LYS B 137     4036   3418   4067    -50    237    684       C  
ATOM   3552  CD  LYS B 137      49.681  89.061  12.178  1.00 33.70           C  
ANISOU 3552  CD  LYS B 137     4466   3779   4560     17    330    670       C  
ATOM   3553  CE  LYS B 137      49.306  88.005  13.189  1.00 37.98           C  
ANISOU 3553  CE  LYS B 137     4960   4362   5106     11    294    754       C  
ATOM   3554  NZ  LYS B 137      48.110  87.271  12.731  1.00 40.67           N  
ANISOU 3554  NZ  LYS B 137     5359   4665   5428     60    366    683       N  
ATOM   3555  N   GLY B 138      53.061  94.178  11.829  1.00 21.47           N  
ANISOU 3555  N   GLY B 138     2926   2288   2941   -160    170    609       N  
ATOM   3556  CA  GLY B 138      54.095  94.896  11.112  1.00 21.27           C  
ANISOU 3556  CA  GLY B 138     2872   2219   2989   -159    191    614       C  
ATOM   3557  C   GLY B 138      53.715  94.996   9.647  1.00 20.90           C  
ANISOU 3557  C   GLY B 138     2882   2084   2974    -85    304    523       C  
ATOM   3558  O   GLY B 138      52.524  94.983   9.320  1.00 19.75           O  
ANISOU 3558  O   GLY B 138     2820   1932   2749    -57    342    433       O  
ATOM   3559  N   ASN B 139      54.721  95.115   8.773  1.00 21.88           N  
ANISOU 3559  N   ASN B 139     2959   2141   3211    -61    358    551       N  
ATOM   3560  CA  ASN B 139      54.502  95.281   7.336  1.00 22.74           C  
ANISOU 3560  CA  ASN B 139     3125   2170   3342     -9    466    469       C  
ATOM   3561  C   ASN B 139      54.126  93.919   6.746  1.00 22.43           C  
ANISOU 3561  C   ASN B 139     3079   2072   3370     42    559    479       C  
ATOM   3562  O   ASN B 139      54.860  92.985   6.965  1.00 22.36           O  
ANISOU 3562  O   ASN B 139     2978   2032   3486     54    580    580       O  
ATOM   3563  CB  ASN B 139      55.747  95.865   6.653  1.00 22.59           C  
ANISOU 3563  CB  ASN B 139     3061   2100   3421     -9    498    497       C  
ATOM   3564  CG  ASN B 139      56.097  97.238   7.195  1.00 23.71           C  
ANISOU 3564  CG  ASN B 139     3214   2296   3496    -67    413    477       C  
ATOM   3565  OD1 ASN B 139      55.230  98.106   7.254  1.00 23.83           O  
ANISOU 3565  OD1 ASN B 139     3318   2342   3392    -82    394    383       O  
ATOM   3566  ND2 ASN B 139      57.300  97.403   7.709  1.00 22.99           N  
ANISOU 3566  ND2 ASN B 139     3032   2220   3483   -105    358    573       N  
ATOM   3567  N   VAL B 140      52.982  93.836   6.042  1.00 20.60           N  
ANISOU 3567  N   VAL B 140     2942   1825   3058     64    611    382       N  
ATOM   3568  CA  VAL B 140      52.475  92.563   5.507  1.00 21.53           C  
ANISOU 3568  CA  VAL B 140     3071   1893   3217     98    699    375       C  
ATOM   3569  C   VAL B 140      52.310  92.762   4.000  1.00 20.42           C  
ANISOU 3569  C   VAL B 140     3003   1687   3067    108    802    293       C  
ATOM   3570  O   VAL B 140      51.517  93.560   3.567  1.00 19.41           O  
ANISOU 3570  O   VAL B 140     2956   1586   2830     97    785    216       O  
ATOM   3571  CB  VAL B 140      51.126  92.144   6.142  1.00 20.59           C  
ANISOU 3571  CB  VAL B 140     3000   1829   2995     97    657    343       C  
ATOM   3572  CG1 VAL B 140      50.603  90.832   5.580  1.00 20.05           C  
ANISOU 3572  CG1 VAL B 140     2944   1706   2967    124    749    331       C  
ATOM   3573  CG2 VAL B 140      51.190  92.099   7.662  1.00 20.51           C  
ANISOU 3573  CG2 VAL B 140     2935   1895   2960     70    550    414       C  
ATOM   3574  N   ALA B 141      53.084  92.033   3.205  1.00 21.56           N  
ANISOU 3574  N   ALA B 141     3116   1744   3332    124    914    317       N  
ATOM   3575  CA  ALA B 141      53.078  92.220   1.758  1.00 21.94           C  
ANISOU 3575  CA  ALA B 141     3236   1730   3368    117   1020    242       C  
ATOM   3576  C   ALA B 141      51.834  91.587   1.128  1.00 21.68           C  
ANISOU 3576  C   ALA B 141     3295   1695   3245    105   1070    165       C  
ATOM   3577  O   ALA B 141      51.241  92.167   0.202  1.00 20.89           O  
ANISOU 3577  O   ALA B 141     3283   1605   3047     79   1086     91       O  
ATOM   3578  CB  ALA B 141      54.340  91.636   1.181  1.00 25.45           C  
ANISOU 3578  CB  ALA B 141     3619   2073   3976    130   1138    290       C  
ATOM   3579  N   LYS B 142      51.457  90.397   1.629  1.00 22.09           N  
ANISOU 3579  N   LYS B 142     3321   1737   3335    118   1091    192       N  
ATOM   3580  CA  LYS B 142      50.322  89.640   1.169  1.00 23.02           C  
ANISOU 3580  CA  LYS B 142     3512   1851   3381    102   1136    130       C  
ATOM   3581  C   LYS B 142      49.444  89.236   2.368  1.00 24.11           C  
ANISOU 3581  C   LYS B 142     3628   2056   3475    118   1044    158       C  
ATOM   3582  O   LYS B 142      49.623  88.155   2.940  1.00 23.56           O  
ANISOU 3582  O   LYS B 142     3498   1959   3494    138   1073    214       O  
ATOM   3583  CB  LYS B 142      50.838  88.382   0.463  1.00 27.53           C  
ANISOU 3583  CB  LYS B 142     4074   2314   4070     99   1296    129       C  
ATOM   3584  CG  LYS B 142      51.455  88.618  -0.903  1.00 29.20           C  
ANISOU 3584  CG  LYS B 142     4339   2452   4302     68   1417     76       C  
ATOM   3585  CD  LYS B 142      50.394  88.685  -1.986  1.00 32.12           C  
ANISOU 3585  CD  LYS B 142     4838   2841   4523      7   1449    -25       C  
ATOM   3586  CE  LYS B 142      50.976  88.578  -3.380  1.00 34.71           C  
ANISOU 3586  CE  LYS B 142     5231   3086   4871    -41   1599    -83       C  
ATOM   3587  NZ  LYS B 142      51.463  89.890  -3.843  1.00 35.51           N  
ANISOU 3587  NZ  LYS B 142     5347   3212   4931    -49   1558    -87       N  
ATOM   3588  N   ALA B 143      48.482  90.087   2.720  1.00 21.64           N  
ANISOU 3588  N   ALA B 143     3363   1825   3033    108    944    123       N  
ATOM   3589  CA  ALA B 143      47.704  89.965   3.931  1.00 20.95           C  
ANISOU 3589  CA  ALA B 143     3259   1806   2895    119    852    147       C  
ATOM   3590  C   ALA B 143      46.469  89.109   3.665  1.00 20.65           C  
ANISOU 3590  C   ALA B 143     3274   1769   2802    112    882    105       C  
ATOM   3591  O   ALA B 143      46.042  88.937   2.511  1.00 21.06           O  
ANISOU 3591  O   ALA B 143     3394   1791   2817     86    949     46       O  
ATOM   3592  CB  ALA B 143      47.299  91.339   4.394  1.00 19.84           C  
ANISOU 3592  CB  ALA B 143     3145   1734   2658    108    754    125       C  
ATOM   3593  N   ASP B 144      45.914  88.564   4.746  1.00 20.19           N  
ANISOU 3593  N   ASP B 144     3186   1750   2734    128    830    139       N  
ATOM   3594  CA  ASP B 144      44.738  87.718   4.701  1.00 22.09           C  
ANISOU 3594  CA  ASP B 144     3465   1996   2931    125    848    110       C  
ATOM   3595  C   ASP B 144      43.654  88.329   5.615  1.00 21.31           C  
ANISOU 3595  C   ASP B 144     3386   1977   2732    127    747    103       C  
ATOM   3596  O   ASP B 144      43.972  88.813   6.715  1.00 20.69           O  
ANISOU 3596  O   ASP B 144     3267   1943   2649    134    676    144       O  
ATOM   3597  CB  ASP B 144      45.148  86.293   5.083  1.00 24.60           C  
ANISOU 3597  CB  ASP B 144     3721   2265   3361    144    910    165       C  
ATOM   3598  CG  ASP B 144      46.234  85.709   4.168  1.00 29.65           C  
ANISOU 3598  CG  ASP B 144     4338   2805   4121    142   1035    171       C  
ATOM   3599  OD1 ASP B 144      45.878  85.264   3.065  1.00 29.69           O  
ANISOU 3599  OD1 ASP B 144     4409   2760   4108    113   1129    103       O  
ATOM   3600  OD2 ASP B 144      47.426  85.694   4.566  1.00 34.63           O  
ANISOU 3600  OD2 ASP B 144     4884   3408   4864    163   1042    247       O  
ATOM   3601  N   ILE B 145      42.394  88.304   5.156  1.00 18.36           N  
ANISOU 3601  N   ILE B 145     3074   1621   2280    113    746     54       N  
ATOM   3602  CA  ILE B 145      41.282  88.981   5.809  1.00 18.95           C  
ANISOU 3602  CA  ILE B 145     3172   1755   2271    115    672     42       C  
ATOM   3603  C   ILE B 145      41.190  88.506   7.264  1.00 18.79           C  
ANISOU 3603  C   ILE B 145     3107   1769   2263    135    627     88       C  
ATOM   3604  O   ILE B 145      41.048  89.329   8.180  1.00 21.77           O  
ANISOU 3604  O   ILE B 145     3481   2192   2597    132    566     93       O  
ATOM   3605  CB  ILE B 145      39.952  88.770   5.056  1.00 19.50           C  
ANISOU 3605  CB  ILE B 145     3297   1831   2278     95    683      3       C  
ATOM   3606  CG1 ILE B 145      39.969  89.443   3.679  1.00 20.07           C  
ANISOU 3606  CG1 ILE B 145     3417   1890   2317     61    707    -30       C  
ATOM   3607  CG2 ILE B 145      38.779  89.216   5.914  1.00 21.01           C  
ANISOU 3607  CG2 ILE B 145     3495   2072   2416    107    621      7       C  
ATOM   3608  CD1 ILE B 145      38.803  89.051   2.739  1.00 19.87           C  
ANISOU 3608  CD1 ILE B 145     3444   1872   2230     18    719    -55       C  
ATOM   3609  N   ILE B 146      41.247  87.197   7.491  1.00 19.03           N  
ANISOU 3609  N   ILE B 146     3105   1776   2349    146    663    120       N  
ATOM   3610  CA  ILE B 146      40.997  86.690   8.821  1.00 19.01           C  
ANISOU 3610  CA  ILE B 146     3063   1812   2346    159    619    169       C  
ATOM   3611  C   ILE B 146      42.251  86.874   9.679  1.00 20.36           C  
ANISOU 3611  C   ILE B 146     3166   2001   2567    156    580    240       C  
ATOM   3612  O   ILE B 146      42.180  87.499  10.713  1.00 20.38           O  
ANISOU 3612  O   ILE B 146     3166   2063   2514    139    510    256       O  
ATOM   3613  CB  ILE B 146      40.490  85.230   8.781  1.00 20.34           C  
ANISOU 3613  CB  ILE B 146     3218   1950   2559    172    670    184       C  
ATOM   3614  CG1 ILE B 146      39.081  85.178   8.172  1.00 22.22           C  
ANISOU 3614  CG1 ILE B 146     3522   2193   2726    161    681    122       C  
ATOM   3615  CG2 ILE B 146      40.524  84.639  10.184  1.00 22.34           C  
ANISOU 3615  CG2 ILE B 146     3414   2241   2832    184    626    257       C  
ATOM   3616  CD1 ILE B 146      38.619  83.813   7.733  1.00 24.57           C  
ANISOU 3616  CD1 ILE B 146     3824   2447   3062    159    749    114       C  
ATOM   3617  N   ASP B 147      43.396  86.389   9.203  1.00 20.76           N  
ANISOU 3617  N   ASP B 147     3166   1999   2723    164    630    281       N  
ATOM   3618  CA  ASP B 147      44.654  86.347   9.987  1.00 21.91           C  
ANISOU 3618  CA  ASP B 147     3225   2157   2942    158    593    377       C  
ATOM   3619  C   ASP B 147      45.165  87.757  10.330  1.00 21.20           C  
ANISOU 3619  C   ASP B 147     3146   2115   2792    127    521    367       C  
ATOM   3620  O   ASP B 147      45.843  87.927  11.347  1.00 20.96           O  
ANISOU 3620  O   ASP B 147     3061   2133   2769    101    452    441       O  
ATOM   3621  CB  ASP B 147      45.775  85.612   9.256  1.00 24.08           C  
ANISOU 3621  CB  ASP B 147     3438   2347   3364    177    681    425       C  
ATOM   3622  CG  ASP B 147      46.888  85.192  10.201  1.00 27.64           C  
ANISOU 3622  CG  ASP B 147     3773   2809   3918    176    642    558       C  
ATOM   3623  OD1 ASP B 147      46.576  84.588  11.230  1.00 30.78           O  
ANISOU 3623  OD1 ASP B 147     4130   3250   4311    173    594    624       O  
ATOM   3624  OD2 ASP B 147      48.037  85.547   9.946  1.00 34.13           O  
ANISOU 3624  OD2 ASP B 147     4544   3603   4818    172    651    602       O  
ATOM   3625  N   ASN B 148      44.874  88.737   9.483  1.00 19.76           N  
ANISOU 3625  N   ASN B 148     3030   1921   2555    123    536    284       N  
ATOM   3626  CA  ASN B 148      45.324  90.125   9.711  1.00 20.07           C  
ANISOU 3626  CA  ASN B 148     3085   1994   2545     95    483    264       C  
ATOM   3627  C   ASN B 148      44.177  91.057  10.113  1.00 21.10           C  
ANISOU 3627  C   ASN B 148     3287   2170   2560     79    446    196       C  
ATOM   3628  O   ASN B 148      44.336  92.297  10.041  1.00 19.27           O  
ANISOU 3628  O   ASN B 148     3084   1948   2289     58    427    157       O  
ATOM   3629  CB  ASN B 148      46.025  90.716   8.490  1.00 20.26           C  
ANISOU 3629  CB  ASN B 148     3121   1966   2611    101    532    233       C  
ATOM   3630  CG  ASN B 148      47.303  89.981   8.156  1.00 21.50           C  
ANISOU 3630  CG  ASN B 148     3201   2067   2898    113    580    303       C  
ATOM   3631  OD1 ASN B 148      47.330  89.268   7.154  1.00 22.87           O  
ANISOU 3631  OD1 ASN B 148     3384   2175   3131    133    671    285       O  
ATOM   3632  ND2 ASN B 148      48.316  90.074   9.017  1.00 20.21           N  
ANISOU 3632  ND2 ASN B 148     2962   1932   2785     94    524    388       N  
ATOM   3633  N   SER B 149      43.054  90.495  10.575  1.00 19.08           N  
ANISOU 3633  N   SER B 149     3054   1934   2260     88    443    185       N  
ATOM   3634  CA  SER B 149      42.015  91.257  11.309  1.00 19.47           C  
ANISOU 3634  CA  SER B 149     3155   2024   2215     69    411    140       C  
ATOM   3635  C   SER B 149      41.405  92.363  10.453  1.00 20.18           C  
ANISOU 3635  C   SER B 149     3299   2090   2275     76    437     71       C  
ATOM   3636  O   SER B 149      41.024  93.397  10.982  1.00 19.78           O  
ANISOU 3636  O   SER B 149     3281   2058   2175     55    422     36       O  
ATOM   3637  CB  SER B 149      42.565  91.850  12.575  1.00 21.92           C  
ANISOU 3637  CB  SER B 149     3456   2391   2483     18    352    163       C  
ATOM   3638  OG  SER B 149      42.933  90.820  13.459  1.00 22.80           O  
ANISOU 3638  OG  SER B 149     3514   2536   2612      5    318    242       O  
ATOM   3639  N   ILE B 150      41.280  92.126   9.144  1.00 18.91           N  
ANISOU 3639  N   ILE B 150     3149   1887   2146     99    480     55       N  
ATOM   3640  CA  ILE B 150      40.807  93.131   8.263  1.00 19.25           C  
ANISOU 3640  CA  ILE B 150     3232   1913   2169    100    496     12       C  
ATOM   3641  C   ILE B 150      39.311  93.433   8.505  1.00 19.40           C  
ANISOU 3641  C   ILE B 150     3283   1944   2142    106    494    -10       C  
ATOM   3642  O   ILE B 150      38.875  94.590   8.269  1.00 18.83           O  
ANISOU 3642  O   ILE B 150     3232   1863   2057    103    498    -33       O  
ATOM   3643  CB  ILE B 150      41.134  92.786   6.801  1.00 19.39           C  
ANISOU 3643  CB  ILE B 150     3257   1890   2219    104    541      7       C  
ATOM   3644  CG1 ILE B 150      42.653  92.617   6.619  1.00 20.17           C  
ANISOU 3644  CG1 ILE B 150     3317   1964   2381    101    558     32       C  
ATOM   3645  CG2 ILE B 150      40.547  93.845   5.881  1.00 20.12           C  
ANISOU 3645  CG2 ILE B 150     3385   1974   2283     97    547    -20       C  
ATOM   3646  CD1 ILE B 150      43.116  92.394   5.170  1.00 21.24           C  
ANISOU 3646  CD1 ILE B 150     3468   2051   2549     97    620     18       C  
ATOM   3647  N   PHE B 151      38.559  92.495   9.089  1.00 17.64           N  
ANISOU 3647  N   PHE B 151     3057   1737   1906    116    490      2       N  
ATOM   3648  CA  PHE B 151      37.137  92.722   9.329  1.00 18.26           C  
ANISOU 3648  CA  PHE B 151     3159   1822   1956    124    493    -11       C  
ATOM   3649  C   PHE B 151      36.945  93.752  10.440  1.00 18.06           C  
ANISOU 3649  C   PHE B 151     3148   1810   1903    109    487    -32       C  
ATOM   3650  O   PHE B 151      35.839  94.235  10.607  1.00 18.56           O  
ANISOU 3650  O   PHE B 151     3227   1862   1960    117    506    -45       O  
ATOM   3651  CB  PHE B 151      36.402  91.436   9.727  1.00 19.16           C  
ANISOU 3651  CB  PHE B 151     3265   1948   2066    136    494      8       C  
ATOM   3652  CG  PHE B 151      35.978  90.543   8.596  1.00 20.44           C  
ANISOU 3652  CG  PHE B 151     3430   2091   2243    140    515     13       C  
ATOM   3653  CD1 PHE B 151      35.579  91.060   7.372  1.00 21.10           C  
ANISOU 3653  CD1 PHE B 151     3534   2160   2321    128    524      3       C  
ATOM   3654  CD2 PHE B 151      36.030  89.157   8.749  1.00 21.48           C  
ANISOU 3654  CD2 PHE B 151     3545   2219   2394    146    529     31       C  
ATOM   3655  CE1 PHE B 151      35.161  90.214   6.352  1.00 22.81           C  
ANISOU 3655  CE1 PHE B 151     3765   2367   2533    109    541      4       C  
ATOM   3656  CE2 PHE B 151      35.614  88.318   7.727  1.00 20.74           C  
ANISOU 3656  CE2 PHE B 151     3466   2105   2309    135    559     25       C  
ATOM   3657  CZ  PHE B 151      35.165  88.841   6.538  1.00 21.32           C  
ANISOU 3657  CZ  PHE B 151     3569   2171   2358    110    564      8       C  
ATOM   3658  N   TYR B 152      38.005  93.986  11.238  1.00 17.32           N  
ANISOU 3658  N   TYR B 152     3047   1738   1796     81    465    -31       N  
ATOM   3659  CA  TYR B 152      38.039  94.949  12.314  1.00 19.02           C  
ANISOU 3659  CA  TYR B 152     3287   1968   1971     43    464    -61       C  
ATOM   3660  C   TYR B 152      38.585  96.313  11.855  1.00 20.63           C  
ANISOU 3660  C   TYR B 152     3503   2145   2190     28    479    -93       C  
ATOM   3661  O   TYR B 152      38.742  97.212  12.683  1.00 19.86           O  
ANISOU 3661  O   TYR B 152     3432   2052   2061    -13    488   -128       O  
ATOM   3662  CB  TYR B 152      38.829  94.349  13.477  1.00 19.94           C  
ANISOU 3662  CB  TYR B 152     3387   2134   2052      2    422    -32       C  
ATOM   3663  CG  TYR B 152      38.126  93.152  14.058  1.00 20.74           C  
ANISOU 3663  CG  TYR B 152     3481   2260   2140     16    415     -1       C  
ATOM   3664  CD1 TYR B 152      38.345  91.883  13.541  1.00 20.56           C  
ANISOU 3664  CD1 TYR B 152     3416   2233   2163     50    407     46       C  
ATOM   3665  CD2 TYR B 152      37.205  93.276  15.095  1.00 22.31           C  
ANISOU 3665  CD2 TYR B 152     3714   2476   2285     -5    430    -24       C  
ATOM   3666  CE1 TYR B 152      37.652  90.782  14.009  1.00 20.37           C  
ANISOU 3666  CE1 TYR B 152     3381   2222   2134     65    408     74       C  
ATOM   3667  CE2 TYR B 152      36.545  92.167  15.606  1.00 21.93           C  
ANISOU 3667  CE2 TYR B 152     3656   2449   2227      9    425      5       C  
ATOM   3668  CZ  TYR B 152      36.756  90.923  15.057  1.00 22.31           C  
ANISOU 3668  CZ  TYR B 152     3658   2493   2323     46    411     56       C  
ATOM   3669  OH  TYR B 152      36.079  89.828  15.537  1.00 22.24           O  
ANISOU 3669  OH  TYR B 152     3637   2498   2312     62    412     87       O  
ATOM   3670  N   ALA B 153      38.856  96.472  10.554  1.00 17.98           N  
ANISOU 3670  N   ALA B 153     3153   1780   1897     55    487    -84       N  
ATOM   3671  CA  ALA B 153      39.365  97.742  10.002  1.00 18.87           C  
ANISOU 3671  CA  ALA B 153     3272   1863   2031     46    503   -107       C  
ATOM   3672  C   ALA B 153      38.722  98.045   8.652  1.00 18.93           C  
ANISOU 3672  C   ALA B 153     3278   1838   2074     78    526    -96       C  
ATOM   3673  O   ALA B 153      39.432  98.280   7.692  1.00 22.57           O  
ANISOU 3673  O   ALA B 153     3731   2285   2558     80    525    -87       O  
ATOM   3674  CB  ALA B 153      40.864  97.670   9.894  1.00 19.16           C  
ANISOU 3674  CB  ALA B 153     3286   1912   2081     26    475    -91       C  
ATOM   3675  N   LEU B 154      37.395  98.050   8.553  1.00 19.63           N  
ANISOU 3675  N   LEU B 154     3373   1916   2169     98    544    -88       N  
ATOM   3676  CA  LEU B 154      36.759  98.120   7.219  1.00 21.09           C  
ANISOU 3676  CA  LEU B 154     3548   2085   2378    114    548    -55       C  
ATOM   3677  C   LEU B 154      36.429  99.550   6.721  1.00 22.12           C  
ANISOU 3677  C   LEU B 154     3672   2179   2553    118    575    -47       C  
ATOM   3678  O   LEU B 154      35.702  99.673   5.711  1.00 22.35           O  
ANISOU 3678  O   LEU B 154     3686   2202   2603    125    571     -1       O  
ATOM   3679  CB  LEU B 154      35.475  97.295   7.272  1.00 23.84           C  
ANISOU 3679  CB  LEU B 154     3893   2445   2720    128    544    -30       C  
ATOM   3680  CG  LEU B 154      35.666  95.776   7.423  1.00 22.78           C  
ANISOU 3680  CG  LEU B 154     3759   2339   2555    127    524    -27       C  
ATOM   3681  CD1 LEU B 154      34.329  95.102   7.664  1.00 23.74           C  
ANISOU 3681  CD1 LEU B 154     3878   2469   2672    138    524     -7       C  
ATOM   3682  CD2 LEU B 154      36.359  95.193   6.220  1.00 22.11           C  
ANISOU 3682  CD2 LEU B 154     3677   2254   2468    114    519    -17       C  
ATOM   3683  N   SER B 155      37.014 100.615   7.280  1.00 25.82           N  
ANISOU 3683  N   SER B 155     4148   2624   3038    107    600    -81       N  
ATOM   3684  CA  SER B 155      36.861 101.968   6.659  1.00 26.10           C  
ANISOU 3684  CA  SER B 155     4169   2614   3130    113    634    -68       C  
ATOM   3685  C   SER B 155      37.487 101.995   5.244  1.00 28.32           C  
ANISOU 3685  C   SER B 155     4441   2904   3416    111    608    -34       C  
ATOM   3686  O   SER B 155      38.380 101.187   4.942  1.00 29.13           O  
ANISOU 3686  O   SER B 155     4552   3032   3481    100    581    -43       O  
ATOM   3687  CB  SER B 155      37.490 103.041   7.529  1.00 26.37           C  
ANISOU 3687  CB  SER B 155     4220   2619   3178     91    673   -123       C  
ATOM   3688  OG  SER B 155      38.907 103.009   7.426  1.00 30.18           O  
ANISOU 3688  OG  SER B 155     4709   3121   3634     68    643   -144       O  
ATOM   3689  N   VAL B 156      37.101 102.989   4.429  1.00 27.52           N  
ANISOU 3689  N   VAL B 156     4317   2772   3366    118    626      6       N  
ATOM   3690  CA  VAL B 156      37.661 103.201   3.091  1.00 26.64           C  
ANISOU 3690  CA  VAL B 156     4199   2666   3253    106    607     40       C  
ATOM   3691  C   VAL B 156      38.823 104.207   3.125  1.00 28.29           C  
ANISOU 3691  C   VAL B 156     4411   2847   3490    101    630      7       C  
ATOM   3692  O   VAL B 156      39.223 104.763   2.061  1.00 26.79           O  
ANISOU 3692  O   VAL B 156     4212   2648   3318     94    630     40       O  
ATOM   3693  CB  VAL B 156      36.580 103.680   2.106  1.00 28.37           C  
ANISOU 3693  CB  VAL B 156     4387   2882   3511    107    602    124       C  
ATOM   3694  CG1 VAL B 156      35.466 102.658   1.970  1.00 28.80           C  
ANISOU 3694  CG1 VAL B 156     4436   2970   3534    101    570    163       C  
ATOM   3695  CG2 VAL B 156      36.030 105.038   2.485  1.00 29.40           C  
ANISOU 3695  CG2 VAL B 156     4481   2954   3735    129    651    147       C  
ATOM   3696  N   LEU B 157      39.424 104.417   4.303  1.00 27.53           N  
ANISOU 3696  N   LEU B 157     4329   2740   3390     94    647    -53       N  
ATOM   3697  CA  LEU B 157      40.627 105.255   4.428  1.00 25.45           C  
ANISOU 3697  CA  LEU B 157     4070   2455   3144     77    661    -88       C  
ATOM   3698  C   LEU B 157      41.839 104.390   4.117  1.00 24.85           C  
ANISOU 3698  C   LEU B 157     3999   2411   3030     65    624    -94       C  
ATOM   3699  O   LEU B 157      42.729 104.130   4.942  1.00 25.27           O  
ANISOU 3699  O   LEU B 157     4056   2479   3064     45    609   -127       O  
ATOM   3700  CB  LEU B 157      40.681 105.896   5.809  1.00 30.13           C  
ANISOU 3700  CB  LEU B 157     4679   3025   3741     56    695   -148       C  
ATOM   3701  CG  LEU B 157      39.362 106.529   6.254  1.00 28.35           C  
ANISOU 3701  CG  LEU B 157     4451   2757   3563     69    754   -146       C  
ATOM   3702  CD1 LEU B 157      39.440 106.997   7.696  1.00 30.21           C  
ANISOU 3702  CD1 LEU B 157     4721   2973   3783     30    800   -221       C  
ATOM   3703  CD2 LEU B 157      38.957 107.653   5.333  1.00 26.47           C  
ANISOU 3703  CD2 LEU B 157     4179   2465   3413     92    794    -98       C  
ATOM   3704  N   LYS B 158      41.864 103.986   2.849  1.00 23.42           N  
ANISOU 3704  N   LYS B 158     3815   2239   2843     71    615    -55       N  
ATOM   3705  CA  LYS B 158      42.804 103.045   2.304  1.00 20.92           C  
ANISOU 3705  CA  LYS B 158     3504   1939   2505     61    603    -54       C  
ATOM   3706  C   LYS B 158      43.078 103.430   0.844  1.00 18.86           C  
ANISOU 3706  C   LYS B 158     3247   1666   2251     52    617    -24       C  
ATOM   3707  O   LYS B 158      42.297 104.204   0.243  1.00 17.33           O  
ANISOU 3707  O   LYS B 158     3047   1465   2070     52    621     11       O  
ATOM   3708  CB  LYS B 158      42.208 101.636   2.372  1.00 20.62           C  
ANISOU 3708  CB  LYS B 158     3476   1931   2427     63    588    -46       C  
ATOM   3709  CG  LYS B 158      41.918 101.109   3.782  1.00 21.94           C  
ANISOU 3709  CG  LYS B 158     3640   2116   2579     69    572    -68       C  
ATOM   3710  CD  LYS B 158      41.094  99.857   3.783  1.00 20.96           C  
ANISOU 3710  CD  LYS B 158     3524   2016   2424     75    562    -55       C  
ATOM   3711  CE  LYS B 158      40.918  99.252   5.170  1.00 23.71           C  
ANISOU 3711  CE  LYS B 158     3867   2385   2755     78    545    -70       C  
ATOM   3712  NZ  LYS B 158      40.442 100.232   6.193  1.00 24.32           N  
ANISOU 3712  NZ  LYS B 158     3949   2456   2834     74    552    -93       N  
ATOM   3713  N   MET B 159      44.106 102.796   0.273  1.00 18.73           N  
ANISOU 3713  N   MET B 159     3238   1647   2229     40    629    -30       N  
ATOM   3714  CA  MET B 159      44.483 102.942  -1.153  1.00 18.67           C  
ANISOU 3714  CA  MET B 159     3248   1631   2214     18    653     -9       C  
ATOM   3715  C   MET B 159      43.920 101.757  -1.952  1.00 18.10           C  
ANISOU 3715  C   MET B 159     3209   1582   2085     -9    660      0       C  
ATOM   3716  O   MET B 159      44.295 100.627  -1.695  1.00 19.39           O  
ANISOU 3716  O   MET B 159     3379   1743   2244     -9    677    -22       O  
ATOM   3717  CB  MET B 159      46.009 103.018  -1.323  1.00 19.83           C  
ANISOU 3717  CB  MET B 159     3385   1749   2400     17    681    -27       C  
ATOM   3718  CG  MET B 159      46.438 103.484  -2.731  1.00 21.01           C  
ANISOU 3718  CG  MET B 159     3554   1882   2545     -7    714     -8       C  
ATOM   3719  SD  MET B 159      48.218 103.858  -2.858  1.00 22.44           S  
ANISOU 3719  SD  MET B 159     3713   2019   2794     -2    753    -22       S  
ATOM   3720  CE  MET B 159      48.228 105.484  -2.105  1.00 24.28           C  
ANISOU 3720  CE  MET B 159     3913   2241   3070     15    723    -23       C  
ATOM   3721  N   PHE B 160      42.996 102.043  -2.873  1.00 18.11           N  
ANISOU 3721  N   PHE B 160     3227   1605   2048    -38    647     40       N  
ATOM   3722  CA  PHE B 160      42.237 101.063  -3.633  1.00 19.29           C  
ANISOU 3722  CA  PHE B 160     3413   1787   2129    -84    643     53       C  
ATOM   3723  C   PHE B 160      42.640 101.123  -5.104  1.00 20.74           C  
ANISOU 3723  C   PHE B 160     3638   1976   2266   -146    671     67       C  
ATOM   3724  O   PHE B 160      42.624 102.225  -5.672  1.00 20.49           O  
ANISOU 3724  O   PHE B 160     3594   1947   2244   -155    659    110       O  
ATOM   3725  CB  PHE B 160      40.740 101.361  -3.602  1.00 19.92           C  
ANISOU 3725  CB  PHE B 160     3476   1901   2192    -89    595    108       C  
ATOM   3726  CG  PHE B 160      40.077 101.189  -2.258  1.00 19.37           C  
ANISOU 3726  CG  PHE B 160     3376   1828   2154    -41    575     96       C  
ATOM   3727  CD1 PHE B 160      40.032 102.224  -1.342  1.00 20.98           C  
ANISOU 3727  CD1 PHE B 160     3543   2006   2420      3    575     95       C  
ATOM   3728  CD2 PHE B 160      39.528  99.968  -1.900  1.00 21.55           C  
ANISOU 3728  CD2 PHE B 160     3667   2125   2396    -48    568     80       C  
ATOM   3729  CE1 PHE B 160      39.436 102.050  -0.097  1.00 21.74           C  
ANISOU 3729  CE1 PHE B 160     3624   2099   2536     35    569     77       C  
ATOM   3730  CE2 PHE B 160      38.906  99.798  -0.672  1.00 21.22           C  
ANISOU 3730  CE2 PHE B 160     3601   2082   2378     -7    553     71       C  
ATOM   3731  CZ  PHE B 160      38.866 100.847   0.229  1.00 22.29           C  
ANISOU 3731  CZ  PHE B 160     3705   2194   2568     31    555     68       C  
ATOM   3732  N   LYS B 161      42.947  99.957  -5.717  1.00 20.70           N  
ANISOU 3732  N   LYS B 161     3683   1969   2213   -193    717     33       N  
ATOM   3733  CA  LYS B 161      43.266  99.898  -7.141  1.00 21.25           C  
ANISOU 3733  CA  LYS B 161     3809   2045   2219   -272    756     35       C  
ATOM   3734  C   LYS B 161      41.981 100.139  -7.941  1.00 22.03           C  
ANISOU 3734  C   LYS B 161     3926   2207   2235   -341    697     99       C  
ATOM   3735  O   LYS B 161      40.975  99.488  -7.758  1.00 21.01           O  
ANISOU 3735  O   LYS B 161     3803   2112   2068   -362    663    112       O  
ATOM   3736  CB  LYS B 161      43.894  98.554  -7.535  1.00 25.65           C  
ANISOU 3736  CB  LYS B 161     4420   2571   2753   -313    841    -27       C  
ATOM   3737  CG  LYS B 161      44.335  98.459  -8.999  1.00 28.28           C  
ANISOU 3737  CG  LYS B 161     4827   2901   3016   -407    905    -40       C  
ATOM   3738  CD  LYS B 161      45.102  97.205  -9.335  1.00 32.84           C  
ANISOU 3738  CD  LYS B 161     5455   3422   3597   -443   1020   -111       C  
ATOM   3739  CE  LYS B 161      46.603  97.354  -9.156  1.00 39.55           C  
ANISOU 3739  CE  LYS B 161     6277   4196   4552   -390   1099   -137       C  
ATOM   3740  NZ  LYS B 161      47.385  96.200  -9.684  1.00 44.70           N  
ANISOU 3740  NZ  LYS B 161     6979   4779   5225   -433   1236   -198       N  
ATOM   3741  N   LYS B 162      42.045 101.093  -8.872  1.00 22.70           N  
ANISOU 3741  N   LYS B 162     4017   2312   2296   -382    683    151       N  
ATOM   3742  CA  LYS B 162      40.871 101.675  -9.488  1.00 25.26           C  
ANISOU 3742  CA  LYS B 162     4327   2697   2572   -433    610    247       C  
ATOM   3743  C   LYS B 162      40.232 100.718 -10.505  1.00 26.85           C  
ANISOU 3743  C   LYS B 162     4600   2957   2645   -557    601    255       C  
ATOM   3744  O   LYS B 162      39.020 100.717 -10.671  1.00 29.18           O  
ANISOU 3744  O   LYS B 162     4876   3309   2901   -599    528    330       O  
ATOM   3745  CB  LYS B 162      41.261 103.000 -10.141  1.00 26.81           C  
ANISOU 3745  CB  LYS B 162     4499   2892   2792   -438    601    308       C  
ATOM   3746  CG  LYS B 162      40.143 103.686 -10.895  1.00 31.72           C  
ANISOU 3746  CG  LYS B 162     5094   3578   3379   -498    524    433       C  
ATOM   3747  CD  LYS B 162      38.985 104.088 -10.034  1.00 35.54           C  
ANISOU 3747  CD  LYS B 162     5497   4067   3938   -437    465    499       C  
ATOM   3748  CE  LYS B 162      38.377 105.394 -10.491  1.00 39.22           C  
ANISOU 3748  CE  LYS B 162     5892   4550   4457   -441    415    634       C  
ATOM   3749  NZ  LYS B 162      37.827 105.283 -11.863  1.00 38.61           N  
ANISOU 3749  NZ  LYS B 162     5843   4555   4269   -570    360    730       N  
ATOM   3750  N   SER B 163      41.044  99.947 -11.220  1.00 25.42           N  
ANISOU 3750  N   SER B 163     4499   2758   2399   -624    681    183       N  
ATOM   3751  CA  SER B 163      40.531  98.939 -12.165  1.00 30.28           C  
ANISOU 3751  CA  SER B 163     5202   3421   2882   -759    694    167       C  
ATOM   3752  C   SER B 163      39.569  97.933 -11.490  1.00 28.81           C  
ANISOU 3752  C   SER B 163     5009   3252   2686   -754    664    152       C  
ATOM   3753  O   SER B 163      38.568  97.509 -12.091  1.00 29.34           O  
ANISOU 3753  O   SER B 163     5108   3385   2652   -859    615    191       O  
ATOM   3754  CB  SER B 163      41.685  98.203 -12.824  1.00 32.22           C  
ANISOU 3754  CB  SER B 163     5535   3615   3090   -816    820     68       C  
ATOM   3755  OG  SER B 163      42.476  97.568 -11.834  1.00 32.66           O  
ANISOU 3755  OG  SER B 163     5567   3591   3251   -717    892     -9       O  
ATOM   3756  N   VAL B 164      39.841  97.557 -10.233  1.00 26.12           N  
ANISOU 3756  N   VAL B 164     4621   2855   2445   -641    687    102       N  
ATOM   3757  CA  VAL B 164      38.975  96.621  -9.520  1.00 27.11           C  
ANISOU 3757  CA  VAL B 164     4736   2992   2571   -627    663     89       C  
ATOM   3758  C   VAL B 164      37.569  97.234  -9.340  1.00 28.12           C  
ANISOU 3758  C   VAL B 164     4805   3184   2694   -626    550    194       C  
ATOM   3759  O   VAL B 164      36.548  96.577  -9.621  1.00 27.02           O  
ANISOU 3759  O   VAL B 164     4686   3094   2485   -700    509    220       O  
ATOM   3760  CB  VAL B 164      39.612  96.233  -8.170  1.00 27.65           C  
ANISOU 3760  CB  VAL B 164     4759   2994   2750   -506    704     31       C  
ATOM   3761  CG1 VAL B 164      38.662  95.408  -7.321  1.00 29.09           C  
ANISOU 3761  CG1 VAL B 164     4920   3190   2940   -480    671     29       C  
ATOM   3762  CG2 VAL B 164      40.939  95.506  -8.341  1.00 27.24           C  
ANISOU 3762  CG2 VAL B 164     4749   2874   2724   -507    819    -52       C  
ATOM   3763  N   ILE B 165      37.521  98.493  -8.862  1.00 25.70           N  
ANISOU 3763  N   ILE B 165     4423   2868   2471   -545    507    256       N  
ATOM   3764  CA  ILE B 165      36.291  99.293  -8.696  1.00 25.54           C  
ANISOU 3764  CA  ILE B 165     4330   2888   2484   -532    418    369       C  
ATOM   3765  C   ILE B 165      35.559  99.448 -10.039  1.00 27.67           C  
ANISOU 3765  C   ILE B 165     4621   3237   2652   -664    357    465       C  
ATOM   3766  O   ILE B 165      34.341  99.315 -10.078  1.00 28.11           O  
ANISOU 3766  O   ILE B 165     4644   3343   2693   -701    285    547       O  
ATOM   3767  CB  ILE B 165      36.620 100.678  -8.087  1.00 25.37           C  
ANISOU 3767  CB  ILE B 165     4235   2824   2578   -432    416    404       C  
ATOM   3768  CG1 ILE B 165      37.015 100.567  -6.613  1.00 24.10           C  
ANISOU 3768  CG1 ILE B 165     4044   2603   2507   -319    453    330       C  
ATOM   3769  CG2 ILE B 165      35.469 101.654  -8.275  1.00 26.08           C  
ANISOU 3769  CG2 ILE B 165     4250   2946   2713   -435    344    540       C  
ATOM   3770  CD1 ILE B 165      37.954 101.629  -6.170  1.00 25.07           C  
ANISOU 3770  CD1 ILE B 165     4137   2675   2712   -249    486    310       C  
ATOM   3771  N   ASP B 166      36.286  99.828 -11.097  1.00 30.40           N  
ANISOU 3771  N   ASP B 166     5015   3597   2936   -735    379    468       N  
ATOM   3772  CA  ASP B 166      35.684 100.107 -12.419  1.00 33.76           C  
ANISOU 3772  CA  ASP B 166     5463   4107   3254   -875    314    572       C  
ATOM   3773  C   ASP B 166      35.056  98.827 -13.012  1.00 32.41           C  
ANISOU 3773  C   ASP B 166     5371   3996   2946  -1012    300    547       C  
ATOM   3774  O   ASP B 166      33.874  98.821 -13.374  1.00 32.43           O  
ANISOU 3774  O   ASP B 166     5344   4074   2902  -1090    206    655       O  
ATOM   3775  CB  ASP B 166      36.699 100.709 -13.399  1.00 34.00           C  
ANISOU 3775  CB  ASP B 166     5541   4137   3238   -928    355    566       C  
ATOM   3776  CG  ASP B 166      37.101 102.153 -13.109  1.00 40.98           C  
ANISOU 3776  CG  ASP B 166     6342   4982   4243   -827    347    628       C  
ATOM   3777  OD1 ASP B 166      36.368 102.855 -12.340  1.00 41.57           O  
ANISOU 3777  OD1 ASP B 166     6317   5045   4432   -739    297    706       O  
ATOM   3778  OD2 ASP B 166      38.141 102.593 -13.671  1.00 46.19           O  
ANISOU 3778  OD2 ASP B 166     7039   5620   4890   -840    399    598       O  
ATOM   3779  N   LYS B 167      35.844  97.754 -13.140  1.00 33.28           N  
ANISOU 3779  N   LYS B 167     5577   4069   2996  -1048    398    410       N  
ATOM   3780  CA  LYS B 167      35.357  96.541 -13.846  1.00 38.96           C  
ANISOU 3780  CA  LYS B 167     6390   4837   3573  -1200    408    371       C  
ATOM   3781  C   LYS B 167      34.225  95.859 -13.055  1.00 36.53           C  
ANISOU 3781  C   LYS B 167     6038   4547   3294  -1172    353    391       C  
ATOM   3782  O   LYS B 167      33.355  95.271 -13.668  1.00 37.97           O  
ANISOU 3782  O   LYS B 167     6259   4799   3367  -1306    302    425       O  
ATOM   3783  CB  LYS B 167      36.515  95.606 -14.224  1.00 43.31           C  
ANISOU 3783  CB  LYS B 167     7054   5327   4073  -1247    551    220       C  
ATOM   3784  CG  LYS B 167      37.123  94.799 -13.092  1.00 45.03           C  
ANISOU 3784  CG  LYS B 167     7259   5448   4400  -1121    642    110       C  
ATOM   3785  N   ASN B 168      34.177  96.012 -11.722  1.00 32.97           N  
ANISOU 3785  N   ASN B 168     5504   4037   2984  -1010    354    379       N  
ATOM   3786  CA  ASN B 168      33.108  95.392 -10.900  1.00 32.99           C  
ANISOU 3786  CA  ASN B 168     5461   4049   3021   -974    309    398       C  
ATOM   3787  C   ASN B 168      31.998  96.385 -10.542  1.00 34.58           C  
ANISOU 3787  C   ASN B 168     5550   4287   3301   -925    202    546       C  
ATOM   3788  O   ASN B 168      31.095  96.050  -9.763  1.00 35.71           O  
ANISOU 3788  O   ASN B 168     5639   4429   3496   -878    167    573       O  
ATOM   3789  CB  ASN B 168      33.691  94.780  -9.625  1.00 32.68           C  
ANISOU 3789  CB  ASN B 168     5410   3926   3080   -842    386    292       C  
ATOM   3790  CG  ASN B 168      34.717  93.731  -9.972  1.00 32.92           C  
ANISOU 3790  CG  ASN B 168     5537   3910   3060   -888    501    164       C  
ATOM   3791  OD1 ASN B 168      34.355  92.723 -10.545  1.00 36.68           O  
ANISOU 3791  OD1 ASN B 168     6083   4409   3441  -1001    523    126       O  
ATOM   3792  ND2 ASN B 168      35.989  93.999  -9.727  1.00 33.06           N  
ANISOU 3792  ND2 ASN B 168     5558   3861   3141   -815    579    102       N  
ATOM   3793  N   LYS B 169      32.100  97.614 -11.059  1.00 34.84           N  
ANISOU 3793  N   LYS B 169     5539   4340   3357   -928    162    641       N  
ATOM   3794  CA  LYS B 169      31.125  98.669 -10.874  1.00 35.38           C  
ANISOU 3794  CA  LYS B 169     5493   4431   3517   -888     76    797       C  
ATOM   3795  C   LYS B 169      30.844  98.882  -9.383  1.00 34.85           C  
ANISOU 3795  C   LYS B 169     5347   4292   3602   -728    100    777       C  
ATOM   3796  O   LYS B 169      29.699  99.051  -9.003  1.00 34.18           O  
ANISOU 3796  O   LYS B 169     5183   4221   3581   -708     44    875       O  
ATOM   3797  CB  LYS B 169      29.843  98.347 -11.649  1.00 40.10           C  
ANISOU 3797  CB  LYS B 169     6076   5127   4034  -1026    -27    922       C  
ATOM   3798  CG  LYS B 169      30.019  98.214 -13.155  1.00 44.74           C  
ANISOU 3798  CG  LYS B 169     6745   5800   4453  -1211    -62    956       C  
ATOM   3799  CD  LYS B 169      28.711  98.121 -13.933  1.00 50.22           C  
ANISOU 3799  CD  LYS B 169     7405   6604   5071  -1358   -189   1115       C  
ATOM   3800  CE  LYS B 169      28.154  96.713 -14.015  1.00 58.66           C  
ANISOU 3800  CE  LYS B 169     8546   7711   6028  -1463   -196   1049       C  
ATOM   3801  N   ILE B 170      31.900  98.942  -8.558  1.00 31.89           N  
ANISOU 3801  N   ILE B 170     4991   3841   3285   -622    184    660       N  
ATOM   3802  CA  ILE B 170      31.740  99.096  -7.107  1.00 28.46           C  
ANISOU 3802  CA  ILE B 170     4499   3342   2972   -488    214    627       C  
ATOM   3803  C   ILE B 170      31.448 100.573  -6.801  1.00 28.61           C  
ANISOU 3803  C   ILE B 170     4424   3329   3116   -415    201    722       C  
ATOM   3804  O   ILE B 170      32.154 101.458  -7.246  1.00 28.69           O  
ANISOU 3804  O   ILE B 170     4431   3324   3144   -411    217    737       O  
ATOM   3805  CB  ILE B 170      32.975  98.585  -6.344  1.00 27.71           C  
ANISOU 3805  CB  ILE B 170     4454   3187   2885   -420    298    480       C  
ATOM   3806  CG1 ILE B 170      33.365  97.173  -6.802  1.00 28.65           C  
ANISOU 3806  CG1 ILE B 170     4663   3324   2898   -496    331    393       C  
ATOM   3807  CG2 ILE B 170      32.724  98.648  -4.832  1.00 27.91           C  
ANISOU 3807  CG2 ILE B 170     4430   3162   3011   -305    320    449       C  
ATOM   3808  CD1 ILE B 170      34.550  96.551  -6.073  1.00 27.09           C  
ANISOU 3808  CD1 ILE B 170     4500   3065   2726   -432    414    271       C  
ATOM   3809  N   LYS B 171      30.386 100.820  -6.034  1.00 29.02           N  
ANISOU 3809  N   LYS B 171     4398   3361   3264   -359    183    787       N  
ATOM   3810  CA  LYS B 171      29.882 102.153  -5.713  1.00 30.30           C  
ANISOU 3810  CA  LYS B 171     4463   3481   3568   -294    187    889       C  
ATOM   3811  C   LYS B 171      29.437 102.183  -4.253  1.00 29.31           C  
ANISOU 3811  C   LYS B 171     4299   3289   3548   -191    239    846       C  
ATOM   3812  O   LYS B 171      28.986 101.162  -3.731  1.00 26.39           O  
ANISOU 3812  O   LYS B 171     3951   2932   3143   -191    233    802       O  
ATOM   3813  CB  LYS B 171      28.667 102.488  -6.582  1.00 33.34           C  
ANISOU 3813  CB  LYS B 171     4772   3921   3972   -365    103   1071       C  
ATOM   3814  CG  LYS B 171      28.957 102.644  -8.064  1.00 36.20           C  
ANISOU 3814  CG  LYS B 171     5163   4359   4229   -484     42   1142       C  
ATOM   3815  CD  LYS B 171      27.699 102.962  -8.891  1.00 40.74           C  
ANISOU 3815  CD  LYS B 171     5652   5002   4823   -568    -57   1346       C  
ATOM   3816  N   PHE B 172      29.522 103.357  -3.617  1.00 27.09           N  
ANISOU 3816  N   PHE B 172     3963   2934   3394   -113    294    860       N  
ATOM   3817  CA  PHE B 172      28.967 103.535  -2.286  1.00 27.44           C  
ANISOU 3817  CA  PHE B 172     3971   2912   3544    -30    354    832       C  
ATOM   3818  C   PHE B 172      27.435 103.569  -2.384  1.00 30.57           C  
ANISOU 3818  C   PHE B 172     4278   3315   4022    -38    318    974       C  
ATOM   3819  O   PHE B 172      26.867 104.205  -3.295  1.00 28.42           O  
ANISOU 3819  O   PHE B 172     3934   3063   3800    -76    271   1124       O  
ATOM   3820  CB  PHE B 172      29.513 104.809  -1.641  1.00 27.84           C  
ANISOU 3820  CB  PHE B 172     3998   2876   3704     37    438    799       C  
ATOM   3821  CG  PHE B 172      30.987 104.777  -1.357  1.00 24.78           C  
ANISOU 3821  CG  PHE B 172     3688   2478   3249     48    472    662       C  
ATOM   3822  CD1 PHE B 172      31.908 105.079  -2.342  1.00 24.27           C  
ANISOU 3822  CD1 PHE B 172     3648   2438   3132     10    450    665       C  
ATOM   3823  CD2 PHE B 172      31.451 104.440  -0.098  1.00 23.54           C  
ANISOU 3823  CD2 PHE B 172     3574   2288   3082     90    524    539       C  
ATOM   3824  CE1 PHE B 172      33.265 105.042  -2.067  1.00 24.48           C  
ANISOU 3824  CE1 PHE B 172     3736   2451   3112     21    483    549       C  
ATOM   3825  CE2 PHE B 172      32.811 104.380   0.164  1.00 23.55           C  
ANISOU 3825  CE2 PHE B 172     3634   2285   3027     92    545    431       C  
ATOM   3826  CZ  PHE B 172      33.716 104.670  -0.827  1.00 23.41           C  
ANISOU 3826  CZ  PHE B 172     3636   2287   2971     61    525    438       C  
ATOM   3827  N   LYS B 173      26.769 102.900  -1.427  1.00 32.68           N  
ANISOU 3827  N   LYS B 173     4543   3563   4309     -3    341    937       N  
ATOM   3828  CA  LYS B 173      25.292 102.826  -1.361  1.00 37.38           C  
ANISOU 3828  CA  LYS B 173     5051   4156   4993     -3    316   1065       C  
ATOM   3829  C   LYS B 173      24.769 103.797  -0.285  1.00 43.22           C  
ANISOU 3829  C   LYS B 173     5723   4787   5910     86    420   1082       C  
ATOM   3830  O   LYS B 173      25.562 104.352   0.521  1.00 38.14           O  
ANISOU 3830  O   LYS B 173     5120   4079   5292    138    508    970       O  
ATOM   3831  CB  LYS B 173      24.823 101.399  -1.054  1.00 35.48           C  
ANISOU 3831  CB  LYS B 173     4852   3963   4663    -30    279   1018       C  
ATOM   3832  CG  LYS B 173      25.332 100.308  -1.984  1.00 39.79           C  
ANISOU 3832  CG  LYS B 173     5479   4601   5038   -123    204    977       C  
ATOM   3833  CD  LYS B 173      25.216 100.633  -3.459  1.00 41.73           C  
ANISOU 3833  CD  LYS B 173     5703   4915   5237   -219    121   1098       C  
ATOM   3834  N   THR B 174      23.432 103.938  -0.240  1.00 43.19           N  
ANISOU 3834  N   THR B 174     5620   4761   6026     96    415   1218       N  
ATOM   3835  CA  THR B 174      22.717 104.870   0.641  1.00 41.49           C  
ANISOU 3835  CA  THR B 174     5325   4432   6007    174    527   1262       C  
ATOM   3836  C   THR B 174      21.635 104.148   1.467  1.00 46.31           C  
ANISOU 3836  C   THR B 174     5910   5022   6663    199    551   1270       C  
ATOM   3837  O   THR B 174      20.635 104.779   1.890  1.00 40.24           O  
ANISOU 3837  O   THR B 174     5043   4169   6076    246    623   1368       O  
ATOM   3838  CB  THR B 174      22.097 105.985  -0.211  1.00 43.84           C  
ANISOU 3838  CB  THR B 174     5494   4701   6459    169    514   1460       C  
ATOM   3839  OG1 THR B 174      21.020 105.424  -0.960  1.00 45.93           O  
ANISOU 3839  OG1 THR B 174     5683   5037   6728    112    406   1623       O  
ATOM   3840  CG2 THR B 174      23.072 106.625  -1.175  1.00 44.20           C  
ANISOU 3840  CG2 THR B 174     5559   4781   6453    133    475   1474       C  
ATOM   3841  N   PHE B 175      21.813 102.836   1.707  1.00 49.20           N  
ANISOU 3841  N   PHE B 175     6359   5456   6878    171    500   1172       N  
ATOM   3842  CA  PHE B 175      20.873 102.033   2.541  1.00 49.87           C  
ANISOU 3842  CA  PHE B 175     6432   5526   6989    194    522   1164       C  
ATOM   3843  C   PHE B 175      20.791 102.564   3.975  1.00 48.84           C  
ANISOU 3843  C   PHE B 175     6312   5285   6960    272    670   1075       C  
ATOM   3844  O   PHE B 175      19.691 102.618   4.546  1.00 49.62           O  
ANISOU 3844  O   PHE B 175     6344   5324   7183    306    728   1139       O  
ATOM   3845  CB  PHE B 175      21.307 100.573   2.681  1.00 52.28           C  
ANISOU 3845  CB  PHE B 175     6837   5911   7115    157    463   1048       C  
ATOM   3846  CG  PHE B 175      21.276  99.795   1.399  1.00 56.06           C  
ANISOU 3846  CG  PHE B 175     7326   6496   7476     65    334   1110       C  
ATOM   3847  CD1 PHE B 175      20.093  99.661   0.685  1.00 60.61           C  
ANISOU 3847  CD1 PHE B 175     7814   7111   8104     17    258   1275       C  
ATOM   3848  CD2 PHE B 175      22.431  99.212   0.903  1.00 56.93           C  
ANISOU 3848  CD2 PHE B 175     7534   6667   7429     18    295   1007       C  
ATOM   3849  CE1 PHE B 175      20.061  98.943  -0.502  1.00 60.89           C  
ANISOU 3849  CE1 PHE B 175     7871   7251   8014    -90    140   1325       C  
ATOM   3850  CE2 PHE B 175      22.397  98.505  -0.290  1.00 61.87           C  
ANISOU 3850  CE2 PHE B 175     8182   7384   7941    -80    194   1052       C  
ATOM   3851  CZ  PHE B 175      21.214  98.371  -0.988  1.00 60.38           C  
ANISOU 3851  CZ  PHE B 175     7917   7240   7784   -141    115   1207       C  
ATOM   3852  N   SER B 176      21.954 102.898   4.559  1.00 46.56           N  
ANISOU 3852  N   SER B 176     6109   4971   6609    289    731    929       N  
ATOM   3853  CA  SER B 176      22.058 103.220   5.993  1.00 46.95           C  
ANISOU 3853  CA  SER B 176     6202   4934   6700    335    864    812       C  
ATOM   3854  C   SER B 176      23.036 104.374   6.263  1.00 48.65           C  
ANISOU 3854  C   SER B 176     6452   5089   6943    347    947    733       C  
ATOM   3855  O   SER B 176      23.848 104.761   5.419  1.00 49.80           O  
ANISOU 3855  O   SER B 176     6605   5268   7048    325    895    744       O  
ATOM   3856  CB  SER B 176      22.439 102.000   6.793  1.00 46.74           C  
ANISOU 3856  CB  SER B 176     6270   4961   6529    324    844    684       C  
ATOM   3857  OG  SER B 176      23.552 101.330   6.215  1.00 42.00           O  
ANISOU 3857  OG  SER B 176     5737   4449   5771    284    750    622       O  
ATOM   3858  N   LYS B 177      22.915 104.922   7.478  1.00 53.44           N  
ANISOU 3858  N   LYS B 177     7084   5602   7618    376   1086    652       N  
ATOM   3859  CA  LYS B 177      23.713 106.061   7.935  1.00 58.49           C  
ANISOU 3859  CA  LYS B 177     7761   6168   8294    379   1190    566       C  
ATOM   3860  C   LYS B 177      25.124 105.553   8.232  1.00 51.04           C  
ANISOU 3860  C   LYS B 177     6929   5299   7163    342   1135    423       C  
ATOM   3861  O   LYS B 177      26.095 106.249   7.985  1.00 50.17           O  
ANISOU 3861  O   LYS B 177     6844   5181   7034    328   1142    380       O  
ATOM   3862  CB  LYS B 177      23.056 106.732   9.153  1.00 57.42           C  
ANISOU 3862  CB  LYS B 177     7625   5907   8284    403   1367    520       C  
ATOM   3863  N   THR B 178      25.195 104.300   8.699  1.00 43.52           N  
ANISOU 3863  N   THR B 178     6032   4419   6084    326   1076    366       N  
ATOM   3864  CA  THR B 178      26.423 103.637   9.095  1.00 43.63           C  
ANISOU 3864  CA  THR B 178     6138   4503   5935    293   1024    250       C  
ATOM   3865  C   THR B 178      26.696 102.421   8.181  1.00 44.89           C  
ANISOU 3865  C   THR B 178     6300   4766   5988    277    886    286       C  
ATOM   3866  O   THR B 178      25.802 101.869   7.497  1.00 40.18           O  
ANISOU 3866  O   THR B 178     5651   4198   5418    281    831    382       O  
ATOM   3867  CB  THR B 178      26.373 103.181  10.565  1.00 46.04           C  
ANISOU 3867  CB  THR B 178     6511   4799   6182    281   1087    147       C  
ATOM   3868  OG1 THR B 178      25.410 102.136  10.716  1.00 45.82           O  
ANISOU 3868  OG1 THR B 178     6462   4799   6148    296   1056    192       O  
ATOM   3869  CG2 THR B 178      26.020 104.286  11.538  1.00 47.24           C  
ANISOU 3869  CG2 THR B 178     6677   4843   6428    280   1242     96       C  
ATOM   3870  N   ALA B 179      27.971 102.035   8.165  1.00 37.77           N  
ANISOU 3870  N   ALA B 179     5459   3918   4972    251    838    210       N  
ATOM   3871  CA  ALA B 179      28.448 100.804   7.583  1.00 38.68           C  
ANISOU 3871  CA  ALA B 179     5597   4117   4980    230    739    209       C  
ATOM   3872  C   ALA B 179      28.439 100.833   6.042  1.00 32.41           C  
ANISOU 3872  C   ALA B 179     4766   3356   4190    214    668    294       C  
ATOM   3873  O   ALA B 179      28.684  99.812   5.445  1.00 30.29           O  
ANISOU 3873  O   ALA B 179     4517   3148   3840    188    601    296       O  
ATOM   3874  CB  ALA B 179      27.635  99.648   8.134  1.00 41.40           C  
ANISOU 3874  CB  ALA B 179     5945   4487   5297    237    725    213       C  
ATOM   3875  N   GLU B 180      28.172 101.976   5.398  1.00 32.26           N  
ANISOU 3875  N   GLU B 180     4696   3297   4262    221    689    365       N  
ATOM   3876  CA  GLU B 180      28.291 102.050   3.936  1.00 37.57           C  
ANISOU 3876  CA  GLU B 180     5342   4011   4919    190    617    446       C  
ATOM   3877  C   GLU B 180      29.758 101.971   3.481  1.00 35.35           C  
ANISOU 3877  C   GLU B 180     5118   3764   4549    165    590    377       C  
ATOM   3878  O   GLU B 180      30.039 101.471   2.397  1.00 32.86           O  
ANISOU 3878  O   GLU B 180     4813   3501   4167    124    527    407       O  
ATOM   3879  CB  GLU B 180      27.642 103.308   3.368  1.00 39.56           C  
ANISOU 3879  CB  GLU B 180     5515   4214   5302    203    643    558       C  
ATOM   3880  CG  GLU B 180      26.121 103.282   3.454  1.00 53.01           C  
ANISOU 3880  CG  GLU B 180     7139   5893   7106    219    652    667       C  
ATOM   3881  CD  GLU B 180      25.404 102.120   2.762  1.00 60.39           C  
ANISOU 3881  CD  GLU B 180     8061   6907   7975    177    554    738       C  
ATOM   3882  OE1 GLU B 180      26.032 101.424   1.906  1.00 66.93           O  
ANISOU 3882  OE1 GLU B 180     8936   7810   8681    123    476    720       O  
ATOM   3883  OE2 GLU B 180      24.207 101.926   3.049  1.00 43.92           O  
ANISOU 3883  OE2 GLU B 180     5917   4803   5965    191    562    811       O  
ATOM   3884  N   ASP B 181      30.677 102.490   4.291  1.00 31.39           N  
ANISOU 3884  N   ASP B 181     4652   3228   4046    181    642    288       N  
ATOM   3885  CA  ASP B 181      32.108 102.320   4.043  1.00 35.73           C  
ANISOU 3885  CA  ASP B 181     5249   3804   4520    161    620    222       C  
ATOM   3886  C   ASP B 181      32.534 100.852   4.243  1.00 34.26           C  
ANISOU 3886  C   ASP B 181     5107   3672   4236    144    579    172       C  
ATOM   3887  O   ASP B 181      33.384 100.344   3.514  1.00 27.75           O  
ANISOU 3887  O   ASP B 181     4308   2881   3355    119    547    158       O  
ATOM   3888  CB  ASP B 181      32.928 103.258   4.928  1.00 37.58           C  
ANISOU 3888  CB  ASP B 181     5505   3992   4782    171    681    147       C  
ATOM   3889  CG  ASP B 181      32.624 103.084   6.404  1.00 44.24           C  
ANISOU 3889  CG  ASP B 181     6372   4813   5621    180    730     83       C  
ATOM   3890  OD1 ASP B 181      31.468 102.627   6.742  1.00 48.81           O  
ANISOU 3890  OD1 ASP B 181     6933   5389   6224    195    740    116       O  
ATOM   3891  OD2 ASP B 181      33.532 103.384   7.205  1.00 48.06           O  
ANISOU 3891  OD2 ASP B 181     6895   5290   6076    163    755      5       O  
ATOM   3892  N   GLN B 182      31.960 100.160   5.237  1.00 29.16           N  
ANISOU 3892  N   GLN B 182     4469   3030   3580    158    590    148       N  
ATOM   3893  CA  GLN B 182      32.223  98.740   5.428  1.00 27.67           C  
ANISOU 3893  CA  GLN B 182     4310   2885   3317    147    557    116       C  
ATOM   3894  C   GLN B 182      31.795  97.936   4.208  1.00 24.57           C  
ANISOU 3894  C   GLN B 182     3913   2531   2892    117    510    168       C  
ATOM   3895  O   GLN B 182      32.539  97.037   3.753  1.00 24.59           O  
ANISOU 3895  O   GLN B 182     3946   2560   2836     92    491    139       O  
ATOM   3896  CB  GLN B 182      31.441  98.161   6.611  1.00 32.49           C  
ANISOU 3896  CB  GLN B 182     4922   3493   3929    165    577    100       C  
ATOM   3897  CG  GLN B 182      32.059  98.442   7.964  1.00 36.33           C  
ANISOU 3897  CG  GLN B 182     5436   3966   4402    169    614     30       C  
ATOM   3898  CD  GLN B 182      31.207  97.863   9.073  1.00 39.94           C  
ANISOU 3898  CD  GLN B 182     5899   4423   4852    179    636     19       C  
ATOM   3899  OE1 GLN B 182      30.553  98.615   9.793  1.00 41.61           O  
ANISOU 3899  OE1 GLN B 182     6108   4592   5109    188    696      9       O  
ATOM   3900  NE2 GLN B 182      31.151  96.532   9.168  1.00 35.72           N  
ANISOU 3900  NE2 GLN B 182     5370   3928   4271    178    600     22       N  
ATOM   3901  N   LEU B 183      30.605  98.239   3.681  1.00 21.31           N  
ANISOU 3901  N   LEU B 183     3460   2117   2519    111    494    247       N  
ATOM   3902  CA  LEU B 183      30.108  97.472   2.545  1.00 23.55           C  
ANISOU 3902  CA  LEU B 183     3744   2446   2756     61    442    299       C  
ATOM   3903  C   LEU B 183      31.049  97.699   1.340  1.00 23.28           C  
ANISOU 3903  C   LEU B 183     3736   2431   2675     16    424    299       C  
ATOM   3904  O   LEU B 183      31.394  96.760   0.612  1.00 22.75           O  
ANISOU 3904  O   LEU B 183     3710   2398   2535    -32    406    278       O  
ATOM   3905  CB  LEU B 183      28.652  97.863   2.228  1.00 23.38           C  
ANISOU 3905  CB  LEU B 183     3662   2425   2796     55    419    405       C  
ATOM   3906  CG  LEU B 183      28.074  97.289   0.934  1.00 24.07           C  
ANISOU 3906  CG  LEU B 183     3745   2570   2830    -18    351    479       C  
ATOM   3907  CD1 LEU B 183      28.148  95.759   0.921  1.00 26.64           C  
ANISOU 3907  CD1 LEU B 183     4122   2931   3068    -53    337    422       C  
ATOM   3908  CD2 LEU B 183      26.639  97.725   0.730  1.00 23.47           C  
ANISOU 3908  CD2 LEU B 183     3591   2495   2831    -23    322    604       C  
ATOM   3909  N   PHE B 184      31.439  98.952   1.100  1.00 21.18           N  
ANISOU 3909  N   PHE B 184     3450   2139   2456     30    439    320       N  
ATOM   3910  CA  PHE B 184      32.355  99.269  -0.022  1.00 22.98           C  
ANISOU 3910  CA  PHE B 184     3703   2383   2645    -10    427    322       C  
ATOM   3911  C   PHE B 184      33.657  98.447   0.075  1.00 19.99           C  
ANISOU 3911  C   PHE B 184     3380   2006   2207    -17    450    228       C  
ATOM   3912  O   PHE B 184      34.062  97.812  -0.901  1.00 20.14           O  
ANISOU 3912  O   PHE B 184     3438   2051   2162    -72    442    220       O  
ATOM   3913  CB  PHE B 184      32.646 100.771  -0.106  1.00 23.08           C  
ANISOU 3913  CB  PHE B 184     3681   2357   2731     15    450    352       C  
ATOM   3914  CG  PHE B 184      33.452 101.143  -1.328  1.00 22.27           C  
ANISOU 3914  CG  PHE B 184     3597   2272   2589    -29    436    369       C  
ATOM   3915  CD1 PHE B 184      34.845 101.076  -1.304  1.00 21.71           C  
ANISOU 3915  CD1 PHE B 184     3570   2189   2490    -25    465    289       C  
ATOM   3916  CD2 PHE B 184      32.832 101.508  -2.514  1.00 22.95           C  
ANISOU 3916  CD2 PHE B 184     3659   2392   2667    -82    392    472       C  
ATOM   3917  CE1 PHE B 184      35.596 101.433  -2.419  1.00 21.57           C  
ANISOU 3917  CE1 PHE B 184     3572   2180   2441    -66    463    302       C  
ATOM   3918  CE2 PHE B 184      33.588 101.850  -3.626  1.00 23.92           C  
ANISOU 3918  CE2 PHE B 184     3808   2535   2745   -131    383    486       C  
ATOM   3919  CZ  PHE B 184      34.968 101.810  -3.576  1.00 21.40           C  
ANISOU 3919  CZ  PHE B 184     3535   2194   2401   -120    424    396       C  
ATOM   3920  N   THR B 185      34.305  98.453   1.245  1.00 19.79           N  
ANISOU 3920  N   THR B 185     3358   1952   2206     30    482    164       N  
ATOM   3921  CA  THR B 185      35.542  97.702   1.442  1.00 19.53           C  
ANISOU 3921  CA  THR B 185     3359   1917   2142     29    501     98       C  
ATOM   3922  C   THR B 185      35.329  96.179   1.302  1.00 20.74           C  
ANISOU 3922  C   THR B 185     3537   2091   2248      4    499     81       C  
ATOM   3923  O   THR B 185      36.111  95.534   0.641  1.00 19.71           O  
ANISOU 3923  O   THR B 185     3438   1960   2090    -26    520     55       O  
ATOM   3924  CB  THR B 185      36.155  98.005   2.800  1.00 19.06           C  
ANISOU 3924  CB  THR B 185     3291   1835   2115     71    521     52       C  
ATOM   3925  OG1 THR B 185      36.410  99.397   2.880  1.00 22.95           O  
ANISOU 3925  OG1 THR B 185     3767   2300   2650     84    535     57       O  
ATOM   3926  CG2 THR B 185      37.446  97.274   3.073  1.00 20.89           C  
ANISOU 3926  CG2 THR B 185     3537   2065   2333     70    533      8       C  
ATOM   3927  N   ILE B 186      34.244  95.632   1.857  1.00 20.87           N  
ANISOU 3927  N   ILE B 186     3541   2121   2265     14    484     98       N  
ATOM   3928  CA  ILE B 186      33.941  94.196   1.709  1.00 21.65           C  
ANISOU 3928  CA  ILE B 186     3662   2236   2324    -12    486     84       C  
ATOM   3929  C   ILE B 186      33.780  93.840   0.219  1.00 22.55           C  
ANISOU 3929  C   ILE B 186     3811   2373   2382    -89    478    101       C  
ATOM   3930  O   ILE B 186      34.303  92.808  -0.254  1.00 21.80           O  
ANISOU 3930  O   ILE B 186     3755   2273   2252   -126    512     60       O  
ATOM   3931  CB  ILE B 186      32.672  93.814   2.495  1.00 23.02           C  
ANISOU 3931  CB  ILE B 186     3813   2421   2512      9    467    108       C  
ATOM   3932  CG1 ILE B 186      32.875  93.913   4.011  1.00 23.67           C  
ANISOU 3932  CG1 ILE B 186     3878   2486   2628     66    484     79       C  
ATOM   3933  CG2 ILE B 186      32.172  92.460   2.012  1.00 26.43           C  
ANISOU 3933  CG2 ILE B 186     4268   2873   2900    -35    464    105       C  
ATOM   3934  CD1 ILE B 186      33.703  92.845   4.631  1.00 24.70           C  
ANISOU 3934  CD1 ILE B 186     4020   2614   2749     77    503     38       C  
ATOM   3935  N   GLU B 187      33.025  94.651  -0.524  1.00 21.71           N  
ANISOU 3935  N   GLU B 187     3689   2291   2267   -121    439    166       N  
ATOM   3936  CA  GLU B 187      32.775  94.342  -1.911  1.00 25.05           C  
ANISOU 3936  CA  GLU B 187     4149   2750   2619   -214    420    192       C  
ATOM   3937  C   GLU B 187      34.128  94.365  -2.652  1.00 23.08           C  
ANISOU 3937  C   GLU B 187     3946   2482   2339   -244    467    141       C  
ATOM   3938  O   GLU B 187      34.387  93.561  -3.517  1.00 24.04           O  
ANISOU 3938  O   GLU B 187     4124   2613   2397   -319    495    109       O  
ATOM   3939  CB  GLU B 187      31.751  95.307  -2.527  1.00 28.65           C  
ANISOU 3939  CB  GLU B 187     4563   3239   3081   -246    359    295       C  
ATOM   3940  CG  GLU B 187      30.334  95.073  -2.036  1.00 32.19           C  
ANISOU 3940  CG  GLU B 187     4966   3705   3559   -235    319    356       C  
ATOM   3941  CD  GLU B 187      29.201  95.896  -2.641  1.00 36.41           C  
ANISOU 3941  CD  GLU B 187     5441   4271   4119   -270    256    483       C  
ATOM   3942  OE1 GLU B 187      29.434  97.052  -3.029  1.00 33.55           O  
ANISOU 3942  OE1 GLU B 187     5050   3902   3795   -262    249    534       O  
ATOM   3943  OE2 GLU B 187      28.055  95.381  -2.667  1.00 47.63           O  
ANISOU 3943  OE2 GLU B 187     6838   5723   5537   -302    214    540       O  
ATOM   3944  N   PHE B 188      35.011  95.286  -2.269  1.00 22.82           N  
ANISOU 3944  N   PHE B 188     3892   2418   2358   -188    485    128       N  
ATOM   3945  CA  PHE B 188      36.314  95.371  -2.888  1.00 22.97           C  
ANISOU 3945  CA  PHE B 188     3946   2414   2366   -207    532     86       C  
ATOM   3946  C   PHE B 188      37.126  94.110  -2.535  1.00 21.01           C  
ANISOU 3946  C   PHE B 188     3724   2132   2125   -199    594     16       C  
ATOM   3947  O   PHE B 188      37.751  93.526  -3.391  1.00 19.73           O  
ANISOU 3947  O   PHE B 188     3610   1954   1929   -253    648    -18       O  
ATOM   3948  CB  PHE B 188      36.993  96.686  -2.496  1.00 23.06           C  
ANISOU 3948  CB  PHE B 188     3921   2400   2438   -150    531     95       C  
ATOM   3949  CG  PHE B 188      38.259  96.937  -3.260  1.00 20.83           C  
ANISOU 3949  CG  PHE B 188     3668   2096   2149   -173    574     67       C  
ATOM   3950  CD1 PHE B 188      39.454  96.342  -2.874  1.00 21.19           C  
ANISOU 3950  CD1 PHE B 188     3722   2101   2226   -148    629      9       C  
ATOM   3951  CD2 PHE B 188      38.234  97.739  -4.391  1.00 22.88           C  
ANISOU 3951  CD2 PHE B 188     3942   2374   2376   -224    561    109       C  
ATOM   3952  CE1 PHE B 188      40.609  96.516  -3.631  1.00 20.73           C  
ANISOU 3952  CE1 PHE B 188     3689   2015   2172   -171    680    -13       C  
ATOM   3953  CE2 PHE B 188      39.395  97.948  -5.112  1.00 22.49           C  
ANISOU 3953  CE2 PHE B 188     3923   2302   2320   -247    608     81       C  
ATOM   3954  CZ  PHE B 188      40.575  97.336  -4.739  1.00 21.47           C  
ANISOU 3954  CZ  PHE B 188     3804   2126   2226   -219    671     17       C  
ATOM   3955  N   LEU B 189      37.156  93.741  -1.259  1.00 20.16           N  
ANISOU 3955  N   LEU B 189     3581   2008   2068   -132    594      1       N  
ATOM   3956  CA  LEU B 189      37.945  92.583  -0.769  1.00 22.17           C  
ANISOU 3956  CA  LEU B 189     3840   2227   2354   -113    650    -43       C  
ATOM   3957  C   LEU B 189      37.498  91.301  -1.480  1.00 22.42           C  
ANISOU 3957  C   LEU B 189     3919   2259   2340   -178    688    -66       C  
ATOM   3958  O   LEU B 189      38.306  90.458  -1.832  1.00 22.99           O  
ANISOU 3958  O   LEU B 189     4015   2288   2429   -199    765   -106       O  
ATOM   3959  CB  LEU B 189      37.735  92.404   0.735  1.00 18.63           C  
ANISOU 3959  CB  LEU B 189     3345   1780   1950    -46    624    -36       C  
ATOM   3960  CG  LEU B 189      38.471  93.354   1.672  1.00 17.66           C  
ANISOU 3960  CG  LEU B 189     3185   1650   1874      5    606    -32       C  
ATOM   3961  CD1 LEU B 189      37.887  93.230   3.094  1.00 16.30           C  
ANISOU 3961  CD1 LEU B 189     2983   1494   1716     46    575    -23       C  
ATOM   3962  CD2 LEU B 189      39.969  93.086   1.716  1.00 17.87           C  
ANISOU 3962  CD2 LEU B 189     3200   1641   1948     15    649    -48       C  
ATOM   3963  N   MET B 190      36.195  91.203  -1.743  1.00 23.69           N  
ANISOU 3963  N   MET B 190     4090   2462   2448   -217    641    -38       N  
ATOM   3964  CA  MET B 190      35.616  90.010  -2.319  1.00 22.24           C  
ANISOU 3964  CA  MET B 190     3951   2284   2212   -289    668    -61       C  
ATOM   3965  C   MET B 190      35.857  89.964  -3.830  1.00 22.58           C  
ANISOU 3965  C   MET B 190     4065   2335   2178   -397    704    -82       C  
ATOM   3966  O   MET B 190      35.521  88.981  -4.453  1.00 20.95           O  
ANISOU 3966  O   MET B 190     3913   2130   1917   -480    743   -114       O  
ATOM   3967  CB  MET B 190      34.116  89.939  -2.027  1.00 22.24           C  
ANISOU 3967  CB  MET B 190     3931   2332   2186   -298    597    -14       C  
ATOM   3968  CG  MET B 190      33.835  89.753  -0.541  1.00 19.79           C  
ANISOU 3968  CG  MET B 190     3565   2010   1942   -205    580     -6       C  
ATOM   3969  SD  MET B 190      34.522  88.199   0.075  1.00 22.11           S  
ANISOU 3969  SD  MET B 190     3866   2255   2280   -181    660    -61       S  
ATOM   3970  CE  MET B 190      35.847  88.709   1.166  1.00 19.34           C  
ANISOU 3970  CE  MET B 190     3465   1871   2010    -91    674    -62       C  
ATOM   3971  N   ASN B 191      36.378  91.052  -4.405  1.00 22.34           N  
ANISOU 3971  N   ASN B 191     4038   2313   2136   -406    691    -62       N  
ATOM   3972  CA  ASN B 191      36.671  91.101  -5.819  1.00 22.66           C  
ANISOU 3972  CA  ASN B 191     4150   2364   2096   -514    725    -79       C  
ATOM   3973  C   ASN B 191      38.176  91.268  -6.057  1.00 24.12           C  
ANISOU 3973  C   ASN B 191     4349   2488   2326   -492    812   -125       C  
ATOM   3974  O   ASN B 191      38.581  91.565  -7.187  1.00 23.94           O  
ANISOU 3974  O   ASN B 191     4382   2469   2243   -572    846   -137       O  
ATOM   3975  CB  ASN B 191      35.877  92.215  -6.504  1.00 25.70           C  
ANISOU 3975  CB  ASN B 191     4525   2818   2419   -564    633      1       C  
ATOM   3976  CG  ASN B 191      34.425  91.855  -6.707  1.00 26.71           C  
ANISOU 3976  CG  ASN B 191     4654   3008   2486   -630    561     52       C  
ATOM   3977  OD1 ASN B 191      34.102  91.027  -7.544  1.00 27.40           O  
ANISOU 3977  OD1 ASN B 191     4809   3119   2482   -747    582     27       O  
ATOM   3978  ND2 ASN B 191      33.556  92.436  -5.897  1.00 29.34           N  
ANISOU 3978  ND2 ASN B 191     4910   3362   2874   -559    485    122       N  
ATOM   3979  N   SER B 192      39.006  91.075  -5.023  1.00 22.04           N  
ANISOU 3979  N   SER B 192     4036   2171   2167   -394    848   -144       N  
ATOM   3980  CA  SER B 192      40.459  91.219  -5.176  1.00 24.64           C  
ANISOU 3980  CA  SER B 192     4364   2439   2559   -368    927   -174       C  
ATOM   3981  C   SER B 192      41.189  90.213  -4.278  1.00 24.39           C  
ANISOU 3981  C   SER B 192     4294   2343   2631   -305    995   -199       C  
ATOM   3982  O   SER B 192      40.610  89.711  -3.335  1.00 25.54           O  
ANISOU 3982  O   SER B 192     4402   2500   2800   -262    959   -184       O  
ATOM   3983  CB  SER B 192      40.875  92.649  -4.852  1.00 24.80           C  
ANISOU 3983  CB  SER B 192     4335   2474   2614   -308    867   -133       C  
ATOM   3984  OG  SER B 192      40.554  92.967  -3.498  1.00 26.73           O  
ANISOU 3984  OG  SER B 192     4510   2731   2912   -221    801   -103       O  
ATOM   3985  N   LYS B 193      42.471  89.947  -4.554  1.00 23.46           N  
ANISOU 3985  N   LYS B 193     4175   2153   2583   -298   1094   -225       N  
ATOM   3986  CA  LYS B 193      43.171  88.916  -3.794  1.00 26.58           C  
ANISOU 3986  CA  LYS B 193     4523   2482   3092   -245   1166   -229       C  
ATOM   3987  C   LYS B 193      44.390  89.459  -3.060  1.00 23.28           C  
ANISOU 3987  C   LYS B 193     4026   2033   2785   -166   1160   -191       C  
ATOM   3988  O   LYS B 193      44.789  88.863  -2.069  1.00 22.53           O  
ANISOU 3988  O   LYS B 193     3864   1912   2784   -108   1166   -160       O  
ATOM   3989  CB  LYS B 193      43.596  87.750  -4.699  1.00 32.18           C  
ANISOU 3989  CB  LYS B 193     5292   3114   3821   -313   1318   -288       C  
ATOM   3990  CG  LYS B 193      44.323  88.149  -5.969  1.00 37.82           C  
ANISOU 3990  CG  LYS B 193     6071   3794   4506   -382   1404   -327       C  
ATOM   3991  CD  LYS B 193      44.985  86.965  -6.687  1.00 46.30           C  
ANISOU 3991  CD  LYS B 193     7193   4762   5633   -439   1588   -389       C  
ATOM   3992  CE  LYS B 193      45.189  87.216  -8.166  1.00 49.21           C  
ANISOU 3992  CE  LYS B 193     7670   5120   5907   -555   1672   -448       C  
ATOM   3993  NZ  LYS B 193      46.378  88.050  -8.455  1.00 49.25           N  
ANISOU 3993  NZ  LYS B 193     7651   5086   5973   -523   1708   -433       N  
ATOM   3994  N   ASN B 194      44.958  90.586  -3.521  1.00 21.26           N  
ANISOU 3994  N   ASN B 194     3774   1784   2516   -169   1143   -184       N  
ATOM   3995  CA  ASN B 194      46.240  91.037  -3.016  1.00 21.62           C  
ANISOU 3995  CA  ASN B 194     3752   1793   2669   -112   1153   -152       C  
ATOM   3996  C   ASN B 194      46.064  92.298  -2.147  1.00 20.72           C  
ANISOU 3996  C   ASN B 194     3592   1741   2537    -65   1027   -114       C  
ATOM   3997  O   ASN B 194      45.719  93.384  -2.644  1.00 20.46           O  
ANISOU 3997  O   ASN B 194     3589   1745   2437    -85    981   -117       O  
ATOM   3998  CB  ASN B 194      47.207  91.299  -4.165  1.00 22.47           C  
ANISOU 3998  CB  ASN B 194     3895   1844   2797   -150   1250   -178       C  
ATOM   3999  CG  ASN B 194      47.695  90.046  -4.848  1.00 25.77           C  
ANISOU 3999  CG  ASN B 194     4346   2174   3270   -190   1405   -217       C  
ATOM   4000  OD1 ASN B 194      47.440  88.930  -4.394  1.00 24.83           O  
ANISOU 4000  OD1 ASN B 194     4210   2027   3196   -179   1445   -219       O  
ATOM   4001  ND2 ASN B 194      48.402  90.228  -5.949  1.00 25.77           N  
ANISOU 4001  ND2 ASN B 194     4395   2123   3272   -238   1506   -251       N  
ATOM   4002  N   TYR B 195      46.352  92.151  -0.851  1.00 20.16           N  
ANISOU 4002  N   TYR B 195     3449   1678   2531    -10    980    -74       N  
ATOM   4003  CA  TYR B 195      46.201  93.197   0.120  1.00 20.14           C  
ANISOU 4003  CA  TYR B 195     3410   1728   2511     21    877    -48       C  
ATOM   4004  C   TYR B 195      47.547  93.370   0.837  1.00 20.96           C  
ANISOU 4004  C   TYR B 195     3439   1808   2715     51    873     -5       C  
ATOM   4005  O   TYR B 195      48.207  92.386   1.128  1.00 21.95           O  
ANISOU 4005  O   TYR B 195     3517   1892   2927     65    920     26       O  
ATOM   4006  CB  TYR B 195      45.131  92.828   1.160  1.00 19.50           C  
ANISOU 4006  CB  TYR B 195     3319   1696   2393     38    812    -38       C  
ATOM   4007  CG  TYR B 195      43.969  92.020   0.636  1.00 19.92           C  
ANISOU 4007  CG  TYR B 195     3423   1758   2386     10    833    -64       C  
ATOM   4008  CD1 TYR B 195      43.218  92.453  -0.445  1.00 18.43           C  
ANISOU 4008  CD1 TYR B 195     3296   1588   2118    -34    834    -89       C  
ATOM   4009  CD2 TYR B 195      43.585  90.842   1.262  1.00 20.03           C  
ANISOU 4009  CD2 TYR B 195     3420   1768   2423     23    845    -54       C  
ATOM   4010  CE1 TYR B 195      42.152  91.696  -0.921  1.00 18.85           C  
ANISOU 4010  CE1 TYR B 195     3393   1656   2111    -74    845   -106       C  
ATOM   4011  CE2 TYR B 195      42.496  90.094   0.822  1.00 18.55           C  
ANISOU 4011  CE2 TYR B 195     3277   1590   2180     -7    862    -79       C  
ATOM   4012  CZ  TYR B 195      41.776  90.524  -0.276  1.00 19.17           C  
ANISOU 4012  CZ  TYR B 195     3420   1689   2175    -60    859   -106       C  
ATOM   4013  OH  TYR B 195      40.708  89.783  -0.697  1.00 20.63           O  
ANISOU 4013  OH  TYR B 195     3647   1890   2301   -103    867   -124       O  
ATOM   4014  N   SER B 196      47.905  94.606   1.164  1.00 18.77           N  
ANISOU 4014  N   SER B 196     3146   1556   2430     57    815      3       N  
ATOM   4015  CA  SER B 196      49.144  94.927   1.855  1.00 19.90           C  
ANISOU 4015  CA  SER B 196     3218   1688   2653     71    794     48       C  
ATOM   4016  C   SER B 196      48.838  95.862   3.016  1.00 19.55           C  
ANISOU 4016  C   SER B 196     3161   1705   2562     69    695     53       C  
ATOM   4017  O   SER B 196      47.922  96.673   2.935  1.00 19.97           O  
ANISOU 4017  O   SER B 196     3260   1786   2539     63    666     16       O  
ATOM   4018  CB  SER B 196      50.134  95.587   0.919  1.00 23.04           C  
ANISOU 4018  CB  SER B 196     3617   2041   3095     62    844     42       C  
ATOM   4019  OG  SER B 196      50.416  94.728  -0.171  1.00 26.93           O  
ANISOU 4019  OG  SER B 196     4134   2470   3626     52    953     27       O  
ATOM   4020  N   ILE B 197      49.661  95.763   4.056  1.00 19.87           N  
ANISOU 4020  N   ILE B 197     3135   1760   2653     67    652    106       N  
ATOM   4021  CA  ILE B 197      49.540  96.566   5.261  1.00 20.63           C  
ANISOU 4021  CA  ILE B 197     3221   1914   2700     45    566    109       C  
ATOM   4022  C   ILE B 197      50.918  97.145   5.529  1.00 20.70           C  
ANISOU 4022  C   ILE B 197     3174   1917   2773     25    542    151       C  
ATOM   4023  O   ILE B 197      51.865  96.411   5.516  1.00 19.90           O  
ANISOU 4023  O   ILE B 197     3006   1788   2765     32    561    216       O  
ATOM   4024  CB  ILE B 197      49.045  95.721   6.457  1.00 21.04           C  
ANISOU 4024  CB  ILE B 197     3252   2012   2729     40    520    142       C  
ATOM   4025  CG1 ILE B 197      47.676  95.094   6.185  1.00 20.65           C  
ANISOU 4025  CG1 ILE B 197     3254   1965   2626     61    545    104       C  
ATOM   4026  CG2 ILE B 197      49.049  96.545   7.746  1.00 21.42           C  
ANISOU 4026  CG2 ILE B 197     3298   2121   2718     -2    439    142       C  
ATOM   4027  CD1 ILE B 197      47.369  93.944   7.123  1.00 20.80           C  
ANISOU 4027  CD1 ILE B 197     3242   2011   2650     65    523    147       C  
ATOM   4028  N   LYS B 198      50.991  98.465   5.727  1.00 21.21           N  
ANISOU 4028  N   LYS B 198     3261   2001   2795     -1    507    117       N  
ATOM   4029  CA  LYS B 198      52.241  99.183   5.999  1.00 24.36           C  
ANISOU 4029  CA  LYS B 198     3612   2399   3242    -31    477    150       C  
ATOM   4030  C   LYS B 198      52.105  99.898   7.347  1.00 23.68           C  
ANISOU 4030  C   LYS B 198     3533   2377   3084    -90    396    140       C  
ATOM   4031  O   LYS B 198      51.099 100.572   7.581  1.00 23.48           O  
ANISOU 4031  O   LYS B 198     3573   2368   2979    -99    395     73       O  
ATOM   4032  CB  LYS B 198      52.504 100.123   4.820  1.00 27.38           C  
ANISOU 4032  CB  LYS B 198     4024   2733   3643    -18    528    109       C  
ATOM   4033  CG  LYS B 198      53.906 100.715   4.720  1.00 35.86           C  
ANISOU 4033  CG  LYS B 198     5044   3786   4794    -37    522    146       C  
ATOM   4034  CD  LYS B 198      54.921  99.837   4.058  1.00 37.13           C  
ANISOU 4034  CD  LYS B 198     5144   3892   5072    -11    578    208       C  
ATOM   4035  CE  LYS B 198      56.036 100.598   3.380  1.00 40.09           C  
ANISOU 4035  CE  LYS B 198     5490   4222   5519    -14    609    221       C  
ATOM   4036  NZ  LYS B 198      56.957 101.206   4.364  1.00 43.01           N  
ANISOU 4036  NZ  LYS B 198     5798   4627   5916    -62    527    270       N  
ATOM   4037  N   THR B 199      53.120  99.788   8.212  1.00 23.52           N  
ANISOU 4037  N   THR B 199     3448   2390   3095   -138    334    209       N  
ATOM   4038  CA  THR B 199      53.049 100.267   9.618  1.00 23.12           C  
ANISOU 4038  CA  THR B 199     3409   2414   2961   -219    252    207       C  
ATOM   4039  C   THR B 199      54.276 101.096  10.026  1.00 24.18           C  
ANISOU 4039  C   THR B 199     3501   2567   3116   -290    199    240       C  
ATOM   4040  O   THR B 199      54.461 101.380  11.205  1.00 23.83           O  
ANISOU 4040  O   THR B 199     3456   2591   3004   -378    125    255       O  
ATOM   4041  CB  THR B 199      52.915  99.071  10.578  1.00 24.12           C  
ANISOU 4041  CB  THR B 199     3494   2593   3076   -236    202    281       C  
ATOM   4042  OG1 THR B 199      54.081  98.239  10.479  1.00 25.70           O  
ANISOU 4042  OG1 THR B 199     3589   2780   3394   -227    186    398       O  
ATOM   4043  CG2 THR B 199      51.673  98.274  10.278  1.00 24.11           C  
ANISOU 4043  CG2 THR B 199     3535   2576   3048   -176    250    246       C  
ATOM   4044  N   ASP B 200      55.086 101.547   9.063  1.00 24.07           N  
ANISOU 4044  N   ASP B 200     3460   2499   3187   -261    238    247       N  
ATOM   4045  CA  ASP B 200      56.335 102.243   9.389  1.00 26.14           C  
ANISOU 4045  CA  ASP B 200     3669   2775   3486   -326    186    291       C  
ATOM   4046  C   ASP B 200      56.066 103.638   9.968  1.00 25.02           C  
ANISOU 4046  C   ASP B 200     3598   2661   3245   -402    164    203       C  
ATOM   4047  O   ASP B 200      56.858 104.141  10.758  1.00 24.55           O  
ANISOU 4047  O   ASP B 200     3513   2647   3166   -496     94    232       O  
ATOM   4048  CB  ASP B 200      57.256 102.300   8.173  1.00 28.87           C  
ANISOU 4048  CB  ASP B 200     3966   3046   3957   -271    246    323       C  
ATOM   4049  CG  ASP B 200      57.804 100.929   7.781  1.00 33.32           C  
ANISOU 4049  CG  ASP B 200     4444   3575   4641   -218    276    423       C  
ATOM   4050  OD1 ASP B 200      57.966 100.065   8.666  1.00 32.39           O  
ANISOU 4050  OD1 ASP B 200     4267   3502   4536   -244    218    509       O  
ATOM   4051  OD2 ASP B 200      58.106 100.759   6.600  1.00 43.95           O  
ANISOU 4051  OD2 ASP B 200     5783   4845   6072   -156    364    419       O  
ATOM   4052  N   TYR B 201      54.966 104.262   9.554  1.00 23.30           N  
ANISOU 4052  N   TYR B 201     3466   2411   2973   -368    227    100       N  
ATOM   4053  CA  TYR B 201      54.542 105.541  10.118  1.00 25.72           C  
ANISOU 4053  CA  TYR B 201     3845   2726   3199   -434    232      8       C  
ATOM   4054  C   TYR B 201      53.048 105.526  10.432  1.00 25.02           C  
ANISOU 4054  C   TYR B 201     3834   2641   3032   -416    272    -63       C  
ATOM   4055  O   TYR B 201      52.314 104.670   9.950  1.00 24.02           O  
ANISOU 4055  O   TYR B 201     3708   2501   2917   -342    299    -50       O  
ATOM   4056  CB  TYR B 201      54.780 106.674   9.110  1.00 25.96           C  
ANISOU 4056  CB  TYR B 201     3891   2688   3281   -403    294    -39       C  
ATOM   4057  CG  TYR B 201      56.218 106.900   8.740  1.00 27.67           C  
ANISOU 4057  CG  TYR B 201     4039   2892   3582   -420    269     19       C  
ATOM   4058  CD1 TYR B 201      57.056 107.645   9.555  1.00 30.23           C  
ANISOU 4058  CD1 TYR B 201     4349   3250   3884   -525    212     22       C  
ATOM   4059  CD2 TYR B 201      56.745 106.380   7.566  1.00 30.46           C  
ANISOU 4059  CD2 TYR B 201     4341   3194   4035   -340    308     72       C  
ATOM   4060  CE1 TYR B 201      58.388 107.854   9.224  1.00 31.40           C  
ANISOU 4060  CE1 TYR B 201     4425   3386   4118   -543    185     86       C  
ATOM   4061  CE2 TYR B 201      58.072 106.579   7.223  1.00 32.20           C  
ANISOU 4061  CE2 TYR B 201     4493   3395   4347   -353    295    131       C  
ATOM   4062  CZ  TYR B 201      58.895 107.332   8.045  1.00 33.75           C  
ANISOU 4062  CZ  TYR B 201     4666   3627   4530   -450    230    142       C  
ATOM   4063  OH  TYR B 201      60.204 107.534   7.705  1.00 36.20           O  
ANISOU 4063  OH  TYR B 201     4900   3915   4937   -463    215    209       O  
ATOM   4064  N   GLU B 202      52.597 106.543  11.174  1.00 25.72           N  
ANISOU 4064  N   GLU B 202     3989   2736   3048   -487    287   -144       N  
ATOM   4065  CA  GLU B 202      51.183 106.873  11.195  1.00 25.65           C  
ANISOU 4065  CA  GLU B 202     4049   2695   2999   -456    357   -221       C  
ATOM   4066  C   GLU B 202      50.868 107.642   9.907  1.00 23.96           C  
ANISOU 4066  C   GLU B 202     3842   2401   2858   -377    434   -250       C  
ATOM   4067  O   GLU B 202      51.046 108.850   9.824  1.00 22.90           O  
ANISOU 4067  O   GLU B 202     3730   2227   2741   -407    474   -301       O  
ATOM   4068  CB  GLU B 202      50.828 107.676  12.437  1.00 27.88           C  
ANISOU 4068  CB  GLU B 202     4401   2999   3191   -564    369   -299       C  
ATOM   4069  CG  GLU B 202      50.955 106.878  13.716  1.00 33.41           C  
ANISOU 4069  CG  GLU B 202     5105   3788   3800   -650    293   -267       C  
ATOM   4070  CD  GLU B 202      50.591 107.659  14.975  1.00 35.94           C  
ANISOU 4070  CD  GLU B 202     5510   4132   4012   -777    315   -355       C  
ATOM   4071  OE1 GLU B 202      50.609 108.900  14.945  1.00 40.16           O  
ANISOU 4071  OE1 GLU B 202     6091   4615   4551   -819    380   -436       O  
ATOM   4072  OE2 GLU B 202      50.296 107.021  15.970  1.00 39.04           O  
ANISOU 4072  OE2 GLU B 202     5925   4590   4316   -839    275   -343       O  
ATOM   4073  N   TYR B 203      50.453 106.909   8.890  1.00 21.59           N  
ANISOU 4073  N   TYR B 203     3521   2081   2602   -285    452   -212       N  
ATOM   4074  CA  TYR B 203      50.337 107.424   7.541  1.00 22.55           C  
ANISOU 4074  CA  TYR B 203     3637   2142   2789   -219    507   -212       C  
ATOM   4075  C   TYR B 203      49.108 108.328   7.405  1.00 22.66           C  
ANISOU 4075  C   TYR B 203     3697   2112   2801   -200    574   -265       C  
ATOM   4076  O   TYR B 203      49.059 109.210   6.551  1.00 21.71           O  
ANISOU 4076  O   TYR B 203     3575   1941   2733   -172    620   -272       O  
ATOM   4077  CB  TYR B 203      50.279 106.239   6.575  1.00 24.24           C  
ANISOU 4077  CB  TYR B 203     3822   2356   3031   -150    505   -156       C  
ATOM   4078  CG  TYR B 203      51.598 105.561   6.325  1.00 25.06           C  
ANISOU 4078  CG  TYR B 203     3869   2469   3184   -152    473    -96       C  
ATOM   4079  CD1 TYR B 203      52.579 106.241   5.640  1.00 27.09           C  
ANISOU 4079  CD1 TYR B 203     4101   2691   3501   -153    489    -86       C  
ATOM   4080  CD2 TYR B 203      51.876 104.250   6.734  1.00 28.56           C  
ANISOU 4080  CD2 TYR B 203     4274   2946   3629   -150    435    -42       C  
ATOM   4081  CE1 TYR B 203      53.804 105.665   5.360  1.00 30.22           C  
ANISOU 4081  CE1 TYR B 203     4437   3082   3961   -151    473    -25       C  
ATOM   4082  CE2 TYR B 203      53.114 103.665   6.474  1.00 28.58           C  
ANISOU 4082  CE2 TYR B 203     4211   2942   3705   -148    421     25       C  
ATOM   4083  CZ  TYR B 203      54.075 104.379   5.773  1.00 30.47           C  
ANISOU 4083  CZ  TYR B 203     4427   3142   4008   -148    442     32       C  
ATOM   4084  OH  TYR B 203      55.318 103.917   5.435  1.00 38.64           O  
ANISOU 4084  OH  TYR B 203     5391   4155   5132   -142    443    101       O  
ATOM   4085  N   TYR B 204      48.101 108.067   8.248  1.00 25.09           N  
ANISOU 4085  N   TYR B 204     4039   2437   3057   -213    583   -294       N  
ATOM   4086  CA  TYR B 204      46.792 108.714   8.225  1.00 27.77           C  
ANISOU 4086  CA  TYR B 204     4411   2731   3409   -190    653   -330       C  
ATOM   4087  C   TYR B 204      46.419 109.063   9.668  1.00 29.99           C  
ANISOU 4087  C   TYR B 204     4740   3021   3631   -265    675   -396       C  
ATOM   4088  O   TYR B 204      46.398 108.153  10.503  1.00 29.30           O  
ANISOU 4088  O   TYR B 204     4662   2993   3475   -297    627   -389       O  
ATOM   4089  CB  TYR B 204      45.789 107.734   7.612  1.00 27.62           C  
ANISOU 4089  CB  TYR B 204     4381   2722   3389   -121    648   -286       C  
ATOM   4090  CG  TYR B 204      44.433 108.323   7.382  1.00 27.73           C  
ANISOU 4090  CG  TYR B 204     4407   2688   3438    -86    713   -293       C  
ATOM   4091  CD1 TYR B 204      43.625 108.656   8.453  1.00 27.26           C  
ANISOU 4091  CD1 TYR B 204     4383   2613   3361   -116    759   -342       C  
ATOM   4092  CD2 TYR B 204      43.975 108.605   6.095  1.00 30.25           C  
ANISOU 4092  CD2 TYR B 204     4701   2975   3815    -31    734   -245       C  
ATOM   4093  CE1 TYR B 204      42.380 109.231   8.252  1.00 30.83           C  
ANISOU 4093  CE1 TYR B 204     4833   3008   3870    -80    831   -338       C  
ATOM   4094  CE2 TYR B 204      42.730 109.186   5.880  1.00 30.83           C  
ANISOU 4094  CE2 TYR B 204     4770   3004   3940     -2    790   -229       C  
ATOM   4095  CZ  TYR B 204      41.920 109.497   6.966  1.00 33.79           C  
ANISOU 4095  CZ  TYR B 204     5168   3352   4315    -20    842   -273       C  
ATOM   4096  OH  TYR B 204      40.699 110.122   6.795  1.00 37.15           O  
ANISOU 4096  OH  TYR B 204     5578   3720   4817     11    911   -249       O  
ATOM   4097  N   ILE B 205      46.168 110.345   9.960  1.00 28.54           N  
ANISOU 4097  N   ILE B 205     4589   2780   3475   -299    753   -458       N  
ATOM   4098  CA  ILE B 205      45.723 110.789  11.293  1.00 33.17           C  
ANISOU 4098  CA  ILE B 205     5237   3359   4005   -382    803   -536       C  
ATOM   4099  C   ILE B 205      44.219 111.113  11.283  1.00 32.90           C  
ANISOU 4099  C   ILE B 205     5220   3259   4018   -334    901   -556       C  
ATOM   4100  O   ILE B 205      43.757 112.011  10.588  1.00 26.96           O  
ANISOU 4100  O   ILE B 205     4451   2428   3363   -288    977   -552       O  
ATOM   4101  CB  ILE B 205      46.539 111.984  11.797  1.00 35.95           C  
ANISOU 4101  CB  ILE B 205     5621   3683   4352   -475    839   -605       C  
ATOM   4102  CG1 ILE B 205      48.036 111.759  11.595  1.00 41.66           C  
ANISOU 4102  CG1 ILE B 205     6307   4462   5058   -510    742   -566       C  
ATOM   4103  CG2 ILE B 205      46.193 112.304  13.241  1.00 36.98           C  
ANISOU 4103  CG2 ILE B 205     5829   3820   4400   -587    888   -694       C  
ATOM   4104  CD1 ILE B 205      48.648 110.833  12.605  1.00 44.12           C  
ANISOU 4104  CD1 ILE B 205     6624   4871   5267   -591    645   -546       C  
ATOM   4105  N   VAL B 206      43.459 110.340  12.063  1.00 36.76           N  
ANISOU 4105  N   VAL B 206     5736   3781   4447   -345    897   -564       N  
ATOM   4106  CA  VAL B 206      42.056 110.616  12.320  1.00 37.66           C  
ANISOU 4106  CA  VAL B 206     5870   3833   4603   -317    996   -587       C  
ATOM   4107  C   VAL B 206      42.000 111.697  13.402  1.00 39.39           C  
ANISOU 4107  C   VAL B 206     6159   3998   4807   -415   1103   -692       C  
ATOM   4108  O   VAL B 206      42.474 111.497  14.527  1.00 42.44           O  
ANISOU 4108  O   VAL B 206     6602   4438   5081   -520   1079   -748       O  
ATOM   4109  CB  VAL B 206      41.282 109.360  12.755  1.00 38.15           C  
ANISOU 4109  CB  VAL B 206     5937   3949   4609   -295    957   -559       C  
ATOM   4110  CG1 VAL B 206      39.838 109.691  13.121  1.00 42.66           C  
ANISOU 4110  CG1 VAL B 206     6526   4449   5231   -272   1068   -582       C  
ATOM   4111  CG2 VAL B 206      41.323 108.272  11.701  1.00 40.58           C  
ANISOU 4111  CG2 VAL B 206     6184   4303   4929   -211    866   -466       C  
ATOM   4112  N   VAL B 207      41.407 112.838  13.060  1.00 37.30           N  
ANISOU 4112  N   VAL B 207     5890   3625   4656   -387   1226   -715       N  
ATOM   4113  CA  VAL B 207      41.341 113.959  13.966  1.00 43.10           C  
ANISOU 4113  CA  VAL B 207     6692   4286   5398   -479   1356   -822       C  
ATOM   4114  C   VAL B 207      39.955 113.991  14.624  1.00 47.21           C  
ANISOU 4114  C   VAL B 207     7244   4742   5952   -472   1478   -855       C  
ATOM   4115  O   VAL B 207      38.937 114.039  13.928  1.00 45.09           O  
ANISOU 4115  O   VAL B 207     6917   4412   5804   -370   1527   -788       O  
ATOM   4116  CB  VAL B 207      41.611 115.277  13.227  1.00 45.69           C  
ANISOU 4116  CB  VAL B 207     6991   4516   5851   -457   1437   -828       C  
ATOM   4117  CG1 VAL B 207      41.465 116.479  14.149  1.00 46.94           C  
ANISOU 4117  CG1 VAL B 207     7222   4577   6033   -555   1599   -948       C  
ATOM   4118  CG2 VAL B 207      42.969 115.251  12.557  1.00 45.86           C  
ANISOU 4118  CG2 VAL B 207     6980   4597   5847   -462   1324   -794       C  
ATOM   4119  N   ASN B 208      39.928 113.926  15.960  1.00 51.83           N  
ANISOU 4119  N   ASN B 208     7919   5346   6427   -587   1522   -950       N  
ATOM   4120  CA  ASN B 208      38.685 114.050  16.730  1.00 54.45           C  
ANISOU 4120  CA  ASN B 208     8296   5606   6787   -599   1662  -1000       C  
ATOM   4121  C   ASN B 208      38.446 115.545  16.994  1.00 55.10           C  
ANISOU 4121  C   ASN B 208     8417   5545   6972   -648   1858  -1092       C  
ATOM   4122  O   ASN B 208      39.109 116.148  17.830  1.00 60.28           O  
ANISOU 4122  O   ASN B 208     9161   6197   7545   -783   1909  -1202       O  
ATOM   4123  CB  ASN B 208      38.709 113.197  18.001  1.00 54.13           C  
ANISOU 4123  CB  ASN B 208     8334   5656   6573   -702   1621  -1053       C  
ATOM   4124  CG  ASN B 208      38.734 111.712  17.693  1.00 55.70           C  
ANISOU 4124  CG  ASN B 208     8481   5972   6709   -635   1456   -952       C  
ATOM   4125  OD1 ASN B 208      37.948 111.227  16.880  1.00 52.11           O  
ANISOU 4125  OD1 ASN B 208     7955   5498   6345   -511   1440   -867       O  
ATOM   4126  ND2 ASN B 208      39.624 110.975  18.339  1.00 55.06           N  
ANISOU 4126  ND2 ASN B 208     8432   6011   6475   -721   1333   -955       N  
ATOM   4127  N   ASP B 209      37.553 116.130  16.187  1.00 57.89           N  
ANISOU 4127  N   ASP B 209     8697   5781   7514   -537   1959  -1032       N  
ATOM   4128  CA  ASP B 209      37.038 117.491  16.365  1.00 64.63           C  
ANISOU 4128  CA  ASP B 209     9567   6472   8517   -555   2174  -1096       C  
ATOM   4129  C   ASP B 209      35.686 117.374  17.076  1.00 61.90           C  
ANISOU 4129  C   ASP B 209     9245   6046   8227   -546   2321  -1120       C  
ATOM   4130  O   ASP B 209      35.269 116.281  17.461  1.00 58.23           O  
ANISOU 4130  O   ASP B 209     8793   5663   7667   -538   2244  -1097       O  
ATOM   4131  CB  ASP B 209      36.897 118.238  15.032  1.00 65.52           C  
ANISOU 4131  CB  ASP B 209     9568   6501   8824   -439   2198   -993       C  
ATOM   4132  CG  ASP B 209      38.185 118.466  14.260  1.00 65.97           C  
ANISOU 4132  CG  ASP B 209     9598   6618   8848   -441   2076   -968       C  
ATOM   4133  OD1 ASP B 209      39.149 119.002  14.845  1.00 74.53           O  
ANISOU 4133  OD1 ASP B 209    10756   7709   9851   -555   2095  -1073       O  
ATOM   4134  OD2 ASP B 209      38.203 118.124  13.064  1.00 65.63           O  
ANISOU 4134  OD2 ASP B 209     9462   6613   8861   -336   1969   -842       O  
ATOM   4135  N   PHE B 210      35.006 118.505  17.271  1.00 62.80           N  
ANISOU 4135  N   PHE B 210     9364   5992   8504   -550   2542  -1167       N  
ATOM   4136  CA  PHE B 210      33.801 118.508  18.093  1.00 63.98           C  
ANISOU 4136  CA  PHE B 210     9550   6047   8710   -562   2715  -1211       C  
ATOM   4137  C   PHE B 210      32.631 117.889  17.312  1.00 68.61           C  
ANISOU 4137  C   PHE B 210    10013   6619   9434   -407   2679  -1053       C  
ATOM   4138  O   PHE B 210      32.541 118.029  16.088  1.00 75.75           O  
ANISOU 4138  O   PHE B 210    10799   7514  10465   -296   2610   -919       O  
ATOM   4139  CB  PHE B 210      33.527 119.931  18.578  1.00 56.33           C  
ANISOU 4139  CB  PHE B 210     8628   4891   7882   -624   2981  -1318       C  
ATOM   4140  CG  PHE B 210      34.483 120.426  19.634  1.00 51.54           C  
ANISOU 4140  CG  PHE B 210     8171   4300   7110   -812   3039  -1499       C  
ATOM   4141  CD1 PHE B 210      34.375 119.985  20.950  1.00 50.67           C  
ANISOU 4141  CD1 PHE B 210     8193   4233   6823   -949   3086  -1621       C  
ATOM   4142  CD2 PHE B 210      35.464 121.352  19.319  1.00 46.98           C  
ANISOU 4142  CD2 PHE B 210     7603   3695   6550   -862   3050  -1544       C  
ATOM   4143  CE1 PHE B 210      35.231 120.471  21.930  1.00 50.46           C  
ANISOU 4143  CE1 PHE B 210     8310   4228   6633  -1144   3137  -1783       C  
ATOM   4144  CE2 PHE B 210      36.317 121.833  20.298  1.00 48.89           C  
ANISOU 4144  CE2 PHE B 210     7984   3952   6637  -1050   3104  -1709       C  
ATOM   4145  CZ  PHE B 210      36.203 121.389  21.598  1.00 49.88           C  
ANISOU 4145  CZ  PHE B 210     8243   4128   6579  -1196   3143  -1827       C  
ATOM   4146  N   ASN B 224      18.120 104.467   6.395  1.00 41.61           N  
ANISOU 4146  N   ASN B 224     5200   4030   6580    435   1052   1196       N  
ATOM   4147  CA  ASN B 224      18.275 104.032   7.801  1.00 43.72           C  
ANISOU 4147  CA  ASN B 224     5564   4258   6788    455   1153   1030       C  
ATOM   4148  C   ASN B 224      18.013 102.518   7.986  1.00 39.69           C  
ANISOU 4148  C   ASN B 224     5099   3842   6138    432   1058    996       C  
ATOM   4149  O   ASN B 224      17.344 102.076   8.964  1.00 37.50           O  
ANISOU 4149  O   ASN B 224     4831   3523   5891    455   1132    961       O  
ATOM   4150  CB  ASN B 224      17.338 104.827   8.713  1.00 46.79           C  
ANISOU 4150  CB  ASN B 224     5893   4497   7385    507   1336   1057       C  
ATOM   4151  CG  ASN B 224      17.554 104.526  10.176  1.00 44.49           C  
ANISOU 4151  CG  ASN B 224     5714   4165   7024    512   1453    881       C  
ATOM   4152  OD1 ASN B 224      18.662 104.175  10.574  1.00 41.43           O  
ANISOU 4152  OD1 ASN B 224     5446   3837   6457    480   1424    730       O  
ATOM   4153  ND2 ASN B 224      16.515 104.678  10.974  1.00 46.32           N  
ANISOU 4153  ND2 ASN B 224     5904   4294   7398    545   1588    905       N  
ATOM   4154  N   GLN B 225      18.544 101.710   7.065  1.00 39.67           N  
ANISOU 4154  N   GLN B 225     5127   3960   5984    383    905   1003       N  
ATOM   4155  CA  GLN B 225      18.331 100.264   7.043  1.00 34.47           C  
ANISOU 4155  CA  GLN B 225     4506   3390   5198    352    810    980       C  
ATOM   4156  C   GLN B 225      19.700  99.615   7.237  1.00 32.09           C  
ANISOU 4156  C   GLN B 225     4330   3157   4705    327    771    822       C  
ATOM   4157  O   GLN B 225      20.278  99.088   6.296  1.00 29.91           O  
ANISOU 4157  O   GLN B 225     4080   2965   4317    279    664    826       O  
ATOM   4158  CB  GLN B 225      17.621  99.854   5.737  1.00 38.92           C  
ANISOU 4158  CB  GLN B 225     4987   4029   5770    303    677   1142       C  
ATOM   4159  CG  GLN B 225      16.785  98.576   5.813  1.00 38.37           C  
ANISOU 4159  CG  GLN B 225     4909   4011   5657    280    614   1171       C  
ATOM   4160  CD  GLN B 225      16.009  98.257   4.544  1.00 40.13           C  
ANISOU 4160  CD  GLN B 225     5048   4308   5890    212    483   1340       C  
ATOM   4161  OE1 GLN B 225      15.875  99.099   3.669  1.00 39.47           O  
ANISOU 4161  OE1 GLN B 225     4890   4227   5880    190    446   1466       O  
ATOM   4162  NE2 GLN B 225      15.507  97.027   4.413  1.00 35.72           N  
ANISOU 4162  NE2 GLN B 225     4503   3816   5252    169    407   1347       N  
ATOM   4163  N   TYR B 226      20.197  99.645   8.480  1.00 28.76           N  
ANISOU 4163  N   TYR B 226     3983   2694   4248    352    864    688       N  
ATOM   4164  CA  TYR B 226      21.469  99.052   8.844  1.00 26.63           C  
ANISOU 4164  CA  TYR B 226     3818   2481   3817    330    835    552       C  
ATOM   4165  C   TYR B 226      21.563  97.583   8.416  1.00 25.12           C  
ANISOU 4165  C   TYR B 226     3655   2383   3504    298    727    546       C  
ATOM   4166  O   TYR B 226      22.623  97.134   7.928  1.00 24.97           O  
ANISOU 4166  O   TYR B 226     3690   2425   3372    267    664    492       O  
ATOM   4167  CB  TYR B 226      21.651  99.144  10.351  1.00 25.77           C  
ANISOU 4167  CB  TYR B 226     3772   2323   3694    348    943    438       C  
ATOM   4168  CG  TYR B 226      22.834  98.425  10.928  1.00 25.95           C  
ANISOU 4168  CG  TYR B 226     3890   2406   3561    322    911    317       C  
ATOM   4169  CD1 TYR B 226      24.123  98.891  10.739  1.00 26.32           C  
ANISOU 4169  CD1 TYR B 226     3983   2472   3544    301    894    254       C  
ATOM   4170  CD2 TYR B 226      22.658  97.283  11.690  1.00 25.74           C  
ANISOU 4170  CD2 TYR B 226     3901   2417   3463    319    898    276       C  
ATOM   4171  CE1 TYR B 226      25.213  98.246  11.304  1.00 24.92           C  
ANISOU 4171  CE1 TYR B 226     3879   2348   3241    276    864    162       C  
ATOM   4172  CE2 TYR B 226      23.730  96.642  12.281  1.00 24.96           C  
ANISOU 4172  CE2 TYR B 226     3875   2370   3237    295    871    185       C  
ATOM   4173  CZ  TYR B 226      25.013  97.132  12.099  1.00 27.14           C  
ANISOU 4173  CZ  TYR B 226     4189   2664   3458    273    852    131       C  
ATOM   4174  OH  TYR B 226      26.067  96.512  12.714  1.00 28.49           O  
ANISOU 4174  OH  TYR B 226     4419   2886   3519    247    823     60       O  
ATOM   4175  N   PHE B 227      20.501  96.801   8.631  1.00 24.28           N  
ANISOU 4175  N   PHE B 227     3516   2284   3425    303    715    595       N  
ATOM   4176  CA  PHE B 227      20.589  95.389   8.250  1.00 22.30           C  
ANISOU 4176  CA  PHE B 227     3296   2114   3063    268    626    581       C  
ATOM   4177  C   PHE B 227      20.508  95.219   6.725  1.00 24.12           C  
ANISOU 4177  C   PHE B 227     3494   2403   3266    212    522    668       C  
ATOM   4178  O   PHE B 227      20.874  94.157   6.261  1.00 23.46           O  
ANISOU 4178  O   PHE B 227     3454   2383   3077    169    458    635       O  
ATOM   4179  CB  PHE B 227      19.599  94.527   9.024  1.00 22.49           C  
ANISOU 4179  CB  PHE B 227     3306   2129   3110    286    647    591       C  
ATOM   4180  CG  PHE B 227      20.019  94.405  10.459  1.00 21.93           C  
ANISOU 4180  CG  PHE B 227     3298   2029   3005    316    730    481       C  
ATOM   4181  CD1 PHE B 227      21.128  93.647  10.792  1.00 23.33           C  
ANISOU 4181  CD1 PHE B 227     3550   2256   3056    299    702    386       C  
ATOM   4182  CD2 PHE B 227      19.378  95.130  11.452  1.00 23.11           C  
ANISOU 4182  CD2 PHE B 227     3431   2099   3250    352    841    478       C  
ATOM   4183  CE1 PHE B 227      21.567  93.581  12.104  1.00 22.70           C  
ANISOU 4183  CE1 PHE B 227     3526   2161   2935    311    765    299       C  
ATOM   4184  CE2 PHE B 227      19.833  95.076  12.756  1.00 22.55           C  
ANISOU 4184  CE2 PHE B 227     3431   2010   3127    358    916    373       C  
ATOM   4185  CZ  PHE B 227      20.904  94.286  13.079  1.00 24.39           C  
ANISOU 4185  CZ  PHE B 227     3735   2307   3223    335    868    290       C  
ATOM   4186  N   ALA B 228      20.059  96.235   5.968  1.00 23.83           N  
ANISOU 4186  N   ALA B 228     3385   2346   3322    206    510    778       N  
ATOM   4187  CA  ALA B 228      20.148  96.152   4.496  1.00 26.21           C  
ANISOU 4187  CA  ALA B 228     3669   2716   3573    134    407    857       C  
ATOM   4188  C   ALA B 228      21.633  96.105   4.108  1.00 27.82           C  
ANISOU 4188  C   ALA B 228     3957   2952   3658    111    392    754       C  
ATOM   4189  O   ALA B 228      22.047  95.312   3.252  1.00 26.38           O  
ANISOU 4189  O   ALA B 228     3819   2837   3365     45    324    738       O  
ATOM   4190  CB  ALA B 228      19.419  97.279   3.820  1.00 27.33           C  
ANISOU 4190  CB  ALA B 228     3709   2832   3844    131    396   1009       C  
ATOM   4191  N   THR B 229      22.437  96.894   4.825  1.00 26.42           N  
ANISOU 4191  N   THR B 229     3809   2724   3505    160    467    676       N  
ATOM   4192  CA  THR B 229      23.866  96.957   4.581  1.00 27.25           C  
ANISOU 4192  CA  THR B 229     3984   2850   3519    145    462    585       C  
ATOM   4193  C   THR B 229      24.550  95.649   5.018  1.00 23.68           C  
ANISOU 4193  C   THR B 229     3606   2435   2955    135    451    481       C  
ATOM   4194  O   THR B 229      25.429  95.134   4.299  1.00 22.16           O  
ANISOU 4194  O   THR B 229     3460   2283   2674     93    414    442       O  
ATOM   4195  CB  THR B 229      24.454  98.207   5.241  1.00 29.59           C  
ANISOU 4195  CB  THR B 229     4283   3080   3879    191    542    541       C  
ATOM   4196  OG1 THR B 229      23.755  99.344   4.713  1.00 29.99           O  
ANISOU 4196  OG1 THR B 229     4252   3090   4050    200    556    655       O  
ATOM   4197  CG2 THR B 229      25.941  98.341   4.998  1.00 28.52           C  
ANISOU 4197  CG2 THR B 229     4210   2964   3661    176    534    457       C  
ATOM   4198  N   ILE B 230      24.200  95.137   6.207  1.00 22.99           N  
ANISOU 4198  N   ILE B 230     3529   2326   2879    172    494    437       N  
ATOM   4199  CA  ILE B 230      24.798  93.914   6.734  1.00 21.70           C  
ANISOU 4199  CA  ILE B 230     3421   2192   2629    167    488    354       C  
ATOM   4200  C   ILE B 230      24.468  92.778   5.765  1.00 19.57           C  
ANISOU 4200  C   ILE B 230     3157   1974   2303    114    425    385       C  
ATOM   4201  O   ILE B 230      25.340  91.965   5.427  1.00 19.95           O  
ANISOU 4201  O   ILE B 230     3254   2049   2275     85    411    329       O  
ATOM   4202  CB  ILE B 230      24.361  93.618   8.185  1.00 23.43           C  
ANISOU 4202  CB  ILE B 230     3646   2383   2870    209    543    317       C  
ATOM   4203  CG1 ILE B 230      24.762  94.720   9.170  1.00 24.07           C  
ANISOU 4203  CG1 ILE B 230     3741   2415   2988    240    617    270       C  
ATOM   4204  CG2 ILE B 230      24.848  92.252   8.662  1.00 22.66           C  
ANISOU 4204  CG2 ILE B 230     3592   2321   2696    203    529    259       C  
ATOM   4205  CD1 ILE B 230      26.213  95.150   9.146  1.00 24.38           C  
ANISOU 4205  CD1 ILE B 230     3824   2464   2974    228    616    204       C  
ATOM   4206  N   ASN B 231      23.240  92.754   5.266  1.00 18.74           N  
ANISOU 4206  N   ASN B 231     3000   1878   2240     91    391    477       N  
ATOM   4207  CA  ASN B 231      22.783  91.704   4.330  1.00 20.51           C  
ANISOU 4207  CA  ASN B 231     3231   2155   2404     20    328    510       C  
ATOM   4208  C   ASN B 231      23.645  91.714   3.060  1.00 21.64           C  
ANISOU 4208  C   ASN B 231     3416   2337   2468    -49    291    497       C  
ATOM   4209  O   ASN B 231      24.043  90.659   2.524  1.00 19.58           O  
ANISOU 4209  O   ASN B 231     3209   2107   2124   -106    278    449       O  
ATOM   4210  CB  ASN B 231      21.323  91.925   3.957  1.00 22.50           C  
ANISOU 4210  CB  ASN B 231     3407   2415   2726     -1    287    634       C  
ATOM   4211  CG  ASN B 231      20.792  90.874   3.005  1.00 25.80           C  
ANISOU 4211  CG  ASN B 231     3835   2894   3073    -93    217    670       C  
ATOM   4212  OD1 ASN B 231      20.337  91.230   1.927  1.00 31.43           O  
ANISOU 4212  OD1 ASN B 231     4516   3646   3779   -164    152    764       O  
ATOM   4213  ND2 ASN B 231      20.848  89.595   3.371  1.00 25.33           N  
ANISOU 4213  ND2 ASN B 231     3820   2844   2960   -102    229    601       N  
ATOM   4214  N   GLU B 232      23.930  92.922   2.555  1.00 20.57           N  
ANISOU 4214  N   GLU B 232     3258   2193   2363    -48    284    539       N  
ATOM   4215  CA  GLU B 232      24.744  93.073   1.337  1.00 22.37           C  
ANISOU 4215  CA  GLU B 232     3526   2456   2516   -116    254    532       C  
ATOM   4216  C   GLU B 232      26.183  92.623   1.592  1.00 19.72           C  
ANISOU 4216  C   GLU B 232     3261   2106   2124   -100    301    412       C  
ATOM   4217  O   GLU B 232      26.791  92.102   0.677  1.00 21.50           O  
ANISOU 4217  O   GLU B 232     3538   2358   2272   -166    292    381       O  
ATOM   4218  CB  GLU B 232      24.713  94.511   0.817  1.00 26.22           C  
ANISOU 4218  CB  GLU B 232     3965   2933   3062   -112    240    613       C  
ATOM   4219  CG  GLU B 232      23.349  94.942   0.320  1.00 31.47           C  
ANISOU 4219  CG  GLU B 232     4546   3617   3791   -144    185    761       C  
ATOM   4220  CD  GLU B 232      22.851  94.268  -0.955  1.00 43.12           C  
ANISOU 4220  CD  GLU B 232     6032   5172   5177   -266     98    827       C  
ATOM   4221  OE1 GLU B 232      23.689  93.963  -1.834  1.00 53.85           O  
ANISOU 4221  OE1 GLU B 232     7462   6568   6427   -338     84    778       O  
ATOM   4222  OE2 GLU B 232      21.614  94.060  -1.082  1.00 53.63           O  
ANISOU 4222  OE2 GLU B 232     7302   6526   6546   -297     48    932       O  
ATOM   4223  N   ILE B 233      26.700  92.772   2.820  1.00 18.63           N  
ANISOU 4223  N   ILE B 233     3126   1928   2025    -22    352    351       N  
ATOM   4224  CA  ILE B 233      28.008  92.249   3.164  1.00 18.43           C  
ANISOU 4224  CA  ILE B 233     3151   1891   1959     -7    389    258       C  
ATOM   4225  C   ILE B 233      28.009  90.708   3.048  1.00 20.76           C  
ANISOU 4225  C   ILE B 233     3480   2202   2202    -42    393    220       C  
ATOM   4226  O   ILE B 233      28.901  90.106   2.391  1.00 18.73           O  
ANISOU 4226  O   ILE B 233     3270   1948   1899    -82    412    173       O  
ATOM   4227  CB  ILE B 233      28.437  92.737   4.548  1.00 19.36           C  
ANISOU 4227  CB  ILE B 233     3260   1974   2121     64    430    217       C  
ATOM   4228  CG1 ILE B 233      28.822  94.222   4.529  1.00 21.78           C  
ANISOU 4228  CG1 ILE B 233     3549   2254   2469     86    444    228       C  
ATOM   4229  CG2 ILE B 233      29.554  91.903   5.114  1.00 20.98           C  
ANISOU 4229  CG2 ILE B 233     3501   2177   2295     77    455    145       C  
ATOM   4230  CD1 ILE B 233      29.063  94.777   5.918  1.00 20.25           C  
ANISOU 4230  CD1 ILE B 233     3354   2027   2312    137    490    186       C  
ATOM   4231  N   TYR B 234      27.006  90.035   3.626  1.00 17.79           N  
ANISOU 4231  N   TYR B 234     3084   1830   1843    -30    386    239       N  
ATOM   4232  CA  TYR B 234      26.976  88.568   3.511  1.00 19.25           C  
ANISOU 4232  CA  TYR B 234     3300   2023   1988    -64    398    203       C  
ATOM   4233  C   TYR B 234      26.771  88.151   2.048  1.00 19.37           C  
ANISOU 4233  C   TYR B 234     3349   2071   1939   -167    372    217       C  
ATOM   4234  O   TYR B 234      27.392  87.179   1.545  1.00 19.38           O  
ANISOU 4234  O   TYR B 234     3402   2066   1894   -215    408    159       O  
ATOM   4235  CB  TYR B 234      25.892  87.985   4.424  1.00 18.74           C  
ANISOU 4235  CB  TYR B 234     3204   1956   1957    -32    395    226       C  
ATOM   4236  CG  TYR B 234      26.199  88.022   5.903  1.00 19.49           C  
ANISOU 4236  CG  TYR B 234     3287   2026   2092     47    432    196       C  
ATOM   4237  CD1 TYR B 234      27.227  87.266   6.427  1.00 19.66           C  
ANISOU 4237  CD1 TYR B 234     3331   2036   2100     65    465    141       C  
ATOM   4238  CD2 TYR B 234      25.442  88.778   6.793  1.00 19.06           C  
ANISOU 4238  CD2 TYR B 234     3195   1957   2088     95    437    229       C  
ATOM   4239  CE1 TYR B 234      27.509  87.261   7.781  1.00 20.74           C  
ANISOU 4239  CE1 TYR B 234     3458   2163   2259    120    487    125       C  
ATOM   4240  CE2 TYR B 234      25.702  88.771   8.161  1.00 19.04           C  
ANISOU 4240  CE2 TYR B 234     3194   1937   2101    147    473    196       C  
ATOM   4241  CZ  TYR B 234      26.747  88.022   8.659  1.00 19.40           C  
ANISOU 4241  CZ  TYR B 234     3265   1987   2117    155    490    147       C  
ATOM   4242  OH  TYR B 234      27.024  87.969   9.999  1.00 22.65           O  
ANISOU 4242  OH  TYR B 234     3678   2395   2530    190    513    127       O  
ATOM   4243  N   LYS B 235      25.898  88.854   1.322  1.00 21.60           N  
ANISOU 4243  N   LYS B 235     3604   2386   2216   -213    315    297       N  
ATOM   4244  CA  LYS B 235      25.707  88.536  -0.095  1.00 22.80           C  
ANISOU 4244  CA  LYS B 235     3794   2582   2286   -333    280    317       C  
ATOM   4245  C   LYS B 235      27.048  88.627  -0.858  1.00 25.18           C  
ANISOU 4245  C   LYS B 235     4158   2875   2534   -370    321    252       C  
ATOM   4246  O   LYS B 235      27.348  87.767  -1.715  1.00 21.79           O  
ANISOU 4246  O   LYS B 235     3793   2455   2029   -462    346    205       O  
ATOM   4247  CB  LYS B 235      24.694  89.473  -0.754  1.00 26.52           C  
ANISOU 4247  CB  LYS B 235     4211   3095   2768   -377    202    437       C  
ATOM   4248  CG  LYS B 235      23.230  89.190  -0.430  1.00 33.66           C  
ANISOU 4248  CG  LYS B 235     5056   4017   3714   -382    156    519       C  
ATOM   4249  CD  LYS B 235      22.253  90.246  -0.981  1.00 38.12           C  
ANISOU 4249  CD  LYS B 235     5543   4615   4324   -412     81    664       C  
ATOM   4250  CE  LYS B 235      22.220  90.346  -2.491  1.00 42.01           C  
ANISOU 4250  CE  LYS B 235     6063   5177   4721   -551     14    720       C  
ATOM   4251  N   ALA B 236      27.837  89.680  -0.593  1.00 22.61           N  
ANISOU 4251  N   ALA B 236     3814   2525   2248   -306    334    249       N  
ATOM   4252  CA  ALA B 236      29.122  89.866  -1.321  1.00 24.51           C  
ANISOU 4252  CA  ALA B 236     4107   2754   2450   -337    374    196       C  
ATOM   4253  C   ALA B 236      30.063  88.667  -1.062  1.00 23.40           C  
ANISOU 4253  C   ALA B 236     4014   2573   2303   -330    453    101       C  
ATOM   4254  O   ALA B 236      30.721  88.191  -1.975  1.00 22.23           O  
ANISOU 4254  O   ALA B 236     3926   2417   2103   -402    498     54       O  
ATOM   4255  CB  ALA B 236      29.790  91.146  -0.910  1.00 23.06           C  
ANISOU 4255  CB  ALA B 236     3891   2547   2322   -263    377    207       C  
ATOM   4256  N   ILE B 237      30.159  88.224   0.194  1.00 21.14           N  
ANISOU 4256  N   ILE B 237     3697   2256   2077   -245    477     78       N  
ATOM   4257  CA  ILE B 237      30.966  87.057   0.533  1.00 21.86           C  
ANISOU 4257  CA  ILE B 237     3812   2305   2186   -232    550     12       C  
ATOM   4258  C   ILE B 237      30.480  85.837  -0.267  1.00 22.75           C  
ANISOU 4258  C   ILE B 237     3975   2422   2245   -326    579    -15       C  
ATOM   4259  O   ILE B 237      31.270  85.150  -0.923  1.00 21.81           O  
ANISOU 4259  O   ILE B 237     3908   2269   2109   -377    654    -73       O  
ATOM   4260  CB  ILE B 237      30.951  86.764   2.048  1.00 22.22           C  
ANISOU 4260  CB  ILE B 237     3811   2332   2298   -137    555     14       C  
ATOM   4261  CG1 ILE B 237      31.633  87.885   2.831  1.00 21.70           C  
ANISOU 4261  CG1 ILE B 237     3712   2260   2273    -66    541     24       C  
ATOM   4262  CG2 ILE B 237      31.578  85.404   2.313  1.00 21.61           C  
ANISOU 4262  CG2 ILE B 237     3747   2215   2249   -134    626    -30       C  
ATOM   4263  CD1 ILE B 237      31.407  87.820   4.331  1.00 23.31           C  
ANISOU 4263  CD1 ILE B 237     3876   2461   2518      5    533     35       C  
ATOM   4264  N   TYR B 238      29.176  85.557  -0.226  1.00 22.95           N  
ANISOU 4264  N   TYR B 238     3986   2483   2248   -356    527     24       N  
ATOM   4265  CA  TYR B 238      28.675  84.313  -0.814  1.00 23.14           C  
ANISOU 4265  CA  TYR B 238     4058   2509   2225   -447    557     -7       C  
ATOM   4266  C   TYR B 238      28.617  84.360  -2.335  1.00 24.57           C  
ANISOU 4266  C   TYR B 238     4307   2723   2304   -588    552    -17       C  
ATOM   4267  O   TYR B 238      28.377  83.314  -2.922  1.00 26.38           O  
ANISOU 4267  O   TYR B 238     4592   2948   2481   -684    594    -63       O  
ATOM   4268  CB  TYR B 238      27.328  83.888  -0.217  1.00 22.21           C  
ANISOU 4268  CB  TYR B 238     3899   2416   2120   -437    506     37       C  
ATOM   4269  CG  TYR B 238      27.537  83.136   1.057  1.00 21.62           C  
ANISOU 4269  CG  TYR B 238     3793   2297   2122   -342    552     12       C  
ATOM   4270  CD1 TYR B 238      27.883  81.788   1.034  1.00 22.43           C  
ANISOU 4270  CD1 TYR B 238     3928   2356   2235   -368    632    -46       C  
ATOM   4271  CD2 TYR B 238      27.459  83.780   2.268  1.00 19.79           C  
ANISOU 4271  CD2 TYR B 238     3502   2063   1952   -235    524     48       C  
ATOM   4272  CE1 TYR B 238      28.125  81.102   2.215  1.00 21.79           C  
ANISOU 4272  CE1 TYR B 238     3809   2237   2231   -281    671    -53       C  
ATOM   4273  CE2 TYR B 238      27.667  83.107   3.452  1.00 20.53           C  
ANISOU 4273  CE2 TYR B 238     3569   2128   2103   -160    559     34       C  
ATOM   4274  CZ  TYR B 238      28.006  81.759   3.428  1.00 19.41           C  
ANISOU 4274  CZ  TYR B 238     3449   1949   1977   -180    627     -9       C  
ATOM   4275  OH  TYR B 238      28.233  81.117   4.616  1.00 18.69           O  
ANISOU 4275  OH  TYR B 238     3321   1831   1948   -106    656     -6       O  
ATOM   4276  N   LYS B 239      28.846  85.524  -2.960  1.00 23.53           N  
ANISOU 4276  N   LYS B 239     4175   2624   2141   -608    508     21       N  
ATOM   4277  CA  LYS B 239      28.922  85.589  -4.428  1.00 25.66           C  
ANISOU 4277  CA  LYS B 239     4517   2930   2301   -753    507     12       C  
ATOM   4278  C   LYS B 239      30.354  85.894  -4.885  1.00 23.74           C  
ANISOU 4278  C   LYS B 239     4318   2643   2058   -749    586    -48       C  
ATOM   4279  O   LYS B 239      30.560  86.156  -6.053  1.00 24.46           O  
ANISOU 4279  O   LYS B 239     4469   2763   2061   -859    590    -53       O  
ATOM   4280  CB  LYS B 239      27.957  86.641  -4.989  1.00 30.06           C  
ANISOU 4280  CB  LYS B 239     5039   3567   2816   -805    388    124       C  
ATOM   4281  CG  LYS B 239      26.480  86.364  -4.721  1.00 36.45           C  
ANISOU 4281  CG  LYS B 239     5799   4421   3627   -829    307    201       C  
ATOM   4282  N   SER B 240      31.340  85.868  -3.980  1.00 21.91           N  
ANISOU 4282  N   SER B 240     4055   2347   1922   -630    647    -85       N  
ATOM   4283  CA  SER B 240      32.717  86.289  -4.336  1.00 21.33           C  
ANISOU 4283  CA  SER B 240     4005   2230   1868   -614    715   -126       C  
ATOM   4284  C   SER B 240      33.283  85.442  -5.467  1.00 22.76           C  
ANISOU 4284  C   SER B 240     4282   2378   1985   -733    820   -206       C  
ATOM   4285  O   SER B 240      33.300  84.208  -5.396  1.00 22.30           O  
ANISOU 4285  O   SER B 240     4256   2275   1942   -762    903   -265       O  
ATOM   4286  CB  SER B 240      33.646  86.219  -3.149  1.00 21.41           C  
ANISOU 4286  CB  SER B 240     3960   2179   1993   -482    759   -144       C  
ATOM   4287  OG  SER B 240      34.983  86.492  -3.571  1.00 21.42           O  
ANISOU 4287  OG  SER B 240     3983   2134   2019   -477    831   -181       O  
ATOM   4288  N   PRO B 241      33.745  86.068  -6.573  1.00 25.36           N  
ANISOU 4288  N   PRO B 241     4665   2725   2243   -815    831   -213       N  
ATOM   4289  CA  PRO B 241      34.472  85.342  -7.597  1.00 27.65           C  
ANISOU 4289  CA  PRO B 241     5054   2970   2482   -925    958   -300       C  
ATOM   4290  C   PRO B 241      35.942  85.060  -7.236  1.00 27.98           C  
ANISOU 4290  C   PRO B 241     5084   2908   2638   -842   1086   -358       C  
ATOM   4291  O   PRO B 241      36.627  84.436  -8.013  1.00 32.57           O  
ANISOU 4291  O   PRO B 241     5740   3430   3203   -921   1215   -433       O  
ATOM   4292  CB  PRO B 241      34.366  86.301  -8.800  1.00 29.00           C  
ANISOU 4292  CB  PRO B 241     5273   3208   2534  -1035    904   -266       C  
ATOM   4293  CG  PRO B 241      34.378  87.665  -8.190  1.00 26.95           C  
ANISOU 4293  CG  PRO B 241     4922   2981   2336   -918    800   -178       C  
ATOM   4294  CD  PRO B 241      33.584  87.490  -6.904  1.00 25.25           C  
ANISOU 4294  CD  PRO B 241     4622   2772   2199   -811    734   -136       C  
ATOM   4295  N   ILE B 242      36.417  85.561  -6.097  1.00 24.08           N  
ANISOU 4295  N   ILE B 242     4497   2393   2258   -693   1051   -317       N  
ATOM   4296  CA  ILE B 242      37.742  85.297  -5.603  1.00 25.03           C  
ANISOU 4296  CA  ILE B 242     4583   2424   2500   -609   1150   -345       C  
ATOM   4297  C   ILE B 242      37.712  84.140  -4.602  1.00 25.56           C  
ANISOU 4297  C   ILE B 242     4605   2439   2665   -544   1198   -354       C  
ATOM   4298  O   ILE B 242      38.434  83.173  -4.743  1.00 26.27           O  
ANISOU 4298  O   ILE B 242     4712   2442   2826   -554   1332   -403       O  
ATOM   4299  CB  ILE B 242      38.336  86.557  -4.960  1.00 24.40           C  
ANISOU 4299  CB  ILE B 242     4430   2360   2478   -503   1077   -289       C  
ATOM   4300  CG1 ILE B 242      38.532  87.678  -5.991  1.00 27.62           C  
ANISOU 4300  CG1 ILE B 242     4879   2806   2809   -563   1048   -278       C  
ATOM   4301  CG2 ILE B 242      39.626  86.222  -4.205  1.00 24.42           C  
ANISOU 4301  CG2 ILE B 242     4375   2281   2620   -410   1156   -295       C  
ATOM   4302  CD1 ILE B 242      39.521  87.383  -7.076  1.00 28.02           C  
ANISOU 4302  CD1 ILE B 242     5002   2798   2845   -640   1177   -341       C  
ATOM   4303  N   TYR B 243      36.860  84.262  -3.586  1.00 22.59           N  
ANISOU 4303  N   TYR B 243     4168   2112   2301   -476   1094   -302       N  
ATOM   4304  CA  TYR B 243      36.674  83.230  -2.572  1.00 24.59           C  
ANISOU 4304  CA  TYR B 243     4375   2331   2637   -416   1120   -297       C  
ATOM   4305  C   TYR B 243      35.486  82.375  -2.999  1.00 24.66           C  
ANISOU 4305  C   TYR B 243     4435   2362   2569   -505   1121   -324       C  
ATOM   4306  O   TYR B 243      34.380  82.626  -2.568  1.00 23.27           O  
ANISOU 4306  O   TYR B 243     4236   2253   2353   -494   1017   -281       O  
ATOM   4307  CB  TYR B 243      36.486  83.877  -1.194  1.00 23.85           C  
ANISOU 4307  CB  TYR B 243     4192   2277   2593   -299   1014   -229       C  
ATOM   4308  CG  TYR B 243      37.631  84.775  -0.824  1.00 23.10           C  
ANISOU 4308  CG  TYR B 243     4052   2167   2557   -232   1005   -204       C  
ATOM   4309  CD1 TYR B 243      38.777  84.254  -0.257  1.00 22.59           C  
ANISOU 4309  CD1 TYR B 243     3938   2036   2607   -175   1076   -196       C  
ATOM   4310  CD2 TYR B 243      37.586  86.149  -1.068  1.00 21.97           C  
ANISOU 4310  CD2 TYR B 243     3910   2073   2364   -229    928   -181       C  
ATOM   4311  CE1 TYR B 243      39.843  85.068   0.097  1.00 24.06           C  
ANISOU 4311  CE1 TYR B 243     4078   2214   2849   -122   1060   -166       C  
ATOM   4312  CE2 TYR B 243      38.647  86.972  -0.721  1.00 21.41           C  
ANISOU 4312  CE2 TYR B 243     3800   1987   2347   -174    922   -162       C  
ATOM   4313  CZ  TYR B 243      39.783  86.433  -0.147  1.00 22.48           C  
ANISOU 4313  CZ  TYR B 243     3888   2063   2588   -123    984   -156       C  
ATOM   4314  OH  TYR B 243      40.855  87.220   0.174  1.00 22.77           O  
ANISOU 4314  OH  TYR B 243     3882   2088   2678    -79    973   -132       O  
ATOM   4315  N   LYS B 244      35.756  81.429  -3.909  1.00 25.16           N  
ANISOU 4315  N   LYS B 244     4574   2368   2615   -603   1247   -398       N  
ATOM   4316  CA  LYS B 244      34.743  80.667  -4.606  1.00 29.38           C  
ANISOU 4316  CA  LYS B 244     5182   2924   3053   -727   1262   -439       C  
ATOM   4317  C   LYS B 244      34.346  79.426  -3.808  1.00 26.08           C  
ANISOU 4317  C   LYS B 244     4733   2462   2714   -689   1309   -449       C  
ATOM   4318  O   LYS B 244      33.269  78.924  -4.014  1.00 26.93           O  
ANISOU 4318  O   LYS B 244     4873   2606   2751   -763   1277   -459       O  
ATOM   4319  CB  LYS B 244      35.233  80.255  -5.994  1.00 32.61           C  
ANISOU 4319  CB  LYS B 244     5704   3290   3394   -870   1390   -526       C  
ATOM   4320  CG  LYS B 244      35.290  81.406  -6.977  1.00 38.76           C  
ANISOU 4320  CG  LYS B 244     6533   4137   4057   -946   1328   -513       C  
ATOM   4321  CD  LYS B 244      35.723  81.005  -8.350  1.00 44.52           C  
ANISOU 4321  CD  LYS B 244     7385   4830   4700  -1105   1456   -602       C  
ATOM   4322  CE  LYS B 244      37.157  80.529  -8.392  1.00 51.84           C  
ANISOU 4322  CE  LYS B 244     8318   5628   5751  -1063   1636   -663       C  
ATOM   4323  NZ  LYS B 244      37.627  80.376  -9.795  1.00 59.44           N  
ANISOU 4323  NZ  LYS B 244     9408   6558   6619  -1222   1765   -751       N  
ATOM   4324  N   ASN B 245      35.221  78.961  -2.913  1.00 24.46           N  
ANISOU 4324  N   ASN B 245     4458   2181   2654   -579   1378   -435       N  
ATOM   4325  CA  ASN B 245      35.008  77.692  -2.197  1.00 25.74           C  
ANISOU 4325  CA  ASN B 245     4585   2285   2909   -544   1444   -439       C  
ATOM   4326  C   ASN B 245      33.940  77.936  -1.130  1.00 23.14           C  
ANISOU 4326  C   ASN B 245     4192   2034   2564   -474   1302   -370       C  
ATOM   4327  O   ASN B 245      34.049  78.907  -0.374  1.00 20.67           O  
ANISOU 4327  O   ASN B 245     3817   1771   2264   -385   1199   -306       O  
ATOM   4328  CB  ASN B 245      36.308  77.143  -1.598  1.00 25.46           C  
ANISOU 4328  CB  ASN B 245     4482   2145   3045   -453   1559   -424       C  
ATOM   4329  CG  ASN B 245      36.046  75.939  -0.732  1.00 26.53           C  
ANISOU 4329  CG  ASN B 245     4563   2231   3285   -404   1609   -403       C  
ATOM   4330  OD1 ASN B 245      35.911  76.071   0.492  1.00 23.70           O  
ANISOU 4330  OD1 ASN B 245     4116   1908   2981   -300   1520   -324       O  
ATOM   4331  ND2 ASN B 245      35.900  74.776  -1.371  1.00 27.19           N  
ANISOU 4331  ND2 ASN B 245     4705   2236   3388   -488   1750   -476       N  
ATOM   4332  N   GLN B 246      32.941  77.050  -1.065  1.00 22.16           N  
ANISOU 4332  N   GLN B 246     4086   1915   2417   -518   1306   -386       N  
ATOM   4333  CA  GLN B 246      31.806  77.258  -0.204  1.00 23.95           C  
ANISOU 4333  CA  GLN B 246     4263   2214   2621   -469   1181   -325       C  
ATOM   4334  C   GLN B 246      32.237  77.224   1.272  1.00 24.12           C  
ANISOU 4334  C   GLN B 246     4186   2220   2758   -327   1159   -261       C  
ATOM   4335  O   GLN B 246      31.746  78.030   2.043  1.00 23.58           O  
ANISOU 4335  O   GLN B 246     4072   2217   2670   -264   1045   -204       O  
ATOM   4336  CB  GLN B 246      30.672  76.268  -0.499  1.00 26.42           C  
ANISOU 4336  CB  GLN B 246     4616   2532   2888   -555   1196   -356       C  
ATOM   4337  CG  GLN B 246      29.288  76.822  -0.154  1.00 27.86           C  
ANISOU 4337  CG  GLN B 246     4773   2811   3000   -553   1049   -295       C  
ATOM   4338  CD  GLN B 246      28.843  78.087  -0.873  1.00 29.17           C  
ANISOU 4338  CD  GLN B 246     4962   3061   3059   -608    940   -263       C  
ATOM   4339  OE1 GLN B 246      29.459  78.597  -1.797  1.00 27.98           O  
ANISOU 4339  OE1 GLN B 246     4861   2911   2855   -670    962   -292       O  
ATOM   4340  NE2 GLN B 246      27.705  78.602  -0.466  1.00 29.86           N  
ANISOU 4340  NE2 GLN B 246     5007   3217   3120   -589    823   -195       N  
ATOM   4341  N   GLU B 247      33.146  76.318   1.671  1.00 22.73           N  
ANISOU 4341  N   GLU B 247     3973   1957   2704   -283   1270   -264       N  
ATOM   4342  CA  GLU B 247      33.621  76.295   3.077  1.00 22.55           C  
ANISOU 4342  CA  GLU B 247     3852   1931   2784   -162   1238   -187       C  
ATOM   4343  C   GLU B 247      34.382  77.583   3.449  1.00 21.12           C  
ANISOU 4343  C   GLU B 247     3635   1790   2598   -104   1162   -144       C  
ATOM   4344  O   GLU B 247      34.269  78.080   4.597  1.00 18.77           O  
ANISOU 4344  O   GLU B 247     3278   1542   2309    -30   1072    -82       O  
ATOM   4345  CB  GLU B 247      34.545  75.115   3.341  1.00 23.93           C  
ANISOU 4345  CB  GLU B 247     3982   2001   3107   -131   1372   -178       C  
ATOM   4346  CG  GLU B 247      34.553  74.666   4.777  1.00 26.75           C  
ANISOU 4346  CG  GLU B 247     4243   2365   3554    -37   1336    -91       C  
ATOM   4347  CD  GLU B 247      33.184  74.401   5.409  1.00 27.21           C  
ANISOU 4347  CD  GLU B 247     4300   2481   3556    -30   1259    -76       C  
ATOM   4348  OE1 GLU B 247      32.295  73.785   4.756  1.00 27.06           O  
ANISOU 4348  OE1 GLU B 247     4339   2451   3491   -101   1295   -133       O  
ATOM   4349  OE2 GLU B 247      32.994  74.849   6.558  1.00 27.78           O  
ANISOU 4349  OE2 GLU B 247     4317   2613   3624     37   1162     -8       O  
ATOM   4350  N   LYS B 248      35.183  78.106   2.512  1.00 20.54           N  
ANISOU 4350  N   LYS B 248     3601   1693   2510   -143   1205   -180       N  
ATOM   4351  CA  LYS B 248      35.879  79.385   2.745  1.00 20.85           C  
ANISOU 4351  CA  LYS B 248     3613   1769   2538    -98   1135   -147       C  
ATOM   4352  C   LYS B 248      34.857  80.517   2.956  1.00 19.14           C  
ANISOU 4352  C   LYS B 248     3408   1647   2215    -96   1001   -130       C  
ATOM   4353  O   LYS B 248      35.078  81.394   3.758  1.00 19.00           O  
ANISOU 4353  O   LYS B 248     3348   1668   2202    -37    927    -87       O  
ATOM   4354  CB  LYS B 248      36.828  79.720   1.594  1.00 21.80           C  
ANISOU 4354  CB  LYS B 248     3780   1845   2658   -148   1212   -192       C  
ATOM   4355  CG  LYS B 248      37.633  80.989   1.817  1.00 20.59           C  
ANISOU 4355  CG  LYS B 248     3594   1720   2506   -103   1149   -158       C  
ATOM   4356  CD  LYS B 248      38.657  80.889   2.943  1.00 20.52           C  
ANISOU 4356  CD  LYS B 248     3492   1688   2617    -17   1148    -89       C  
ATOM   4357  CE  LYS B 248      39.269  82.237   3.311  1.00 20.03           C  
ANISOU 4357  CE  LYS B 248     3401   1671   2537     18   1064    -56       C  
ATOM   4358  NZ  LYS B 248      40.167  82.171   4.503  1.00 20.17           N  
ANISOU 4358  NZ  LYS B 248     3326   1685   2652     84   1039     22       N  
ATOM   4359  N   ARG B 249      33.771  80.521   2.173  1.00 18.65           N  
ANISOU 4359  N   ARG B 249     3404   1618   2061   -171    977   -160       N  
ATOM   4360  CA  ARG B 249      32.743  81.541   2.311  1.00 18.61           C  
ANISOU 4360  CA  ARG B 249     3399   1692   1979   -169    862   -129       C  
ATOM   4361  C   ARG B 249      32.125  81.422   3.716  1.00 18.29           C  
ANISOU 4361  C   ARG B 249     3298   1676   1973    -92    807    -81       C  
ATOM   4362  O   ARG B 249      31.902  82.419   4.407  1.00 18.06           O  
ANISOU 4362  O   ARG B 249     3239   1688   1933    -44    734    -45       O  
ATOM   4363  CB  ARG B 249      31.720  81.385   1.173  1.00 18.74           C  
ANISOU 4363  CB  ARG B 249     3479   1739   1903   -276    848   -154       C  
ATOM   4364  CG  ARG B 249      32.216  81.782  -0.217  1.00 19.88           C  
ANISOU 4364  CG  ARG B 249     3690   1880   1983   -368    882   -193       C  
ATOM   4365  CD  ARG B 249      31.297  81.289  -1.338  1.00 20.78           C  
ANISOU 4365  CD  ARG B 249     3874   2021   1998   -501    884   -222       C  
ATOM   4366  NE  ARG B 249      31.593  81.823  -2.648  1.00 21.59           N  
ANISOU 4366  NE  ARG B 249     4045   2143   2014   -603    893   -246       N  
ATOM   4367  CZ  ARG B 249      30.932  81.544  -3.768  1.00 23.59           C  
ANISOU 4367  CZ  ARG B 249     4371   2432   2159   -746    889   -268       C  
ATOM   4368  NH1 ARG B 249      29.901  80.713  -3.768  1.00 22.50           N  
ANISOU 4368  NH1 ARG B 249     4246   2312   1988   -805    874   -271       N  
ATOM   4369  NH2 ARG B 249      31.282  82.139  -4.888  1.00 21.96           N  
ANISOU 4369  NH2 ARG B 249     4224   2249   1869   -837    892   -281       N  
ATOM   4370  N   HIS B 250      31.856  80.188   4.152  1.00 17.49           N  
ANISOU 4370  N   HIS B 250     3183   1544   1916    -84    853    -83       N  
ATOM   4371  CA  HIS B 250      31.316  79.938   5.477  1.00 18.09           C  
ANISOU 4371  CA  HIS B 250     3207   1642   2025    -18    812    -38       C  
ATOM   4372  C   HIS B 250      32.249  80.472   6.559  1.00 18.05           C  
ANISOU 4372  C   HIS B 250     3148   1642   2065     54    789      2       C  
ATOM   4373  O   HIS B 250      31.749  81.025   7.557  1.00 17.73           O  
ANISOU 4373  O   HIS B 250     3083   1646   2007     95    725     35       O  
ATOM   4374  CB  HIS B 250      31.037  78.443   5.779  1.00 17.54           C  
ANISOU 4374  CB  HIS B 250     3123   1530   2009    -19    876    -41       C  
ATOM   4375  CG  HIS B 250      30.006  77.804   4.907  1.00 19.42           C  
ANISOU 4375  CG  HIS B 250     3412   1767   2199    -99    895    -79       C  
ATOM   4376  ND1 HIS B 250      28.914  78.506   4.406  1.00 17.56           N  
ANISOU 4376  ND1 HIS B 250     3203   1589   1877   -146    817    -74       N  
ATOM   4377  CD2 HIS B 250      29.926  76.541   4.392  1.00 20.94           C  
ANISOU 4377  CD2 HIS B 250     3632   1905   2418   -153    985   -120       C  
ATOM   4378  CE1 HIS B 250      28.181  77.695   3.651  1.00 21.67           C  
ANISOU 4378  CE1 HIS B 250     3766   2103   2364   -231    845   -106       C  
ATOM   4379  NE2 HIS B 250      28.786  76.482   3.606  1.00 20.66           N  
ANISOU 4379  NE2 HIS B 250     3646   1904   2298   -240    953   -144       N  
ATOM   4380  N   GLN B 251      33.563  80.257   6.388  1.00 18.55           N  
ANISOU 4380  N   GLN B 251     3196   1661   2190     63    846      1       N  
ATOM   4381  CA  GLN B 251      34.556  80.731   7.351  1.00 17.90           C  
ANISOU 4381  CA  GLN B 251     3060   1589   2152    117    818     49       C  
ATOM   4382  C   GLN B 251      34.506  82.272   7.392  1.00 18.70           C  
ANISOU 4382  C   GLN B 251     3178   1741   2185    120    743     44       C  
ATOM   4383  O   GLN B 251      34.478  82.848   8.466  1.00 17.16           O  
ANISOU 4383  O   GLN B 251     2956   1586   1977    152    686     76       O  
ATOM   4384  CB  GLN B 251      35.968  80.283   6.990  1.00 19.19           C  
ANISOU 4384  CB  GLN B 251     3196   1689   2406    120    896     58       C  
ATOM   4385  CG  GLN B 251      36.996  80.503   8.099  1.00 19.41           C  
ANISOU 4385  CG  GLN B 251     3149   1729   2494    168    862    132       C  
ATOM   4386  CD  GLN B 251      38.418  80.434   7.589  1.00 19.20           C  
ANISOU 4386  CD  GLN B 251     3093   1644   2558    168    927    147       C  
ATOM   4387  OE1 GLN B 251      38.687  80.749   6.441  1.00 20.36           O  
ANISOU 4387  OE1 GLN B 251     3287   1757   2690    135    976     92       O  
ATOM   4388  NE2 GLN B 251      39.358  80.034   8.440  1.00 21.45           N  
ANISOU 4388  NE2 GLN B 251     3294   1916   2940    203    928    232       N  
ATOM   4389  N   LEU B 252      34.528  82.915   6.216  1.00 17.91           N  
ANISOU 4389  N   LEU B 252     3123   1636   2043     78    750      4       N  
ATOM   4390  CA  LEU B 252      34.525  84.408   6.140  1.00 17.98           C  
ANISOU 4390  CA  LEU B 252     3144   1683   2003     81    690      3       C  
ATOM   4391  C   LEU B 252      33.238  84.937   6.813  1.00 19.36           C  
ANISOU 4391  C   LEU B 252     3317   1903   2135     97    628     20       C  
ATOM   4392  O   LEU B 252      33.305  85.863   7.631  1.00 18.99           O  
ANISOU 4392  O   LEU B 252     3255   1881   2080    125    589     34       O  
ATOM   4393  CB  LEU B 252      34.638  84.876   4.684  1.00 17.83           C  
ANISOU 4393  CB  LEU B 252     3174   1653   1946     26    710    -31       C  
ATOM   4394  CG  LEU B 252      35.986  84.671   4.007  1.00 17.32           C  
ANISOU 4394  CG  LEU B 252     3115   1538   1924     12    779    -51       C  
ATOM   4395  CD1 LEU B 252      35.871  84.901   2.515  1.00 18.80           C  
ANISOU 4395  CD1 LEU B 252     3367   1720   2057    -61    808    -91       C  
ATOM   4396  CD2 LEU B 252      37.042  85.588   4.599  1.00 18.65           C  
ANISOU 4396  CD2 LEU B 252     3247   1713   2127     53    752    -27       C  
ATOM   4397  N   ALA B 253      32.088  84.304   6.526  1.00 18.04           N  
ANISOU 4397  N   ALA B 253     3164   1741   1946     74    628     17       N  
ATOM   4398  CA  ALA B 253      30.805  84.714   7.061  1.00 17.85           C  
ANISOU 4398  CA  ALA B 253     3132   1749   1899     88    582     40       C  
ATOM   4399  C   ALA B 253      30.782  84.587   8.589  1.00 19.06           C  
ANISOU 4399  C   ALA B 253     3253   1914   2073    139    571     62       C  
ATOM   4400  O   ALA B 253      30.311  85.506   9.285  1.00 19.12           O  
ANISOU 4400  O   ALA B 253     3254   1942   2067    160    543     72       O  
ATOM   4401  CB  ALA B 253      29.656  83.977   6.400  1.00 18.43           C  
ANISOU 4401  CB  ALA B 253     3222   1827   1953     45    582     41       C  
ATOM   4402  N   GLY B 254      31.314  83.487   9.122  1.00 18.46           N  
ANISOU 4402  N   GLY B 254     3155   1823   2033    154    600     72       N  
ATOM   4403  CA  GLY B 254      31.334  83.292  10.559  1.00 19.67           C  
ANISOU 4403  CA  GLY B 254     3279   1997   2197    188    585    103       C  
ATOM   4404  C   GLY B 254      32.248  84.279  11.273  1.00 20.17           C  
ANISOU 4404  C   GLY B 254     3333   2082   2247    198    557    111       C  
ATOM   4405  O   GLY B 254      31.983  84.665  12.404  1.00 19.44           O  
ANISOU 4405  O   GLY B 254     3237   2019   2127    207    534    124       O  
ATOM   4406  N   LYS B 255      33.384  84.616  10.656  1.00 20.67           N  
ANISOU 4406  N   LYS B 255     3395   2129   2328    187    566    103       N  
ATOM   4407  CA  LYS B 255      34.341  85.551  11.257  1.00 21.19           C  
ANISOU 4407  CA  LYS B 255     3451   2216   2383    186    537    112       C  
ATOM   4408  C   LYS B 255      33.758  86.967  11.242  1.00 20.43           C  
ANISOU 4408  C   LYS B 255     3388   2134   2240    180    516     80       C  
ATOM   4409  O   LYS B 255      34.008  87.764  12.176  1.00 19.99           O  
ANISOU 4409  O   LYS B 255     3336   2104   2156    173    495     79       O  
ATOM   4410  CB  LYS B 255      35.690  85.474  10.537  1.00 22.82           C  
ANISOU 4410  CB  LYS B 255     3639   2392   2637    180    559    117       C  
ATOM   4411  CG  LYS B 255      36.378  84.142  10.699  1.00 23.54           C  
ANISOU 4411  CG  LYS B 255     3684   2457   2803    190    594    162       C  
ATOM   4412  CD  LYS B 255      36.666  83.843  12.123  1.00 25.30           C  
ANISOU 4412  CD  LYS B 255     3862   2719   3031    198    555    224       C  
ATOM   4413  CE  LYS B 255      37.378  82.523  12.293  1.00 30.42           C  
ANISOU 4413  CE  LYS B 255     4446   3335   3775    212    592    290       C  
ATOM   4414  NZ  LYS B 255      37.947  82.446  13.655  1.00 31.47           N  
ANISOU 4414  NZ  LYS B 255     4526   3519   3911    206    535    372       N  
ATOM   4415  N   TYR B 256      32.963  87.265  10.208  1.00 19.77           N  
ANISOU 4415  N   TYR B 256     3326   2034   2149    174    526     59       N  
ATOM   4416  CA  TYR B 256      32.267  88.511  10.139  1.00 19.57           C  
ANISOU 4416  CA  TYR B 256     3318   2012   2104    173    515     47       C  
ATOM   4417  C   TYR B 256      31.151  88.536  11.207  1.00 20.60           C  
ANISOU 4417  C   TYR B 256     3447   2154   2223    188    516     54       C  
ATOM   4418  O   TYR B 256      30.976  89.535  11.880  1.00 18.05           O  
ANISOU 4418  O   TYR B 256     3135   1832   1890    188    522     41       O  
ATOM   4419  CB  TYR B 256      31.695  88.813   8.744  1.00 21.86           C  
ANISOU 4419  CB  TYR B 256     3620   2288   2395    155    515     46       C  
ATOM   4420  CG  TYR B 256      31.058  90.174   8.759  1.00 23.48           C  
ANISOU 4420  CG  TYR B 256     3826   2490   2604    160    508     51       C  
ATOM   4421  CD1 TYR B 256      31.838  91.320   8.730  1.00 25.36           C  
ANISOU 4421  CD1 TYR B 256     4070   2720   2845    159    510     35       C  
ATOM   4422  CD2 TYR B 256      29.696  90.327   8.956  1.00 24.69           C  
ANISOU 4422  CD2 TYR B 256     3967   2640   2771    170    509     76       C  
ATOM   4423  CE1 TYR B 256      31.273  92.582   8.874  1.00 25.68           C  
ANISOU 4423  CE1 TYR B 256     4106   2744   2905    167    521     40       C  
ATOM   4424  CE2 TYR B 256      29.114  91.581   9.081  1.00 24.88           C  
ANISOU 4424  CE2 TYR B 256     3981   2646   2823    180    520     88       C  
ATOM   4425  CZ  TYR B 256      29.907  92.714   9.066  1.00 26.33           C  
ANISOU 4425  CZ  TYR B 256     4174   2817   3014    179    531     68       C  
ATOM   4426  OH  TYR B 256      29.350  93.953   9.218  1.00 28.51           O  
ANISOU 4426  OH  TYR B 256     4437   3061   3333    190    558     79       O  
ATOM   4427  N   THR B 257      30.344  87.470  11.293  1.00 18.43           N  
ANISOU 4427  N   THR B 257     3164   1881   1956    195    521     71       N  
ATOM   4428  CA  THR B 257      29.329  87.343  12.345  1.00 19.12           C  
ANISOU 4428  CA  THR B 257     3249   1976   2038    210    530     81       C  
ATOM   4429  C   THR B 257      29.961  87.658  13.710  1.00 18.31           C  
ANISOU 4429  C   THR B 257     3154   1896   1904    205    530     74       C  
ATOM   4430  O   THR B 257      29.388  88.419  14.524  1.00 16.69           O  
ANISOU 4430  O   THR B 257     2968   1690   1683    201    550     58       O  
ATOM   4431  CB  THR B 257      28.694  85.948  12.396  1.00 17.73           C  
ANISOU 4431  CB  THR B 257     3058   1802   1876    218    534    103       C  
ATOM   4432  OG1 THR B 257      28.005  85.698  11.173  1.00 17.87           O  
ANISOU 4432  OG1 THR B 257     3075   1805   1907    203    531    108       O  
ATOM   4433  CG2 THR B 257      27.685  85.845  13.528  1.00 19.42           C  
ANISOU 4433  CG2 THR B 257     3270   2022   2084    234    548    114       C  
ATOM   4434  N   THR B 258      31.133  87.066  13.957  1.00 17.00           N  
ANISOU 4434  N   THR B 258     2975   1749   1734    195    512     88       N  
ATOM   4435  CA  THR B 258      31.864  87.291  15.231  1.00 17.54           C  
ANISOU 4435  CA  THR B 258     3046   1852   1763    171    495     96       C  
ATOM   4436  C   THR B 258      32.147  88.789  15.376  1.00 19.69           C  
ANISOU 4436  C   THR B 258     3351   2124   2006    146    500     56       C  
ATOM   4437  O   THR B 258      31.890  89.337  16.462  1.00 19.12           O  
ANISOU 4437  O   THR B 258     3308   2070   1887    117    512     37       O  
ATOM   4438  CB  THR B 258      33.164  86.481  15.279  1.00 18.31           C  
ANISOU 4438  CB  THR B 258     3107   1967   1883    163    469    140       C  
ATOM   4439  OG1 THR B 258      32.828  85.095  15.221  1.00 19.23           O  
ANISOU 4439  OG1 THR B 258     3192   2075   2039    186    480    177       O  
ATOM   4440  CG2 THR B 258      33.985  86.764  16.518  1.00 19.80           C  
ANISOU 4440  CG2 THR B 258     3293   2205   2023    121    435    164       C  
ATOM   4441  N   ARG B 259      32.662  89.410  14.310  1.00 21.29           N  
ANISOU 4441  N   ARG B 259     3551   2302   2235    151    498     41       N  
ATOM   4442  CA  ARG B 259      32.969  90.864  14.319  1.00 22.60           C  
ANISOU 4442  CA  ARG B 259     3741   2457   2387    131    508      4       C  
ATOM   4443  C   ARG B 259      31.680  91.635  14.621  1.00 21.50           C  
ANISOU 4443  C   ARG B 259     3627   2291   2250    137    554    -21       C  
ATOM   4444  O   ARG B 259      31.726  92.554  15.457  1.00 20.95           O  
ANISOU 4444  O   ARG B 259     3589   2217   2151    106    582    -57       O  
ATOM   4445  CB  ARG B 259      33.583  91.284  12.979  1.00 23.28           C  
ANISOU 4445  CB  ARG B 259     3817   2519   2508    140    502      0       C  
ATOM   4446  CG  ARG B 259      33.042  92.592  12.421  1.00 29.83           C  
ANISOU 4446  CG  ARG B 259     4662   3314   3355    143    528    -25       C  
ATOM   4447  CD  ARG B 259      33.477  93.803  13.220  1.00 34.52           C  
ANISOU 4447  CD  ARG B 259     5282   3904   3928    114    547    -61       C  
ATOM   4448  NE  ARG B 259      33.168  95.049  12.534  1.00 35.86           N  
ANISOU 4448  NE  ARG B 259     5457   4031   4138    123    581    -77       N  
ATOM   4449  CZ  ARG B 259      32.048  95.742  12.697  1.00 38.21           C  
ANISOU 4449  CZ  ARG B 259     5759   4290   4469    135    632    -82       C  
ATOM   4450  NH1 ARG B 259      32.078  96.910  13.315  1.00 36.43           N  
ANISOU 4450  NH1 ARG B 259     5557   4033   4251    114    682   -123       N  
ATOM   4451  NH2 ARG B 259      30.904  95.272  12.234  1.00 30.03           N  
ANISOU 4451  NH2 ARG B 259     4699   3242   3468    166    637    -45       N  
ATOM   4452  N   LEU B 260      30.578  91.255  13.967  1.00 21.21           N  
ANISOU 4452  N   LEU B 260     3574   2230   2252    170    567     -2       N  
ATOM   4453  CA  LEU B 260      29.292  91.900  14.170  1.00 22.35           C  
ANISOU 4453  CA  LEU B 260     3723   2340   2427    183    615     -6       C  
ATOM   4454  C   LEU B 260      28.846  91.820  15.646  1.00 22.85           C  
ANISOU 4454  C   LEU B 260     3815   2412   2455    167    652    -27       C  
ATOM   4455  O   LEU B 260      28.418  92.794  16.233  1.00 22.21           O  
ANISOU 4455  O   LEU B 260     3759   2298   2380    153    712    -59       O  
ATOM   4456  CB  LEU B 260      28.307  91.264  13.189  1.00 22.22           C  
ANISOU 4456  CB  LEU B 260     3675   2312   2455    211    602     36       C  
ATOM   4457  CG  LEU B 260      26.901  91.831  13.141  1.00 27.52           C  
ANISOU 4457  CG  LEU B 260     4327   2943   3185    230    642     60       C  
ATOM   4458  CD1 LEU B 260      26.909  93.281  12.673  1.00 29.00           C  
ANISOU 4458  CD1 LEU B 260     4508   3090   3419    231    671     58       C  
ATOM   4459  CD2 LEU B 260      26.034  90.987  12.214  1.00 24.99           C  
ANISOU 4459  CD2 LEU B 260     3972   2629   2892    240    609    112       C  
ATOM   4460  N   LEU B 261      28.995  90.669  16.290  1.00 25.22           N  
ANISOU 4460  N   LEU B 261     4113   2752   2716    160    625     -9       N  
ATOM   4461  CA  LEU B 261      28.573  90.501  17.683  1.00 24.00           C  
ANISOU 4461  CA  LEU B 261     3988   2613   2515    135    657    -22       C  
ATOM   4462  C   LEU B 261      29.531  91.205  18.656  1.00 26.55           C  
ANISOU 4462  C   LEU B 261     4355   2966   2763     69    659    -60       C  
ATOM   4463  O   LEU B 261      29.101  91.641  19.749  1.00 25.14           O  
ANISOU 4463  O   LEU B 261     4224   2787   2540     28    713    -96       O  
ATOM   4464  CB  LEU B 261      28.497  89.011  18.005  1.00 25.23           C  
ANISOU 4464  CB  LEU B 261     4121   2807   2657    147    621     21       C  
ATOM   4465  CG  LEU B 261      27.359  88.258  17.321  1.00 26.14           C  
ANISOU 4465  CG  LEU B 261     4203   2895   2832    195    629     51       C  
ATOM   4466  CD1 LEU B 261      27.510  86.778  17.600  1.00 31.05           C  
ANISOU 4466  CD1 LEU B 261     4801   3550   3446    202    598     91       C  
ATOM   4467  CD2 LEU B 261      25.994  88.736  17.788  1.00 26.49           C  
ANISOU 4467  CD2 LEU B 261     4258   2901   2903    207    694     41       C  
ATOM   4468  N   ARG B 262      30.808  91.368  18.291  1.00 25.05           N  
ANISOU 4468  N   ARG B 262     4156   2802   2557     49    608    -56       N  
ATOM   4469  CA  ARG B 262      31.772  92.018  19.217  1.00 27.59           C  
ANISOU 4469  CA  ARG B 262     4517   3163   2803    -27    597    -84       C  
ATOM   4470  C   ARG B 262      31.678  93.554  19.114  1.00 28.06           C  
ANISOU 4470  C   ARG B 262     4617   3172   2871    -50    660   -151       C  
ATOM   4471  O   ARG B 262      31.817  94.246  20.112  1.00 31.43           O  
ANISOU 4471  O   ARG B 262     5100   3608   3233   -122    698   -200       O  
ATOM   4472  CB  ARG B 262      33.220  91.621  18.918  1.00 31.81           C  
ANISOU 4472  CB  ARG B 262     5015   3741   3329    -44    519    -42       C  
ATOM   4473  CG  ARG B 262      33.638  90.220  19.330  1.00 33.96           C  
ANISOU 4473  CG  ARG B 262     5245   4066   3591    -44    461     31       C  
ATOM   4474  CD  ARG B 262      35.109  89.948  19.038  1.00 35.63           C  
ANISOU 4474  CD  ARG B 262     5410   4307   3820    -60    397     83       C  
ATOM   4475  NE  ARG B 262      35.563  88.658  19.558  1.00 45.43           N  
ANISOU 4475  NE  ARG B 262     6599   5593   5066    -65    349    169       N  
ATOM   4476  CZ  ARG B 262      36.376  87.800  18.918  1.00 55.54           C  
ANISOU 4476  CZ  ARG B 262     7811   6865   6425    -31    321    235       C  
ATOM   4477  NH1 ARG B 262      36.920  88.119  17.749  1.00 46.78           N  
ANISOU 4477  NH1 ARG B 262     6685   5711   5377      1    333    218       N  
ATOM   4478  NH2 ARG B 262      36.631  86.615  19.449  1.00 44.58           N  
ANISOU 4478  NH2 ARG B 262     6371   5508   5059    -31    292    321       N  
ATOM   4479  N   HIS B 263      31.485  94.093  17.903  1.00 26.63           N  
ANISOU 4479  N   HIS B 263     4408   2938   2770      2    675   -151       N  
ATOM   4480  CA  HIS B 263      31.634  95.550  17.658  1.00 30.31           C  
ANISOU 4480  CA  HIS B 263     4898   3355   3261    -15    728   -201       C  
ATOM   4481  C   HIS B 263      30.489  96.137  16.831  1.00 27.80           C  
ANISOU 4481  C   HIS B 263     4555   2962   3043     44    789   -193       C  
ATOM   4482  O   HIS B 263      30.538  97.312  16.538  1.00 26.64           O  
ANISOU 4482  O   HIS B 263     4416   2764   2939     39    839   -221       O  
ATOM   4483  CB  HIS B 263      32.972  95.876  16.969  1.00 33.05           C  
ANISOU 4483  CB  HIS B 263     5228   3721   3608    -26    671   -195       C  
ATOM   4484  CG  HIS B 263      34.139  95.588  17.855  1.00 38.57           C  
ANISOU 4484  CG  HIS B 263     5944   4488   4222    -98    615   -194       C  
ATOM   4485  ND1 HIS B 263      34.191  96.002  19.173  1.00 42.33           N  
ANISOU 4485  ND1 HIS B 263     6479   4989   4613   -183    643   -238       N  
ATOM   4486  CD2 HIS B 263      35.276  94.905  17.638  1.00 41.02           C  
ANISOU 4486  CD2 HIS B 263     6217   4848   4521   -105    535   -145       C  
ATOM   4487  CE1 HIS B 263      35.317  95.586  19.726  1.00 45.37           C  
ANISOU 4487  CE1 HIS B 263     6858   5447   4931   -244    566   -207       C  
ATOM   4488  NE2 HIS B 263      36.001  94.909  18.799  1.00 42.16           N  
ANISOU 4488  NE2 HIS B 263     6386   5052   4579   -191    501   -145       N  
ATOM   4489  N   GLY B 264      29.450  95.364  16.512  1.00 24.17           N  
ANISOU 4489  N   GLY B 264     4063   2493   2626     93    788   -149       N  
ATOM   4490  CA  GLY B 264      28.323  95.885  15.716  1.00 26.82           C  
ANISOU 4490  CA  GLY B 264     4360   2764   3063    142    834   -118       C  
ATOM   4491  C   GLY B 264      27.610  97.053  16.405  1.00 28.64           C  
ANISOU 4491  C   GLY B 264     4616   2921   3343    130    951   -157       C  
ATOM   4492  O   GLY B 264      27.679  97.213  17.637  1.00 27.69           O  
ANISOU 4492  O   GLY B 264     4554   2802   3165     80   1006   -216       O  
ATOM   4493  N   GLN B 265      26.849  97.811  15.605  1.00 27.97           N  
ANISOU 4493  N   GLN B 265     4485   2770   3372    170    994   -118       N  
ATOM   4494  CA  GLN B 265      25.923  98.886  16.064  1.00 32.88           C  
ANISOU 4494  CA  GLN B 265     5105   3295   4090    176   1125   -132       C  
ATOM   4495  C   GLN B 265      24.918  98.288  17.075  1.00 31.40           C  
ANISOU 4495  C   GLN B 265     4935   3094   3900    177   1186   -140       C  
ATOM   4496  O   GLN B 265      24.445  97.177  16.886  1.00 29.25           O  
ANISOU 4496  O   GLN B 265     4634   2864   3615    204   1124    -90       O  
ATOM   4497  CB  GLN B 265      25.294  99.448  14.780  1.00 38.01           C  
ANISOU 4497  CB  GLN B 265     5673   3896   4870    229   1122    -44       C  
ATOM   4498  CG  GLN B 265      24.233 100.514  14.955  1.00 51.07           C  
ANISOU 4498  CG  GLN B 265     7291   5439   6671    253   1254    -21       C  
ATOM   4499  CD  GLN B 265      24.816 101.899  15.042  1.00 54.81           C  
ANISOU 4499  CD  GLN B 265     7789   5848   7188    230   1339    -73       C  
ATOM   4500  OE1 GLN B 265      26.002 102.103  14.771  1.00 57.78           O  
ANISOU 4500  OE1 GLN B 265     8196   6267   7488    200   1281   -113       O  
ATOM   4501  NE2 GLN B 265      23.976 102.846  15.438  1.00 52.84           N  
ANISOU 4501  NE2 GLN B 265     7520   5485   7069    242   1486    -71       N  
ATOM   4502  N   LYS B 266      24.633  98.985  18.183  1.00 28.03           N  
ANISOU 4502  N   LYS B 266     4563   2608   3478    139   1314   -209       N  
ATOM   4503  CA  LYS B 266      23.612  98.554  19.172  1.00 32.69           C  
ANISOU 4503  CA  LYS B 266     5174   3170   4075    136   1397   -221       C  
ATOM   4504  C   LYS B 266      23.773  97.073  19.548  1.00 31.09           C  
ANISOU 4504  C   LYS B 266     4985   3065   3759    128   1295   -206       C  
ATOM   4505  O   LYS B 266      22.772  96.346  19.671  1.00 28.71           O  
ANISOU 4505  O   LYS B 266     4652   2756   3498    164   1306   -161       O  
ATOM   4506  CB  LYS B 266      22.210  98.790  18.599  1.00 33.20           C  
ANISOU 4506  CB  LYS B 266     5153   3148   4311    207   1460   -136       C  
ATOM   4507  CG  LYS B 266      21.951 100.237  18.218  1.00 37.97           C  
ANISOU 4507  CG  LYS B 266     5725   3642   5057    222   1571   -129       C  
ATOM   4508  CD  LYS B 266      20.617 100.477  17.550  1.00 43.98           C  
ANISOU 4508  CD  LYS B 266     6379   4323   6006    293   1618    -15       C  
ATOM   4509  CE  LYS B 266      20.412 101.940  17.217  1.00 50.82           C  
ANISOU 4509  CE  LYS B 266     7206   5073   7030    309   1737      3       C  
ATOM   4510  NZ  LYS B 266      19.185 102.128  16.411  1.00 59.75           N  
ANISOU 4510  NZ  LYS B 266     8209   6139   8354    376   1754    148       N  
ATOM   4511  N   LYS B 267      25.012  96.625  19.777  1.00 31.03           N  
ANISOU 4511  N   LYS B 267     5018   3146   3623     80   1204   -238       N  
ATOM   4512  CA  LYS B 267      25.258  95.177  20.018  1.00 32.91           C  
ANISOU 4512  CA  LYS B 267     5254   3474   3775     79   1104   -206       C  
ATOM   4513  C   LYS B 267      24.536  94.705  21.300  1.00 31.77           C  
ANISOU 4513  C   LYS B 267     5154   3330   3585     49   1172   -230       C  
ATOM   4514  O   LYS B 267      24.144  93.528  21.369  1.00 28.73           O  
ANISOU 4514  O   LYS B 267     4743   2986   3187     77   1121   -183       O  
ATOM   4515  CB  LYS B 267      26.753  94.874  20.098  1.00 33.69           C  
ANISOU 4515  CB  LYS B 267     5377   3657   3765     30   1006   -221       C  
ATOM   4516  CG  LYS B 267      27.440  95.384  21.352  1.00 38.55           C  
ANISOU 4516  CG  LYS B 267     6075   4299   4270    -68   1044   -294       C  
ATOM   4517  CD  LYS B 267      28.915  95.114  21.365  1.00 45.48           C  
ANISOU 4517  CD  LYS B 267     6959   5260   5059   -116    937   -288       C  
ATOM   4518  CE  LYS B 267      29.533  95.486  22.694  1.00 54.59           C  
ANISOU 4518  CE  LYS B 267     8195   6459   6086   -234    958   -346       C  
ATOM   4519  NZ  LYS B 267      30.998  95.676  22.584  1.00 60.26           N  
ANISOU 4519  NZ  LYS B 267     8913   7238   6743   -288    869   -341       N  
ATOM   4520  N   ASN B 268      24.364  95.603  22.289  1.00 30.88           N  
ANISOU 4520  N   ASN B 268     5113   3171   3450    -11   1293   -306       N  
ATOM   4521  CA  ASN B 268      23.652  95.296  23.559  1.00 32.70           C  
ANISOU 4521  CA  ASN B 268     5399   3392   3631    -54   1381   -340       C  
ATOM   4522  C   ASN B 268      22.215  95.853  23.540  1.00 30.00           C  
ANISOU 4522  C   ASN B 268     5033   2931   3435     -4   1527   -335       C  
ATOM   4523  O   ASN B 268      21.667  96.247  24.576  1.00 30.80           O  
ANISOU 4523  O   ASN B 268     5199   2979   3524    -53   1664   -396       O  
ATOM   4524  CB  ASN B 268      24.482  95.741  24.772  1.00 35.11           C  
ANISOU 4524  CB  ASN B 268     5812   3739   3788   -179   1417   -429       C  
ATOM   4525  CG  ASN B 268      25.753  94.925  24.922  1.00 38.54           C  
ANISOU 4525  CG  ASN B 268     6251   4300   4090   -226   1263   -400       C  
ATOM   4526  OD1 ASN B 268      25.774  93.742  24.611  1.00 46.48           O  
ANISOU 4526  OD1 ASN B 268     7312   5350   4999   -317   1242   -446       O  
ATOM   4527  ND2 ASN B 268      26.827  95.542  25.403  1.00 38.82           N  
ANISOU 4527  ND2 ASN B 268     6225   4392   4131   -169   1158   -319       N  
ATOM   4528  N   PHE B 269      21.552  95.798  22.378  1.00 27.86           N  
ANISOU 4528  N   PHE B 269     4663   2616   3303     88   1498   -253       N  
ATOM   4529  CA  PHE B 269      20.203  96.403  22.239  1.00 29.32           C  
ANISOU 4529  CA  PHE B 269     4801   2682   3656    141   1630   -222       C  
ATOM   4530  C   PHE B 269      19.181  95.734  23.165  1.00 27.74           C  
ANISOU 4530  C   PHE B 269     4617   2462   3460    142   1706   -220       C  
ATOM   4531  O   PHE B 269      18.237  96.380  23.623  1.00 28.69           O  
ANISOU 4531  O   PHE B 269     4740   2475   3686    148   1865   -235       O  
ATOM   4532  CB  PHE B 269      19.719  96.342  20.787  1.00 28.97           C  
ANISOU 4532  CB  PHE B 269     4640   2620   3745    225   1555   -112       C  
ATOM   4533  CG  PHE B 269      19.382  94.955  20.325  1.00 28.66           C  
ANISOU 4533  CG  PHE B 269     4550   2653   3685    265   1432    -37       C  
ATOM   4534  CD1 PHE B 269      20.371  94.093  19.890  1.00 27.68           C  
ANISOU 4534  CD1 PHE B 269     4433   2632   3450    253   1288    -32       C  
ATOM   4535  CD2 PHE B 269      18.069  94.510  20.339  1.00 31.59           C  
ANISOU 4535  CD2 PHE B 269     4864   2981   4158    310   1472     29       C  
ATOM   4536  CE1 PHE B 269      20.049  92.807  19.478  1.00 30.69           C  
ANISOU 4536  CE1 PHE B 269     4772   3068   3819    282   1194     27       C  
ATOM   4537  CE2 PHE B 269      17.756  93.220  19.942  1.00 30.56           C  
ANISOU 4537  CE2 PHE B 269     4691   2915   4005    337   1365     90       C  
ATOM   4538  CZ  PHE B 269      18.748  92.369  19.530  1.00 30.37           C  
ANISOU 4538  CZ  PHE B 269     4683   2989   3866    321   1231     84       C  
ATOM   4539  N   ALA B 270      19.348  94.439  23.451  1.00 25.51           N  
ANISOU 4539  N   ALA B 270     4343   2275   3074    136   1603   -198       N  
ATOM   4540  CA  ALA B 270      18.270  93.640  24.073  1.00 24.98           C  
ANISOU 4540  CA  ALA B 270     4266   2192   3032    157   1652   -170       C  
ATOM   4541  C   ALA B 270      17.875  94.132  25.480  1.00 25.67           C  
ANISOU 4541  C   ALA B 270     4447   2223   3081     89   1822   -257       C  
ATOM   4542  O   ALA B 270      16.679  94.145  25.822  1.00 25.44           O  
ANISOU 4542  O   ALA B 270     4398   2112   3156    121   1940   -238       O  
ATOM   4543  CB  ALA B 270      18.664  92.176  24.082  1.00 23.44           C  
ANISOU 4543  CB  ALA B 270     4061   2110   2733    161   1508   -131       C  
ATOM   4544  N   ASN B 271      18.850  94.486  26.317  1.00 25.09           N  
ANISOU 4544  N   ASN B 271     4479   2197   2856    -11   1837   -348       N  
ATOM   4545  CA  ASN B 271      18.573  94.972  27.654  1.00 28.04           C  
ANISOU 4545  CA  ASN B 271     4961   2526   3165   -102   2000   -443       C  
ATOM   4546  C   ASN B 271      18.662  96.515  27.714  1.00 28.92           C  
ANISOU 4546  C   ASN B 271     5118   2530   3341   -143   2154   -526       C  
ATOM   4547  O   ASN B 271      18.719  97.084  28.780  1.00 28.91           O  
ANISOU 4547  O   ASN B 271     5227   2495   3260   -246   2291   -628       O  
ATOM   4548  CB  ASN B 271      19.515  94.364  28.701  1.00 29.35           C  
ANISOU 4548  CB  ASN B 271     5226   2819   3107   -217   1929   -491       C  
ATOM   4549  CG  ASN B 271      19.307  92.877  28.870  1.00 29.15           C  
ANISOU 4549  CG  ASN B 271     5163   2881   3030   -184   1817   -414       C  
ATOM   4550  OD1 ASN B 271      18.276  92.439  29.376  1.00 33.88           O  
ANISOU 4550  OD1 ASN B 271     5761   3440   3670   -163   1899   -400       O  
ATOM   4551  ND2 ASN B 271      20.271  92.092  28.431  1.00 28.98           N  
ANISOU 4551  ND2 ASN B 271     5105   2970   2934   -177   1639   -360       N  
ATOM   4552  N   SER B 272      18.682  97.184  26.564  1.00 30.40           N  
ANISOU 4552  N   SER B 272     5222   2661   3667    -70   2135   -481       N  
ATOM   4553  CA  SER B 272      18.808  98.650  26.507  1.00 32.45           C  
ANISOU 4553  CA  SER B 272     5509   2811   4007    -99   2277   -548       C  
ATOM   4554  C   SER B 272      17.451  99.309  26.765  1.00 35.49           C  
ANISOU 4554  C   SER B 272     5869   3031   4583    -61   2497   -547       C  
ATOM   4555  O   SER B 272      16.418  98.650  26.874  1.00 32.51           O  
ANISOU 4555  O   SER B 272     5442   2627   4282     -4   2524   -484       O  
ATOM   4556  CB  SER B 272      19.374  99.059  25.173  1.00 31.77           C  
ANISOU 4556  CB  SER B 272     5338   2734   3997    -37   2166   -487       C  
ATOM   4557  OG  SER B 272      18.375  98.980  24.157  1.00 30.76           O  
ANISOU 4557  OG  SER B 272     5079   2543   4063     79   2157   -368       O  
ATOM   4558  N   LYS B 273      17.470 100.644  26.826  1.00 40.15           N  
ANISOU 4558  N   LYS B 273     6487   3501   5264    -90   2660   -611       N  
ATOM   4559  CA  LYS B 273      16.279 101.432  27.071  1.00 42.31           C  
ANISOU 4559  CA  LYS B 273     6734   3596   5745    -57   2897   -612       C  
ATOM   4560  C   LYS B 273      15.581 101.836  25.759  1.00 40.24           C  
ANISOU 4560  C   LYS B 273     6303   3247   5736     74   2882   -469       C  
ATOM   4561  O   LYS B 273      14.693 102.659  25.762  1.00 42.27           O  
ANISOU 4561  O   LYS B 273     6511   3344   6204    111   3073   -446       O  
ATOM   4562  CB  LYS B 273      16.678 102.605  27.969  1.00 45.81           C  
ANISOU 4562  CB  LYS B 273     7309   3951   6145   -176   3101   -768       C  
ATOM   4563  CG  LYS B 273      16.879 102.186  29.420  1.00 47.32           C  
ANISOU 4563  CG  LYS B 273     7660   4198   6120   -314   3167   -892       C  
ATOM   4564  N   MET B 274      15.956 101.207  24.646  1.00 36.14           N  
ANISOU 4564  N   MET B 274     5694   2836   5198    138   2658   -364       N  
ATOM   4565  CA  MET B 274      15.213 101.258  23.388  1.00 34.81           C  
ANISOU 4565  CA  MET B 274     5365   2626   5235    251   2599   -204       C  
ATOM   4566  C   MET B 274      13.740 100.884  23.650  1.00 34.64           C  
ANISOU 4566  C   MET B 274     5270   2517   5372    309   2702   -124       C  
ATOM   4567  O   MET B 274      13.445  99.932  24.353  1.00 33.62           O  
ANISOU 4567  O   MET B 274     5187   2441   5146    291   2686   -147       O  
ATOM   4568  CB  MET B 274      15.851 100.251  22.423  1.00 36.64           C  
ANISOU 4568  CB  MET B 274     5550   3017   5353    280   2336   -131       C  
ATOM   4569  CG  MET B 274      15.661 100.504  20.961  1.00 37.49           C  
ANISOU 4569  CG  MET B 274     5523   3119   5600    354   2234      5       C  
ATOM   4570  SD  MET B 274      16.671  99.365  19.970  1.00 40.59           S  
ANISOU 4570  SD  MET B 274     5906   3698   5818    356   1954     44       S  
ATOM   4571  CE  MET B 274      18.265  99.520  20.767  1.00 36.60           C  
ANISOU 4571  CE  MET B 274     5549   3267   5088    260   1935   -116       C  
ATOM   4572  N   LYS B 275      12.816 101.652  23.075  1.00 33.87           N  
ANISOU 4572  N   LYS B 275     5052   2285   5532    379   2808    -17       N  
ATOM   4573  CA  LYS B 275      11.400 101.363  23.044  1.00 36.41           C  
ANISOU 4573  CA  LYS B 275     5264   2521   6047    449   2883    100       C  
ATOM   4574  C   LYS B 275      11.138  99.975  22.442  1.00 34.50           C  
ANISOU 4574  C   LYS B 275     4956   2415   5735    489   2661    204       C  
ATOM   4575  O   LYS B 275      11.762  99.594  21.454  1.00 33.54           O  
ANISOU 4575  O   LYS B 275     4798   2408   5535    499   2458    257       O  
ATOM   4576  CB  LYS B 275      10.726 102.427  22.184  1.00 41.95           C  
ANISOU 4576  CB  LYS B 275     5818   3086   7032    519   2969    234       C  
ATOM   4577  CG  LYS B 275       9.212 102.398  22.150  1.00 50.99           C  
ANISOU 4577  CG  LYS B 275     6830   4111   8432    591   3080    375       C  
ATOM   4578  CD  LYS B 275       8.633 103.750  21.771  1.00 58.60           C  
ANISOU 4578  CD  LYS B 275     7680   4892   9692    638   3259    466       C  
ATOM   4579  CE  LYS B 275       8.827 104.103  20.310  1.00 65.60           C  
ANISOU 4579  CE  LYS B 275     8429   5824  10669    683   3092    625       C  
ATOM   4580  NZ  LYS B 275       7.616 103.768  19.521  1.00 75.90           N  
ANISOU 4580  NZ  LYS B 275     9545   7108  12183    756   3025    852       N  
ATOM   4581  N   TYR B 276      10.151  99.257  22.993  1.00 33.86           N  
ANISOU 4581  N   TYR B 276     4855   2309   5701    510   2713    238       N  
ATOM   4582  CA  TYR B 276       9.866  97.918  22.547  1.00 32.64           C  
ANISOU 4582  CA  TYR B 276     4649   2273   5479    538   2525    322       C  
ATOM   4583  C   TYR B 276       9.694  97.856  21.023  1.00 31.56           C  
ANISOU 4583  C   TYR B 276     4369   2180   5439    590   2353    484       C  
ATOM   4584  O   TYR B 276      10.298  96.990  20.414  1.00 29.47           O  
ANISOU 4584  O   TYR B 276     4114   2055   5026    577   2153    494       O  
ATOM   4585  CB  TYR B 276       8.641  97.303  23.224  1.00 33.01           C  
ANISOU 4585  CB  TYR B 276     4664   2261   5616    566   2621    363       C  
ATOM   4586  CG  TYR B 276       8.336  95.901  22.745  1.00 31.08           C  
ANISOU 4586  CG  TYR B 276     4366   2137   5306    591   2428    448       C  
ATOM   4587  CD1 TYR B 276       9.071  94.819  23.208  1.00 28.91           C  
ANISOU 4587  CD1 TYR B 276     4193   1994   4795    547   2314    361       C  
ATOM   4588  CD2 TYR B 276       7.318  95.648  21.834  1.00 30.21           C  
ANISOU 4588  CD2 TYR B 276     4100   2007   5371    651   2360    622       C  
ATOM   4589  CE1 TYR B 276       8.789  93.521  22.821  1.00 28.61           C  
ANISOU 4589  CE1 TYR B 276     4111   2052   4704    566   2158    430       C  
ATOM   4590  CE2 TYR B 276       7.034  94.350  21.427  1.00 30.64           C  
ANISOU 4590  CE2 TYR B 276     4115   2167   5357    659   2192    688       C  
ATOM   4591  CZ  TYR B 276       7.757  93.286  21.936  1.00 28.52           C  
ANISOU 4591  CZ  TYR B 276     3956   2017   4861    620   2101    586       C  
ATOM   4592  OH  TYR B 276       7.539  92.006  21.532  1.00 30.51           O  
ANISOU 4592  OH  TYR B 276     4175   2367   5049    626   1948    642       O  
ATOM   4593  N   GLU B 277       8.848  98.724  20.453  1.00 33.06           N  
ANISOU 4593  N   GLU B 277     4428   2252   5879    641   2437    612       N  
ATOM   4594  CA  GLU B 277       8.552  98.685  19.016  1.00 35.66           C  
ANISOU 4594  CA  GLU B 277     4614   2627   6308    676   2275    788       C  
ATOM   4595  C   GLU B 277       9.859  98.772  18.196  1.00 33.22           C  
ANISOU 4595  C   GLU B 277     4351   2433   5835    642   2111    746       C  
ATOM   4596  O   GLU B 277      10.042  97.987  17.278  1.00 30.49           O  
ANISOU 4596  O   GLU B 277     3971   2208   5405    634   1914    813       O  
ATOM   4597  CB  GLU B 277       7.555  99.769  18.601  1.00 40.15           C  
ANISOU 4597  CB  GLU B 277     5031   3043   7180    729   2403    940       C  
ATOM   4598  CG  GLU B 277       6.808  99.432  17.323  1.00 42.02           C  
ANISOU 4598  CG  GLU B 277     5100   3329   7536    758   2238   1158       C  
ATOM   4599  CD  GLU B 277       5.908 100.517  16.753  1.00 48.30           C  
ANISOU 4599  CD  GLU B 277     5723   3990   8640    806   2333   1345       C  
ATOM   4600  OE1 GLU B 277       5.393 100.322  15.625  1.00 49.05           O  
ANISOU 4600  OE1 GLU B 277     5678   4140   8818    812   2178   1536       O  
ATOM   4601  OE2 GLU B 277       5.715 101.565  17.432  1.00 52.45           O  
ANISOU 4601  OE2 GLU B 277     6249   4352   9325    830   2565   1306       O  
ATOM   4602  N   ASP B 278      10.773  99.685  18.553  1.00 33.02           N  
ANISOU 4602  N   ASP B 278     4413   2371   5761    613   2199    628       N  
ATOM   4603  CA  ASP B 278      12.100  99.793  17.916  1.00 31.49           C  
ANISOU 4603  CA  ASP B 278     4276   2280   5407    578   2062    572       C  
ATOM   4604  C   ASP B 278      12.966  98.551  18.175  1.00 30.13           C  
ANISOU 4604  C   ASP B 278     4210   2258   4978    535   1916    474       C  
ATOM   4605  O   ASP B 278      13.641  98.052  17.266  1.00 25.33           O  
ANISOU 4605  O   ASP B 278     3596   1761   4265    523   1740    499       O  
ATOM   4606  CB  ASP B 278      12.852 101.026  18.407  1.00 35.57           C  
ANISOU 4606  CB  ASP B 278     4868   2716   5929    550   2205    458       C  
ATOM   4607  CG  ASP B 278      12.191 102.336  18.018  1.00 42.41           C  
ANISOU 4607  CG  ASP B 278     5625   3430   7057    592   2348    557       C  
ATOM   4608  OD1 ASP B 278      11.273 102.321  17.156  1.00 43.81           O  
ANISOU 4608  OD1 ASP B 278     5652   3585   7406    643   2298    738       O  
ATOM   4609  OD2 ASP B 278      12.576 103.368  18.615  1.00 51.98           O  
ANISOU 4609  OD2 ASP B 278     6900   4542   8306    569   2516    456       O  
ATOM   4610  N   LYS B 279      12.932  98.023  19.415  1.00 26.94           N  
ANISOU 4610  N   LYS B 279     3901   1854   4479    509   1995    368       N  
ATOM   4611  CA  LYS B 279      13.800  96.937  19.831  1.00 26.05           C  
ANISOU 4611  CA  LYS B 279     3889   1871   4137    466   1880    277       C  
ATOM   4612  C   LYS B 279      13.411  95.622  19.128  1.00 24.17           C  
ANISOU 4612  C   LYS B 279     3588   1727   3867    490   1714    370       C  
ATOM   4613  O   LYS B 279      14.266  94.843  18.702  1.00 24.07           O  
ANISOU 4613  O   LYS B 279     3608   1828   3706    467   1566    347       O  
ATOM   4614  CB  LYS B 279      13.676  96.765  21.350  1.00 27.87           C  
ANISOU 4614  CB  LYS B 279     4223   2070   4295    427   2017    164       C  
ATOM   4615  CG  LYS B 279      14.629  95.759  21.970  1.00 27.41           C  
ANISOU 4615  CG  LYS B 279     4270   2138   4004    372   1917     74       C  
ATOM   4616  CD  LYS B 279      14.390  95.627  23.487  1.00 29.33           C  
ANISOU 4616  CD  LYS B 279     4614   2352   4177    321   2057    -22       C  
ATOM   4617  CE  LYS B 279      14.993  96.780  24.262  1.00 27.52           C  
ANISOU 4617  CE  LYS B 279     4486   2064   3904    250   2200   -144       C  
ATOM   4618  NZ  LYS B 279      14.940  96.546  25.715  1.00 29.27           N  
ANISOU 4618  NZ  LYS B 279     4825   2286   4008    174   2311   -245       N  
ATOM   4619  N   ILE B 280      12.102  95.375  19.018  1.00 25.22           N  
ANISOU 4619  N   ILE B 280     3627   1805   4148    531   1750    476       N  
ATOM   4620  CA  ILE B 280      11.575  94.166  18.400  1.00 24.24           C  
ANISOU 4620  CA  ILE B 280     3442   1759   4009    545   1610    566       C  
ATOM   4621  C   ILE B 280      11.829  94.222  16.887  1.00 23.15           C  
ANISOU 4621  C   ILE B 280     3230   1681   3885    542   1456    662       C  
ATOM   4622  O   ILE B 280      12.066  93.176  16.283  1.00 20.70           O  
ANISOU 4622  O   ILE B 280     2921   1472   3472    523   1310    680       O  
ATOM   4623  CB  ILE B 280      10.098  93.895  18.775  1.00 25.96           C  
ANISOU 4623  CB  ILE B 280     3580   1900   4383    583   1694    654       C  
ATOM   4624  CG1 ILE B 280       9.734  92.413  18.616  1.00 27.22           C  
ANISOU 4624  CG1 ILE B 280     3725   2149   4468    580   1570    691       C  
ATOM   4625  CG2 ILE B 280       9.109  94.747  18.015  1.00 26.51           C  
ANISOU 4625  CG2 ILE B 280     3508   1878   4685    622   1734    806       C  
ATOM   4626  CD1 ILE B 280      10.654  91.450  19.342  1.00 27.95           C  
ANISOU 4626  CD1 ILE B 280     3937   2332   4350    546   1524    566       C  
ATOM   4627  N   GLU B 281      11.792  95.427  16.309  1.00 23.15           N  
ANISOU 4627  N   GLU B 281     3170   1616   4007    555   1498    719       N  
ATOM   4628  CA  GLU B 281      12.124  95.639  14.889  1.00 23.68           C  
ANISOU 4628  CA  GLU B 281     3177   1741   4078    541   1361    808       C  
ATOM   4629  C   GLU B 281      13.602  95.319  14.660  1.00 22.27           C  
ANISOU 4629  C   GLU B 281     3101   1662   3698    501   1264    696       C  
ATOM   4630  O   GLU B 281      13.945  94.604  13.716  1.00 22.55           O  
ANISOU 4630  O   GLU B 281     3129   1792   3646    474   1117    729       O  
ATOM   4631  CB  GLU B 281      11.764  97.057  14.427  1.00 24.10           C  
ANISOU 4631  CB  GLU B 281     3141   1695   4320    566   1441    901       C  
ATOM   4632  CG  GLU B 281      10.264  97.283  14.243  1.00 26.71           C  
ANISOU 4632  CG  GLU B 281     3328   1942   4877    604   1494   1068       C  
ATOM   4633  CD  GLU B 281       9.783  98.729  14.192  1.00 27.12           C  
ANISOU 4633  CD  GLU B 281     3290   1855   5159    642   1638   1152       C  
ATOM   4634  OE1 GLU B 281      10.623  99.611  14.235  1.00 29.53           O  
ANISOU 4634  OE1 GLU B 281     3645   2129   5444    636   1694   1077       O  
ATOM   4635  OE2 GLU B 281       8.573  98.978  14.049  1.00 27.70           O  
ANISOU 4635  OE2 GLU B 281     3232   1849   5443    676   1691   1304       O  
ATOM   4636  N   TRP B 282      14.462  95.825  15.545  1.00 21.88           N  
ANISOU 4636  N   TRP B 282     3148   1587   3576    491   1352    565       N  
ATOM   4637  CA  TRP B 282      15.863  95.611  15.459  1.00 22.35           C  
ANISOU 4637  CA  TRP B 282     3297   1728   3466    454   1276    466       C  
ATOM   4638  C   TRP B 282      16.137  94.099  15.419  1.00 21.67           C  
ANISOU 4638  C   TRP B 282     3245   1746   3241    436   1158    445       C  
ATOM   4639  O   TRP B 282      16.799  93.600  14.513  1.00 19.99           O  
ANISOU 4639  O   TRP B 282     3036   1611   2947    414   1037    455       O  
ATOM   4640  CB  TRP B 282      16.595  96.299  16.616  1.00 24.65           C  
ANISOU 4640  CB  TRP B 282     3686   1978   3702    433   1395    335       C  
ATOM   4641  CG  TRP B 282      18.078  96.296  16.448  1.00 27.20           C  
ANISOU 4641  CG  TRP B 282     4083   2376   3875    394   1317    252       C  
ATOM   4642  CD1 TRP B 282      18.957  95.370  16.933  1.00 26.37           C  
ANISOU 4642  CD1 TRP B 282     4053   2357   3607    361   1249    177       C  
ATOM   4643  CD2 TRP B 282      18.861  97.256  15.709  1.00 27.36           C  
ANISOU 4643  CD2 TRP B 282     4097   2388   3909    386   1298    250       C  
ATOM   4644  NE1 TRP B 282      20.231  95.690  16.554  1.00 25.99           N  
ANISOU 4644  NE1 TRP B 282     4044   2354   3476    334   1191    130       N  
ATOM   4645  CE2 TRP B 282      20.209  96.839  15.804  1.00 28.50           C  
ANISOU 4645  CE2 TRP B 282     4318   2616   3893    347   1220    167       C  
ATOM   4646  CE3 TRP B 282      18.561  98.395  14.953  1.00 28.66           C  
ANISOU 4646  CE3 TRP B 282     4191   2484   4214    408   1337    320       C  
ATOM   4647  CZ2 TRP B 282      21.251  97.523  15.153  1.00 29.96           C  
ANISOU 4647  CZ2 TRP B 282     4515   2818   4051    331   1180    146       C  
ATOM   4648  CZ3 TRP B 282      19.586  99.063  14.305  1.00 28.48           C  
ANISOU 4648  CZ3 TRP B 282     4184   2480   4157    391   1296    299       C  
ATOM   4649  CH2 TRP B 282      20.912  98.648  14.430  1.00 27.79           C  
ANISOU 4649  CH2 TRP B 282     4177   2473   3905    353   1222    207       C  
ATOM   4650  N   LEU B 283      15.595  93.371  16.394  1.00 20.29           N  
ANISOU 4650  N   LEU B 283     3095   1565   3049    443   1206    418       N  
ATOM   4651  CA  LEU B 283      15.835  91.948  16.513  1.00 20.57           C  
ANISOU 4651  CA  LEU B 283     3163   1686   2967    428   1117    396       C  
ATOM   4652  C   LEU B 283      15.352  91.211  15.252  1.00 19.29           C  
ANISOU 4652  C   LEU B 283     2928   1571   2829    426    996    495       C  
ATOM   4653  O   LEU B 283      16.026  90.338  14.734  1.00 19.93           O  
ANISOU 4653  O   LEU B 283     3035   1728   2806    400    897    474       O  
ATOM   4654  CB  LEU B 283      15.114  91.409  17.755  1.00 20.96           C  
ANISOU 4654  CB  LEU B 283     3235   1706   3022    440   1202    371       C  
ATOM   4655  CG  LEU B 283      15.083  89.876  17.846  1.00 20.63           C  
ANISOU 4655  CG  LEU B 283     3203   1738   2894    434   1118    374       C  
ATOM   4656  CD1 LEU B 283      16.488  89.319  17.959  1.00 21.94           C  
ANISOU 4656  CD1 LEU B 283     3442   1985   2907    401   1046    299       C  
ATOM   4657  CD2 LEU B 283      14.250  89.410  19.018  1.00 22.21           C  
ANISOU 4657  CD2 LEU B 283     3417   1905   3115    447   1206    364       C  
ATOM   4658  N   ASN B 284      14.143  91.519  14.805  1.00 19.93           N  
ANISOU 4658  N   ASN B 284     2916   1604   3050    445   1011    605       N  
ATOM   4659  CA  ASN B 284      13.571  90.852  13.682  1.00 21.23           C  
ANISOU 4659  CA  ASN B 284     3013   1818   3234    425    898    705       C  
ATOM   4660  C   ASN B 284      14.414  91.095  12.424  1.00 20.44           C  
ANISOU 4660  C   ASN B 284     2918   1776   3072    385    796    718       C  
ATOM   4661  O   ASN B 284      14.702  90.175  11.675  1.00 20.53           O  
ANISOU 4661  O   ASN B 284     2945   1862   2994    343    695    719       O  
ATOM   4662  CB  ASN B 284      12.123  91.277  13.465  1.00 23.06           C  
ANISOU 4662  CB  ASN B 284     3131   1985   3643    447    932    841       C  
ATOM   4663  CG  ASN B 284      11.181  90.387  14.249  1.00 27.34           C  
ANISOU 4663  CG  ASN B 284     3659   2510   4217    467    970    853       C  
ATOM   4664  OD1 ASN B 284      10.662  89.412  13.714  1.00 28.42           O  
ANISOU 4664  OD1 ASN B 284     3760   2698   4337    441    880    910       O  
ATOM   4665  ND2 ASN B 284      10.963  90.714  15.511  1.00 25.48           N  
ANISOU 4665  ND2 ASN B 284     3456   2202   4022    504   1108    795       N  
ATOM   4666  N   ASN B 285      14.858  92.328  12.220  1.00 21.07           N  
ANISOU 4666  N   ASN B 285     2991   1817   3195    393    835    718       N  
ATOM   4667  CA  ASN B 285      15.700  92.625  11.052  1.00 21.13           C  
ANISOU 4667  CA  ASN B 285     3007   1877   3143    355    746    728       C  
ATOM   4668  C   ASN B 285      17.042  91.905  11.168  1.00 19.90           C  
ANISOU 4668  C   ASN B 285     2950   1785   2825    332    706    607       C  
ATOM   4669  O   ASN B 285      17.543  91.393  10.184  1.00 20.80           O  
ANISOU 4669  O   ASN B 285     3078   1961   2861    288    615    612       O  
ATOM   4670  CB  ASN B 285      15.887  94.128  10.850  1.00 20.75           C  
ANISOU 4670  CB  ASN B 285     2926   1767   3188    374    804    757       C  
ATOM   4671  CG  ASN B 285      14.633  94.830  10.393  1.00 22.48           C  
ANISOU 4671  CG  ASN B 285     3024   1930   3586    390    823    911       C  
ATOM   4672  OD1 ASN B 285      13.822  94.261   9.663  1.00 21.48           O  
ANISOU 4672  OD1 ASN B 285     2830   1844   3485    361    737   1021       O  
ATOM   4673  ND2 ASN B 285      14.487  96.093  10.808  1.00 22.47           N  
ANISOU 4673  ND2 ASN B 285     2990   1831   3714    429    940    925       N  
ATOM   4674  N   PHE B 286      17.603  91.826  12.375  1.00 20.18           N  
ANISOU 4674  N   PHE B 286     3053   1803   2811    353    776    506       N  
ATOM   4675  CA  PHE B 286      18.844  91.074  12.609  1.00 20.59           C  
ANISOU 4675  CA  PHE B 286     3183   1912   2726    333    738    411       C  
ATOM   4676  C   PHE B 286      18.641  89.565  12.302  1.00 20.81           C  
ANISOU 4676  C   PHE B 286     3212   1995   2696    313    669    421       C  
ATOM   4677  O   PHE B 286      19.381  88.944  11.512  1.00 20.02           O  
ANISOU 4677  O   PHE B 286     3138   1946   2523    279    602    403       O  
ATOM   4678  CB  PHE B 286      19.281  91.332  14.048  1.00 21.27           C  
ANISOU 4678  CB  PHE B 286     3328   1972   2780    348    825    325       C  
ATOM   4679  CG  PHE B 286      20.722  91.037  14.361  1.00 21.36           C  
ANISOU 4679  CG  PHE B 286     3408   2032   2674    326    796    242       C  
ATOM   4680  CD1 PHE B 286      21.511  90.309  13.493  1.00 21.05           C  
ANISOU 4680  CD1 PHE B 286     3377   2049   2572    304    711    240       C  
ATOM   4681  CD2 PHE B 286      21.257  91.438  15.572  1.00 22.77           C  
ANISOU 4681  CD2 PHE B 286     3643   2199   2808    317    860    170       C  
ATOM   4682  CE1 PHE B 286      22.823  90.006  13.820  1.00 23.92           C  
ANISOU 4682  CE1 PHE B 286     3790   2449   2849    288    691    179       C  
ATOM   4683  CE2 PHE B 286      22.580  91.156  15.887  1.00 22.84           C  
ANISOU 4683  CE2 PHE B 286     3702   2257   2715    290    824    112       C  
ATOM   4684  CZ  PHE B 286      23.355  90.435  15.013  1.00 22.70           C  
ANISOU 4684  CZ  PHE B 286     3678   2288   2656    281    740    123       C  
ATOM   4685  N   SER B 287      17.543  89.023  12.821  1.00 20.11           N  
ANISOU 4685  N   SER B 287     3093   1889   2657    330    694    458       N  
ATOM   4686  CA  SER B 287      17.180  87.626  12.683  1.00 20.82           C  
ANISOU 4686  CA  SER B 287     3181   2018   2711    313    646    469       C  
ATOM   4687  C   SER B 287      17.032  87.223  11.207  1.00 21.32           C  
ANISOU 4687  C   SER B 287     3217   2123   2758    260    554    524       C  
ATOM   4688  O   SER B 287      17.557  86.141  10.748  1.00 19.15           O  
ANISOU 4688  O   SER B 287     2977   1892   2403    223    508    488       O  
ATOM   4689  CB  SER B 287      15.916  87.344  13.447  1.00 19.29           C  
ANISOU 4689  CB  SER B 287     2948   1787   2593    343    695    512       C  
ATOM   4690  OG  SER B 287      15.668  85.950  13.429  1.00 23.18           O  
ANISOU 4690  OG  SER B 287     3445   2316   3045    327    655    511       O  
ATOM   4691  N   LYS B 288      16.287  88.031  10.458  1.00 22.41           N  
ANISOU 4691  N   LYS B 288     3291   2248   2974    247    531    616       N  
ATOM   4692  CA  LYS B 288      15.971  87.648   9.119  1.00 26.20           C  
ANISOU 4692  CA  LYS B 288     3745   2776   3432    179    440    681       C  
ATOM   4693  C   LYS B 288      17.213  87.811   8.232  1.00 25.33           C  
ANISOU 4693  C   LYS B 288     3689   2705   3230    135    400    631       C  
ATOM   4694  O   LYS B 288      17.381  87.045   7.277  1.00 22.23           O  
ANISOU 4694  O   LYS B 288     3319   2361   2764     65    338    629       O  
ATOM   4695  CB  LYS B 288      14.728  88.375   8.611  1.00 29.85           C  
ANISOU 4695  CB  LYS B 288     4109   3220   4012    169    417    819       C  
ATOM   4696  CG  LYS B 288      14.894  89.824   8.240  1.00 37.08           C  
ANISOU 4696  CG  LYS B 288     4986   4105   4996    184    432    871       C  
ATOM   4697  CD  LYS B 288      13.584  90.449   7.788  1.00 43.58           C  
ANISOU 4697  CD  LYS B 288     5692   4904   5960    178    412   1032       C  
ATOM   4698  CE  LYS B 288      12.610  90.699   8.925  1.00 45.50           C  
ANISOU 4698  CE  LYS B 288     5881   5065   6340    250    511   1065       C  
ATOM   4699  NZ  LYS B 288      11.208  90.451   8.503  1.00 50.62           N  
ANISOU 4699  NZ  LYS B 288     6423   5716   7094    226    463   1216       N  
ATOM   4700  N   THR B 289      18.123  88.716   8.621  1.00 22.49           N  
ANISOU 4700  N   THR B 289     3358   2320   2868    173    444    579       N  
ATOM   4701  CA  THR B 289      19.383  88.877   7.917  1.00 21.42           C  
ANISOU 4701  CA  THR B 289     3273   2213   2652    141    418    525       C  
ATOM   4702  C   THR B 289      20.279  87.657   8.168  1.00 21.53           C  
ANISOU 4702  C   THR B 289     3353   2251   2577    131    422    434       C  
ATOM   4703  O   THR B 289      20.823  87.072   7.245  1.00 17.98           O  
ANISOU 4703  O   THR B 289     2936   1833   2061     75    386    412       O  
ATOM   4704  CB  THR B 289      20.065  90.195   8.303  1.00 22.61           C  
ANISOU 4704  CB  THR B 289     3430   2326   2834    182    466    499       C  
ATOM   4705  OG1 THR B 289      19.156  91.227   7.900  1.00 22.39           O  
ANISOU 4705  OG1 THR B 289     3329   2270   2908    187    466    601       O  
ATOM   4706  CG2 THR B 289      21.440  90.334   7.691  1.00 22.48           C  
ANISOU 4706  CG2 THR B 289     3466   2335   2740    156    446    440       C  
ATOM   4707  N   ILE B 290      20.475  87.302   9.429  1.00 21.40           N  
ANISOU 4707  N   ILE B 290     3355   2214   2562    181    473    383       N  
ATOM   4708  CA  ILE B 290      21.349  86.184   9.742  1.00 22.26           C  
ANISOU 4708  CA  ILE B 290     3510   2340   2608    177    480    316       C  
ATOM   4709  C   ILE B 290      20.729  84.873   9.247  1.00 22.60           C  
ANISOU 4709  C   ILE B 290     3549   2402   2635    137    454    332       C  
ATOM   4710  O   ILE B 290      21.480  83.946   8.905  1.00 22.48           O  
ANISOU 4710  O   ILE B 290     3569   2398   2573    109    455    286       O  
ATOM   4711  CB  ILE B 290      21.670  86.108  11.244  1.00 26.01           C  
ANISOU 4711  CB  ILE B 290     4001   2799   3082    228    531    275       C  
ATOM   4712  CG1 ILE B 290      22.934  85.296  11.516  1.00 33.85           C  
ANISOU 4712  CG1 ILE B 290     5030   3809   4020    225    534    221       C  
ATOM   4713  CG2 ILE B 290      20.502  85.531  11.993  1.00 28.24           C  
ANISOU 4713  CG2 ILE B 290     4257   3069   3402    249    553    305       C  
ATOM   4714  CD1 ILE B 290      24.134  85.784  10.751  1.00 38.32           C  
ANISOU 4714  CD1 ILE B 290     5618   4382   4557    203    518    193       C  
ATOM   4715  N   ASN B 291      19.396  84.763   9.180  1.00 22.23           N  
ANISOU 4715  N   ASN B 291     3457   2353   2634    129    437    397       N  
ATOM   4716  CA  ASN B 291      18.805  83.481   8.735  1.00 23.10           C  
ANISOU 4716  CA  ASN B 291     3567   2482   2726     81    412    407       C  
ATOM   4717  C   ASN B 291      18.966  83.274   7.221  1.00 23.42           C  
ANISOU 4717  C   ASN B 291     3629   2557   2710    -13    360    414       C  
ATOM   4718  O   ASN B 291      18.697  82.175   6.724  1.00 23.00           O  
ANISOU 4718  O   ASN B 291     3594   2520   2623    -73    348    402       O  
ATOM   4719  CB  ASN B 291      17.370  83.281   9.199  1.00 23.92           C  
ANISOU 4719  CB  ASN B 291     3617   2575   2896     96    410    474       C  
ATOM   4720  CG  ASN B 291      17.351  82.855  10.659  1.00 26.09           C  
ANISOU 4720  CG  ASN B 291     3897   2823   3194    166    471    440       C  
ATOM   4721  OD1 ASN B 291      18.281  82.196  11.154  1.00 27.93           O  
ANISOU 4721  OD1 ASN B 291     4170   3058   3383    181    497    376       O  
ATOM   4722  ND2 ASN B 291      16.344  83.287  11.374  1.00 23.94           N  
ANISOU 4722  ND2 ASN B 291     3579   2522   2993    207    498    489       N  
ATOM   4723  N   LYS B 292      19.507  84.258   6.513  1.00 22.45           N  
ANISOU 4723  N   LYS B 292     3514   2445   2569    -33    339    423       N  
ATOM   4724  CA  LYS B 292      19.911  84.043   5.099  1.00 23.21           C  
ANISOU 4724  CA  LYS B 292     3649   2576   2590   -132    301    413       C  
ATOM   4725  C   LYS B 292      21.361  83.548   4.984  1.00 21.68           C  
ANISOU 4725  C   LYS B 292     3522   2369   2344   -134    349    316       C  
ATOM   4726  O   LYS B 292      21.821  83.230   3.871  1.00 23.26           O  
ANISOU 4726  O   LYS B 292     3769   2587   2480   -219    343    287       O  
ATOM   4727  CB  LYS B 292      19.694  85.347   4.339  1.00 25.41           C  
ANISOU 4727  CB  LYS B 292     3896   2875   2882   -157    252    488       C  
ATOM   4728  CG  LYS B 292      18.222  85.648   4.113  1.00 28.20           C  
ANISOU 4728  CG  LYS B 292     4174   3247   3293   -183    196    607       C  
ATOM   4729  CD  LYS B 292      18.010  86.915   3.352  1.00 33.71           C  
ANISOU 4729  CD  LYS B 292     4826   3961   4018   -209    148    701       C  
ATOM   4730  CE  LYS B 292      17.719  88.128   4.200  1.00 35.11           C  
ANISOU 4730  CE  LYS B 292     4938   4086   4313   -110    187    750       C  
ATOM   4731  NZ  LYS B 292      17.225  89.237   3.351  1.00 38.20           N  
ANISOU 4731  NZ  LYS B 292     5262   4494   4756   -145    133    874       N  
ATOM   4732  N   VAL B 293      22.080  83.521   6.106  1.00 18.42           N  
ANISOU 4732  N   VAL B 293     3112   1925   1960    -50    399    271       N  
ATOM   4733  CA  VAL B 293      23.433  83.045   6.186  1.00 19.85           C  
ANISOU 4733  CA  VAL B 293     3334   2087   2118    -40    446    200       C  
ATOM   4734  C   VAL B 293      23.371  81.568   6.595  1.00 20.72           C  
ANISOU 4734  C   VAL B 293     3455   2180   2238    -41    486    169       C  
ATOM   4735  O   VAL B 293      22.742  81.233   7.603  1.00 18.99           O  
ANISOU 4735  O   VAL B 293     3205   1955   2055      7    491    190       O  
ATOM   4736  CB  VAL B 293      24.267  83.857   7.187  1.00 20.78           C  
ANISOU 4736  CB  VAL B 293     3442   2189   2262     37    467    184       C  
ATOM   4737  CG1 VAL B 293      25.716  83.383   7.240  1.00 20.86           C  
ANISOU 4737  CG1 VAL B 293     3481   2180   2261     45    508    130       C  
ATOM   4738  CG2 VAL B 293      24.182  85.347   6.875  1.00 23.81           C  
ANISOU 4738  CG2 VAL B 293     3812   2581   2654     43    439    217       C  
ATOM   4739  N   PRO B 294      23.977  80.647   5.808  1.00 21.68           N  
ANISOU 4739  N   PRO B 294     3619   2286   2330   -101    523    120       N  
ATOM   4740  CA  PRO B 294      24.007  79.231   6.166  1.00 19.48           C  
ANISOU 4740  CA  PRO B 294     3346   1978   2078   -101    578     91       C  
ATOM   4741  C   PRO B 294      24.489  79.006   7.598  1.00 20.97           C  
ANISOU 4741  C   PRO B 294     3498   2145   2321     -5    605     98       C  
ATOM   4742  O   PRO B 294      25.501  79.617   8.034  1.00 20.59           O  
ANISOU 4742  O   PRO B 294     3444   2093   2283     39    612     93       O  
ATOM   4743  CB  PRO B 294      25.027  78.649   5.175  1.00 21.90           C  
ANISOU 4743  CB  PRO B 294     3704   2253   2362   -164    639     29       C  
ATOM   4744  CG  PRO B 294      24.917  79.524   3.954  1.00 21.79           C  
ANISOU 4744  CG  PRO B 294     3725   2274   2279   -242    595     32       C  
ATOM   4745  CD  PRO B 294      24.590  80.909   4.494  1.00 22.71           C  
ANISOU 4745  CD  PRO B 294     3796   2423   2407   -179    527     91       C  
ATOM   4746  N   ARG B 295      23.827  78.076   8.301  1.00 21.08           N  
ANISOU 4746  N   ARG B 295     3491   2150   2368     15    621    113       N  
ATOM   4747  CA  ARG B 295      24.266  77.647   9.612  1.00 22.01           C  
ANISOU 4747  CA  ARG B 295     3577   2254   2531     88    648    128       C  
ATOM   4748  C   ARG B 295      25.666  77.027   9.623  1.00 20.48           C  
ANISOU 4748  C   ARG B 295     3384   2024   2373     99    706    106       C  
ATOM   4749  O   ARG B 295      26.273  76.957  10.696  1.00 20.98           O  
ANISOU 4749  O   ARG B 295     3414   2087   2468    155    712    135       O  
ATOM   4750  CB  ARG B 295      23.234  76.725  10.270  1.00 23.36           C  
ANISOU 4750  CB  ARG B 295     3723   2421   2731    103    657    153       C  
ATOM   4751  CG  ARG B 295      22.040  77.457  10.856  1.00 22.63           C  
ANISOU 4751  CG  ARG B 295     3608   2358   2632    129    610    193       C  
ATOM   4752  CD  ARG B 295      20.981  76.479  11.332  1.00 24.61           C  
ANISOU 4752  CD  ARG B 295     3836   2600   2914    134    622    217       C  
ATOM   4753  NE  ARG B 295      19.955  77.128  12.118  1.00 24.74           N  
ANISOU 4753  NE  ARG B 295     3824   2632   2942    172    597    259       N  
ATOM   4754  CZ  ARG B 295      20.055  77.404  13.401  1.00 25.21           C  
ANISOU 4754  CZ  ARG B 295     3871   2695   3011    231    612    274       C  
ATOM   4755  NH1 ARG B 295      21.174  77.142  14.060  1.00 25.87           N  
ANISOU 4755  NH1 ARG B 295     3959   2779   3088    256    634    263       N  
ATOM   4756  NH2 ARG B 295      19.024  77.952  14.017  1.00 24.59           N  
ANISOU 4756  NH2 ARG B 295     3772   2619   2950    256    608    306       N  
ATOM   4757  N   ASP B 296      26.189  76.593   8.469  1.00 22.30           N  
ANISOU 4757  N   ASP B 296     3649   2221   2601     40    753     62       N  
ATOM   4758  CA  ASP B 296      27.588  76.093   8.353  1.00 25.04           C  
ANISOU 4758  CA  ASP B 296     3991   2519   3002     50    823     46       C  
ATOM   4759  C   ASP B 296      28.623  77.116   8.824  1.00 22.79           C  
ANISOU 4759  C   ASP B 296     3687   2253   2719     96    793     67       C  
ATOM   4760  O   ASP B 296      29.718  76.745   9.233  1.00 21.44           O  
ANISOU 4760  O   ASP B 296     3483   2052   2611    127    832     88       O  
ATOM   4761  CB  ASP B 296      27.947  75.725   6.917  1.00 24.95           C  
ANISOU 4761  CB  ASP B 296     4035   2468   2976    -32    887    -15       C  
ATOM   4762  CG  ASP B 296      26.928  74.806   6.282  1.00 35.43           C  
ANISOU 4762  CG  ASP B 296     5397   3782   4281   -106    914    -47       C  
ATOM   4763  OD1 ASP B 296      25.753  75.245   6.174  1.00 45.19           O  
ANISOU 4763  OD1 ASP B 296     6639   5071   5457   -132    839    -30       O  
ATOM   4764  OD2 ASP B 296      27.309  73.654   5.922  1.00 32.10           O  
ANISOU 4764  OD2 ASP B 296     4991   3294   3912   -139   1016    -85       O  
ATOM   4765  N   SER B 297      28.259  78.401   8.777  1.00 20.82           N  
ANISOU 4765  N   SER B 297     3451   2050   2409     97    725     70       N  
ATOM   4766  CA  SER B 297      29.138  79.452   9.188  1.00 20.86           C  
ANISOU 4766  CA  SER B 297     3444   2074   2407    129    695     83       C  
ATOM   4767  C   SER B 297      29.246  79.517  10.718  1.00 19.34           C  
ANISOU 4767  C   SER B 297     3210   1905   2231    186    669    129       C  
ATOM   4768  O   SER B 297      30.242  80.037  11.248  1.00 20.74           O  
ANISOU 4768  O   SER B 297     3369   2094   2415    206    656    147       O  
ATOM   4769  CB  SER B 297      28.686  80.789   8.592  1.00 19.29           C  
ANISOU 4769  CB  SER B 297     3273   1907   2150    108    644     72       C  
ATOM   4770  OG  SER B 297      27.504  81.244   9.236  1.00 20.87           O  
ANISOU 4770  OG  SER B 297     3459   2137   2331    128    601     98       O  
ATOM   4771  N   ASP B 298      28.233  79.028  11.445  1.00 20.14           N  
ANISOU 4771  N   ASP B 298     3299   2021   2333    202    660    150       N  
ATOM   4772  CA  ASP B 298      28.154  79.286  12.893  1.00 20.67           C  
ANISOU 4772  CA  ASP B 298     3341   2121   2389    240    632    189       C  
ATOM   4773  C   ASP B 298      29.307  78.587  13.612  1.00 22.22           C  
ANISOU 4773  C   ASP B 298     3496   2313   2632    258    648    233       C  
ATOM   4774  O   ASP B 298      29.709  79.052  14.640  1.00 21.13           O  
ANISOU 4774  O   ASP B 298     3344   2212   2471    268    615    264       O  
ATOM   4775  CB  ASP B 298      26.800  78.886  13.494  1.00 21.73           C  
ANISOU 4775  CB  ASP B 298     3471   2267   2518    252    628    204       C  
ATOM   4776  CG  ASP B 298      25.602  79.650  12.941  1.00 24.47           C  
ANISOU 4776  CG  ASP B 298     3839   2620   2836    237    606    186       C  
ATOM   4777  OD1 ASP B 298      25.813  80.716  12.201  1.00 22.88           O  
ANISOU 4777  OD1 ASP B 298     3659   2423   2611    219    587    166       O  
ATOM   4778  OD2 ASP B 298      24.440  79.232  13.276  1.00 24.20           O  
ANISOU 4778  OD2 ASP B 298     3796   2587   2811    244    608    203       O  
ATOM   4779  N   LYS B 299      29.876  77.498  13.047  1.00 22.67           N  
ANISOU 4779  N   LYS B 299     3531   2320   2759    254    702    239       N  
ATOM   4780  CA  LYS B 299      30.998  76.813  13.734  1.00 23.98           C  
ANISOU 4780  CA  LYS B 299     3639   2475   2997    275    720    305       C  
ATOM   4781  C   LYS B 299      32.259  77.687  13.777  1.00 22.65           C  
ANISOU 4781  C   LYS B 299     3458   2322   2825    271    693    320       C  
ATOM   4782  O   LYS B 299      33.162  77.437  14.607  1.00 22.39           O  
ANISOU 4782  O   LYS B 299     3369   2304   2834    283    677    395       O  
ATOM   4783  CB  LYS B 299      31.273  75.422  13.151  1.00 25.33           C  
ANISOU 4783  CB  LYS B 299     3783   2573   3269    275    807    312       C  
ATOM   4784  CG  LYS B 299      31.864  75.394  11.756  1.00 25.89           C  
ANISOU 4784  CG  LYS B 299     3882   2584   3370    244    871    255       C  
ATOM   4785  CD  LYS B 299      32.061  73.982  11.273  1.00 27.52           C  
ANISOU 4785  CD  LYS B 299     4068   2706   3680    236    978    253       C  
ATOM   4786  CE  LYS B 299      32.376  73.926   9.800  1.00 28.79           C  
ANISOU 4786  CE  LYS B 299     4283   2806   3848    185   1057    174       C  
ATOM   4787  NZ  LYS B 299      31.213  74.351   8.979  1.00 28.46           N  
ANISOU 4787  NZ  LYS B 299     4320   2795   3697    130   1026     99       N  
ATOM   4788  N   TYR B 300      32.316  78.762  12.973  1.00 20.33           N  
ANISOU 4788  N   TYR B 300     3210   2033   2481    252    678    263       N  
ATOM   4789  CA  TYR B 300      33.495  79.611  12.960  1.00 20.97           C  
ANISOU 4789  CA  TYR B 300     3280   2125   2560    247    654    273       C  
ATOM   4790  C   TYR B 300      33.332  80.810  13.914  1.00 22.43           C  
ANISOU 4790  C   TYR B 300     3483   2376   2663    241    583    276       C  
ATOM   4791  O   TYR B 300      34.240  81.611  14.004  1.00 24.18           O  
ANISOU 4791  O   TYR B 300     3699   2613   2872    229    556    282       O  
ATOM   4792  CB  TYR B 300      33.803  80.080  11.529  1.00 20.83           C  
ANISOU 4792  CB  TYR B 300     3301   2068   2542    225    688    212       C  
ATOM   4793  CG  TYR B 300      34.107  78.952  10.585  1.00 20.29           C  
ANISOU 4793  CG  TYR B 300     3228   1928   2550    214    776    198       C  
ATOM   4794  CD1 TYR B 300      35.334  78.313  10.621  1.00 22.61           C  
ANISOU 4794  CD1 TYR B 300     3467   2174   2947    228    828    244       C  
ATOM   4795  CD2 TYR B 300      33.144  78.460   9.723  1.00 21.04           C  
ANISOU 4795  CD2 TYR B 300     3370   2000   2624    184    813    144       C  
ATOM   4796  CE1 TYR B 300      35.605  77.223   9.807  1.00 25.71           C  
ANISOU 4796  CE1 TYR B 300     3855   2484   3426    216    934    227       C  
ATOM   4797  CE2 TYR B 300      33.405  77.385   8.884  1.00 21.75           C  
ANISOU 4797  CE2 TYR B 300     3466   2017   2778    160    910    118       C  
ATOM   4798  CZ  TYR B 300      34.630  76.752   8.939  1.00 23.85           C  
ANISOU 4798  CZ  TYR B 300     3682   2225   3155    178    980    155       C  
ATOM   4799  OH  TYR B 300      34.880  75.686   8.124  1.00 26.44           O  
ANISOU 4799  OH  TYR B 300     4019   2466   3559    151   1098    124       O  
ATOM   4800  N   VAL B 301      32.175  80.934  14.580  1.00 21.62           N  
ANISOU 4800  N   VAL B 301     3402   2303   2506    244    564    267       N  
ATOM   4801  CA  VAL B 301      31.891  82.005  15.553  1.00 20.48           C  
ANISOU 4801  CA  VAL B 301     3284   2209   2285    230    521    259       C  
ATOM   4802  C   VAL B 301      32.442  81.585  16.910  1.00 23.85           C  
ANISOU 4802  C   VAL B 301     3677   2682   2701    218    491    328       C  
ATOM   4803  O   VAL B 301      32.259  80.442  17.324  1.00 22.25           O  
ANISOU 4803  O   VAL B 301     3437   2476   2537    232    503    378       O  
ATOM   4804  CB  VAL B 301      30.386  82.283  15.687  1.00 20.70           C  
ANISOU 4804  CB  VAL B 301     3348   2239   2276    238    531    225       C  
ATOM   4805  CG1 VAL B 301      30.121  83.371  16.719  1.00 23.02           C  
ANISOU 4805  CG1 VAL B 301     3674   2569   2502    219    514    209       C  
ATOM   4806  CG2 VAL B 301      29.710  82.616  14.361  1.00 20.64           C  
ANISOU 4806  CG2 VAL B 301     3364   2197   2280    240    548    180       C  
ATOM   4807  N   THR B 302      33.064  82.528  17.614  1.00 23.74           N  
ANISOU 4807  N   THR B 302     3676   2713   2631    182    451    332       N  
ATOM   4808  CA  THR B 302      33.624  82.281  18.921  1.00 27.77           C  
ANISOU 4808  CA  THR B 302     4159   3283   3107    146    408    403       C  
ATOM   4809  C   THR B 302      32.535  81.701  19.834  1.00 28.85           C  
ANISOU 4809  C   THR B 302     4309   3443   3208    148    417    417       C  
ATOM   4810  O   THR B 302      31.395  82.200  19.826  1.00 26.97           O  
ANISOU 4810  O   THR B 302     4124   3192   2930    155    446    353       O  
ATOM   4811  CB  THR B 302      34.170  83.591  19.506  1.00 31.60           C  
ANISOU 4811  CB  THR B 302     4683   3815   3508     89    369    378       C  
ATOM   4812  OG1 THR B 302      35.112  84.067  18.557  1.00 34.36           O  
ANISOU 4812  OG1 THR B 302     5016   4135   3902     96    366    365       O  
ATOM   4813  CG2 THR B 302      34.848  83.423  20.843  1.00 34.37           C  
ANISOU 4813  CG2 THR B 302     5012   4242   3805     26    311    456       C  
ATOM   4814  N   GLN B 303      32.921  80.707  20.645  1.00 28.04           N  
ANISOU 4814  N   GLN B 303     4154   3373   3126    138    393    509       N  
ATOM   4815  CA  GLN B 303      32.019  79.792  21.364  1.00 31.76           C  
ANISOU 4815  CA  GLN B 303     4617   3855   3592    150    407    544       C  
ATOM   4816  C   GLN B 303      31.160  80.529  22.410  1.00 29.15           C  
ANISOU 4816  C   GLN B 303     4356   3572   3146    107    405    502       C  
ATOM   4817  O   GLN B 303      29.986  80.161  22.621  1.00 27.67           O  
ANISOU 4817  O   GLN B 303     4190   3368   2954    130    442    481       O  
ATOM   4818  CB  GLN B 303      32.862  78.679  22.000  1.00 40.35           C  
ANISOU 4818  CB  GLN B 303     5621   4972   4737    142    376    671       C  
ATOM   4819  CG  GLN B 303      32.075  77.659  22.810  1.00 50.84           C  
ANISOU 4819  CG  GLN B 303     6931   6317   6068    151    386    725       C  
ATOM   4820  CD  GLN B 303      31.135  76.827  21.970  1.00 63.28           C  
ANISOU 4820  CD  GLN B 303     8501   7816   7724    216    454    685       C  
ATOM   4821  OE1 GLN B 303      29.946  76.711  22.274  1.00 71.47           O  
ANISOU 4821  OE1 GLN B 303     9576   8852   8725    227    478    649       O  
ATOM   4822  NE2 GLN B 303      31.667  76.219  20.919  1.00 78.42           N  
ANISOU 4822  NE2 GLN B 303    10373   9667   9754    253    491    693       N  
ATOM   4823  N   ILE B 304      31.722  81.571  23.037  1.00 29.37           N  
ANISOU 4823  N   ILE B 304     4424   3651   3084     40    371    486       N  
ATOM   4824  CA  ILE B 304      31.016  82.355  24.043  1.00 29.02           C  
ANISOU 4824  CA  ILE B 304     4457   3642   2927    -16    388    435       C  
ATOM   4825  C   ILE B 304      29.712  82.928  23.488  1.00 27.51           C  
ANISOU 4825  C   ILE B 304     4316   3385   2750     28    460    339       C  
ATOM   4826  O   ILE B 304      28.802  83.169  24.294  1.00 23.81           O  
ANISOU 4826  O   ILE B 304     3897   2923   2223      4    501    308       O  
ATOM   4827  CB  ILE B 304      31.877  83.478  24.650  1.00 33.64           C  
ANISOU 4827  CB  ILE B 304     5085   4282   3414   -107    351    416       C  
ATOM   4828  CG1 ILE B 304      32.417  84.446  23.598  1.00 32.99           C  
ANISOU 4828  CG1 ILE B 304     5011   4157   3367    -89    356    355       C  
ATOM   4829  CG2 ILE B 304      32.973  82.898  25.522  1.00 36.39           C  
ANISOU 4829  CG2 ILE B 304     5384   4714   3727   -175    269    531       C  
ATOM   4830  CD1 ILE B 304      33.365  85.492  24.156  1.00 39.58           C  
ANISOU 4830  CD1 ILE B 304     5881   5043   4114   -182    318    341       C  
ATOM   4831  N   PHE B 305      29.615  83.125  22.164  1.00 21.42           N  
ANISOU 4831  N   PHE B 305     3529   2553   2056     85    479    302       N  
ATOM   4832  CA  PHE B 305      28.431  83.701  21.534  1.00 22.99           C  
ANISOU 4832  CA  PHE B 305     3759   2694   2282    123    535    234       C  
ATOM   4833  C   PHE B 305      27.404  82.670  21.060  1.00 23.18           C  
ANISOU 4833  C   PHE B 305     3751   2681   2373    180    559    253       C  
ATOM   4834  O   PHE B 305      26.412  83.066  20.392  1.00 22.24           O  
ANISOU 4834  O   PHE B 305     3643   2514   2290    210    595    215       O  
ATOM   4835  CB  PHE B 305      28.798  84.549  20.305  1.00 23.38           C  
ANISOU 4835  CB  PHE B 305     3810   2704   2369    142    535    191       C  
ATOM   4836  CG  PHE B 305      29.600  85.776  20.620  1.00 24.81           C  
ANISOU 4836  CG  PHE B 305     4028   2905   2494     90    525    156       C  
ATOM   4837  CD1 PHE B 305      29.124  86.728  21.496  1.00 26.34           C  
ANISOU 4837  CD1 PHE B 305     4282   3103   2624     45    567    106       C  
ATOM   4838  CD2 PHE B 305      30.835  85.991  20.029  1.00 28.46           C  
ANISOU 4838  CD2 PHE B 305     4467   3375   2971     81    484    168       C  
ATOM   4839  CE1 PHE B 305      29.855  87.871  21.768  1.00 26.68           C  
ANISOU 4839  CE1 PHE B 305     4364   3158   2614    -11    567     65       C  
ATOM   4840  CE2 PHE B 305      31.571  87.127  20.317  1.00 30.15           C  
ANISOU 4840  CE2 PHE B 305     4713   3607   3134     29    474    135       C  
ATOM   4841  CZ  PHE B 305      31.078  88.064  21.188  1.00 27.77           C  
ANISOU 4841  CZ  PHE B 305     4475   3311   2763    -19    514     81       C  
ATOM   4842  N   ASN B 306      27.628  81.389  21.341  1.00 23.52           N  
ANISOU 4842  N   ASN B 306     3751   2742   2443    191    540    317       N  
ATOM   4843  CA  ASN B 306      26.745  80.309  20.883  1.00 25.65           C  
ANISOU 4843  CA  ASN B 306     3989   2975   2779    237    565    335       C  
ATOM   4844  C   ASN B 306      25.271  80.608  21.186  1.00 23.22           C  
ANISOU 4844  C   ASN B 306     3713   2647   2462    250    609    302       C  
ATOM   4845  O   ASN B 306      24.430  80.474  20.295  1.00 24.00           O  
ANISOU 4845  O   ASN B 306     3800   2701   2614    282    628    285       O  
ATOM   4846  CB  ASN B 306      27.144  78.940  21.458  1.00 28.07           C  
ANISOU 4846  CB  ASN B 306     4246   3304   3114    242    550    414       C  
ATOM   4847  CG  ASN B 306      26.827  78.703  22.930  1.00 32.10           C  
ANISOU 4847  CG  ASN B 306     4768   3865   3560    212    546    455       C  
ATOM   4848  OD1 ASN B 306      27.027  79.574  23.798  1.00 29.90           O  
ANISOU 4848  OD1 ASN B 306     4536   3633   3191    159    535    439       O  
ATOM   4849  ND2 ASN B 306      26.360  77.494  23.229  1.00 34.14           N  
ANISOU 4849  ND2 ASN B 306     4989   4118   3863    237    559    508       N  
ATOM   4850  N   LEU B 307      24.957  80.976  22.429  1.00 22.02           N  
ANISOU 4850  N   LEU B 307     3597   2525   2243    218    628    299       N  
ATOM   4851  CA  LEU B 307      23.541  81.208  22.852  1.00 22.79           C  
ANISOU 4851  CA  LEU B 307     3720   2593   2344    231    688    274       C  
ATOM   4852  C   LEU B 307      22.983  82.477  22.189  1.00 22.43           C  
ANISOU 4852  C   LEU B 307     3699   2499   2325    241    725    217       C  
ATOM   4853  O   LEU B 307      21.859  82.480  21.610  1.00 21.56           O  
ANISOU 4853  O   LEU B 307     3569   2341   2282    278    755    216       O  
ATOM   4854  CB  LEU B 307      23.487  81.292  24.379  1.00 22.05           C  
ANISOU 4854  CB  LEU B 307     3670   2545   2163    179    710    281       C  
ATOM   4855  CG  LEU B 307      22.167  81.755  25.004  1.00 24.37           C  
ANISOU 4855  CG  LEU B 307     4003   2803   2451    180    793    245       C  
ATOM   4856  CD1 LEU B 307      20.996  80.885  24.577  1.00 26.44           C  
ANISOU 4856  CD1 LEU B 307     4221   3023   2802    241    814    273       C  
ATOM   4857  CD2 LEU B 307      22.295  81.787  26.514  1.00 25.10           C  
ANISOU 4857  CD2 LEU B 307     4150   2948   2436    109    815    247       C  
ATOM   4858  N   LYS B 308      23.780  83.545  22.227  1.00 22.32           N  
ANISOU 4858  N   LYS B 308     3717   2494   2266    206    720    180       N  
ATOM   4859  CA  LYS B 308      23.331  84.823  21.695  1.00 22.14           C  
ANISOU 4859  CA  LYS B 308     3713   2421   2275    213    763    133       C  
ATOM   4860  C   LYS B 308      23.016  84.674  20.202  1.00 21.11           C  
ANISOU 4860  C   LYS B 308     3535   2256   2228    259    736    150       C  
ATOM   4861  O   LYS B 308      21.949  85.129  19.734  1.00 20.75           O  
ANISOU 4861  O   LYS B 308     3474   2162   2246    284    773    152       O  
ATOM   4862  CB  LYS B 308      24.334  85.939  21.973  1.00 23.19           C  
ANISOU 4862  CB  LYS B 308     3891   2572   2348    163    762     89       C  
ATOM   4863  CG  LYS B 308      23.838  87.308  21.513  1.00 23.77           C  
ANISOU 4863  CG  LYS B 308     3981   2583   2466    170    822     43       C  
ATOM   4864  CD  LYS B 308      24.690  88.475  21.954  1.00 26.14           C  
ANISOU 4864  CD  LYS B 308     4334   2891   2706    112    842    -10       C  
ATOM   4865  CE  LYS B 308      23.993  89.817  21.782  1.00 28.78           C  
ANISOU 4865  CE  LYS B 308     4687   3147   3098    118    934    -56       C  
ATOM   4866  NZ  LYS B 308      24.833  90.929  22.295  1.00 27.78           N  
ANISOU 4866  NZ  LYS B 308     4621   3025   2907     51    964   -119       N  
ATOM   4867  N   LEU B 309      23.890  83.969  19.475  1.00 22.93           N  
ANISOU 4867  N   LEU B 309     3739   2509   2462    263    677    171       N  
ATOM   4868  CA  LEU B 309      23.700  83.769  18.051  1.00 22.75           C  
ANISOU 4868  CA  LEU B 309     3685   2461   2497    285    653    180       C  
ATOM   4869  C   LEU B 309      22.438  82.941  17.796  1.00 21.52           C  
ANISOU 4869  C   LEU B 309     3500   2283   2391    308    665    210       C  
ATOM   4870  O   LEU B 309      21.624  83.294  16.903  1.00 19.32           O  
ANISOU 4870  O   LEU B 309     3202   1976   2160    316    665    220       O  
ATOM   4871  CB  LEU B 309      24.933  83.103  17.420  1.00 22.93           C  
ANISOU 4871  CB  LEU B 309     3692   2502   2515    277    610    189       C  
ATOM   4872  CG  LEU B 309      24.782  82.775  15.940  1.00 25.14           C  
ANISOU 4872  CG  LEU B 309     3954   2758   2838    281    594    190       C  
ATOM   4873  CD1 LEU B 309      24.347  83.981  15.136  1.00 26.75           C  
ANISOU 4873  CD1 LEU B 309     4166   2942   3056    276    594    174       C  
ATOM   4874  CD2 LEU B 309      26.077  82.203  15.362  1.00 26.58           C  
ANISOU 4874  CD2 LEU B 309     4128   2946   3024    270    576    189       C  
ATOM   4875  N   GLU B 310      22.266  81.850  18.553  1.00 20.67           N  
ANISOU 4875  N   GLU B 310     3383   2192   2276    315    670    233       N  
ATOM   4876  CA  GLU B 310      21.101  80.987  18.317  1.00 21.54           C  
ANISOU 4876  CA  GLU B 310     3464   2282   2436    334    681    262       C  
ATOM   4877  C   GLU B 310      19.806  81.751  18.659  1.00 21.12           C  
ANISOU 4877  C   GLU B 310     3410   2196   2416    347    726    266       C  
ATOM   4878  O   GLU B 310      18.777  81.615  17.951  1.00 19.72           O  
ANISOU 4878  O   GLU B 310     3199   1993   2299    357    723    293       O  
ATOM   4879  CB  GLU B 310      21.225  79.676  19.091  1.00 24.40           C  
ANISOU 4879  CB  GLU B 310     3814   2664   2792    340    683    290       C  
ATOM   4880  CG  GLU B 310      20.101  78.701  18.800  1.00 27.07           C  
ANISOU 4880  CG  GLU B 310     4121   2979   3183    356    694    316       C  
ATOM   4881  CD  GLU B 310      20.053  78.292  17.333  1.00 31.54           C  
ANISOU 4881  CD  GLU B 310     4669   3526   3785    342    668    311       C  
ATOM   4882  OE1 GLU B 310      21.123  77.944  16.796  1.00 33.85           O  
ANISOU 4882  OE1 GLU B 310     4966   3824   4069    328    653    298       O  
ATOM   4883  OE2 GLU B 310      18.962  78.356  16.718  1.00 27.01           O  
ANISOU 4883  OE2 GLU B 310     4080   2935   3248    336    665    324       O  
ATOM   4884  N   ALA B 311      19.856  82.567  19.721  1.00 19.58           N  
ANISOU 4884  N   ALA B 311     3249   2000   2187    340    771    242       N  
ATOM   4885  CA  ALA B 311      18.710  83.364  20.120  1.00 20.25           C  
ANISOU 4885  CA  ALA B 311     3335   2039   2318    353    840    242       C  
ATOM   4886  C   ALA B 311      18.297  84.350  19.023  1.00 21.95           C  
ANISOU 4886  C   ALA B 311     3522   2214   2603    363    838    253       C  
ATOM   4887  O   ALA B 311      17.096  84.498  18.737  1.00 20.46           O  
ANISOU 4887  O   ALA B 311     3291   1984   2497    383    864    294       O  
ATOM   4888  CB  ALA B 311      19.015  84.048  21.428  1.00 21.97           C  
ANISOU 4888  CB  ALA B 311     3611   2261   2473    325    901    199       C  
ATOM   4889  N   ILE B 312      19.286  84.951  18.335  1.00 20.34           N  
ANISOU 4889  N   ILE B 312     3330   2025   2372    346    800    230       N  
ATOM   4890  CA  ILE B 312      18.992  85.821  17.230  1.00 19.79           C  
ANISOU 4890  CA  ILE B 312     3229   1925   2362    350    788    252       C  
ATOM   4891  C   ILE B 312      18.359  85.033  16.075  1.00 19.12           C  
ANISOU 4891  C   ILE B 312     3096   1849   2319    349    729    306       C  
ATOM   4892  O   ILE B 312      17.341  85.489  15.467  1.00 19.67           O  
ANISOU 4892  O   ILE B 312     3117   1888   2467    354    730    361       O  
ATOM   4893  CB  ILE B 312      20.242  86.636  16.823  1.00 20.57           C  
ANISOU 4893  CB  ILE B 312     3358   2039   2417    330    765    213       C  
ATOM   4894  CG1 ILE B 312      20.631  87.639  17.920  1.00 22.31           C  
ANISOU 4894  CG1 ILE B 312     3626   2242   2607    318    833    161       C  
ATOM   4895  CG2 ILE B 312      19.987  87.350  15.508  1.00 22.25           C  
ANISOU 4895  CG2 ILE B 312     3533   2232   2688    330    737    248       C  
ATOM   4896  CD1 ILE B 312      22.078  88.078  17.900  1.00 21.61           C  
ANISOU 4896  CD1 ILE B 312     3575   2186   2448    288    802    117       C  
ATOM   4897  N   ARG B 313      18.939  83.880  15.726  1.00 20.51           N  
ANISOU 4897  N   ARG B 313     3281   2063   2448    333    680    297       N  
ATOM   4898  CA  ARG B 313      18.387  83.018  14.677  1.00 21.80           C  
ANISOU 4898  CA  ARG B 313     3412   2235   2633    313    633    333       C  
ATOM   4899  C   ARG B 313      16.935  82.629  14.984  1.00 22.84           C  
ANISOU 4899  C   ARG B 313     3502   2345   2828    328    652    384       C  
ATOM   4900  O   ARG B 313      16.091  82.660  14.085  1.00 23.81           O  
ANISOU 4900  O   ARG B 313     3583   2464   2998    306    618    438       O  
ATOM   4901  CB  ARG B 313      19.217  81.753  14.483  1.00 22.99           C  
ANISOU 4901  CB  ARG B 313     3583   2413   2737    295    609    306       C  
ATOM   4902  CG  ARG B 313      20.517  81.968  13.730  1.00 22.85           C  
ANISOU 4902  CG  ARG B 313     3592   2411   2677    271    584    271       C  
ATOM   4903  CD  ARG B 313      21.019  80.679  13.083  1.00 23.23           C  
ANISOU 4903  CD  ARG B 313     3648   2466   2712    243    573    256       C  
ATOM   4904  NE  ARG B 313      22.305  80.905  12.415  1.00 22.08           N  
ANISOU 4904  NE  ARG B 313     3526   2325   2536    223    564    223       N  
ATOM   4905  CZ  ARG B 313      22.436  81.231  11.150  1.00 20.03           C  
ANISOU 4905  CZ  ARG B 313     3279   2067   2263    179    541    215       C  
ATOM   4906  NH1 ARG B 313      21.352  81.417  10.411  1.00 19.29           N  
ANISOU 4906  NH1 ARG B 313     3170   1978   2178    146    513    248       N  
ATOM   4907  NH2 ARG B 313      23.656  81.313  10.631  1.00 19.74           N  
ANISOU 4907  NH2 ARG B 313     3266   2029   2204    164    546    183       N  
ATOM   4908  N   GLN B 314      16.655  82.315  16.253  1.00 22.12           N  
ANISOU 4908  N   GLN B 314     3422   2243   2739    357    705    374       N  
ATOM   4909  CA  GLN B 314      15.305  81.968  16.695  1.00 24.66           C  
ANISOU 4909  CA  GLN B 314     3705   2537   3127    377    737    420       C  
ATOM   4910  C   GLN B 314      14.379  83.186  16.835  1.00 23.56           C  
ANISOU 4910  C   GLN B 314     3531   2346   3074    397    788    459       C  
ATOM   4911  O   GLN B 314      13.175  82.996  17.120  1.00 23.47           O  
ANISOU 4911  O   GLN B 314     3475   2302   3139    415    820    511       O  
ATOM   4912  CB  GLN B 314      15.361  81.254  18.054  1.00 23.66           C  
ANISOU 4912  CB  GLN B 314     3606   2416   2968    397    784    397       C  
ATOM   4913  CG  GLN B 314      16.102  79.920  18.021  1.00 25.05           C  
ANISOU 4913  CG  GLN B 314     3795   2629   3091    385    746    381       C  
ATOM   4914  CD  GLN B 314      15.459  78.896  17.125  1.00 28.27           C  
ANISOU 4914  CD  GLN B 314     4167   3037   3536    367    708    413       C  
ATOM   4915  OE1 GLN B 314      14.273  78.942  16.848  1.00 29.90           O  
ANISOU 4915  OE1 GLN B 314     4333   3222   3804    368    709    458       O  
ATOM   4916  NE2 GLN B 314      16.245  77.936  16.676  1.00 28.28           N  
ANISOU 4916  NE2 GLN B 314     4181   3058   3505    346    681    392       N  
ATOM   4917  N   ASN B 315      14.915  84.411  16.798  1.00 22.95           N  
ANISOU 4917  N   ASN B 315     3471   2251   2995    399    813    436       N  
ATOM   4918  CA  ASN B 315      14.073  85.607  16.823  1.00 25.47           C  
ANISOU 4918  CA  ASN B 315     3749   2507   3419    419    874    479       C  
ATOM   4919  C   ASN B 315      13.370  85.705  18.192  1.00 26.19           C  
ANISOU 4919  C   ASN B 315     3853   2549   3549    448    984    465       C  
ATOM   4920  O   ASN B 315      12.176  85.991  18.253  1.00 25.17           O  
ANISOU 4920  O   ASN B 315     3664   2362   3535    471   1036    529       O  
ATOM   4921  CB  ASN B 315      13.022  85.579  15.704  1.00 27.00           C  
ANISOU 4921  CB  ASN B 315     3858   2693   3708    411    821    582       C  
ATOM   4922  CG  ASN B 315      12.396  86.930  15.456  1.00 30.63           C  
ANISOU 4922  CG  ASN B 315     4259   3089   4289    429    870    646       C  
ATOM   4923  OD1 ASN B 315      13.031  87.954  15.679  1.00 34.26           O  
ANISOU 4923  OD1 ASN B 315     4750   3522   4745    437    919    603       O  
ATOM   4924  ND2 ASN B 315      11.170  86.951  14.959  1.00 35.01           N  
ANISOU 4924  ND2 ASN B 315     4723   3618   4960    432    855    757       N  
ATOM   4925  N   ASP B 316      14.135  85.484  19.270  1.00 23.32           N  
ANISOU 4925  N   ASP B 316     3564   2207   3088    438   1021    388       N  
ATOM   4926  CA  ASP B 316      13.594  85.309  20.599  1.00 24.98           C  
ANISOU 4926  CA  ASP B 316     3804   2389   3298    447   1116    366       C  
ATOM   4927  C   ASP B 316      14.222  86.359  21.504  1.00 23.12           C  
ANISOU 4927  C   ASP B 316     3642   2131   3012    424   1204    289       C  
ATOM   4928  O   ASP B 316      15.355  86.174  21.953  1.00 21.15           O  
ANISOU 4928  O   ASP B 316     3455   1939   2641    389   1172    232       O  
ATOM   4929  CB  ASP B 316      13.917  83.906  21.120  1.00 25.17           C  
ANISOU 4929  CB  ASP B 316     3854   2474   3235    438   1071    353       C  
ATOM   4930  CG  ASP B 316      13.233  83.506  22.416  1.00 30.84           C  
ANISOU 4930  CG  ASP B 316     4595   3171   3950    444   1157    346       C  
ATOM   4931  OD1 ASP B 316      13.101  84.351  23.334  1.00 28.47           O  
ANISOU 4931  OD1 ASP B 316     4340   2829   3645    432   1263    304       O  
ATOM   4932  OD2 ASP B 316      12.869  82.306  22.505  1.00 39.66           O  
ANISOU 4932  OD2 ASP B 316     5690   4314   5066    455   1123    378       O  
ATOM   4933  N   LEU B 317      13.476  87.439  21.763  1.00 24.16           N  
ANISOU 4933  N   LEU B 317     3759   2175   3243    437   1317    294       N  
ATOM   4934  CA  LEU B 317      14.013  88.587  22.449  1.00 24.01           C  
ANISOU 4934  CA  LEU B 317     3809   2121   3192    406   1414    216       C  
ATOM   4935  C   LEU B 317      14.407  88.212  23.877  1.00 23.67           C  
ANISOU 4935  C   LEU B 317     3860   2110   3020    358   1467    142       C  
ATOM   4936  O   LEU B 317      15.470  88.648  24.351  1.00 23.06           O  
ANISOU 4936  O   LEU B 317     3860   2071   2831    303   1468     70       O  
ATOM   4937  CB  LEU B 317      12.986  89.717  22.452  1.00 26.34           C  
ANISOU 4937  CB  LEU B 317     4061   2297   3647    433   1548    244       C  
ATOM   4938  CG  LEU B 317      13.323  90.903  23.357  1.00 26.58           C  
ANISOU 4938  CG  LEU B 317     4173   2265   3659    394   1693    152       C  
ATOM   4939  CD1 LEU B 317      14.658  91.540  22.999  1.00 27.32           C  
ANISOU 4939  CD1 LEU B 317     4313   2403   3662    355   1635     94       C  
ATOM   4940  CD2 LEU B 317      12.217  91.917  23.287  1.00 27.59           C  
ANISOU 4940  CD2 LEU B 317     4241   2259   3980    430   1839    194       C  
ATOM   4941  N   LEU B 318      13.556  87.418  24.544  1.00 23.94           N  
ANISOU 4941  N   LEU B 318     3890   2136   3070    371   1508    165       N  
ATOM   4942  CA  LEU B 318      13.838  86.954  25.915  1.00 24.32           C  
ANISOU 4942  CA  LEU B 318     4024   2224   2991    318   1554    109       C  
ATOM   4943  C   LEU B 318      15.191  86.236  25.967  1.00 22.07           C  
ANISOU 4943  C   LEU B 318     3776   2054   2556    278   1425     93       C  
ATOM   4944  O   LEU B 318      15.965  86.499  26.849  1.00 22.24           O  
ANISOU 4944  O   LEU B 318     3879   2116   2455    209   1445     35       O  
ATOM   4945  CB  LEU B 318      12.695  86.081  26.449  1.00 24.78           C  
ANISOU 4945  CB  LEU B 318     4056   2259   3100    347   1601    152       C  
ATOM   4946  CG  LEU B 318      11.352  86.793  26.620  1.00 26.99           C  
ANISOU 4946  CG  LEU B 318     4302   2417   3537    381   1753    171       C  
ATOM   4947  CD1 LEU B 318      10.237  85.800  26.874  1.00 27.43           C  
ANISOU 4947  CD1 LEU B 318     4307   2456   3659    420   1769    234       C  
ATOM   4948  CD2 LEU B 318      11.418  87.833  27.731  1.00 28.79           C  
ANISOU 4948  CD2 LEU B 318     4627   2585   3726    322   1920     78       C  
ATOM   4949  N   ALA B 319      15.463  85.332  25.018  1.00 23.25           N  
ANISOU 4949  N   ALA B 319     3862   2251   2719    315   1298    150       N  
ATOM   4950  CA  ALA B 319      16.720  84.560  25.016  1.00 22.64           C  
ANISOU 4950  CA  ALA B 319     3803   2269   2530    286   1186    149       C  
ATOM   4951  C   ALA B 319      17.924  85.483  24.753  1.00 22.58           C  
ANISOU 4951  C   ALA B 319     3832   2284   2462    247   1156    103       C  
ATOM   4952  O   ALA B 319      18.982  85.286  25.349  1.00 21.52           O  
ANISOU 4952  O   ALA B 319     3742   2217   2214    194   1113     84       O  
ATOM   4953  CB  ALA B 319      16.648  83.427  24.014  1.00 22.92           C  
ANISOU 4953  CB  ALA B 319     3766   2329   2613    332   1087    212       C  
ATOM   4954  N   VAL B 320      17.751  86.508  23.896  1.00 22.29           N  
ANISOU 4954  N   VAL B 320     3772   2190   2506    270   1179     93       N  
ATOM   4955  CA  VAL B 320      18.825  87.475  23.649  1.00 22.41           C  
ANISOU 4955  CA  VAL B 320     3821   2216   2474    234   1162     47       C  
ATOM   4956  C   VAL B 320      19.086  88.295  24.908  1.00 22.70           C  
ANISOU 4956  C   VAL B 320     3948   2246   2429    162   1258    -27       C  
ATOM   4957  O   VAL B 320      20.251  88.510  25.238  1.00 21.24           O  
ANISOU 4957  O   VAL B 320     3812   2120   2138    102   1214    -62       O  
ATOM   4958  CB  VAL B 320      18.602  88.406  22.446  1.00 22.78           C  
ANISOU 4958  CB  VAL B 320     3820   2205   2628    272   1165     61       C  
ATOM   4959  CG1 VAL B 320      19.836  89.272  22.238  1.00 24.51           C  
ANISOU 4959  CG1 VAL B 320     4077   2445   2788    233   1140     12       C  
ATOM   4960  CG2 VAL B 320      18.310  87.654  21.160  1.00 22.56           C  
ANISOU 4960  CG2 VAL B 320     3714   2191   2666    320   1072    132       C  
ATOM   4961  N   MET B 321      18.010  88.718  25.594  1.00 22.23           N  
ANISOU 4961  N   MET B 321     3912   2114   2419    161   1389    -49       N  
ATOM   4962  CA  MET B 321      18.156  89.402  26.841  1.00 23.82           C  
ANISOU 4962  CA  MET B 321     4212   2304   2533     77   1498   -129       C  
ATOM   4963  C   MET B 321      18.955  88.529  27.816  1.00 24.30           C  
ANISOU 4963  C   MET B 321     4329   2475   2428      4   1429   -133       C  
ATOM   4964  O   MET B 321      19.871  89.031  28.483  1.00 23.88           O  
ANISOU 4964  O   MET B 321     4353   2469   2251    -89   1430   -189       O  
ATOM   4965  CB  MET B 321      16.811  89.795  27.460  1.00 25.61           C  
ANISOU 4965  CB  MET B 321     4453   2430   2848     89   1665   -148       C  
ATOM   4966  CG  MET B 321      16.017  90.823  26.648  1.00 25.49           C  
ANISOU 4966  CG  MET B 321     4378   2294   3013    151   1754   -133       C  
ATOM   4967  SD  MET B 321      14.399  91.094  27.338  1.00 27.31           S  
ANISOU 4967  SD  MET B 321     4601   2398   3378    176   1951   -130       S  
ATOM   4968  CE  MET B 321      14.893  92.022  28.785  1.00 31.64           C  
ANISOU 4968  CE  MET B 321     5304   2923   3793     50   2110   -269       C  
ATOM   4969  N   ILE B 322      18.596  87.238  27.911  1.00 24.37           N  
ANISOU 4969  N   ILE B 322     4296   2525   2436     40   1370    -68       N  
ATOM   4970  CA  ILE B 322      19.234  86.337  28.903  1.00 24.73           C  
ANISOU 4970  CA  ILE B 322     4382   2673   2341    -26   1310    -50       C  
ATOM   4971  C   ILE B 322      20.700  86.151  28.495  1.00 22.89           C  
ANISOU 4971  C   ILE B 322     4134   2524   2039    -53   1175    -26       C  
ATOM   4972  O   ILE B 322      21.586  86.238  29.339  1.00 23.05           O  
ANISOU 4972  O   ILE B 322     4212   2619   1926   -149   1145    -40       O  
ATOM   4973  CB  ILE B 322      18.463  85.002  29.028  1.00 24.88           C  
ANISOU 4973  CB  ILE B 322     4349   2704   2400     27   1287     20       C  
ATOM   4974  CG1 ILE B 322      17.145  85.185  29.776  1.00 24.76           C  
ANISOU 4974  CG1 ILE B 322     4365   2616   2423     28   1430     -4       C  
ATOM   4975  CG2 ILE B 322      19.305  83.886  29.649  1.00 23.90           C  
ANISOU 4975  CG2 ILE B 322     4226   2689   2165    -17   1185     75       C  
ATOM   4976  CD1 ILE B 322      16.044  84.293  29.261  1.00 24.75           C  
ANISOU 4976  CD1 ILE B 322     4280   2574   2547    121   1426     62       C  
ATOM   4977  N   ALA B 323      20.937  85.941  27.196  1.00 23.12           N  
ANISOU 4977  N   ALA B 323     4085   2539   2160     22   1099     10       N  
ATOM   4978  CA  ALA B 323      22.284  85.687  26.657  1.00 24.97           C  
ANISOU 4978  CA  ALA B 323     4291   2838   2358     12    981     39       C  
ATOM   4979  C   ALA B 323      23.228  86.842  27.036  1.00 28.04           C  
ANISOU 4979  C   ALA B 323     4745   3247   2659    -72    991    -21       C  
ATOM   4980  O   ALA B 323      24.373  86.611  27.508  1.00 26.32           O  
ANISOU 4980  O   ALA B 323     4543   3114   2344   -140    913      0       O  
ATOM   4981  CB  ALA B 323      22.214  85.511  25.166  1.00 25.53           C  
ANISOU 4981  CB  ALA B 323     4286   2869   2543     97    933     67       C  
ATOM   4982  N   ASP B 324      22.721  88.083  26.907  1.00 26.51           N  
ANISOU 4982  N   ASP B 324     4589   2976   2505    -75   1092    -92       N  
ATOM   4983  CA  ASP B 324      23.500  89.272  27.263  1.00 28.59           C  
ANISOU 4983  CA  ASP B 324     4922   3244   2695   -160   1122   -163       C  
ATOM   4984  C   ASP B 324      23.779  89.337  28.773  1.00 28.41           C  
ANISOU 4984  C   ASP B 324     4995   3282   2516   -287   1156   -200       C  
ATOM   4985  O   ASP B 324      24.843  89.749  29.197  1.00 29.53           O  
ANISOU 4985  O   ASP B 324     5182   3486   2549   -382   1112   -222       O  
ATOM   4986  CB  ASP B 324      22.804  90.530  26.763  1.00 32.04           C  
ANISOU 4986  CB  ASP B 324     5368   3570   3234   -128   1238   -223       C  
ATOM   4987  CG  ASP B 324      23.150  90.867  25.318  1.00 31.75           C  
ANISOU 4987  CG  ASP B 324     5260   3505   3297    -55   1177   -196       C  
ATOM   4988  OD1 ASP B 324      24.121  90.267  24.789  1.00 36.82           O  
ANISOU 4988  OD1 ASP B 324     5864   4213   3909    -46   1055   -153       O  
ATOM   4989  OD2 ASP B 324      22.468  91.752  24.739  1.00 39.60           O  
ANISOU 4989  OD2 ASP B 324     6235   4407   4402    -12   1259   -214       O  
ATOM   4990  N   LYS B 325      22.815  88.932  29.594  1.00 28.78           N  
ANISOU 4990  N   LYS B 325     5073   3313   2545   -299   1235   -205       N  
ATOM   4991  CA  LYS B 325      23.010  88.889  31.042  1.00 30.44           C  
ANISOU 4991  CA  LYS B 325     5380   3590   2593   -431   1267   -235       C  
ATOM   4992  C   LYS B 325      24.078  87.857  31.443  1.00 31.64           C  
ANISOU 4992  C   LYS B 325     5507   3876   2637   -483   1113   -145       C  
ATOM   4993  O   LYS B 325      24.743  88.036  32.469  1.00 31.82           O  
ANISOU 4993  O   LYS B 325     5604   3981   2503   -621   1093   -159       O  
ATOM   4994  CB  LYS B 325      21.693  88.583  31.760  1.00 31.00           C  
ANISOU 4994  CB  LYS B 325     5484   3611   2683   -423   1389   -250       C  
ATOM   4995  CG  LYS B 325      20.767  89.787  31.899  1.00 33.71           C  
ANISOU 4995  CG  LYS B 325     5886   3828   3094   -429   1578   -350       C  
ATOM   4996  CD  LYS B 325      19.428  89.465  32.511  1.00 34.35           C  
ANISOU 4996  CD  LYS B 325     5985   3844   3220   -407   1706   -357       C  
ATOM   4997  CE  LYS B 325      18.464  90.619  32.359  1.00 37.35           C  
ANISOU 4997  CE  LYS B 325     6386   4073   3730   -378   1896   -431       C  
ATOM   4998  NZ  LYS B 325      18.959  91.844  33.025  1.00 37.66           N  
ANISOU 4998  NZ  LYS B 325     6544   4090   3675   -507   2006   -547       N  
ATOM   4999  N   LEU B 326      24.216  86.774  30.671  1.00 29.85           N  
ANISOU 4999  N   LEU B 326     5174   3669   2496   -383   1010    -50       N  
ATOM   5000  CA  LEU B 326      25.172  85.699  30.996  1.00 32.72           C  
ANISOU 5000  CA  LEU B 326     5492   4143   2796   -415    875     53       C  
ATOM   5001  C   LEU B 326      26.597  86.009  30.495  1.00 36.59           C  
ANISOU 5001  C   LEU B 326     5950   4682   3268   -444    770     79       C  
ATOM   5002  O   LEU B 326      27.542  85.439  31.030  1.00 38.90           O  
ANISOU 5002  O   LEU B 326     6221   5072   3483   -511    669    160       O  
ATOM   5003  CB  LEU B 326      24.646  84.385  30.404  1.00 31.81           C  
ANISOU 5003  CB  LEU B 326     5281   4010   2796   -297    836    137       C  
ATOM   5004  CG  LEU B 326      23.395  83.850  31.094  1.00 31.54           C  
ANISOU 5004  CG  LEU B 326     5268   3951   2762   -284    918    137       C  
ATOM   5005  CD1 LEU B 326      22.947  82.538  30.482  1.00 31.20           C  
ANISOU 5005  CD1 LEU B 326     5129   3892   2833   -175    875    219       C  
ATOM   5006  CD2 LEU B 326      23.639  83.700  32.588  1.00 33.10           C  
ANISOU 5006  CD2 LEU B 326     5540   4239   2796   -416    918    152       C  
ATOM   5007  N   LEU B 327      26.746  86.911  29.511  1.00 34.88           N  
ANISOU 5007  N   LEU B 327     5727   4399   3126   -397    793     20       N  
ATOM   5008  CA  LEU B 327      28.058  87.276  28.963  1.00 41.13           C  
ANISOU 5008  CA  LEU B 327     6489   5226   3913   -418    705     38       C  
ATOM   5009  C   LEU B 327      28.813  88.210  29.919  1.00 45.10           C  
ANISOU 5009  C   LEU B 327     7080   5788   4266   -571    705    -10       C  
ATOM   5010  O   LEU B 327      28.211  89.088  30.528  1.00 51.10           O  
ANISOU 5010  O   LEU B 327     7936   6512   4967   -636    815   -107       O  
ATOM   5011  CB  LEU B 327      27.840  87.932  27.600  1.00 40.71           C  
ANISOU 5011  CB  LEU B 327     6402   5078   3986   -319    739     -8       C  
ATOM   5012  CG  LEU B 327      27.615  86.930  26.472  1.00 43.94           C  
ANISOU 5012  CG  LEU B 327     6714   5457   4524   -196    694     57       C  
ATOM   5013  CD1 LEU B 327      26.932  87.583  25.280  1.00 44.58           C  
ANISOU 5013  CD1 LEU B 327     6777   5442   4717   -111    750      9       C  
ATOM   5014  CD2 LEU B 327      28.933  86.294  26.057  1.00 41.79           C  
ANISOU 5014  CD2 LEU B 327     6374   5240   4262   -194    581    136       C  
TER    5015      LEU B 327                                                      
ATOM   5016  N   MET C   1     -21.939 118.068  62.783  1.00 57.99           N  
ATOM   5017  CA  MET C   1     -21.116 117.142  61.933  1.00 60.48           C  
ATOM   5018  C   MET C   1     -19.847 116.737  62.695  1.00 48.68           C  
ATOM   5019  O   MET C   1     -19.076 117.584  63.133  1.00 47.03           O  
ATOM   5020  CB  MET C   1     -20.721 117.807  60.607  1.00 64.68           C  
ATOM   5021  CG  MET C   1     -19.706 117.003  59.804  1.00 61.86           C  
ATOM   5022  SD  MET C   1     -19.388 117.643  58.143  1.00 72.72           S  
ATOM   5023  CE  MET C   1     -20.916 117.209  57.309  1.00 76.45           C  
ATOM   5024  N   LYS C   2     -19.608 115.426  62.796  1.00 43.19           N  
ATOM   5025  CA  LYS C   2     -18.447 114.908  63.505  1.00 38.23           C  
ATOM   5026  C   LYS C   2     -17.169 115.119  62.675  1.00 31.39           C  
ATOM   5027  O   LYS C   2     -17.202 115.259  61.448  1.00 28.42           O  
ATOM   5028  CB  LYS C   2     -18.672 113.431  63.841  1.00 44.73           C  
ATOM   5029  CG  LYS C   2     -19.952 113.151  64.619  1.00 48.04           C  
ATOM   5030  CD  LYS C   2     -19.744 112.332  65.867  1.00 46.58           C  
ATOM   5031  CE  LYS C   2     -21.012 112.180  66.683  1.00 55.19           C  
ATOM   5032  NZ  LYS C   2     -21.315 113.409  67.456  1.00 54.94           N  
ATOM   5033  N   LYS C   3     -16.031 115.140  63.370  1.00 26.70           N  
ATOM   5034  CA  LYS C   3     -14.725 115.261  62.747  1.00 27.16           C  
ATOM   5035  C   LYS C   3     -14.333 113.950  62.065  1.00 28.98           C  
ATOM   5036  O   LYS C   3     -13.763 113.972  60.967  1.00 27.57           O  
ATOM   5037  CB  LYS C   3     -13.658 115.630  63.779  1.00 28.66           C  
ATOM   5038  CG  LYS C   3     -13.790 117.047  64.327  1.00 30.01           C  
ATOM   5039  CD  LYS C   3     -12.748 117.394  65.369  1.00 34.60           C  
ATOM   5040  CE  LYS C   3     -12.896 118.823  65.862  1.00 39.48           C  
ATOM   5041  NZ  LYS C   3     -11.992 119.096  67.003  1.00 42.65           N  
ATOM   5042  N   VAL C   4     -14.602 112.826  62.743  1.00 27.81           N  
ATOM   5043  CA  VAL C   4     -14.112 111.501  62.329  1.00 27.07           C  
ATOM   5044  C   VAL C   4     -15.167 110.441  62.644  1.00 29.26           C  
ATOM   5045  O   VAL C   4     -15.720 110.433  63.751  1.00 28.37           O  
ATOM   5046  CB  VAL C   4     -12.787 111.134  63.022  1.00 26.79           C  
ATOM   5047  CG1 VAL C   4     -12.271 109.781  62.536  1.00 31.94           C  
ATOM   5048  CG2 VAL C   4     -11.732 112.209  62.847  1.00 30.71           C  
ATOM   5049  N   SER C   5     -15.407 109.552  61.667  1.00 28.50           N  
ATOM   5050  CA  SER C   5     -16.071 108.267  61.860  1.00 24.48           C  
ATOM   5051  C   SER C   5     -15.039 107.140  61.750  1.00 27.76           C  
ATOM   5052  O   SER C   5     -14.446 106.954  60.698  1.00 25.09           O  
ATOM   5053  CB  SER C   5     -17.167 108.023  60.857  1.00 27.42           C  
ATOM   5054  OG  SER C   5     -18.173 109.015  60.909  1.00 35.46           O  
ATOM   5055  N   VAL C   6     -14.856 106.365  62.826  1.00 23.99           N  
ATOM   5056  CA  VAL C   6     -14.104 105.124  62.748  1.00 23.79           C  
ATOM   5057  C   VAL C   6     -15.085 104.022  62.335  1.00 25.65           C  
ATOM   5058  O   VAL C   6     -16.091 103.812  63.002  1.00 27.53           O  
ATOM   5059  CB  VAL C   6     -13.364 104.806  64.061  1.00 23.51           C  
ATOM   5060  CG1 VAL C   6     -12.590 103.496  63.972  1.00 25.63           C  
ATOM   5061  CG2 VAL C   6     -12.432 105.939  64.456  1.00 22.75           C  
ATOM   5062  N   ILE C   7     -14.798 103.367  61.201  1.00 24.60           N  
ATOM   5063  CA  ILE C   7     -15.639 102.335  60.614  1.00 26.05           C  
ATOM   5064  C   ILE C   7     -14.939 100.981  60.795  1.00 27.14           C  
ATOM   5065  O   ILE C   7     -13.823 100.768  60.292  1.00 22.98           O  
ATOM   5066  CB  ILE C   7     -15.940 102.655  59.133  1.00 30.02           C  
ATOM   5067  CG1 ILE C   7     -16.762 103.940  59.005  1.00 33.77           C  
ATOM   5068  CG2 ILE C   7     -16.615 101.484  58.435  1.00 29.38           C  
ATOM   5069  CD1 ILE C   7     -17.015 104.386  57.585  1.00 34.75           C  
ATOM   5070  N   MET C   8     -15.611 100.070  61.513  1.00 26.36           N  
ATOM   5071  CA  MET C   8     -15.020  98.792  61.904  1.00 27.69           C  
ATOM   5072  C   MET C   8     -15.962  97.644  61.554  1.00 28.67           C  
ATOM   5073  O   MET C   8     -17.002  97.474  62.187  1.00 29.98           O  
ATOM   5074  CB  MET C   8     -14.725  98.763  63.404  1.00 27.20           C  
ATOM   5075  CG  MET C   8     -13.901  97.576  63.829  1.00 31.74           C  
ATOM   5076  SD  MET C   8     -13.624  97.536  65.613  1.00 38.85           S  
ATOM   5077  CE  MET C   8     -15.223  96.923  66.134  1.00 41.49           C  
ATOM   5078  N   PRO C   9     -15.614  96.806  60.548  1.00 28.74           N  
ATOM   5079  CA  PRO C   9     -16.372  95.597  60.260  1.00 29.22           C  
ATOM   5080  C   PRO C   9     -15.998  94.527  61.292  1.00 24.23           C  
ATOM   5081  O   PRO C   9     -14.859  94.497  61.759  1.00 27.85           O  
ATOM   5082  CB  PRO C   9     -15.946  95.196  58.836  1.00 30.43           C  
ATOM   5083  CG  PRO C   9     -14.648  95.925  58.565  1.00 31.02           C  
ATOM   5084  CD  PRO C   9     -14.447  96.950  59.664  1.00 34.37           C  
ATOM   5085  N   THR C  10     -16.971  93.686  61.652  1.00 27.62           N  
ATOM   5086  CA  THR C  10     -16.760  92.564  62.582  1.00 28.81           C  
ATOM   5087  C   THR C  10     -17.367  91.279  62.003  1.00 29.04           C  
ATOM   5088  O   THR C  10     -18.338  91.317  61.219  1.00 26.25           O  
ATOM   5089  CB  THR C  10     -17.358  92.840  63.972  1.00 29.05           C  
ATOM   5090  OG1 THR C  10     -18.776  92.970  63.850  1.00 24.82           O  
ATOM   5091  CG2 THR C  10     -16.789  94.084  64.616  1.00 30.06           C  
ATOM   5092  N   PHE C  11     -16.778  90.147  62.410  1.00 30.33           N  
ATOM   5093  CA  PHE C  11     -17.302  88.807  62.133  1.00 35.17           C  
ATOM   5094  C   PHE C  11     -16.632  87.814  63.086  1.00 33.73           C  
ATOM   5095  O   PHE C  11     -15.441  87.589  62.997  1.00 31.41           O  
ATOM   5096  CB  PHE C  11     -17.061  88.412  60.676  1.00 41.60           C  
ATOM   5097  CG  PHE C  11     -17.596  87.048  60.321  1.00 41.58           C  
ATOM   5098  CD1 PHE C  11     -18.956  86.853  60.125  1.00 40.21           C  
ATOM   5099  CD2 PHE C  11     -16.747  85.960  60.211  1.00 44.38           C  
ATOM   5100  CE1 PHE C  11     -19.455  85.596  59.817  1.00 47.72           C  
ATOM   5101  CE2 PHE C  11     -17.247  84.702  59.903  1.00 48.03           C  
ATOM   5102  CZ  PHE C  11     -18.598  84.525  59.700  1.00 48.02           C  
ATOM   5103  N   ASN C  12     -17.410  87.277  64.032  1.00 36.10           N  
ATOM   5104  CA  ASN C  12     -16.990  86.163  64.904  1.00 37.10           C  
ATOM   5105  C   ASN C  12     -15.722  86.508  65.701  1.00 37.81           C  
ATOM   5106  O   ASN C  12     -14.887  85.634  65.942  1.00 40.71           O  
ATOM   5107  CB  ASN C  12     -16.792  84.871  64.100  1.00 36.80           C  
ATOM   5108  CG  ASN C  12     -18.093  84.175  63.756  1.00 41.74           C  
ATOM   5109  OD1 ASN C  12     -19.169  84.776  63.783  1.00 39.12           O  
ATOM   5110  ND2 ASN C  12     -18.008  82.892  63.442  1.00 53.34           N  
ATOM   5111  N   ASN C  13     -15.599  87.760  66.156  1.00 29.00           N  
ATOM   5112  CA  ASN C  13     -14.419  88.194  66.923  1.00 29.32           C  
ATOM   5113  C   ASN C  13     -14.589  87.908  68.419  1.00 30.28           C  
ATOM   5114  O   ASN C  13     -13.592  87.733  69.115  1.00 33.64           O  
ATOM   5115  CB  ASN C  13     -14.140  89.686  66.761  1.00 27.56           C  
ATOM   5116  CG  ASN C  13     -13.930  90.052  65.313  1.00 24.93           C  
ATOM   5117  OD1 ASN C  13     -14.878  90.404  64.629  1.00 26.26           O  
ATOM   5118  ND2 ASN C  13     -12.716  89.877  64.825  1.00 36.20           N  
ATOM   5119  N   GLY C  14     -15.838  87.949  68.905  1.00 32.40           N  
ATOM   5120  CA  GLY C  14     -16.141  87.762  70.321  1.00 35.93           C  
ATOM   5121  C   GLY C  14     -15.328  88.702  71.203  1.00 37.82           C  
ATOM   5122  O   GLY C  14     -15.120  89.859  70.857  1.00 36.40           O  
ATOM   5123  N   GLU C  15     -14.812  88.172  72.315  1.00 33.34           N  
ATOM   5124  CA  GLU C  15     -14.286  88.960  73.444  1.00 39.57           C  
ATOM   5125  C   GLU C  15     -13.001  89.708  73.055  1.00 38.11           C  
ATOM   5126  O   GLU C  15     -12.614  90.670  73.734  1.00 33.20           O  
ATOM   5127  CB  GLU C  15     -14.019  88.045  74.646  1.00 45.64           C  
ATOM   5128  CG  GLU C  15     -15.228  87.233  75.097  1.00 57.15           C  
ATOM   5129  CD  GLU C  15     -15.998  87.801  76.277  1.00 67.76           C  
ATOM   5130  OE1 GLU C  15     -15.367  88.041  77.324  1.00 97.35           O  
ATOM   5131  OE2 GLU C  15     -17.227  87.990  76.150  1.00 83.50           O  
ATOM   5132  N   LYS C  16     -12.330  89.255  71.986  1.00 31.97           N  
ATOM   5133  CA  LYS C  16     -11.153  89.941  71.438  1.00 33.00           C  
ATOM   5134  C   LYS C  16     -11.485  91.411  71.123  1.00 32.21           C  
ATOM   5135  O   LYS C  16     -10.618  92.273  71.274  1.00 37.67           O  
ATOM   5136  CB  LYS C  16     -10.644  89.225  70.182  1.00 34.46           C  
ATOM   5137  N   LEU C  17     -12.732  91.683  70.704  1.00 30.58           N  
ATOM   5138  CA  LEU C  17     -13.204  93.031  70.323  1.00 31.74           C  
ATOM   5139  C   LEU C  17     -12.996  94.057  71.444  1.00 37.12           C  
ATOM   5140  O   LEU C  17     -12.839  95.248  71.138  1.00 34.29           O  
ATOM   5141  CB  LEU C  17     -14.697  92.992  69.985  1.00 30.28           C  
ATOM   5142  CG  LEU C  17     -15.088  92.875  68.520  1.00 32.00           C  
ATOM   5143  CD1 LEU C  17     -16.605  92.880  68.384  1.00 31.71           C  
ATOM   5144  CD2 LEU C  17     -14.480  93.991  67.679  1.00 36.03           C  
ATOM   5145  N   HIS C  18     -13.083  93.617  72.712  1.00 32.02           N  
ATOM   5146  CA  HIS C  18     -13.004  94.522  73.866  1.00 31.92           C  
ATOM   5147  C   HIS C  18     -11.785  95.434  73.731  1.00 31.38           C  
ATOM   5148  O   HIS C  18     -11.920  96.651  73.897  1.00 29.89           O  
ATOM   5149  CB  HIS C  18     -12.965  93.777  75.211  1.00 32.72           C  
ATOM   5150  CG  HIS C  18     -14.263  93.152  75.603  1.00 39.43           C  
ATOM   5151  ND1 HIS C  18     -15.430  93.884  75.722  1.00 40.80           N  
ATOM   5152  CD2 HIS C  18     -14.580  91.883  75.940  1.00 39.50           C  
ATOM   5153  CE1 HIS C  18     -16.414  93.085  76.085  1.00 43.65           C  
ATOM   5154  NE2 HIS C  18     -15.920  91.855  76.223  1.00 40.01           N  
ATOM   5155  N   ARG C  19     -10.610  94.837  73.478  1.00 37.27           N  
ANISOU 5155  N   ARG C  19     6602   3972   3584    376   1480    599       N  
ATOM   5156  CA  ARG C  19      -9.352  95.596  73.400  1.00 36.00           C  
ANISOU 5156  CA  ARG C  19     6399   3876   3400    455   1348    603       C  
ATOM   5157  C   ARG C  19      -9.446  96.662  72.289  1.00 32.41           C  
ANISOU 5157  C   ARG C  19     5809   3483   3020    390   1262    547       C  
ATOM   5158  O   ARG C  19      -9.040  97.838  72.464  1.00 28.24           O  
ANISOU 5158  O   ARG C  19     5227   3020   2481    418   1170    526       O  
ATOM   5159  CB  ARG C  19      -8.188  94.633  73.161  1.00 37.93           C  
ANISOU 5159  CB  ARG C  19     6708   4089   3615    526   1343    643       C  
ATOM   5160  CG  ARG C  19      -6.802  95.260  73.169  1.00 40.20           C  
ANISOU 5160  CG  ARG C  19     6951   4453   3868    611   1216    641       C  
ATOM   5161  CD  ARG C  19      -5.729  94.239  72.769  1.00 38.41           C  
ANISOU 5161  CD  ARG C  19     6776   4201   3616    681   1217    677       C  
ATOM   5162  NE  ARG C  19      -5.642  93.966  71.331  1.00 36.56           N  
ANISOU 5162  NE  ARG C  19     6481   3946   3462    607   1211    655       N  
ATOM   5163  CZ  ARG C  19      -4.712  93.209  70.747  1.00 34.22           C  
ANISOU 5163  CZ  ARG C  19     6208   3634   3158    655   1201    677       C  
ATOM   5164  NH1 ARG C  19      -3.675  92.770  71.443  1.00 31.32           N  
ANISOU 5164  NH1 ARG C  19     5906   3289   2703    787   1180    717       N  
ATOM   5165  NH2 ARG C  19      -4.840  92.853  69.471  1.00 34.34           N  
ANISOU 5165  NH2 ARG C  19     6183   3615   3247    580   1217    658       N  
ATOM   5166  N   THR C  20      -9.990  96.266  71.136  1.00 29.93           N  
ANISOU 5166  N   THR C  20     5446   3148   2776    306   1296    519       N  
ATOM   5167  CA  THR C  20     -10.112  97.183  70.001  1.00 29.24           C  
ANISOU 5167  CA  THR C  20     5244   3114   2750    257   1224    471       C  
ATOM   5168  C   THR C  20     -11.071  98.325  70.337  1.00 28.35           C  
ANISOU 5168  C   THR C  20     5076   3053   2641    235   1210    437       C  
ATOM   5169  O   THR C  20     -10.747  99.475  70.130  1.00 25.88           O  
ANISOU 5169  O   THR C  20     4711   2788   2332    254   1129    417       O  
ATOM   5170  CB  THR C  20     -10.600  96.467  68.742  1.00 31.51           C  
ANISOU 5170  CB  THR C  20     5492   3376   3102    176   1268    443       C  
ATOM   5171  OG1 THR C  20      -9.594  95.511  68.417  1.00 35.35           O  
ANISOU 5171  OG1 THR C  20     6034   3815   3581    208   1272    477       O  
ATOM   5172  CG2 THR C  20     -10.806  97.399  67.570  1.00 31.55           C  
ANISOU 5172  CG2 THR C  20     5386   3439   3160    139   1199    395       C  
ATOM   5173  N   ILE C  21     -12.271  97.993  70.816  1.00 27.27           N  
ANISOU 5173  N   ILE C  21     4952   2904   2503    193   1299    426       N  
ATOM   5174  CA  ILE C  21     -13.265  99.048  71.070  1.00 29.33           C  
ANISOU 5174  CA  ILE C  21     5155   3222   2767    178   1291    391       C  
ATOM   5175  C   ILE C  21     -12.762 100.006  72.162  1.00 28.41           C  
ANISOU 5175  C   ILE C  21     5075   3127   2591    254   1234    412       C  
ATOM   5176  O   ILE C  21     -12.907 101.207  72.016  1.00 28.66           O  
ANISOU 5176  O   ILE C  21     5055   3207   2626    265   1176    385       O  
ATOM   5177  CB  ILE C  21     -14.644  98.440  71.393  1.00 30.83           C  
ANISOU 5177  CB  ILE C  21     5344   3404   2965    113   1404    369       C  
ATOM   5178  CG1 ILE C  21     -15.167  97.618  70.210  1.00 31.37           C  
ANISOU 5178  CG1 ILE C  21     5357   3466   3093     25   1453    328       C  
ATOM   5179  CG2 ILE C  21     -15.636  99.524  71.788  1.00 30.79           C  
ANISOU 5179  CG2 ILE C  21     5281   3466   2950    116   1396    336       C  
ATOM   5180  CD1 ILE C  21     -16.461  96.877  70.511  1.00 32.60           C  
ANISOU 5180  CD1 ILE C  21     5510   3615   3259    -58   1578    293       C  
ATOM   5181  N   SER C  22     -12.181  99.474  73.250  1.00 29.72           N  
ANISOU 5181  N   SER C  22     5335   3259   2698    310   1256    457       N  
ATOM   5182  CA  SER C  22     -11.564 100.292  74.315  1.00 30.71           C  
ANISOU 5182  CA  SER C  22     5496   3413   2759    386   1197    470       C  
ATOM   5183  C   SER C  22     -10.565 101.325  73.768  1.00 28.64           C  
ANISOU 5183  C   SER C  22     5178   3196   2507    405   1084    445       C  
ATOM   5184  O   SER C  22     -10.603 102.476  74.158  1.00 30.07           O  
ANISOU 5184  O   SER C  22     5342   3413   2669    420   1040    421       O  
ATOM   5185  CB  SER C  22     -10.901  99.427  75.326  1.00 33.33           C  
ANISOU 5185  CB  SER C  22     5932   3710   3021    457   1226    520       C  
ATOM   5186  OG  SER C  22     -11.887  98.731  76.039  1.00 39.53           O  
ANISOU 5186  OG  SER C  22     6782   4451   3786    441   1338    541       O  
ATOM   5187  N   SER C  23      -9.667 100.890  72.877  1.00 28.05           N  
ANISOU 5187  N   SER C  23     5082   3112   2460    401   1048    448       N  
ATOM   5188  CA  SER C  23      -8.622 101.734  72.305  1.00 27.67           C  
ANISOU 5188  CA  SER C  23     4985   3101   2425    410    955    422       C  
ATOM   5189  C   SER C  23      -9.233 102.919  71.538  1.00 27.12           C  
ANISOU 5189  C   SER C  23     4850   3054   2401    363    931    379       C  
ATOM   5190  O   SER C  23      -8.619 103.993  71.511  1.00 28.05           O  
ANISOU 5190  O   SER C  23     4949   3198   2510    372    871    352       O  
ATOM   5191  CB  SER C  23      -7.652 100.921  71.432  1.00 27.47           C  
ANISOU 5191  CB  SER C  23     4950   3063   2425    412    935    434       C  
ATOM   5192  OG  SER C  23      -8.061 100.852  70.077  1.00 27.14           O  
ANISOU 5192  OG  SER C  23     4850   3005   2454    349    944    416       O  
ATOM   5193  N   VAL C  24     -10.414 102.715  70.926  1.00 26.53           N  
ANISOU 5193  N   VAL C  24     4743   2969   2367    318    983    370       N  
ATOM   5194  CA  VAL C  24     -11.142 103.737  70.165  1.00 27.31           C  
ANISOU 5194  CA  VAL C  24     4784   3096   2497    294    969    333       C  
ATOM   5195  C   VAL C  24     -11.912 104.675  71.098  1.00 27.86           C  
ANISOU 5195  C   VAL C  24     4869   3188   2527    318    980    322       C  
ATOM   5196  O   VAL C  24     -12.035 105.873  70.830  1.00 27.78           O  
ANISOU 5196  O   VAL C  24     4842   3196   2514    330    948    296       O  
ATOM   5197  CB  VAL C  24     -12.106 103.102  69.152  1.00 28.29           C  
ANISOU 5197  CB  VAL C  24     4854   3223   2670    245   1015    317       C  
ATOM   5198  CG1 VAL C  24     -12.977 104.152  68.472  1.00 28.79           C  
ANISOU 5198  CG1 VAL C  24     4859   3330   2746    245   1002    279       C  
ATOM   5199  CG2 VAL C  24     -11.365 102.267  68.126  1.00 30.41           C  
ANISOU 5199  CG2 VAL C  24     5108   3467   2977    221   1002    324       C  
ATOM   5200  N   LEU C  25     -12.515 104.144  72.170  1.00 30.03           N  
ANISOU 5200  N   LEU C  25     5184   3457   2769    328   1037    341       N  
ATOM   5201  CA  LEU C  25     -13.209 105.012  73.138  1.00 31.68           C  
ANISOU 5201  CA  LEU C  25     5413   3687   2935    356   1049    332       C  
ATOM   5202  C   LEU C  25     -12.207 105.826  73.989  1.00 31.58           C  
ANISOU 5202  C   LEU C  25     5450   3677   2872    401    991    333       C  
ATOM   5203  O   LEU C  25     -12.567 106.867  74.491  1.00 31.89           O  
ANISOU 5203  O   LEU C  25     5502   3732   2883    422    982    315       O  
ATOM   5204  CB  LEU C  25     -14.126 104.174  74.036  1.00 32.35           C  
ANISOU 5204  CB  LEU C  25     5530   3762   2999    349   1135    351       C  
ATOM   5205  CG  LEU C  25     -15.237 103.400  73.332  1.00 33.92           C  
ANISOU 5205  CG  LEU C  25     5674   3969   3244    289   1207    333       C  
ATOM   5206  CD1 LEU C  25     -16.098 102.678  74.339  1.00 37.82           C  
ANISOU 5206  CD1 LEU C  25     6208   4448   3712    274   1304    346       C  
ATOM   5207  CD2 LEU C  25     -16.096 104.288  72.451  1.00 37.55           C  
ANISOU 5207  CD2 LEU C  25     6048   4487   3732    279   1189    288       C  
ATOM   5208  N   ASN C  26     -10.964 105.363  74.155  1.00 30.73           N  
ANISOU 5208  N   ASN C  26     5366   3559   2748    418    952    347       N  
ATOM   5209  CA AASN C  26      -9.944 106.080  74.937  0.90 33.90           C  
ANISOU 5209  CA AASN C  26     5799   3983   3099    454    892    332       C  
ATOM   5210  CA BASN C  26      -9.947 106.080  74.942  0.10 31.36           C  
ANISOU 5210  CA BASN C  26     5477   3661   2777    454    892    332       C  
ATOM   5211  C   ASN C  26      -9.078 106.940  74.012  1.00 31.97           C  
ANISOU 5211  C   ASN C  26     5513   3747   2885    427    830    294       C  
ATOM   5212  O   ASN C  26      -7.891 106.697  73.862  1.00 39.40           O  
ANISOU 5212  O   ASN C  26     6444   4703   3822    431    785    287       O  
ATOM   5213  CB AASN C  26      -9.048 105.125  75.727  0.90 40.18           C  
ANISOU 5213  CB AASN C  26     6637   4783   3843    502    882    361       C  
ATOM   5214  CB BASN C  26      -9.105 105.112  75.778  0.10 30.92           C  
ANISOU 5214  CB BASN C  26     5468   3610   2669    503    886    363       C  
ATOM   5215  CG AASN C  26      -8.070 105.840  76.638  0.90 46.42           C  
ANISOU 5215  CG AASN C  26     7448   5619   4570    543    819    333       C  
ATOM   5216  CG BASN C  26      -9.878 104.520  76.938  0.10 30.54           C  
ANISOU 5216  CG BASN C  26     5485   3547   2570    540    952    398       C  
ATOM   5217  OD1AASN C  26      -8.424 106.820  77.296  0.90 58.85           O  
ANISOU 5217  OD1AASN C  26     9040   7206   6113    548    814    308       O  
ATOM   5218  OD1BASN C  26     -10.838 105.118  77.413  0.10 29.55           O  
ANISOU 5218  OD1BASN C  26     5368   3423   2434    535    984    389       O  
ATOM   5219  ND2AASN C  26      -6.844 105.344  76.705  0.90 49.84           N  
ANISOU 5219  ND2AASN C  26     7877   6083   4976    577    773    333       N  
ATOM   5220  ND2BASN C  26      -9.470 103.349  77.398  0.10 30.10           N  
ANISOU 5220  ND2BASN C  26     5482   3474   2478    583    979    439       N  
ATOM   5221  N   GLN C  27      -9.691 107.931  73.374  1.00 30.67           N  
ANISOU 5221  N   GLN C  27     5329   3576   2748    404    835    269       N  
ATOM   5222  CA  GLN C  27      -8.966 108.864  72.494  1.00 30.33           C  
ANISOU 5222  CA  GLN C  27     5266   3527   2731    377    794    233       C  
ATOM   5223  C   GLN C  27      -8.846 110.218  73.201  1.00 32.59           C  
ANISOU 5223  C   GLN C  27     5594   3814   2974    384    781    195       C  
ATOM   5224  O   GLN C  27      -9.682 110.567  74.047  1.00 28.92           O  
ANISOU 5224  O   GLN C  27     5162   3352   2472    412    809    199       O  
ATOM   5225  CB  GLN C  27      -9.697 109.036  71.170  1.00 27.50           C  
ANISOU 5225  CB  GLN C  27     4871   3152   2424    358    816    232       C  
ATOM   5226  CG  GLN C  27      -9.605 107.819  70.270  1.00 27.66           C  
ANISOU 5226  CG  GLN C  27     4849   3169   2492    338    822    255       C  
ATOM   5227  CD  GLN C  27      -8.196 107.603  69.789  1.00 27.49           C  
ANISOU 5227  CD  GLN C  27     4813   3142   2486    320    778    248       C  
ATOM   5228  OE1 GLN C  27      -7.600 108.490  69.174  1.00 27.52           O  
ANISOU 5228  OE1 GLN C  27     4814   3139   2504    301    753    218       O  
ATOM   5229  NE2 GLN C  27      -7.650 106.436  70.097  1.00 26.17           N  
ANISOU 5229  NE2 GLN C  27     4647   2981   2313    330    774    273       N  
ATOM   5230  N   THR C  28      -7.804 110.973  72.840  1.00 29.59           N  
ANISOU 5230  N   THR C  28     5212   3429   2598    352    746    153       N  
ATOM   5231  CA  THR C  28      -7.634 112.328  73.366  1.00 31.31           C  
ANISOU 5231  CA  THR C  28     5477   3638   2781    342    744    106       C  
ATOM   5232  C   THR C  28      -8.666 113.275  72.752  1.00 30.35           C  
ANISOU 5232  C   THR C  28     5386   3473   2670    352    787    106       C  
ATOM   5233  O   THR C  28      -9.057 114.237  73.386  1.00 31.40           O  
ANISOU 5233  O   THR C  28     5574   3591   2763    368    806     86       O  
ATOM   5234  CB  THR C  28      -6.209 112.855  73.175  1.00 29.50           C  
ANISOU 5234  CB  THR C  28     5238   3417   2553    292    707     49       C  
ATOM   5235  OG1 THR C  28      -5.833 112.782  71.802  1.00 30.26           O  
ANISOU 5235  OG1 THR C  28     5301   3487   2706    257    709     50       O  
ATOM   5236  CG2 THR C  28      -5.221 112.124  74.057  1.00 31.18           C  
ANISOU 5236  CG2 THR C  28     5422   3694   2728    303    659     36       C  
ATOM   5237  N   MET C  29      -9.093 112.992  71.526  1.00 29.22           N  
ANISOU 5237  N   MET C  29     5211   3316   2575    353    802    129       N  
ATOM   5238  CA  MET C  29     -10.167 113.729  70.864  1.00 31.02           C  
ANISOU 5238  CA  MET C  29     5460   3522   2804    386    840    134       C  
ATOM   5239  C   MET C  29     -11.444 113.674  71.725  1.00 30.60           C  
ANISOU 5239  C   MET C  29     5415   3496   2716    436    870    153       C  
ATOM   5240  O   MET C  29     -11.831 112.617  72.179  1.00 30.66           O  
ANISOU 5240  O   MET C  29     5385   3535   2727    440    874    179       O  
ATOM   5241  CB  MET C  29     -10.447 113.153  69.468  1.00 29.61           C  
ANISOU 5241  CB  MET C  29     5228   3346   2675    387    843    154       C  
ATOM   5242  CG  MET C  29     -11.514 113.916  68.728  1.00 31.13           C  
ANISOU 5242  CG  MET C  29     5436   3532   2857    439    876    155       C  
ATOM   5243  SD  MET C  29     -11.845 113.405  67.048  1.00 31.58           S  
ANISOU 5243  SD  MET C  29     5434   3604   2958    451    875    168       S  
ATOM   5244  CE  MET C  29     -10.473 114.191  66.205  1.00 32.52           C  
ANISOU 5244  CE  MET C  29     5606   3656   3094    413    867    147       C  
ATOM   5245  N   LYS C  30     -12.118 114.814  71.892  1.00 32.55           N  
ANISOU 5245  N   LYS C  30     5717   3725   2926    476    899    140       N  
ATOM   5246  CA  LYS C  30     -13.392 114.907  72.658  1.00 36.08           C  
ANISOU 5246  CA  LYS C  30     6170   4202   3335    531    933    154       C  
ATOM   5247  C   LYS C  30     -14.407 113.927  72.065  1.00 34.06           C  
ANISOU 5247  C   LYS C  30     5833   3998   3111    547    950    178       C  
ATOM   5248  O   LYS C  30     -14.551 113.892  70.865  1.00 30.69           O  
ANISOU 5248  O   LYS C  30     5371   3576   2713    553    947    177       O  
ATOM   5249  CB  LYS C  30     -13.969 116.330  72.591  1.00 41.06           C  
ANISOU 5249  CB  LYS C  30     6873   4805   3923    586    965    138       C  
ATOM   5250  N   SER C  31     -15.122 113.164  72.908  1.00 35.52           N  
ANISOU 5250  N   SER C  31     5990   4220   3284    552    973    193       N  
ATOM   5251  CA  SER C  31     -15.920 112.012  72.416  1.00 35.77           C  
ANISOU 5251  CA  SER C  31     5939   4299   3352    537    997    205       C  
ATOM   5252  C   SER C  31     -17.124 112.489  71.588  1.00 36.95           C  
ANISOU 5252  C   SER C  31     6043   4499   3498    587   1020    188       C  
ATOM   5253  O   SER C  31     -17.692 111.732  70.772  1.00 35.59           O  
ANISOU 5253  O   SER C  31     5790   4373   3359    572   1030    180       O  
ATOM   5254  CB  SER C  31     -16.323 111.105  73.539  1.00 39.74           C  
ANISOU 5254  CB  SER C  31     6438   4818   3842    522   1031    222       C  
ATOM   5255  OG  SER C  31     -16.783 111.870  74.634  1.00 49.80           O  
ANISOU 5255  OG  SER C  31     7764   6097   5061    565   1051    219       O  
ATOM   5256  N   THR C  32     -17.499 113.763  71.754  1.00 35.33           N  
ANISOU 5256  N   THR C  32     5889   4288   3244    653   1028    178       N  
ATOM   5257  CA  THR C  32     -18.567 114.361  70.954  1.00 37.87           C  
ANISOU 5257  CA  THR C  32     6179   4664   3546    727   1045    163       C  
ATOM   5258  C   THR C  32     -18.140 114.573  69.499  1.00 34.12           C  
ANISOU 5258  C   THR C  32     5694   4175   3095    737   1019    158       C  
ATOM   5259  O   THR C  32     -18.998 114.755  68.652  1.00 34.59           O  
ANISOU 5259  O   THR C  32     5705   4297   3140    799   1027    144       O  
ATOM   5260  CB  THR C  32     -18.982 115.739  71.482  1.00 40.06           C  
ANISOU 5260  CB  THR C  32     6537   4925   3756    809   1066    159       C  
ATOM   5261  OG1 THR C  32     -19.041 115.679  72.900  1.00 49.29           O  
ANISOU 5261  OG1 THR C  32     7742   6085   4901    794   1083    165       O  
ATOM   5262  CG2 THR C  32     -20.319 116.175  70.932  1.00 44.71           C  
ANISOU 5262  CG2 THR C  32     7080   5598   4309    906   1090    144       C  
ATOM   5263  N   ASP C  33     -16.825 114.598  69.246  1.00 32.29           N  
ANISOU 5263  N   ASP C  33     5508   3869   2890    684    991    165       N  
ATOM   5264  CA  ASP C  33     -16.276 114.953  67.941  1.00 33.35           C  
ANISOU 5264  CA  ASP C  33     5656   3973   3042    693    974    162       C  
ATOM   5265  C   ASP C  33     -16.090 113.741  67.013  1.00 32.98           C  
ANISOU 5265  C   ASP C  33     5520   3957   3053    643    952    164       C  
ATOM   5266  O   ASP C  33     -15.789 113.937  65.812  1.00 30.20           O  
ANISOU 5266  O   ASP C  33     5167   3592   2715    658    939    161       O  
ATOM   5267  CB  ASP C  33     -14.940 115.689  68.094  1.00 35.95           C  
ANISOU 5267  CB  ASP C  33     6078   4208   3371    654    964    160       C  
ATOM   5268  CG  ASP C  33     -15.071 117.122  68.596  1.00 41.09           C  
ANISOU 5268  CG  ASP C  33     6838   4810   3961    707    995    150       C  
ATOM   5269  OD1 ASP C  33     -16.155 117.708  68.425  1.00 41.24           O  
ANISOU 5269  OD1 ASP C  33     6870   4861   3936    799   1023    152       O  
ATOM   5270  OD2 ASP C  33     -14.080 117.637  69.156  1.00 44.26           O  
ANISOU 5270  OD2 ASP C  33     7310   5147   4358    656    994    135       O  
ATOM   5271  N   TYR C  34     -16.247 112.520  67.532  1.00 31.78           N  
ANISOU 5271  N   TYR C  34     5305   3836   2931    586    954    168       N  
ATOM   5272  CA  TYR C  34     -16.090 111.303  66.682  1.00 30.73           C  
ANISOU 5272  CA  TYR C  34     5097   3725   2852    534    942    166       C  
ATOM   5273  C   TYR C  34     -17.040 110.193  67.111  1.00 30.88           C  
ANISOU 5273  C   TYR C  34     5041   3805   2884    502    975    157       C  
ATOM   5274  O   TYR C  34     -17.585 110.237  68.177  1.00 26.35           O  
ANISOU 5274  O   TYR C  34     4479   3247   2285    509   1004    159       O  
ATOM   5275  CB  TYR C  34     -14.666 110.764  66.731  1.00 28.50           C  
ANISOU 5275  CB  TYR C  34     4843   3379   2606    468    915    184       C  
ATOM   5276  CG  TYR C  34     -14.255 110.114  68.020  1.00 27.99           C  
ANISOU 5276  CG  TYR C  34     4800   3296   2539    429    921    201       C  
ATOM   5277  CD1 TYR C  34     -13.880 110.885  69.117  1.00 29.32           C  
ANISOU 5277  CD1 TYR C  34     5036   3436   2666    445    916    203       C  
ATOM   5278  CD2 TYR C  34     -14.261 108.740  68.150  1.00 26.34           C  
ANISOU 5278  CD2 TYR C  34     4553   3095   2359    383    936    213       C  
ATOM   5279  CE1 TYR C  34     -13.453 110.304  70.294  1.00 28.24           C  
ANISOU 5279  CE1 TYR C  34     4924   3290   2516    423    917    218       C  
ATOM   5280  CE2 TYR C  34     -13.829 108.139  69.316  1.00 27.96           C  
ANISOU 5280  CE2 TYR C  34     4795   3279   2550    365    945    235       C  
ATOM   5281  CZ  TYR C  34     -13.438 108.920  70.396  1.00 28.98           C  
ANISOU 5281  CZ  TYR C  34     4985   3390   2634    390    932    238       C  
ATOM   5282  OH  TYR C  34     -13.010 108.305  71.536  1.00 26.63           O  
ANISOU 5282  OH  TYR C  34     4724   3081   2312    386    938    258       O  
ATOM   5283  N   GLU C  35     -17.188 109.197  66.237  1.00 27.95           N  
ANISOU 5283  N   GLU C  35     4599   3465   2555    460    977    143       N  
ATOM   5284  CA  GLU C  35     -18.065 108.080  66.472  1.00 29.23           C  
ANISOU 5284  CA  GLU C  35     4690   3680   2736    411   1021    122       C  
ATOM   5285  C   GLU C  35     -17.342 106.818  65.983  1.00 29.42           C  
ANISOU 5285  C   GLU C  35     4701   3665   2813    334   1020    131       C  
ATOM   5286  O   GLU C  35     -16.568 106.879  65.020  1.00 28.23           O  
ANISOU 5286  O   GLU C  35     4555   3487   2684    335    981    136       O  
ATOM   5287  CB  GLU C  35     -19.397 108.311  65.748  1.00 30.36           C  
ANISOU 5287  CB  GLU C  35     4741   3932   2862    452   1034     73       C  
ATOM   5288  CG  GLU C  35     -19.245 108.496  64.249  1.00 30.69           C  
ANISOU 5288  CG  GLU C  35     4746   4000   2913    482    995     54       C  
ATOM   5289  CD  GLU C  35     -20.532 108.788  63.496  1.00 33.24           C  
ANISOU 5289  CD  GLU C  35     4973   4449   3204    544    998      0       C  
ATOM   5290  OE1 GLU C  35     -21.594 108.762  64.130  1.00 35.08           O  
ANISOU 5290  OE1 GLU C  35     5154   4760   3415    553   1034    -29       O  
ATOM   5291  OE2 GLU C  35     -20.470 109.022  62.277  1.00 30.26           O  
ANISOU 5291  OE2 GLU C  35     4572   4103   2822    588    966    -15       O  
ATOM   5292  N   LEU C  36     -17.563 105.702  66.685  1.00 29.95           N  
ANISOU 5292  N   LEU C  36     4764   3720   2895    273   1071    135       N  
ATOM   5293  CA  LEU C  36     -17.208 104.389  66.207  1.00 27.51           C  
ANISOU 5293  CA  LEU C  36     4440   3382   2629    202   1092    134       C  
ATOM   5294  C   LEU C  36     -18.464 103.738  65.623  1.00 26.90           C  
ANISOU 5294  C   LEU C  36     4265   3383   2570    155   1141     74       C  
ATOM   5295  O   LEU C  36     -19.442 103.551  66.302  1.00 27.09           O  
ANISOU 5295  O   LEU C  36     4261   3450   2581    135   1198     50       O  
ATOM   5296  CB  LEU C  36     -16.631 103.570  67.360  1.00 29.17           C  
ANISOU 5296  CB  LEU C  36     4727   3520   2835    171   1129    176       C  
ATOM   5297  CG  LEU C  36     -16.350 102.096  67.068  1.00 30.51           C  
ANISOU 5297  CG  LEU C  36     4904   3645   3040    102   1174    181       C  
ATOM   5298  CD1 LEU C  36     -15.413 101.955  65.875  1.00 30.60           C  
ANISOU 5298  CD1 LEU C  36     4906   3635   3084    100   1120    186       C  
ATOM   5299  CD2 LEU C  36     -15.755 101.438  68.296  1.00 33.43           C  
ANISOU 5299  CD2 LEU C  36     5370   3945   3386    102   1211    231       C  
ATOM   5300  N   ILE C  37     -18.392 103.381  64.345  1.00 27.42           N  
ANISOU 5300  N   ILE C  37     4277   3473   2666    135   1120     45       N  
ATOM   5301  CA  ILE C  37     -19.442 102.649  63.667  1.00 28.73           C  
ANISOU 5301  CA  ILE C  37     4343   3720   2852     78   1161    -23       C  
ATOM   5302  C   ILE C  37     -18.968 101.210  63.454  1.00 28.27           C  
ANISOU 5302  C   ILE C  37     4307   3594   2838    -15   1207    -21       C  
ATOM   5303  O   ILE C  37     -18.021 100.987  62.704  1.00 28.78           O  
ANISOU 5303  O   ILE C  37     4400   3610   2925    -13   1167      1       O  
ATOM   5304  CB  ILE C  37     -19.825 103.307  62.331  1.00 29.87           C  
ANISOU 5304  CB  ILE C  37     4407   3955   2986    133   1106    -68       C  
ATOM   5305  CG1 ILE C  37     -20.190 104.787  62.510  1.00 30.38           C  
ANISOU 5305  CG1 ILE C  37     4475   4069   2997    245   1067    -60       C  
ATOM   5306  CG2 ILE C  37     -20.948 102.520  61.660  1.00 30.93           C  
ANISOU 5306  CG2 ILE C  37     4422   4194   3135     70   1147   -156       C  
ATOM   5307  CD1 ILE C  37     -20.525 105.494  61.222  1.00 30.55           C  
ANISOU 5307  CD1 ILE C  37     4440   4173   2993    324   1017    -95       C  
ATOM   5308  N   ILE C  38     -19.676 100.263  64.077  1.00 28.26           N  
ANISOU 5308  N   ILE C  38     4297   3591   2847    -97   1297    -49       N  
ATOM   5309  CA  ILE C  38     -19.414  98.832  63.976  1.00 29.34           C  
ANISOU 5309  CA  ILE C  38     4470   3657   3019   -192   1367    -52       C  
ATOM   5310  C   ILE C  38     -20.477  98.198  63.068  1.00 29.71           C  
ANISOU 5310  C   ILE C  38     4402   3792   3091   -277   1412   -152       C  
ATOM   5311  O   ILE C  38     -21.656  98.330  63.331  1.00 32.25           O  
ANISOU 5311  O   ILE C  38     4643   4207   3402   -305   1455   -215       O  
ATOM   5312  CB  ILE C  38     -19.429  98.199  65.384  1.00 30.26           C  
ANISOU 5312  CB  ILE C  38     4679   3694   3121   -225   1455    -13       C  
ATOM   5313  CG1 ILE C  38     -18.377  98.851  66.292  1.00 30.94           C  
ANISOU 5313  CG1 ILE C  38     4868   3712   3173   -135   1402     73       C  
ATOM   5314  CG2 ILE C  38     -19.255  96.696  65.273  1.00 31.01           C  
ANISOU 5314  CG2 ILE C  38     4828   3707   3246   -320   1547    -19       C  
ATOM   5315  CD1 ILE C  38     -18.320  98.331  67.703  1.00 34.62           C  
ANISOU 5315  CD1 ILE C  38     5435   4107   3612   -142   1478    118       C  
ATOM   5316  N   ILE C  39     -20.047  97.501  62.016  1.00 30.54           N  
ANISOU 5316  N   ILE C  39     4498   3876   3229   -319   1403   -172       N  
ATOM   5317  CA  ILE C  39     -20.946  96.816  61.102  1.00 32.12           C  
ANISOU 5317  CA  ILE C  39     4592   4159   3453   -409   1445   -275       C  
ATOM   5318  C   ILE C  39     -20.647  95.313  61.206  1.00 32.35           C  
ANISOU 5318  C   ILE C  39     4696   4077   3516   -523   1545   -277       C  
ATOM   5319  O   ILE C  39     -19.562  94.879  60.846  1.00 30.02           O  
ANISOU 5319  O   ILE C  39     4483   3686   3236   -509   1524   -222       O  
ATOM   5320  CB  ILE C  39     -20.783  97.303  59.651  1.00 33.64           C  
ANISOU 5320  CB  ILE C  39     4707   4428   3646   -357   1351   -308       C  
ATOM   5321  CG1 ILE C  39     -20.711  98.831  59.554  1.00 35.34           C  
ANISOU 5321  CG1 ILE C  39     4902   4705   3820   -221   1253   -276       C  
ATOM   5322  CG2 ILE C  39     -21.879  96.707  58.770  1.00 32.81           C  
ANISOU 5322  CG2 ILE C  39     4470   4442   3553   -443   1388   -432       C  
ATOM   5323  CD1 ILE C  39     -22.040  99.483  59.546  1.00 39.66           C  
ANISOU 5323  CD1 ILE C  39     5330   5405   4332   -191   1252   -350       C  
ATOM   5324  N   ASP C  40     -21.595  94.539  61.747  1.00 34.86           N  
ANISOU 5324  N   ASP C  40     4996   4404   3843   -632   1663   -337       N  
ATOM   5325  CA  ASP C  40     -21.355  93.100  61.943  1.00 35.97           C  
ANISOU 5325  CA  ASP C  40     5234   4422   4011   -741   1782   -337       C  
ATOM   5326  C   ASP C  40     -21.834  92.340  60.704  1.00 36.43           C  
ANISOU 5326  C   ASP C  40     5205   4534   4103   -847   1812   -445       C  
ATOM   5327  O   ASP C  40     -22.995  92.460  60.299  1.00 37.24           O  
ANISOU 5327  O   ASP C  40     5164   4777   4208   -908   1828   -558       O  
ATOM   5328  CB  ASP C  40     -22.024  92.564  63.201  1.00 36.43           C  
ANISOU 5328  CB  ASP C  40     5348   4433   4059   -814   1916   -342       C  
ATOM   5329  CG  ASP C  40     -21.723  91.090  63.406  1.00 36.40           C  
ANISOU 5329  CG  ASP C  40     5473   4281   4074   -916   2052   -333       C  
ATOM   5330  OD1 ASP C  40     -20.558  90.775  63.745  1.00 34.70           O  
ANISOU 5330  OD1 ASP C  40     5403   3935   3846   -851   2043   -230       O  
ATOM   5331  OD2 ASP C  40     -22.642  90.280  63.174  1.00 36.74           O  
ANISOU 5331  OD2 ASP C  40     5468   4347   4142  -1059   2165   -435       O  
ATOM   5332  N   ASP C  41     -20.933  91.530  60.147  1.00 39.58           N  
ANISOU 5332  N   ASP C  41     5690   4825   4522   -868   1822   -413       N  
ATOM   5333  CA  ASP C  41     -21.161  90.810  58.870  1.00 42.64           C  
ANISOU 5333  CA  ASP C  41     6010   5248   4939   -957   1838   -506       C  
ATOM   5334  C   ASP C  41     -21.859  89.466  59.144  1.00 43.04           C  
ANISOU 5334  C   ASP C  41     6097   5242   5015  -1128   2009   -584       C  
ATOM   5335  O   ASP C  41     -21.389  88.422  58.703  1.00 43.00           O  
ANISOU 5335  O   ASP C  41     6175   5132   5030  -1195   2072   -588       O  
ATOM   5336  CB  ASP C  41     -19.842  90.647  58.108  1.00 41.26           C  
ANISOU 5336  CB  ASP C  41     5914   4987   4773   -891   1766   -434       C  
ATOM   5337  CG  ASP C  41     -20.036  90.414  56.617  1.00 46.77           C  
ANISOU 5337  CG  ASP C  41     6512   5765   5491   -933   1727   -524       C  
ATOM   5338  OD1 ASP C  41     -21.196  90.539  56.161  1.00 46.96           O  
ANISOU 5338  OD1 ASP C  41     6393   5934   5516   -996   1735   -644       O  
ATOM   5339  OD2 ASP C  41     -19.035  90.103  55.926  1.00 46.86           O  
ANISOU 5339  OD2 ASP C  41     6588   5703   5513   -899   1688   -478       O  
ATOM   5340  N   HIS C  42     -22.979  89.544  59.874  1.00 43.79           N  
ANISOU 5340  N   HIS C  42     6129   5406   5104  -1197   2086   -648       N  
ATOM   5341  CA  HIS C  42     -23.818  88.431  60.361  1.00 50.19           C  
ANISOU 5341  CA  HIS C  42     6966   6171   5933  -1368   2267   -730       C  
ATOM   5342  C   HIS C  42     -22.972  87.324  61.013  1.00 49.68           C  
ANISOU 5342  C   HIS C  42     7124   5880   5869  -1397   2386   -639       C  
ATOM   5343  O   HIS C  42     -22.902  86.203  60.514  1.00 51.17           O  
ANISOU 5343  O   HIS C  42     7373   5986   6082  -1508   2485   -686       O  
ATOM   5344  CB  HIS C  42     -24.716  87.923  59.225  1.00 54.96           C  
ANISOU 5344  CB  HIS C  42     7420   6898   6565  -1507   2300   -897       C  
ATOM   5345  CG  HIS C  42     -26.040  87.444  59.703  1.00 59.42           C  
ANISOU 5345  CG  HIS C  42     7906   7529   7140  -1667   2443  -1023       C  
ATOM   5346  ND1 HIS C  42     -27.035  88.318  60.100  1.00 63.28           N  
ANISOU 5346  ND1 HIS C  42     8246   8186   7608  -1644   2412  -1079       N  
ATOM   5347  CD2 HIS C  42     -26.539  86.201  59.858  1.00 63.04           C  
ANISOU 5347  CD2 HIS C  42     8415   7910   7625  -1855   2625  -1109       C  
ATOM   5348  CE1 HIS C  42     -28.093  87.636  60.487  1.00 63.58           C  
ANISOU 5348  CE1 HIS C  42     8235   8258   7663  -1813   2566  -1197       C  
ATOM   5349  NE2 HIS C  42     -27.816  86.334  60.342  1.00 66.15           N  
ANISOU 5349  NE2 HIS C  42     8683   8431   8019  -1951   2703  -1219       N  
ATOM   5350  N   SER C  43     -22.326  87.652  62.135  1.00 45.69           N  
ANISOU 5350  N   SER C  43     6747   5281   5332  -1289   2378   -511       N  
ATOM   5351  CA  SER C  43     -21.604  86.678  62.935  1.00 46.05           C  
ANISOU 5351  CA  SER C  43     7009   5126   5360  -1289   2495   -419       C  
ATOM   5352  C   SER C  43     -22.538  85.500  63.237  1.00 46.65           C  
ANISOU 5352  C   SER C  43     7132   5138   5454  -1475   2705   -510       C  
ATOM   5353  O   SER C  43     -23.734  85.682  63.426  1.00 48.24           O  
ANISOU 5353  O   SER C  43     7213   5446   5667  -1574   2760   -612       O  
ATOM   5354  CB  SER C  43     -21.093  87.290  64.225  1.00 44.07           C  
ANISOU 5354  CB  SER C  43     6856   4825   5062  -1156   2464   -296       C  
ATOM   5355  OG  SER C  43     -20.101  88.270  63.987  1.00 38.27           O  
ANISOU 5355  OG  SER C  43     6101   4128   4311   -998   2289   -213       O  
ATOM   5356  N   ASN C  44     -21.975  84.294  63.307  1.00 51.26           N  
ANISOU 5356  N   ASN C  44     7899   5543   6035  -1519   2828   -473       N  
ATOM   5357  CA  ASN C  44     -22.749  83.090  63.653  1.00 53.96           C  
ANISOU 5357  CA  ASN C  44     8328   5786   6389  -1700   3054   -550       C  
ATOM   5358  C   ASN C  44     -22.057  82.323  64.786  1.00 56.49           C  
ANISOU 5358  C   ASN C  44     8912   5890   6661  -1642   3184   -423       C  
ATOM   5359  O   ASN C  44     -22.085  81.084  64.796  1.00 66.12           O  
ANISOU 5359  O   ASN C  44    10283   6957   7882  -1748   3362   -443       O  
ATOM   5360  CB  ASN C  44     -22.954  82.196  62.433  1.00 55.38           C  
ANISOU 5360  CB  ASN C  44     8473   5955   6611  -1845   3114   -664       C  
ATOM   5361  CG  ASN C  44     -21.649  81.822  61.768  1.00 56.74           C  
ANISOU 5361  CG  ASN C  44     8759   6023   6777  -1747   3047   -577       C  
ATOM   5362  OD1 ASN C  44     -20.577  82.045  62.323  1.00 60.20           O  
ANISOU 5362  OD1 ASN C  44     9324   6375   7174  -1582   2985   -431       O  
ATOM   5363  ND2 ASN C  44     -21.726  81.254  60.577  1.00 57.60           N  
ANISOU 5363  ND2 ASN C  44     8817   6146   6920  -1845   3058   -670       N  
ATOM   5364  N   ASP C  45     -21.512  83.062  65.766  1.00 53.50           N  
ANISOU 5364  N   ASP C  45     8589   5504   6234  -1478   3104   -301       N  
ATOM   5365  CA  ASP C  45     -20.742  82.502  66.892  1.00 51.32           C  
ANISOU 5365  CA  ASP C  45     8556   5047   5894  -1377   3195   -167       C  
ATOM   5366  C   ASP C  45     -21.620  82.433  68.155  1.00 53.39           C  
ANISOU 5366  C   ASP C  45     8875   5279   6130  -1431   3339   -173       C  
ATOM   5367  O   ASP C  45     -21.152  82.698  69.260  1.00 52.80           O  
ANISOU 5367  O   ASP C  45     8918   5149   5995  -1298   3332    -62       O  
ATOM   5368  CB  ASP C  45     -19.426  83.272  67.097  1.00 49.39           C  
ANISOU 5368  CB  ASP C  45     8345   4815   5606  -1155   3012    -33       C  
ATOM   5369  CG  ASP C  45     -19.568  84.752  67.463  1.00 48.79           C  
ANISOU 5369  CG  ASP C  45     8117   4896   5523  -1060   2848    -17       C  
ATOM   5370  OD1 ASP C  45     -20.689  85.308  67.325  1.00 43.60           O  
ANISOU 5370  OD1 ASP C  45     7296   4368   4901  -1153   2842   -115       O  
ATOM   5371  OD2 ASP C  45     -18.552  85.341  67.897  1.00 45.81           O  
ANISOU 5371  OD2 ASP C  45     7788   4515   5102   -892   2729     88       O  
ATOM   5372  N   ASN C  46     -22.895  82.058  67.991  1.00 55.70           N  
ANISOU 5372  N   ASN C  46     9082   5614   6467  -1629   3474   -310       N  
ATOM   5373  CA  ASN C  46     -23.803  81.804  69.101  1.00 57.30           C  
ANISOU 5373  CA  ASN C  46     9346   5773   6650  -1714   3647   -332       C  
ATOM   5374  C   ASN C  46     -24.016  83.080  69.924  1.00 55.07           C  
ANISOU 5374  C   ASN C  46     8966   5616   6341  -1596   3526   -287       C  
ATOM   5375  O   ASN C  46     -24.155  83.025  71.158  1.00 54.05           O  
ANISOU 5375  O   ASN C  46     8961   5411   6163  -1557   3622   -223       O  
ATOM   5376  CB  ASN C  46     -23.313  80.629  69.951  1.00 60.50           C  
ANISOU 5376  CB  ASN C  46    10050   5936   7001  -1698   3844   -240       C  
ATOM   5377  CG  ASN C  46     -23.504  79.331  69.211  1.00 64.19           C  
ANISOU 5377  CG  ASN C  46    10604   6283   7502  -1869   4015   -322       C  
ATOM   5378  OD1 ASN C  46     -24.634  78.882  69.047  1.00 73.52           O  
ANISOU 5378  OD1 ASN C  46    11719   7487   8728  -2080   4165   -461       O  
ATOM   5379  ND2 ASN C  46     -22.420  78.766  68.702  1.00 69.49           N  
ANISOU 5379  ND2 ASN C  46    11406   6841   8154  -1784   3988   -249       N  
ATOM   5380  N   GLY C  47     -24.069  84.216  69.222  1.00 51.85           N  
ANISOU 5380  N   GLY C  47     8343   5395   5960  -1540   3324   -322       N  
ATOM   5381  CA  GLY C  47     -24.390  85.513  69.815  1.00 48.63           C  
ANISOU 5381  CA  GLY C  47     7817   5125   5533  -1443   3204   -301       C  
ATOM   5382  C   GLY C  47     -23.204  86.170  70.507  1.00 46.47           C  
ANISOU 5382  C   GLY C  47     7650   4803   5200  -1229   3075   -147       C  
ATOM   5383  O   GLY C  47     -23.360  87.269  71.007  1.00 43.24           O  
ANISOU 5383  O   GLY C  47     7160   4496   4771  -1141   2972   -124       O  
ATOM   5384  N   GLU C  48     -22.017  85.539  70.501  1.00 46.63           N  
ANISOU 5384  N   GLU C  48     7843   4683   5191  -1144   3075    -49       N  
ATOM   5385  CA  GLU C  48     -20.845  86.028  71.304  1.00 47.81           C  
ANISOU 5385  CA  GLU C  48     8109   4785   5272   -941   2972     92       C  
ATOM   5386  C   GLU C  48     -20.407  87.439  70.860  1.00 42.10           C  
ANISOU 5386  C   GLU C  48     7224   4213   4558   -828   2742    104       C  
ATOM   5387  O   GLU C  48     -20.169  88.283  71.700  1.00 41.99           O  
ANISOU 5387  O   GLU C  48     7217   4236   4500   -715   2667    165       O  
ATOM   5388  CB  GLU C  48     -19.668  85.047  71.235  1.00 49.84           C  
ANISOU 5388  CB  GLU C  48     8561   4884   5492   -867   3012    180       C  
ATOM   5389  CG  GLU C  48     -18.615  85.282  72.309  1.00 53.60           C  
ANISOU 5389  CG  GLU C  48     9183   5302   5881   -671   2959    315       C  
ATOM   5390  N   THR C  49     -20.289  87.668  69.543  1.00 39.48           N  
ANISOU 5390  N   THR C  49     6758   3960   4279   -861   2641     46       N  
ATOM   5391  CA  THR C  49     -19.770  88.921  68.974  1.00 36.82           C  
ANISOU 5391  CA  THR C  49     6291   3746   3950   -757   2437     60       C  
ATOM   5392  C   THR C  49     -20.776  90.060  69.172  1.00 35.99           C  
ANISOU 5392  C   THR C  49     6028   3790   3853   -767   2383      2       C  
ATOM   5393  O   THR C  49     -20.441  91.148  69.664  1.00 33.21           O  
ANISOU 5393  O   THR C  49     5654   3492   3470   -650   2270     52       O  
ATOM   5394  CB  THR C  49     -19.430  88.760  67.486  1.00 35.36           C  
ANISOU 5394  CB  THR C  49     6023   3596   3816   -792   2364     13       C  
ATOM   5395  OG1 THR C  49     -18.298  87.903  67.411  1.00 35.60           O  
ANISOU 5395  OG1 THR C  49     6206   3494   3826   -741   2388     88       O  
ATOM   5396  CG2 THR C  49     -19.082  90.069  66.816  1.00 35.40           C  
ANISOU 5396  CG2 THR C  49     5889   3729   3832   -703   2175     12       C  
ATOM   5397  N   LEU C  50     -22.025  89.800  68.799  1.00 38.81           N  
ANISOU 5397  N   LEU C  50     6277   4218   4249   -907   2468   -111       N  
ATOM   5398  CA  LEU C  50     -23.109  90.753  69.005  1.00 40.20           C  
ANISOU 5398  CA  LEU C  50     6303   4543   4428   -919   2438   -177       C  
ATOM   5399  C   LEU C  50     -23.332  91.023  70.507  1.00 39.32           C  
ANISOU 5399  C   LEU C  50     6280   4392   4266   -870   2498   -117       C  
ATOM   5400  O   LEU C  50     -23.634  92.134  70.901  1.00 36.32           O  
ANISOU 5400  O   LEU C  50     5824   4109   3865   -796   2417   -112       O  
ATOM   5401  CB  LEU C  50     -24.359  90.178  68.349  1.00 44.75           C  
ANISOU 5401  CB  LEU C  50     6753   5198   5049  -1091   2540   -320       C  
ATOM   5402  CG  LEU C  50     -25.503  91.170  68.199  1.00 50.37           C  
ANISOU 5402  CG  LEU C  50     7267   6104   5765  -1099   2487   -411       C  
ATOM   5403  CD1 LEU C  50     -25.609  91.676  66.772  1.00 50.57           C  
ANISOU 5403  CD1 LEU C  50     7127   6270   5818  -1088   2360   -484       C  
ATOM   5404  CD2 LEU C  50     -26.805  90.527  68.633  1.00 56.45           C  
ANISOU 5404  CD2 LEU C  50     7989   6908   6549  -1257   2659   -516       C  
ATOM   5405  N   ASN C  51     -23.159  90.004  71.348  1.00 40.42           N  
ANISOU 5405  N   ASN C  51     6593   4383   4380   -902   2646    -69       N  
ATOM   5406  CA  ASN C  51     -23.230  90.201  72.800  1.00 43.68           C  
ANISOU 5406  CA  ASN C  51     7115   4745   4736   -838   2703      0       C  
ATOM   5407  C   ASN C  51     -22.163  91.217  73.236  1.00 40.28           C  
ANISOU 5407  C   ASN C  51     6719   4326   4256   -655   2539    101       C  
ATOM   5408  O   ASN C  51     -22.444  92.078  74.062  1.00 38.72           O  
ANISOU 5408  O   ASN C  51     6503   4182   4025   -590   2504    121       O  
ATOM   5409  CB  ASN C  51     -23.071  88.902  73.592  1.00 46.90           C  
ANISOU 5409  CB  ASN C  51     7732   4975   5111   -879   2889     47       C  
ATOM   5410  CG  ASN C  51     -23.082  89.153  75.081  1.00 54.20           C  
ANISOU 5410  CG  ASN C  51     8774   5851   5965   -793   2939    125       C  
ATOM   5411  OD1 ASN C  51     -24.071  89.652  75.622  1.00 61.87           O  
ANISOU 5411  OD1 ASN C  51     9670   6900   6936   -832   2978     79       O  
ATOM   5412  ND2 ASN C  51     -21.978  88.842  75.743  1.00 57.28           N  
ANISOU 5412  ND2 ASN C  51     9345   6125   6291   -664   2930    239       N  
ATOM   5413  N   VAL C  52     -20.944  91.104  72.693  1.00 37.77           N  
ANISOU 5413  N   VAL C  52     6453   3960   3936   -578   2446    158       N  
ATOM   5414  CA  VAL C  52     -19.851  92.016  73.063  1.00 37.82           C  
ANISOU 5414  CA  VAL C  52     6489   3982   3899   -419   2295    242       C  
ATOM   5415  C   VAL C  52     -20.201  93.444  72.618  1.00 35.17           C  
ANISOU 5415  C   VAL C  52     5985   3794   3584   -387   2156    198       C  
ATOM   5416  O   VAL C  52     -20.084  94.398  73.416  1.00 33.33           O  
ANISOU 5416  O   VAL C  52     5757   3598   3309   -296   2091    235       O  
ATOM   5417  CB  VAL C  52     -18.478  91.582  72.519  1.00 37.06           C  
ANISOU 5417  CB  VAL C  52     6467   3816   3795   -350   2229    301       C  
ATOM   5418  CG1 VAL C  52     -17.511  92.751  72.471  1.00 37.49           C  
ANISOU 5418  CG1 VAL C  52     6478   3937   3830   -222   2051    344       C  
ATOM   5419  CG2 VAL C  52     -17.896  90.451  73.350  1.00 41.09           C  
ANISOU 5419  CG2 VAL C  52     7180   4181   4249   -309   2343    377       C  
ATOM   5420  N   ILE C  53     -20.668  93.577  71.376  1.00 33.15           N  
ANISOU 5420  N   ILE C  53     5589   3619   3384   -458   2118    118       N  
ATOM   5421  CA  ILE C  53     -20.963  94.881  70.792  1.00 33.55           C  
ANISOU 5421  CA  ILE C  53     5492   3804   3448   -415   1990     78       C  
ATOM   5422  C   ILE C  53     -22.046  95.582  71.621  1.00 34.49           C  
ANISOU 5422  C   ILE C  53     5558   4003   3544   -413   2023     49       C  
ATOM   5423  O   ILE C  53     -21.946  96.768  71.874  1.00 30.83           O  
ANISOU 5423  O   ILE C  53     5060   3600   3055   -321   1925     69       O  
ATOM   5424  CB  ILE C  53     -21.374  94.747  69.317  1.00 33.75           C  
ANISOU 5424  CB  ILE C  53     5385   3907   3529   -489   1962     -7       C  
ATOM   5425  CG1 ILE C  53     -20.168  94.345  68.462  1.00 34.18           C  
ANISOU 5425  CG1 ILE C  53     5488   3896   3603   -462   1898     31       C  
ATOM   5426  CG2 ILE C  53     -22.027  96.027  68.829  1.00 33.36           C  
ANISOU 5426  CG2 ILE C  53     5186   4007   3481   -446   1864    -59       C  
ATOM   5427  CD1 ILE C  53     -20.520  93.757  67.118  1.00 36.38           C  
ANISOU 5427  CD1 ILE C  53     5677   4212   3932   -556   1912    -49       C  
ATOM   5428  N   LYS C  54     -23.063  94.830  72.057  1.00 37.61           N  
ANISOU 5428  N   LYS C  54     5952   4390   3947   -518   2169      0       N  
ATOM   5429  CA  LYS C  54     -24.191  95.436  72.759  1.00 40.90           C  
ANISOU 5429  CA  LYS C  54     6300   4894   4344   -527   2209    -41       C  
ATOM   5430  C   LYS C  54     -23.816  95.951  74.165  1.00 39.13           C  
ANISOU 5430  C   LYS C  54     6192   4616   4057   -424   2204     45       C  
ATOM   5431  O   LYS C  54     -24.515  96.827  74.675  1.00 35.25           O  
ANISOU 5431  O   LYS C  54     5640   4209   3543   -388   2189     26       O  
ATOM   5432  CB  LYS C  54     -25.378  94.473  72.746  1.00 47.79           C  
ANISOU 5432  CB  LYS C  54     7126   5783   5247   -683   2373   -133       C  
ATOM   5433  CG  LYS C  54     -26.173  94.571  71.452  1.00 54.32           C  
ANISOU 5433  CG  LYS C  54     7763   6752   6121   -761   2343   -253       C  
ATOM   5434  CD  LYS C  54     -27.043  93.369  71.159  1.00 62.56           C  
ANISOU 5434  CD  LYS C  54     8769   7794   7205   -939   2501   -354       C  
ATOM   5435  CE  LYS C  54     -27.794  93.498  69.847  1.00 67.34           C  
ANISOU 5435  CE  LYS C  54     9174   8561   7849  -1007   2457   -483       C  
ATOM   5436  NZ  LYS C  54     -28.996  92.623  69.815  1.00 72.42           N  
ANISOU 5436  NZ  LYS C  54     9737   9257   8522  -1186   2618   -611       N  
ATOM   5437  N   LYS C  55     -22.707  95.486  74.758  1.00 37.74           N  
ANISOU 5437  N   LYS C  55     6177   4315   3847   -364   2207    137       N  
ATOM   5438  CA  LYS C  55     -22.203  96.024  76.048  1.00 36.75           C  
ANISOU 5438  CA  LYS C  55     6160   4150   3653   -251   2181    218       C  
ATOM   5439  C   LYS C  55     -21.686  97.479  75.909  1.00 35.36           C  
ANISOU 5439  C   LYS C  55     5922   4050   3459   -140   2014    235       C  
ATOM   5440  O   LYS C  55     -21.259  98.073  76.915  1.00 31.76           O  
ANISOU 5440  O   LYS C  55     5541   3578   2947    -47   1977    289       O  
ATOM   5441  CB  LYS C  55     -21.051  95.179  76.612  1.00 38.69           C  
ANISOU 5441  CB  LYS C  55     6581   4260   3856   -195   2210    307       C  
ATOM   5442  CG  LYS C  55     -21.330  93.698  76.897  1.00 42.58           C  
ANISOU 5442  CG  LYS C  55     7190   4638   4347   -280   2388    312       C  
ATOM   5443  CD  LYS C  55     -22.574  93.401  77.699  1.00 43.77           C  
ANISOU 5443  CD  LYS C  55     7354   4786   4490   -360   2542    277       C  
ATOM   5444  CE  LYS C  55     -23.762  92.897  76.891  1.00 47.35           C  
ANISOU 5444  CE  LYS C  55     7688   5289   5013   -527   2642    166       C  
ATOM   5445  NZ  LYS C  55     -24.949  92.582  77.742  1.00 48.34           N  
ANISOU 5445  NZ  LYS C  55     7826   5413   5128   -612   2806    126       N  
ATOM   5446  N   TYR C  56     -21.648  98.020  74.679  1.00 32.66           N  
ANISOU 5446  N   TYR C  56     5462   3784   3162   -147   1918    190       N  
ATOM   5447  CA  TYR C  56     -21.250  99.405  74.395  1.00 32.80           C  
ANISOU 5447  CA  TYR C  56     5425   3869   3168    -55   1777    197       C  
ATOM   5448  C   TYR C  56     -22.409 100.246  73.838  1.00 32.42           C  
ANISOU 5448  C   TYR C  56     5233   3949   3136    -68   1758    122       C  
ATOM   5449  O   TYR C  56     -22.179 101.327  73.293  1.00 31.98           O  
ANISOU 5449  O   TYR C  56     5126   3948   3077      0   1652    117       O  
ATOM   5450  CB  TYR C  56     -20.090  99.422  73.402  1.00 32.23           C  
ANISOU 5450  CB  TYR C  56     5353   3771   3121    -30   1679    217       C  
ATOM   5451  CG  TYR C  56     -18.842  98.789  73.950  1.00 32.93           C  
ANISOU 5451  CG  TYR C  56     5574   3757   3181     11   1675    290       C  
ATOM   5452  CD1 TYR C  56     -17.962  99.497  74.757  1.00 31.24           C  
ANISOU 5452  CD1 TYR C  56     5427   3527   2913    109   1602    342       C  
ATOM   5453  CD2 TYR C  56     -18.556  97.458  73.674  1.00 33.32           C  
ANISOU 5453  CD2 TYR C  56     5681   3729   3249    -42   1750    303       C  
ATOM   5454  CE1 TYR C  56     -16.817  98.894  75.269  1.00 33.85           C  
ANISOU 5454  CE1 TYR C  56     5868   3785   3206    161   1595    402       C  
ATOM   5455  CE2 TYR C  56     -17.409  96.853  74.160  1.00 33.59           C  
ANISOU 5455  CE2 TYR C  56     5838   3677   3245     15   1747    371       C  
ATOM   5456  CZ  TYR C  56     -16.541  97.567  74.966  1.00 34.29           C  
ANISOU 5456  CZ  TYR C  56     5982   3769   3278    122   1666    420       C  
ATOM   5457  OH  TYR C  56     -15.435  96.931  75.434  1.00 38.11           O  
ANISOU 5457  OH  TYR C  56     6576   4187   3715    189   1662    481       O  
ATOM   5458  N   LYS C  57     -23.647  99.782  74.008  1.00 35.86           N  
ANISOU 5458  N   LYS C  57     5607   4433   3583   -147   1864     63       N  
ATOM   5459  CA  LYS C  57     -24.834 100.515  73.597  1.00 38.80           C  
ANISOU 5459  CA  LYS C  57     5836   4946   3959   -148   1854    -13       C  
ATOM   5460  C   LYS C  57     -24.801 101.948  74.143  1.00 37.97           C  
ANISOU 5460  C   LYS C  57     5739   4882   3804    -27   1773     16       C  
ATOM   5461  O   LYS C  57     -24.465 102.164  75.313  1.00 36.78           O  
ANISOU 5461  O   LYS C  57     5693   4669   3611     18   1787     73       O  
ATOM   5462  CB  LYS C  57     -26.098  99.846  74.122  1.00 43.01           C  
ANISOU 5462  CB  LYS C  57     6323   5520   4498   -244   1994    -74       C  
ATOM   5463  CG  LYS C  57     -27.324 100.104  73.266  1.00 49.98           C  
ANISOU 5463  CG  LYS C  57     7022   6565   5401   -285   1999   -184       C  
ATOM   5464  CD  LYS C  57     -27.546  99.007  72.239  1.00 54.78           C  
ANISOU 5464  CD  LYS C  57     7561   7187   6065   -411   2050   -256       C  
ATOM   5465  CE  LYS C  57     -28.712  99.293  71.317  1.00 60.40           C  
ANISOU 5465  CE  LYS C  57     8076   8083   6788   -441   2039   -376       C  
ATOM   5466  NZ  LYS C  57     -30.018  98.991  71.959  1.00 61.92           N  
ANISOU 5466  NZ  LYS C  57     8190   8360   6977   -524   2163   -455       N  
ATOM   5467  N   GLY C  58     -25.110 102.911  73.264  1.00 36.47           N  
ANISOU 5467  N   GLY C  58     5449   4792   3614     27   1689    -22       N  
ATOM   5468  CA  GLY C  58     -25.059 104.326  73.560  1.00 35.46           C  
ANISOU 5468  CA  GLY C  58     5335   4698   3439    144   1613      0       C  
ATOM   5469  C   GLY C  58     -23.676 104.944  73.380  1.00 34.77           C  
ANISOU 5469  C   GLY C  58     5338   4529   3343    212   1511     62       C  
ATOM   5470  O   GLY C  58     -23.577 106.162  73.328  1.00 34.23           O  
ANISOU 5470  O   GLY C  58     5278   4486   3242    301   1445     71       O  
ATOM   5471  N   LEU C  59     -22.603 104.139  73.289  1.00 31.18           N  
ANISOU 5471  N   LEU C  59     4953   3977   2913    172   1504    103       N  
ATOM   5472  CA  LEU C  59     -21.245 104.692  73.159  1.00 30.94           C  
ANISOU 5472  CA  LEU C  59     5000   3882   2875    229   1411    153       C  
ATOM   5473  C   LEU C  59     -20.692 104.492  71.741  1.00 30.46           C  
ANISOU 5473  C   LEU C  59     4891   3821   2858    209   1356    138       C  
ATOM   5474  O   LEU C  59     -19.678 105.077  71.384  1.00 28.04           O  
ANISOU 5474  O   LEU C  59     4623   3479   2550    251   1279    165       O  
ATOM   5475  CB  LEU C  59     -20.304 104.019  74.158  1.00 30.37           C  
ANISOU 5475  CB  LEU C  59     5043   3710   2783    223   1432    212       C  
ATOM   5476  CG  LEU C  59     -20.637 104.172  75.635  1.00 30.54           C  
ANISOU 5476  CG  LEU C  59     5136   3716   2752    253   1482    238       C  
ATOM   5477  CD1 LEU C  59     -19.581 103.473  76.471  1.00 31.71           C  
ANISOU 5477  CD1 LEU C  59     5401   3775   2872    266   1491    296       C  
ATOM   5478  CD2 LEU C  59     -20.751 105.638  76.023  1.00 31.73           C  
ANISOU 5478  CD2 LEU C  59     5291   3904   2860    333   1425    235       C  
ATOM   5479  N   VAL C  60     -21.327 103.606  70.965  1.00 31.64           N  
ANISOU 5479  N   VAL C  60     4961   4010   3048    135   1402     91       N  
ATOM   5480  CA  VAL C  60     -20.930 103.291  69.593  1.00 30.22           C  
ANISOU 5480  CA  VAL C  60     4732   3838   2910    110   1359     70       C  
ATOM   5481  C   VAL C  60     -22.213 103.250  68.766  1.00 31.34           C  
ANISOU 5481  C   VAL C  60     4740   4101   3066     82   1384    -11       C  
ATOM   5482  O   VAL C  60     -23.302 103.124  69.341  1.00 31.95           O  
ANISOU 5482  O   VAL C  60     4769   4239   3129     56   1452    -49       O  
ATOM   5483  CB  VAL C  60     -20.207 101.932  69.515  1.00 31.61           C  
ANISOU 5483  CB  VAL C  60     4961   3926   3121     37   1399     94       C  
ATOM   5484  CG1 VAL C  60     -19.001 101.855  70.443  1.00 31.28           C  
ANISOU 5484  CG1 VAL C  60     5044   3785   3053     75   1381    169       C  
ATOM   5485  CG2 VAL C  60     -21.165 100.796  69.795  1.00 31.60           C  
ANISOU 5485  CG2 VAL C  60     4934   3935   3138    -58   1515     54       C  
ATOM   5486  N   ARG C  61     -22.078 103.267  67.442  1.00 28.90           N  
ANISOU 5486  N   ARG C  61     4369   3831   2781     84   1334    -42       N  
ATOM   5487  CA  ARG C  61     -23.197 102.981  66.555  1.00 31.20           C  
ANISOU 5487  CA  ARG C  61     4525   4244   3085     47   1357   -130       C  
ATOM   5488  C   ARG C  61     -22.989 101.606  65.938  1.00 32.45           C  
ANISOU 5488  C   ARG C  61     4668   4366   3294    -64   1401   -157       C  
ATOM   5489  O   ARG C  61     -21.862 101.219  65.663  1.00 32.10           O  
ANISOU 5489  O   ARG C  61     4700   4223   3273    -72   1373   -107       O  
ATOM   5490  CB  ARG C  61     -23.311 104.037  65.458  1.00 32.58           C  
ANISOU 5490  CB  ARG C  61     4639   4503   3235    145   1271   -152       C  
ATOM   5491  CG  ARG C  61     -23.833 105.390  65.927  1.00 35.35           C  
ANISOU 5491  CG  ARG C  61     4991   4912   3527    259   1243   -144       C  
ATOM   5492  CD  ARG C  61     -23.756 106.421  64.815  1.00 36.97           C  
ANISOU 5492  CD  ARG C  61     5173   5170   3700    368   1166   -152       C  
ATOM   5493  NE  ARG C  61     -24.629 106.080  63.703  1.00 37.87           N  
ANISOU 5493  NE  ARG C  61     5153   5420   3815    363   1162   -235       N  
ATOM   5494  CZ  ARG C  61     -24.589 106.654  62.503  1.00 40.19           C  
ANISOU 5494  CZ  ARG C  61     5416   5770   4084    447   1100   -251       C  
ATOM   5495  NH1 ARG C  61     -23.631 107.517  62.207  1.00 36.35           N  
ANISOU 5495  NH1 ARG C  61     5033   5196   3582    525   1048   -187       N  
ATOM   5496  NH2 ARG C  61     -25.521 106.375  61.608  1.00 40.00           N  
ANISOU 5496  NH2 ARG C  61     5256   5894   4047    453   1097   -338       N  
ATOM   5497  N   PHE C  62     -24.071 100.875  65.683  1.00 35.96           N  
ANISOU 5497  N   PHE C  62     5010   4895   3756   -151   1472   -244       N  
ATOM   5498  CA  PHE C  62     -23.887  99.627  65.015  1.00 38.98           C  
ANISOU 5498  CA  PHE C  62     5383   5241   4186   -260   1517   -278       C  
ATOM   5499  C   PHE C  62     -25.133  99.181  64.262  1.00 38.50           C  
ANISOU 5499  C   PHE C  62     5167   5324   4138   -337   1560   -403       C  
ATOM   5500  O   PHE C  62     -26.217  99.690  64.458  1.00 38.19           O  
ANISOU 5500  O   PHE C  62     5025   5413   4069   -317   1572   -463       O  
ATOM   5501  CB  PHE C  62     -23.437  98.532  65.982  1.00 44.61           C  
ANISOU 5501  CB  PHE C  62     6216   5815   4917   -342   1615   -231       C  
ATOM   5502  CG  PHE C  62     -24.530  98.028  66.873  1.00 48.86           C  
ANISOU 5502  CG  PHE C  62     6729   6382   5451   -424   1735   -279       C  
ATOM   5503  CD1 PHE C  62     -25.396  97.033  66.446  1.00 52.10           C  
ANISOU 5503  CD1 PHE C  62     7058   6842   5894   -558   1831   -378       C  
ATOM   5504  CD2 PHE C  62     -24.719  98.591  68.125  1.00 55.81           C  
ANISOU 5504  CD2 PHE C  62     7663   7247   6294   -373   1757   -234       C  
ATOM   5505  CE1 PHE C  62     -26.422  96.601  67.272  1.00 57.24           C  
ANISOU 5505  CE1 PHE C  62     7682   7522   6542   -643   1953   -430       C  
ATOM   5506  CE2 PHE C  62     -25.745  98.156  68.948  1.00 56.08           C  
ANISOU 5506  CE2 PHE C  62     7674   7309   6323   -448   1874   -279       C  
ATOM   5507  CZ  PHE C  62     -26.595  97.160  68.520  1.00 58.39           C  
ANISOU 5507  CZ  PHE C  62     7885   7648   6650   -586   1976   -377       C  
ATOM   5508  N   LYS C  63     -24.889  98.194  63.398  1.00 38.07           N  
ANISOU 5508  N   LYS C  63     5097   5244   4123   -425   1582   -441       N  
ATOM   5509  CA  LYS C  63     -25.864  97.550  62.570  1.00 42.16           C  
ANISOU 5509  CA  LYS C  63     5476   5881   4659   -522   1625   -567       C  
ATOM   5510  C   LYS C  63     -25.279  96.180  62.208  1.00 41.36           C  
ANISOU 5510  C   LYS C  63     5445   5662   4608   -644   1692   -571       C  
ATOM   5511  O   LYS C  63     -24.073  96.061  61.901  1.00 37.52           O  
ANISOU 5511  O   LYS C  63     5062   5059   4134   -604   1643   -490       O  
ATOM   5512  CB  LYS C  63     -26.171  98.437  61.350  1.00 48.17           C  
ANISOU 5512  CB  LYS C  63     6114   6794   5391   -423   1513   -619       C  
ATOM   5513  CG  LYS C  63     -26.674  97.744  60.084  1.00 50.29           C  
ANISOU 5513  CG  LYS C  63     6258   7169   5678   -502   1517   -736       C  
ATOM   5514  CD  LYS C  63     -27.160  98.706  58.996  1.00 52.24           C  
ANISOU 5514  CD  LYS C  63     6377   7593   5877   -380   1411   -792       C  
ATOM   5515  CE  LYS C  63     -28.582  99.189  59.199  1.00 52.78           C  
ANISOU 5515  CE  LYS C  63     6290   7862   5901   -356   1425   -892       C  
ATOM   5516  N   GLN C  64     -26.135  95.161  62.252  1.00 40.70           N  
ANISOU 5516  N   GLN C  64     5304   5609   4549   -794   1811   -669       N  
ATOM   5517  CA  GLN C  64     -25.798  93.827  61.808  1.00 42.48           C  
ANISOU 5517  CA  GLN C  64     5584   5738   4819   -922   1892   -698       C  
ATOM   5518  C   GLN C  64     -26.407  93.615  60.418  1.00 44.26           C  
ANISOU 5518  C   GLN C  64     5651   6108   5055   -977   1861   -828       C  
ATOM   5519  O   GLN C  64     -27.568  93.881  60.220  1.00 48.76           O  
ANISOU 5519  O   GLN C  64     6062   6852   5610  -1005   1869   -940       O  
ATOM   5520  CB  GLN C  64     -26.338  92.773  62.778  1.00 44.81           C  
ANISOU 5520  CB  GLN C  64     5939   5954   5132  -1067   2065   -728       C  
ATOM   5521  CG  GLN C  64     -25.812  91.377  62.464  1.00 48.20           C  
ANISOU 5521  CG  GLN C  64     6476   6239   5599  -1188   2164   -733       C  
ATOM   5522  CD  GLN C  64     -26.201  90.388  63.529  1.00 50.47           C  
ANISOU 5522  CD  GLN C  64     6865   6413   5895  -1312   2346   -739       C  
ATOM   5523  OE1 GLN C  64     -27.378  90.162  63.754  1.00 52.12           O  
ANISOU 5523  OE1 GLN C  64     6974   6714   6111  -1425   2442   -850       O  
ATOM   5524  NE2 GLN C  64     -25.214  89.812  64.199  1.00 50.55           N  
ANISOU 5524  NE2 GLN C  64     7077   6230   5900  -1286   2398   -623       N  
ATOM   5525  N   LEU C  65     -25.617  93.129  59.464  1.00 44.50           N  
ANISOU 5525  N   LEU C  65     5722   6076   5108   -986   1825   -815       N  
ATOM   5526  CA  LEU C  65     -26.163  92.809  58.168  1.00 48.52           C  
ANISOU 5526  CA  LEU C  65     6092   6716   5626  -1046   1804   -943       C  
ATOM   5527  C   LEU C  65     -26.978  91.521  58.290  1.00 54.43           C  
ANISOU 5527  C   LEU C  65     6807   7464   6409  -1250   1961  -1064       C  
ATOM   5528  O   LEU C  65     -26.738  90.725  59.183  1.00 51.30           O  
ANISOU 5528  O   LEU C  65     6546   6911   6035  -1335   2083  -1019       O  
ATOM   5529  CB  LEU C  65     -25.022  92.658  57.167  1.00 47.75           C  
ANISOU 5529  CB  LEU C  65     6062   6537   5541   -995   1725   -887       C  
ATOM   5530  CG  LEU C  65     -24.140  93.895  57.008  1.00 46.02           C  
ANISOU 5530  CG  LEU C  65     5887   6304   5292   -809   1584   -772       C  
ATOM   5531  CD1 LEU C  65     -23.024  93.628  56.009  1.00 45.83           C  
ANISOU 5531  CD1 LEU C  65     5928   6198   5285   -777   1524   -725       C  
ATOM   5532  CD2 LEU C  65     -24.974  95.091  56.589  1.00 45.04           C  
ANISOU 5532  CD2 LEU C  65     5616   6377   5120   -703   1494   -827       C  
ATOM   5533  N   LYS C  66     -27.926  91.345  57.364  1.00 61.34           N  
ANISOU 5533  N   LYS C  66     7505   8518   7282  -1323   1959  -1221       N  
ATOM   5534  CA  LYS C  66     -28.860  90.216  57.354  1.00 62.34           C  
ANISOU 5534  CA  LYS C  66     7562   8683   7439  -1533   2108  -1371       C  
ATOM   5535  C   LYS C  66     -28.150  88.928  56.922  1.00 59.51           C  
ANISOU 5535  C   LYS C  66     7333   8153   7125  -1654   2192  -1368       C  
ATOM   5536  O   LYS C  66     -28.428  87.868  57.449  1.00 68.12           O  
ANISOU 5536  O   LYS C  66     8495   9142   8246  -1818   2357  -1412       O  
ATOM   5537  CB  LYS C  66     -30.043  90.510  56.423  1.00 64.49           C  
ANISOU 5537  CB  LYS C  66     7588   9227   7687  -1558   2060  -1550       C  
ATOM   5538  CG  LYS C  66     -31.075  91.487  56.977  1.00 63.96           C  
ANISOU 5538  CG  LYS C  66     7377   9348   7576  -1486   2030  -1595       C  
ATOM   5539  CD  LYS C  66     -32.229  91.770  56.034  1.00 65.17           C  
ANISOU 5539  CD  LYS C  66     7278   9789   7692  -1492   1977  -1776       C  
ATOM   5540  N   LYS C  67     -27.281  89.020  55.916  1.00 63.14           N  
ANISOU 5540  N   LYS C  67     7822   8583   7584  -1573   2087  -1324       N  
ATOM   5541  CA  LYS C  67     -26.548  87.872  55.422  1.00 63.96           C  
ANISOU 5541  CA  LYS C  67     8049   8529   7723  -1665   2154  -1315       C  
ATOM   5542  C   LYS C  67     -25.057  88.177  55.560  1.00 63.25           C  
ANISOU 5542  C   LYS C  67     8133   8269   7629  -1516   2074  -1130       C  
ATOM   5543  O   LYS C  67     -24.653  89.329  55.482  1.00 62.46           O  
ANISOU 5543  O   LYS C  67     8007   8222   7500  -1351   1935  -1051       O  
ATOM   5544  CB  LYS C  67     -26.919  87.560  53.965  1.00 62.91           C  
ANISOU 5544  CB  LYS C  67     7777   8532   7593  -1725   2111  -1457       C  
ATOM   5545  N   ASN C  68     -24.254  87.133  55.779  1.00 62.09           N  
ANISOU 5545  N   ASN C  68     8164   7918   7506  -1576   2168  -1068       N  
ATOM   5546  CA  ASN C  68     -22.807  87.263  55.789  1.00 60.29           C  
ANISOU 5546  CA  ASN C  68     8090   7543   7275  -1446   2098   -911       C  
ATOM   5547  C   ASN C  68     -22.342  87.468  54.349  1.00 62.17           C  
ANISOU 5547  C   ASN C  68     8261   7845   7513  -1392   1980   -935       C  
ATOM   5548  O   ASN C  68     -22.632  86.642  53.500  1.00 68.51           O  
ANISOU 5548  O   ASN C  68     9029   8665   8336  -1505   2031  -1039       O  
ATOM   5549  CB  ASN C  68     -22.108  86.044  56.396  1.00 61.24           C  
ANISOU 5549  CB  ASN C  68     8420   7438   7409  -1511   2236   -842       C  
ATOM   5550  CG  ASN C  68     -20.617  86.044  56.134  1.00 62.29           C  
ANISOU 5550  CG  ASN C  68     8685   7446   7536  -1384   2159   -707       C  
ATOM   5551  OD1 ASN C  68     -19.882  86.885  56.645  1.00 59.91           O  
ANISOU 5551  OD1 ASN C  68     8424   7126   7211  -1238   2065   -590       O  
ATOM   5552  ND2 ASN C  68     -20.161  85.115  55.311  1.00 65.80           N  
ANISOU 5552  ND2 ASN C  68     9190   7812   7998  -1441   2199   -730       N  
ATOM   5553  N   SER C  69     -21.597  88.552  54.105  1.00 61.04           N  
ANISOU 5553  N   SER C  69     8113   7729   7348  -1223   1833   -839       N  
ATOM   5554  CA  SER C  69     -21.233  88.991  52.755  1.00 57.83           C  
ANISOU 5554  CA  SER C  69     7634   7404   6934  -1148   1711   -858       C  
ATOM   5555  C   SER C  69     -19.932  88.324  52.293  1.00 60.83           C  
ANISOU 5555  C   SER C  69     8153   7625   7332  -1128   1711   -777       C  
ATOM   5556  O   SER C  69     -19.682  88.234  51.089  1.00 66.75           O  
ANISOU 5556  O   SER C  69     8861   8416   8084  -1116   1654   -815       O  
ATOM   5557  CB  SER C  69     -21.125  90.499  52.687  1.00 55.62           C  
ANISOU 5557  CB  SER C  69     7287   7228   6618   -983   1570   -803       C  
ATOM   5558  OG  SER C  69     -19.884  90.937  53.215  1.00 51.18           O  
ANISOU 5558  OG  SER C  69     6857   6535   6053   -872   1523   -653       O  
ATOM   5559  N   GLY C  70     -19.084  87.896  53.234  1.00 58.42           N  
ANISOU 5559  N   GLY C  70     8013   7149   7033  -1110   1769   -663       N  
ATOM   5560  CA  GLY C  70     -17.886  87.171  52.860  1.00 54.90           C  
ANISOU 5560  CA  GLY C  70     7701   6559   6598  -1088   1780   -590       C  
ATOM   5561  C   GLY C  70     -16.603  87.934  53.105  1.00 52.80           C  
ANISOU 5561  C   GLY C  70     7509   6236   6317   -929   1677   -450       C  
ATOM   5562  O   GLY C  70     -15.616  87.319  53.481  1.00 55.92           O  
ANISOU 5562  O   GLY C  70     8044   6490   6710   -900   1715   -363       O  
ATOM   5563  N   ASN C  71     -16.584  89.250  52.855  1.00 52.02           N  
ANISOU 5563  N   ASN C  71     7316   6246   6200   -823   1552   -431       N  
ATOM   5564  CA  ASN C  71     -15.374  90.065  53.113  1.00 50.59           C  
ANISOU 5564  CA  ASN C  71     7199   6019   6005   -685   1459   -309       C  
ATOM   5565  C   ASN C  71     -15.797  91.419  53.692  1.00 44.50           C  
ANISOU 5565  C   ASN C  71     6359   5341   5209   -608   1389   -293       C  
ATOM   5566  O   ASN C  71     -16.974  91.692  53.834  1.00 46.33           O  
ANISOU 5566  O   ASN C  71     6494   5674   5432   -649   1407   -369       O  
ATOM   5567  CB  ASN C  71     -14.471  90.208  51.880  1.00 53.19           C  
ANISOU 5567  CB  ASN C  71     7524   6345   6339   -624   1378   -289       C  
ATOM   5568  CG  ASN C  71     -15.194  90.774  50.678  1.00 62.87           C  
ANISOU 5568  CG  ASN C  71     8614   7714   7560   -621   1312   -379       C  
ATOM   5569  OD1 ASN C  71     -16.292  91.321  50.808  1.00 67.67           O  
ANISOU 5569  OD1 ASN C  71     9119   8439   8151   -633   1303   -446       O  
ATOM   5570  ND2 ASN C  71     -14.586  90.644  49.507  1.00 64.08           N  
ANISOU 5570  ND2 ASN C  71     8765   7862   7717   -593   1266   -382       N  
ATOM   5571  N   ALA C  72     -14.797  92.226  54.044  1.00 40.98           N  
ANISOU 5571  N   ALA C  72     5964   4856   4748   -498   1315   -196       N  
ATOM   5572  CA  ALA C  72     -14.950  93.524  54.682  1.00 39.25           C  
ANISOU 5572  CA  ALA C  72     5714   4696   4503   -416   1254   -163       C  
ATOM   5573  C   ALA C  72     -15.625  94.572  53.774  1.00 38.41           C  
ANISOU 5573  C   ALA C  72     5488   4725   4379   -368   1176   -221       C  
ATOM   5574  O   ALA C  72     -15.957  95.653  54.246  1.00 33.79           O  
ANISOU 5574  O   ALA C  72     4873   4196   3767   -303   1136   -207       O  
ATOM   5575  CB  ALA C  72     -13.587  93.998  55.125  1.00 38.39           C  
ANISOU 5575  CB  ALA C  72     5692   4507   4384   -326   1201    -59       C  
ATOM   5576  N   SER C  73     -15.833  94.274  52.486  1.00 38.75           N  
ANISOU 5576  N   SER C  73     5469   4823   4430   -389   1157   -285       N  
ATOM   5577  CA  SER C  73     -16.201  95.296  51.507  1.00 36.40           C  
ANISOU 5577  CA  SER C  73     5083   4643   4104   -310   1074   -321       C  
ATOM   5578  C   SER C  73     -17.609  95.837  51.784  1.00 35.17           C  
ANISOU 5578  C   SER C  73     4819   4625   3917   -308   1078   -397       C  
ATOM   5579  O   SER C  73     -17.791  97.046  51.954  1.00 39.77           O  
ANISOU 5579  O   SER C  73     5382   5264   4464   -209   1023   -373       O  
ATOM   5580  CB  SER C  73     -16.026  94.782  50.083  1.00 37.75           C  
ANISOU 5580  CB  SER C  73     5222   4837   4283   -326   1053   -369       C  
ATOM   5581  OG  SER C  73     -14.630  94.663  49.764  1.00 38.93           O  
ANISOU 5581  OG  SER C  73     5465   4875   4450   -289   1028   -287       O  
ATOM   5582  N   VAL C  74     -18.598  94.957  51.898  1.00 36.09           N  
ANISOU 5582  N   VAL C  74     4871   4793   4046   -419   1151   -489       N  
ATOM   5583  CA  VAL C  74     -19.995  95.384  52.044  1.00 38.42           C  
ANISOU 5583  CA  VAL C  74     5040   5246   4311   -424   1157   -581       C  
ATOM   5584  C   VAL C  74     -20.215  96.028  53.424  1.00 40.09           C  
ANISOU 5584  C   VAL C  74     5285   5437   4509   -391   1176   -527       C  
ATOM   5585  O   VAL C  74     -20.906  97.050  53.529  1.00 35.47           O  
ANISOU 5585  O   VAL C  74     4630   4964   3881   -309   1133   -546       O  
ATOM   5586  CB  VAL C  74     -20.960  94.217  51.734  1.00 41.22           C  
ANISOU 5586  CB  VAL C  74     5308   5668   4686   -570   1238   -710       C  
ATOM   5587  CG1 VAL C  74     -22.397  94.489  52.179  1.00 40.77           C  
ANISOU 5587  CG1 VAL C  74     5121   5766   4603   -600   1268   -809       C  
ATOM   5588  CG2 VAL C  74     -20.909  93.878  50.240  1.00 40.60           C  
ANISOU 5588  CG2 VAL C  74     5169   5652   4603   -575   1196   -779       C  
ATOM   5589  N   PRO C  75     -19.670  95.474  54.535  1.00 40.52           N  
ANISOU 5589  N   PRO C  75     5450   5355   4591   -443   1241   -458       N  
ATOM   5590  CA  PRO C  75     -19.725  96.169  55.821  1.00 39.07           C  
ANISOU 5590  CA  PRO C  75     5311   5146   4388   -395   1248   -397       C  
ATOM   5591  C   PRO C  75     -19.099  97.574  55.789  1.00 35.21           C  
ANISOU 5591  C   PRO C  75     4852   4659   3866   -252   1150   -322       C  
ATOM   5592  O   PRO C  75     -19.679  98.489  56.282  1.00 33.58           O  
ANISOU 5592  O   PRO C  75     4613   4519   3626   -191   1131   -324       O  
ATOM   5593  CB  PRO C  75     -18.941  95.265  56.783  1.00 40.86           C  
ANISOU 5593  CB  PRO C  75     5671   5212   4641   -454   1322   -326       C  
ATOM   5594  CG  PRO C  75     -18.960  93.903  56.147  1.00 41.69           C  
ANISOU 5594  CG  PRO C  75     5781   5276   4780   -567   1392   -380       C  
ATOM   5595  CD  PRO C  75     -19.124  94.112  54.658  1.00 40.41           C  
ANISOU 5595  CD  PRO C  75     5522   5213   4617   -548   1323   -446       C  
ATOM   5596  N   ARG C  76     -17.915  97.722  55.202  1.00 34.78           N  
ANISOU 5596  N   ARG C  76     4864   4528   3821   -204   1097   -261       N  
ATOM   5597  CA  ARG C  76     -17.293  99.052  55.083  1.00 33.88           C  
ANISOU 5597  CA  ARG C  76     4785   4409   3679    -84   1017   -199       C  
ATOM   5598  C   ARG C  76     -18.153 100.020  54.250  1.00 31.64           C  
ANISOU 5598  C   ARG C  76     4410   4262   3350      0    966   -254       C  
ATOM   5599  O   ARG C  76     -18.340 101.172  54.631  1.00 30.85           O  
ANISOU 5599  O   ARG C  76     4320   4190   3210     88    936   -229       O  
ATOM   5600  CB  ARG C  76     -15.904  98.907  54.481  1.00 32.10           C  
ANISOU 5600  CB  ARG C  76     4634   4086   3474    -65    982   -140       C  
ATOM   5601  CG  ARG C  76     -14.866  98.424  55.477  1.00 32.51           C  
ANISOU 5601  CG  ARG C  76     4791   4014   3548    -91   1009    -64       C  
ATOM   5602  CD  ARG C  76     -13.670  98.012  54.676  1.00 34.04           C  
ANISOU 5602  CD  ARG C  76     5030   4138   3765    -87    983    -30       C  
ATOM   5603  NE  ARG C  76     -12.519  97.720  55.504  1.00 37.80           N  
ANISOU 5603  NE  ARG C  76     5598   4512   4249    -83    991     42       N  
ATOM   5604  CZ  ARG C  76     -11.486  97.015  55.075  1.00 39.87           C  
ANISOU 5604  CZ  ARG C  76     5907   4708   4533    -92    991     73       C  
ATOM   5605  NH1 ARG C  76     -11.524  96.505  53.851  1.00 34.80           N  
ANISOU 5605  NH1 ARG C  76     5232   4079   3909   -116    988     36       N  
ATOM   5606  NH2 ARG C  76     -10.449  96.806  55.872  1.00 37.89           N  
ANISOU 5606  NH2 ARG C  76     5731   4385   4278    -71    992    135       N  
ATOM   5607  N   ASN C  77     -18.680  99.561  53.116  1.00 30.42           N  
ANISOU 5607  N   ASN C  77     4169   4194   3193    -21    958   -332       N  
ATOM   5608  CA  ASN C  77     -19.579 100.389  52.289  1.00 31.69           C  
ANISOU 5608  CA  ASN C  77     4235   4506   3298     72    909   -393       C  
ATOM   5609  C   ASN C  77     -20.791 100.824  53.110  1.00 34.31           C  
ANISOU 5609  C   ASN C  77     4495   4943   3596     87    933   -438       C  
ATOM   5610  O   ASN C  77     -21.297 101.932  52.957  1.00 33.30           O  
ANISOU 5610  O   ASN C  77     4338   4903   3409    207    892   -443       O  
ATOM   5611  CB  ASN C  77     -19.993  99.675  50.996  1.00 32.64           C  
ANISOU 5611  CB  ASN C  77     4265   4717   3418     37    899   -483       C  
ATOM   5612  CG  ASN C  77     -18.834  99.522  50.037  1.00 32.43           C  
ANISOU 5612  CG  ASN C  77     4308   4603   3410     57    864   -436       C  
ATOM   5613  OD1 ASN C  77     -17.859 100.261  50.114  1.00 32.01           O  
ANISOU 5613  OD1 ASN C  77     4351   4457   3354    128    832   -346       O  
ATOM   5614  ND2 ASN C  77     -18.894  98.517  49.182  1.00 32.68           N  
ANISOU 5614  ND2 ASN C  77     4295   4657   3464    -16    877   -498       N  
ATOM   5615  N   THR C  78     -21.252  99.944  54.002  1.00 35.74           N  
ANISOU 5615  N   THR C  78     4657   5111   3811    -29   1008   -469       N  
ATOM   5616  CA  THR C  78     -22.405 100.228  54.836  1.00 35.03           C  
ANISOU 5616  CA  THR C  78     4495   5120   3695    -31   1043   -516       C  
ATOM   5617  C   THR C  78     -22.057 101.314  55.864  1.00 35.75           C  
ANISOU 5617  C   THR C  78     4675   5147   3760     57   1026   -425       C  
ATOM   5618  O   THR C  78     -22.879 102.209  56.122  1.00 36.16           O  
ANISOU 5618  O   THR C  78     4677   5301   3761    142   1010   -447       O  
ATOM   5619  CB  THR C  78     -22.929  98.930  55.463  1.00 37.37           C  
ANISOU 5619  CB  THR C  78     4760   5402   4036   -193   1143   -574       C  
ATOM   5620  OG1 THR C  78     -23.273  98.038  54.398  1.00 35.11           O  
ANISOU 5620  OG1 THR C  78     4388   5185   3767   -273   1156   -671       O  
ATOM   5621  CG2 THR C  78     -24.124  99.154  56.361  1.00 38.07           C  
ANISOU 5621  CG2 THR C  78     4771   5592   4101   -209   1191   -628       C  
ATOM   5622  N   GLY C  79     -20.855 101.229  56.453  1.00 32.63           N  
ANISOU 5622  N   GLY C  79     4410   4590   3396     41   1030   -330       N  
ATOM   5623  CA  GLY C  79     -20.360 102.245  57.358  1.00 32.39           C  
ANISOU 5623  CA  GLY C  79     4470   4492   3343    118   1009   -249       C  
ATOM   5624  C   GLY C  79     -20.233 103.594  56.658  1.00 33.59           C  
ANISOU 5624  C   GLY C  79     4635   4683   3444    257    940   -229       C  
ATOM   5625  O   GLY C  79     -20.631 104.632  57.216  1.00 31.71           O  
ANISOU 5625  O   GLY C  79     4413   4475   3161    341    931   -212       O  
ATOM   5626  N   LEU C  80     -19.712 103.580  55.424  1.00 33.04           N  
ANISOU 5626  N   LEU C  80     4566   4610   3378    285    898   -231       N  
ATOM   5627  CA  LEU C  80     -19.616 104.800  54.597  1.00 34.65           C  
ANISOU 5627  CA  LEU C  80     4792   4846   3527    421    843   -215       C  
ATOM   5628  C   LEU C  80     -20.977 105.508  54.474  1.00 35.59           C  
ANISOU 5628  C   LEU C  80     4822   5122   3575    518    835   -275       C  
ATOM   5629  O   LEU C  80     -21.039 106.695  54.724  1.00 35.56           O  
ANISOU 5629  O   LEU C  80     4875   5115   3521    629    820   -238       O  
ATOM   5630  CB  LEU C  80     -19.036 104.469  53.210  1.00 32.12           C  
ANISOU 5630  CB  LEU C  80     4468   4516   3218    427    810   -223       C  
ATOM   5631  CG  LEU C  80     -17.522 104.292  53.195  1.00 32.07           C  
ANISOU 5631  CG  LEU C  80     4569   4356   3259    387    804   -148       C  
ATOM   5632  CD1 LEU C  80     -17.023 103.878  51.814  1.00 31.60           C  
ANISOU 5632  CD1 LEU C  80     4499   4294   3210    389    778   -161       C  
ATOM   5633  CD2 LEU C  80     -16.841 105.573  53.678  1.00 32.21           C  
ANISOU 5633  CD2 LEU C  80     4693   4294   3250    465    791    -78       C  
ATOM   5634  N   LYS C  81     -22.055 104.787  54.118  1.00 36.39           N  
ANISOU 5634  N   LYS C  81     4789   5364   3673    476    848   -370       N  
ATOM   5635  CA  LYS C  81     -23.400 105.390  53.993  1.00 38.03           C  
ANISOU 5635  CA  LYS C  81     4890   5750   3808    573    838   -441       C  
ATOM   5636  C   LYS C  81     -23.889 105.929  55.346  1.00 39.20           C  
ANISOU 5636  C   LYS C  81     5058   5896   3940    589    872   -418       C  
ATOM   5637  O   LYS C  81     -24.657 106.885  55.392  1.00 42.61           O  
ANISOU 5637  O   LYS C  81     5461   6429   4299    716    857   -434       O  
ATOM   5638  CB  LYS C  81     -24.438 104.399  53.450  1.00 39.46           C  
ANISOU 5638  CB  LYS C  81     4907   6092   3994    498    853   -564       C  
ATOM   5639  CG  LYS C  81     -24.643 104.408  51.938  1.00 42.30           C  
ANISOU 5639  CG  LYS C  81     5194   6564   4311    570    798   -624       C  
ATOM   5640  N   MET C  82     -23.489 105.313  56.458  1.00 38.73           N  
ANISOU 5640  N   MET C  82     5048   5727   3938    471    922   -383       N  
ATOM   5641  CA  MET C  82     -24.029 105.763  57.761  1.00 40.32           C  
ANISOU 5641  CA  MET C  82     5262   5935   4120    484    959   -368       C  
ATOM   5642  C   MET C  82     -23.268 106.993  58.251  1.00 40.74           C  
ANISOU 5642  C   MET C  82     5455   5879   4143    584    934   -274       C  
ATOM   5643  O   MET C  82     -23.781 107.724  59.081  1.00 42.24           O  
ANISOU 5643  O   MET C  82     5661   6094   4293    643    949   -263       O  
ATOM   5644  CB  MET C  82     -23.941 104.684  58.845  1.00 40.50           C  
ANISOU 5644  CB  MET C  82     5298   5883   4204    333   1030   -364       C  
ATOM   5645  CG  MET C  82     -24.797 103.455  58.564  1.00 43.69           C  
ANISOU 5645  CG  MET C  82     5574   6385   4639    211   1081   -466       C  
ATOM   5646  SD  MET C  82     -24.318 102.060  59.614  1.00 45.63           S  
ANISOU 5646  SD  MET C  82     5889   6486   4960     35   1175   -439       S  
ATOM   5647  CE  MET C  82     -24.798 102.668  61.228  1.00 46.11           C  
ANISOU 5647  CE  MET C  82     5990   6535   4992     63   1219   -403       C  
ATOM   5648  N   SER C  83     -22.036 107.194  57.769  1.00 39.34           N  
ANISOU 5648  N   SER C  83     5378   5580   3986    592    902   -212       N  
ATOM   5649  CA  SER C  83     -21.189 108.264  58.289  1.00 38.75           C  
ANISOU 5649  CA  SER C  83     5440   5389   3893    655    890   -133       C  
ATOM   5650  C   SER C  83     -21.552 109.606  57.641  1.00 40.68           C  
ANISOU 5650  C   SER C  83     5713   5684   4057    817    862   -130       C  
ATOM   5651  O   SER C  83     -21.695 109.695  56.413  1.00 41.96           O  
ANISOU 5651  O   SER C  83     5841   5909   4193    881    833   -156       O  
ATOM   5652  CB  SER C  83     -19.740 107.968  58.086  1.00 34.36           C  
ANISOU 5652  CB  SER C  83     4973   4692   3388    595    876    -77       C  
ATOM   5653  OG  SER C  83     -18.985 109.136  58.335  1.00 34.15           O  
ANISOU 5653  OG  SER C  83     5064   4574   3334    662    863    -20       O  
ATOM   5654  N   LYS C  84     -21.629 110.656  58.466  1.00 43.52           N  
ANISOU 5654  N   LYS C  84     6153   6008   4374    888    876    -94       N  
ATOM   5655  CA  LYS C  84     -21.774 112.040  57.964  1.00 43.23           C  
ANISOU 5655  CA  LYS C  84     6192   5978   4256   1048    864    -74       C  
ATOM   5656  C   LYS C  84     -20.586 112.905  58.426  1.00 41.15           C  
ANISOU 5656  C   LYS C  84     6091   5545   3997   1048    875     -3       C  
ATOM   5657  O   LYS C  84     -20.672 114.143  58.386  1.00 42.96           O  
ANISOU 5657  O   LYS C  84     6415   5746   4159   1165    887     20       O  
ATOM   5658  CB  LYS C  84     -23.137 112.595  58.404  1.00 47.34           C  
ANISOU 5658  CB  LYS C  84     6653   6630   4705   1152    878   -111       C  
ATOM   5659  CG  LYS C  84     -24.349 111.895  57.788  1.00 46.61           C  
ANISOU 5659  CG  LYS C  84     6385   6730   4593   1167    866   -198       C  
ATOM   5660  N   ALA C  85     -19.466 112.275  58.816  1.00 34.56           N  
ANISOU 5660  N   ALA C  85     5293   4600   3236    921    874     25       N  
ATOM   5661  CA  ALA C  85     -18.322 112.979  59.421  1.00 32.80           C  
ANISOU 5661  CA  ALA C  85     5202   4235   3022    896    885     76       C  
ATOM   5662  C   ALA C  85     -17.481 113.637  58.325  1.00 31.97           C  
ANISOU 5662  C   ALA C  85     5183   4056   2906    941    878     98       C  
ATOM   5663  O   ALA C  85     -17.697 113.388  57.128  1.00 29.43           O  
ANISOU 5663  O   ALA C  85     4816   3788   2575    983    861     82       O  
ATOM   5664  CB  ALA C  85     -17.482 112.028  60.235  1.00 32.43           C  
ANISOU 5664  CB  ALA C  85     5150   4124   3048    760    883     91       C  
ATOM   5665  N   GLU C  86     -16.476 114.426  58.713  1.00 30.92           N  
ANISOU 5665  N   GLU C  86     5171   3801   2774    921    897    131       N  
ATOM   5666  CA  GLU C  86     -15.686 115.042  57.666  1.00 33.95           C  
ANISOU 5666  CA  GLU C  86     5640   4110   3148    953    905    148       C  
ATOM   5667  C   GLU C  86     -14.550 114.111  57.187  1.00 28.74           C  
ANISOU 5667  C   GLU C  86     4949   3404   2563    842    882    154       C  
ATOM   5668  O   GLU C  86     -14.139 114.221  56.045  1.00 25.96           O  
ANISOU 5668  O   GLU C  86     4622   3029   2211    868    881    159       O  
ATOM   5669  CB  GLU C  86     -15.306 116.464  58.048  1.00 38.58           C  
ANISOU 5669  CB  GLU C  86     6376   4595   3686   1001    950    169       C  
ATOM   5670  CG  GLU C  86     -13.978 116.679  58.713  1.00 44.26           C  
ANISOU 5670  CG  GLU C  86     7168   5198   4449    890    964    179       C  
ATOM   5671  CD  GLU C  86     -13.672 118.175  58.795  1.00 46.76           C  
ANISOU 5671  CD  GLU C  86     7643   5411   4710    942   1023    188       C  
ATOM   5672  OE1 GLU C  86     -13.183 118.725  57.789  1.00 48.88           O  
ANISOU 5672  OE1 GLU C  86     7992   5616   4963    973   1054    197       O  
ATOM   5673  OE2 GLU C  86     -13.978 118.792  59.829  1.00 46.65           O  
ANISOU 5673  OE2 GLU C  86     7680   5380   4664    955   1045    184       O  
ATOM   5674  N   TYR C  87     -14.035 113.251  58.067  1.00 27.88           N  
ANISOU 5674  N   TYR C  87     4799   3281   2513    731    867    155       N  
ATOM   5675  CA  TYR C  87     -13.066 112.231  57.728  1.00 24.83           C  
ANISOU 5675  CA  TYR C  87     4373   2867   2192    637    845    159       C  
ATOM   5676  C   TYR C  87     -13.582 110.856  58.191  1.00 25.55           C  
ANISOU 5676  C   TYR C  87     4360   3025   2321    577    830    145       C  
ATOM   5677  O   TYR C  87     -14.284 110.747  59.206  1.00 24.54           O  
ANISOU 5677  O   TYR C  87     4209   2933   2179    574    841    139       O  
ATOM   5678  CB  TYR C  87     -11.731 112.521  58.415  1.00 24.90           C  
ANISOU 5678  CB  TYR C  87     4450   2781   2227    563    850    174       C  
ATOM   5679  CG  TYR C  87     -10.955 113.656  57.803  1.00 27.01           C  
ANISOU 5679  CG  TYR C  87     4818   2966   2476    584    877    179       C  
ATOM   5680  CD1 TYR C  87     -10.102 113.451  56.734  1.00 26.49           C  
ANISOU 5680  CD1 TYR C  87     4759   2865   2439    558    874    183       C  
ATOM   5681  CD2 TYR C  87     -11.040 114.939  58.322  1.00 28.56           C  
ANISOU 5681  CD2 TYR C  87     5114   3112   2624    623    914    178       C  
ATOM   5682  CE1 TYR C  87      -9.400 114.496  56.152  1.00 27.80           C  
ANISOU 5682  CE1 TYR C  87     5025   2948   2587    571    913    186       C  
ATOM   5683  CE2 TYR C  87     -10.338 115.995  57.756  1.00 29.93           C  
ANISOU 5683  CE2 TYR C  87     5396   3196   2778    634    956    179       C  
ATOM   5684  CZ  TYR C  87      -9.508 115.773  56.679  1.00 27.01           C  
ANISOU 5684  CZ  TYR C  87     5030   2792   2440    604    959    183       C  
ATOM   5685  OH  TYR C  87      -8.810 116.812  56.154  1.00 27.52           O  
ANISOU 5685  OH  TYR C  87     5209   2762   2485    605   1014    181       O  
ATOM   5686  N   VAL C  88     -13.200 109.797  57.471  1.00 23.63           N  
ANISOU 5686  N   VAL C  88     4063   2790   2123    525    814    141       N  
ATOM   5687  CA  VAL C  88     -13.442 108.446  57.935  1.00 24.01           C  
ANISOU 5687  CA  VAL C  88     4040   2872   2211    452    814    131       C  
ATOM   5688  C   VAL C  88     -12.086 107.772  58.159  1.00 24.64           C  
ANISOU 5688  C   VAL C  88     4145   2878   2337    377    804    157       C  
ATOM   5689  O   VAL C  88     -11.074 108.095  57.529  1.00 24.59           O  
ANISOU 5689  O   VAL C  88     4177   2821   2344    374    791    170       O  
ATOM   5690  CB  VAL C  88     -14.326 107.647  56.962  1.00 25.47           C  
ANISOU 5690  CB  VAL C  88     4133   3140   2402    455    812     92       C  
ATOM   5691  CG1 VAL C  88     -15.737 108.207  56.913  1.00 26.46           C  
ANISOU 5691  CG1 VAL C  88     4211   3366   2474    532    819     57       C  
ATOM   5692  CG2 VAL C  88     -13.723 107.606  55.566  1.00 24.35           C  
ANISOU 5692  CG2 VAL C  88     3996   2982   2272    471    791     93       C  
ATOM   5693  N   PHE C  89     -12.079 106.814  59.074  1.00 23.10           N  
ANISOU 5693  N   PHE C  89     3932   2682   2163    321    816    163       N  
ATOM   5694  CA  PHE C  89     -10.916 106.031  59.348  1.00 24.53           C  
ANISOU 5694  CA  PHE C  89     4132   2811   2378    268    808    187       C  
ATOM   5695  C   PHE C  89     -11.357 104.563  59.494  1.00 23.95           C  
ANISOU 5695  C   PHE C  89     4016   2754   2329    218    834    182       C  
ATOM   5696  O   PHE C  89     -12.205 104.231  60.359  1.00 25.56           O  
ANISOU 5696  O   PHE C  89     4208   2983   2521    205    866    174       O  
ATOM   5697  CB  PHE C  89     -10.211 106.561  60.598  1.00 26.20           C  
ANISOU 5697  CB  PHE C  89     4400   2985   2570    266    802    206       C  
ATOM   5698  CG  PHE C  89      -8.926 105.838  60.887  1.00 27.39           C  
ANISOU 5698  CG  PHE C  89     4565   3099   2742    229    786    227       C  
ATOM   5699  CD1 PHE C  89      -8.933 104.548  61.388  1.00 27.98           C  
ANISOU 5699  CD1 PHE C  89     4630   3172   2828    203    803    242       C  
ATOM   5700  CD2 PHE C  89      -7.711 106.410  60.565  1.00 26.85           C  
ANISOU 5700  CD2 PHE C  89     4521   3001   2680    224    761    227       C  
ATOM   5701  CE1 PHE C  89      -7.747 103.860  61.593  1.00 28.94           C  
ANISOU 5701  CE1 PHE C  89     4768   3268   2959    190    788    263       C  
ATOM   5702  CE2 PHE C  89      -6.525 105.734  60.805  1.00 27.22           C  
ANISOU 5702  CE2 PHE C  89     4569   3033   2740    201    743    239       C  
ATOM   5703  CZ  PHE C  89      -6.543 104.457  61.314  1.00 29.84           C  
ANISOU 5703  CZ  PHE C  89     4892   3369   3075    193    753    260       C  
ATOM   5704  N   PHE C  90     -10.788 103.681  58.672  1.00 23.18           N  
ANISOU 5704  N   PHE C  90     3904   2636   2265    187    829    184       N  
ATOM   5705  CA  PHE C  90     -11.128 102.264  58.715  1.00 24.15           C  
ANISOU 5705  CA  PHE C  90     4004   2758   2412    134    866    177       C  
ATOM   5706  C   PHE C  90     -10.193 101.548  59.684  1.00 25.15           C  
ANISOU 5706  C   PHE C  90     4186   2828   2541    116    877    217       C  
ATOM   5707  O   PHE C  90      -8.994 101.598  59.530  1.00 25.09           O  
ANISOU 5707  O   PHE C  90     4205   2787   2539    128    847    241       O  
ATOM   5708  CB  PHE C  90     -11.037 101.661  57.318  1.00 25.59           C  
ANISOU 5708  CB  PHE C  90     4151   2949   2624    115    860    156       C  
ATOM   5709  CG  PHE C  90     -11.991 102.283  56.333  1.00 24.88           C  
ANISOU 5709  CG  PHE C  90     4003   2930   2520    147    847    112       C  
ATOM   5710  CD1 PHE C  90     -13.321 101.896  56.321  1.00 26.49           C  
ANISOU 5710  CD1 PHE C  90     4141   3205   2716    126    877     62       C  
ATOM   5711  CD2 PHE C  90     -11.570 103.251  55.438  1.00 26.08           C  
ANISOU 5711  CD2 PHE C  90     4166   3082   2659    203    809    117       C  
ATOM   5712  CE1 PHE C  90     -14.212 102.453  55.423  1.00 27.39           C  
ANISOU 5712  CE1 PHE C  90     4193   3406   2805    170    859     15       C  
ATOM   5713  CE2 PHE C  90     -12.470 103.827  54.546  1.00 25.91           C  
ANISOU 5713  CE2 PHE C  90     4100   3132   2610    254    798     79       C  
ATOM   5714  CZ  PHE C  90     -13.782 103.415  54.526  1.00 26.77           C  
ANISOU 5714  CZ  PHE C  90     4134   3327   2707    244    817     28       C  
ATOM   5715  N   LEU C  91     -10.791 100.840  60.646  1.00 25.63           N  
ANISOU 5715  N   LEU C  91     4262   2884   2592     91    926    221       N  
ATOM   5716  CA  LEU C  91     -10.072 100.061  61.659  1.00 27.28           C  
ANISOU 5716  CA  LEU C  91     4534   3041   2788     91    948    262       C  
ATOM   5717  C   LEU C  91     -10.595  98.616  61.614  1.00 29.09           C  
ANISOU 5717  C   LEU C  91     4776   3242   3033     38   1021    256       C  
ATOM   5718  O   LEU C  91     -11.813  98.386  61.597  1.00 31.07           O  
ANISOU 5718  O   LEU C  91     4990   3522   3290     -4   1070    218       O  
ATOM   5719  CB  LEU C  91     -10.313 100.692  63.035  1.00 28.26           C  
ANISOU 5719  CB  LEU C  91     4690   3174   2871    119    952    276       C  
ATOM   5720  CG  LEU C  91      -9.465 100.111  64.165  1.00 29.50           C  
ANISOU 5720  CG  LEU C  91     4918   3292   2997    145    962    319       C  
ATOM   5721  CD1 LEU C  91      -7.994 100.449  63.956  1.00 28.91           C  
ANISOU 5721  CD1 LEU C  91     4854   3212   2918    180    898    335       C  
ATOM   5722  CD2 LEU C  91      -9.940 100.593  65.520  1.00 32.75           C  
ANISOU 5722  CD2 LEU C  91     5361   3715   3365    169    977    327       C  
ATOM   5723  N   ASP C  92      -9.682  97.644  61.521  1.00 29.60           N  
ANISOU 5723  N   ASP C  92     4890   3252   3104     39   1034    287       N  
ATOM   5724  CA  ASP C  92     -10.088  96.247  61.522  1.00 31.71           C  
ANISOU 5724  CA  ASP C  92     5194   3472   3381    -10   1117    285       C  
ATOM   5725  C   ASP C  92     -10.250  95.804  62.968  1.00 30.96           C  
ANISOU 5725  C   ASP C  92     5177   3340   3246      3   1176    319       C  
ATOM   5726  O   ASP C  92      -9.672  96.397  63.895  1.00 29.25           O  
ANISOU 5726  O   ASP C  92     4991   3129   2991     65   1138    353       O  
ATOM   5727  CB  ASP C  92      -9.116  95.348  60.754  1.00 35.36           C  
ANISOU 5727  CB  ASP C  92     5689   3886   3861     -7   1117    305       C  
ATOM   5728  CG  ASP C  92      -9.044  95.700  59.282  1.00 42.82           C  
ANISOU 5728  CG  ASP C  92     6561   4864   4842    -24   1069    270       C  
ATOM   5729  OD1 ASP C  92     -10.100  96.090  58.709  1.00 49.38           O  
ANISOU 5729  OD1 ASP C  92     7323   5748   5690    -62   1072    217       O  
ATOM   5730  OD2 ASP C  92      -7.942  95.596  58.730  1.00 49.68           O  
ANISOU 5730  OD2 ASP C  92     7443   5713   5718      7   1030    293       O  
ATOM   5731  N   SER C  93     -11.020  94.725  63.123  1.00 32.44           N  
ANISOU 5731  N   SER C  93     5397   3485   3440    -58   1276    304       N  
ATOM   5732  CA  SER C  93     -11.571  94.307  64.372  1.00 32.73           C  
ANISOU 5732  CA  SER C  93     5502   3488   3443    -65   1356    322       C  
ATOM   5733  C   SER C  93     -10.509  93.832  65.374  1.00 32.77           C  
ANISOU 5733  C   SER C  93     5623   3432   3395     17   1365    395       C  
ATOM   5734  O   SER C  93     -10.834  93.702  66.547  1.00 34.77           O  
ANISOU 5734  O   SER C  93     5939   3662   3606     37   1417    419       O  
ATOM   5735  CB  SER C  93     -12.612  93.249  64.154  1.00 36.99           C  
ANISOU 5735  CB  SER C  93     6051   3994   4007   -165   1472    279       C  
ATOM   5736  OG  SER C  93     -12.051  92.140  63.476  1.00 39.89           O  
ANISOU 5736  OG  SER C  93     6474   4292   4391   -186   1511    288       O  
ATOM   5737  N   ASP C  94      -9.270  93.562  64.955  1.00 31.40           N  
ANISOU 5737  N   ASP C  94     5477   3239   3215     73   1316    428       N  
ATOM   5738  CA  ASP C  94      -8.225  93.183  65.941  1.00 35.67           C  
ANISOU 5738  CA  ASP C  94     6116   3746   3691    173   1313    493       C  
ATOM   5739  C   ASP C  94      -7.140  94.264  66.100  1.00 35.48           C  
ANISOU 5739  C   ASP C  94     6043   3791   3644    250   1192    503       C  
ATOM   5740  O   ASP C  94      -6.148  94.015  66.774  1.00 37.25           O  
ANISOU 5740  O   ASP C  94     6326   4015   3812    340   1170    544       O  
ATOM   5741  CB  ASP C  94      -7.543  91.867  65.564  1.00 38.29           C  
ANISOU 5741  CB  ASP C  94     6534   4002   4012    196   1366    526       C  
ATOM   5742  N   ASP C  95      -7.346  95.457  65.527  1.00 33.37           N  
ANISOU 5742  N   ASP C  95     5676   3587   3414    218   1121    462       N  
ATOM   5743  CA  ASP C  95      -6.351  96.530  65.540  1.00 32.19           C  
ANISOU 5743  CA  ASP C  95     5481   3496   3252    268   1019    458       C  
ATOM   5744  C   ASP C  95      -6.465  97.372  66.824  1.00 31.72           C  
ANISOU 5744  C   ASP C  95     5434   3472   3143    306    997    461       C  
ATOM   5745  O   ASP C  95      -7.447  97.288  67.531  1.00 31.47           O  
ANISOU 5745  O   ASP C  95     5433   3426   3097    289   1053    463       O  
ATOM   5746  CB  ASP C  95      -6.492  97.379  64.281  1.00 33.23           C  
ANISOU 5746  CB  ASP C  95     5522   3662   3441    219    970    415       C  
ATOM   5747  CG  ASP C  95      -6.149  96.638  62.998  1.00 35.79           C  
ANISOU 5747  CG  ASP C  95     5831   3959   3807    193    977    411       C  
ATOM   5748  OD1 ASP C  95      -5.407  95.605  63.074  1.00 33.95           O  
ANISOU 5748  OD1 ASP C  95     5655   3689   3556    229    999    445       O  
ATOM   5749  OD2 ASP C  95      -6.638  97.090  61.930  1.00 35.34           O  
ANISOU 5749  OD2 ASP C  95     5711   3921   3793    147    962    375       O  
ATOM   5750  N   LEU C  96      -5.406  98.127  67.140  1.00 29.76           N  
ANISOU 5750  N   LEU C  96     5167   3273   2866    357    919    457       N  
ATOM   5751  CA  LEU C  96      -5.346  99.042  68.304  1.00 31.36           C  
ANISOU 5751  CA  LEU C  96     5376   3518   3019    392    885    450       C  
ATOM   5752  C   LEU C  96      -5.061 100.450  67.797  1.00 28.82           C  
ANISOU 5752  C   LEU C  96     4984   3241   2724    363    817    404       C  
ATOM   5753  O   LEU C  96      -4.166 100.611  66.980  1.00 28.82           O  
ANISOU 5753  O   LEU C  96     4943   3256   2748    357    774    389       O  
ATOM   5754  CB  LEU C  96      -4.195  98.659  69.239  1.00 31.90           C  
ANISOU 5754  CB  LEU C  96     5490   3616   3015    483    855    474       C  
ATOM   5755  CG  LEU C  96      -4.272  97.277  69.861  1.00 36.59           C  
ANISOU 5755  CG  LEU C  96     6180   4159   3561    540    926    528       C  
ATOM   5756  CD1 LEU C  96      -3.172  97.098  70.901  1.00 35.68           C  
ANISOU 5756  CD1 LEU C  96     6105   4094   3355    654    886    548       C  
ATOM   5757  CD2 LEU C  96      -5.636  97.073  70.498  1.00 42.73           C  
ANISOU 5757  CD2 LEU C  96     7010   4889   4335    506   1011    541       C  
ATOM   5758  N   LEU C  97      -5.747 101.446  68.355  1.00 27.82           N  
ANISOU 5758  N   LEU C  97     4852   3130   2586    350    814    383       N  
ATOM   5759  CA  LEU C  97      -5.410 102.847  68.161  1.00 27.62           C  
ANISOU 5759  CA  LEU C  97     4788   3138   2568    333    761    342       C  
ATOM   5760  C   LEU C  97      -4.652 103.362  69.383  1.00 27.32           C  
ANISOU 5760  C   LEU C  97     4770   3142   2466    375    721    329       C  
ATOM   5761  O   LEU C  97      -5.024 103.100  70.498  1.00 26.54           O  
ANISOU 5761  O   LEU C  97     4717   3047   2319    413    743    348       O  
ATOM   5762  CB  LEU C  97      -6.679 103.665  67.948  1.00 28.65           C  
ANISOU 5762  CB  LEU C  97     4907   3259   2719    300    787    324       C  
ATOM   5763  CG  LEU C  97      -7.293 103.635  66.557  1.00 30.29           C  
ANISOU 5763  CG  LEU C  97     5072   3451   2983    261    803    313       C  
ATOM   5764  CD1 LEU C  97      -8.520 104.519  66.527  1.00 31.85           C  
ANISOU 5764  CD1 LEU C  97     5259   3660   3182    254    824    293       C  
ATOM   5765  CD2 LEU C  97      -6.287 104.078  65.495  1.00 32.56           C  
ANISOU 5765  CD2 LEU C  97     5330   3740   3301    247    760    295       C  
ATOM   5766  N   HIS C  98      -3.548 104.065  69.123  1.00 27.81           N  
ANISOU 5766  N   HIS C  98     4796   3241   2528    366    666    290       N  
ATOM   5767  CA  HIS C  98      -2.914 104.943  70.095  1.00 29.69           C  
ANISOU 5767  CA  HIS C  98     5035   3530   2715    380    625    250       C  
ATOM   5768  C   HIS C  98      -3.937 106.012  70.508  1.00 27.26           C  
ANISOU 5768  C   HIS C  98     4752   3200   2402    357    647    234       C  
ATOM   5769  O   HIS C  98      -4.696 106.474  69.683  1.00 24.21           O  
ANISOU 5769  O   HIS C  98     4360   2777   2062    320    673    232       O  
ATOM   5770  CB  HIS C  98      -1.658 105.573  69.479  1.00 28.51           C  
ANISOU 5770  CB  HIS C  98     4830   3417   2582    346    577    198       C  
ATOM   5771  CG  HIS C  98      -0.837 106.340  70.462  1.00 32.28           C  
ANISOU 5771  CG  HIS C  98     5297   3963   3004    353    533    141       C  
ATOM   5772  ND1 HIS C  98      -1.213 107.587  70.935  1.00 33.90           N  
ANISOU 5772  ND1 HIS C  98     5469   4250   3161    399    485    120       N  
ATOM   5773  CD2 HIS C  98       0.333 106.043  71.069  1.00 28.40           C  
ANISOU 5773  CD2 HIS C  98     4821   3476   2493    320    530     94       C  
ATOM   5774  CE1 HIS C  98      -0.301 108.017  71.790  1.00 33.26           C  
ANISOU 5774  CE1 HIS C  98     5374   4230   3033    388    452     56       C  
ATOM   5775  NE2 HIS C  98       0.659 107.095  71.874  1.00 31.52           N  
ANISOU 5775  NE2 HIS C  98     5189   3955   2831    336    482     40       N  
ATOM   5776  N   GLU C  99      -3.909 106.420  71.771  1.00 28.61           N  
ANISOU 5776  N   GLU C  99     4953   3402   2512    387    635    219       N  
ATOM   5777  CA  GLU C  99      -4.904 107.370  72.308  1.00 31.78           C  
ANISOU 5777  CA  GLU C  99     5389   3785   2900    376    660    207       C  
ATOM   5778  C   GLU C  99      -4.870 108.743  71.607  1.00 29.67           C  
ANISOU 5778  C   GLU C  99     5111   3497   2663    322    656    159       C  
ATOM   5779  O   GLU C  99      -5.865 109.421  71.621  1.00 31.19           O  
ANISOU 5779  O   GLU C  99     5331   3659   2858    319    688    161       O  
ATOM   5780  CB  GLU C  99      -4.759 107.525  73.825  1.00 35.50           C  
ANISOU 5780  CB  GLU C  99     5898   4296   3293    423    645    198       C  
ATOM   5781  CG  GLU C  99      -3.507 108.236  74.305  1.00 40.07           C  
ANISOU 5781  CG  GLU C  99     6455   4936   3831    416    586    133       C  
ATOM   5782  CD  GLU C  99      -3.590 108.614  75.786  1.00 49.88           C  
ANISOU 5782  CD  GLU C  99     7740   6219   4994    458    575    114       C  
ATOM   5783  OE1 GLU C  99      -4.686 108.475  76.385  1.00 46.96           O  
ANISOU 5783  OE1 GLU C  99     7420   5816   4605    488    618    154       O  
ATOM   5784  OE2 GLU C  99      -2.563 109.044  76.347  1.00 63.17           O  
ANISOU 5784  OE2 GLU C  99     9400   7971   6631    460    524     54       O  
ATOM   5785  N   ARG C 100      -3.744 109.134  71.014  1.00 28.74           N  
ANISOU 5785  N   ARG C 100     4960   3394   2563    284    623    118       N  
ATOM   5786  CA  ARG C 100      -3.590 110.449  70.320  1.00 31.71           C  
ANISOU 5786  CA  ARG C 100     5344   3737   2966    228    634     70       C  
ATOM   5787  C   ARG C 100      -3.935 110.369  68.825  1.00 30.18           C  
ANISOU 5787  C   ARG C 100     5136   3496   2834    208    659     92       C  
ATOM   5788  O   ARG C 100      -3.902 111.392  68.158  1.00 25.71           O  
ANISOU 5788  O   ARG C 100     4592   2891   2285    174    679     64       O  
ATOM   5789  CB  ARG C 100      -2.160 110.976  70.451  1.00 31.88           C  
ANISOU 5789  CB  ARG C 100     5337   3801   2974    183    598      0       C  
ATOM   5790  CG  ARG C 100      -1.781 111.358  71.875  1.00 34.68           C  
ANISOU 5790  CG  ARG C 100     5704   4212   3260    195    570    -43       C  
ATOM   5791  CD  ARG C 100      -0.352 111.859  71.978  1.00 38.52           C  
ANISOU 5791  CD  ARG C 100     6144   4759   3732    141    534   -129       C  
ATOM   5792  NE  ARG C 100      -0.187 113.103  71.225  1.00 43.40           N  
ANISOU 5792  NE  ARG C 100     6784   5319   4384     57    573   -182       N  
ATOM   5793  CZ  ARG C 100      -0.550 114.310  71.658  1.00 44.78           C  
ANISOU 5793  CZ  ARG C 100     7023   5452   4538     22    606   -224       C  
ATOM   5794  NH1 ARG C 100      -0.835 114.507  72.933  1.00 47.04           N  
ANISOU 5794  NH1 ARG C 100     7337   5772   4764     52    591   -239       N  
ATOM   5795  NH2 ARG C 100      -0.639 115.317  70.812  1.00 43.89           N  
ANISOU 5795  NH2 ARG C 100     6957   5260   4458    -36    660   -248       N  
ATOM   5796  N   ALA C 101      -4.266 109.168  68.324  1.00 28.66           N  
ANISOU 5796  N   ALA C 101     4916   3304   2669    231    663    141       N  
ATOM   5797  CA  ALA C 101      -4.414 108.910  66.872  1.00 28.67           C  
ANISOU 5797  CA  ALA C 101     4892   3273   2724    214    677    157       C  
ATOM   5798  C   ALA C 101      -5.420 109.856  66.201  1.00 27.21           C  
ANISOU 5798  C   ALA C 101     4736   3049   2551    215    712    154       C  
ATOM   5799  O   ALA C 101      -5.046 110.534  65.257  1.00 28.26           O  
ANISOU 5799  O   ALA C 101     4877   3153   2706    192    720    134       O  
ATOM   5800  CB  ALA C 101      -4.790 107.473  66.601  1.00 27.73           C  
ANISOU 5800  CB  ALA C 101     4750   3160   2627    236    685    204       C  
ATOM   5801  N   LEU C 102      -6.674 109.889  66.661  1.00 25.71           N  
ANISOU 5801  N   LEU C 102     4564   2861   2343    248    738    173       N  
ATOM   5802  CA  LEU C 102      -7.691 110.623  65.908  1.00 26.73           C  
ANISOU 5802  CA  LEU C 102     4710   2970   2477    270    768    173       C  
ATOM   5803  C   LEU C 102      -7.380 112.130  65.961  1.00 27.43           C  
ANISOU 5803  C   LEU C 102     4860   3020   2539    265    781    139       C  
ATOM   5804  O   LEU C 102      -7.455 112.814  64.952  1.00 25.18           O  
ANISOU 5804  O   LEU C 102     4600   2701   2264    272    802    132       O  
ATOM   5805  CB  LEU C 102      -9.091 110.313  66.441  1.00 28.12           C  
ANISOU 5805  CB  LEU C 102     4878   3171   2633    308    794    192       C  
ATOM   5806  CG  LEU C 102      -9.516 108.846  66.350  1.00 29.17           C  
ANISOU 5806  CG  LEU C 102     4962   3330   2792    301    802    218       C  
ATOM   5807  CD1 LEU C 102     -10.933 108.656  66.859  1.00 28.94           C  
ANISOU 5807  CD1 LEU C 102     4920   3329   2744    325    839    224       C  
ATOM   5808  CD2 LEU C 102      -9.396 108.326  64.916  1.00 30.16           C  
ANISOU 5808  CD2 LEU C 102     5045   3451   2963    285    797    220       C  
ATOM   5809  N   GLU C 103      -6.945 112.617  67.117  1.00 26.96           N  
ANISOU 5809  N   GLU C 103     4832   2964   2445    251    774    114       N  
ATOM   5810  CA  GLU C 103      -6.744 114.047  67.325  1.00 29.98           C  
ANISOU 5810  CA  GLU C 103     5286   3305   2799    237    798     75       C  
ATOM   5811  C   GLU C 103      -5.558 114.526  66.484  1.00 27.59           C  
ANISOU 5811  C   GLU C 103     4992   2968   2522    179    802     40       C  
ATOM   5812  O   GLU C 103      -5.667 115.552  65.753  1.00 26.49           O  
ANISOU 5812  O   GLU C 103     4915   2768   2379    179    846     27       O  
ATOM   5813  CB  GLU C 103      -6.510 114.334  68.811  1.00 35.62           C  
ANISOU 5813  CB  GLU C 103     6024   4041   3467    229    785     49       C  
ATOM   5814  CG  GLU C 103      -6.278 115.805  69.127  1.00 43.01           C  
ANISOU 5814  CG  GLU C 103     7041   4929   4370    204    817      0       C  
ATOM   5815  CD  GLU C 103      -7.510 116.690  69.277  1.00 53.51           C  
ANISOU 5815  CD  GLU C 103     8444   6222   5665    263    864     13       C  
ATOM   5816  OE1 GLU C 103      -7.318 117.873  69.667  1.00 61.70           O  
ANISOU 5816  OE1 GLU C 103     9562   7212   6668    244    897    -27       O  
ATOM   5817  OE2 GLU C 103      -8.654 116.228  68.995  1.00 54.16           O  
ANISOU 5817  OE2 GLU C 103     8503   6324   5749    326    872     59       O  
ATOM   5818  N   ASP C 104      -4.434 113.808  66.612  1.00 26.84           N  
ANISOU 5818  N   ASP C 104     4839   2912   2447    136    762     24       N  
ATOM   5819  CA  ASP C 104      -3.188 114.152  65.947  1.00 27.88           C  
ANISOU 5819  CA  ASP C 104     4959   3028   2603     71    764    -18       C  
ATOM   5820  C   ASP C 104      -3.327 114.079  64.429  1.00 28.32           C  
ANISOU 5820  C   ASP C 104     5018   3042   2700     77    789      7       C  
ATOM   5821  O   ASP C 104      -2.838 114.971  63.720  1.00 28.06           O  
ANISOU 5821  O   ASP C 104     5030   2955   2676     39    829    -22       O  
ATOM   5822  CB  ASP C 104      -2.019 113.295  66.402  1.00 28.29           C  
ANISOU 5822  CB  ASP C 104     4937   3152   2661     42    712    -41       C  
ATOM   5823  CG  ASP C 104      -1.479 113.740  67.741  1.00 30.53           C  
ANISOU 5823  CG  ASP C 104     5223   3479   2896     18    691    -96       C  
ATOM   5824  OD1 ASP C 104      -2.152 114.552  68.405  1.00 34.89           O  
ANISOU 5824  OD1 ASP C 104     5838   4002   3413     28    716   -106       O  
ATOM   5825  OD2 ASP C 104      -0.415 113.258  68.116  1.00 33.54           O  
ANISOU 5825  OD2 ASP C 104     5543   3929   3269     -1    648   -130       O  
ATOM   5826  N   LEU C 105      -3.996 113.047  63.913  1.00 27.02           N  
ANISOU 5826  N   LEU C 105     4809   2898   2557    124    772     59       N  
ATOM   5827  CA  LEU C 105      -4.142 112.928  62.446  1.00 28.15           C  
ANISOU 5827  CA  LEU C 105     4949   3011   2733    136    791     81       C  
ATOM   5828  C   LEU C 105      -5.145 113.969  61.924  1.00 26.46           C  
ANISOU 5828  C   LEU C 105     4810   2748   2494    185    838     89       C  
ATOM   5829  O   LEU C 105      -4.938 114.558  60.875  1.00 26.36           O  
ANISOU 5829  O   LEU C 105     4840   2686   2488    186    872     85       O  
ATOM   5830  CB  LEU C 105      -4.563 111.505  62.060  1.00 27.72           C  
ANISOU 5830  CB  LEU C 105     4827   2998   2707    164    762    123       C  
ATOM   5831  CG  LEU C 105      -3.430 110.544  61.685  1.00 29.12           C  
ANISOU 5831  CG  LEU C 105     4946   3198   2918    130    732    122       C  
ATOM   5832  CD1 LEU C 105      -2.423 110.378  62.815  1.00 31.08           C  
ANISOU 5832  CD1 LEU C 105     5173   3487   3149    100    701     95       C  
ATOM   5833  CD2 LEU C 105      -4.014 109.201  61.309  1.00 28.30           C  
ANISOU 5833  CD2 LEU C 105     4797   3118   2836    158    719    163       C  
ATOM   5834  N   TYR C 106      -6.259 114.148  62.638  1.00 26.16           N  
ANISOU 5834  N   TYR C 106     4790   2726   2421    237    844    103       N  
ATOM   5835  CA  TYR C 106      -7.302 115.081  62.223  1.00 26.53           C  
ANISOU 5835  CA  TYR C 106     4904   2743   2433    306    886    113       C  
ATOM   5836  C   TYR C 106      -6.737 116.506  62.178  1.00 26.66           C  
ANISOU 5836  C   TYR C 106     5027   2678   2423    284    938     81       C  
ATOM   5837  O   TYR C 106      -6.859 117.205  61.169  1.00 29.69           O  
ANISOU 5837  O   TYR C 106     5477   3008   2794    318    983     87       O  
ATOM   5838  CB  TYR C 106      -8.506 115.066  63.176  1.00 28.39           C  
ANISOU 5838  CB  TYR C 106     5135   3018   2631    361    885    126       C  
ATOM   5839  CG  TYR C 106      -9.481 116.154  62.822  1.00 27.77           C  
ANISOU 5839  CG  TYR C 106     5132   2914   2504    444    929    132       C  
ATOM   5840  CD1 TYR C 106     -10.369 115.957  61.780  1.00 26.62           C  
ANISOU 5840  CD1 TYR C 106     4960   2800   2352    519    933    152       C  
ATOM   5841  CD2 TYR C 106      -9.414 117.416  63.416  1.00 28.99           C  
ANISOU 5841  CD2 TYR C 106     5389   3010   2614    452    971    112       C  
ATOM   5842  CE1 TYR C 106     -11.232 116.959  61.376  1.00 29.74           C  
ANISOU 5842  CE1 TYR C 106     5426   3182   2691    617    972    158       C  
ATOM   5843  CE2 TYR C 106     -10.272 118.428  63.026  1.00 28.56           C  
ANISOU 5843  CE2 TYR C 106     5419   2925   2507    544   1019    121       C  
ATOM   5844  CZ  TYR C 106     -11.171 118.199  61.996  1.00 28.56           C  
ANISOU 5844  CZ  TYR C 106     5389   2966   2495    634   1018    147       C  
ATOM   5845  OH  TYR C 106     -12.060 119.149  61.620  1.00 31.92           O  
ANISOU 5845  OH  TYR C 106     5893   3377   2855    747   1061    157       O  
ATOM   5846  N   ASN C 107      -6.050 116.894  63.249  1.00 27.08           N  
ANISOU 5846  N   ASN C 107     5099   2722   2465    222    937     42       N  
ATOM   5847  CA  ASN C 107      -5.524 118.265  63.390  1.00 29.74           C  
ANISOU 5847  CA  ASN C 107     5543   2979   2775    183    997     -1       C  
ATOM   5848  C   ASN C 107      -4.487 118.532  62.303  1.00 31.37           C  
ANISOU 5848  C   ASN C 107     5771   3134   3014    123   1030    -24       C  
ATOM   5849  O   ASN C 107      -4.518 119.608  61.694  1.00 32.18           O  
ANISOU 5849  O   ASN C 107     5985   3149   3094    133   1104    -32       O  
ATOM   5850  CB  ASN C 107      -4.932 118.538  64.774  1.00 30.81           C  
ANISOU 5850  CB  ASN C 107     5680   3132   2893    117    983    -52       C  
ATOM   5851  CG  ASN C 107      -5.991 118.716  65.841  1.00 32.19           C  
ANISOU 5851  CG  ASN C 107     5879   3329   3022    179    978    -36       C  
ATOM   5852  OD1 ASN C 107      -7.161 118.922  65.533  1.00 34.66           O  
ANISOU 5852  OD1 ASN C 107     6225   3631   3310    268   1000      4       O  
ATOM   5853  ND2 ASN C 107      -5.595 118.624  67.097  1.00 31.18           N  
ANISOU 5853  ND2 ASN C 107     5730   3240   2877    139    949    -70       N  
ATOM   5854  N   TYR C 108      -3.617 117.548  62.039  1.00 29.36           N  
ANISOU 5854  N   TYR C 108     5418   2929   2807     70    983    -29       N  
ATOM   5855  CA  TYR C 108      -2.613 117.692  61.000  1.00 30.01           C  
ANISOU 5855  CA  TYR C 108     5506   2972   2922     12   1013    -51       C  
ATOM   5856  C   TYR C 108      -3.266 117.777  59.615  1.00 30.42           C  
ANISOU 5856  C   TYR C 108     5603   2979   2974     87   1046     -2       C  
ATOM   5857  O   TYR C 108      -2.839 118.575  58.759  1.00 32.96           O  
ANISOU 5857  O   TYR C 108     6009   3221   3293     67   1115    -15       O  
ATOM   5858  CB  TYR C 108      -1.609 116.551  61.037  1.00 29.55           C  
ANISOU 5858  CB  TYR C 108     5329   2989   2909    -42    951    -63       C  
ATOM   5859  CG  TYR C 108      -0.321 116.807  60.298  1.00 31.24           C  
ANISOU 5859  CG  TYR C 108     5537   3177   3155   -128    983   -109       C  
ATOM   5860  CD1 TYR C 108       0.569 117.776  60.724  1.00 32.39           C  
ANISOU 5860  CD1 TYR C 108     5722   3291   3291   -223   1029   -186       C  
ATOM   5861  CD2 TYR C 108       0.036 116.023  59.207  1.00 31.43           C  
ANISOU 5861  CD2 TYR C 108     5509   3214   3218   -120    968    -81       C  
ATOM   5862  CE1 TYR C 108       1.775 117.984  60.064  1.00 34.67           C  
ANISOU 5862  CE1 TYR C 108     5996   3566   3612   -313   1065   -237       C  
ATOM   5863  CE2 TYR C 108       1.249 116.190  58.568  1.00 32.06           C  
ANISOU 5863  CE2 TYR C 108     5574   3279   3328   -200    997   -124       C  
ATOM   5864  CZ  TYR C 108       2.109 117.195  58.976  1.00 32.97           C  
ANISOU 5864  CZ  TYR C 108     5726   3365   3435   -299   1050   -203       C  
ATOM   5865  OH  TYR C 108       3.284 117.366  58.302  1.00 35.30           O  
ANISOU 5865  OH  TYR C 108     6001   3649   3762   -385   1088   -253       O  
ATOM   5866  N   GLY C 109      -4.320 116.996  59.396  1.00 27.63           N  
ANISOU 5866  N   GLY C 109     5200   2678   2617    173   1005     48       N  
ATOM   5867  CA  GLY C 109      -5.094 117.092  58.142  1.00 28.88           C  
ANISOU 5867  CA  GLY C 109     5394   2817   2762    262   1029     88       C  
ATOM   5868  C   GLY C 109      -5.747 118.458  57.967  1.00 30.16           C  
ANISOU 5868  C   GLY C 109     5693   2904   2863    331   1102     92       C  
ATOM   5869  O   GLY C 109      -5.756 119.049  56.884  1.00 29.51           O  
ANISOU 5869  O   GLY C 109     5692   2759   2759    375   1156    105       O  
ATOM   5870  N   LYS C 110      -6.303 118.965  59.065  1.00 31.64           N  
ANISOU 5870  N   LYS C 110     5915   3093   3013    349   1108     82       N  
ATOM   5871  CA  LYS C 110      -7.038 120.199  59.048  1.00 36.15           C  
ANISOU 5871  CA  LYS C 110     6617   3599   3517    431   1176     90       C  
ATOM   5872  C   LYS C 110      -6.078 121.356  58.745  1.00 35.51           C  
ANISOU 5872  C   LYS C 110     6670   3396   3426    367   1267     55       C  
ATOM   5873  O   LYS C 110      -6.379 122.208  57.901  1.00 35.82           O  
ANISOU 5873  O   LYS C 110     6833   3356   3420    440   1341     74       O  
ATOM   5874  CB  LYS C 110      -7.778 120.373  60.376  1.00 37.21           C  
ANISOU 5874  CB  LYS C 110     6748   3770   3619    456   1158     85       C  
ATOM   5875  CG  LYS C 110      -8.923 121.362  60.313  1.00 44.85           C  
ANISOU 5875  CG  LYS C 110     7824   4705   4509    583   1211    107       C  
ATOM   5876  CD  LYS C 110     -10.026 120.927  59.362  1.00 48.09           C  
ANISOU 5876  CD  LYS C 110     8190   5185   4896    713   1187    149       C  
ATOM   5877  CE  LYS C 110     -11.287 121.737  59.551  1.00 48.92           C  
ANISOU 5877  CE  LYS C 110     8369   5298   4917    854   1221    167       C  
ATOM   5878  NZ  LYS C 110     -12.184 121.620  58.380  1.00 54.42           N  
ANISOU 5878  NZ  LYS C 110     9051   6052   5574    991   1216    197       N  
ATOM   5879  N   GLU C 111      -4.923 121.362  59.418  1.00 34.51           N  
ANISOU 5879  N   GLU C 111     6517   3257   3336    231   1265      0       N  
ATOM   5880  CA  GLU C 111      -3.891 122.363  59.203  1.00 37.14           C  
ANISOU 5880  CA  GLU C 111     6956   3484   3671    137   1355    -51       C  
ATOM   5881  C   GLU C 111      -3.437 122.377  57.741  1.00 35.43           C  
ANISOU 5881  C   GLU C 111     6775   3213   3471    141   1401    -33       C  
ATOM   5882  O   GLU C 111      -3.112 123.443  57.218  1.00 33.95           O  
ANISOU 5882  O   GLU C 111     6733   2908   3257    125   1508    -50       O  
ATOM   5883  CB  GLU C 111      -2.646 122.109  60.051  1.00 40.34           C  
ANISOU 5883  CB  GLU C 111     7281   3926   4120    -13   1327   -124       C  
ATOM   5884  CG  GLU C 111      -2.833 122.385  61.529  1.00 49.54           C  
ANISOU 5884  CG  GLU C 111     8443   5121   5258    -38   1304   -160       C  
ATOM   5885  CD  GLU C 111      -1.802 121.714  62.430  1.00 58.48           C  
ANISOU 5885  CD  GLU C 111     9448   6344   6427   -148   1236   -220       C  
ATOM   5886  OE1 GLU C 111      -2.008 121.709  63.669  1.00 65.30           O  
ANISOU 5886  OE1 GLU C 111    10288   7255   7265   -152   1199   -242       O  
ATOM   5887  OE2 GLU C 111      -0.780 121.207  61.897  1.00 66.58           O  
ANISOU 5887  OE2 GLU C 111    10399   7400   7499   -220   1220   -245       O  
ATOM   5888  N   ASN C 112      -3.320 121.198  57.119  1.00 31.26           N  
ANISOU 5888  N   ASN C 112     6122   2764   2988    153   1328     -4       N  
ATOM   5889  CA  ASN C 112      -2.725 121.077  55.795  1.00 31.01           C  
ANISOU 5889  CA  ASN C 112     6106   2693   2980    141   1363      6       C  
ATOM   5890  C   ASN C 112      -3.766 120.836  54.697  1.00 29.27           C  
ANISOU 5890  C   ASN C 112     5907   2486   2727    290   1354     73       C  
ATOM   5891  O   ASN C 112      -3.404 120.551  53.551  1.00 31.14           O  
ANISOU 5891  O   ASN C 112     6142   2707   2981    299   1368     90       O  
ATOM   5892  CB  ASN C 112      -1.643 119.999  55.794  1.00 34.57           C  
ANISOU 5892  CB  ASN C 112     6412   3217   3503     39   1299    -20       C  
ATOM   5893  CG  ASN C 112      -0.494 120.404  56.686  1.00 36.98           C  
ANISOU 5893  CG  ASN C 112     6704   3514   3830   -103   1320   -100       C  
ATOM   5894  OD1 ASN C 112       0.231 121.335  56.356  1.00 37.89           O  
ANISOU 5894  OD1 ASN C 112     6913   3538   3942   -179   1415   -145       O  
ATOM   5895  ND2 ASN C 112      -0.365 119.759  57.833  1.00 37.84           N  
ANISOU 5895  ND2 ASN C 112     6705   3717   3953   -137   1240   -122       N  
ATOM   5896  N   ASN C 113      -5.043 121.013  55.000  1.00 28.51           N  
ANISOU 5896  N   ASN C 113     5833   2420   2577    408   1337    105       N  
ATOM   5897  CA  ASN C 113      -6.120 120.824  54.009  1.00 31.45           C  
ANISOU 5897  CA  ASN C 113     6213   2829   2905    560   1324    157       C  
ATOM   5898  C   ASN C 113      -5.975 119.472  53.295  1.00 29.22           C  
ANISOU 5898  C   ASN C 113     5789   2635   2677    549   1246    171       C  
ATOM   5899  O   ASN C 113      -6.158 119.376  52.085  1.00 29.85           O  
ANISOU 5899  O   ASN C 113     5889   2711   2738    622   1258    197       O  
ATOM   5900  CB  ASN C 113      -6.163 121.937  52.968  1.00 34.91           C  
ANISOU 5900  CB  ASN C 113     6826   3155   3281    643   1429    176       C  
ATOM   5901  CG  ASN C 113      -7.446 121.903  52.168  1.00 39.38           C  
ANISOU 5901  CG  ASN C 113     7406   3778   3777    828   1411    223       C  
ATOM   5902  OD1 ASN C 113      -8.476 121.447  52.674  1.00 42.10           O  
ANISOU 5902  OD1 ASN C 113     7662   4228   4104    896   1343    231       O  
ATOM   5903  ND2 ASN C 113      -7.387 122.372  50.931  1.00 39.28           N  
ANISOU 5903  ND2 ASN C 113     7499   3703   3719    910   1473    249       N  
ATOM   5904  N   SER C 114      -5.747 118.432  54.099  1.00 29.99           N  
ANISOU 5904  N   SER C 114     5750   2814   2831    471   1168    156       N  
ATOM   5905  CA  SER C 114      -5.415 117.070  53.609  1.00 28.83           C  
ANISOU 5905  CA  SER C 114     5472   2739   2743    436   1100    164       C  
ATOM   5906  C   SER C 114      -6.674 116.310  53.180  1.00 27.06           C  
ANISOU 5906  C   SER C 114     5173   2608   2499    538   1047    191       C  
ATOM   5907  O   SER C 114      -7.677 116.261  53.911  1.00 27.03           O  
ANISOU 5907  O   SER C 114     5140   2659   2467    587   1022    194       O  
ATOM   5908  CB  SER C 114      -4.690 116.300  54.671  1.00 27.54           C  
ANISOU 5908  CB  SER C 114     5211   2619   2633    327   1048    139       C  
ATOM   5909  OG  SER C 114      -3.524 117.011  55.082  1.00 31.11           O  
ANISOU 5909  OG  SER C 114     5714   3005   3098    228   1094     98       O  
ATOM   5910  N   ASP C 115      -6.581 115.683  52.009  1.00 26.60           N  
ANISOU 5910  N   ASP C 115     5077   2571   2455    561   1030    204       N  
ATOM   5911  CA  ASP C 115      -7.558 114.724  51.536  1.00 25.63           C  
ANISOU 5911  CA  ASP C 115     4858   2549   2329    625    974    213       C  
ATOM   5912  C   ASP C 115      -7.334 113.378  52.229  1.00 23.76           C  
ANISOU 5912  C   ASP C 115     4496   2373   2156    537    914    204       C  
ATOM   5913  O   ASP C 115      -8.258 112.591  52.355  1.00 23.60           O  
ANISOU 5913  O   ASP C 115     4394   2437   2136    563    875    201       O  
ATOM   5914  CB  ASP C 115      -7.460 114.544  50.028  1.00 26.56           C  
ANISOU 5914  CB  ASP C 115     4988   2665   2438    678    981    225       C  
ATOM   5915  CG  ASP C 115      -7.682 115.815  49.220  1.00 26.91           C  
ANISOU 5915  CG  ASP C 115     5171   2644   2407    785   1049    241       C  
ATOM   5916  OD1 ASP C 115      -8.730 116.430  49.408  1.00 29.30           O  
ANISOU 5916  OD1 ASP C 115     5512   2975   2643    891   1059    246       O  
ATOM   5917  OD2 ASP C 115      -6.803 116.165  48.411  1.00 27.06           O  
ANISOU 5917  OD2 ASP C 115     5264   2584   2433    765   1097    248       O  
ATOM   5918  N   LEU C 116      -6.103 113.134  52.689  1.00 23.37           N  
ANISOU 5918  N   LEU C 116     4437   2285   2156    434    912    195       N  
ATOM   5919  CA  LEU C 116      -5.680 111.862  53.215  1.00 23.96           C  
ANISOU 5919  CA  LEU C 116     4413   2405   2283    363    863    192       C  
ATOM   5920  C   LEU C 116      -4.568 112.115  54.233  1.00 25.15           C  
ANISOU 5920  C   LEU C 116     4576   2524   2456    278    868    174       C  
ATOM   5921  O   LEU C 116      -3.638 112.877  53.924  1.00 25.23           O  
ANISOU 5921  O   LEU C 116     4642   2473   2469    240    907    158       O  
ATOM   5922  CB  LEU C 116      -5.150 111.032  52.039  1.00 25.69           C  
ANISOU 5922  CB  LEU C 116     4593   2630   2538    350    850    199       C  
ATOM   5923  CG  LEU C 116      -4.757 109.597  52.353  1.00 25.98           C  
ANISOU 5923  CG  LEU C 116     4538   2708   2622    294    807    201       C  
ATOM   5924  CD1 LEU C 116      -5.998 108.767  52.662  1.00 27.38           C  
ANISOU 5924  CD1 LEU C 116     4655   2952   2793    322    781    202       C  
ATOM   5925  CD2 LEU C 116      -3.965 108.995  51.200  1.00 26.73           C  
ANISOU 5925  CD2 LEU C 116     4615   2790   2750    277    804    206       C  
ATOM   5926  N   ILE C 117      -4.684 111.522  55.429  1.00 22.81           N  
ANISOU 5926  N   ILE C 117     4228   2269   2168    250    834    171       N  
ATOM   5927  CA  ILE C 117      -3.593 111.533  56.438  1.00 23.66           C  
ANISOU 5927  CA  ILE C 117     4325   2374   2291    177    823    149       C  
ATOM   5928  C   ILE C 117      -3.227 110.084  56.750  1.00 24.09           C  
ANISOU 5928  C   ILE C 117     4295   2480   2376    154    777    161       C  
ATOM   5929  O   ILE C 117      -4.127 109.285  57.051  1.00 23.76           O  
ANISOU 5929  O   ILE C 117     4219   2475   2332    183    759    181       O  
ATOM   5930  CB  ILE C 117      -3.952 112.297  57.733  1.00 23.74           C  
ANISOU 5930  CB  ILE C 117     4373   2380   2264    176    832    133       C  
ATOM   5931  CG1 ILE C 117      -4.681 113.610  57.442  1.00 25.49           C  
ANISOU 5931  CG1 ILE C 117     4689   2551   2442    227    883    131       C  
ATOM   5932  CG2 ILE C 117      -2.693 112.541  58.548  1.00 22.31           C  
ANISOU 5932  CG2 ILE C 117     4187   2199   2091    101    826     94       C  
ATOM   5933  CD1 ILE C 117      -6.178 113.503  57.393  1.00 26.46           C  
ANISOU 5933  CD1 ILE C 117     4806   2711   2535    314    878    156       C  
ATOM   5934  N   ILE C 118      -1.916 109.795  56.715  1.00 24.19           N  
ANISOU 5934  N   ILE C 118     4280   2496   2414    103    765    145       N  
ATOM   5935  CA  ILE C 118      -1.359 108.474  56.959  1.00 25.77           C  
ANISOU 5935  CA  ILE C 118     4415   2740   2636     92    727    157       C  
ATOM   5936  C   ILE C 118      -0.495 108.539  58.217  1.00 26.73           C  
ANISOU 5936  C   ILE C 118     4518   2897   2741     62    705    130       C  
ATOM   5937  O   ILE C 118       0.483 109.268  58.261  1.00 26.92           O  
ANISOU 5937  O   ILE C 118     4545   2918   2765     16    713     89       O  
ATOM   5938  CB  ILE C 118      -0.518 107.989  55.774  1.00 28.17           C  
ANISOU 5938  CB  ILE C 118     4693   3035   2974     77    728    160       C  
ATOM   5939  CG1 ILE C 118      -1.308 108.039  54.460  1.00 31.14           C  
ANISOU 5939  CG1 ILE C 118     5090   3381   3357    112    750    179       C  
ATOM   5940  CG2 ILE C 118       0.033 106.589  56.069  1.00 26.89           C  
ANISOU 5940  CG2 ILE C 118     4474   2916   2826     81    693    177       C  
ATOM   5941  CD1 ILE C 118      -0.439 108.123  53.226  1.00 33.01           C  
ANISOU 5941  CD1 ILE C 118     5331   3591   3619     94    767    174       C  
ATOM   5942  N   GLY C 119      -0.858 107.754  59.229  1.00 24.52           N  
ANISOU 5942  N   GLY C 119     4220   2654   2443     88    679    149       N  
ATOM   5943  CA  GLY C 119      -0.066 107.700  60.432  1.00 24.16           C  
ANISOU 5943  CA  GLY C 119     4154   2655   2370     78    651    126       C  
ATOM   5944  C   GLY C 119       0.901 106.536  60.401  1.00 24.45           C  
ANISOU 5944  C   GLY C 119     4140   2736   2413     91    621    135       C  
ATOM   5945  O   GLY C 119       0.561 105.437  59.954  1.00 25.21           O  
ANISOU 5945  O   GLY C 119     4228   2823   2525    121    622    177       O  
ATOM   5946  N   LYS C 120       2.084 106.745  60.970  1.00 24.67           N  
ANISOU 5946  N   LYS C 120     4132   2819   2422     73    595     93       N  
ATOM   5947  CA  LYS C 120       3.015 105.682  61.253  1.00 23.78           C  
ANISOU 5947  CA  LYS C 120     3971   2769   2294    109    560     99       C  
ATOM   5948  C   LYS C 120       2.333 104.624  62.139  1.00 24.67           C  
ANISOU 5948  C   LYS C 120     4109   2889   2372    178    552    151       C  
ATOM   5949  O   LYS C 120       1.575 104.938  63.051  1.00 26.46           O  
ANISOU 5949  O   LYS C 120     4371   3109   2571    189    557    156       O  
ATOM   5950  CB  LYS C 120       4.237 106.267  61.951  1.00 25.54           C  
ANISOU 5950  CB  LYS C 120     4145   3071   2486     83    530     29       C  
ATOM   5951  CG  LYS C 120       5.421 105.329  62.019  1.00 29.39           C  
ANISOU 5951  CG  LYS C 120     4568   3643   2956    125    492     22       C  
ATOM   5952  CD  LYS C 120       6.641 105.906  62.694  1.00 32.58           C  
ANISOU 5952  CD  LYS C 120     4903   4150   3323     99    458    -61       C  
ATOM   5953  CE  LYS C 120       6.386 106.283  64.133  1.00 35.05           C  
ANISOU 5953  CE  LYS C 120     5232   4508   3578    120    433    -86       C  
ATOM   5954  NZ  LYS C 120       7.587 106.892  64.749  1.00 37.59           N  
ANISOU 5954  NZ  LYS C 120     5476   4944   3862     86    399   -184       N  
ATOM   5955  N   TYR C 121       2.651 103.357  61.885  1.00 24.84           N  
ANISOU 5955  N   TYR C 121     4121   2920   2394    225    546    188       N  
ATOM   5956  CA  TYR C 121       2.079 102.240  62.611  1.00 26.53           C  
ANISOU 5956  CA  TYR C 121     4377   3125   2575    288    556    240       C  
ATOM   5957  C   TYR C 121       3.061 101.072  62.604  1.00 26.10           C  
ANISOU 5957  C   TYR C 121     4308   3110   2497    352    540    261       C  
ATOM   5958  O   TYR C 121       4.047 101.044  61.850  1.00 23.95           O  
ANISOU 5958  O   TYR C 121     3987   2868   2243    344    522    240       O  
ATOM   5959  CB  TYR C 121       0.773 101.788  61.962  1.00 27.59           C  
ANISOU 5959  CB  TYR C 121     4550   3183   2747    271    603    280       C  
ATOM   5960  CG  TYR C 121       0.952 101.101  60.642  1.00 28.52           C  
ANISOU 5960  CG  TYR C 121     4655   3270   2910    261    617    296       C  
ATOM   5961  CD1 TYR C 121       0.982 101.827  59.459  1.00 29.49           C  
ANISOU 5961  CD1 TYR C 121     4753   3373   3078    212    619    272       C  
ATOM   5962  CD2 TYR C 121       1.084  99.721  60.572  1.00 28.82           C  
ANISOU 5962  CD2 TYR C 121     4717   3292   2939    304    635    335       C  
ATOM   5963  CE1 TYR C 121       1.148 101.199  58.236  1.00 28.99           C  
ANISOU 5963  CE1 TYR C 121     4679   3283   3051    207    632    285       C  
ATOM   5964  CE2 TYR C 121       1.274  99.079  59.356  1.00 31.67           C  
ANISOU 5964  CE2 TYR C 121     5070   3623   3339    294    650    347       C  
ATOM   5965  CZ  TYR C 121       1.278  99.819  58.186  1.00 31.01           C  
ANISOU 5965  CZ  TYR C 121     4953   3528   3301    244    645    321       C  
ATOM   5966  OH  TYR C 121       1.431  99.164  57.000  1.00 35.23           O  
ANISOU 5966  OH  TYR C 121     5482   4034   3869    238    659    332       O  
ATOM   5967  N   GLY C 122       2.734 100.085  63.430  1.00 24.60           N  
ANISOU 5967  N   GLY C 122     4171   2913   2262    421    555    306       N  
ATOM   5968  CA  GLY C 122       3.479  98.877  63.533  1.00 25.19           C  
ANISOU 5968  CA  GLY C 122     4259   3010   2298    504    552    339       C  
ATOM   5969  C   GLY C 122       2.568  97.662  63.673  1.00 26.31           C  
ANISOU 5969  C   GLY C 122     4490   3072   2432    538    615    403       C  
ATOM   5970  O   GLY C 122       1.344  97.749  63.617  1.00 24.66           O  
ANISOU 5970  O   GLY C 122     4315   2799   2253    487    658    415       O  
ATOM   5971  N   VAL C 123       3.225  96.514  63.805  1.00 26.81           N  
ANISOU 5971  N   VAL C 123     4590   3142   2452    625    624    440       N  
ATOM   5972  CA  VAL C 123       2.606  95.213  63.804  1.00 28.61           C  
ANISOU 5972  CA  VAL C 123     4915   3285   2670    659    696    498       C  
ATOM   5973  C   VAL C 123       2.692  94.606  65.210  1.00 28.62           C  
ANISOU 5973  C   VAL C 123     4996   3301   2578    766    713    536       C  
ATOM   5974  O   VAL C 123       3.690  94.768  65.925  1.00 28.48           O  
ANISOU 5974  O   VAL C 123     4950   3377   2491    853    658    523       O  
ATOM   5975  CB  VAL C 123       3.298  94.330  62.749  1.00 31.10           C  
ANISOU 5975  CB  VAL C 123     5231   3580   3004    685    708    516       C  
ATOM   5976  CG1 VAL C 123       2.845  92.894  62.831  1.00 34.83           C  
ANISOU 5976  CG1 VAL C 123     5820   3962   3452    730    791    574       C  
ATOM   5977  CG2 VAL C 123       3.066  94.872  61.345  1.00 29.56           C  
ANISOU 5977  CG2 VAL C 123     4972   3361   2897    582    701    484       C  
ATOM   5978  N   GLU C 124       1.647  93.863  65.587  1.00 28.72           N  
ANISOU 5978  N   GLU C 124     5107   3221   2582    761    796    578       N  
ATOM   5979  CA  GLU C 124       1.598  93.203  66.879  1.00 29.17           C  
ANISOU 5979  CA  GLU C 124     5265   3269   2548    863    833    623       C  
ATOM   5980  C   GLU C 124       2.865  92.381  67.084  1.00 27.31           C  
ANISOU 5980  C   GLU C 124     5062   3081   2233   1005    813    652       C  
ATOM   5981  O   GLU C 124       3.324  91.755  66.168  1.00 26.62           O  
ANISOU 5981  O   GLU C 124     4974   2968   2169   1014    825    663       O  
ATOM   5982  CB  GLU C 124       0.355  92.322  66.961  1.00 32.47           C  
ANISOU 5982  CB  GLU C 124     5792   3562   2980    822    948    662       C  
ATOM   5983  CG  GLU C 124      -0.897  93.093  67.288  1.00 34.04           C  
ANISOU 5983  CG  GLU C 124     5972   3743   3218    725    968    637       C  
ATOM   5984  CD  GLU C 124      -1.099  93.432  68.752  1.00 37.70           C  
ANISOU 5984  CD  GLU C 124     6479   4236   3607    784    967    649       C  
ATOM   5985  OE1 GLU C 124      -0.290  92.972  69.598  1.00 41.42           O  
ANISOU 5985  OE1 GLU C 124     7008   4742   3987    912    955    682       O  
ATOM   5986  OE2 GLU C 124      -2.074  94.167  69.044  1.00 39.31           O  
ANISOU 5986  OE2 GLU C 124     6659   4435   3841    710    977    626       O  
ATOM   5987  N   GLY C 125       3.442  92.449  68.279  1.00 26.42           N  
ANISOU 5987  N   GLY C 125     4968   3046   2021   1122    777    659       N  
ATOM   5988  CA  GLY C 125       4.579  91.665  68.640  1.00 28.79           C  
ANISOU 5988  CA  GLY C 125     5304   3407   2225   1283    758    688       C  
ATOM   5989  C   GLY C 125       5.866  92.464  68.637  1.00 29.70           C  
ANISOU 5989  C   GLY C 125     5280   3687   2316   1322    642    624       C  
ATOM   5990  O   GLY C 125       6.781  92.234  69.469  1.00 29.87           O  
ANISOU 5990  O   GLY C 125     5303   3817   2229   1471    597    624       O  
ATOM   5991  N   LYS C 126       5.938  93.399  67.697  1.00 29.96           N  
ANISOU 5991  N   LYS C 126     5194   3743   2445   1192    598    564       N  
ATOM   5992  CA  LYS C 126       7.190  93.998  67.293  1.00 33.89           C  
ANISOU 5992  CA  LYS C 126     5558   4373   2943   1199    511    500       C  
ATOM   5993  C   LYS C 126       7.615  95.101  68.264  1.00 32.84           C  
ANISOU 5993  C   LYS C 126     5342   4370   2763   1202    434    430       C  
ATOM   5994  O   LYS C 126       8.786  95.282  68.493  1.00 34.26           O  
ANISOU 5994  O   LYS C 126     5436   4691   2887   1271    366    381       O  
ATOM   5995  CB  LYS C 126       7.030  94.585  65.897  1.00 35.14           C  
ANISOU 5995  CB  LYS C 126     5642   4488   3221   1053    511    465       C  
ATOM   5996  CG  LYS C 126       6.788  93.562  64.805  1.00 40.20           C  
ANISOU 5996  CG  LYS C 126     6342   5023   3909   1045    574    516       C  
ATOM   5997  CD  LYS C 126       7.930  92.604  64.625  1.00 44.31           C  
ANISOU 5997  CD  LYS C 126     6869   5596   4368   1176    563    539       C  
ATOM   5998  CE  LYS C 126       8.173  92.246  63.177  1.00 52.08           C  
ANISOU 5998  CE  LYS C 126     7829   6532   5425   1126    583    542       C  
ATOM   5999  NZ  LYS C 126       9.488  91.580  63.012  1.00 59.75           N  
ANISOU 5999  NZ  LYS C 126     8774   7592   6335   1255    554    546       N  
ATOM   6000  N   GLY C 127       6.643  95.848  68.784  1.00 31.04           N  
ANISOU 6000  N   GLY C 127     5136   4097   2560   1122    448    420       N  
ATOM   6001  CA  GLY C 127       6.894  96.954  69.679  1.00 33.30           C  
ANISOU 6001  CA  GLY C 127     5356   4487   2809   1106    386    351       C  
ATOM   6002  C   GLY C 127       7.491  98.169  68.960  1.00 35.04           C  
ANISOU 6002  C   GLY C 127     5442   4773   3097    985    333    259       C  
ATOM   6003  O   GLY C 127       8.011  99.055  69.590  1.00 35.28           O  
ANISOU 6003  O   GLY C 127     5400   4910   3093    971    278    185       O  
ATOM   6004  N   ARG C 128       7.448  98.184  67.626  1.00 35.28           N  
ANISOU 6004  N   ARG C 128     5445   4739   3220    899    357    262       N  
ATOM   6005  CA  ARG C 128       8.021  99.286  66.846  1.00 36.57           C  
ANISOU 6005  CA  ARG C 128     5499   4948   3448    785    325    181       C  
ATOM   6006  C   ARG C 128       7.260  99.384  65.527  1.00 32.80           C  
ANISOU 6006  C   ARG C 128     5044   4341   3075    681    378    209       C  
ATOM   6007  O   ARG C 128       6.556  98.465  65.163  1.00 30.45           O  
ANISOU 6007  O   ARG C 128     4824   3948   2796    706    427    280       O  
ATOM   6008  CB  ARG C 128       9.531  99.098  66.672  1.00 39.95           C  
ANISOU 6008  CB  ARG C 128     5826   5516   3837    843    271    128       C  
ATOM   6009  CG  ARG C 128       9.951  97.878  65.865  1.00 47.48           C  
ANISOU 6009  CG  ARG C 128     6799   6446   4792    920    291    185       C  
ATOM   6010  CD  ARG C 128      11.468  97.741  65.763  1.00 53.25           C  
ANISOU 6010  CD  ARG C 128     7418   7337   5475    987    234    126       C  
ATOM   6011  NE  ARG C 128      12.094  98.928  65.185  1.00 60.14           N  
ANISOU 6011  NE  ARG C 128     8169   8273   6407    856    208     27       N  
ATOM   6012  CZ  ARG C 128      13.403  99.207  65.187  1.00 63.07           C  
ANISOU 6012  CZ  ARG C 128     8411   8805   6745    869    157    -60       C  
ATOM   6013  NH1 ARG C 128      14.282  98.372  65.718  1.00 57.70           N  
ANISOU 6013  NH1 ARG C 128     7697   8257   5968   1025    113    -60       N  
ATOM   6014  NH2 ARG C 128      13.829 100.335  64.642  1.00 63.39           N  
ANISOU 6014  NH2 ARG C 128     8359   8876   6848    727    155   -151       N  
ATOM   6015  N   SER C 129       7.414 100.517  64.830  1.00 33.16           N  
ANISOU 6015  N   SER C 129     5026   4387   3185    566    371    148       N  
ATOM   6016  CA  SER C 129       6.675 100.800  63.596  1.00 30.58           C  
ANISOU 6016  CA  SER C 129     4721   3949   2948    473    417    167       C  
ATOM   6017  C   SER C 129       7.215  99.960  62.434  1.00 27.91           C  
ANISOU 6017  C   SER C 129     4366   3595   2643    492    429    193       C  
ATOM   6018  O   SER C 129       8.320  99.488  62.491  1.00 27.56           O  
ANISOU 6018  O   SER C 129     4272   3638   2562    555    397    177       O  
ATOM   6019  CB  SER C 129       6.766 102.253  63.305  1.00 34.86           C  
ANISOU 6019  CB  SER C 129     5218   4496   3530    364    413     96       C  
ATOM   6020  OG  SER C 129       6.145 102.997  64.345  1.00 39.58           O  
ANISOU 6020  OG  SER C 129     5846   5094   4098    348    410     78       O  
ATOM   6021  N   VAL C 130       6.414  99.758  61.385  1.00 26.96           N  
ANISOU 6021  N   VAL C 130     4285   3370   2586    444    473    230       N  
ATOM   6022  CA  VAL C 130       6.868  99.023  60.207  1.00 28.79           C  
ANISOU 6022  CA  VAL C 130     4506   3579   2853    454    488    251       C  
ATOM   6023  C   VAL C 130       7.994  99.816  59.534  1.00 33.61           C  
ANISOU 6023  C   VAL C 130     5026   4254   3489    403    463    186       C  
ATOM   6024  O   VAL C 130       8.082 101.037  59.636  1.00 33.05           O  
ANISOU 6024  O   VAL C 130     4919   4202   3433    327    456    129       O  
ATOM   6025  CB  VAL C 130       5.742  98.711  59.196  1.00 30.37           C  
ANISOU 6025  CB  VAL C 130     4761   3664   3113    408    538    293       C  
ATOM   6026  CG1 VAL C 130       4.747  97.704  59.746  1.00 30.62           C  
ANISOU 6026  CG1 VAL C 130     4876   3634   3121    452    576    350       C  
ATOM   6027  CG2 VAL C 130       5.013  99.969  58.723  1.00 32.17           C  
ANISOU 6027  CG2 VAL C 130     4981   3851   3389    314    550    262       C  
ATOM   6028  N   PRO C 131       8.932  99.132  58.857  1.00 34.39           N  
ANISOU 6028  N   PRO C 131     5086   4389   3589    442    457    189       N  
ATOM   6029  CA  PRO C 131      10.085  99.812  58.270  1.00 35.91           C  
ANISOU 6029  CA  PRO C 131     5186   4655   3803    393    440    121       C  
ATOM   6030  C   PRO C 131       9.836 100.368  56.858  1.00 35.43           C  
ANISOU 6030  C   PRO C 131     5129   4511   3818    301    480    116       C  
ATOM   6031  O   PRO C 131      10.649 100.172  55.978  1.00 42.43           O  
ANISOU 6031  O   PRO C 131     5972   5421   4728    296    486    102       O  
ATOM   6032  CB  PRO C 131      11.092  98.655  58.252  1.00 37.52           C  
ANISOU 6032  CB  PRO C 131     5358   4935   3962    501    418    139       C  
ATOM   6033  CG  PRO C 131      10.224  97.464  57.892  1.00 38.32           C  
ANISOU 6033  CG  PRO C 131     5560   4927   4070    556    456    228       C  
ATOM   6034  CD  PRO C 131       8.975  97.668  58.727  1.00 34.91           C  
ANISOU 6034  CD  PRO C 131     5201   4431   3628    540    471    254       C  
ATOM   6035  N   LYS C 132       8.712 101.036  56.638  1.00 31.35           N  
ANISOU 6035  N   LYS C 132     4669   3903   3337    239    510    128       N  
ATOM   6036  CA  LYS C 132       8.375 101.474  55.307  1.00 32.69           C  
ANISOU 6036  CA  LYS C 132     4859   3995   3566    177    549    132       C  
ATOM   6037  C   LYS C 132       8.999 102.839  55.057  1.00 33.00           C  
ANISOU 6037  C   LYS C 132     4858   4054   3624     89    563     61       C  
ATOM   6038  O   LYS C 132       9.078 103.638  55.952  1.00 33.57           O  
ANISOU 6038  O   LYS C 132     4917   4162   3674     57    552     16       O  
ATOM   6039  CB  LYS C 132       6.863 101.505  55.118  1.00 31.57           C  
ANISOU 6039  CB  LYS C 132     4794   3758   3442    167    575    176       C  
ATOM   6040  CG  LYS C 132       6.219 100.149  55.262  1.00 32.89           C  
ANISOU 6040  CG  LYS C 132     5004   3895   3596    232    579    237       C  
ATOM   6041  CD  LYS C 132       4.823 100.087  54.731  1.00 34.56           C  
ANISOU 6041  CD  LYS C 132     5270   4025   3835    210    610    266       C  
ATOM   6042  CE  LYS C 132       4.360  98.656  54.597  1.00 38.67           C  
ANISOU 6042  CE  LYS C 132     5830   4511   4352    254    629    313       C  
ATOM   6043  NZ  LYS C 132       3.031  98.600  53.962  1.00 44.58           N  
ANISOU 6043  NZ  LYS C 132     6612   5196   5127    222    659    324       N  
ATOM   6044  N   ALA C 133       9.391 103.081  53.800  1.00 32.10           N  
ANISOU 6044  N   ALA C 133     4736   3907   3553     48    596     51       N  
ATOM   6045  CA  ALA C 133      10.026 104.311  53.386  1.00 31.86           C  
ANISOU 6045  CA  ALA C 133     4683   3878   3544    -41    631    -14       C  
ATOM   6046  C   ALA C 133       9.121 105.515  53.658  1.00 31.25           C  
ANISOU 6046  C   ALA C 133     4672   3731   3469    -94    662    -27       C  
ATOM   6047  O   ALA C 133       9.628 106.572  54.031  1.00 33.64           O  
ANISOU 6047  O   ALA C 133     4960   4054   3767   -166    682    -95       O  
ATOM   6048  CB  ALA C 133      10.383 104.217  51.925  1.00 34.82           C  
ANISOU 6048  CB  ALA C 133     5060   4208   3959    -60    670     -4       C  
ATOM   6049  N   ILE C 134       7.798 105.333  53.511  1.00 29.96           N  
ANISOU 6049  N   ILE C 134     4582   3493   3308    -58    667     32       N  
ATOM   6050  CA  ILE C 134       6.790 106.398  53.710  1.00 29.75           C  
ANISOU 6050  CA  ILE C 134     4626   3400   3277    -85    697     30       C  
ATOM   6051  C   ILE C 134       6.979 107.116  55.049  1.00 28.04           C  
ANISOU 6051  C   ILE C 134     4397   3228   3028   -116    682    -19       C  
ATOM   6052  O   ILE C 134       6.702 108.298  55.115  1.00 30.36           O  
ANISOU 6052  O   ILE C 134     4740   3475   3319   -166    722    -50       O  
ATOM   6053  CB  ILE C 134       5.351 105.869  53.572  1.00 29.27           C  
ANISOU 6053  CB  ILE C 134     4618   3289   3213    -27    691     94       C  
ATOM   6054  CG1 ILE C 134       4.344 107.022  53.526  1.00 28.11           C  
ANISOU 6054  CG1 ILE C 134     4543   3079   3058    -42    726     92       C  
ATOM   6055  CG2 ILE C 134       4.981 104.885  54.678  1.00 27.07           C  
ANISOU 6055  CG2 ILE C 134     4322   3054   2908     24    648    122       C  
ATOM   6056  CD1 ILE C 134       2.966 106.582  53.087  1.00 26.71           C  
ANISOU 6056  CD1 ILE C 134     4403   2865   2879     10    727    141       C  
ATOM   6057  N   PHE C 135       7.467 106.421  56.085  1.00 29.83           N  
ANISOU 6057  N   PHE C 135     4566   3544   3224    -81    630    -29       N  
ATOM   6058  CA  PHE C 135       7.581 106.989  57.440  1.00 31.33           C  
ANISOU 6058  CA  PHE C 135     4741   3787   3373    -98    607    -76       C  
ATOM   6059  C   PHE C 135       9.029 107.376  57.789  1.00 33.57           C  
ANISOU 6059  C   PHE C 135     4938   4170   3644   -151    595   -166       C  
ATOM   6060  O   PHE C 135       9.306 107.803  58.922  1.00 37.32           O  
ANISOU 6060  O   PHE C 135     5385   4712   4080   -166    570   -220       O  
ATOM   6061  CB  PHE C 135       7.036 106.005  58.478  1.00 30.77           C  
ANISOU 6061  CB  PHE C 135     4674   3753   3262    -12    560    -28       C  
ATOM   6062  CG  PHE C 135       5.624 105.535  58.222  1.00 29.07           C  
ANISOU 6062  CG  PHE C 135     4529   3456   3059     29    576     46       C  
ATOM   6063  CD1 PHE C 135       4.589 106.443  58.045  1.00 27.98           C  
ANISOU 6063  CD1 PHE C 135     4454   3245   2931      1    611     51       C  
ATOM   6064  CD2 PHE C 135       5.326 104.182  58.193  1.00 27.43           C  
ANISOU 6064  CD2 PHE C 135     4325   3249   2845     99    561    105       C  
ATOM   6065  CE1 PHE C 135       3.288 106.012  57.825  1.00 26.59           C  
ANISOU 6065  CE1 PHE C 135     4324   3016   2761     40    623    107       C  
ATOM   6066  CE2 PHE C 135       4.029 103.753  57.949  1.00 28.71           C  
ANISOU 6066  CE2 PHE C 135     4541   3345   3019    121    582    158       C  
ATOM   6067  CZ  PHE C 135       3.011 104.665  57.764  1.00 26.88           C  
ANISOU 6067  CZ  PHE C 135     4353   3059   2799     91    609    156       C  
ATOM   6068  N   GLU C 136       9.946 107.265  56.830  1.00 34.76           N  
ANISOU 6068  N   GLU C 136     5042   4339   3825   -182    614   -190       N  
ATOM   6069  CA  GLU C 136      11.379 107.415  57.144  1.00 39.69           C  
ANISOU 6069  CA  GLU C 136     5558   5085   4434   -225    596   -281       C  
ATOM   6070  C   GLU C 136      11.836 108.879  56.979  1.00 40.03           C  
ANISOU 6070  C   GLU C 136     5606   5105   4497   -358    660   -374       C  
ATOM   6071  O   GLU C 136      12.925 109.200  57.417  1.00 40.52           O  
ANISOU 6071  O   GLU C 136     5576   5275   4543   -415    651   -471       O  
ATOM   6072  CB  GLU C 136      12.221 106.452  56.303  1.00 40.15           C  
ANISOU 6072  CB  GLU C 136     5552   5193   4509   -185    584   -265       C  
ATOM   6073  CG  GLU C 136      12.205 105.025  56.826  1.00 41.89           C  
ANISOU 6073  CG  GLU C 136     5748   5477   4688    -56    520   -205       C  
ATOM   6074  N   LYS C 137      10.975 109.766  56.444  1.00 40.31           N  
ANISOU 6074  N   LYS C 137     5751   5006   4558   -403    726   -351       N  
ATOM   6075  CA  LYS C 137      11.295 111.204  56.252  1.00 39.69           C  
ANISOU 6075  CA  LYS C 137     5712   4872   4493   -528    807   -432       C  
ATOM   6076  C   LYS C 137      10.592 112.088  57.290  1.00 42.52           C  
ANISOU 6076  C   LYS C 137     6136   5198   4821   -551    815   -455       C  
ATOM   6077  O   LYS C 137      10.644 113.312  57.181  1.00 42.73           O  
ANISOU 6077  O   LYS C 137     6227   5155   4853   -646    893   -512       O  
ATOM   6078  CB  LYS C 137      10.934 111.643  54.828  1.00 37.80           C  
ANISOU 6078  CB  LYS C 137     5566   4500   4295   -550    890   -390       C  
ATOM   6079  CG  LYS C 137      11.809 111.015  53.751  1.00 38.25           C  
ANISOU 6079  CG  LYS C 137     5561   4585   4384   -554    900   -388       C  
ATOM   6080  CD  LYS C 137      11.505 111.439  52.320  1.00 39.28           C  
ANISOU 6080  CD  LYS C 137     5787   4588   4548   -569    984   -347       C  
ATOM   6081  N   GLY C 138       9.947 111.498  58.310  1.00 39.61           N  
ANISOU 6081  N   GLY C 138     5761   4874   4415   -467    745   -414       N  
ATOM   6082  CA  GLY C 138       9.297 112.307  59.354  1.00 35.76           C  
ANISOU 6082  CA  GLY C 138     5332   4361   3892   -484    750   -437       C  
ATOM   6083  C   GLY C 138       7.996 112.907  58.837  1.00 34.42           C  
ANISOU 6083  C   GLY C 138     5296   4045   3734   -464    806   -370       C  
ATOM   6084  O   GLY C 138       7.435 112.395  57.846  1.00 33.45           O  
ANISOU 6084  O   GLY C 138     5208   3862   3637   -408    815   -292       O  
ATOM   6085  N   ASN C 139       7.502 113.975  59.487  1.00 34.33           N  
ANISOU 6085  N   ASN C 139     5361   3982   3698   -501    843   -402       N  
ATOM   6086  CA  ASN C 139       6.187 114.535  59.130  1.00 32.55           C  
ANISOU 6086  CA  ASN C 139     5263   3634   3468   -458    890   -337       C  
ATOM   6087  C   ASN C 139       6.268 115.194  57.741  1.00 34.33           C  
ANISOU 6087  C   ASN C 139     5565   3752   3724   -496    980   -330       C  
ATOM   6088  O   ASN C 139       7.199 115.924  57.424  1.00 33.60           O  
ANISOU 6088  O   ASN C 139     5479   3640   3646   -598   1043   -405       O  
ATOM   6089  CB  ASN C 139       5.635 115.491  60.193  1.00 33.37           C  
ANISOU 6089  CB  ASN C 139     5436   3710   3532   -477    909   -370       C  
ATOM   6090  CG  ASN C 139       5.404 114.840  61.542  1.00 33.22           C  
ANISOU 6090  CG  ASN C 139     5357   3787   3476   -423    826   -365       C  
ATOM   6091  OD1 ASN C 139       5.306 113.626  61.661  1.00 34.81           O  
ANISOU 6091  OD1 ASN C 139     5493   4053   3678   -349    759   -312       O  
ATOM   6092  ND2 ASN C 139       5.348 115.632  62.585  1.00 31.26           N  
ANISOU 6092  ND2 ASN C 139     5139   3545   3190   -461    834   -421       N  
ATOM   6093  N   VAL C 140       5.295 114.879  56.882  1.00 32.61           N  
ANISOU 6093  N   VAL C 140     5405   3471   3515   -410    987   -243       N  
ATOM   6094  CA  VAL C 140       5.236 115.430  55.545  1.00 33.06           C  
ANISOU 6094  CA  VAL C 140     5545   3427   3587   -417   1067   -223       C  
ATOM   6095  C   VAL C 140       3.834 116.004  55.348  1.00 32.71           C  
ANISOU 6095  C   VAL C 140     5620   3295   3510   -333   1099   -164       C  
ATOM   6096  O   VAL C 140       2.870 115.267  55.374  1.00 29.85           O  
ANISOU 6096  O   VAL C 140     5239   2962   3141   -240   1044   -100       O  
ATOM   6097  CB  VAL C 140       5.573 114.388  54.460  1.00 34.16           C  
ANISOU 6097  CB  VAL C 140     5623   3593   3763   -383   1040   -181       C  
ATOM   6098  CG1 VAL C 140       5.592 115.025  53.076  1.00 34.19           C  
ANISOU 6098  CG1 VAL C 140     5720   3493   3775   -389   1129   -166       C  
ATOM   6099  CG2 VAL C 140       6.888 113.677  54.738  1.00 35.43           C  
ANISOU 6099  CG2 VAL C 140     5655   3859   3947   -439    996   -233       C  
ATOM   6100  N   ALA C 141       3.760 117.319  55.105  1.00 32.01           N  
ANISOU 6100  N   ALA C 141     5658   3103   3400   -368   1197   -191       N  
ATOM   6101  CA  ALA C 141       2.520 118.044  55.054  1.00 30.64           C  
ANISOU 6101  CA  ALA C 141     5607   2852   3182   -284   1236   -146       C  
ATOM   6102  C   ALA C 141       1.824 117.814  53.716  1.00 29.03           C  
ANISOU 6102  C   ALA C 141     5451   2605   2972   -183   1252    -74       C  
ATOM   6103  O   ALA C 141       0.605 117.707  53.681  1.00 31.69           O  
ANISOU 6103  O   ALA C 141     5817   2946   3277    -75   1227    -20       O  
ATOM   6104  CB  ALA C 141       2.785 119.507  55.264  1.00 33.28           C  
ANISOU 6104  CB  ALA C 141     6071   3085   3489   -354   1344   -202       C  
ATOM   6105  N   LYS C 142       2.611 117.846  52.642  1.00 30.45           N  
ANISOU 6105  N   LYS C 142     5645   2746   3177   -222   1301    -82       N  
ATOM   6106  CA  LYS C 142       2.180 117.613  51.277  1.00 30.83           C  
ANISOU 6106  CA  LYS C 142     5735   2758   3219   -136   1320    -23       C  
ATOM   6107  C   LYS C 142       3.096 116.562  50.634  1.00 30.85           C  
ANISOU 6107  C   LYS C 142     5627   2819   3275   -176   1280    -26       C  
ATOM   6108  O   LYS C 142       4.121 116.907  50.073  1.00 29.41           O  
ANISOU 6108  O   LYS C 142     5462   2596   3114   -255   1345    -63       O  
ATOM   6109  CB  LYS C 142       2.309 118.894  50.453  1.00 35.44           C  
ANISOU 6109  CB  LYS C 142     6486   3209   3770   -139   1450    -29       C  
ATOM   6110  CG  LYS C 142       1.268 119.949  50.742  1.00 43.44           C  
ANISOU 6110  CG  LYS C 142     7641   4147   4715    -59   1504     -8       C  
ATOM   6111  CD  LYS C 142       0.054 119.873  49.841  1.00 46.85           C  
ANISOU 6111  CD  LYS C 142     8133   4571   5097    106   1495     66       C  
ATOM   6112  CE  LYS C 142      -0.854 121.072  50.043  1.00 50.40           C  
ANISOU 6112  CE  LYS C 142     8741   4938   5468    194   1567     83       C  
ATOM   6113  NZ  LYS C 142      -1.364 121.123  51.439  1.00 50.85           N  
ANISOU 6113  NZ  LYS C 142     8756   5044   5518    183   1517     64       N  
ATOM   6114  N   ALA C 143       2.691 115.290  50.689  1.00 28.81           N  
ANISOU 6114  N   ALA C 143     5261   2651   3034   -121   1182     11       N  
ATOM   6115  CA  ALA C 143       3.468 114.169  50.196  1.00 29.15           C  
ANISOU 6115  CA  ALA C 143     5198   2754   3122   -144   1137     14       C  
ATOM   6116  C   ALA C 143       3.225 113.937  48.694  1.00 29.06           C  
ANISOU 6116  C   ALA C 143     5227   2704   3110    -80   1161     58       C  
ATOM   6117  O   ALA C 143       2.249 114.414  48.111  1.00 30.07           O  
ANISOU 6117  O   ALA C 143     5444   2783   3196      7   1190     95       O  
ATOM   6118  CB  ALA C 143       3.107 112.936  50.989  1.00 28.01           C  
ANISOU 6118  CB  ALA C 143     4943   2708   2989   -113   1035     34       C  
ATOM   6119  N   ASP C 144       4.123 113.160  48.093  1.00 28.12           N  
ANISOU 6119  N   ASP C 144     5036   2616   3029   -113   1146     53       N  
ATOM   6120  CA  ASP C 144       4.083 112.776  46.694  1.00 30.96           C  
ANISOU 6120  CA  ASP C 144     5416   2952   3393    -62   1162     90       C  
ATOM   6121  C   ASP C 144       4.039 111.246  46.619  1.00 28.16           C  
ANISOU 6121  C   ASP C 144     4948   2684   3068    -32   1073    115       C  
ATOM   6122  O   ASP C 144       4.727 110.587  47.381  1.00 28.30           O  
ANISOU 6122  O   ASP C 144     4873   2765   3113    -81   1027     92       O  
ATOM   6123  CB  ASP C 144       5.342 113.302  45.987  1.00 36.85           C  
ANISOU 6123  CB  ASP C 144     6193   3646   4161   -142   1245     54       C  
ATOM   6124  CG  ASP C 144       5.379 113.054  44.493  1.00 41.30           C  
ANISOU 6124  CG  ASP C 144     6796   4172   4722    -89   1277     90       C  
ATOM   6125  OD1 ASP C 144       4.738 113.843  43.765  1.00 47.75           O  
ANISOU 6125  OD1 ASP C 144     7736   4910   5494    -24   1339    118       O  
ATOM   6126  OD2 ASP C 144       6.052 112.076  44.061  1.00 42.73           O  
ANISOU 6126  OD2 ASP C 144     6889   4404   4940   -105   1241     92       O  
ATOM   6127  N   ILE C 145       3.225 110.691  45.719  1.00 26.37           N  
ANISOU 6127  N   ILE C 145     4731   2460   2827     52   1051    158       N  
ATOM   6128  CA  ILE C 145       3.067 109.233  45.617  1.00 27.21           C  
ANISOU 6128  CA  ILE C 145     4745   2635   2958     77    977    178       C  
ATOM   6129  C   ILE C 145       4.439 108.555  45.421  1.00 27.11           C  
ANISOU 6129  C   ILE C 145     4664   2648   2988     18    973    162       C  
ATOM   6130  O   ILE C 145       4.736 107.516  46.061  1.00 29.34           O  
ANISOU 6130  O   ILE C 145     4862   2993   3291      7    916    162       O  
ATOM   6131  CB  ILE C 145       2.061 108.867  44.504  1.00 26.40           C  
ANISOU 6131  CB  ILE C 145     4668   2531   2831    167    967    212       C  
ATOM   6132  CG1 ILE C 145       0.636 109.235  44.927  1.00 28.29           C  
ANISOU 6132  CG1 ILE C 145     4936   2786   3027    233    950    221       C  
ATOM   6133  CG2 ILE C 145       2.174 107.393  44.136  1.00 26.76           C  
ANISOU 6133  CG2 ILE C 145     4632   2627   2906    173    914    224       C  
ATOM   6134  CD1 ILE C 145      -0.395 109.130  43.829  1.00 28.64           C  
ANISOU 6134  CD1 ILE C 145     5006   2842   3031    329    944    240       C  
ATOM   6135  N   ILE C 146       5.280 109.135  44.556  1.00 28.87           N  
ANISOU 6135  N   ILE C 146     4926   2823   3219    -13   1037    147       N  
ATOM   6136  CA  ILE C 146       6.547 108.548  44.224  1.00 30.74           C  
ANISOU 6136  CA  ILE C 146     5097   3089   3492    -62   1039    129       C  
ATOM   6137  C   ILE C 146       7.607 108.903  45.275  1.00 30.90           C  
ANISOU 6137  C   ILE C 146     5060   3149   3529   -152   1045     72       C  
ATOM   6138  O   ILE C 146       8.274 108.024  45.761  1.00 33.26           O  
ANISOU 6138  O   ILE C 146     5265   3524   3847   -164    995     60       O  
ATOM   6139  CB  ILE C 146       6.974 108.932  42.794  1.00 33.39           C  
ANISOU 6139  CB  ILE C 146     5494   3362   3828    -57   1110    136       C  
ATOM   6140  CG1 ILE C 146       5.994 108.328  41.786  1.00 34.19           C  
ANISOU 6140  CG1 ILE C 146     5625   3454   3908     39   1084    185       C  
ATOM   6141  CG2 ILE C 146       8.408 108.489  42.526  1.00 32.87           C  
ANISOU 6141  CG2 ILE C 146     5356   3330   3800   -119   1124    106       C  
ATOM   6142  CD1 ILE C 146       6.044 108.963  40.433  1.00 39.12           C  
ANISOU 6142  CD1 ILE C 146     6345   4007   4511     72   1157    199       C  
ATOM   6143  N   ASP C 147       7.753 110.178  45.631  1.00 30.61           N  
ANISOU 6143  N   ASP C 147     5083   3065   3480   -209   1108     33       N  
ATOM   6144  CA  ASP C 147       8.861 110.581  46.459  1.00 32.71           C  
ANISOU 6144  CA  ASP C 147     5290   3374   3761   -308   1123    -36       C  
ATOM   6145  C   ASP C 147       8.705 110.002  47.872  1.00 32.47           C  
ANISOU 6145  C   ASP C 147     5179   3433   3723   -298   1038    -46       C  
ATOM   6146  O   ASP C 147       9.724 109.833  48.552  1.00 33.36           O  
ANISOU 6146  O   ASP C 147     5203   3627   3846   -354   1017   -101       O  
ATOM   6147  CB  ASP C 147       9.001 112.100  46.532  1.00 37.60           C  
ANISOU 6147  CB  ASP C 147     6006   3912   4367   -382   1221    -83       C  
ATOM   6148  CG  ASP C 147       9.247 112.800  45.203  1.00 45.69           C  
ANISOU 6148  CG  ASP C 147     7131   4836   5391   -396   1327    -77       C  
ATOM   6149  OD1 ASP C 147       9.488 112.101  44.190  1.00 48.85           O  
ANISOU 6149  OD1 ASP C 147     7511   5242   5807   -358   1321    -44       O  
ATOM   6150  OD2 ASP C 147       9.207 114.057  45.194  1.00 53.16           O  
ANISOU 6150  OD2 ASP C 147     8187   5692   6318   -444   1422   -104       O  
ATOM   6151  N   ASN C 148       7.455 109.731  48.316  1.00 29.22           N  
ANISOU 6151  N   ASN C 148     4798   3013   3289   -226    992      1       N  
ATOM   6152  CA  ASN C 148       7.195 109.285  49.691  1.00 30.00           C  
ANISOU 6152  CA  ASN C 148     4842   3181   3374   -213    924     -4       C  
ATOM   6153  C   ASN C 148       6.712 107.820  49.711  1.00 29.70           C  
ANISOU 6153  C   ASN C 148     4756   3189   3339   -136    854     50       C  
ATOM   6154  O   ASN C 148       6.144 107.354  50.708  1.00 27.33           O  
ANISOU 6154  O   ASN C 148     4437   2924   3020   -104    806     65       O  
ATOM   6155  CB  ASN C 148       6.261 110.253  50.441  1.00 29.78           C  
ANISOU 6155  CB  ASN C 148     4887   3111   3315   -212    941     -8       C  
ATOM   6156  CG  ASN C 148       6.808 111.661  50.520  1.00 30.44           C  
ANISOU 6156  CG  ASN C 148     5028   3142   3393   -297   1020    -68       C  
ATOM   6157  OD1 ASN C 148       6.383 112.531  49.768  1.00 30.55           O  
ANISOU 6157  OD1 ASN C 148     5147   3063   3395   -290   1091    -56       O  
ATOM   6158  ND2 ASN C 148       7.779 111.892  51.385  1.00 30.97           N  
ANISOU 6158  ND2 ASN C 148     5032   3270   3463   -376   1014   -138       N  
ATOM   6159  N   SER C 149       6.912 107.107  48.599  1.00 27.96           N  
ANISOU 6159  N   SER C 149     4525   2958   3138   -108    857     78       N  
ATOM   6160  CA  SER C 149       6.769 105.672  48.516  1.00 28.48           C  
ANISOU 6160  CA  SER C 149     4546   3063   3210    -52    806    118       C  
ATOM   6161  C   SER C 149       5.366 105.207  48.945  1.00 28.79           C  
ANISOU 6161  C   SER C 149     4614   3092   3233      0    776    158       C  
ATOM   6162  O   SER C 149       5.240 104.187  49.621  1.00 27.98           O  
ANISOU 6162  O   SER C 149     4477   3030   3125     29    735    176       O  
ATOM   6163  CB  SER C 149       7.831 105.003  49.341  1.00 30.53           C  
ANISOU 6163  CB  SER C 149     4723   3408   3469    -59    767     94       C  
ATOM   6164  OG  SER C 149       9.109 105.261  48.800  1.00 32.84           O  
ANISOU 6164  OG  SER C 149     4973   3725   3779   -105    795     54       O  
ATOM   6165  N   ILE C 150       4.321 105.908  48.485  1.00 28.19           N  
ANISOU 6165  N   ILE C 150     4601   2963   3143     18    801    170       N  
ATOM   6166  CA  ILE C 150       2.959 105.657  48.948  1.00 30.09           C  
ANISOU 6166  CA  ILE C 150     4859   3207   3365     59    779    193       C  
ATOM   6167  C   ILE C 150       2.419 104.356  48.343  1.00 27.57           C  
ANISOU 6167  C   ILE C 150     4518   2899   3056     98    756    223       C  
ATOM   6168  O   ILE C 150       1.562 103.753  48.969  1.00 26.65           O  
ANISOU 6168  O   ILE C 150     4391   2802   2930    116    735    235       O  
ATOM   6169  CB  ILE C 150       2.002 106.868  48.747  1.00 28.65           C  
ANISOU 6169  CB  ILE C 150     4746   2981   3155     79    811    191       C  
ATOM   6170  CG1 ILE C 150       2.580 108.128  49.381  1.00 27.18           C  
ANISOU 6170  CG1 ILE C 150     4595   2771   2958     30    845    157       C  
ATOM   6171  CG2 ILE C 150       0.610 106.577  49.304  1.00 26.18           C  
ANISOU 6171  CG2 ILE C 150     4433   2690   2820    121    786    207       C  
ATOM   6172  CD1 ILE C 150       1.741 109.366  49.165  1.00 31.60           C  
ANISOU 6172  CD1 ILE C 150     5244   3277   3484     58    890    158       C  
ATOM   6173  N   PHE C 151       2.902 103.931  47.164  1.00 24.53           N  
ANISOU 6173  N   PHE C 151     4129   2500   2688    105    767    230       N  
ATOM   6174  CA  PHE C 151       2.468 102.671  46.555  1.00 24.94           C  
ANISOU 6174  CA  PHE C 151     4165   2561   2751    133    751    249       C  
ATOM   6175  C   PHE C 151       2.897 101.451  47.395  1.00 23.75           C  
ANISOU 6175  C   PHE C 151     3977   2439   2607    131    726    261       C  
ATOM   6176  O   PHE C 151       2.408 100.376  47.186  1.00 23.29           O  
ANISOU 6176  O   PHE C 151     3916   2379   2554    147    722    275       O  
ATOM   6177  CB  PHE C 151       3.002 102.519  45.125  1.00 28.62           C  
ANISOU 6177  CB  PHE C 151     4639   3004   3229    143    771    252       C  
ATOM   6178  CG  PHE C 151       2.213 103.209  44.045  1.00 28.66           C  
ANISOU 6178  CG  PHE C 151     4690   2984   3215    176    792    251       C  
ATOM   6179  CD1 PHE C 151       0.856 103.444  44.166  1.00 36.34           C  
ANISOU 6179  CD1 PHE C 151     5676   3970   4160    209    782    248       C  
ATOM   6180  CD2 PHE C 151       2.836 103.612  42.882  1.00 33.32           C  
ANISOU 6180  CD2 PHE C 151     5309   3542   3807    184    824    251       C  
ATOM   6181  CE1 PHE C 151       0.151 104.083  43.156  1.00 43.76           C  
ANISOU 6181  CE1 PHE C 151     6656   4900   5067    260    798    245       C  
ATOM   6182  CE2 PHE C 151       2.132 104.247  41.876  1.00 32.30           C  
ANISOU 6182  CE2 PHE C 151     5233   3391   3647    233    846    254       C  
ATOM   6183  CZ  PHE C 151       0.784 104.453  41.994  1.00 34.39           C  
ANISOU 6183  CZ  PHE C 151     5509   3680   3878    277    829    250       C  
ATOM   6184  N   TYR C 152       3.825 101.635  48.330  1.00 23.47           N  
ANISOU 6184  N   TYR C 152     3917   2431   2569    115    715    252       N  
ATOM   6185  CA  TYR C 152       4.257 100.597  49.252  1.00 25.93           C  
ANISOU 6185  CA  TYR C 152     4205   2776   2872    134    693    266       C  
ATOM   6186  C   TYR C 152       3.475 100.636  50.575  1.00 27.78           C  
ANISOU 6186  C   TYR C 152     4450   3022   3081    139    680    270       C  
ATOM   6187  O   TYR C 152       3.790  99.866  51.482  1.00 26.75           O  
ANISOU 6187  O   TYR C 152     4312   2917   2931    164    666    284       O  
ATOM   6188  CB  TYR C 152       5.767 100.737  49.477  1.00 27.12           C  
ANISOU 6188  CB  TYR C 152     4310   2971   3021    127    683    246       C  
ATOM   6189  CG  TYR C 152       6.535 100.422  48.222  1.00 27.55           C  
ANISOU 6189  CG  TYR C 152     4351   3016   3098    129    699    247       C  
ATOM   6190  CD1 TYR C 152       6.780 101.414  47.281  1.00 29.19           C  
ANISOU 6190  CD1 TYR C 152     4569   3197   3324     93    729    225       C  
ATOM   6191  CD2 TYR C 152       6.924  99.122  47.927  1.00 28.73           C  
ANISOU 6191  CD2 TYR C 152     4494   3174   3249    171    693    272       C  
ATOM   6192  CE1 TYR C 152       7.461 101.139  46.105  1.00 27.59           C  
ANISOU 6192  CE1 TYR C 152     4359   2984   3140     96    749    227       C  
ATOM   6193  CE2 TYR C 152       7.588  98.830  46.741  1.00 28.71           C  
ANISOU 6193  CE2 TYR C 152     4482   3161   3266    176    709    273       C  
ATOM   6194  CZ  TYR C 152       7.859  99.846  45.834  1.00 27.35           C  
ANISOU 6194  CZ  TYR C 152     4310   2969   3112    137    736    251       C  
ATOM   6195  OH  TYR C 152       8.486  99.591  44.649  1.00 28.89           O  
ANISOU 6195  OH  TYR C 152     4500   3150   3324    142    757    253       O  
ATOM   6196  N   ALA C 153       2.453 101.499  50.666  1.00 24.75           N  
ANISOU 6196  N   ALA C 153     4091   2621   2692    126    689    261       N  
ATOM   6197  CA  ALA C 153       1.635 101.622  51.878  1.00 24.81           C  
ANISOU 6197  CA  ALA C 153     4111   2640   2676    130    682    264       C  
ATOM   6198  C   ALA C 153       0.169 101.809  51.498  1.00 25.33           C  
ANISOU 6198  C   ALA C 153     4197   2687   2740    134    697    264       C  
ATOM   6199  O   ALA C 153      -0.381 102.829  51.843  1.00 28.18           O  
ANISOU 6199  O   ALA C 153     4574   3048   3085    132    701    252       O  
ATOM   6200  CB  ALA C 153       2.120 102.798  52.692  1.00 24.16           C  
ANISOU 6200  CB  ALA C 153     4026   2576   2577    109    675    238       C  
ATOM   6201  N   LEU C 154      -0.428 100.843  50.782  1.00 22.93           N  
ANISOU 6201  N   LEU C 154     3889   2374   2448    140    707    273       N  
ATOM   6202  CA  LEU C 154      -1.777 100.982  50.199  1.00 25.53           C  
ANISOU 6202  CA  LEU C 154     4219   2708   2773    146    717    259       C  
ATOM   6203  C   LEU C 154      -2.913 100.428  51.093  1.00 26.07           C  
ANISOU 6203  C   LEU C 154     4282   2792   2829    137    728    256       C  
ATOM   6204  O   LEU C 154      -4.076 100.415  50.680  1.00 24.06           O  
ANISOU 6204  O   LEU C 154     4013   2559   2570    138    737    234       O  
ATOM   6205  CB  LEU C 154      -1.777 100.314  48.820  1.00 27.80           C  
ANISOU 6205  CB  LEU C 154     4497   2986   3077    149    723    254       C  
ATOM   6206  CG  LEU C 154      -0.987 101.048  47.729  1.00 27.79           C  
ANISOU 6206  CG  LEU C 154     4507   2969   3082    163    723    252       C  
ATOM   6207  CD1 LEU C 154      -0.961 100.241  46.435  1.00 29.48           C  
ANISOU 6207  CD1 LEU C 154     4714   3176   3309    170    728    249       C  
ATOM   6208  CD2 LEU C 154      -1.553 102.424  47.475  1.00 28.99           C  
ANISOU 6208  CD2 LEU C 154     4682   3123   3209    186    729    240       C  
ATOM   6209  N   SER C 155      -2.637 100.068  52.358  1.00 33.08           N  
ANISOU 6209  N   SER C 155     5182   3677   3707    132    729    272       N  
ATOM   6210  CA  SER C 155      -3.726  99.739  53.343  1.00 31.63           C  
ANISOU 6210  CA  SER C 155     5003   3505   3508    123    749    270       C  
ATOM   6211  C   SER C 155      -4.743 100.901  53.468  1.00 35.06           C  
ANISOU 6211  C   SER C 155     5428   3968   3925    132    745    248       C  
ATOM   6212  O   SER C 155      -4.456 102.083  53.155  1.00 36.09           O  
ANISOU 6212  O   SER C 155     5566   4099   4047    151    730    242       O  
ATOM   6213  CB  SER C 155      -3.152  99.394  54.706  1.00 29.28           C  
ANISOU 6213  CB  SER C 155     4731   3200   3190    132    750    295       C  
ATOM   6214  OG  SER C 155      -2.957 100.581  55.512  1.00 35.42           O  
ANISOU 6214  OG  SER C 155     5513   3998   3947    144    727    290       O  
ATOM   6215  N   VAL C 156      -5.932 100.591  53.995  1.00 33.06           N  
ANISOU 6215  N   VAL C 156     5163   3736   3661    120    768    235       N  
ATOM   6216  CA  VAL C 156      -6.933 101.616  54.252  1.00 32.51           C  
ANISOU 6216  CA  VAL C 156     5082   3702   3567    140    766    215       C  
ATOM   6217  C   VAL C 156      -6.931 102.025  55.739  1.00 33.83           C  
ANISOU 6217  C   VAL C 156     5275   3865   3711    144    769    230       C  
ATOM   6218  O   VAL C 156      -7.904 102.656  56.210  1.00 33.12           O  
ANISOU 6218  O   VAL C 156     5179   3805   3599    159    777    215       O  
ATOM   6219  CB  VAL C 156      -8.319 101.158  53.774  1.00 32.91           C  
ANISOU 6219  CB  VAL C 156     5087   3800   3617    128    787    176       C  
ATOM   6220  CG1 VAL C 156      -8.363 101.089  52.251  1.00 32.52           C  
ANISOU 6220  CG1 VAL C 156     5010   3768   3576    140    774    153       C  
ATOM   6221  CG2 VAL C 156      -8.751  99.850  54.421  1.00 34.10           C  
ANISOU 6221  CG2 VAL C 156     5234   3941   3780     76    830    172       C  
ATOM   6222  N   LEU C 157      -5.817 101.781  56.460  1.00 32.10           N  
ANISOU 6222  N   LEU C 157     5085   3620   3492    142    759    256       N  
ATOM   6223  CA  LEU C 157      -5.625 102.372  57.787  1.00 32.21           C  
ANISOU 6223  CA  LEU C 157     5124   3636   3475    154    752    265       C  
ATOM   6224  C   LEU C 157      -5.044 103.772  57.629  1.00 27.23           C  
ANISOU 6224  C   LEU C 157     4505   3003   2835    165    728    252       C  
ATOM   6225  O   LEU C 157      -3.891 104.078  57.947  1.00 25.91           O  
ANISOU 6225  O   LEU C 157     4348   2830   2665    160    708    252       O  
ATOM   6226  CB  LEU C 157      -4.781 101.472  58.678  1.00 37.86           C  
ANISOU 6226  CB  LEU C 157     5862   4339   4181    158    752    291       C  
ATOM   6227  CG  LEU C 157      -5.668 100.492  59.434  1.00 41.38           C  
ANISOU 6227  CG  LEU C 157     6327   4778   4616    150    795    304       C  
ATOM   6228  CD1 LEU C 157      -6.073  99.343  58.532  1.00 43.22           C  
ANISOU 6228  CD1 LEU C 157     6550   4991   4878    121    830    301       C  
ATOM   6229  CD2 LEU C 157      -5.024 100.024  60.723  1.00 41.95           C  
ANISOU 6229  CD2 LEU C 157     6442   4843   4652    179    797    333       C  
ATOM   6230  N   LYS C 158      -5.928 104.607  57.114  1.00 26.13           N  
ANISOU 6230  N   LYS C 158     4365   2873   2687    182    736    236       N  
ATOM   6231  CA  LYS C 158      -5.681 106.001  56.864  1.00 26.48           C  
ANISOU 6231  CA  LYS C 158     4442   2903   2717    198    733    223       C  
ATOM   6232  C   LYS C 158      -6.950 106.774  57.232  1.00 26.28           C  
ANISOU 6232  C   LYS C 158     4428   2898   2657    234    749    213       C  
ATOM   6233  O   LYS C 158      -8.039 106.217  57.316  1.00 26.85           O  
ANISOU 6233  O   LYS C 158     4468   3006   2725    243    759    209       O  
ATOM   6234  CB  LYS C 158      -5.309 106.188  55.394  1.00 24.73           C  
ANISOU 6234  CB  LYS C 158     4218   2663   2512    205    734    219       C  
ATOM   6235  CG  LYS C 158      -4.112 105.378  54.902  1.00 25.29           C  
ANISOU 6235  CG  LYS C 158     4271   2719   2617    176    722    227       C  
ATOM   6236  CD  LYS C 158      -3.882 105.537  53.417  1.00 24.78           C  
ANISOU 6236  CD  LYS C 158     4209   2638   2567    186    728    224       C  
ATOM   6237  CE  LYS C 158      -2.574 104.938  52.912  1.00 25.75           C  
ANISOU 6237  CE  LYS C 158     4318   2746   2721    159    719    230       C  
ATOM   6238  NZ  LYS C 158      -2.375 103.562  53.404  1.00 27.54           N  
ANISOU 6238  NZ  LYS C 158     4514   2987   2961    147    707    245       N  
ATOM   6239  N   MET C 159      -6.795 108.079  57.428  1.00 27.46           N  
ANISOU 6239  N   MET C 159     4628   3024   2781    252    756    204       N  
ATOM   6240  CA  MET C 159      -7.910 108.983  57.581  1.00 24.74           C  
ANISOU 6240  CA  MET C 159     4308   2694   2397    303    774    197       C  
ATOM   6241  C   MET C 159      -8.203 109.618  56.221  1.00 23.09           C  
ANISOU 6241  C   MET C 159     4120   2477   2174    354    787    192       C  
ATOM   6242  O   MET C 159      -7.353 110.317  55.690  1.00 23.05           O  
ANISOU 6242  O   MET C 159     4166   2419   2170    348    800    192       O  
ATOM   6243  CB  MET C 159      -7.547 110.040  58.628  1.00 25.56           C  
ANISOU 6243  CB  MET C 159     4472   2766   2472    298    785    190       C  
ATOM   6244  CG  MET C 159      -8.725 110.880  59.084  1.00 26.74           C  
ANISOU 6244  CG  MET C 159     4652   2932   2576    355    805    185       C  
ATOM   6245  SD  MET C 159      -8.245 111.943  60.470  1.00 28.59           S  
ANISOU 6245  SD  MET C 159     4956   3126   2777    336    818    173       S  
ATOM   6246  CE  MET C 159      -8.331 110.777  61.825  1.00 29.51           C  
ANISOU 6246  CE  MET C 159     5020   3288   2903    304    793    182       C  
ATOM   6247  N   PHE C 160      -9.386 109.327  55.670  1.00 23.58           N  
ANISOU 6247  N   PHE C 160     4140   2597   2220    403    786    184       N  
ATOM   6248  CA  PHE C 160      -9.831 109.723  54.329  1.00 23.73           C  
ANISOU 6248  CA  PHE C 160     4166   2634   2216    470    790    177       C  
ATOM   6249  C   PHE C 160     -10.898 110.823  54.413  1.00 26.55           C  
ANISOU 6249  C   PHE C 160     4560   3020   2508    564    809    170       C  
ATOM   6250  O   PHE C 160     -11.847 110.692  55.159  1.00 27.11           O  
ANISOU 6250  O   PHE C 160     4592   3148   2561    579    807    158       O  
ATOM   6251  CB  PHE C 160     -10.474 108.544  53.595  1.00 23.86           C  
ANISOU 6251  CB  PHE C 160     4094   2720   2251    465    772    158       C  
ATOM   6252  CG  PHE C 160      -9.571 107.364  53.297  1.00 23.54           C  
ANISOU 6252  CG  PHE C 160     4022   2655   2267    390    759    165       C  
ATOM   6253  CD1 PHE C 160      -9.385 106.356  54.225  1.00 23.45           C  
ANISOU 6253  CD1 PHE C 160     3980   2641   2287    323    758    170       C  
ATOM   6254  CD2 PHE C 160      -8.941 107.242  52.067  1.00 25.08           C  
ANISOU 6254  CD2 PHE C 160     4225   2827   2475    396    754    169       C  
ATOM   6255  CE1 PHE C 160      -8.579 105.267  53.944  1.00 23.61           C  
ANISOU 6255  CE1 PHE C 160     3983   2638   2350    270    751    180       C  
ATOM   6256  CE2 PHE C 160      -8.143 106.142  51.778  1.00 25.10           C  
ANISOU 6256  CE2 PHE C 160     4200   2809   2525    336    744    175       C  
ATOM   6257  CZ  PHE C 160      -7.951 105.164  52.728  1.00 24.31           C  
ANISOU 6257  CZ  PHE C 160     4074   2707   2454    275    743    181       C  
ATOM   6258  N   LYS C 161     -10.770 111.883  53.600  1.00 26.56           N  
ANISOU 6258  N   LYS C 161     4639   2982   2468    635    832    178       N  
ATOM   6259  CA  LYS C 161     -11.771 112.916  53.565  1.00 27.46           C  
ANISOU 6259  CA  LYS C 161     4800   3123   2510    746    853    175       C  
ATOM   6260  C   LYS C 161     -13.031 112.355  52.895  1.00 26.13           C  
ANISOU 6260  C   LYS C 161     4537   3077   2312    818    827    149       C  
ATOM   6261  O   LYS C 161     -13.017 111.867  51.756  1.00 26.07           O  
ANISOU 6261  O   LYS C 161     4493   3102   2309    837    810    139       O  
ATOM   6262  CB  LYS C 161     -11.265 114.179  52.847  1.00 29.50           C  
ANISOU 6262  CB  LYS C 161     5188   3294   2724    810    898    193       C  
ATOM   6263  CG  LYS C 161     -12.297 115.294  52.733  1.00 31.80           C  
ANISOU 6263  CG  LYS C 161     5548   3607   2925    951    928    197       C  
ATOM   6264  CD  LYS C 161     -11.732 116.642  52.297  1.00 36.84           C  
ANISOU 6264  CD  LYS C 161     6350   4129   3516   1004    995    219       C  
ATOM   6265  CE  LYS C 161     -10.976 117.325  53.416  1.00 40.43           C  
ANISOU 6265  CE  LYS C 161     6886   4484   3990    920   1034    219       C  
ATOM   6266  NZ  LYS C 161     -10.627 118.733  53.103  1.00 43.54           N  
ANISOU 6266  NZ  LYS C 161     7453   4761   4328    973   1117    233       N  
ATOM   6267  N   LYS C 162     -14.142 112.448  53.616  1.00 27.25           N  
ANISOU 6267  N   LYS C 162     4635   3295   2421    858    825    131       N  
ATOM   6268  CA  LYS C 162     -15.391 111.832  53.220  1.00 29.81           C  
ANISOU 6268  CA  LYS C 162     4846   3757   2723    905    801     89       C  
ATOM   6269  C   LYS C 162     -15.994 112.426  51.935  1.00 29.73           C  
ANISOU 6269  C   LYS C 162     4847   3811   2637   1046    796     77       C  
ATOM   6270  O   LYS C 162     -16.611 111.712  51.140  1.00 28.26           O  
ANISOU 6270  O   LYS C 162     4560   3731   2444   1065    767     35       O  
ATOM   6271  CB  LYS C 162     -16.403 111.986  54.349  1.00 31.28           C  
ANISOU 6271  CB  LYS C 162     4993   4009   2883    922    810     72       C  
ATOM   6272  CG  LYS C 162     -17.746 111.326  54.076  1.00 34.25           C  
ANISOU 6272  CG  LYS C 162     5233   4542   3237    953    792     14       C  
ATOM   6273  CD  LYS C 162     -17.654 109.843  53.799  1.00 39.10           C  
ANISOU 6273  CD  LYS C 162     5745   5191   3920    836    777    -18       C  
ATOM   6274  CE  LYS C 162     -18.794 109.059  54.426  1.00 42.55           C  
ANISOU 6274  CE  LYS C 162     6060   5740   4363    790    786    -73       C  
ATOM   6275  NZ  LYS C 162     -20.084 109.313  53.731  1.00 41.57           N  
ANISOU 6275  NZ  LYS C 162     5844   5779   4171    896    771   -135       N  
ATOM   6276  N   SER C 163     -15.880 113.739  51.745  1.00 30.54           N  
ANISOU 6276  N   SER C 163     5073   3853   2675   1152    828    107       N  
ATOM   6277  CA  SER C 163     -16.449 114.374  50.528  1.00 32.34           C  
ANISOU 6277  CA  SER C 163     5333   4138   2815   1313    828    102       C  
ATOM   6278  C   SER C 163     -15.805 113.795  49.262  1.00 31.39           C  
ANISOU 6278  C   SER C 163     5201   4005   2720   1292    811    101       C  
ATOM   6279  O   SER C 163     -16.452 113.652  48.200  1.00 34.05           O  
ANISOU 6279  O   SER C 163     5489   4445   3003   1393    786     73       O  
ATOM   6280  CB  SER C 163     -16.331 115.895  50.595  1.00 33.06           C  
ANISOU 6280  CB  SER C 163     5591   4138   2829   1428    883    143       C  
ATOM   6281  OG  SER C 163     -14.972 116.298  50.725  1.00 33.66           O  
ANISOU 6281  OG  SER C 163     5787   4048   2951   1340    925    181       O  
ATOM   6282  N   VAL C 164     -14.525 113.434  49.349  1.00 31.69           N  
ANISOU 6282  N   VAL C 164     5278   3926   2837   1166    822    127       N  
ATOM   6283  CA  VAL C 164     -13.850 112.848  48.199  1.00 30.53           C  
ANISOU 6283  CA  VAL C 164     5120   3760   2718   1140    808    128       C  
ATOM   6284  C   VAL C 164     -14.519 111.517  47.831  1.00 31.38           C  
ANISOU 6284  C   VAL C 164     5071   3997   2852   1101    757     76       C  
ATOM   6285  O   VAL C 164     -14.779 111.241  46.632  1.00 29.66           O  
ANISOU 6285  O   VAL C 164     4820   3846   2604   1164    735     53       O  
ATOM   6286  CB  VAL C 164     -12.346 112.638  48.432  1.00 31.84           C  
ANISOU 6286  CB  VAL C 164     5340   3791   2964   1008    828    159       C  
ATOM   6287  CG1 VAL C 164     -11.710 111.943  47.229  1.00 34.70           C  
ANISOU 6287  CG1 VAL C 164     5682   4146   3356    983    814    158       C  
ATOM   6288  CG2 VAL C 164     -11.620 113.941  48.726  1.00 34.94           C  
ANISOU 6288  CG2 VAL C 164     5885   4055   3333   1025    888    196       C  
ATOM   6289  N   ILE C 165     -14.761 110.689  48.855  1.00 30.24           N  
ANISOU 6289  N   ILE C 165     4840   3884   2766    993    744     55       N  
ATOM   6290  CA  ILE C 165     -15.445 109.395  48.688  1.00 30.89           C  
ANISOU 6290  CA  ILE C 165     4780   4078   2878    933    713     -2       C  
ATOM   6291  C   ILE C 165     -16.872 109.593  48.135  1.00 32.10           C  
ANISOU 6291  C   ILE C 165     4849   4396   2949   1053    691    -60       C  
ATOM   6292  O   ILE C 165     -17.253 108.884  47.222  1.00 32.24           O  
ANISOU 6292  O   ILE C 165     4781   4506   2961   1057    664   -111       O  
ATOM   6293  CB  ILE C 165     -15.435 108.633  50.028  1.00 30.43           C  
ANISOU 6293  CB  ILE C 165     4674   4002   2885    806    723     -6       C  
ATOM   6294  CG1 ILE C 165     -14.012 108.220  50.406  1.00 27.18           C  
ANISOU 6294  CG1 ILE C 165     4322   3456   2546    697    734     40       C  
ATOM   6295  CG2 ILE C 165     -16.380 107.438  49.984  1.00 31.37           C  
ANISOU 6295  CG2 ILE C 165     4655   4239   3023    747    711    -74       C  
ATOM   6296  CD1 ILE C 165     -13.817 107.920  51.871  1.00 26.46           C  
ANISOU 6296  CD1 ILE C 165     4234   3323   2495    611    749     56       C  
ATOM   6297  N   ASP C 166     -17.646 110.544  48.690  1.00 31.52           N  
ANISOU 6297  N   ASP C 166     4797   4367   2810   1153    703    -59       N  
ATOM   6298  CA  ASP C 166     -19.064 110.735  48.318  1.00 34.34           C  
ANISOU 6298  CA  ASP C 166     5060   4904   3084   1276    680   -121       C  
ATOM   6299  C   ASP C 166     -19.174 111.281  46.888  1.00 36.56           C  
ANISOU 6299  C   ASP C 166     5377   5234   3280   1430    662   -124       C  
ATOM   6300  O   ASP C 166     -19.930 110.746  46.085  1.00 38.95           O  
ANISOU 6300  O   ASP C 166     5564   5688   3547   1473    625   -193       O  
ATOM   6301  CB  ASP C 166     -19.815 111.677  49.260  1.00 35.70           C  
ANISOU 6301  CB  ASP C 166     5258   5107   3198   1361    700   -112       C  
ATOM   6302  CG  ASP C 166     -19.992 111.165  50.688  1.00 40.15           C  
ANISOU 6302  CG  ASP C 166     5772   5657   3826   1233    718   -119       C  
ATOM   6303  OD1 ASP C 166     -19.777 109.952  50.941  1.00 37.97           O  
ANISOU 6303  OD1 ASP C 166     5419   5376   3631   1084    715   -145       O  
ATOM   6304  OD2 ASP C 166     -20.316 111.991  51.547  1.00 42.03           O  
ANISOU 6304  OD2 ASP C 166     6061   5879   4028   1288    741    -97       O  
ATOM   6305  N   LYS C 167     -18.380 112.308  46.558  1.00 37.40           N  
ANISOU 6305  N   LYS C 167     5646   5210   3353   1508    693    -54       N  
ATOM   6306  CA  LYS C 167     -18.531 113.000  45.264  1.00 40.99           C  
ANISOU 6306  CA  LYS C 167     6165   5701   3709   1683    689    -47       C  
ATOM   6307  C   LYS C 167     -18.116 112.077  44.101  1.00 38.76           C  
ANISOU 6307  C   LYS C 167     5827   5442   3455   1638    657    -73       C  
ATOM   6308  O   LYS C 167     -18.676 112.140  43.012  1.00 38.08           O  
ANISOU 6308  O   LYS C 167     5709   5472   3288   1768    629   -108       O  
ATOM   6309  CB  LYS C 167     -17.766 114.327  45.290  1.00 43.33           C  
ANISOU 6309  CB  LYS C 167     6666   5830   3965   1761    750     34       C  
ATOM   6310  CG  LYS C 167     -18.375 115.417  44.418  1.00 52.71           C  
ANISOU 6310  CG  LYS C 167     7946   7069   5012   1996    766     46       C  
ATOM   6311  N   ASN C 168     -17.125 111.211  44.320  1.00 36.34           N  
ANISOU 6311  N   ASN C 168     5512   5034   3260   1462    662    -58       N  
ATOM   6312  CA  ASN C 168     -16.655 110.313  43.285  1.00 36.57           C  
ANISOU 6312  CA  ASN C 168     5498   5071   3323   1411    637    -80       C  
ATOM   6313  C   ASN C 168     -17.219 108.892  43.456  1.00 36.50           C  
ANISOU 6313  C   ASN C 168     5319   5174   3372   1287    602   -158       C  
ATOM   6314  O   ASN C 168     -16.782 108.038  42.774  1.00 33.19           O  
ANISOU 6314  O   ASN C 168     4866   4748   2994   1219    588   -177       O  
ATOM   6315  CB  ASN C 168     -15.124 110.302  43.228  1.00 38.17           C  
ANISOU 6315  CB  ASN C 168     5813   5089   3599   1316    671    -13       C  
ATOM   6316  CG  ASN C 168     -14.565 111.701  43.065  1.00 41.24           C  
ANISOU 6316  CG  ASN C 168     6375   5360   3933   1418    723     54       C  
ATOM   6317  OD1 ASN C 168     -14.640 112.280  41.975  1.00 44.84           O  
ANISOU 6317  OD1 ASN C 168     6900   5827   4308   1555    732     65       O  
ATOM   6318  ND2 ASN C 168     -14.061 112.273  44.149  1.00 34.60           N  
ANISOU 6318  ND2 ASN C 168     5610   4409   3126   1359    762     94       N  
ATOM   6319  N   LYS C 169     -18.157 108.654  44.387  1.00 39.11           N  
ANISOU 6319  N   LYS C 169     5553   5598   3708   1252    598   -204       N  
ATOM   6320  CA  LYS C 169     -18.814 107.345  44.563  1.00 37.38           C  
ANISOU 6320  CA  LYS C 169     5177   5488   3537   1131    581   -290       C  
ATOM   6321  C   LYS C 169     -17.774 106.226  44.734  1.00 36.78           C  
ANISOU 6321  C   LYS C 169     5113   5288   3571    955    598   -269       C  
ATOM   6322  O   LYS C 169     -17.870 105.182  44.113  1.00 36.55           O  
ANISOU 6322  O   LYS C 169     5005   5310   3569    884    585   -325       O  
ATOM   6323  CB  LYS C 169     -19.723 107.056  43.364  1.00 42.72           C  
ANISOU 6323  CB  LYS C 169     5742   6348   4142   1217    538   -380       C  
ATOM   6324  CG  LYS C 169     -21.016 107.853  43.322  1.00 45.31           C  
ANISOU 6324  CG  LYS C 169     6005   6850   4358   1380    516   -429       C  
ATOM   6325  CD  LYS C 169     -22.081 107.226  42.423  1.00 47.17           C  
ANISOU 6325  CD  LYS C 169     6074   7310   4539   1417    471   -553       C  
ATOM   6326  N   ILE C 170     -16.765 106.449  45.584  1.00 34.92           N  
ANISOU 6326  N   ILE C 170     4979   4894   3392    890    628   -190       N  
ATOM   6327  CA  ILE C 170     -15.739 105.455  45.834  1.00 32.17           C  
ANISOU 6327  CA  ILE C 170     4651   4435   3137    745    644   -164       C  
ATOM   6328  C   ILE C 170     -16.282 104.413  46.813  1.00 34.28           C  
ANISOU 6328  C   ILE C 170     4832   4735   3456    619    663   -207       C  
ATOM   6329  O   ILE C 170     -16.730 104.764  47.927  1.00 32.65           O  
ANISOU 6329  O   ILE C 170     4623   4535   3246    613    681   -200       O  
ATOM   6330  CB  ILE C 170     -14.447 106.102  46.356  1.00 31.77           C  
ANISOU 6330  CB  ILE C 170     4730   4222   3118    731    665    -75       C  
ATOM   6331  CG1 ILE C 170     -13.940 107.203  45.414  1.00 33.59           C  
ANISOU 6331  CG1 ILE C 170     5059   4408   3294    849    665    -35       C  
ATOM   6332  CG2 ILE C 170     -13.395 105.033  46.568  1.00 31.75           C  
ANISOU 6332  CG2 ILE C 170     4737   4125   3201    600    677    -53       C  
ATOM   6333  CD1 ILE C 170     -12.670 107.864  45.883  1.00 34.30           C  
ANISOU 6333  CD1 ILE C 170     5269   4346   3415    819    696     35       C  
ATOM   6334  N   LYS C 171     -16.217 103.140  46.404  1.00 33.93           N  
ANISOU 6334  N   LYS C 171     4730   4702   3458    518    669   -251       N  
ATOM   6335  CA  LYS C 171     -16.746 102.018  47.200  1.00 34.47           C  
ANISOU 6335  CA  LYS C 171     4728   4793   3575    389    704   -299       C  
ATOM   6336  C   LYS C 171     -15.738 100.873  47.165  1.00 30.99           C  
ANISOU 6336  C   LYS C 171     4330   4237   3206    276    729   -273       C  
ATOM   6337  O   LYS C 171     -15.004 100.702  46.197  1.00 28.53           O  
ANISOU 6337  O   LYS C 171     4051   3886   2902    291    711   -257       O  
ATOM   6338  CB  LYS C 171     -18.079 101.492  46.649  1.00 36.45           C  
ANISOU 6338  CB  LYS C 171     4841   5214   3795    377    699   -415       C  
ATOM   6339  CG  LYS C 171     -19.230 102.491  46.660  1.00 42.32           C  
ANISOU 6339  CG  LYS C 171     5517   6104   4456    498    674   -457       C  
ATOM   6340  CD  LYS C 171     -20.482 101.997  45.933  1.00 43.81           C  
ANISOU 6340  CD  LYS C 171     5553   6488   4604    498    659   -585       C  
ATOM   6341  N   PHE C 172     -15.743 100.067  48.217  1.00 28.64           N  
ANISOU 6341  N   PHE C 172     4036   3888   2955    170    776   -270       N  
ATOM   6342  CA  PHE C 172     -14.991  98.846  48.199  1.00 29.95           C  
ANISOU 6342  CA  PHE C 172     4239   3960   3178     69    810   -257       C  
ATOM   6343  C   PHE C 172     -15.673  97.880  47.220  1.00 31.42           C  
ANISOU 6343  C   PHE C 172     4341   4229   3367     10    821   -353       C  
ATOM   6344  O   PHE C 172     -16.888  97.843  47.154  1.00 31.57           O  
ANISOU 6344  O   PHE C 172     4260   4374   3359     -1    827   -439       O  
ATOM   6345  CB  PHE C 172     -14.888  98.259  49.608  1.00 29.58           C  
ANISOU 6345  CB  PHE C 172     4231   3839   3167    -12    865   -227       C  
ATOM   6346  CG  PHE C 172     -14.081  99.086  50.576  1.00 27.86           C  
ANISOU 6346  CG  PHE C 172     4098   3540   2948     35    852   -138       C  
ATOM   6347  CD1 PHE C 172     -14.670 100.121  51.291  1.00 28.39           C  
ANISOU 6347  CD1 PHE C 172     4154   3652   2979     92    841   -132       C  
ATOM   6348  CD2 PHE C 172     -12.741  98.813  50.780  1.00 26.72           C  
ANISOU 6348  CD2 PHE C 172     4037   3280   2832     24    852    -69       C  
ATOM   6349  CE1 PHE C 172     -13.919 100.856  52.192  1.00 28.34           C  
ANISOU 6349  CE1 PHE C 172     4226   3571   2970    126    833    -60       C  
ATOM   6350  CE2 PHE C 172     -11.994  99.547  51.684  1.00 25.63           C  
ANISOU 6350  CE2 PHE C 172     3965   3082   2690     61    839     -2       C  
ATOM   6351  CZ  PHE C 172     -12.582 100.578  52.374  1.00 26.81           C  
ANISOU 6351  CZ  PHE C 172     4107   3271   2806    108    830      0       C  
ATOM   6352  N   LYS C 173     -14.866  97.141  46.453  1.00 32.78           N  
ANISOU 6352  N   LYS C 173     4550   4334   3568    -23    823   -342       N  
ATOM   6353  CA  LYS C 173     -15.327  96.151  45.490  1.00 39.82           C  
ANISOU 6353  CA  LYS C 173     5379   5284   4466    -88    838   -432       C  
ATOM   6354  C   LYS C 173     -15.311  94.773  46.163  1.00 41.44           C  
ANISOU 6354  C   LYS C 173     5611   5410   4722   -228    920   -450       C  
ATOM   6355  O   LYS C 173     -14.575  94.556  47.124  1.00 38.74           O  
ANISOU 6355  O   LYS C 173     5358   4949   4410   -250    953   -371       O  
ATOM   6356  CB  LYS C 173     -14.413  96.132  44.258  1.00 43.21           C  
ANISOU 6356  CB  LYS C 173     5849   5675   4893    -39    800   -405       C  
ATOM   6357  CG  LYS C 173     -14.785  97.098  43.144  1.00 43.27           C  
ANISOU 6357  CG  LYS C 173     5810   5793   4838     81    735   -434       C  
ATOM   6358  CD  LYS C 173     -14.941  98.510  43.588  1.00 45.84           C  
ANISOU 6358  CD  LYS C 173     6153   6145   5120    194    702   -386       C  
ATOM   6359  N   THR C 174     -16.120  93.849  45.642  1.00 51.13           N  
ANISOU 6359  N   THR C 174     6766   6706   5955   -320    958   -558       N  
ATOM   6360  CA  THR C 174     -16.166  92.449  46.117  1.00 59.29           C  
ANISOU 6360  CA  THR C 174     7836   7655   7033   -464   1054   -588       C  
ATOM   6361  C   THR C 174     -15.610  91.508  45.031  1.00 70.65           C  
ANISOU 6361  C   THR C 174     9306   9046   8491   -507   1067   -614       C  
ATOM   6362  O   THR C 174     -16.129  90.410  44.847  1.00 77.24           O  
ANISOU 6362  O   THR C 174    10121   9883   9344   -629   1138   -701       O  
ATOM   6363  CB  THR C 174     -17.596  92.076  46.524  1.00 58.60           C  
ANISOU 6363  CB  THR C 174     7646   7677   6941   -562   1111   -704       C  
ATOM   6364  OG1 THR C 174     -18.508  92.517  45.519  1.00 60.82           O  
ANISOU 6364  OG1 THR C 174     7791   8138   7179   -525   1055   -810       O  
ATOM   6365  CG2 THR C 174     -18.027  92.703  47.829  1.00 63.90           C  
ANISOU 6365  CG2 THR C 174     8316   8356   7604   -543   1128   -668       C  
ATOM   6366  N   PHE C 175     -14.570  91.958  44.306  1.00 82.17           N  
ANISOU 6366  N   PHE C 175    10815  10461   9943   -412   1004   -543       N  
ATOM   6367  CA  PHE C 175     -13.964  91.221  43.164  1.00 81.22           C  
ANISOU 6367  CA  PHE C 175    10725  10301   9834   -430   1003   -559       C  
ATOM   6368  C   PHE C 175     -13.167  90.039  43.720  1.00 81.73           C  
ANISOU 6368  C   PHE C 175    10905  10204   9941   -509   1085   -509       C  
ATOM   6369  O   PHE C 175     -13.267  88.918  43.219  1.00 83.84           O  
ANISOU 6369  O   PHE C 175    11190  10440  10226   -598   1143   -569       O  
ATOM   6370  CB  PHE C 175     -13.062  92.123  42.308  1.00 73.17           C  
ANISOU 6370  CB  PHE C 175     9731   9278   8792   -301    920   -491       C  
ATOM   6371  N   SER C 176     -12.397  90.322  44.776  1.00 75.02           N  
ANISOU 6371  N   SER C 176    10139   9259   9104   -468   1092   -402       N  
ATOM   6372  CA  SER C 176     -11.557  89.343  45.452  1.00 72.11           C  
ANISOU 6372  CA  SER C 176     9892   8743   8763   -506   1163   -338       C  
ATOM   6373  C   SER C 176     -11.350  89.779  46.905  1.00 66.21           C  
ANISOU 6373  C   SER C 176     9192   7950   8013   -475   1176   -261       C  
ATOM   6374  O   SER C 176     -11.557  90.941  47.233  1.00 67.57           O  
ANISOU 6374  O   SER C 176     9315   8190   8168   -411   1115   -241       O  
ATOM   6375  CB  SER C 176     -10.239  89.170  44.734  1.00 71.26           C  
ANISOU 6375  CB  SER C 176     9852   8561   8662   -444   1133   -272       C  
ATOM   6376  OG  SER C 176      -9.578  90.416  44.543  1.00 62.00           O  
ANISOU 6376  OG  SER C 176     8662   7419   7474   -333   1044   -209       O  
ATOM   6377  N   LYS C 177     -10.946  88.834  47.762  1.00 68.84           N  
ANISOU 6377  N   LYS C 177     9628   8167   8357   -515   1257   -218       N  
ATOM   6378  CA  LYS C 177     -10.599  89.169  49.139  1.00 70.08           C  
ANISOU 6378  CA  LYS C 177     9844   8277   8506   -473   1267   -139       C  
ATOM   6379  C   LYS C 177      -9.335  90.033  49.090  1.00 69.36           C  
ANISOU 6379  C   LYS C 177     9774   8172   8405   -356   1180    -49       C  
ATOM   6380  O   LYS C 177      -9.318  91.172  49.612  1.00 77.19           O  
ANISOU 6380  O   LYS C 177    10733   9212   9384   -298   1122    -19       O  
ATOM   6381  CB  LYS C 177     -10.413  87.915  50.000  1.00 74.26           C  
ANISOU 6381  CB  LYS C 177    10494   8683   9037   -525   1380   -111       C  
ATOM   6382  N   THR C 178      -8.324  89.512  48.381  1.00 57.04           N  
ANISOU 6382  N   THR C 178     8263   6554   6852   -329   1173    -18       N  
ATOM   6383  CA  THR C 178      -7.014  90.138  48.246  1.00 55.88           C  
ANISOU 6383  CA  THR C 178     8138   6392   6700   -233   1105     56       C  
ATOM   6384  C   THR C 178      -7.132  91.439  47.424  1.00 60.68           C  
ANISOU 6384  C   THR C 178     8660   7090   7305   -187   1019     37       C  
ATOM   6385  O   THR C 178      -7.862  91.515  46.400  1.00 59.63           O  
ANISOU 6385  O   THR C 178     8464   7020   7172   -212   1005    -30       O  
ATOM   6386  CB  THR C 178      -5.993  89.173  47.622  1.00 50.18           C  
ANISOU 6386  CB  THR C 178     7487   5594   5986   -217   1128     86       C  
ATOM   6387  N   ALA C 179      -6.421  92.464  47.902  1.00 48.52           N  
ANISOU 6387  N   ALA C 179     7122   5558   5755   -118    966     93       N  
ATOM   6388  CA  ALA C 179      -6.132  93.686  47.167  1.00 49.69           C  
ANISOU 6388  CA  ALA C 179     7226   5756   5896    -60    897     97       C  
ATOM   6389  C   ALA C 179      -7.356  94.615  47.046  1.00 42.63           C  
ANISOU 6389  C   ALA C 179     6263   4951   4984    -57    873     47       C  
ATOM   6390  O   ALA C 179      -7.296  95.601  46.316  1.00 43.81           O  
ANISOU 6390  O   ALA C 179     6385   5140   5117     -4    827     44       O  
ATOM   6391  CB  ALA C 179      -5.574  93.349  45.801  1.00 51.78           C  
ANISOU 6391  CB  ALA C 179     7491   6010   6170    -48    884     88       C  
ATOM   6392  N   GLU C 180      -8.459  94.323  47.727  1.00 39.45           N  
ANISOU 6392  N   GLU C 180     5834   4577   4576   -106    909      7       N  
ATOM   6393  CA  GLU C 180      -9.627  95.214  47.703  1.00 44.96           C  
ANISOU 6393  CA  GLU C 180     6460   5371   5249    -91    886    -40       C  
ATOM   6394  C   GLU C 180      -9.305  96.505  48.461  1.00 40.95           C  
ANISOU 6394  C   GLU C 180     5970   4865   4723    -25    849     10       C  
ATOM   6395  O   GLU C 180      -9.830  97.571  48.118  1.00 34.94           O  
ANISOU 6395  O   GLU C 180     5172   4170   3934     28    814     -7       O  
ATOM   6396  CB  GLU C 180     -10.853  94.551  48.329  1.00 52.84           C  
ANISOU 6396  CB  GLU C 180     7421   6405   6248   -168    942   -100       C  
ATOM   6397  CG  GLU C 180     -11.897  94.141  47.306  1.00 61.30           C  
ANISOU 6397  CG  GLU C 180     8412   7566   7314   -211    949   -198       C  
ATOM   6398  CD  GLU C 180     -11.393  93.540  46.002  1.00 60.43           C  
ANISOU 6398  CD  GLU C 180     8307   7439   7213   -217    939   -218       C  
ATOM   6399  OE2 GLU C 180     -12.165  93.542  45.008  1.00 59.82           O  
ANISOU 6399  OE2 GLU C 180     8152   7457   7117   -221    920   -299       O  
ATOM   6400  N   ASP C 181      -8.460  96.384  49.492  1.00 36.82           N  
ANISOU 6400  N   ASP C 181     5507   4272   4210    -25    861     70       N  
ATOM   6401  CA  ASP C 181      -8.027  97.530  50.274  1.00 35.63           C  
ANISOU 6401  CA  ASP C 181     5377   4117   4042     23    831    112       C  
ATOM   6402  C   ASP C 181      -7.090  98.400  49.421  1.00 31.22           C  
ANISOU 6402  C   ASP C 181     4831   3548   3481     77    788    136       C  
ATOM   6403  O   ASP C 181      -7.190  99.635  49.439  1.00 29.25           O  
ANISOU 6403  O   ASP C 181     4581   3321   3209    123    763    140       O  
ATOM   6404  CB  ASP C 181      -7.399  97.099  51.600  1.00 37.84           C  
ANISOU 6404  CB  ASP C 181     5710   4340   4325     11    853    159       C  
ATOM   6405  CG  ASP C 181      -6.134  96.270  51.467  1.00 48.48           C  
ANISOU 6405  CG  ASP C 181     7106   5625   5688     14    859    198       C  
ATOM   6406  OD1 ASP C 181      -6.002  95.551  50.422  1.00 54.50           O  
ANISOU 6406  OD1 ASP C 181     7863   6374   6467     -2    870    181       O  
ATOM   6407  OD2 ASP C 181      -5.283  96.342  52.407  1.00 49.75           O  
ANISOU 6407  OD2 ASP C 181     7305   5757   5838     40    853    241       O  
ATOM   6408  N   GLN C 182      -6.190  97.762  48.662  1.00 28.37           N  
ANISOU 6408  N   GLN C 182     4488   3148   3140     72    787    150       N  
ATOM   6409  CA  GLN C 182      -5.267  98.478  47.791  1.00 28.04           C  
ANISOU 6409  CA  GLN C 182     4460   3093   3099    113    759    169       C  
ATOM   6410  C   GLN C 182      -6.050  99.279  46.760  1.00 25.34           C  
ANISOU 6410  C   GLN C 182     4091   2804   2733    153    741    134       C  
ATOM   6411  O   GLN C 182      -5.668 100.399  46.470  1.00 24.78           O  
ANISOU 6411  O   GLN C 182     4043   2726   2644    199    727    151       O  
ATOM   6412  CB  GLN C 182      -4.326  97.551  47.032  1.00 33.52           C  
ANISOU 6412  CB  GLN C 182     5171   3747   3817    102    766    182       C  
ATOM   6413  CG  GLN C 182      -3.140  97.056  47.834  1.00 36.64           C  
ANISOU 6413  CG  GLN C 182     5601   4096   4225     99    772    226       C  
ATOM   6414  CD  GLN C 182      -2.329  96.113  46.972  1.00 42.98           C  
ANISOU 6414  CD  GLN C 182     6418   4866   5045     98    782    235       C  
ATOM   6415  OE1 GLN C 182      -2.089  94.975  47.354  1.00 44.46           O  
ANISOU 6415  OE1 GLN C 182     6633   5019   5237     84    810    249       O  
ATOM   6416  NE2 GLN C 182      -1.957  96.552  45.772  1.00 37.14           N  
ANISOU 6416  NE2 GLN C 182     5669   4131   4309    119    766    228       N  
ATOM   6417  N   LEU C 183      -7.090  98.667  46.177  1.00 24.32           N  
ANISOU 6417  N   LEU C 183     3917   2727   2596    137    748     84       N  
ATOM   6418  CA  LEU C 183      -7.830  99.290  45.098  1.00 24.20           C  
ANISOU 6418  CA  LEU C 183     3869   2778   2545    191    727     45       C  
ATOM   6419  C   LEU C 183      -8.539 100.552  45.594  1.00 27.17           C  
ANISOU 6419  C   LEU C 183     4242   3198   2882    247    714     43       C  
ATOM   6420  O   LEU C 183      -8.570 101.562  44.910  1.00 26.07           O  
ANISOU 6420  O   LEU C 183     4123   3075   2705    323    699     48       O  
ATOM   6421  CB  LEU C 183      -8.841  98.300  44.537  1.00 24.21           C  
ANISOU 6421  CB  LEU C 183     3809   2844   2545    152    736    -23       C  
ATOM   6422  CG  LEU C 183      -9.818  98.882  43.519  1.00 24.27           C  
ANISOU 6422  CG  LEU C 183     3764   2954   2502    217    708    -79       C  
ATOM   6423  CD1 LEU C 183      -9.117  99.563  42.366  1.00 24.34           C  
ANISOU 6423  CD1 LEU C 183     3814   2944   2488    295    685    -52       C  
ATOM   6424  CD2 LEU C 183     -10.744  97.803  43.020  1.00 25.30           C  
ANISOU 6424  CD2 LEU C 183     3821   3156   2633    160    719   -162       C  
ATOM   6425  N   PHE C 184      -9.125 100.476  46.792  1.00 26.72           N  
ANISOU 6425  N   PHE C 184     4168   3155   2827    216    728     38       N  
ATOM   6426  CA  PHE C 184      -9.829 101.587  47.365  1.00 25.20           C  
ANISOU 6426  CA  PHE C 184     3975   3004   2596    267    721     36       C  
ATOM   6427  C   PHE C 184      -8.851 102.755  47.553  1.00 23.24           C  
ANISOU 6427  C   PHE C 184     3801   2688   2339    311    716     90       C  
ATOM   6428  O   PHE C 184      -9.169 103.891  47.220  1.00 22.92           O  
ANISOU 6428  O   PHE C 184     3785   2667   2254    387    710     91       O  
ATOM   6429  CB  PHE C 184     -10.491 101.158  48.679  1.00 25.27           C  
ANISOU 6429  CB  PHE C 184     3958   3028   2615    215    744     25       C  
ATOM   6430  CG  PHE C 184     -11.329 102.241  49.316  1.00 25.31           C  
ANISOU 6430  CG  PHE C 184     3956   3083   2578    269    740     19       C  
ATOM   6431  CD1 PHE C 184     -10.757 103.164  50.173  1.00 26.75           C  
ANISOU 6431  CD1 PHE C 184     4199   3209   2752    293    739     66       C  
ATOM   6432  CD2 PHE C 184     -12.678 102.364  49.024  1.00 26.62           C  
ANISOU 6432  CD2 PHE C 184     4050   3358   2707    301    736    -40       C  
ATOM   6433  CE1 PHE C 184     -11.514 104.166  50.745  1.00 25.67           C  
ANISOU 6433  CE1 PHE C 184     4067   3111   2574    347    740     61       C  
ATOM   6434  CE2 PHE C 184     -13.432 103.376  49.588  1.00 26.48           C  
ANISOU 6434  CE2 PHE C 184     4028   3388   2644    365    733    -43       C  
ATOM   6435  CZ  PHE C 184     -12.844 104.281  50.436  1.00 26.79           C  
ANISOU 6435  CZ  PHE C 184     4143   3357   2678    389    737     10       C  
ATOM   6436  N   THR C 185      -7.672 102.476  48.127  1.00 22.08           N  
ANISOU 6436  N   THR C 185     3692   2466   2229    265    723    130       N  
ATOM   6437  CA  THR C 185      -6.664 103.519  48.359  1.00 22.83           C  
ANISOU 6437  CA  THR C 185     3849   2504   2321    284    724    166       C  
ATOM   6438  C   THR C 185      -6.188 104.141  47.034  1.00 24.40           C  
ANISOU 6438  C   THR C 185     4081   2682   2504    332    725    171       C  
ATOM   6439  O   THR C 185      -6.078 105.374  46.899  1.00 21.79           O  
ANISOU 6439  O   THR C 185     3805   2328   2142    379    737    181       O  
ATOM   6440  CB  THR C 185      -5.498 102.984  49.194  1.00 23.38           C  
ANISOU 6440  CB  THR C 185     3933   2522   2426    228    726    194       C  
ATOM   6441  OG1 THR C 185      -6.019 102.596  50.465  1.00 26.40           O  
ANISOU 6441  OG1 THR C 185     4300   2919   2808    202    731    194       O  
ATOM   6442  CG2 THR C 185      -4.433 104.026  49.441  1.00 23.72           C  
ANISOU 6442  CG2 THR C 185     4024   2520   2467    232    729    214       C  
ATOM   6443  N   ILE C 186      -5.956 103.281  46.034  1.00 23.85           N  
ANISOU 6443  N   ILE C 186     3990   2618   2453    322    719    162       N  
ATOM   6444  CA  ILE C 186      -5.568 103.747  44.708  1.00 24.91           C  
ANISOU 6444  CA  ILE C 186     4156   2736   2569    371    723    166       C  
ATOM   6445  C   ILE C 186      -6.654 104.665  44.131  1.00 23.76           C  
ANISOU 6445  C   ILE C 186     4023   2643   2360    463    721    146       C  
ATOM   6446  O   ILE C 186      -6.320 105.751  43.649  1.00 23.04           O  
ANISOU 6446  O   ILE C 186     4002   2513   2237    520    741    166       O  
ATOM   6447  CB  ILE C 186      -5.267 102.568  43.762  1.00 25.55           C  
ANISOU 6447  CB  ILE C 186     4207   2822   2676    347    716    154       C  
ATOM   6448  CG1 ILE C 186      -4.018 101.803  44.198  1.00 28.98           C  
ANISOU 6448  CG1 ILE C 186     4646   3201   3161    282    723    181       C  
ATOM   6449  CG2 ILE C 186      -5.188 103.046  42.314  1.00 23.63           C  
ANISOU 6449  CG2 ILE C 186     3994   2583   2401    413    718    151       C  
ATOM   6450  CD1 ILE C 186      -2.732 102.506  43.910  1.00 31.57           C  
ANISOU 6450  CD1 ILE C 186     5021   3472   3499    285    737    210       C  
ATOM   6451  N   GLU C 187      -7.924 104.240  44.160  1.00 25.12           N  
ANISOU 6451  N   GLU C 187     4130   2904   2510    480    702    105       N  
ATOM   6452  CA  GLU C 187      -9.038 105.061  43.611  1.00 26.74           C  
ANISOU 6452  CA  GLU C 187     4332   3184   2642    586    693     79       C  
ATOM   6453  C   GLU C 187      -9.084 106.421  44.328  1.00 26.75           C  
ANISOU 6453  C   GLU C 187     4404   3150   2608    638    714    109       C  
ATOM   6454  O   GLU C 187      -9.252 107.499  43.670  1.00 25.08           O  
ANISOU 6454  O   GLU C 187     4260   2933   2334    741    729    121       O  
ATOM   6455  CB  GLU C 187     -10.382 104.332  43.660  1.00 28.04           C  
ANISOU 6455  CB  GLU C 187     4394   3467   2790    583    670     16       C  
ATOM   6456  CG  GLU C 187     -10.390 103.101  42.759  1.00 31.71           C  
ANISOU 6456  CG  GLU C 187     4802   3967   3279    538    657    -23       C  
ATOM   6457  CD  GLU C 187     -11.704 102.367  42.546  1.00 34.81           C  
ANISOU 6457  CD  GLU C 187     5086   4487   3651    526    641   -105       C  
ATOM   6458  OE1 GLU C 187     -12.527 102.352  43.442  1.00 42.28           O  
ANISOU 6458  OE1 GLU C 187     5985   5485   4594    503    646   -132       O  
ATOM   6459  OE2 GLU C 187     -11.898 101.816  41.451  1.00 47.48           O  
ANISOU 6459  OE2 GLU C 187     6653   6145   5241    537    625   -149       O  
ATOM   6460  N   PHE C 188      -8.877 106.388  45.647  1.00 25.54           N  
ANISOU 6460  N   PHE C 188     4249   2964   2489    571    722    123       N  
ATOM   6461  CA  PHE C 188      -8.865 107.617  46.468  1.00 25.55           C  
ANISOU 6461  CA  PHE C 188     4320   2925   2463    603    745    146       C  
ATOM   6462  C   PHE C 188      -7.681 108.521  46.061  1.00 26.32           C  
ANISOU 6462  C   PHE C 188     4520   2920   2560    610    780    181       C  
ATOM   6463  O   PHE C 188      -7.879 109.759  45.843  1.00 26.96           O  
ANISOU 6463  O   PHE C 188     4687   2972   2585    690    812    194       O  
ATOM   6464  CB  PHE C 188      -8.821 107.308  47.966  1.00 25.19           C  
ANISOU 6464  CB  PHE C 188     4250   2868   2453    526    743    150       C  
ATOM   6465  CG  PHE C 188      -9.089 108.521  48.823  1.00 25.06           C  
ANISOU 6465  CG  PHE C 188     4292   2829   2398    565    764    163       C  
ATOM   6466  CD1 PHE C 188      -8.080 109.430  49.108  1.00 24.78           C  
ANISOU 6466  CD1 PHE C 188     4345   2702   2366    548    794    188       C  
ATOM   6467  CD2 PHE C 188     -10.376 108.805  49.256  1.00 25.25           C  
ANISOU 6467  CD2 PHE C 188     4286   2928   2378    622    759    142       C  
ATOM   6468  CE1 PHE C 188      -8.351 110.588  49.833  1.00 25.64           C  
ANISOU 6468  CE1 PHE C 188     4521   2783   2435    584    820    195       C  
ATOM   6469  CE2 PHE C 188     -10.645 109.953  49.994  1.00 25.74           C  
ANISOU 6469  CE2 PHE C 188     4413   2967   2400    668    781    154       C  
ATOM   6470  CZ  PHE C 188      -9.631 110.834  50.288  1.00 26.02           C  
ANISOU 6470  CZ  PHE C 188     4546   2901   2439    648    813    181       C  
ATOM   6471  N   LEU C 189      -6.467 107.947  46.012  1.00 24.62           N  
ANISOU 6471  N   LEU C 189     4302   2649   2402    527    783    195       N  
ATOM   6472  CA  LEU C 189      -5.245 108.702  45.652  1.00 24.51           C  
ANISOU 6472  CA  LEU C 189     4371   2545   2397    510    823    217       C  
ATOM   6473  C   LEU C 189      -5.416 109.353  44.290  1.00 24.02           C  
ANISOU 6473  C   LEU C 189     4374   2467   2283    603    850    224       C  
ATOM   6474  O   LEU C 189      -5.002 110.488  44.076  1.00 25.53           O  
ANISOU 6474  O   LEU C 189     4667   2586   2444    632    903    240       O  
ATOM   6475  CB  LEU C 189      -4.017 107.800  45.615  1.00 26.91           C  
ANISOU 6475  CB  LEU C 189     4637   2820   2764    422    815    222       C  
ATOM   6476  CG  LEU C 189      -3.437 107.391  46.964  1.00 26.94           C  
ANISOU 6476  CG  LEU C 189     4606   2820   2810    340    801    222       C  
ATOM   6477  CD1 LEU C 189      -2.432 106.259  46.744  1.00 27.65           C  
ANISOU 6477  CD1 LEU C 189     4649   2906   2950    283    785    226       C  
ATOM   6478  CD2 LEU C 189      -2.786 108.574  47.654  1.00 25.50           C  
ANISOU 6478  CD2 LEU C 189     4487   2582   2620    314    836    221       C  
ATOM   6479  N   MET C 190      -6.036 108.632  43.362  1.00 26.33           N  
ANISOU 6479  N   MET C 190     4615   2827   2559    650    819    209       N  
ATOM   6480  CA  MET C 190      -6.146 109.130  41.952  1.00 26.49           C  
ANISOU 6480  CA  MET C 190     4698   2842   2524    750    840    216       C  
ATOM   6481  C   MET C 190      -7.228 110.219  41.838  1.00 28.67           C  
ANISOU 6481  C   MET C 190     5033   3150   2710    881    854    216       C  
ATOM   6482  O   MET C 190      -7.407 110.820  40.750  1.00 28.88           O  
ANISOU 6482  O   MET C 190     5132   3171   2669    991    879    226       O  
ATOM   6483  CB  MET C 190      -6.467 107.967  41.010  1.00 25.22           C  
ANISOU 6483  CB  MET C 190     4456   2755   2370    759    797    190       C  
ATOM   6484  CG  MET C 190      -5.313 106.996  40.865  1.00 24.68           C  
ANISOU 6484  CG  MET C 190     4357   2642   2376    657    794    198       C  
ATOM   6485  SD  MET C 190      -3.834 107.767  40.199  1.00 26.25           S  
ANISOU 6485  SD  MET C 190     4662   2725   2586    645    857    235       S  
ATOM   6486  CE  MET C 190      -2.740 107.777  41.619  1.00 26.08           C  
ANISOU 6486  CE  MET C 190     4627   2645   2634    519    870    243       C  
ATOM   6487  N   ASN C 191      -7.967 110.445  42.936  1.00 27.72           N  
ANISOU 6487  N   ASN C 191     4884   3068   2580    880    841    205       N  
ATOM   6488  CA  ASN C 191      -9.079 111.404  43.005  1.00 28.51           C  
ANISOU 6488  CA  ASN C 191     5026   3212   2592   1009    851    202       C  
ATOM   6489  C   ASN C 191      -8.803 112.541  44.006  1.00 27.97           C  
ANISOU 6489  C   ASN C 191     5056   3055   2514    998    902    227       C  
ATOM   6490  O   ASN C 191      -9.684 113.329  44.314  1.00 27.93           O  
ANISOU 6490  O   ASN C 191     5091   3079   2442   1095    914    227       O  
ATOM   6491  CB  ASN C 191     -10.371 110.686  43.383  1.00 29.91           C  
ANISOU 6491  CB  ASN C 191     5075   3530   2757   1028    793    158       C  
ATOM   6492  CG  ASN C 191     -11.070 110.096  42.181  1.00 33.46           C  
ANISOU 6492  CG  ASN C 191     5457   4089   3164   1104    754    121       C  
ATOM   6493  OD1 ASN C 191     -11.551 110.824  41.322  1.00 45.57           O  
ANISOU 6493  OD1 ASN C 191     7046   5657   4609   1248    763    123       O  
ATOM   6494  ND2 ASN C 191     -11.170 108.784  42.127  1.00 34.89           N  
ANISOU 6494  ND2 ASN C 191     5522   4331   3401   1015    714     83       N  
ATOM   6495  N   SER C 192      -7.573 112.633  44.503  1.00 26.36           N  
ANISOU 6495  N   SER C 192     4891   2750   2373    883    934    241       N  
ATOM   6496  CA  SER C 192      -7.201 113.623  45.509  1.00 27.09           C  
ANISOU 6496  CA  SER C 192     5067   2760   2464    847    982    252       C  
ATOM   6497  C   SER C 192      -5.753 114.032  45.254  1.00 27.20           C  
ANISOU 6497  C   SER C 192     5160   2657   2516    763   1041    262       C  
ATOM   6498  O   SER C 192      -5.097 113.417  44.417  1.00 28.13           O  
ANISOU 6498  O   SER C 192     5251   2769   2667    732   1035    265       O  
ATOM   6499  CB  SER C 192      -7.358 113.040  46.898  1.00 28.21           C  
ANISOU 6499  CB  SER C 192     5119   2944   2655    759    940    235       C  
ATOM   6500  OG  SER C 192      -6.671 111.805  47.009  1.00 25.59           O  
ANISOU 6500  OG  SER C 192     4691   2632   2400    654    900    226       O  
ATOM   6501  N   LYS C 193      -5.251 115.034  45.979  1.00 28.59           N  
ANISOU 6501  N   LYS C 193     5427   2745   2688    720   1101    261       N  
ATOM   6502  CA  LYS C 193      -3.895 115.526  45.718  1.00 27.10           C  
ANISOU 6502  CA  LYS C 193     5314   2450   2532    632   1170    258       C  
ATOM   6503  C   LYS C 193      -3.146 115.968  46.975  1.00 26.98           C  
ANISOU 6503  C   LYS C 193     5309   2388   2555    512   1195    231       C  
ATOM   6504  O   LYS C 193      -1.919 116.091  46.909  1.00 26.53           O  
ANISOU 6504  O   LYS C 193     5265   2274   2541    409   1235    210       O  
ATOM   6505  CB  LYS C 193      -3.913 116.652  44.688  1.00 29.97           C  
ANISOU 6505  CB  LYS C 193     5840   2722   2825    724   1263    280       C  
ATOM   6506  CG  LYS C 193      -4.634 117.915  45.074  1.00 29.86           C  
ANISOU 6506  CG  LYS C 193     5957   2656   2732    813   1323    290       C  
ATOM   6507  CD  LYS C 193      -4.519 118.920  43.968  1.00 33.29           C  
ANISOU 6507  CD  LYS C 193     6565   2987   3095    906   1426    317       C  
ATOM   6508  CE  LYS C 193      -5.319 120.162  44.243  1.00 31.74           C  
ANISOU 6508  CE  LYS C 193     6517   2735   2804   1024   1492    334       C  
ATOM   6509  NZ  LYS C 193      -5.315 121.035  43.043  1.00 35.88           N  
ANISOU 6509  NZ  LYS C 193     7222   3165   3244   1145   1592    368       N  
ATOM   6510  N   ASN C 194      -3.859 116.194  48.085  1.00 26.68           N  
ANISOU 6510  N   ASN C 194     5257   2380   2497    526   1171    224       N  
ATOM   6511  CA  ASN C 194      -3.261 116.669  49.319  1.00 27.29           C  
ANISOU 6511  CA  ASN C 194     5348   2422   2598    425   1192    193       C  
ATOM   6512  C   ASN C 194      -3.135 115.478  50.271  1.00 27.54           C  
ANISOU 6512  C   ASN C 194     5231   2546   2686    355   1103    180       C  
ATOM   6513  O   ASN C 194      -4.138 115.025  50.875  1.00 27.11           O  
ANISOU 6513  O   ASN C 194     5119   2562   2618    402   1050    189       O  
ATOM   6514  CB  ASN C 194      -4.076 117.800  49.945  1.00 27.66           C  
ANISOU 6514  CB  ASN C 194     5499   2428   2579    490   1236    196       C  
ATOM   6515  CG  ASN C 194      -3.969 119.139  49.226  1.00 29.09           C  
ANISOU 6515  CG  ASN C 194     5862   2489   2702    543   1349    205       C  
ATOM   6516  OD1 ASN C 194      -3.347 119.250  48.177  1.00 29.53           O  
ANISOU 6516  OD1 ASN C 194     5969   2490   2761    537   1397    213       O  
ATOM   6517  ND2 ASN C 194      -4.526 120.182  49.832  1.00 28.54           N  
ANISOU 6517  ND2 ASN C 194     5900   2368   2573    591   1400    205       N  
ATOM   6518  N   TYR C 195      -1.901 114.994  50.440  1.00 27.01           N  
ANISOU 6518  N   TYR C 195     5106   2478   2676    246   1093    155       N  
ATOM   6519  CA  TYR C 195      -1.641 113.809  51.261  1.00 26.32           C  
ANISOU 6519  CA  TYR C 195     4891   2473   2634    192   1015    147       C  
ATOM   6520  C   TYR C 195      -0.653 114.176  52.367  1.00 28.16           C  
ANISOU 6520  C   TYR C 195     5115   2698   2886     91   1024    103       C  
ATOM   6521  O   TYR C 195       0.352 114.851  52.084  1.00 30.33           O  
ANISOU 6521  O   TYR C 195     5433   2917   3171     22   1081     69       O  
ATOM   6522  CB  TYR C 195      -1.032 112.688  50.420  1.00 24.80           C  
ANISOU 6522  CB  TYR C 195     4622   2313   2486    173    982    157       C  
ATOM   6523  CG  TYR C 195      -1.562 112.522  49.020  1.00 24.00           C  
ANISOU 6523  CG  TYR C 195     4546   2204   2368    252    993    186       C  
ATOM   6524  CD1 TYR C 195      -2.918 112.363  48.750  1.00 23.37           C  
ANISOU 6524  CD1 TYR C 195     4464   2166   2250    350    968    207       C  
ATOM   6525  CD2 TYR C 195      -0.686 112.448  47.958  1.00 23.62           C  
ANISOU 6525  CD2 TYR C 195     4513   2120   2340    230   1023    186       C  
ATOM   6526  CE1 TYR C 195      -3.374 112.118  47.457  1.00 22.44           C  
ANISOU 6526  CE1 TYR C 195     4353   2060   2111    425    968    224       C  
ATOM   6527  CE2 TYR C 195      -1.127 112.208  46.666  1.00 23.72           C  
ANISOU 6527  CE2 TYR C 195     4544   2132   2334    305   1027    211       C  
ATOM   6528  CZ  TYR C 195      -2.475 112.047  46.407  1.00 23.90           C  
ANISOU 6528  CZ  TYR C 195     4562   2203   2315    406    997    228       C  
ATOM   6529  OH  TYR C 195      -2.858 111.854  45.100  1.00 24.67           O  
ANISOU 6529  OH  TYR C 195     4675   2310   2385    484    999    244       O  
ATOM   6530  N   SER C 196      -0.969 113.795  53.609  1.00 26.92           N  
ANISOU 6530  N   SER C 196     4904   2596   2728     81    975     96       N  
ATOM   6531  CA  SER C 196      -0.143 114.113  54.754  1.00 28.54           C  
ANISOU 6531  CA  SER C 196     5092   2812   2938      0    973     49       C  
ATOM   6532  C   SER C 196       0.313 112.821  55.443  1.00 28.28           C  
ANISOU 6532  C   SER C 196     4942   2867   2933    -23    897     49       C  
ATOM   6533  O   SER C 196      -0.397 111.818  55.438  1.00 26.77           O  
ANISOU 6533  O   SER C 196     4704   2719   2747     29    852     89       O  
ATOM   6534  CB  SER C 196      -0.877 115.017  55.711  1.00 31.39           C  
ANISOU 6534  CB  SER C 196     5520   3150   3256     18    993     39       C  
ATOM   6535  OG  SER C 196      -1.011 116.320  55.148  1.00 40.95           O  
ANISOU 6535  OG  SER C 196     6856   4266   4435     30   1078     31       O  
ATOM   6536  N   ILE C 197       1.494 112.876  56.063  1.00 26.98           N  
ANISOU 6536  N   ILE C 197     4736   2732   2780   -100    889      0       N  
ATOM   6537  CA  ILE C 197       2.096 111.756  56.729  1.00 27.06           C  
ANISOU 6537  CA  ILE C 197     4648   2829   2805   -109    824     -4       C  
ATOM   6538  C   ILE C 197       2.529 112.234  58.119  1.00 29.24           C  
ANISOU 6538  C   ILE C 197     4911   3145   3054   -152    809    -57       C  
ATOM   6539  O   ILE C 197       3.322 113.126  58.213  1.00 27.81           O  
ANISOU 6539  O   ILE C 197     4746   2949   2871   -226    846   -119       O  
ATOM   6540  CB  ILE C 197       3.289 111.192  55.923  1.00 28.87           C  
ANISOU 6540  CB  ILE C 197     4817   3083   3069   -145    820    -19       C  
ATOM   6541  CG1 ILE C 197       2.880 110.750  54.519  1.00 27.51           C  
ANISOU 6541  CG1 ILE C 197     4662   2869   2919   -102    835     28       C  
ATOM   6542  CG2 ILE C 197       3.968 110.050  56.681  1.00 31.99           C  
ANISOU 6542  CG2 ILE C 197     5116   3573   3465   -137    753    -24       C  
ATOM   6543  CD1 ILE C 197       4.052 110.539  53.539  1.00 29.43           C  
ANISOU 6543  CD1 ILE C 197     4871   3114   3196   -144    854     10       C  
ATOM   6544  N   LYS C 198       2.038 111.582  59.173  1.00 27.49           N  
ANISOU 6544  N   LYS C 198     4659   2976   2809   -109    759    -36       N  
ATOM   6545  CA  LYS C 198       2.340 111.931  60.545  1.00 32.29           C  
ANISOU 6545  CA  LYS C 198     5255   3631   3382   -133    737    -81       C  
ATOM   6546  C   LYS C 198       3.014 110.745  61.258  1.00 33.80           C  
ANISOU 6546  C   LYS C 198     5357   3920   3562   -108    671    -80       C  
ATOM   6547  O   LYS C 198       2.481 109.642  61.213  1.00 30.23           O  
ANISOU 6547  O   LYS C 198     4890   3481   3114    -44    645    -20       O  
ATOM   6548  CB  LYS C 198       1.017 112.314  61.213  1.00 33.66           C  
ANISOU 6548  CB  LYS C 198     5492   3773   3524    -85    747    -51       C  
ATOM   6549  CG  LYS C 198       1.151 112.918  62.588  1.00 39.62           C  
ANISOU 6549  CG  LYS C 198     6258   4558   4236   -108    736    -98       C  
ATOM   6550  CD  LYS C 198       1.228 114.416  62.554  1.00 39.65           C  
ANISOU 6550  CD  LYS C 198     6342   4495   4228   -166    799   -151       C  
ATOM   6551  CE  LYS C 198       0.891 115.024  63.894  1.00 41.60           C  
ANISOU 6551  CE  LYS C 198     6623   4755   4427   -168    795   -182       C  
ATOM   6552  NZ  LYS C 198       2.120 115.362  64.634  1.00 48.04           N  
ANISOU 6552  NZ  LYS C 198     7393   5630   5226   -248    779   -272       N  
ATOM   6553  N   THR C 199       4.120 111.001  61.978  1.00 31.52           N  
ANISOU 6553  N   THR C 199     5019   3704   3254   -153    649   -151       N  
ATOM   6554  CA  THR C 199       5.041 109.961  62.434  1.00 31.62           C  
ANISOU 6554  CA  THR C 199     4943   3822   3250   -122    590   -161       C  
ATOM   6555  C   THR C 199       5.578 110.208  63.851  1.00 32.92           C  
ANISOU 6555  C   THR C 199     5071   4079   3358   -126    550   -224       C  
ATOM   6556  O   THR C 199       6.625 109.659  64.188  1.00 32.83           O  
ANISOU 6556  O   THR C 199     4977   4172   3323   -112    505   -261       O  
ATOM   6557  CB  THR C 199       6.289 109.866  61.546  1.00 34.07           C  
ANISOU 6557  CB  THR C 199     5186   4167   3591   -170    595   -203       C  
ATOM   6558  OG1 THR C 199       7.025 111.084  61.670  1.00 36.06           O  
ANISOU 6558  OG1 THR C 199     5430   4427   3841   -271    628   -299       O  
ATOM   6559  CG2 THR C 199       5.981 109.615  60.086  1.00 34.62           C  
ANISOU 6559  CG2 THR C 199     5284   4156   3711   -168    632   -151       C  
ATOM   6560  N   ASP C 200       4.880 111.014  64.656  1.00 31.53           N  
ANISOU 6560  N   ASP C 200     4954   3872   3153   -138    565   -238       N  
ATOM   6561  CA  ASP C 200       5.327 111.335  66.021  1.00 36.05           C  
ANISOU 6561  CA  ASP C 200     5499   4530   3666   -143    528   -303       C  
ATOM   6562  C   ASP C 200       5.193 110.115  66.943  1.00 34.25           C  
ANISOU 6562  C   ASP C 200     5244   4378   3389    -34    468   -253       C  
ATOM   6563  O   ASP C 200       5.896 110.022  67.940  1.00 32.86           O  
ANISOU 6563  O   ASP C 200     5019   4310   3156    -13    420   -306       O  
ATOM   6564  CB  ASP C 200       4.544 112.515  66.595  1.00 38.92           C  
ANISOU 6564  CB  ASP C 200     5947   4829   4011   -179    568   -326       C  
ATOM   6565  CG  ASP C 200       4.789 113.816  65.839  1.00 42.53           C  
ANISOU 6565  CG  ASP C 200     6449   5208   4502   -286    639   -386       C  
ATOM   6566  OD1 ASP C 200       4.181 113.991  64.775  1.00 39.84           O  
ANISOU 6566  OD1 ASP C 200     6167   4768   4202   -283    688   -334       O  
ATOM   6567  OD2 ASP C 200       5.599 114.627  66.315  1.00 52.97           O  
ANISOU 6567  OD2 ASP C 200     7751   6570   5805   -369    650   -487       O  
ATOM   6568  N   TYR C 201       4.272 109.198  66.604  1.00 33.28           N  
ANISOU 6568  N   TYR C 201     5161   4199   3284     35    476   -155       N  
ATOM   6569  CA  TYR C 201       3.958 108.040  67.451  1.00 33.17           C  
ANISOU 6569  CA  TYR C 201     5153   4225   3222    137    443    -97       C  
ATOM   6570  C   TYR C 201       3.649 106.845  66.556  1.00 29.99           C  
ANISOU 6570  C   TYR C 201     4756   3780   2857    183    455    -18       C  
ATOM   6571  O   TYR C 201       3.438 106.993  65.380  1.00 30.43           O  
ANISOU 6571  O   TYR C 201     4817   3772   2971    141    486     -3       O  
ATOM   6572  CB  TYR C 201       2.733 108.290  68.335  1.00 33.86           C  
ANISOU 6572  CB  TYR C 201     5314   4268   3282    165    461    -63       C  
ATOM   6573  CG  TYR C 201       2.864 109.424  69.312  1.00 38.60           C  
ANISOU 6573  CG  TYR C 201     5926   4900   3839    128    453   -135       C  
ATOM   6574  CD1 TYR C 201       3.434 109.233  70.568  1.00 40.86           C  
ANISOU 6574  CD1 TYR C 201     6185   5287   4051    174    404   -171       C  
ATOM   6575  CD2 TYR C 201       2.404 110.688  68.985  1.00 37.76           C  
ANISOU 6575  CD2 TYR C 201     5864   4721   3759     53    498   -167       C  
ATOM   6576  CE1 TYR C 201       3.572 110.285  71.459  1.00 43.88           C  
ANISOU 6576  CE1 TYR C 201     6577   5703   4392    134    397   -246       C  
ATOM   6577  CE2 TYR C 201       2.533 111.749  69.861  1.00 39.36           C  
ANISOU 6577  CE2 TYR C 201     6088   4942   3922     12    499   -238       C  
ATOM   6578  CZ  TYR C 201       3.130 111.546  71.093  1.00 42.19           C  
ANISOU 6578  CZ  TYR C 201     6410   5406   4212     46    447   -282       C  
ATOM   6579  OH  TYR C 201       3.253 112.581  71.954  1.00 44.43           O  
ANISOU 6579  OH  TYR C 201     6713   5712   4455      1    448   -358       O  
ATOM   6580  N   GLU C 202       3.646 105.667  67.160  1.00 28.24           N  
ANISOU 6580  N   GLU C 202     4541   3594   2594    273    435     30       N  
ATOM   6581  CA  GLU C 202       3.061 104.512  66.565  1.00 28.65           C  
ANISOU 6581  CA  GLU C 202     4625   3587   2671    316    462    108       C  
ATOM   6582  C   GLU C 202       1.545 104.626  66.794  1.00 28.55           C  
ANISOU 6582  C   GLU C 202     4682   3495   2670    311    506    152       C  
ATOM   6583  O   GLU C 202       1.020 104.164  67.801  1.00 27.50           O  
ANISOU 6583  O   GLU C 202     4592   3365   2490    364    513    184       O  
ATOM   6584  CB  GLU C 202       3.727 103.273  67.171  1.00 29.41           C  
ANISOU 6584  CB  GLU C 202     4716   3748   2709    417    435    138       C  
ATOM   6585  CG  GLU C 202       3.447 101.990  66.428  1.00 30.42           C  
ANISOU 6585  CG  GLU C 202     4876   3818   2862    457    467    208       C  
ATOM   6586  CD  GLU C 202       4.067 100.737  67.039  1.00 31.65           C  
ANISOU 6586  CD  GLU C 202     5052   4023   2950    572    454    246       C  
ATOM   6587  OE1 GLU C 202       3.842  99.651  66.485  1.00 35.55           O  
ANISOU 6587  OE1 GLU C 202     5587   4460   3460    605    490    303       O  
ATOM   6588  OE2 GLU C 202       4.800 100.840  68.039  1.00 34.05           O  
ANISOU 6588  OE2 GLU C 202     5333   4423   3179    635    409    215       O  
ATOM   6589  N   TYR C 203       0.863 105.259  65.833  1.00 27.15           N  
ANISOU 6589  N   TYR C 203     4514   3251   2550    250    538    151       N  
ATOM   6590  CA  TYR C 203      -0.544 105.669  65.961  1.00 28.04           C  
ANISOU 6590  CA  TYR C 203     4675   3306   2671    239    576    174       C  
ATOM   6591  C   TYR C 203      -1.517 104.476  65.950  1.00 27.82           C  
ANISOU 6591  C   TYR C 203     4677   3243   2650    276    610    236       C  
ATOM   6592  O   TYR C 203      -2.626 104.562  66.515  1.00 26.28           O  
ANISOU 6592  O   TYR C 203     4517   3025   2441    284    639    253       O  
ATOM   6593  CB  TYR C 203      -0.870 106.696  64.870  1.00 29.22           C  
ANISOU 6593  CB  TYR C 203     4826   3408   2869    182    599    151       C  
ATOM   6594  CG  TYR C 203      -0.296 108.064  65.158  1.00 31.88           C  
ANISOU 6594  CG  TYR C 203     5165   3755   3190    137    592     88       C  
ATOM   6595  CD1 TYR C 203      -0.800 108.809  66.212  1.00 33.40           C  
ANISOU 6595  CD1 TYR C 203     5396   3951   3344    140    597     70       C  
ATOM   6596  CD2 TYR C 203       0.759 108.602  64.434  1.00 32.35           C  
ANISOU 6596  CD2 TYR C 203     5195   3822   3274     85    588     41       C  
ATOM   6597  CE1 TYR C 203      -0.298 110.058  66.533  1.00 34.98           C  
ANISOU 6597  CE1 TYR C 203     5608   4154   3526     91    599      5       C  
ATOM   6598  CE2 TYR C 203       1.254 109.871  64.720  1.00 35.83           C  
ANISOU 6598  CE2 TYR C 203     5647   4264   3702     28    597    -25       C  
ATOM   6599  CZ  TYR C 203       0.723 110.601  65.777  1.00 37.77           C  
ANISOU 6599  CZ  TYR C 203     5935   4507   3906     30    603    -44       C  
ATOM   6600  OH  TYR C 203       1.180 111.846  66.135  1.00 44.37           O  
ANISOU 6600  OH  TYR C 203     6793   5339   4725    -31    619   -117       O  
ATOM   6601  N   TYR C 204      -1.146 103.377  65.286  1.00 26.63           N  
ANISOU 6601  N   TYR C 204     4514   3083   2519    293    614    265       N  
ATOM   6602  CA  TYR C 204      -1.910 102.162  65.412  1.00 27.11           C  
ANISOU 6602  CA  TYR C 204     4613   3109   2578    321    656    315       C  
ATOM   6603  C   TYR C 204      -1.000 100.928  65.362  1.00 26.98           C  
ANISOU 6603  C   TYR C 204     4602   3103   2543    372    651    343       C  
ATOM   6604  O   TYR C 204       0.134 100.975  64.921  1.00 26.38           O  
ANISOU 6604  O   TYR C 204     4486   3065   2471    380    613    324       O  
ATOM   6605  CB  TYR C 204      -3.012 102.065  64.357  1.00 28.52           C  
ANISOU 6605  CB  TYR C 204     4786   3237   2811    276    696    323       C  
ATOM   6606  CG  TYR C 204      -2.918 102.979  63.169  1.00 27.80           C  
ANISOU 6606  CG  TYR C 204     4658   3140   2764    234    681    292       C  
ATOM   6607  CD1 TYR C 204      -3.281 104.307  63.289  1.00 31.00           C  
ANISOU 6607  CD1 TYR C 204     5065   3547   3164    215    676    262       C  
ATOM   6608  CD2 TYR C 204      -2.592 102.511  61.910  1.00 28.89           C  
ANISOU 6608  CD2 TYR C 204     4772   3260   2943    218    683    296       C  
ATOM   6609  CE1 TYR C 204      -3.258 105.164  62.196  1.00 29.54           C  
ANISOU 6609  CE1 TYR C 204     4866   3345   3010    187    676    239       C  
ATOM   6610  CE2 TYR C 204      -2.567 103.346  60.806  1.00 30.26           C  
ANISOU 6610  CE2 TYR C 204     4924   3423   3150    188    677    272       C  
ATOM   6611  CZ  TYR C 204      -2.882 104.691  60.954  1.00 30.52           C  
ANISOU 6611  CZ  TYR C 204     4967   3455   3173    175    676    245       C  
ATOM   6612  OH  TYR C 204      -2.896 105.562  59.897  1.00 31.00           O  
ANISOU 6612  OH  TYR C 204     5026   3495   3256    157    682    225       O  
ATOM   6613  N   ILE C 205      -1.552  99.833  65.864  1.00 27.65           N  
ANISOU 6613  N   ILE C 205     4746   3153   2604    408    697    388       N  
ATOM   6614  CA  ILE C 205      -0.906  98.523  65.952  1.00 29.70           C  
ANISOU 6614  CA  ILE C 205     5045   3406   2834    473    713    428       C  
ATOM   6615  C   ILE C 205      -1.843  97.529  65.273  1.00 30.76           C  
ANISOU 6615  C   ILE C 205     5219   3459   3008    438    786    458       C  
ATOM   6616  O   ILE C 205      -2.990  97.423  65.662  1.00 28.00           O  
ANISOU 6616  O   ILE C 205     4903   3072   2661    409    838    466       O  
ATOM   6617  CB  ILE C 205      -0.562  98.127  67.402  1.00 31.21           C  
ANISOU 6617  CB  ILE C 205     5291   3629   2937    564    710    452       C  
ATOM   6618  CG1 ILE C 205       0.349  99.158  68.074  1.00 32.18           C  
ANISOU 6618  CG1 ILE C 205     5360   3846   3017    589    634    405       C  
ATOM   6619  CG2 ILE C 205       0.080  96.747  67.448  1.00 31.24           C  
ANISOU 6619  CG2 ILE C 205     5352   3617   2899    649    736    499       C  
ATOM   6620  CD1 ILE C 205      -0.393 100.207  68.822  1.00 38.46           C  
ANISOU 6620  CD1 ILE C 205     6159   4649   3804    553    631    379       C  
ATOM   6621  N   VAL C 206      -1.343  96.873  64.220  1.00 32.02           N  
ANISOU 6621  N   VAL C 206     5367   3598   3199    434    790    465       N  
ATOM   6622  CA  VAL C 206      -2.158  95.989  63.361  1.00 33.80           C  
ANISOU 6622  CA  VAL C 206     5619   3752   3469    385    856    477       C  
ATOM   6623  C   VAL C 206      -1.679  94.541  63.502  1.00 29.87           C  
ANISOU 6623  C   VAL C 206     5202   3209   2937    446    905    523       C  
ATOM   6624  O   VAL C 206      -0.587  94.285  63.952  1.00 27.18           O  
ANISOU 6624  O   VAL C 206     4877   2903   2544    532    873    543       O  
ATOM   6625  CB  VAL C 206      -2.133  96.410  61.883  1.00 34.00           C  
ANISOU 6625  CB  VAL C 206     5576   3779   3561    325    831    445       C  
ATOM   6626  CG1 VAL C 206      -2.936  97.665  61.656  1.00 38.94           C  
ANISOU 6626  CG1 VAL C 206     6149   4428   4216    270    811    407       C  
ATOM   6627  CG2 VAL C 206      -0.719  96.568  61.353  1.00 34.43           C  
ANISOU 6627  CG2 VAL C 206     5590   3874   3615    360    774    440       C  
ATOM   6628  N   VAL C 207      -2.536  93.605  63.119  1.00 35.79           N  
ANISOU 6628  N   VAL C 207     6004   3883   3711    401    987    534       N  
ATOM   6629  CA  VAL C 207      -2.244  92.174  63.336  1.00 43.53           C  
ANISOU 6629  CA  VAL C 207     7089   4795   4652    455   1059    580       C  
ATOM   6630  C   VAL C 207      -1.375  91.637  62.194  1.00 49.40           C  
ANISOU 6630  C   VAL C 207     7819   5530   5419    471   1042    583       C  
ATOM   6631  O   VAL C 207      -1.558  92.025  61.043  1.00 51.90           O  
ANISOU 6631  O   VAL C 207     8064   5856   5800    400   1017    547       O  
ATOM   6632  CB  VAL C 207      -3.540  91.366  63.493  1.00 48.83           C  
ANISOU 6632  CB  VAL C 207     7834   5381   5338    388   1172    582       C  
ATOM   6633  CG1 VAL C 207      -4.081  91.495  64.904  1.00 49.85           C  
ANISOU 6633  CG1 VAL C 207     8021   5506   5414    415   1208    602       C  
ATOM   6634  CG2 VAL C 207      -4.575  91.785  62.461  1.00 49.26           C  
ANISOU 6634  CG2 VAL C 207     7807   5440   5470    267   1177    526       C  
ATOM   6635  N   THR C 222      -5.883  80.108  40.605  1.00 50.94           N  
ANISOU 6635  N   THR C 222     8007   5218   6128   -655   1629   -274       N  
ATOM   6636  CA  THR C 222      -5.916  80.515  39.201  1.00 47.24           C  
ANISOU 6636  CA  THR C 222     7443   4841   5662   -647   1549   -331       C  
ATOM   6637  C   THR C 222      -5.480  81.978  39.085  1.00 44.72           C  
ANISOU 6637  C   THR C 222     7022   4629   5341   -534   1415   -273       C  
ATOM   6638  O   THR C 222      -4.891  82.335  38.085  1.00 39.03           O  
ANISOU 6638  O   THR C 222     6272   3941   4614   -470   1350   -261       O  
ATOM   6639  CB  THR C 222      -7.303  80.303  38.571  1.00 49.15           C  
ANISOU 6639  CB  THR C 222     7596   5167   5910   -784   1573   -483       C  
ATOM   6640  OG1 THR C 222      -7.198  80.313  37.148  1.00 53.03           O  
ANISOU 6640  OG1 THR C 222     8039   5715   6394   -773   1521   -539       O  
ATOM   6641  CG2 THR C 222      -8.326  81.343  38.968  1.00 46.44           C  
ANISOU 6641  CG2 THR C 222     7113   4962   5567   -804   1512   -531       C  
ATOM   6642  N   GLY C 223      -5.799  82.802  40.102  1.00 41.49           N  
ANISOU 6642  N   GLY C 223     6566   4265   4932   -514   1384   -241       N  
ATOM   6643  CA  GLY C 223      -5.474  84.232  40.117  1.00 39.13           C  
ANISOU 6643  CA  GLY C 223     6180   4057   4629   -419   1272   -192       C  
ATOM   6644  C   GLY C 223      -6.482  85.097  39.369  1.00 37.66           C  
ANISOU 6644  C   GLY C 223     5863   4009   4435   -438   1204   -278       C  
ATOM   6645  O   GLY C 223      -6.260  86.285  39.215  1.00 34.67           O  
ANISOU 6645  O   GLY C 223     5425   3700   4046   -357   1120   -243       O  
ATOM   6646  N   ASN C 224      -7.626  84.535  38.963  1.00 36.74           N  
ANISOU 6646  N   ASN C 224     5702   3939   4317   -544   1246   -394       N  
ATOM   6647  CA  ASN C 224      -8.566  85.243  38.095  1.00 39.48           C  
ANISOU 6647  CA  ASN C 224     5921   4435   4644   -547   1179   -487       C  
ATOM   6648  C   ASN C 224      -9.212  86.434  38.829  1.00 39.46           C  
ANISOU 6648  C   ASN C 224     5835   4528   4631   -511   1125   -479       C  
ATOM   6649  O   ASN C 224      -9.368  87.521  38.252  1.00 38.31           O  
ANISOU 6649  O   ASN C 224     5613   4483   4458   -429   1040   -483       O  
ATOM   6650  CB  ASN C 224      -9.655  84.332  37.542  1.00 44.56           C  
ANISOU 6650  CB  ASN C 224     6521   5123   5284   -676   1237   -629       C  
ATOM   6651  CG  ASN C 224     -10.474  85.030  36.484  1.00 47.64           C  
ANISOU 6651  CG  ASN C 224     6778   5683   5640   -653   1156   -726       C  
ATOM   6652  OD1 ASN C 224     -11.594  85.436  36.756  1.00 58.00           O  
ANISOU 6652  OD1 ASN C 224     7986   7111   6937   -689   1143   -804       O  
ATOM   6653  ND2 ASN C 224      -9.915  85.208  35.293  1.00 48.75           N  
ANISOU 6653  ND2 ASN C 224     6918   5843   5760   -580   1101   -719       N  
ATOM   6654  N   GLN C 225      -9.559  86.246  40.106  1.00 38.20           N  
ANISOU 6654  N   GLN C 225     5699   4328   4485   -561   1181   -462       N  
ATOM   6655  CA  GLN C 225     -10.146  87.337  40.899  1.00 40.49           C  
ANISOU 6655  CA  GLN C 225     5920   4699   4764   -526   1137   -450       C  
ATOM   6656  C   GLN C 225      -9.066  88.377  41.243  1.00 35.29           C  
ANISOU 6656  C   GLN C 225     5296   4010   4102   -402   1070   -329       C  
ATOM   6657  O   GLN C 225      -9.320  89.569  41.136  1.00 36.38           O  
ANISOU 6657  O   GLN C 225     5368   4233   4218   -332   1000   -323       O  
ATOM   6658  CB  GLN C 225     -10.792  86.835  42.197  1.00 44.60           C  
ANISOU 6658  CB  GLN C 225     6465   5181   5300   -614   1221   -464       C  
ATOM   6659  CG  GLN C 225     -11.690  85.622  42.033  1.00 52.27           C  
ANISOU 6659  CG  GLN C 225     7432   6146   6282   -760   1320   -578       C  
ATOM   6660  CD  GLN C 225     -11.984  84.993  43.375  1.00 59.10           C  
ANISOU 6660  CD  GLN C 225     8368   6922   7163   -838   1424   -562       C  
ATOM   6661  OE1 GLN C 225     -11.371  83.997  43.769  1.00 62.73           O  
ANISOU 6661  OE1 GLN C 225     8960   7239   7635   -868   1512   -516       O  
ATOM   6662  NE2 GLN C 225     -12.896  85.611  44.109  1.00 59.03           N  
ANISOU 6662  NE2 GLN C 225     8282   6998   7148   -857   1419   -593       N  
ATOM   6663  N   TYR C 226      -7.883  87.917  41.679  1.00 33.39           N  
ANISOU 6663  N   TYR C 226     5158   3649   3877   -374   1097   -239       N  
ATOM   6664  CA  TYR C 226      -6.765  88.787  42.077  1.00 30.39           C  
ANISOU 6664  CA  TYR C 226     4808   3241   3496   -273   1044   -135       C  
ATOM   6665  C   TYR C 226      -6.341  89.684  40.901  1.00 28.87           C  
ANISOU 6665  C   TYR C 226     4574   3105   3290   -195    967   -129       C  
ATOM   6666  O   TYR C 226      -6.277  90.891  41.054  1.00 25.63           O  
ANISOU 6666  O   TYR C 226     4130   2741   2866   -132    913   -100       O  
ATOM   6667  CB  TYR C 226      -5.592  87.962  42.594  1.00 29.79           C  
ANISOU 6667  CB  TYR C 226     4839   3046   3431   -255   1089    -58       C  
ATOM   6668  CG  TYR C 226      -4.314  88.727  42.829  1.00 30.04           C  
ANISOU 6668  CG  TYR C 226     4890   3062   3460   -157   1035     31       C  
ATOM   6669  CD1 TYR C 226      -4.170  89.579  43.915  1.00 28.65           C  
ANISOU 6669  CD1 TYR C 226     4704   2903   3278   -121   1007     77       C  
ATOM   6670  CD2 TYR C 226      -3.218  88.567  41.985  1.00 27.84           C  
ANISOU 6670  CD2 TYR C 226     4639   2754   3184   -107   1016     65       C  
ATOM   6671  CE1 TYR C 226      -2.986  90.263  44.150  1.00 29.66           C  
ANISOU 6671  CE1 TYR C 226     4843   3023   3402    -46    963    145       C  
ATOM   6672  CE2 TYR C 226      -2.017  89.216  42.228  1.00 29.33           C  
ANISOU 6672  CE2 TYR C 226     4837   2934   3370    -30    976    136       C  
ATOM   6673  CZ  TYR C 226      -1.904  90.090  43.297  1.00 30.62           C  
ANISOU 6673  CZ  TYR C 226     4983   3121   3528     -3    948    171       C  
ATOM   6674  OH  TYR C 226      -0.721  90.741  43.506  1.00 30.89           O  
ANISOU 6674  OH  TYR C 226     5017   3157   3560     59    911    225       O  
ATOM   6675  N   PHE C 227      -6.130  89.108  39.716  1.00 26.73           N  
ANISOU 6675  N   PHE C 227     4309   2827   3016   -202    971   -162       N  
ATOM   6676  CA  PHE C 227      -5.711  89.944  38.582  1.00 27.82           C  
ANISOU 6676  CA  PHE C 227     4421   3013   3137   -123    907   -153       C  
ATOM   6677  C   PHE C 227      -6.841  90.858  38.068  1.00 28.60           C  
ANISOU 6677  C   PHE C 227     4429   3236   3200    -98    858   -219       C  
ATOM   6678  O   PHE C 227      -6.546  91.897  37.527  1.00 25.27           O  
ANISOU 6678  O   PHE C 227     3996   2849   2754    -13    808   -191       O  
ATOM   6679  CB  PHE C 227      -5.004  89.117  37.509  1.00 26.07           C  
ANISOU 6679  CB  PHE C 227     4242   2742   2920   -121    923   -156       C  
ATOM   6680  CG  PHE C 227      -3.644  88.672  37.978  1.00 25.94           C  
ANISOU 6680  CG  PHE C 227     4309   2621   2925    -94    949    -68       C  
ATOM   6681  CD1 PHE C 227      -2.646  89.598  38.240  1.00 25.34           C  
ANISOU 6681  CD1 PHE C 227     4240   2536   2851    -19    910      8       C  
ATOM   6682  CD2 PHE C 227      -3.366  87.327  38.180  1.00 27.09           C  
ANISOU 6682  CD2 PHE C 227     4526   2682   3085   -141   1017    -67       C  
ATOM   6683  CE1 PHE C 227      -1.409  89.202  38.724  1.00 26.12           C  
ANISOU 6683  CE1 PHE C 227     4398   2563   2963     11    929     78       C  
ATOM   6684  CE2 PHE C 227      -2.115  86.928  38.629  1.00 26.83           C  
ANISOU 6684  CE2 PHE C 227     4566   2566   3059    -95   1038     13       C  
ATOM   6685  CZ  PHE C 227      -1.138  87.863  38.897  1.00 26.20           C  
ANISOU 6685  CZ  PHE C 227     4476   2499   2980    -17    989     83       C  
ATOM   6686  N   ALA C 228      -8.105  90.521  38.308  1.00 27.88           N  
ANISOU 6686  N   ALA C 228     4278   3214   3101   -166    878   -305       N  
ATOM   6687  CA  ALA C 228      -9.216  91.438  38.050  1.00 30.92           C  
ANISOU 6687  CA  ALA C 228     4570   3733   3444   -129    830   -366       C  
ATOM   6688  C   ALA C 228      -9.072  92.721  38.897  1.00 29.62           C  
ANISOU 6688  C   ALA C 228     4410   3573   3270    -56    798   -295       C  
ATOM   6689  O   ALA C 228      -9.268  93.825  38.393  1.00 28.05           O  
ANISOU 6689  O   ALA C 228     4185   3443   3030     35    747   -292       O  
ATOM   6690  CB  ALA C 228     -10.532  90.742  38.311  1.00 31.82           C  
ANISOU 6690  CB  ALA C 228     4612   3921   3556   -229    868   -475       C  
ATOM   6691  N   THR C 229      -8.654  92.568  40.156  1.00 27.72           N  
ANISOU 6691  N   THR C 229     4216   3252   3061    -89    831   -236       N  
ATOM   6692  CA  THR C 229      -8.420  93.685  41.046  1.00 28.36           C  
ANISOU 6692  CA  THR C 229     4311   3326   3136    -33    807   -172       C  
ATOM   6693  C   THR C 229      -7.222  94.512  40.556  1.00 28.82           C  
ANISOU 6693  C   THR C 229     4418   3339   3190     50    772    -98       C  
ATOM   6694  O   THR C 229      -7.318  95.750  40.481  1.00 25.75           O  
ANISOU 6694  O   THR C 229     4022   2988   2772    122    737    -80       O  
ATOM   6695  CB  THR C 229      -8.281  93.212  42.500  1.00 29.81           C  
ANISOU 6695  CB  THR C 229     4533   3442   3349    -90    852   -135       C  
ATOM   6696  OG1 THR C 229      -9.529  92.602  42.832  1.00 29.52           O  
ANISOU 6696  OG1 THR C 229     4445   3459   3312   -169    891   -214       O  
ATOM   6697  CG2 THR C 229      -7.987  94.317  43.487  1.00 29.74           C  
ANISOU 6697  CG2 THR C 229     4541   3425   3334    -38    828    -73       C  
ATOM   6698  N   ILE C 230      -6.115  93.850  40.222  1.00 24.76           N  
ANISOU 6698  N   ILE C 230     3957   2746   2702     40    788    -59       N  
ATOM   6699  CA  ILE C 230      -4.924  94.545  39.713  1.00 25.01           C  
ANISOU 6699  CA  ILE C 230     4030   2738   2734    106    766      1       C  
ATOM   6700  C   ILE C 230      -5.279  95.325  38.443  1.00 22.94           C  
ANISOU 6700  C   ILE C 230     3746   2538   2430    174    732    -27       C  
ATOM   6701  O   ILE C 230      -4.889  96.457  38.313  1.00 23.75           O  
ANISOU 6701  O   ILE C 230     3871   2636   2514    238    715      9       O  
ATOM   6702  CB  ILE C 230      -3.762  93.561  39.518  1.00 28.10           C  
ANISOU 6702  CB  ILE C 230     4472   3049   3156     86    792     36       C  
ATOM   6703  CG1 ILE C 230      -3.425  92.833  40.829  1.00 26.67           C  
ANISOU 6703  CG1 ILE C 230     4324   2810   3000     43    827     70       C  
ATOM   6704  CG2 ILE C 230      -2.545  94.255  38.915  1.00 26.96           C  
ANISOU 6704  CG2 ILE C 230     4357   2874   3012    146    774     88       C  
ATOM   6705  CD1 ILE C 230      -3.008  93.707  41.959  1.00 28.29           C  
ANISOU 6705  CD1 ILE C 230     4535   3008   3205     67    812    119       C  
ATOM   6706  N   ASN C 231      -6.096  94.747  37.563  1.00 22.60           N  
ANISOU 6706  N   ASN C 231     3661   2556   2366    162    727    -99       N  
ATOM   6707  CA  ASN C 231      -6.589  95.406  36.366  1.00 24.21           C  
ANISOU 6707  CA  ASN C 231     3841   2840   2517    240    692   -136       C  
ATOM   6708  C   ASN C 231      -7.343  96.707  36.703  1.00 26.01           C  
ANISOU 6708  C   ASN C 231     4046   3136   2699    311    666   -137       C  
ATOM   6709  O   ASN C 231      -7.222  97.708  36.000  1.00 23.26           O  
ANISOU 6709  O   ASN C 231     3725   2805   2306    407    647   -117       O  
ATOM   6710  CB  ASN C 231      -7.497  94.461  35.584  1.00 27.21           C  
ANISOU 6710  CB  ASN C 231     4162   3295   2879    200    691   -232       C  
ATOM   6711  CG  ASN C 231      -7.937  95.023  34.251  1.00 29.74           C  
ANISOU 6711  CG  ASN C 231     4458   3707   3134    293    650   -274       C  
ATOM   6712  OD1 ASN C 231      -9.131  95.028  33.960  1.00 36.19           O  
ANISOU 6712  OD1 ASN C 231     5197   4646   3907    304    627   -360       O  
ATOM   6713  ND2 ASN C 231      -6.999  95.489  33.435  1.00 26.44           N  
ANISOU 6713  ND2 ASN C 231     4102   3239   2703    364    644   -220       N  
ATOM   6714  N   GLU C 232      -8.138  96.700  37.784  1.00 26.06           N  
ANISOU 6714  N   GLU C 232     4011   3176   2712    269    672   -159       N  
ATOM   6715  CA  GLU C 232      -8.899  97.897  38.203  1.00 26.35           C  
ANISOU 6715  CA  GLU C 232     4028   3279   2704    339    651   -160       C  
ATOM   6716  C   GLU C 232      -7.945  98.983  38.727  1.00 24.62           C  
ANISOU 6716  C   GLU C 232     3887   2973   2492    384    657    -72       C  
ATOM   6717  O   GLU C 232      -8.237 100.172  38.553  1.00 28.81           O  
ANISOU 6717  O   GLU C 232     4439   3533   2972    475    644    -59       O  
ATOM   6718  CB  GLU C 232      -9.971  97.545  39.239  1.00 29.53           C  
ANISOU 6718  CB  GLU C 232     4364   3740   3115    276    662   -209       C  
ATOM   6719  CG  GLU C 232     -11.102  96.691  38.694  1.00 34.94           C  
ANISOU 6719  CG  GLU C 232     4957   4536   3783    232    659   -317       C  
ATOM   6720  CD  GLU C 232     -11.898  97.298  37.552  1.00 45.93           C  
ANISOU 6720  CD  GLU C 232     6294   6060   5096    335    613   -378       C  
ATOM   6721  OE1 GLU C 232     -12.260  98.492  37.650  1.00 56.43           O  
ANISOU 6721  OE1 GLU C 232     7629   7438   6374    441    588   -357       O  
ATOM   6722  OE2 GLU C 232     -12.151  96.576  36.553  1.00 57.50           O  
ANISOU 6722  OE2 GLU C 232     7717   7581   6547    317    604   -448       O  
ATOM   6723  N   ILE C 233      -6.823  98.585  39.342  1.00 21.27           N  
ANISOU 6723  N   ILE C 233     3508   2449   2124    325    680    -18       N  
ATOM   6724  CA  ILE C 233      -5.814  99.502  39.798  1.00 21.03           C  
ANISOU 6724  CA  ILE C 233     3541   2345   2104    348    690     49       C  
ATOM   6725  C   ILE C 233      -5.220 100.271  38.601  1.00 23.28           C  
ANISOU 6725  C   ILE C 233     3876   2608   2358    424    690     71       C  
ATOM   6726  O   ILE C 233      -5.179 101.527  38.607  1.00 22.30           O  
ANISOU 6726  O   ILE C 233     3800   2473   2201    487    697     96       O  
ATOM   6727  CB  ILE C 233      -4.769  98.741  40.632  1.00 21.25           C  
ANISOU 6727  CB  ILE C 233     3588   2295   2190    274    710     88       C  
ATOM   6728  CG1 ILE C 233      -5.383  98.281  41.956  1.00 22.89           C  
ANISOU 6728  CG1 ILE C 233     3768   2515   2413    219    718     77       C  
ATOM   6729  CG2 ILE C 233      -3.530  99.578  40.858  1.00 22.16           C  
ANISOU 6729  CG2 ILE C 233     3756   2345   2316    291    719    143       C  
ATOM   6730  CD1 ILE C 233      -4.429  97.535  42.853  1.00 23.22           C  
ANISOU 6730  CD1 ILE C 233     3835   2488   2496    167    738    116       C  
ATOM   6731  N   TYR C 234      -4.794  99.552  37.542  1.00 22.66           N  
ANISOU 6731  N   TYR C 234     3801   2521   2287    422    690     61       N  
ATOM   6732  CA  TYR C 234      -4.251 100.221  36.386  1.00 23.19           C  
ANISOU 6732  CA  TYR C 234     3922   2567   2323    494    698     82       C  
ATOM   6733  C   TYR C 234      -5.313 101.107  35.721  1.00 22.68           C  
ANISOU 6733  C   TYR C 234     3860   2579   2179    599    680     54       C  
ATOM   6734  O   TYR C 234      -4.970 102.193  35.195  1.00 22.35           O  
ANISOU 6734  O   TYR C 234     3891   2504   2096    678    700     88       O  
ATOM   6735  CB  TYR C 234      -3.674  99.213  35.386  1.00 23.53           C  
ANISOU 6735  CB  TYR C 234     3963   2592   2384    475    701     73       C  
ATOM   6736  CG  TYR C 234      -2.384  98.586  35.839  1.00 23.83           C  
ANISOU 6736  CG  TYR C 234     4019   2548   2484    407    723    114       C  
ATOM   6737  CD1 TYR C 234      -1.217  99.329  35.937  1.00 23.14           C  
ANISOU 6737  CD1 TYR C 234     3982   2397   2413    414    749    164       C  
ATOM   6738  CD2 TYR C 234      -2.311  97.234  36.128  1.00 23.33           C  
ANISOU 6738  CD2 TYR C 234     3927   2476   2459    339    726     97       C  
ATOM   6739  CE1 TYR C 234      -0.024  98.761  36.343  1.00 22.66           C  
ANISOU 6739  CE1 TYR C 234     3923   2283   2402    362    765    194       C  
ATOM   6740  CE2 TYR C 234      -1.114  96.646  36.522  1.00 23.71           C  
ANISOU 6740  CE2 TYR C 234     3996   2460   2553    299    746    137       C  
ATOM   6741  CZ  TYR C 234       0.029  97.406  36.645  1.00 23.48           C  
ANISOU 6741  CZ  TYR C 234     3998   2385   2536    314    760    183       C  
ATOM   6742  OH  TYR C 234       1.223  96.813  36.980  1.00 23.32           O  
ANISOU 6742  OH  TYR C 234     3984   2322   2552    286    775    214       O  
ATOM   6743  N   LYS C 235      -6.577 100.662  35.705  1.00 23.70           N  
ANISOU 6743  N   LYS C 235     3913   2812   2279    606    650    -10       N  
ATOM   6744  CA  LYS C 235      -7.640 101.465  35.098  1.00 27.95           C  
ANISOU 6744  CA  LYS C 235     4441   3447   2730    723    627    -44       C  
ATOM   6745  C   LYS C 235      -7.807 102.775  35.886  1.00 27.24           C  
ANISOU 6745  C   LYS C 235     4401   3336   2612    778    642     -4       C  
ATOM   6746  O   LYS C 235      -7.986 103.838  35.308  1.00 25.40           O  
ANISOU 6746  O   LYS C 235     4230   3111   2308    896    649     13       O  
ATOM   6747  CB  LYS C 235      -8.975 100.725  35.027  1.00 32.54           C  
ANISOU 6747  CB  LYS C 235     4912   4164   3287    709    591   -135       C  
ATOM   6748  CG  LYS C 235      -9.124  99.827  33.802  1.00 40.67           C  
ANISOU 6748  CG  LYS C 235     5902   5250   4298    709    572   -194       C  
ATOM   6749  CD  LYS C 235     -10.382  98.980  33.801  1.00 46.92           C  
ANISOU 6749  CD  LYS C 235     6574   6176   5076    663    546   -302       C  
ATOM   6750  CE  LYS C 235     -11.653  99.786  33.958  1.00 53.53           C  
ANISOU 6750  CE  LYS C 235     7352   7150   5837    756    515   -349       C  
ATOM   6751  NZ  LYS C 235     -12.845  98.906  33.929  1.00 58.05           N  
ANISOU 6751  NZ  LYS C 235     7792   7865   6397    695    495   -468       N  
ATOM   6752  N   ALA C 236      -7.672 102.685  37.207  1.00 26.02           N  
ANISOU 6752  N   ALA C 236     4232   3143   2511    695    652     13       N  
ATOM   6753  CA  ALA C 236      -7.849 103.839  38.075  1.00 27.62           C  
ANISOU 6753  CA  ALA C 236     4479   3323   2692    733    668     44       C  
ATOM   6754  C   ALA C 236      -6.784 104.904  37.756  1.00 26.21           C  
ANISOU 6754  C   ALA C 236     4417   3037   2503    774    710    107       C  
ATOM   6755  O   ALA C 236      -7.086 106.114  37.709  1.00 28.43           O  
ANISOU 6755  O   ALA C 236     4767   3310   2723    867    731    126       O  
ATOM   6756  CB  ALA C 236      -7.769 103.393  39.518  1.00 27.59           C  
ANISOU 6756  CB  ALA C 236     4439   3293   2749    628    672     50       C  
ATOM   6757  N   ILE C 237      -5.544 104.447  37.582  1.00 23.57           N  
ANISOU 6757  N   ILE C 237     4106   2621   2226    703    730    135       N  
ATOM   6758  CA  ILE C 237      -4.409 105.318  37.296  1.00 25.22           C  
ANISOU 6758  CA  ILE C 237     4414   2729   2439    713    780    183       C  
ATOM   6759  C   ILE C 237      -4.601 106.017  35.936  1.00 26.29           C  
ANISOU 6759  C   ILE C 237     4623   2867   2497    834    801    190       C  
ATOM   6760  O   ILE C 237      -4.436 107.272  35.830  1.00 23.74           O  
ANISOU 6760  O   ILE C 237     4404   2486   2129    899    850    221       O  
ATOM   6761  CB  ILE C 237      -3.089 104.536  37.360  1.00 24.98           C  
ANISOU 6761  CB  ILE C 237     4371   2635   2484    614    792    201       C  
ATOM   6762  CG1 ILE C 237      -2.743 104.116  38.790  1.00 24.21           C  
ANISOU 6762  CG1 ILE C 237     4228   2522   2445    517    783    205       C  
ATOM   6763  CG2 ILE C 237      -1.962 105.361  36.747  1.00 27.05           C  
ANISOU 6763  CG2 ILE C 237     4725   2809   2743    626    850    236       C  
ATOM   6764  CD1 ILE C 237      -1.634 103.086  38.875  1.00 23.42           C  
ANISOU 6764  CD1 ILE C 237     4098   2390   2408    438    783    216       C  
ATOM   6765  N   TYR C 238      -4.949 105.229  34.906  1.00 24.51           N  
ANISOU 6765  N   TYR C 238     4355   2706   2252    869    769    159       N  
ATOM   6766  CA  TYR C 238      -5.036 105.734  33.546  1.00 26.18           C  
ANISOU 6766  CA  TYR C 238     4635   2923   2387    988    785    165       C  
ATOM   6767  C   TYR C 238      -6.304 106.552  33.294  1.00 26.63           C  
ANISOU 6767  C   TYR C 238     4711   3066   2341   1132    769    146       C  
ATOM   6768  O   TYR C 238      -6.382 107.204  32.239  1.00 27.99           O  
ANISOU 6768  O   TYR C 238     4966   3236   2431   1258    792    161       O  
ATOM   6769  CB  TYR C 238      -4.881 104.618  32.506  1.00 26.54           C  
ANISOU 6769  CB  TYR C 238     4633   3007   2442    977    757    137       C  
ATOM   6770  CG  TYR C 238      -3.435 104.320  32.226  1.00 27.49           C  
ANISOU 6770  CG  TYR C 238     4795   3024   2625    903    798    175       C  
ATOM   6771  CD1 TYR C 238      -2.694 105.140  31.380  1.00 28.35           C  
ANISOU 6771  CD1 TYR C 238     5013   3055   2701    963    857    215       C  
ATOM   6772  CD2 TYR C 238      -2.794 103.233  32.804  1.00 26.90           C  
ANISOU 6772  CD2 TYR C 238     4655   2927   2637    781    785    170       C  
ATOM   6773  CE1 TYR C 238      -1.353 104.906  31.142  1.00 26.79           C  
ANISOU 6773  CE1 TYR C 238     4845   2771   2561    891    899    244       C  
ATOM   6774  CE2 TYR C 238      -1.456 102.974  32.558  1.00 28.56           C  
ANISOU 6774  CE2 TYR C 238     4895   3056   2898    724    821    202       C  
ATOM   6775  CZ  TYR C 238      -0.730 103.812  31.718  1.00 28.19           C  
ANISOU 6775  CZ  TYR C 238     4942   2943   2823    775    877    236       C  
ATOM   6776  OH  TYR C 238       0.591 103.565  31.456  1.00 26.37           O  
ANISOU 6776  OH  TYR C 238     4732   2644   2643    716    916    260       O  
ATOM   6777  N   LYS C 239      -7.272 106.533  34.212  1.00 25.59           N  
ANISOU 6777  N   LYS C 239     4507   3010   2203   1126    735    115       N  
ATOM   6778  CA  LYS C 239      -8.428 107.400  34.107  1.00 29.68           C  
ANISOU 6778  CA  LYS C 239     5044   3613   2621   1269    724    100       C  
ATOM   6779  C   LYS C 239      -8.387 108.508  35.179  1.00 27.75           C  
ANISOU 6779  C   LYS C 239     4873   3297   2372   1275    766    141       C  
ATOM   6780  O   LYS C 239      -9.372 109.188  35.342  1.00 28.94           O  
ANISOU 6780  O   LYS C 239     5032   3516   2446   1385    757    129       O  
ATOM   6781  CB  LYS C 239      -9.729 106.595  34.226  1.00 32.41           C  
ANISOU 6781  CB  LYS C 239     5243   4124   2946   1275    654     19       C  
ATOM   6782  CG  LYS C 239      -9.995 105.615  33.096  1.00 34.29           C  
ANISOU 6782  CG  LYS C 239     5407   4454   3165   1287    611    -38       C  
ATOM   6783  N   SER C 240      -7.264 108.707  35.891  1.00 25.79           N  
ANISOU 6783  N   SER C 240     4677   2920   2200   1163    812    183       N  
ATOM   6784  CA  SER C 240      -7.221 109.685  37.001  1.00 26.04           C  
ANISOU 6784  CA  SER C 240     4771   2888   2234   1150    851    210       C  
ATOM   6785  C   SER C 240      -7.639 111.075  36.517  1.00 29.26           C  
ANISOU 6785  C   SER C 240     5313   3268   2534   1309    902    238       C  
ATOM   6786  O   SER C 240      -7.037 111.631  35.603  1.00 25.80           O  
ANISOU 6786  O   SER C 240     4989   2752   2059   1365    958    270       O  
ATOM   6787  CB  SER C 240      -5.878 109.762  37.680  1.00 25.19           C  
ANISOU 6787  CB  SER C 240     4702   2656   2212   1014    896    241       C  
ATOM   6788  OG  SER C 240      -5.847 110.864  38.596  1.00 24.58           O  
ANISOU 6788  OG  SER C 240     4703   2515   2121   1015    941    261       O  
ATOM   6789  N   PRO C 241      -8.669 111.710  37.133  1.00 30.50           N  
ANISOU 6789  N   PRO C 241     5473   3483   2632   1391    893    229       N  
ATOM   6790  CA  PRO C 241      -9.018 113.084  36.761  1.00 30.35           C  
ANISOU 6790  CA  PRO C 241     5603   3423   2504   1552    952    262       C  
ATOM   6791  C   PRO C 241      -8.140 114.151  37.450  1.00 31.96           C  
ANISOU 6791  C   PRO C 241     5949   3461   2731   1494   1045    307       C  
ATOM   6792  O   PRO C 241      -8.328 115.334  37.162  1.00 33.07           O  
ANISOU 6792  O   PRO C 241     6241   3540   2783   1619   1114    339       O  
ATOM   6793  CB  PRO C 241     -10.491 113.114  37.181  1.00 30.99           C  
ANISOU 6793  CB  PRO C 241     5599   3654   2519   1653    895    223       C  
ATOM   6794  CG  PRO C 241     -10.512 112.293  38.445  1.00 29.85           C  
ANISOU 6794  CG  PRO C 241     5325   3537   2478   1489    852    195       C  
ATOM   6795  CD  PRO C 241      -9.571 111.145  38.152  1.00 28.00           C  
ANISOU 6795  CD  PRO C 241     5025   3271   2341   1346    832    187       C  
ATOM   6796  N   ILE C 242      -7.214 113.728  38.336  1.00 28.14           N  
ANISOU 6796  N   ILE C 242     5420   2911   2357   1314   1049    305       N  
ATOM   6797  CA  ILE C 242      -6.158 114.557  38.983  1.00 27.25           C  
ANISOU 6797  CA  ILE C 242     5417   2651   2286   1218   1133    330       C  
ATOM   6798  C   ILE C 242      -4.841 114.483  38.187  1.00 28.76           C  
ANISOU 6798  C   ILE C 242     5665   2743   2519   1147   1190    346       C  
ATOM   6799  O   ILE C 242      -4.223 115.501  37.856  1.00 30.62           O  
ANISOU 6799  O   ILE C 242     6052   2856   2725   1161   1291    370       O  
ATOM   6800  CB  ILE C 242      -5.932 114.087  40.435  1.00 26.41           C  
ANISOU 6800  CB  ILE C 242     5209   2556   2266   1072   1096    308       C  
ATOM   6801  CG1 ILE C 242      -7.201 114.186  41.293  1.00 28.00           C  
ANISOU 6801  CG1 ILE C 242     5358   2849   2430   1132   1050    292       C  
ATOM   6802  CG2 ILE C 242      -4.751 114.808  41.065  1.00 26.15           C  
ANISOU 6802  CG2 ILE C 242     5263   2391   2279    958   1173    317       C  
ATOM   6803  CD1 ILE C 242      -7.691 115.598  41.621  1.00 28.14           C  
ANISOU 6803  CD1 ILE C 242     5513   2811   2364   1235   1114    312       C  
ATOM   6804  N   TYR C 243      -4.363 113.268  37.929  1.00 28.45           N  
ANISOU 6804  N   TYR C 243     5507   2751   2551   1061   1134    329       N  
ATOM   6805  CA  TYR C 243      -3.151 113.029  37.163  1.00 28.37           C  
ANISOU 6805  CA  TYR C 243     5526   2669   2584    995   1176    340       C  
ATOM   6806  C   TYR C 243      -3.563 112.755  35.712  1.00 28.48           C  
ANISOU 6806  C   TYR C 243     5560   2727   2532   1121   1164    348       C  
ATOM   6807  O   TYR C 243      -3.703 111.627  35.278  1.00 26.31           O  
ANISOU 6807  O   TYR C 243     5177   2535   2285   1108   1094    328       O  
ATOM   6808  CB  TYR C 243      -2.320 111.915  37.794  1.00 27.36           C  
ANISOU 6808  CB  TYR C 243     5268   2562   2565    838   1128    319       C  
ATOM   6809  CG  TYR C 243      -1.993 112.138  39.250  1.00 28.24           C  
ANISOU 6809  CG  TYR C 243     5351   2651   2727    731   1129    306       C  
ATOM   6810  CD1 TYR C 243      -0.873 112.855  39.620  1.00 30.90           C  
ANISOU 6810  CD1 TYR C 243     5754   2889   3096    638   1205    304       C  
ATOM   6811  CD2 TYR C 243      -2.794 111.629  40.265  1.00 28.14           C  
ANISOU 6811  CD2 TYR C 243     5243   2720   2729    718   1059    289       C  
ATOM   6812  CE1 TYR C 243      -0.570 113.101  40.953  1.00 31.16           C  
ANISOU 6812  CE1 TYR C 243     5759   2910   3167    544   1204    284       C  
ATOM   6813  CE2 TYR C 243      -2.461 111.798  41.598  1.00 28.32           C  
ANISOU 6813  CE2 TYR C 243     5240   2725   2793    625   1058    277       C  
ATOM   6814  CZ  TYR C 243      -1.346 112.537  41.950  1.00 30.28           C  
ANISOU 6814  CZ  TYR C 243     5554   2882   3068    541   1126    274       C  
ATOM   6815  OH  TYR C 243      -1.006 112.761  43.256  1.00 28.28           O  
ANISOU 6815  OH  TYR C 243     5277   2620   2848    453   1124    254       O  
ATOM   6816  N   LYS C 244      -3.767 113.853  34.980  1.00 30.53           N  
ANISOU 6816  N   LYS C 244     5976   2925   2699   1250   1239    377       N  
ATOM   6817  CA  LYS C 244      -4.329 113.828  33.635  1.00 34.37           C  
ANISOU 6817  CA  LYS C 244     6505   3460   3093   1409   1232    387       C  
ATOM   6818  C   LYS C 244      -3.242 113.715  32.569  1.00 33.38           C  
ANISOU 6818  C   LYS C 244     6445   3251   2984   1382   1292    407       C  
ATOM   6819  O   LYS C 244      -3.545 113.308  31.450  1.00 33.95           O  
ANISOU 6819  O   LYS C 244     6514   3380   3004   1482   1265    407       O  
ATOM   6820  CB  LYS C 244      -5.166 115.083  33.400  1.00 35.67           C  
ANISOU 6820  CB  LYS C 244     6817   3605   3130   1590   1286    413       C  
ATOM   6821  CG  LYS C 244      -6.471 115.069  34.170  1.00 39.53           C  
ANISOU 6821  CG  LYS C 244     7222   4215   3579   1661   1211    388       C  
ATOM   6822  CD  LYS C 244      -7.184 116.384  34.208  1.00 45.15           C  
ANISOU 6822  CD  LYS C 244     8085   4895   4173   1826   1273    416       C  
ATOM   6823  CE  LYS C 244      -8.114 116.571  33.033  1.00 51.63           C  
ANISOU 6823  CE  LYS C 244     8948   5810   4856   2054   1253    420       C  
ATOM   6824  NZ  LYS C 244      -8.738 117.919  33.059  1.00 56.72           N  
ANISOU 6824  NZ  LYS C 244     9765   6411   5374   2234   1326    456       N  
ATOM   6825  N   ASN C 245      -2.010 114.124  32.895  1.00 33.01           N  
ANISOU 6825  N   ASN C 245     6460   3076   3003   1252   1377    420       N  
ATOM   6826  CA  ASN C 245      -0.925 114.088  31.918  1.00 36.12           C  
ANISOU 6826  CA  ASN C 245     6920   3387   3414   1217   1448    436       C  
ATOM   6827  C   ASN C 245      -0.641 112.616  31.589  1.00 33.46           C  
ANISOU 6827  C   ASN C 245     6424   3141   3147   1152   1356    412       C  
ATOM   6828  O   ASN C 245      -0.502 111.805  32.526  1.00 30.78           O  
ANISOU 6828  O   ASN C 245     5946   2855   2892   1035   1287    385       O  
ATOM   6829  CB  ASN C 245       0.330 114.805  32.433  1.00 40.17           C  
ANISOU 6829  CB  ASN C 245     7509   3762   3988   1073   1558    437       C  
ATOM   6830  CG  ASN C 245       1.483 114.738  31.453  1.00 41.44           C  
ANISOU 6830  CG  ASN C 245     7725   3845   4173   1025   1637    448       C  
ATOM   6831  OD1 ASN C 245       2.435 113.984  31.639  1.00 42.95           O  
ANISOU 6831  OD1 ASN C 245     7811   4048   4458    889   1617    425       O  
ATOM   6832  ND2 ASN C 245       1.377 115.484  30.369  1.00 46.07           N  
ANISOU 6832  ND2 ASN C 245     8478   4357   4668   1150   1727    483       N  
ATOM   6833  N   GLN C 246      -0.519 112.266  30.304  1.00 31.16           N  
ANISOU 6833  N   GLN C 246     6162   2860   2818   1226   1362    423       N  
ATOM   6834  CA  GLN C 246      -0.387 110.832  29.913  1.00 32.05           C  
ANISOU 6834  CA  GLN C 246     6131   3061   2983   1180   1274    398       C  
ATOM   6835  C   GLN C 246       0.956 110.262  30.417  1.00 31.36           C  
ANISOU 6835  C   GLN C 246     5977   2925   3014   1002   1290    390       C  
ATOM   6836  O   GLN C 246       1.052 109.104  30.897  1.00 26.78           O  
ANISOU 6836  O   GLN C 246     5256   2413   2504    919   1211    365       O  
ATOM   6837  CB  GLN C 246      -0.587 110.679  28.394  1.00 34.62           C  
ANISOU 6837  CB  GLN C 246     6514   3408   3230   1311   1280    409       C  
ATOM   6838  CG  GLN C 246      -0.986 109.269  27.936  1.00 37.17           C  
ANISOU 6838  CG  GLN C 246     6696   3853   3572   1311   1174    372       C  
ATOM   6839  CD  GLN C 246      -2.271 108.735  28.534  1.00 36.95           C  
ANISOU 6839  CD  GLN C 246     6548   3961   3529   1340   1070    328       C  
ATOM   6840  OE1 GLN C 246      -3.121 109.474  29.047  1.00 36.00           O  
ANISOU 6840  OE1 GLN C 246     6454   3868   3354   1412   1066    328       O  
ATOM   6841  NE2 GLN C 246      -2.422 107.428  28.481  1.00 37.28           N  
ANISOU 6841  NE2 GLN C 246     6458   4087   3619   1279    993    288       N  
ATOM   6842  N   GLU C 247       2.031 111.046  30.308  1.00 30.72           N  
ANISOU 6842  N   GLU C 247     5994   2726   2951    943   1399    408       N  
ATOM   6843  CA  GLU C 247       3.331 110.567  30.766  1.00 30.87           C  
ANISOU 6843  CA  GLU C 247     5940   2716   3072    783   1416    392       C  
ATOM   6844  C   GLU C 247       3.333 110.362  32.293  1.00 27.86           C  
ANISOU 6844  C   GLU C 247     5456   2372   2755    678   1364    366       C  
ATOM   6845  O   GLU C 247       4.002 109.479  32.796  1.00 25.11           O  
ANISOU 6845  O   GLU C 247     4993   2061   2483    578   1320    347       O  
ATOM   6846  CB  GLU C 247       4.450 111.531  30.376  1.00 34.01           C  
ANISOU 6846  CB  GLU C 247     6458   2988   3474    730   1553    403       C  
ATOM   6847  CG  GLU C 247       5.821 110.869  30.371  1.00 35.41           C  
ANISOU 6847  CG  GLU C 247     6552   3161   3740    598   1568    382       C  
ATOM   6848  CD  GLU C 247       5.943 109.672  29.438  1.00 32.32           C  
ANISOU 6848  CD  GLU C 247     6091   2829   3358    635   1510    389       C  
ATOM   6849  OE1 GLU C 247       5.205 109.606  28.436  1.00 35.10           O  
ANISOU 6849  OE1 GLU C 247     6502   3195   3638    763   1497    410       O  
ATOM   6850  OE2 GLU C 247       6.748 108.795  29.728  1.00 36.58           O  
ANISOU 6850  OE2 GLU C 247     6519   3407   3971    543   1476    370       O  
ATOM   6851  N   LYS C 248       2.632 111.213  33.036  1.00 29.93           N  
ANISOU 6851  N   LYS C 248     5768   2620   2982    706   1375    367       N  
ATOM   6852  CA  LYS C 248       2.587 111.043  34.512  1.00 28.83           C  
ANISOU 6852  CA  LYS C 248     5537   2517   2897    613   1325    342       C  
ATOM   6853  C   LYS C 248       1.859 109.740  34.877  1.00 27.08           C  
ANISOU 6853  C   LYS C 248     5175   2413   2699    623   1205    329       C  
ATOM   6854  O   LYS C 248       2.218 109.083  35.883  1.00 24.91           O  
ANISOU 6854  O   LYS C 248     4799   2175   2490    527   1158    311       O  
ATOM   6855  CB  LYS C 248       1.951 112.239  35.218  1.00 29.44           C  
ANISOU 6855  CB  LYS C 248     5705   2553   2927    647   1366    346       C  
ATOM   6856  CG  LYS C 248       1.873 112.094  36.733  1.00 29.85           C  
ANISOU 6856  CG  LYS C 248     5669   2644   3028    559   1316    320       C  
ATOM   6857  CD  LYS C 248       3.220 112.220  37.432  1.00 32.07           C  
ANISOU 6857  CD  LYS C 248     5919   2884   3381    407   1358    292       C  
ATOM   6858  CE  LYS C 248       3.132 112.048  38.938  1.00 33.61           C  
ANISOU 6858  CE  LYS C 248     6028   3127   3615    333   1303    266       C  
ATOM   6859  NZ  LYS C 248       4.466 112.151  39.588  1.00 35.18           N  
ANISOU 6859  NZ  LYS C 248     6184   3308   3875    194   1337    227       N  
ATOM   6860  N   ARG C 249       0.821 109.412  34.094  1.00 26.04           N  
ANISOU 6860  N   ARG C 249     5043   2340   2508    739   1161    335       N  
ATOM   6861  CA  ARG C 249       0.085 108.167  34.217  1.00 26.26           C  
ANISOU 6861  CA  ARG C 249     4949   2474   2553    745   1062    313       C  
ATOM   6862  C   ARG C 249       1.038 106.993  33.967  1.00 24.72           C  
ANISOU 6862  C   ARG C 249     4678   2285   2428    662   1042    307       C  
ATOM   6863  O   ARG C 249       0.992 105.996  34.719  1.00 26.35           O  
ANISOU 6863  O   ARG C 249     4782   2542   2685    597    983    290       O  
ATOM   6864  CB  ARG C 249      -1.115 108.142  33.257  1.00 26.54           C  
ANISOU 6864  CB  ARG C 249     5002   2578   2502    886   1030    307       C  
ATOM   6865  CG  ARG C 249      -2.278 109.017  33.691  1.00 26.38           C  
ANISOU 6865  CG  ARG C 249     5021   2591   2411    979   1024    305       C  
ATOM   6866  CD  ARG C 249      -3.311 109.199  32.589  1.00 27.56           C  
ANISOU 6866  CD  ARG C 249     5203   2811   2457   1141   1005    297       C  
ATOM   6867  NE  ARG C 249      -4.455 109.962  33.058  1.00 27.20           N  
ANISOU 6867  NE  ARG C 249     5179   2815   2339   1239    993    292       N  
ATOM   6868  CZ  ARG C 249      -5.523 110.261  32.330  1.00 26.58           C  
ANISOU 6868  CZ  ARG C 249     5120   2821   2155   1399    970    279       C  
ATOM   6869  NH1 ARG C 249      -5.513 110.038  31.032  1.00 26.83           N  
ANISOU 6869  NH1 ARG C 249     5179   2879   2134   1487    968    278       N  
ATOM   6870  NH2 ARG C 249      -6.587 110.787  32.907  1.00 26.24           N  
ANISOU 6870  NH2 ARG C 249     5068   2844   2055   1478    948    266       N  
ATOM   6871  N   HIS C 250       1.877 107.087  32.913  1.00 25.21           N  
ANISOU 6871  N   HIS C 250     4796   2296   2487    672   1094    322       N  
ATOM   6872  CA  HIS C 250       2.823 106.024  32.604  1.00 25.22           C  
ANISOU 6872  CA  HIS C 250     4732   2301   2547    606   1081    318       C  
ATOM   6873  C   HIS C 250       3.787 105.839  33.781  1.00 23.25           C  
ANISOU 6873  C   HIS C 250     4421   2039   2372    486   1084    310       C  
ATOM   6874  O   HIS C 250       4.134 104.722  34.135  1.00 24.52           O  
ANISOU 6874  O   HIS C 250     4494   2240   2581    437   1037    302       O  
ATOM   6875  CB  HIS C 250       3.631 106.232  31.310  1.00 25.51           C  
ANISOU 6875  CB  HIS C 250     4841   2282   2568    633   1146    336       C  
ATOM   6876  CG  HIS C 250       2.827 106.305  30.051  1.00 25.34           C  
ANISOU 6876  CG  HIS C 250     4879   2280   2467    760   1142    342       C  
ATOM   6877  ND1 HIS C 250       1.788 105.451  29.786  1.00 24.94           N  
ANISOU 6877  ND1 HIS C 250     4763   2321   2389    816   1060    319       N  
ATOM   6878  CD2 HIS C 250       2.907 107.136  28.990  1.00 25.66           C  
ANISOU 6878  CD2 HIS C 250     5041   2265   2442    846   1212    365       C  
ATOM   6879  CE1 HIS C 250       1.235 105.762  28.632  1.00 24.89           C  
ANISOU 6879  CE1 HIS C 250     4824   2330   2302    936   1070    323       C  
ATOM   6880  NE2 HIS C 250       1.910 106.789  28.115  1.00 26.12           N  
ANISOU 6880  NE2 HIS C 250     5102   2393   2430    964   1163    357       N  
ATOM   6881  N   GLN C 251       4.226 106.946  34.371  1.00 24.88           N  
ANISOU 6881  N   GLN C 251     4679   2191   2581    444   1142    310       N  
ATOM   6882  CA  GLN C 251       5.175 106.897  35.443  1.00 25.84           C  
ANISOU 6882  CA  GLN C 251     4742   2313   2763    336   1147    292       C  
ATOM   6883  C   GLN C 251       4.507 106.242  36.663  1.00 24.75           C  
ANISOU 6883  C   GLN C 251     4520   2241   2643    319   1066    283       C  
ATOM   6884  O   GLN C 251       5.094 105.369  37.316  1.00 25.36           O  
ANISOU 6884  O   GLN C 251     4511   2356   2766    262   1029    273       O  
ATOM   6885  CB  GLN C 251       5.661 108.300  35.773  1.00 28.65           C  
ANISOU 6885  CB  GLN C 251     5179   2595   3109    292   1233    283       C  
ATOM   6886  CG  GLN C 251       6.648 108.343  36.934  1.00 33.20           C  
ANISOU 6886  CG  GLN C 251     5686   3188   3741    177   1236    249       C  
ATOM   6887  CD  GLN C 251       6.818 109.747  37.469  1.00 37.35           C  
ANISOU 6887  CD  GLN C 251     6291   3648   4252    129   1314    229       C  
ATOM   6888  OE1 GLN C 251       5.870 110.523  37.517  1.00 40.52           O  
ANISOU 6888  OE1 GLN C 251     6780   4012   4603    189   1333    244       O  
ATOM   6889  NE2 GLN C 251       8.031 110.076  37.885  1.00 42.37           N  
ANISOU 6889  NE2 GLN C 251     6896   4274   4927     20   1363    188       N  
ATOM   6890  N   LEU C 252       3.273 106.647  36.954  1.00 22.05           N  
ANISOU 6890  N   LEU C 252     4204   1914   2258    376   1044    285       N  
ATOM   6891  CA  LEU C 252       2.571 106.061  38.123  1.00 23.23           C  
ANISOU 6891  CA  LEU C 252     4279   2123   2423    357    977    275       C  
ATOM   6892  C   LEU C 252       2.345 104.540  37.921  1.00 23.36           C  
ANISOU 6892  C   LEU C 252     4216   2196   2463    358    917    272       C  
ATOM   6893  O   LEU C 252       2.515 103.747  38.840  1.00 23.57           O  
ANISOU 6893  O   LEU C 252     4177   2253   2525    309    882    267       O  
ATOM   6894  CB  LEU C 252       1.259 106.812  38.351  1.00 23.41           C  
ANISOU 6894  CB  LEU C 252     4346   2159   2390    426    971    275       C  
ATOM   6895  CG  LEU C 252       1.375 108.236  38.893  1.00 24.90           C  
ANISOU 6895  CG  LEU C 252     4617   2288   2556    418   1029    277       C  
ATOM   6896  CD1 LEU C 252       0.010 108.893  38.876  1.00 26.04           C  
ANISOU 6896  CD1 LEU C 252     4809   2451   2631    516   1022    282       C  
ATOM   6897  CD2 LEU C 252       1.952 108.270  40.312  1.00 25.60           C  
ANISOU 6897  CD2 LEU C 252     4656   2379   2688    323   1019    260       C  
ATOM   6898  N   ALA C 253       1.925 104.138  36.711  1.00 24.68           N  
ANISOU 6898  N   ALA C 253     4397   2376   2604    418    911    273       N  
ATOM   6899  CA  ALA C 253       1.698 102.731  36.349  1.00 24.20           C  
ANISOU 6899  CA  ALA C 253     4276   2358   2560    415    867    262       C  
ATOM   6900  C   ALA C 253       2.983 101.909  36.498  1.00 22.72           C  
ANISOU 6900  C   ALA C 253     4051   2152   2426    354    873    272       C  
ATOM   6901  O   ALA C 253       2.962 100.825  37.033  1.00 23.80           O  
ANISOU 6901  O   ALA C 253     4137   2316   2590    325    841    267       O  
ATOM   6902  CB  ALA C 253       1.164 102.638  34.941  1.00 23.97           C  
ANISOU 6902  CB  ALA C 253     4276   2344   2486    491    867    255       C  
ATOM   6903  N   GLY C 254       4.097 102.448  36.017  1.00 22.50           N  
ANISOU 6903  N   GLY C 254     4056   2082   2409    341    920    283       N  
ATOM   6904  CA  GLY C 254       5.399 101.796  36.063  1.00 23.43           C  
ANISOU 6904  CA  GLY C 254     4135   2195   2570    295    930    287       C  
ATOM   6905  C   GLY C 254       5.888 101.621  37.485  1.00 25.32           C  
ANISOU 6905  C   GLY C 254     4320   2460   2841    239    910    281       C  
ATOM   6906  O   GLY C 254       6.418 100.569  37.834  1.00 25.16           O  
ANISOU 6906  O   GLY C 254     4249   2464   2844    225    886    284       O  
ATOM   6907  N   LYS C 255       5.631 102.620  38.332  1.00 25.18           N  
ANISOU 6907  N   LYS C 255     4317   2436   2814    218    918    272       N  
ATOM   6908  CA  LYS C 255       6.002 102.533  39.732  1.00 25.33           C  
ANISOU 6908  CA  LYS C 255     4287   2486   2852    172    895    262       C  
ATOM   6909  C   LYS C 255       5.113 101.484  40.423  1.00 23.07           C  
ANISOU 6909  C   LYS C 255     3968   2234   2564    189    842    270       C  
ATOM   6910  O   LYS C 255       5.582 100.800  41.326  1.00 25.73           O  
ANISOU 6910  O   LYS C 255     4260   2599   2916    170    819    272       O  
ATOM   6911  CB  LYS C 255       5.909 103.925  40.371  1.00 31.23           C  
ANISOU 6911  CB  LYS C 255     5069   3210   3585    143    925    247       C  
ATOM   6912  CG  LYS C 255       6.920 104.927  39.815  1.00 36.02           C  
ANISOU 6912  CG  LYS C 255     5712   3774   4197    105    995    231       C  
ATOM   6913  CD  LYS C 255       8.350 104.533  40.062  1.00 39.41           C  
ANISOU 6913  CD  LYS C 255     6072   4240   4662     50   1001    209       C  
ATOM   6914  CE  LYS C 255       9.328 105.562  39.538  1.00 46.44           C  
ANISOU 6914  CE  LYS C 255     6993   5090   5559     -5   1082    180       C  
ATOM   6915  NZ  LYS C 255      10.668 104.970  39.330  1.00 45.99           N  
ANISOU 6915  NZ  LYS C 255     6861   5078   5533    -39   1089    160       N  
ATOM   6916  N   TYR C 256       3.847 101.355  39.989  1.00 21.63           N  
ANISOU 6916  N   TYR C 256     3807   2051   2358    227    829    271       N  
ATOM   6917  CA  TYR C 256       2.966 100.355  40.553  1.00 24.49           C  
ANISOU 6917  CA  TYR C 256     4141   2443   2721    229    794    269       C  
ATOM   6918  C   TYR C 256       3.422  98.961  40.084  1.00 22.45           C  
ANISOU 6918  C   TYR C 256     3863   2185   2482    229    788    276       C  
ATOM   6919  O   TYR C 256       3.419  98.047  40.875  1.00 24.49           O  
ANISOU 6919  O   TYR C 256     4101   2452   2750    215    775    282       O  
ATOM   6920  CB  TYR C 256       1.470 100.533  40.232  1.00 25.63           C  
ANISOU 6920  CB  TYR C 256     4296   2607   2833    262    781    253       C  
ATOM   6921  CG  TYR C 256       0.655  99.467  40.927  1.00 27.35           C  
ANISOU 6921  CG  TYR C 256     4479   2854   3058    242    758    242       C  
ATOM   6922  CD1 TYR C 256       0.336  99.547  42.278  1.00 27.31           C  
ANISOU 6922  CD1 TYR C 256     4459   2860   3054    218    749    244       C  
ATOM   6923  CD2 TYR C 256       0.314  98.306  40.258  1.00 27.50           C  
ANISOU 6923  CD2 TYR C 256     4486   2881   3082    241    755    228       C  
ATOM   6924  CE1 TYR C 256      -0.327  98.508  42.921  1.00 26.71           C  
ANISOU 6924  CE1 TYR C 256     4364   2800   2985    195    743    236       C  
ATOM   6925  CE2 TYR C 256      -0.342  97.267  40.879  1.00 26.86           C  
ANISOU 6925  CE2 TYR C 256     4384   2812   3008    209    752    214       C  
ATOM   6926  CZ  TYR C 256      -0.669  97.365  42.213  1.00 27.77           C  
ANISOU 6926  CZ  TYR C 256     4490   2934   3126    187    749    220       C  
ATOM   6927  OH  TYR C 256      -1.298  96.292  42.766  1.00 28.87           O  
ANISOU 6927  OH  TYR C 256     4622   3076   3272    153    760    206       O  
ATOM   6928  N   THR C 257       3.797  98.831  38.812  1.00 22.07           N  
ANISOU 6928  N   THR C 257     3832   2120   2433    250    804    277       N  
ATOM   6929  CA  THR C 257       4.333  97.581  38.313  1.00 22.82           C  
ANISOU 6929  CA  THR C 257     3917   2208   2543    254    805    284       C  
ATOM   6930  C   THR C 257       5.528  97.113  39.169  1.00 22.88           C  
ANISOU 6930  C   THR C 257     3898   2223   2572    239    805    301       C  
ATOM   6931  O   THR C 257       5.604  95.925  39.568  1.00 23.43           O  
ANISOU 6931  O   THR C 257     3963   2293   2646    244    799    311       O  
ATOM   6932  CB  THR C 257       4.688  97.680  36.834  1.00 23.23           C  
ANISOU 6932  CB  THR C 257     3995   2242   2588    282    826    283       C  
ATOM   6933  OG1 THR C 257       3.505  98.009  36.100  1.00 23.59           O  
ANISOU 6933  OG1 THR C 257     4062   2299   2602    312    818    264       O  
ATOM   6934  CG2 THR C 257       5.234  96.361  36.354  1.00 24.33           C  
ANISOU 6934  CG2 THR C 257     4129   2372   2742    288    829    290       C  
ATOM   6935  N   THR C 258       6.427  98.035  39.504  1.00 23.81           N  
ANISOU 6935  N   THR C 258     4000   2349   2696    223    816    300       N  
ATOM   6936  CA  THR C 258       7.594  97.730  40.316  1.00 24.78           C  
ANISOU 6936  CA  THR C 258     4082   2504   2830    215    811    303       C  
ATOM   6937  C   THR C 258       7.152  97.163  41.663  1.00 27.22           C  
ANISOU 6937  C   THR C 258     4379   2832   3129    219    783    311       C  
ATOM   6938  O   THR C 258       7.687  96.163  42.150  1.00 24.44           O  
ANISOU 6938  O   THR C 258     4015   2497   2772    245    775    326       O  
ATOM   6939  CB  THR C 258       8.478  98.956  40.536  1.00 25.82           C  
ANISOU 6939  CB  THR C 258     4190   2651   2968    180    830    282       C  
ATOM   6940  OG1 THR C 258       8.853  99.459  39.250  1.00 27.55           O  
ANISOU 6940  OG1 THR C 258     4434   2839   3193    177    870    278       O  
ATOM   6941  CG2 THR C 258       9.704  98.658  41.372  1.00 27.34           C  
ANISOU 6941  CG2 THR C 258     4320   2902   3164    176    818    272       C  
ATOM   6942  N   ARG C 259       6.179  97.845  42.286  1.00 28.15           N  
ANISOU 6942  N   ARG C 259     4509   2948   3238    200    773    303       N  
ATOM   6943  CA  ARG C 259       5.697  97.433  43.587  1.00 27.34           C  
ANISOU 6943  CA  ARG C 259     4402   2862   3123    201    754    309       C  
ATOM   6944  C   ARG C 259       5.098  96.021  43.488  1.00 24.70           C  
ANISOU 6944  C   ARG C 259     4093   2505   2786    219    758    325       C  
ATOM   6945  O   ARG C 259       5.292  95.206  44.397  1.00 26.36           O  
ANISOU 6945  O   ARG C 259     4309   2720   2984    236    756    341       O  
ATOM   6946  CB  ARG C 259       4.697  98.449  44.154  1.00 29.21           C  
ANISOU 6946  CB  ARG C 259     4650   3099   3350    179    748    296       C  
ATOM   6947  CG  ARG C 259       4.112  98.045  45.501  1.00 29.24           C  
ANISOU 6947  CG  ARG C 259     4653   3116   3339    179    733    303       C  
ATOM   6948  CD  ARG C 259       2.691  97.541  45.340  1.00 32.66           C  
ANISOU 6948  CD  ARG C 259     5107   3533   3768    175    739    300       C  
ATOM   6949  NE  ARG C 259       2.279  96.801  46.525  1.00 39.63           N  
ANISOU 6949  NE  ARG C 259     5998   4418   4639    174    739    311       N  
ATOM   6950  CZ  ARG C 259       1.612  95.653  46.536  1.00 45.11           C  
ANISOU 6950  CZ  ARG C 259     6714   5090   5333    169    760    314       C  
ATOM   6951  NH1 ARG C 259       1.214  95.180  47.702  1.00 57.61           N  
ANISOU 6951  NH1 ARG C 259     8316   6670   6902    166    771    325       N  
ATOM   6952  NH2 ARG C 259       1.341  94.985  45.420  1.00 41.05           N  
ANISOU 6952  NH2 ARG C 259     6209   4555   4830    162    776    303       N  
ATOM   6953  N   LEU C 260       4.348  95.767  42.416  1.00 22.83           N  
ANISOU 6953  N   LEU C 260     3875   2243   2553    215    770    314       N  
ATOM   6954  CA  LEU C 260       3.709  94.477  42.179  1.00 25.29           C  
ANISOU 6954  CA  LEU C 260     4213   2530   2864    214    785    314       C  
ATOM   6955  C   LEU C 260       4.766  93.357  42.067  1.00 26.04           C  
ANISOU 6955  C   LEU C 260     4325   2607   2961    244    800    338       C  
ATOM   6956  O   LEU C 260       4.615  92.287  42.668  1.00 24.77           O  
ANISOU 6956  O   LEU C 260     4197   2423   2790    253    819    352       O  
ATOM   6957  CB  LEU C 260       2.857  94.608  40.912  1.00 25.06           C  
ANISOU 6957  CB  LEU C 260     4189   2497   2835    206    788    285       C  
ATOM   6958  CG  LEU C 260       2.071  93.374  40.521  1.00 26.82           C  
ANISOU 6958  CG  LEU C 260     4432   2701   3057    187    808    264       C  
ATOM   6959  CD1 LEU C 260       1.081  93.006  41.603  1.00 30.10           C  
ANISOU 6959  CD1 LEU C 260     4850   3118   3467    153    818    252       C  
ATOM   6960  CD2 LEU C 260       1.354  93.596  39.208  1.00 28.69           C  
ANISOU 6960  CD2 LEU C 260     4661   2954   3285    188    803    226       C  
ATOM   6961  N   LEU C 261       5.844  93.612  41.310  1.00 27.48           N  
ANISOU 6961  N   LEU C 261     4490   2798   3150    266    799    344       N  
ATOM   6962  CA  LEU C 261       6.915  92.635  41.139  1.00 29.06           C  
ANISOU 6962  CA  LEU C 261     4700   2993   3347    307    812    366       C  
ATOM   6963  C   LEU C 261       7.715  92.476  42.430  1.00 30.03           C  
ANISOU 6963  C   LEU C 261     4805   3152   3451    342    800    386       C  
ATOM   6964  O   LEU C 261       8.183  91.382  42.726  1.00 29.74           O  
ANISOU 6964  O   LEU C 261     4798   3106   3395    391    814    410       O  
ATOM   6965  CB  LEU C 261       7.830  93.057  39.999  1.00 29.15           C  
ANISOU 6965  CB  LEU C 261     4689   3014   3371    318    817    361       C  
ATOM   6966  CG  LEU C 261       7.141  93.021  38.645  1.00 29.57           C  
ANISOU 6966  CG  LEU C 261     4769   3033   3430    305    830    345       C  
ATOM   6967  CD1 LEU C 261       8.016  93.670  37.598  1.00 31.06           C  
ANISOU 6967  CD1 LEU C 261     4941   3229   3628    315    841    343       C  
ATOM   6968  CD2 LEU C 261       6.751  91.597  38.284  1.00 29.07           C  
ANISOU 6968  CD2 LEU C 261     4752   2931   3362    315    851    348       C  
ATOM   6969  N   ARG C 262       7.821  93.543  43.215  1.00 28.01           N  
ANISOU 6969  N   ARG C 262     4509   2939   3194    323    776    373       N  
ATOM   6970  CA  ARG C 262       8.554  93.439  44.489  1.00 31.22           C  
ANISOU 6970  CA  ARG C 262     4890   3396   3573    360    757    383       C  
ATOM   6971  C   ARG C 262       7.707  92.777  45.591  1.00 29.44           C  
ANISOU 6971  C   ARG C 262     4714   3147   3324    373    763    403       C  
ATOM   6972  O   ARG C 262       8.267  92.071  46.455  1.00 33.12           O  
ANISOU 6972  O   ARG C 262     5194   3634   3754    434    761    426       O  
ATOM   6973  CB  ARG C 262       9.053  94.806  44.954  1.00 34.79           C  
ANISOU 6973  CB  ARG C 262     5282   3906   4030    327    734    353       C  
ATOM   6974  CG  ARG C 262      10.256  95.345  44.197  1.00 37.20           C  
ANISOU 6974  CG  ARG C 262     5534   4250   4351    319    738    330       C  
ATOM   6975  CD  ARG C 262      11.084  96.226  45.118  1.00 42.29           C  
ANISOU 6975  CD  ARG C 262     6110   4973   4983    302    717    295       C  
ATOM   6976  NE  ARG C 262      11.532  97.449  44.488  1.00 46.18           N  
ANISOU 6976  NE  ARG C 262     6571   5472   5502    237    738    256       N  
ATOM   6977  CZ  ARG C 262      12.779  97.718  44.074  1.00 58.72           C  
ANISOU 6977  CZ  ARG C 262     8098   7113   7098    225    751    224       C  
ATOM   6978  NH1 ARG C 262      13.055  98.934  43.612  1.00 44.83           N  
ANISOU 6978  NH1 ARG C 262     6326   5346   5362    152    785    185       N  
ATOM   6979  NH2 ARG C 262      13.730  96.791  44.136  1.00 58.17           N  
ANISOU 6979  NH2 ARG C 262     7985   7106   7010    288    738    230       N  
ATOM   6980  N   HIS C 263       6.387  93.006  45.637  1.00 27.88           N  
ANISOU 6980  N   HIS C 263     4542   2912   3138    323    772    393       N  
ATOM   6981  CA  HIS C 263       5.616  92.603  46.852  1.00 29.55           C  
ANISOU 6981  CA  HIS C 263     4790   3109   3327    326    781    406       C  
ATOM   6982  C   HIS C 263       4.301  91.907  46.522  1.00 30.46           C  
ANISOU 6982  C   HIS C 263     4955   3164   3453    285    819    399       C  
ATOM   6983  O   HIS C 263       3.569  91.554  47.448  1.00 29.22           O  
ANISOU 6983  O   HIS C 263     4832   2988   3279    276    840    405       O  
ATOM   6984  CB  HIS C 263       5.332  93.793  47.780  1.00 29.55           C  
ANISOU 6984  CB  HIS C 263     4755   3151   3322    301    751    390       C  
ATOM   6985  CG  HIS C 263       6.573  94.418  48.309  1.00 31.54           C  
ANISOU 6985  CG  HIS C 263     4954   3469   3558    329    719    383       C  
ATOM   6986  ND1 HIS C 263       7.437  93.742  49.140  1.00 34.61           N  
ANISOU 6986  ND1 HIS C 263     5345   3897   3908    398    710    403       N  
ATOM   6987  CD2 HIS C 263       7.113  95.637  48.101  1.00 35.24           C  
ANISOU 6987  CD2 HIS C 263     5369   3979   4042    298    698    352       C  
ATOM   6988  CE1 HIS C 263       8.450  94.527  49.447  1.00 37.74           C  
ANISOU 6988  CE1 HIS C 263     5673   4370   4296    404    677    376       C  
ATOM   6989  NE2 HIS C 263       8.278  95.702  48.813  1.00 36.80           N  
ANISOU 6989  NE2 HIS C 263     5521   4246   4213    334    674    343       N  
ATOM   6990  N   GLY C 264       4.022  91.671  45.236  1.00 30.20           N  
ANISOU 6990  N   GLY C 264     4926   3106   3442    261    833    380       N  
ATOM   6991  CA  GLY C 264       2.744  91.073  44.844  1.00 28.59           C  
ANISOU 6991  CA  GLY C 264     4752   2862   3247    211    867    355       C  
ATOM   6992  C   GLY C 264       2.601  89.660  45.369  1.00 28.23           C  
ANISOU 6992  C   GLY C 264     4782   2758   3184    218    923    373       C  
ATOM   6993  O   GLY C 264       3.591  89.037  45.773  1.00 27.94           O  
ANISOU 6993  O   GLY C 264     4783   2707   3125    281    934    412       O  
ATOM   6994  N   GLN C 265       1.362  89.160  45.307  1.00 29.17           N  
ANISOU 6994  N   GLN C 265     4925   2846   3310    156    964    339       N  
ATOM   6995  CA  GLN C 265       1.007  87.831  45.740  1.00 33.48           C  
ANISOU 6995  CA  GLN C 265     5557   3320   3842    140   1038    346       C  
ATOM   6996  C   GLN C 265       1.716  86.805  44.835  1.00 31.01           C  
ANISOU 6996  C   GLN C 265     5298   2955   3527    167   1071    356       C  
ATOM   6997  O   GLN C 265       1.731  86.939  43.587  1.00 28.90           O  
ANISOU 6997  O   GLN C 265     4997   2701   3280    148   1053    326       O  
ATOM   6998  CB  GLN C 265      -0.513  87.653  45.717  1.00 35.59           C  
ANISOU 6998  CB  GLN C 265     5818   3579   4123     46   1076    288       C  
ATOM   6999  CG  GLN C 265      -1.241  88.428  46.813  1.00 44.35           C  
ANISOU 6999  CG  GLN C 265     6895   4728   5227     27   1061    284       C  
ATOM   7000  N   LYS C 266       2.266  85.766  45.473  1.00 30.57           N  
ANISOU 7000  N   LYS C 266     5336   2838   3439    219   1124    400       N  
ATOM   7001  CA  LYS C 266       2.934  84.630  44.779  1.00 33.64           C  
ANISOU 7001  CA  LYS C 266     5801   3163   3816    257   1172    417       C  
ATOM   7002  C   LYS C 266       3.952  85.180  43.772  1.00 34.09           C  
ANISOU 7002  C   LYS C 266     5792   3273   3886    303   1110    423       C  
ATOM   7003  O   LYS C 266       3.958  84.779  42.559  1.00 29.92           O  
ANISOU 7003  O   LYS C 266     5272   2721   3374    281   1124    398       O  
ATOM   7004  CB  LYS C 266       1.914  83.781  44.013  1.00 36.03           C  
ANISOU 7004  CB  LYS C 266     6151   3400   4137    162   1241    361       C  
ATOM   7005  CG  LYS C 266       0.783  83.208  44.845  1.00 41.90           C  
ANISOU 7005  CG  LYS C 266     6956   4088   4875     88   1319    337       C  
ATOM   7006  CD  LYS C 266      -0.101  82.306  44.029  1.00 46.99           C  
ANISOU 7006  CD  LYS C 266     7642   4673   5537    -13   1394    269       C  
ATOM   7007  CE  LYS C 266      -1.230  81.682  44.819  1.00 54.09           C  
ANISOU 7007  CE  LYS C 266     8603   5514   6433   -104   1489    234       C  
ATOM   7008  NZ  LYS C 266      -2.200  81.037  43.899  1.00 58.35           N  
ANISOU 7008  NZ  LYS C 266     9145   6028   6997   -227   1549    139       N  
ATOM   7009  N   LYS C 267       4.782  86.132  44.230  1.00 33.11           N  
ANISOU 7009  N   LYS C 267     5600   3224   3755    359   1045    449       N  
ATOM   7010  CA  LYS C 267       5.665  86.832  43.307  1.00 32.68           C  
ANISOU 7010  CA  LYS C 267     5473   3224   3718    385    993    445       C  
ATOM   7011  C   LYS C 267       6.690  85.853  42.716  1.00 31.77           C  
ANISOU 7011  C   LYS C 267     5407   3077   3583    456   1021    473       C  
ATOM   7012  O   LYS C 267       7.120  86.051  41.571  1.00 30.22           O  
ANISOU 7012  O   LYS C 267     5178   2895   3407    455   1006    460       O  
ATOM   7013  CB  LYS C 267       6.361  88.039  43.942  1.00 35.87           C  
ANISOU 7013  CB  LYS C 267     5795   3714   4120    414    930    455       C  
ATOM   7014  CG  LYS C 267       7.159  87.780  45.207  1.00 39.35           C  
ANISOU 7014  CG  LYS C 267     6252   4183   4515    496    924    494       C  
ATOM   7015  CD  LYS C 267       8.194  88.850  45.440  1.00 41.56           C  
ANISOU 7015  CD  LYS C 267     6438   4559   4794    526    864    489       C  
ATOM   7016  CE  LYS C 267       8.679  88.833  46.871  1.00 45.69           C  
ANISOU 7016  CE  LYS C 267     6959   5131   5268    593    846    511       C  
ATOM   7017  NZ  LYS C 267       9.952  89.570  47.016  1.00 49.61           N  
ANISOU 7017  NZ  LYS C 267     7362   5731   5753    634    795    497       N  
ATOM   7018  N   ASN C 268       7.054  84.814  43.474  1.00 29.85           N  
ANISOU 7018  N   ASN C 268     5251   2790   3297    524   1067    513       N  
ATOM   7019  CA  ASN C 268       8.028  83.815  43.036  1.00 32.54           C  
ANISOU 7019  CA  ASN C 268     5654   3100   3608    611   1101    545       C  
ATOM   7020  C   ASN C 268       7.346  82.490  42.670  1.00 29.15           C  
ANISOU 7020  C   ASN C 268     5351   2551   3170    581   1192    541       C  
ATOM   7021  O   ASN C 268       7.932  81.405  42.801  1.00 29.41           O  
ANISOU 7021  O   ASN C 268     5486   2527   3159    665   1248    579       O  
ATOM   7022  CB  ASN C 268       9.110  83.623  44.097  1.00 36.28           C  
ANISOU 7022  CB  ASN C 268     6137   3621   4024    737   1088    595       C  
ATOM   7023  CG  ASN C 268       9.990  84.848  44.223  1.00 37.20           C  
ANISOU 7023  CG  ASN C 268     6121   3863   4150    760   1004    584       C  
ATOM   7024  OD1 ASN C 268      10.207  85.533  43.242  1.00 39.00           O  
ANISOU 7024  OD1 ASN C 268     6322   4156   4341    821    975    601       O  
ATOM   7025  ND2 ASN C 268      10.483  85.144  45.422  1.00 35.84           N  
ANISOU 7025  ND2 ASN C 268     5870   3724   4022    711    972    553       N  
ATOM   7026  N   PHE C 269       6.164  82.576  42.066  1.00 26.52           N  
ANISOU 7026  N   PHE C 269     5012   2185   2878    464   1209    486       N  
ATOM   7027  CA  PHE C 269       5.431  81.380  41.731  1.00 28.13           C  
ANISOU 7027  CA  PHE C 269     5327   2282   3078    410   1301    463       C  
ATOM   7028  C   PHE C 269       6.209  80.489  40.752  1.00 27.79           C  
ANISOU 7028  C   PHE C 269     5348   2189   3020    464   1337    476       C  
ATOM   7029  O   PHE C 269       6.026  79.292  40.787  1.00 26.56           O  
ANISOU 7029  O   PHE C 269     5321   1930   2839    465   1429    481       O  
ATOM   7030  CB  PHE C 269       4.072  81.727  41.128  1.00 29.30           C  
ANISOU 7030  CB  PHE C 269     5426   2435   3269    275   1300    385       C  
ATOM   7031  CG  PHE C 269       4.117  82.228  39.713  1.00 28.98           C  
ANISOU 7031  CG  PHE C 269     5310   2441   3258    247   1251    344       C  
ATOM   7032  CD1 PHE C 269       4.463  83.532  39.432  1.00 29.35           C  
ANISOU 7032  CD1 PHE C 269     5244   2581   3323    266   1164    346       C  
ATOM   7033  CD2 PHE C 269       3.818  81.375  38.660  1.00 30.54           C  
ANISOU 7033  CD2 PHE C 269     5560   2582   3461    203   1301    301       C  
ATOM   7034  CE1 PHE C 269       4.516  83.981  38.122  1.00 31.36           C  
ANISOU 7034  CE1 PHE C 269     5446   2872   3598    252   1129    314       C  
ATOM   7035  CE2 PHE C 269       3.900  81.815  37.352  1.00 29.57           C  
ANISOU 7035  CE2 PHE C 269     5375   2504   3356    191   1256    266       C  
ATOM   7036  CZ  PHE C 269       4.233  83.117  37.087  1.00 30.31           C  
ANISOU 7036  CZ  PHE C 269     5361   2688   3464    219   1171    275       C  
ATOM   7037  N   ALA C 270       7.011  81.074  39.840  1.00 27.14           N  
ANISOU 7037  N   ALA C 270     5185   2173   2954    501   1275    476       N  
ATOM   7038  CA  ALA C 270       7.503  80.327  38.646  1.00 27.55           C  
ANISOU 7038  CA  ALA C 270     5285   2179   3001    525   1308    471       C  
ATOM   7039  C   ALA C 270       8.350  79.099  39.034  1.00 27.87           C  
ANISOU 7039  C   ALA C 270     5454   2149   2987    638   1377    529       C  
ATOM   7040  O   ALA C 270       8.165  78.041  38.450  1.00 27.25           O  
ANISOU 7040  O   ALA C 270     5483   1974   2897    623   1454    516       O  
ATOM   7041  CB  ALA C 270       8.243  81.246  37.702  1.00 26.96           C  
ANISOU 7041  CB  ALA C 270     5101   2190   2950    549   1234    466       C  
ATOM   7042  N   ASN C 271       9.210  79.215  40.059  1.00 27.75           N  
ANISOU 7042  N   ASN C 271     5433   2179   2929    751   1356    587       N  
ATOM   7043  CA  ASN C 271      10.084  78.123  40.491  1.00 30.12           C  
ANISOU 7043  CA  ASN C 271     5852   2429   3161    889   1415    647       C  
ATOM   7044  C   ASN C 271       9.545  77.442  41.766  1.00 30.85           C  
ANISOU 7044  C   ASN C 271     6069   2443   3209    909   1488    677       C  
ATOM   7045  O   ASN C 271      10.283  76.720  42.418  1.00 31.70           O  
ANISOU 7045  O   ASN C 271     6272   2528   3245   1048   1527    736       O  
ATOM   7046  CB  ASN C 271      11.499  78.626  40.766  1.00 30.17           C  
ANISOU 7046  CB  ASN C 271     5770   2557   3136   1025   1344    687       C  
ATOM   7047  CG  ASN C 271      12.175  79.079  39.497  1.00 31.33           C  
ANISOU 7047  CG  ASN C 271     5824   2762   3317   1021   1299    665       C  
ATOM   7048  OD1 ASN C 271      12.371  78.278  38.585  1.00 37.15           O  
ANISOU 7048  OD1 ASN C 271     6634   3434   4047   1040   1348    666       O  
ATOM   7049  ND2 ASN C 271      12.517  80.350  39.419  1.00 29.42           N  
ANISOU 7049  ND2 ASN C 271     5431   2635   3109    994   1214    645       N  
ATOM   7050  N   SER C 272       8.285  77.715  42.126  1.00 31.29           N  
ANISOU 7050  N   SER C 272     6120   2466   3300    779   1505    636       N  
ATOM   7051  CA  SER C 272       7.657  77.235  43.356  1.00 31.89           C  
ANISOU 7051  CA  SER C 272     6301   2473   3340    777   1574    657       C  
ATOM   7052  C   SER C 272       7.165  75.796  43.166  1.00 34.63           C  
ANISOU 7052  C   SER C 272     6839   2656   3662    749   1716    654       C  
ATOM   7053  O   SER C 272       7.186  75.270  42.084  1.00 34.19           O  
ANISOU 7053  O   SER C 272     6818   2548   3623    714   1751    625       O  
ATOM   7054  CB  SER C 272       6.492  78.122  43.716  1.00 30.49           C  
ANISOU 7054  CB  SER C 272     6035   2333   3215    642   1540    607       C  
ATOM   7055  OG  SER C 272       5.415  77.907  42.799  1.00 29.84           O  
ANISOU 7055  OG  SER C 272     5956   2198   3185    492   1580    532       O  
ATOM   7056  N   LYS C 273       6.586  75.201  44.217  1.00 36.91           N  
ANISOU 7056  N   LYS C 273     7254   2856   3914    744   1807    674       N  
ATOM   7057  CA  LYS C 273       6.098  73.818  44.123  1.00 38.71           C  
ANISOU 7057  CA  LYS C 273     7682   2911   4114    708   1964    668       C  
ATOM   7058  C   LYS C 273       4.648  73.763  43.601  1.00 38.91           C  
ANISOU 7058  C   LYS C 273     7691   2883   4207    492   2016    569       C  
ATOM   7059  O   LYS C 273       4.019  72.724  43.606  1.00 41.85           O  
ANISOU 7059  O   LYS C 273     8217   3115   4568    419   2154    542       O  
ATOM   7060  CB  LYS C 273       6.260  73.139  45.490  1.00 39.10           C  
ANISOU 7060  CB  LYS C 273     7894   2879   4079    821   2053    742       C  
ATOM   7061  CG  LYS C 273       7.703  72.781  45.827  1.00 40.69           C  
ANISOU 7061  CG  LYS C 273     8157   3111   4193   1053   2035    833       C  
ATOM   7062  CD  LYS C 273       7.917  72.331  47.259  1.00 46.08           C  
ANISOU 7062  CD  LYS C 273     8975   3751   4780   1191   2096    909       C  
ATOM   7063  N   MET C 274       4.110  74.894  43.159  1.00 36.63           N  
ANISOU 7063  N   MET C 274     7219   2712   3986    390   1910    509       N  
ATOM   7064  CA  MET C 274       2.792  74.979  42.540  1.00 38.25           C  
ANISOU 7064  CA  MET C 274     7372   2909   4251    200   1934    404       C  
ATOM   7065  C   MET C 274       2.710  74.009  41.345  1.00 39.67           C  
ANISOU 7065  C   MET C 274     7634   2999   4438    141   2011    352       C  
ATOM   7066  O   MET C 274       3.706  73.806  40.675  1.00 39.37           O  
ANISOU 7066  O   MET C 274     7612   2963   4381    241   1984    389       O  
ATOM   7067  CB  MET C 274       2.624  76.423  42.079  1.00 39.52           C  
ANISOU 7067  CB  MET C 274     7322   3228   4465    164   1787    368       C  
ATOM   7068  CG  MET C 274       1.242  76.972  42.126  1.00 45.06           C  
ANISOU 7068  CG  MET C 274     7932   3976   5213     12   1778    283       C  
ATOM   7069  SD  MET C 274       1.312  78.780  41.784  1.00 47.81           S  
ANISOU 7069  SD  MET C 274     8058   4506   5601     26   1604    272       S  
ATOM   7070  CE  MET C 274       0.333  78.814  40.287  1.00 43.08           C  
ANISOU 7070  CE  MET C 274     7382   3942   5044   -108   1594    155       C  
ATOM   7071  N   LYS C 275       1.544  73.370  41.114  1.00 39.89           N  
ANISOU 7071  N   LYS C 275     7717   2948   4488    -20   2113    262       N  
ATOM   7072  CA  LYS C 275       1.327  72.478  39.946  1.00 40.66           C  
ANISOU 7072  CA  LYS C 275     7884   2968   4595   -102   2188    191       C  
ATOM   7073  C   LYS C 275       1.519  73.288  38.661  1.00 37.11           C  
ANISOU 7073  C   LYS C 275     7270   2646   4185   -109   2058    148       C  
ATOM   7074  O   LYS C 275       1.161  74.482  38.593  1.00 35.93           O  
ANISOU 7074  O   LYS C 275     6947   2632   4069   -136   1942    123       O  
ATOM   7075  CB  LYS C 275      -0.084  71.877  39.880  1.00 43.48           C  
ANISOU 7075  CB  LYS C 275     8282   3258   4978   -304   2303     74       C  
ATOM   7076  CG  LYS C 275      -0.411  70.770  40.869  1.00 48.66           C  
ANISOU 7076  CG  LYS C 275     9145   3745   5596   -335   2481     92       C  
ATOM   7077  CD  LYS C 275      -1.788  70.149  40.664  1.00 50.39           C  
ANISOU 7077  CD  LYS C 275     9395   3902   5846   -557   2605    -42       C  
ATOM   7078  N   TYR C 276       2.034  72.622  37.632  1.00 35.10           N  
ANISOU 7078  N   TYR C 276     7079   2338   3919    -87   2088    137       N  
ATOM   7079  CA  TYR C 276       2.266  73.245  36.347  1.00 34.20           C  
ANISOU 7079  CA  TYR C 276     6835   2325   3831    -86   1983     99       C  
ATOM   7080  C   TYR C 276       1.002  73.967  35.852  1.00 33.15           C  
ANISOU 7080  C   TYR C 276     6551   2298   3745   -235   1927    -15       C  
ATOM   7081  O   TYR C 276       1.087  75.128  35.454  1.00 32.88           O  
ANISOU 7081  O   TYR C 276     6363   2396   3732   -205   1800    -15       O  
ATOM   7082  CB  TYR C 276       2.729  72.199  35.326  1.00 35.00           C  
ANISOU 7082  CB  TYR C 276     7053   2332   3913    -73   2054     82       C  
ATOM   7083  CG  TYR C 276       2.792  72.689  33.902  1.00 33.84           C  
ANISOU 7083  CG  TYR C 276     6791   2276   3790    -93   1966     26       C  
ATOM   7084  CD1 TYR C 276       3.791  73.557  33.488  1.00 32.66           C  
ANISOU 7084  CD1 TYR C 276     6542   2224   3642     30   1851     90       C  
ATOM   7085  CD2 TYR C 276       1.863  72.275  32.961  1.00 35.45           C  
ANISOU 7085  CD2 TYR C 276     6986   2471   4010   -236   2004    -96       C  
ATOM   7086  CE1 TYR C 276       3.867  74.017  32.182  1.00 32.91           C  
ANISOU 7086  CE1 TYR C 276     6482   2332   3690     20   1778     44       C  
ATOM   7087  CE2 TYR C 276       1.946  72.696  31.639  1.00 35.21           C  
ANISOU 7087  CE2 TYR C 276     6860   2526   3991   -238   1924   -146       C  
ATOM   7088  CZ  TYR C 276       2.929  73.590  31.257  1.00 34.24           C  
ANISOU 7088  CZ  TYR C 276     6649   2491   3868   -107   1812    -71       C  
ATOM   7089  OH  TYR C 276       2.981  74.041  29.966  1.00 36.50           O  
ANISOU 7089  OH  TYR C 276     6849   2856   4160   -106   1740   -116       O  
ATOM   7090  N   GLU C 277      -0.140  73.267  35.850  1.00 34.49           N  
ANISOU 7090  N   GLU C 277     6768   2410   3924   -391   2026   -115       N  
ATOM   7091  CA  GLU C 277      -1.429  73.790  35.336  1.00 36.85           C  
ANISOU 7091  CA  GLU C 277     6924   2817   4257   -537   1985   -244       C  
ATOM   7092  C   GLU C 277      -1.798  75.096  36.055  1.00 35.50           C  
ANISOU 7092  C   GLU C 277     6606   2774   4105   -517   1881   -222       C  
ATOM   7093  O   GLU C 277      -2.313  76.026  35.438  1.00 32.88           O  
ANISOU 7093  O   GLU C 277     6121   2578   3791   -544   1780   -279       O  
ATOM   7094  CB  GLU C 277      -2.563  72.775  35.525  1.00 39.14           C  
ANISOU 7094  CB  GLU C 277     7295   3021   4552   -712   2129   -355       C  
ATOM   7095  N   ASP C 278      -1.506  75.157  37.356  1.00 34.91           N  
ANISOU 7095  N   ASP C 278     6590   2654   4020   -459   1907   -135       N  
ATOM   7096  CA  ASP C 278      -1.779  76.341  38.187  1.00 35.34           C  
ANISOU 7096  CA  ASP C 278     6525   2813   4087   -434   1819   -105       C  
ATOM   7097  C   ASP C 278      -0.842  77.491  37.793  1.00 34.19           C  
ANISOU 7097  C   ASP C 278     6274   2771   3944   -305   1679    -37       C  
ATOM   7098  O   ASP C 278      -1.260  78.658  37.736  1.00 30.23           O  
ANISOU 7098  O   ASP C 278     5634   2390   3461   -311   1582    -57       O  
ATOM   7099  CB  ASP C 278      -1.677  75.999  39.678  1.00 35.95           C  
ANISOU 7099  CB  ASP C 278     6709   2807   4144   -402   1894    -32       C  
ATOM   7100  CG  ASP C 278      -2.760  75.040  40.142  1.00 43.85           C  
ANISOU 7100  CG  ASP C 278     7803   3712   5146   -548   2040   -108       C  
ATOM   7101  OD1 ASP C 278      -3.817  74.977  39.469  1.00 45.72           O  
ANISOU 7101  OD1 ASP C 278     7965   3996   5408   -691   2055   -233       O  
ATOM   7102  OD2 ASP C 278      -2.522  74.326  41.150  1.00 42.85           O  
ANISOU 7102  OD2 ASP C 278     7828   3465   4988   -516   2144    -46       O  
ATOM   7103  N   LYS C 279       0.426  77.158  37.521  1.00 32.96           N  
ANISOU 7103  N   LYS C 279     6190   2566   3768   -189   1676     41       N  
ATOM   7104  CA  LYS C 279       1.434  78.123  37.109  1.00 29.27           C  
ANISOU 7104  CA  LYS C 279     5634   2184   3302    -74   1563    101       C  
ATOM   7105  C   LYS C 279       1.024  78.761  35.783  1.00 28.06           C  
ANISOU 7105  C   LYS C 279     5368   2122   3169   -118   1491     28       C  
ATOM   7106  O   LYS C 279       1.137  79.966  35.602  1.00 25.70           O  
ANISOU 7106  O   LYS C 279     4955   1926   2882    -80   1393     40       O  
ATOM   7107  CB  LYS C 279       2.799  77.448  36.978  1.00 30.19           C  
ANISOU 7107  CB  LYS C 279     5851   2231   3387     48   1591    182       C  
ATOM   7108  CG  LYS C 279       3.486  77.217  38.307  1.00 31.79           C  
ANISOU 7108  CG  LYS C 279     6130   2390   3555    147   1620    274       C  
ATOM   7109  CD  LYS C 279       4.780  76.470  38.203  1.00 32.42           C  
ANISOU 7109  CD  LYS C 279     6311   2411   3594    280   1653    348       C  
ATOM   7110  CE  LYS C 279       5.482  76.380  39.538  1.00 33.37           C  
ANISOU 7110  CE  LYS C 279     6488   2521   3669    399   1665    436       C  
ATOM   7111  NZ  LYS C 279       6.814  75.735  39.412  1.00 36.68           N  
ANISOU 7111  NZ  LYS C 279     6986   2909   4038    551   1684    507       N  
ATOM   7112  N   ILE C 280       0.520  77.946  34.871  1.00 28.45           N  
ANISOU 7112  N   ILE C 280     5458   2133   3218   -196   1545    -51       N  
ATOM   7113  CA  ILE C 280       0.139  78.427  33.556  1.00 30.77           C  
ANISOU 7113  CA  ILE C 280     5656   2514   3519   -226   1481   -124       C  
ATOM   7114  C   ILE C 280      -1.079  79.355  33.678  1.00 31.61           C  
ANISOU 7114  C   ILE C 280     5633   2737   3639   -298   1424   -197       C  
ATOM   7115  O   ILE C 280      -1.113  80.390  33.034  1.00 29.64           O  
ANISOU 7115  O   ILE C 280     5281   2592   3389   -258   1331   -206       O  
ATOM   7116  CB  ILE C 280      -0.118  77.251  32.601  1.00 32.48           C  
ANISOU 7116  CB  ILE C 280     5951   2662   3726   -297   1558   -202       C  
ATOM   7117  CG1 ILE C 280       1.180  76.505  32.272  1.00 32.94           C  
ANISOU 7117  CG1 ILE C 280     6126   2622   3765   -199   1598   -125       C  
ATOM   7118  CG2 ILE C 280      -0.841  77.702  31.339  1.00 32.57           C  
ANISOU 7118  CG2 ILE C 280     5855   2781   3736   -348   1496   -305       C  
ATOM   7119  CD1 ILE C 280       2.127  77.281  31.406  1.00 34.77           C  
ANISOU 7119  CD1 ILE C 280     6292   2924   3994    -92   1506    -77       C  
ATOM   7120  N   GLU C 281      -2.074  78.935  34.461  1.00 33.20           N  
ANISOU 7120  N   GLU C 281     5848   2917   3847   -401   1488   -250       N  
ATOM   7121  CA  GLU C 281      -3.292  79.703  34.712  1.00 34.32           C  
ANISOU 7121  CA  GLU C 281     5870   3171   3998   -471   1446   -323       C  
ATOM   7122  C   GLU C 281      -2.960  81.059  35.343  1.00 29.17           C  
ANISOU 7122  C   GLU C 281     5140   2592   3349   -379   1353   -245       C  
ATOM   7123  O   GLU C 281      -3.499  82.079  34.925  1.00 28.52           O  
ANISOU 7123  O   GLU C 281     4944   2628   3264   -369   1272   -282       O  
ATOM   7124  CB  GLU C 281      -4.227  78.932  35.646  1.00 37.30           C  
ANISOU 7124  CB  GLU C 281     6296   3493   4384   -592   1550   -378       C  
ATOM   7125  CG  GLU C 281      -5.121  77.922  34.954  1.00 45.03           C  
ANISOU 7125  CG  GLU C 281     7292   4453   5362   -733   1633   -512       C  
ATOM   7126  CD  GLU C 281      -5.967  77.082  35.911  1.00 50.70           C  
ANISOU 7126  CD  GLU C 281     8077   5096   6090   -864   1760   -565       C  
ATOM   7127  OE1 GLU C 281      -6.044  77.443  37.111  1.00 58.35           O  
ANISOU 7127  OE1 GLU C 281     9053   6052   7063   -844   1769   -505       O  
ATOM   7128  OE2 GLU C 281      -6.553  76.073  35.471  1.00 63.19           O  
ANISOU 7128  OE2 GLU C 281     9706   6630   7672   -990   1857   -670       O  
ATOM   7129  N   TRP C 282      -2.138  81.035  36.401  1.00 27.73           N  
ANISOU 7129  N   TRP C 282     5025   2342   3168   -314   1371   -142       N  
ATOM   7130  CA  TRP C 282      -1.668  82.220  37.092  1.00 26.82           C  
ANISOU 7130  CA  TRP C 282     4851   2282   3054   -231   1294    -67       C  
ATOM   7131  C   TRP C 282      -0.961  83.176  36.114  1.00 26.10           C  
ANISOU 7131  C   TRP C 282     4695   2260   2962   -147   1203    -41       C  
ATOM   7132  O   TRP C 282      -1.333  84.357  35.999  1.00 21.95           O  
ANISOU 7132  O   TRP C 282     4075   1827   2436   -130   1131    -52       O  
ATOM   7133  CB  TRP C 282      -0.747  81.823  38.256  1.00 28.56           C  
ANISOU 7133  CB  TRP C 282     5165   2418   3266   -165   1334     30       C  
ATOM   7134  CG  TRP C 282      -0.291  82.984  39.077  1.00 28.57           C  
ANISOU 7134  CG  TRP C 282     5108   2479   3268    -93   1262     95       C  
ATOM   7135  CD1 TRP C 282       0.857  83.712  38.925  1.00 28.87           C  
ANISOU 7135  CD1 TRP C 282     5115   2549   3303      3   1196    160       C  
ATOM   7136  CD2 TRP C 282      -1.013  83.595  40.160  1.00 31.43           C  
ANISOU 7136  CD2 TRP C 282     5428   2878   3633   -123   1250     93       C  
ATOM   7137  NE1 TRP C 282       0.920  84.703  39.867  1.00 29.29           N  
ANISOU 7137  NE1 TRP C 282     5117   2654   3358     32   1149    195       N  
ATOM   7138  CE2 TRP C 282      -0.204  84.646  40.652  1.00 31.06           C  
ANISOU 7138  CE2 TRP C 282     5338   2879   3584    -37   1179    159       C  
ATOM   7139  CE3 TRP C 282      -2.226  83.313  40.805  1.00 32.23           C  
ANISOU 7139  CE3 TRP C 282     5531   2975   3739   -215   1302     39       C  
ATOM   7140  CZ2 TRP C 282      -0.603  85.450  41.726  1.00 32.76           C  
ANISOU 7140  CZ2 TRP C 282     5511   3136   3797    -38   1152    174       C  
ATOM   7141  CZ3 TRP C 282      -2.614  84.109  41.864  1.00 31.41           C  
ANISOU 7141  CZ3 TRP C 282     5384   2916   3635   -211   1275     58       C  
ATOM   7142  CH2 TRP C 282      -1.813  85.160  42.313  1.00 30.91           C  
ANISOU 7142  CH2 TRP C 282     5281   2896   3566   -121   1199    126       C  
ATOM   7143  N   LEU C 283       0.062  82.666  35.407  1.00 24.35           N  
ANISOU 7143  N   LEU C 283     4529   1987   2733    -92   1215     -5       N  
ATOM   7144  CA  LEU C 283       0.804  83.490  34.490  1.00 24.96           C  
ANISOU 7144  CA  LEU C 283     4557   2117   2809    -16   1145     20       C  
ATOM   7145  C   LEU C 283      -0.125  84.025  33.391  1.00 24.94           C  
ANISOU 7145  C   LEU C 283     4477   2201   2798    -51   1102    -62       C  
ATOM   7146  O   LEU C 283       0.023  85.172  33.017  1.00 24.51           O  
ANISOU 7146  O   LEU C 283     4360   2215   2738      1   1036    -46       O  
ATOM   7147  CB  LEU C 283       1.989  82.724  33.897  1.00 27.92           C  
ANISOU 7147  CB  LEU C 283     5007   2423   3176     42   1176     64       C  
ATOM   7148  CG  LEU C 283       2.802  83.495  32.852  1.00 28.12           C  
ANISOU 7148  CG  LEU C 283     4987   2495   3198    114   1118     88       C  
ATOM   7149  CD1 LEU C 283       3.441  84.744  33.479  1.00 29.25           C  
ANISOU 7149  CD1 LEU C 283     5072   2690   3350    173   1062    150       C  
ATOM   7150  CD2 LEU C 283       3.852  82.609  32.213  1.00 29.00           C  
ANISOU 7150  CD2 LEU C 283     5174   2543   3302    166   1156    120       C  
ATOM   7151  N   ASN C 284      -1.067  83.219  32.878  1.00 25.85           N  
ANISOU 7151  N   ASN C 284     4599   2316   2907   -136   1141   -155       N  
ATOM   7152  CA  ASN C 284      -1.957  83.690  31.786  1.00 27.22           C  
ANISOU 7152  CA  ASN C 284     4690   2591   3059   -156   1093   -245       C  
ATOM   7153  C   ASN C 284      -2.795  84.912  32.235  1.00 28.30           C  
ANISOU 7153  C   ASN C 284     4729   2834   3189   -148   1032   -262       C  
ATOM   7154  O   ASN C 284      -3.005  85.853  31.468  1.00 26.68           O  
ANISOU 7154  O   ASN C 284     4462   2715   2958    -93    968   -279       O  
ATOM   7155  CB  ASN C 284      -2.917  82.591  31.333  1.00 29.84           C  
ANISOU 7155  CB  ASN C 284     5032   2920   3385   -265   1150   -360       C  
ATOM   7156  CG  ASN C 284      -3.631  82.937  30.042  1.00 35.07           C  
ANISOU 7156  CG  ASN C 284     5614   3695   4014   -267   1097   -455       C  
ATOM   7157  OD1 ASN C 284      -3.006  83.308  29.050  1.00 38.36           O  
ANISOU 7157  OD1 ASN C 284     6033   4130   4412   -186   1054   -430       O  
ATOM   7158  ND2 ASN C 284      -4.942  82.783  30.023  1.00 40.55           N  
ANISOU 7158  ND2 ASN C 284     6237   4472   4697   -356   1102   -571       N  
ATOM   7159  N   ASN C 285      -3.360  84.839  33.449  1.00 27.07           N  
ANISOU 7159  N   ASN C 285     4567   2668   3048   -203   1061   -264       N  
ATOM   7160  CA  ASN C 285      -4.152  85.941  34.032  1.00 28.22           C  
ANISOU 7160  CA  ASN C 285     4628   2905   3186   -194   1012   -276       C  
ATOM   7161  C   ASN C 285      -3.269  87.184  34.175  1.00 26.34           C  
ANISOU 7161  C   ASN C 285     4382   2677   2946    -89    953   -183       C  
ATOM   7162  O   ASN C 285      -3.697  88.275  33.805  1.00 25.21           O  
ANISOU 7162  O   ASN C 285     4177   2620   2779    -42    896   -198       O  
ATOM   7163  CB  ASN C 285      -4.817  85.559  35.361  1.00 28.23           C  
ANISOU 7163  CB  ASN C 285     4637   2882   3206   -272   1064   -289       C  
ATOM   7164  CG  ASN C 285      -6.017  84.666  35.153  1.00 32.81           C  
ANISOU 7164  CG  ASN C 285     5191   3490   3783   -391   1118   -409       C  
ATOM   7165  OD1 ASN C 285      -6.848  84.936  34.298  1.00 37.11           O  
ANISOU 7165  OD1 ASN C 285     5651   4144   4303   -407   1080   -501       O  
ATOM   7166  ND2 ASN C 285      -6.086  83.559  35.870  1.00 33.32           N  
ANISOU 7166  ND2 ASN C 285     5334   3457   3867   -474   1212   -416       N  
ATOM   7167  N   PHE C 286      -2.056  86.984  34.706  1.00 26.41           N  
ANISOU 7167  N   PHE C 286     4457   2601   2975    -52    973    -94       N  
ATOM   7168  CA  PHE C 286      -1.083  88.028  34.976  1.00 25.64           C  
ANISOU 7168  CA  PHE C 286     4356   2504   2881     27    932    -12       C  
ATOM   7169  C   PHE C 286      -0.730  88.731  33.668  1.00 25.31           C  
ANISOU 7169  C   PHE C 286     4294   2502   2821     90    891    -14       C  
ATOM   7170  O   PHE C 286      -0.713  89.975  33.586  1.00 25.18           O  
ANISOU 7170  O   PHE C 286     4244   2532   2791    139    849      5       O  
ATOM   7171  CB  PHE C 286       0.181  87.445  35.615  1.00 25.63           C  
ANISOU 7171  CB  PHE C 286     4421   2419   2897     55    964     63       C  
ATOM   7172  CG  PHE C 286       1.082  88.419  36.326  1.00 24.84           C  
ANISOU 7172  CG  PHE C 286     4306   2326   2803    113    932    134       C  
ATOM   7173  CD1 PHE C 286       0.940  89.790  36.195  1.00 25.86           C  
ANISOU 7173  CD1 PHE C 286     4383   2515   2926    141    884    137       C  
ATOM   7174  CD2 PHE C 286       2.099  87.946  37.126  1.00 24.95           C  
ANISOU 7174  CD2 PHE C 286     4363   2292   2824    143    954    193       C  
ATOM   7175  CE1 PHE C 286       1.764  90.650  36.894  1.00 25.10           C  
ANISOU 7175  CE1 PHE C 286     4276   2422   2836    177    864    190       C  
ATOM   7176  CE2 PHE C 286       2.938  88.816  37.794  1.00 25.76           C  
ANISOU 7176  CE2 PHE C 286     4441   2416   2929    188    924    244       C  
ATOM   7177  CZ  PHE C 286       2.748  90.166  37.704  1.00 24.03           C  
ANISOU 7177  CZ  PHE C 286     4169   2250   2710    195    881    238       C  
ATOM   7178  N   SER C 287      -0.497  87.918  32.640  1.00 23.85           N  
ANISOU 7178  N   SER C 287     4139   2292   2629     86    910    -41       N  
ATOM   7179  CA  SER C 287      -0.054  88.382  31.357  1.00 23.60           C  
ANISOU 7179  CA  SER C 287     4105   2284   2576    148    883    -38       C  
ATOM   7180  C   SER C 287      -1.159  89.168  30.635  1.00 25.61           C  
ANISOU 7180  C   SER C 287     4300   2638   2790    167    839   -103       C  
ATOM   7181  O   SER C 287      -0.882  90.245  30.061  1.00 25.46           O  
ANISOU 7181  O   SER C 287     4274   2650   2746    242    807    -76       O  
ATOM   7182  CB  SER C 287       0.428  87.224  30.524  1.00 24.74           C  
ANISOU 7182  CB  SER C 287     4301   2376   2721    138    919    -53       C  
ATOM   7183  OG  SER C 287       0.785  87.673  29.231  1.00 25.71           O  
ANISOU 7183  OG  SER C 287     4423   2525   2818    199    894    -55       O  
ATOM   7184  N   LYS C 288      -2.387  88.629  30.619  1.00 26.69           N  
ANISOU 7184  N   LYS C 288     4397   2828   2913    104    842   -192       N  
ATOM   7185  CA  LYS C 288      -3.573  89.316  30.010  1.00 28.63           C  
ANISOU 7185  CA  LYS C 288     4571   3196   3110    130    795   -268       C  
ATOM   7186  C   LYS C 288      -3.791  90.693  30.685  1.00 27.39           C  
ANISOU 7186  C   LYS C 288     4384   3080   2941    185    760   -225       C  
ATOM   7187  O   LYS C 288      -4.211  91.638  30.044  1.00 26.84           O  
ANISOU 7187  O   LYS C 288     4289   3087   2822    263    720   -240       O  
ATOM   7188  CB  LYS C 288      -4.859  88.515  30.224  1.00 32.03           C  
ANISOU 7188  CB  LYS C 288     4947   3686   3536     34    811   -376       C  
ATOM   7189  CG  LYS C 288      -5.120  87.370  29.260  1.00 39.42           C  
ANISOU 7189  CG  LYS C 288     5888   4628   4461    -21    836   -463       C  
ATOM   7190  CD  LYS C 288      -6.408  86.597  29.575  1.00 42.14           C  
ANISOU 7190  CD  LYS C 288     6173   5033   4805   -137    865   -583       C  
ATOM   7191  N   THR C 289      -3.502  90.781  31.991  1.00 26.94           N  
ANISOU 7191  N   THR C 289     4341   2970   2923    152    780   -173       N  
ATOM   7192  CA  THR C 289      -3.685  92.008  32.738  1.00 27.45           C  
ANISOU 7192  CA  THR C 289     4386   3063   2980    193    754   -135       C  
ATOM   7193  C   THR C 289      -2.593  93.030  32.401  1.00 26.72           C  
ANISOU 7193  C   THR C 289     4338   2931   2882    274    744    -57       C  
ATOM   7194  O   THR C 289      -2.898  94.191  32.186  1.00 24.27           O  
ANISOU 7194  O   THR C 289     4020   2665   2535    340    719    -50       O  
ATOM   7195  CB  THR C 289      -3.697  91.765  34.248  1.00 28.78           C  
ANISOU 7195  CB  THR C 289     4557   3189   3187    132    779   -107       C  
ATOM   7196  OG1 THR C 289      -4.821  90.956  34.576  1.00 30.09           O  
ANISOU 7196  OG1 THR C 289     4684   3394   3354     52    800   -185       O  
ATOM   7197  CG2 THR C 289      -3.787  93.052  35.042  1.00 27.19           C  
ANISOU 7197  CG2 THR C 289     4344   3010   2978    174    755    -66       C  
ATOM   7198  N   ILE C 290      -1.324  92.613  32.475  1.00 25.51           N  
ANISOU 7198  N   ILE C 290     4232   2694   2764    266    770      0       N  
ATOM   7199  CA  ILE C 290      -0.203  93.494  32.200  1.00 26.79           C  
ANISOU 7199  CA  ILE C 290     4430   2819   2929    322    773     64       C  
ATOM   7200  C   ILE C 290      -0.258  93.964  30.742  1.00 27.58           C  
ANISOU 7200  C   ILE C 290     4546   2947   2983    392    762     47       C  
ATOM   7201  O   ILE C 290       0.117  95.105  30.474  1.00 29.04           O  
ANISOU 7201  O   ILE C 290     4759   3126   3148    450    764     83       O  
ATOM   7202  CB  ILE C 290       1.148  92.850  32.560  1.00 30.44           C  
ANISOU 7202  CB  ILE C 290     4925   3207   3434    302    802    116       C  
ATOM   7203  CG1 ILE C 290       1.315  92.755  34.075  1.00 33.58           C  
ANISOU 7203  CG1 ILE C 290     5313   3583   3862    262    809    145       C  
ATOM   7204  CG2 ILE C 290       2.323  93.580  31.942  1.00 35.14           C  
ANISOU 7204  CG2 ILE C 290     5548   3774   4029    350    813    163       C  
ATOM   7205  CD1 ILE C 290       1.415  94.094  34.765  1.00 37.94           C  
ANISOU 7205  CD1 ILE C 290     5853   4150   4410    281    795    172       C  
ATOM   7206  N   ASN C 291      -0.756  93.138  29.824  1.00 26.30           N  
ANISOU 7206  N   ASN C 291     4375   2817   2800    388    756     -8       N  
ATOM   7207  CA  ASN C 291      -0.782  93.526  28.402  1.00 29.82           C  
ANISOU 7207  CA  ASN C 291     4840   3294   3193    465    744    -24       C  
ATOM   7208  C   ASN C 291      -1.855  94.581  28.095  1.00 28.33           C  
ANISOU 7208  C   ASN C 291     4630   3195   2939    538    710    -56       C  
ATOM   7209  O   ASN C 291      -1.880  95.081  27.005  1.00 27.98           O  
ANISOU 7209  O   ASN C 291     4613   3177   2840    622    702    -61       O  
ATOM   7210  CB  ASN C 291      -0.877  92.313  27.473  1.00 30.97           C  
ANISOU 7210  CB  ASN C 291     4986   3447   3332    443    749    -77       C  
ATOM   7211  CG  ASN C 291       0.471  91.629  27.363  1.00 31.23           C  
ANISOU 7211  CG  ASN C 291     5070   3387   3409    424    787    -24       C  
ATOM   7212  OD1 ASN C 291       1.504  92.290  27.417  1.00 35.22           O  
ANISOU 7212  OD1 ASN C 291     5606   3844   3928    458    804     42       O  
ATOM   7213  ND2 ASN C 291       0.475  90.310  27.341  1.00 29.64           N  
ANISOU 7213  ND2 ASN C 291     4874   3158   3229    364    808    -56       N  
ATOM   7214  N   LYS C 292      -2.708  94.925  29.061  1.00 26.95           N  
ANISOU 7214  N   LYS C 292     4410   3064   2763    516    693    -76       N  
ATOM   7215  CA  LYS C 292      -3.608  96.085  28.941  1.00 28.08           C  
ANISOU 7215  CA  LYS C 292     4540   3287   2842    602    665    -92       C  
ATOM   7216  C   LYS C 292      -2.917  97.363  29.451  1.00 25.45           C  
ANISOU 7216  C   LYS C 292     4267   2887   2513    643    689    -11       C  
ATOM   7217  O   LYS C 292      -3.454  98.441  29.339  1.00 26.55           O  
ANISOU 7217  O   LYS C 292     4424   3065   2596    727    680     -7       O  
ATOM   7218  CB  LYS C 292      -4.922  95.800  29.678  1.00 30.63           C  
ANISOU 7218  CB  LYS C 292     4780   3700   3158    558    639   -161       C  
ATOM   7219  CG  LYS C 292      -5.882  94.912  28.893  1.00 34.08           C  
ANISOU 7219  CG  LYS C 292     5150   4238   3559    542    613   -266       C  
ATOM   7220  CD  LYS C 292      -7.152  94.609  29.653  1.00 37.47           C  
ANISOU 7220  CD  LYS C 292     5489   4761   3986    483    598   -344       C  
ATOM   7221  CE  LYS C 292      -7.061  93.347  30.474  1.00 40.34           C  
ANISOU 7221  CE  LYS C 292     5837   5065   4423    340    636   -364       C  
ATOM   7222  NZ  LYS C 292      -8.372  92.977  31.066  1.00 43.43           N  
ANISOU 7222  NZ  LYS C 292     6138   5554   4809    272    632   -456       N  
ATOM   7223  N   VAL C 293      -1.730  97.222  30.035  1.00 24.67           N  
ANISOU 7223  N   VAL C 293     4200   2694   2479    586    722     46       N  
ATOM   7224  CA  VAL C 293      -0.941  98.316  30.479  1.00 23.78           C  
ANISOU 7224  CA  VAL C 293     4139   2517   2376    603    752    108       C  
ATOM   7225  C   VAL C 293      -0.028  98.739  29.332  1.00 24.94           C  
ANISOU 7225  C   VAL C 293     4356   2616   2504    658    787    142       C  
ATOM   7226  O   VAL C 293       0.795  97.940  28.915  1.00 25.39           O  
ANISOU 7226  O   VAL C 293     4416   2637   2594    626    801    151       O  
ATOM   7227  CB  VAL C 293      -0.103  97.982  31.719  1.00 23.12           C  
ANISOU 7227  CB  VAL C 293     4041   2375   2365    515    769    143       C  
ATOM   7228  CG1 VAL C 293       0.608  99.230  32.252  1.00 23.29           C  
ANISOU 7228  CG1 VAL C 293     4108   2347   2394    523    800    191       C  
ATOM   7229  CG2 VAL C 293      -0.958  97.338  32.809  1.00 24.06           C  
ANISOU 7229  CG2 VAL C 293     4102   2533   2505    456    744    111       C  
ATOM   7230  N   PRO C 294      -0.087 100.016  28.883  1.00 24.81           N  
ANISOU 7230  N   PRO C 294     4404   2587   2433    741    810    166       N  
ATOM   7231  CA  PRO C 294       0.820 100.529  27.864  1.00 23.81           C  
ANISOU 7231  CA  PRO C 294     4358   2401   2287    790    860    202       C  
ATOM   7232  C   PRO C 294       2.293 100.262  28.201  1.00 23.85           C  
ANISOU 7232  C   PRO C 294     4369   2327   2366    707    903    239       C  
ATOM   7233  O   PRO C 294       2.750 100.423  29.355  1.00 21.78           O  
ANISOU 7233  O   PRO C 294     4081   2038   2155    636    911    255       O  
ATOM   7234  CB  PRO C 294       0.574 102.038  27.875  1.00 25.50           C  
ANISOU 7234  CB  PRO C 294     4652   2591   2445    865    897    229       C  
ATOM   7235  CG  PRO C 294      -0.854 102.177  28.354  1.00 27.24           C  
ANISOU 7235  CG  PRO C 294     4826   2902   2622    907    843    190       C  
ATOM   7236  CD  PRO C 294      -1.020 101.058  29.367  1.00 26.80           C  
ANISOU 7236  CD  PRO C 294     4668   2876   2636    797    801    161       C  
ATOM   7237  N   ARG C 295       3.044  99.869  27.174  1.00 24.71           N  
ANISOU 7237  N   ARG C 295     4507   2407   2475    723    929    249       N  
ATOM   7238  CA  ARG C 295       4.456  99.584  27.325  1.00 24.58           C  
ANISOU 7238  CA  ARG C 295     4487   2332   2520    659    969    278       C  
ATOM   7239  C   ARG C 295       5.258 100.854  27.639  1.00 25.51           C  
ANISOU 7239  C   ARG C 295     4657   2388   2646    642   1035    310       C  
ATOM   7240  O   ARG C 295       6.374 100.771  28.136  1.00 30.55           O  
ANISOU 7240  O   ARG C 295     5270   2996   3339    572   1065    323       O  
ATOM   7241  CB  ARG C 295       4.960  98.917  26.044  1.00 25.29           C  
ANISOU 7241  CB  ARG C 295     4600   2411   2597    692    984    278       C  
ATOM   7242  CG  ARG C 295       4.696  97.420  25.995  1.00 24.28           C  
ANISOU 7242  CG  ARG C 295     4414   2320   2491    663    938    246       C  
ATOM   7243  CD  ARG C 295       5.152  96.843  24.656  1.00 25.33           C  
ANISOU 7243  CD  ARG C 295     4580   2441   2603    704    955    244       C  
ATOM   7244  NE  ARG C 295       5.084  95.389  24.627  1.00 23.88           N  
ANISOU 7244  NE  ARG C 295     4354   2273   2444    667    926    216       N  
ATOM   7245  CZ  ARG C 295       6.009  94.594  25.119  1.00 24.72           C  
ANISOU 7245  CZ  ARG C 295     4438   2348   2607    613    941    235       C  
ATOM   7246  NH1 ARG C 295       7.034  95.106  25.784  1.00 24.86           N  
ANISOU 7246  NH1 ARG C 295     4448   2333   2663    584    973    273       N  
ATOM   7247  NH2 ARG C 295       5.906  93.285  24.954  1.00 21.61           N  
ANISOU 7247  NH2 ARG C 295     4030   1957   2224    592    926    210       N  
ATOM   7248  N   ASP C 296       4.695 102.023  27.357  1.00 25.44           N  
ANISOU 7248  N   ASP C 296     4722   2363   2579    706   1063    319       N  
ATOM   7249  CA  ASP C 296       5.319 103.290  27.740  1.00 30.30           C  
ANISOU 7249  CA  ASP C 296     5401   2911   3200    681   1137    342       C  
ATOM   7250  C   ASP C 296       5.584 103.351  29.263  1.00 26.84           C  
ANISOU 7250  C   ASP C 296     4898   2479   2821    585   1120    334       C  
ATOM   7251  O   ASP C 296       6.388 104.155  29.703  1.00 27.59           O  
ANISOU 7251  O   ASP C 296     5018   2523   2939    530   1180    341       O  
ATOM   7252  CB  ASP C 296       4.476 104.478  27.265  1.00 31.05           C  
ANISOU 7252  CB  ASP C 296     5599   2986   3209    782   1169    353       C  
ATOM   7253  CG  ASP C 296       4.637 104.802  25.776  1.00 37.79           C  
ANISOU 7253  CG  ASP C 296     6552   3805   3999    876   1222    372       C  
ATOM   7254  OD1 ASP C 296       5.588 104.277  25.140  1.00 44.99           O  
ANISOU 7254  OD1 ASP C 296     7460   4691   4942    845   1251    378       O  
ATOM   7255  OD2 ASP C 296       3.847 105.614  25.267  1.00 42.24           O  
ANISOU 7255  OD2 ASP C 296     7205   4367   4477    988   1240    382       O  
ATOM   7256  N   SER C 297       4.913 102.518  30.067  1.00 25.18           N  
ANISOU 7256  N   SER C 297     4605   2329   2631    563   1045    315       N  
ATOM   7257  CA  SER C 297       5.107 102.555  31.532  1.00 25.05           C  
ANISOU 7257  CA  SER C 297     4533   2321   2661    485   1028    310       C  
ATOM   7258  C   SER C 297       6.374 101.798  31.934  1.00 24.71           C  
ANISOU 7258  C   SER C 297     4429   2278   2682    412   1031    311       C  
ATOM   7259  O   SER C 297       6.924 102.024  33.028  1.00 23.22           O  
ANISOU 7259  O   SER C 297     4202   2093   2527    349   1034    306       O  
ATOM   7260  CB  SER C 297       3.881 102.030  32.269  1.00 24.37           C  
ANISOU 7260  CB  SER C 297     4395   2296   2568    494    958    291       C  
ATOM   7261  OG  SER C 297       3.656 100.656  32.018  1.00 24.43           O  
ANISOU 7261  OG  SER C 297     4349   2342   2591    488    914    276       O  
ATOM   7262  N   ASP C 298       6.817 100.863  31.071  1.00 27.92           N  
ANISOU 7262  N   ASP C 298     4822   2689   3096    427   1028    314       N  
ATOM   7263  CA  ASP C 298       7.846  99.880  31.434  1.00 26.57           C  
ANISOU 7263  CA  ASP C 298     4587   2532   2974    381   1019    315       C  
ATOM   7264  C   ASP C 298       9.200 100.544  31.741  1.00 27.45           C  
ANISOU 7264  C   ASP C 298     4685   2627   3116    326   1073    315       C  
ATOM   7265  O   ASP C 298       9.979 100.022  32.555  1.00 26.67           O  
ANISOU 7265  O   ASP C 298     4518   2562   3053    285   1057    308       O  
ATOM   7266  CB  ASP C 298       8.026  98.839  30.321  1.00 30.62           C  
ANISOU 7266  CB  ASP C 298     5105   3046   3482    418   1015    319       C  
ATOM   7267  CG  ASP C 298       6.834  97.899  30.151  1.00 32.88           C  
ANISOU 7267  CG  ASP C 298     5382   3363   3748    448    961    302       C  
ATOM   7268  OD1 ASP C 298       5.851  97.988  30.976  1.00 33.12           O  
ANISOU 7268  OD1 ASP C 298     5393   3419   3771    437    925    289       O  
ATOM   7269  OD2 ASP C 298       6.853  97.109  29.177  1.00 28.77           O  
ANISOU 7269  OD2 ASP C 298     4874   2841   3216    477    959    297       O  
ATOM   7270  N   LYS C 299       9.479 101.698  31.116  1.00 26.97           N  
ANISOU 7270  N   LYS C 299     4691   2518   3037    326   1142    316       N  
ATOM   7271  CA  LYS C 299      10.765 102.368  31.290  1.00 30.58           C  
ANISOU 7271  CA  LYS C 299     5136   2959   3524    259   1209    302       C  
ATOM   7272  C   LYS C 299      10.878 102.955  32.696  1.00 28.43           C  
ANISOU 7272  C   LYS C 299     4822   2707   3271    193   1200    279       C  
ATOM   7273  O   LYS C 299      11.975 103.276  33.136  1.00 31.70           O  
ANISOU 7273  O   LYS C 299     5191   3138   3715    124   1236    252       O  
ATOM   7274  CB  LYS C 299      11.012 103.456  30.232  1.00 32.84           C  
ANISOU 7274  CB  LYS C 299     5522   3172   3782    270   1303    308       C  
ATOM   7275  CG  LYS C 299      10.073 104.655  30.289  1.00 34.86           C  
ANISOU 7275  CG  LYS C 299     5874   3377   3991    300   1333    316       C  
ATOM   7276  CD  LYS C 299      10.402 105.739  29.276  1.00 36.49           C  
ANISOU 7276  CD  LYS C 299     6201   3498   4163    316   1444    326       C  
ATOM   7277  CE  LYS C 299       9.350 106.817  29.193  1.00 36.63           C  
ANISOU 7277  CE  LYS C 299     6335   3465   4118    380   1472    342       C  
ATOM   7278  NZ  LYS C 299       8.094 106.346  28.552  1.00 39.83           N  
ANISOU 7278  NZ  LYS C 299     6764   3902   4464    502   1405    364       N  
ATOM   7279  N   TYR C 300       9.759 103.036  33.418  1.00 28.47           N  
ANISOU 7279  N   TYR C 300     4834   2722   3258    214   1149    284       N  
ATOM   7280  CA  TYR C 300       9.761 103.518  34.782  1.00 28.70           C  
ANISOU 7280  CA  TYR C 300     4828   2774   3301    160   1134    263       C  
ATOM   7281  C   TYR C 300       9.895 102.380  35.795  1.00 30.25           C  
ANISOU 7281  C   TYR C 300     4929   3039   3522    150   1060    260       C  
ATOM   7282  O   TYR C 300      10.006 102.646  36.953  1.00 31.43           O  
ANISOU 7282  O   TYR C 300     5041   3218   3681    111   1042    242       O  
ATOM   7283  CB  TYR C 300       8.480 104.302  35.069  1.00 31.11           C  
ANISOU 7283  CB  TYR C 300     5198   3052   3569    193   1126    271       C  
ATOM   7284  CG  TYR C 300       8.368 105.545  34.228  1.00 30.55           C  
ANISOU 7284  CG  TYR C 300     5238   2906   3462    214   1209    277       C  
ATOM   7285  CD1 TYR C 300       9.133 106.663  34.496  1.00 33.97           C  
ANISOU 7285  CD1 TYR C 300     5709   3292   3904    145   1289    254       C  
ATOM   7286  CD2 TYR C 300       7.523 105.576  33.132  1.00 32.41           C  
ANISOU 7286  CD2 TYR C 300     5545   3118   3648    306   1212    302       C  
ATOM   7287  CE1 TYR C 300       9.036 107.802  33.714  1.00 35.68           C  
ANISOU 7287  CE1 TYR C 300     6050   3423   4081    167   1381    264       C  
ATOM   7288  CE2 TYR C 300       7.425 106.695  32.325  1.00 34.04           C  
ANISOU 7288  CE2 TYR C 300     5871   3252   3809    346   1293    314       C  
ATOM   7289  CZ  TYR C 300       8.178 107.813  32.625  1.00 37.53           C  
ANISOU 7289  CZ  TYR C 300     6366   3630   4260    277   1384    299       C  
ATOM   7290  OH  TYR C 300       8.025 108.914  31.842  1.00 35.72           O  
ANISOU 7290  OH  TYR C 300     6276   3315   3979    322   1477    315       O  
ATOM   7291  N   VAL C 301       9.856 101.123  35.351  1.00 28.49           N  
ANISOU 7291  N   VAL C 301     4681   2839   3305    191   1024    278       N  
ATOM   7292  CA  VAL C 301      10.101  99.982  36.246  1.00 27.69           C  
ANISOU 7292  CA  VAL C 301     4510   2791   3219    192    970    280       C  
ATOM   7293  C   VAL C 301      11.617  99.894  36.477  1.00 27.95           C  
ANISOU 7293  C   VAL C 301     4477   2866   3274    160    990    261       C  
ATOM   7294  O   VAL C 301      12.399 100.075  35.524  1.00 28.97           O  
ANISOU 7294  O   VAL C 301     4612   2981   3412    153   1038    255       O  
ATOM   7295  CB  VAL C 301       9.538  98.697  35.611  1.00 29.41           C  
ANISOU 7295  CB  VAL C 301     4740   3003   3429    244    941    301       C  
ATOM   7296  CG1 VAL C 301       9.770  97.464  36.468  1.00 30.53           C  
ANISOU 7296  CG1 VAL C 301     4836   3182   3580    255    902    309       C  
ATOM   7297  CG2 VAL C 301       8.065  98.843  35.257  1.00 30.17           C  
ANISOU 7297  CG2 VAL C 301     4885   3077   3499    272    924    303       C  
ATOM   7298  N   THR C 302      12.024  99.626  37.723  1.00 29.15           N  
ANISOU 7298  N   THR C 302     4565   3077   3431    145    956    247       N  
ATOM   7299  CA  THR C 302      13.445  99.390  38.114  1.00 32.53           C  
ANISOU 7299  CA  THR C 302     4909   3578   3871    129    959    220       C  
ATOM   7300  C   THR C 302      14.065  98.351  37.163  1.00 32.39           C  
ANISOU 7300  C   THR C 302     4881   3567   3856    179    967    240       C  
ATOM   7301  O   THR C 302      13.470  97.298  36.917  1.00 30.32           O  
ANISOU 7301  O   THR C 302     4652   3281   3584    234    940    275       O  
ATOM   7302  CB  THR C 302      13.534  98.880  39.562  1.00 35.29           C  
ANISOU 7302  CB  THR C 302     5203   3998   4208    145    903    215       C  
ATOM   7303  OG1 THR C 302      12.774  99.757  40.394  1.00 42.96           O  
ANISOU 7303  OG1 THR C 302     6195   4953   5174    107    894    202       O  
ATOM   7304  CG2 THR C 302      14.943  98.817  40.111  1.00 37.10           C  
ANISOU 7304  CG2 THR C 302     5334   4326   4437    136    900    175       C  
ATOM   7305  N   GLN C 303      15.271  98.623  36.670  1.00 33.50           N  
ANISOU 7305  N   GLN C 303     4976   3741   4010    154   1009    213       N  
ATOM   7306  CA  GLN C 303      15.812  97.892  35.494  1.00 38.54           C  
ANISOU 7306  CA  GLN C 303     5622   4369   4652    196   1033    231       C  
ATOM   7307  C   GLN C 303      16.085  96.403  35.788  1.00 33.99           C  
ANISOU 7307  C   GLN C 303     5017   3836   4061    275    988    257       C  
ATOM   7308  O   GLN C 303      15.977  95.593  34.866  1.00 29.82           O  
ANISOU 7308  O   GLN C 303     4531   3270   3529    322    996    286       O  
ATOM   7309  CB  GLN C 303      17.081  98.559  34.959  1.00 45.40           C  
ANISOU 7309  CB  GLN C 303     6441   5269   5537    146   1096    190       C  
ATOM   7310  CG  GLN C 303      16.881  99.998  34.479  1.00 57.14           C  
ANISOU 7310  CG  GLN C 303     7984   6689   7034     70   1166    168       C  
ATOM   7311  CD  GLN C 303      15.446 100.430  34.243  1.00 65.65           C  
ANISOU 7311  CD  GLN C 303     9169   7678   8097     87   1160    202       C  
ATOM   7312  OE1 GLN C 303      14.765  99.961  33.320  1.00 61.15           O  
ANISOU 7312  OE1 GLN C 303     8665   7056   7513    143   1155    240       O  
ATOM   7313  NE2 GLN C 303      14.981 101.365  35.071  1.00 66.49           N  
ANISOU 7313  NE2 GLN C 303     9289   7774   8201     39   1161    182       N  
ATOM   7314  N   ILE C 304      16.409  96.033  37.033  1.00 33.61           N  
ANISOU 7314  N   ILE C 304     4910   3862   3999    295    945    248       N  
ATOM   7315  CA  ILE C 304      16.657  94.619  37.375  1.00 34.45           C  
ANISOU 7315  CA  ILE C 304     5008   4000   4079    385    912    278       C  
ATOM   7316  C   ILE C 304      15.469  93.722  36.968  1.00 32.30           C  
ANISOU 7316  C   ILE C 304     4835   3637   3801    422    904    325       C  
ATOM   7317  O   ILE C 304      15.657  92.500  36.798  1.00 30.03           O  
ANISOU 7317  O   ILE C 304     4572   3342   3494    493    901    353       O  
ATOM   7318  CB  ILE C 304      17.002  94.381  38.865  1.00 37.61           C  
ANISOU 7318  CB  ILE C 304     5349   4487   4450    418    866    267       C  
ATOM   7319  CG1 ILE C 304      15.914  94.854  39.824  1.00 36.30           C  
ANISOU 7319  CG1 ILE C 304     5217   4290   4282    383    839    270       C  
ATOM   7320  CG2 ILE C 304      18.354  94.952  39.255  1.00 40.54           C  
ANISOU 7320  CG2 ILE C 304     5603   4980   4818    398    869    209       C  
ATOM   7321  CD1 ILE C 304      16.098  94.310  41.234  1.00 42.24           C  
ANISOU 7321  CD1 ILE C 304     5938   5113   4995    440    794    274       C  
ATOM   7322  N   PHE C 305      14.256  94.286  36.869  1.00 26.60           N  
ANISOU 7322  N   PHE C 305     4168   2850   3088    377    902    328       N  
ATOM   7323  CA  PHE C 305      13.042  93.515  36.570  1.00 25.90           C  
ANISOU 7323  CA  PHE C 305     4156   2692   2992    397    893    354       C  
ATOM   7324  C   PHE C 305      12.733  93.503  35.071  1.00 24.73           C  
ANISOU 7324  C   PHE C 305     4056   2488   2850    395    922    357       C  
ATOM   7325  O   PHE C 305      11.661  93.042  34.694  1.00 25.89           O  
ANISOU 7325  O   PHE C 305     4258   2588   2991    399    916    363       O  
ATOM   7326  CB  PHE C 305      11.835  94.092  37.328  1.00 27.14           C  
ANISOU 7326  CB  PHE C 305     4334   2829   3148    357    871    349       C  
ATOM   7327  CG  PHE C 305      11.913  93.900  38.821  1.00 27.65           C  
ANISOU 7327  CG  PHE C 305     4369   2937   3197    368    841    351       C  
ATOM   7328  CD1 PHE C 305      12.042  92.627  39.368  1.00 30.22           C  
ANISOU 7328  CD1 PHE C 305     4713   3266   3501    427    833    377       C  
ATOM   7329  CD2 PHE C 305      11.907  94.981  39.682  1.00 30.93           C  
ANISOU 7329  CD2 PHE C 305     4747   3387   3616    326    827    328       C  
ATOM   7330  CE1 PHE C 305      12.156  92.443  40.738  1.00 33.11           C  
ANISOU 7330  CE1 PHE C 305     5061   3674   3843    451    809    383       C  
ATOM   7331  CE2 PHE C 305      12.019  94.798  41.055  1.00 33.08           C  
ANISOU 7331  CE2 PHE C 305     4992   3706   3868    343    798    329       C  
ATOM   7332  CZ  PHE C 305      12.132  93.530  41.583  1.00 34.25           C  
ANISOU 7332  CZ  PHE C 305     5161   3862   3990    410    787    358       C  
ATOM   7333  N   ASN C 306      13.630  94.047  34.238  1.00 25.49           N  
ANISOU 7333  N   ASN C 306     4131   2596   2958    388    956    346       N  
ATOM   7334  CA  ASN C 306      13.356  94.220  32.809  1.00 27.29           C  
ANISOU 7334  CA  ASN C 306     4409   2773   3185    391    987    348       C  
ATOM   7335  C   ASN C 306      12.993  92.855  32.190  1.00 24.14           C  
ANISOU 7335  C   ASN C 306     4057   2341   2774    440    980    366       C  
ATOM   7336  O   ASN C 306      12.015  92.757  31.451  1.00 25.26           O  
ANISOU 7336  O   ASN C 306     4251   2440   2904    440    979    363       O  
ATOM   7337  CB  ASN C 306      14.513  94.904  32.066  1.00 27.09           C  
ANISOU 7337  CB  ASN C 306     4357   2762   3171    376   1036    336       C  
ATOM   7338  CG  ASN C 306      15.763  94.059  31.872  1.00 30.73           C  
ANISOU 7338  CG  ASN C 306     4772   3268   3635    416   1048    340       C  
ATOM   7339  OD1 ASN C 306      16.172  93.274  32.749  1.00 31.20           O  
ANISOU 7339  OD1 ASN C 306     4791   3377   3686    451   1019    346       O  
ATOM   7340  ND2 ASN C 306      16.378  94.208  30.705  1.00 32.64           N  
ANISOU 7340  ND2 ASN C 306     5026   3495   3881    422   1096    338       N  
ATOM   7341  N   LEU C 307      13.752  91.809  32.527  1.00 23.78           N  
ANISOU 7341  N   LEU C 307     3994   2318   2723    483    978    381       N  
ATOM   7342  CA  LEU C 307      13.536  90.449  31.921  1.00 23.22           C  
ANISOU 7342  CA  LEU C 307     3980   2204   2636    530    987    397       C  
ATOM   7343  C   LEU C 307      12.215  89.853  32.441  1.00 23.43           C  
ANISOU 7343  C   LEU C 307     4056   2191   2655    513    967    395       C  
ATOM   7344  O   LEU C 307      11.344  89.368  31.666  1.00 20.87           O  
ANISOU 7344  O   LEU C 307     3784   1820   2323    504    973    382       O  
ATOM   7345  CB  LEU C 307      14.739  89.562  32.253  1.00 25.08           C  
ANISOU 7345  CB  LEU C 307     4191   2476   2860    594    996    416       C  
ATOM   7346  CG  LEU C 307      14.640  88.110  31.765  1.00 26.02           C  
ANISOU 7346  CG  LEU C 307     4382   2543   2958    648   1015    435       C  
ATOM   7347  CD1 LEU C 307      14.392  88.078  30.258  1.00 25.13           C  
ANISOU 7347  CD1 LEU C 307     4312   2384   2850    640   1039    425       C  
ATOM   7348  CD2 LEU C 307      15.884  87.324  32.160  1.00 26.88           C  
ANISOU 7348  CD2 LEU C 307     4469   2696   3045    731   1026    458       C  
ATOM   7349  N   LYS C 308      12.036  89.890  33.770  1.00 22.80           N  
ANISOU 7349  N   LYS C 308     3955   2133   2572    504    945    400       N  
ATOM   7350  CA  LYS C 308      10.829  89.281  34.357  1.00 22.61           C  
ANISOU 7350  CA  LYS C 308     3978   2071   2540    484    937    397       C  
ATOM   7351  C   LYS C 308       9.560  89.899  33.768  1.00 23.12           C  
ANISOU 7351  C   LYS C 308     4056   2118   2611    432    927    366       C  
ATOM   7352  O   LYS C 308       8.617  89.181  33.474  1.00 23.57           O  
ANISOU 7352  O   LYS C 308     4155   2140   2661    414    934    347       O  
ATOM   7353  CB  LYS C 308      10.793  89.460  35.866  1.00 23.80           C  
ANISOU 7353  CB  LYS C 308     4104   2253   2686    481    916    407       C  
ATOM   7354  CG  LYS C 308       9.634  88.728  36.526  1.00 25.02           C  
ANISOU 7354  CG  LYS C 308     4312   2364   2831    460    922    405       C  
ATOM   7355  CD  LYS C 308       9.936  88.419  37.975  1.00 26.35           C  
ANISOU 7355  CD  LYS C 308     4479   2552   2980    492    916    429       C  
ATOM   7356  CE  LYS C 308       8.811  87.701  38.687  1.00 26.99           C  
ANISOU 7356  CE  LYS C 308     4622   2581   3050    466    936    429       C  
ATOM   7357  NZ  LYS C 308       9.230  87.307  40.056  1.00 27.94           N  
ANISOU 7357  NZ  LYS C 308     4757   2717   3140    517    937    461       N  
ATOM   7358  N   LEU C 309       9.536  91.243  33.654  1.00 23.57           N  
ANISOU 7358  N   LEU C 309     4075   2202   2675    410    914    356       N  
ATOM   7359  CA  LEU C 309       8.395  91.955  33.126  1.00 22.29           C  
ANISOU 7359  CA  LEU C 309     3926   2035   2506    384    903    330       C  
ATOM   7360  C   LEU C 309       8.106  91.553  31.679  1.00 22.52           C  
ANISOU 7360  C   LEU C 309     3992   2043   2522    402    916    314       C  
ATOM   7361  O   LEU C 309       6.953  91.269  31.333  1.00 22.10           O  
ANISOU 7361  O   LEU C 309     3957   1986   2453    388    905    282       O  
ATOM   7362  CB  LEU C 309       8.642  93.459  33.187  1.00 23.40           C  
ANISOU 7362  CB  LEU C 309     4042   2197   2651    371    903    330       C  
ATOM   7363  CG  LEU C 309       7.472  94.323  32.706  1.00 24.92           C  
ANISOU 7363  CG  LEU C 309     4254   2388   2823    366    893    308       C  
ATOM   7364  CD1 LEU C 309       6.158  93.959  33.395  1.00 24.52           C  
ANISOU 7364  CD1 LEU C 309     4201   2349   2764    345    865    288       C  
ATOM   7365  CD2 LEU C 309       7.801  95.801  32.896  1.00 26.06           C  
ANISOU 7365  CD2 LEU C 309     4394   2537   2968    355    908    313       C  
ATOM   7366  N   GLU C 310       9.149  91.531  30.835  1.00 23.39           N  
ANISOU 7366  N   GLU C 310     4107   2145   2634    433    941    329       N  
ATOM   7367  CA  GLU C 310       8.974  91.170  29.425  1.00 22.96           C  
ANISOU 7367  CA  GLU C 310     4092   2070   2562    457    954    314       C  
ATOM   7368  C   GLU C 310       8.492  89.717  29.337  1.00 22.40           C  
ANISOU 7368  C   GLU C 310     4054   1972   2484    454    957    298       C  
ATOM   7369  O   GLU C 310       7.611  89.385  28.530  1.00 21.04           O  
ANISOU 7369  O   GLU C 310     3906   1795   2292    448    953    260       O  
ATOM   7370  CB  GLU C 310      10.264  91.438  28.639  1.00 25.41           C  
ANISOU 7370  CB  GLU C 310     4400   2376   2876    489    988    336       C  
ATOM   7371  CG  GLU C 310      10.078  91.358  27.128  1.00 26.05           C  
ANISOU 7371  CG  GLU C 310     4525   2438   2932    520   1004    323       C  
ATOM   7372  CD  GLU C 310       8.974  92.257  26.595  1.00 27.79           C  
ANISOU 7372  CD  GLU C 310     4766   2669   3122    525    988    299       C  
ATOM   7373  OE1 GLU C 310       8.917  93.460  26.978  1.00 28.83           O  
ANISOU 7373  OE1 GLU C 310     4888   2811   3255    515    990    307       O  
ATOM   7374  OE2 GLU C 310       8.143  91.751  25.817  1.00 29.60           O  
ANISOU 7374  OE2 GLU C 310     5021   2902   3323    541    973    267       O  
ATOM   7375  N   ALA C 311       9.030  88.867  30.207  1.00 21.40           N  
ANISOU 7375  N   ALA C 311     3930   1830   2368    458    968    320       N  
ATOM   7376  CA  ALA C 311       8.640  87.424  30.215  1.00 22.41           C  
ANISOU 7376  CA  ALA C 311     4112   1914   2488    452    990    308       C  
ATOM   7377  C   ALA C 311       7.137  87.274  30.550  1.00 22.80           C  
ANISOU 7377  C   ALA C 311     4167   1961   2532    393    978    262       C  
ATOM   7378  O   ALA C 311       6.442  86.410  29.999  1.00 23.97           O  
ANISOU 7378  O   ALA C 311     4353   2083   2669    367    996    222       O  
ATOM   7379  CB  ALA C 311       9.525  86.638  31.165  1.00 22.45           C  
ANISOU 7379  CB  ALA C 311     4132   1902   2494    487   1010    348       C  
ATOM   7380  N   ILE C 312       6.620  88.127  31.446  1.00 22.77           N  
ANISOU 7380  N   ILE C 312     4123   1991   2536    368    951    262       N  
ATOM   7381  CA  ILE C 312       5.214  88.107  31.775  1.00 22.32           C  
ANISOU 7381  CA  ILE C 312     4058   1948   2473    314    939    216       C  
ATOM   7382  C   ILE C 312       4.386  88.608  30.595  1.00 23.06           C  
ANISOU 7382  C   ILE C 312     4136   2080   2546    312    918    166       C  
ATOM   7383  O   ILE C 312       3.373  87.982  30.256  1.00 22.39           O  
ANISOU 7383  O   ILE C 312     4056   2002   2446    273    922    107       O  
ATOM   7384  CB  ILE C 312       4.907  88.877  33.068  1.00 22.71           C  
ANISOU 7384  CB  ILE C 312     4070   2024   2531    296    918    231       C  
ATOM   7385  CG1 ILE C 312       5.584  88.228  34.275  1.00 25.40           C  
ANISOU 7385  CG1 ILE C 312     4432   2335   2881    305    938    273       C  
ATOM   7386  CG2 ILE C 312       3.405  88.960  33.234  1.00 23.79           C  
ANISOU 7386  CG2 ILE C 312     4190   2189   2660    245    905    176       C  
ATOM   7387  CD1 ILE C 312       5.799  89.169  35.437  1.00 27.88           C  
ANISOU 7387  CD1 ILE C 312     4705   2683   3202    309    912    299       C  
ATOM   7388  N   ARG C 313       4.814  89.714  29.964  1.00 22.90           N  
ANISOU 7388  N   ARG C 313     4099   2085   2515    356    900    184       N  
ATOM   7389  CA  ARG C 313       4.088  90.235  28.815  1.00 23.87           C  
ANISOU 7389  CA  ARG C 313     4217   2247   2604    378    881    143       C  
ATOM   7390  C   ARG C 313       3.999  89.158  27.723  1.00 25.42           C  
ANISOU 7390  C   ARG C 313     4446   2428   2784    379    897    105       C  
ATOM   7391  O   ARG C 313       2.986  89.042  27.048  1.00 26.20           O  
ANISOU 7391  O   ARG C 313     4533   2569   2851    372    879     42       O  
ATOM   7392  CB  ARG C 313       4.770  91.489  28.259  1.00 23.51           C  
ANISOU 7392  CB  ARG C 313     4177   2208   2547    433    881    179       C  
ATOM   7393  CG  ARG C 313       4.587  92.738  29.097  1.00 25.34           C  
ANISOU 7393  CG  ARG C 313     4385   2459   2781    431    868    198       C  
ATOM   7394  CD  ARG C 313       4.895  94.020  28.338  1.00 25.04           C  
ANISOU 7394  CD  ARG C 313     4371   2424   2717    483    879    216       C  
ATOM   7395  NE  ARG C 313       4.623  95.212  29.138  1.00 25.11           N  
ANISOU 7395  NE  ARG C 313     4372   2445   2724    479    874    229       N  
ATOM   7396  CZ  ARG C 313       3.447  95.849  29.192  1.00 26.22           C  
ANISOU 7396  CZ  ARG C 313     4508   2625   2827    502    849    203       C  
ATOM   7397  NH1 ARG C 313       3.342  96.991  29.866  1.00 23.82           N  
ANISOU 7397  NH1 ARG C 313     4210   2319   2518    505    854    221       N  
ATOM   7398  NH2 ARG C 313       2.403  95.360  28.538  1.00 24.91           N  
ANISOU 7398  NH2 ARG C 313     4332   2507   2625    524    822    155       N  
ATOM   7399  N   GLN C 314       5.078  88.390  27.549  1.00 25.60           N  
ANISOU 7399  N   GLN C 314     4505   2397   2824    393    929    139       N  
ATOM   7400  CA  GLN C 314       5.165  87.364  26.501  1.00 27.01           C  
ANISOU 7400  CA  GLN C 314     4725   2549   2987    399    952    110       C  
ATOM   7401  C   GLN C 314       4.463  86.074  26.952  1.00 26.75           C  
ANISOU 7401  C   GLN C 314     4717   2486   2960    333    976     64       C  
ATOM   7402  O   GLN C 314       4.401  85.118  26.197  1.00 27.40           O  
ANISOU 7402  O   GLN C 314     4840   2539   3029    321   1002     28       O  
ATOM   7403  CB  GLN C 314       6.623  87.039  26.138  1.00 27.52           C  
ANISOU 7403  CB  GLN C 314     4824   2569   3064    446    983    165       C  
ATOM   7404  CG  GLN C 314       7.435  88.205  25.587  1.00 31.10           C  
ANISOU 7404  CG  GLN C 314     5261   3041   3513    499    979    204       C  
ATOM   7405  CD  GLN C 314       6.936  88.711  24.259  1.00 34.38           C  
ANISOU 7405  CD  GLN C 314     5689   3484   3888    533    967    171       C  
ATOM   7406  OE1 GLN C 314       6.405  87.937  23.469  1.00 32.63           O  
ANISOU 7406  OE1 GLN C 314     5492   3264   3642    530    966    124       O  
ATOM   7407  NE2 GLN C 314       7.132  90.005  23.994  1.00 32.50           N  
ANISOU 7407  NE2 GLN C 314     5443   3268   3638    568    963    194       N  
ATOM   7408  N   ASN C 315       4.011  86.000  28.204  1.00 25.65           N  
ANISOU 7408  N   ASN C 315     4563   2343   2840    287    979     67       N  
ATOM   7409  CA  ASN C 315       3.283  84.818  28.698  1.00 24.95           C  
ANISOU 7409  CA  ASN C 315     4508   2215   2756    215   1019     22       C  
ATOM   7410  C   ASN C 315       4.173  83.564  28.572  1.00 27.74           C  
ANISOU 7410  C   ASN C 315     4946   2481   3113    230   1077     50       C  
ATOM   7411  O   ASN C 315       3.711  82.522  28.123  1.00 26.32           O  
ANISOU 7411  O   ASN C 315     4814   2262   2922    183   1118     -4       O  
ATOM   7412  CB  ASN C 315       1.954  84.655  27.939  1.00 25.27           C  
ANISOU 7412  CB  ASN C 315     4518   2310   2771    160   1006    -79       C  
ATOM   7413  CG  ASN C 315       0.920  83.814  28.658  1.00 27.59           C  
ANISOU 7413  CG  ASN C 315     4819   2589   3073     62   1044   -142       C  
ATOM   7414  OD1 ASN C 315       1.052  83.518  29.841  1.00 25.54           O  
ANISOU 7414  OD1 ASN C 315     4587   2279   2835     38   1076   -104       O  
ATOM   7415  ND2 ASN C 315      -0.102  83.394  27.932  1.00 30.99           N  
ANISOU 7415  ND2 ASN C 315     5227   3064   3483      2   1047   -245       N  
ATOM   7416  N   ASP C 316       5.431  83.658  29.033  1.00 28.40           N  
ANISOU 7416  N   ASP C 316     5045   2536   3207    295   1084    131       N  
ATOM   7417  CA  ASP C 316       6.469  82.628  28.811  1.00 29.27           C  
ANISOU 7417  CA  ASP C 316     5230   2578   3311    343   1133    169       C  
ATOM   7418  C   ASP C 316       7.024  82.145  30.159  1.00 28.12           C  
ANISOU 7418  C   ASP C 316     5123   2392   3170    369   1163    226       C  
ATOM   7419  O   ASP C 316       7.922  82.801  30.751  1.00 25.80           O  
ANISOU 7419  O   ASP C 316     4787   2133   2881    427   1136    284       O  
ATOM   7420  CB  ASP C 316       7.580  83.192  27.933  1.00 29.35           C  
ANISOU 7420  CB  ASP C 316     5218   2615   3318    418   1113    207       C  
ATOM   7421  CG  ASP C 316       8.597  82.172  27.444  1.00 35.14           C  
ANISOU 7421  CG  ASP C 316     6020   3290   4038    475   1160    236       C  
ATOM   7422  OD1 ASP C 316       9.097  81.369  28.260  1.00 32.06           O  
ANISOU 7422  OD1 ASP C 316     5683   2852   3644    504   1199    274       O  
ATOM   7423  OD2 ASP C 316       8.907  82.217  26.249  1.00 40.25           O  
ANISOU 7423  OD2 ASP C 316     6674   3944   4676    501   1159    224       O  
ATOM   7424  N   LEU C 317       6.541  80.980  30.603  1.00 26.88           N  
ANISOU 7424  N   LEU C 317     5049   2160   3004    330   1225    208       N  
ATOM   7425  CA  LEU C 317       6.798  80.492  31.954  1.00 26.99           C  
ANISOU 7425  CA  LEU C 317     5113   2130   3009    354   1261    256       C  
ATOM   7426  C   LEU C 317       8.295  80.208  32.133  1.00 27.07           C  
ANISOU 7426  C   LEU C 317     5152   2130   3001    472   1271    332       C  
ATOM   7427  O   LEU C 317       8.863  80.476  33.189  1.00 26.17           O  
ANISOU 7427  O   LEU C 317     5021   2043   2879    527   1256    384       O  
ATOM   7428  CB  LEU C 317       5.963  79.229  32.202  1.00 29.38           C  
ANISOU 7428  CB  LEU C 317     5521   2338   3301    284   1346    215       C  
ATOM   7429  CG  LEU C 317       6.177  78.537  33.548  1.00 31.08           C  
ANISOU 7429  CG  LEU C 317     5823   2486   3497    316   1405    266       C  
ATOM   7430  CD1 LEU C 317       5.875  79.467  34.709  1.00 31.15           C  
ANISOU 7430  CD1 LEU C 317     5759   2558   3519    308   1357    287       C  
ATOM   7431  CD2 LEU C 317       5.317  77.286  33.656  1.00 32.20           C  
ANISOU 7431  CD2 LEU C 317     6086   2520   3629    233   1508    218       C  
ATOM   7432  N   LEU C 318       8.922  79.641  31.093  1.00 26.84           N  
ANISOU 7432  N   LEU C 318     5166   2072   2959    514   1295    334       N  
ATOM   7433  CA  LEU C 318      10.325  79.253  31.189  1.00 27.08           C  
ANISOU 7433  CA  LEU C 318     5223   2098   2965    633   1310    400       C  
ATOM   7434  C   LEU C 318      11.156  80.519  31.432  1.00 25.26           C  
ANISOU 7434  C   LEU C 318     4872   1976   2750    679   1239    432       C  
ATOM   7435  O   LEU C 318      12.102  80.513  32.241  1.00 25.09           O  
ANISOU 7435  O   LEU C 318     4835   1988   2709    763   1234    482       O  
ATOM   7436  CB  LEU C 318      10.742  78.535  29.902  1.00 26.18           C  
ANISOU 7436  CB  LEU C 318     5168   1940   2838    661   1346    388       C  
ATOM   7437  CG  LEU C 318      10.291  77.082  29.798  1.00 26.75           C  
ANISOU 7437  CG  LEU C 318     5385   1892   2885    639   1437    367       C  
ATOM   7438  CD1 LEU C 318      10.475  76.562  28.393  1.00 27.23           C  
ANISOU 7438  CD1 LEU C 318     5489   1919   2938    642   1462    336       C  
ATOM   7439  CD2 LEU C 318      11.027  76.205  30.792  1.00 28.97           C  
ANISOU 7439  CD2 LEU C 318     5763   2118   3126    740   1494    434       C  
ATOM   7440  N   ALA C 319      10.775  81.596  30.740  1.00 25.78           N  
ANISOU 7440  N   ALA C 319     4855   2095   2843    624   1190    398       N  
ATOM   7441  CA  ALA C 319      11.501  82.871  30.832  1.00 25.13           C  
ANISOU 7441  CA  ALA C 319     4668   2102   2778    649   1138    417       C  
ATOM   7442  C   ALA C 319      11.292  83.505  32.217  1.00 23.23           C  
ANISOU 7442  C   ALA C 319     4379   1903   2544    633   1107    431       C  
ATOM   7443  O   ALA C 319      12.221  84.073  32.760  1.00 22.70           O  
ANISOU 7443  O   ALA C 319     4250   1899   2476    679   1083    458       O  
ATOM   7444  CB  ALA C 319      11.119  83.800  29.716  1.00 25.58           C  
ANISOU 7444  CB  ALA C 319     4676   2188   2853    605   1109    382       C  
ATOM   7445  N   VAL C 320      10.103  83.365  32.806  1.00 23.70           N  
ANISOU 7445  N   VAL C 320     4466   1931   2608    568   1111    407       N  
ATOM   7446  CA  VAL C 320       9.907  83.826  34.173  1.00 22.85           C  
ANISOU 7446  CA  VAL C 320     4326   1853   2500    560   1089    423       C  
ATOM   7447  C   VAL C 320      10.760  83.016  35.150  1.00 24.09           C  
ANISOU 7447  C   VAL C 320     4530   1999   2623    647   1116    473       C  
ATOM   7448  O   VAL C 320      11.331  83.592  36.091  1.00 25.18           O  
ANISOU 7448  O   VAL C 320     4611   2201   2753    686   1082    497       O  
ATOM   7449  CB  VAL C 320       8.438  83.821  34.611  1.00 24.74           C  
ANISOU 7449  CB  VAL C 320     4584   2065   2749    473   1094    384       C  
ATOM   7450  CG1 VAL C 320       8.311  84.452  35.982  1.00 24.20           C  
ANISOU 7450  CG1 VAL C 320     4476   2035   2680    470   1067    404       C  
ATOM   7451  CG2 VAL C 320       7.536  84.520  33.607  1.00 25.09           C  
ANISOU 7451  CG2 VAL C 320     4585   2133   2812    405   1068    330       C  
ATOM   7452  N   MET C 321      10.840  81.694  34.944  1.00 22.81           N  
ANISOU 7452  N   MET C 321     4474   1757   2434    684   1177    486       N  
ATOM   7453  CA  MET C 321      11.625  80.848  35.797  1.00 24.24           C  
ANISOU 7453  CA  MET C 321     4719   1920   2568    789   1211    538       C  
ATOM   7454  C   MET C 321      13.083  81.305  35.774  1.00 23.98           C  
ANISOU 7454  C   MET C 321     4604   1984   2522    888   1171    568       C  
ATOM   7455  O   MET C 321      13.740  81.413  36.825  1.00 23.89           O  
ANISOU 7455  O   MET C 321     4564   2033   2478    964   1151    598       O  
ATOM   7456  CB  MET C 321      11.560  79.379  35.344  1.00 26.73           C  
ANISOU 7456  CB  MET C 321     5176   2124   2854    819   1295    546       C  
ATOM   7457  CG  MET C 321      10.208  78.737  35.570  1.00 28.18           C  
ANISOU 7457  CG  MET C 321     5453   2210   3044    721   1353    511       C  
ATOM   7458  SD  MET C 321      10.043  77.092  34.864  1.00 30.76           S  
ANISOU 7458  SD  MET C 321     5951   2393   3341    724   1465    501       S  
ATOM   7459  CE  MET C 321      11.089  76.179  35.994  1.00 33.77           C  
ANISOU 7459  CE  MET C 321     6443   2738   3648    890   1518    588       C  
ATOM   7460  N   ILE C 322      13.587  81.522  34.553  1.00 23.23           N  
ANISOU 7460  N   ILE C 322     4473   1908   2445    888   1164    553       N  
ATOM   7461  CA  ILE C 322      14.941  81.954  34.338  1.00 24.96           C  
ANISOU 7461  CA  ILE C 322     4607   2220   2656    964   1137    569       C  
ATOM   7462  C   ILE C 322      15.144  83.345  34.960  1.00 25.49           C  
ANISOU 7462  C   ILE C 322     4547   2389   2748    926   1076    553       C  
ATOM   7463  O   ILE C 322      16.163  83.565  35.631  1.00 26.66           O  
ANISOU 7463  O   ILE C 322     4628   2628   2871    998   1053    566       O  
ATOM   7464  CB  ILE C 322      15.288  81.956  32.831  1.00 25.05           C  
ANISOU 7464  CB  ILE C 322     4612   2218   2686    956   1151    553       C  
ATOM   7465  CG1 ILE C 322      15.325  80.534  32.256  1.00 26.11           C  
ANISOU 7465  CG1 ILE C 322     4873   2259   2788   1010   1215    569       C  
ATOM   7466  CG2 ILE C 322      16.599  82.690  32.568  1.00 25.84           C  
ANISOU 7466  CG2 ILE C 322     4601   2426   2790   1004   1124    555       C  
ATOM   7467  CD1 ILE C 322      14.998  80.459  30.776  1.00 25.64           C  
ANISOU 7467  CD1 ILE C 322     4838   2153   2751    959   1233    538       C  
ATOM   7468  N   ALA C 323      14.208  84.266  34.714  1.00 24.76           N  
ANISOU 7468  N   ALA C 323     4423   2287   2697    819   1053    519       N  
ATOM   7469  CA  ALA C 323      14.312  85.637  35.253  1.00 25.12           C  
ANISOU 7469  CA  ALA C 323     4365   2413   2766    773   1005    501       C  
ATOM   7470  C   ALA C 323      14.505  85.560  36.775  1.00 28.61           C  
ANISOU 7470  C   ALA C 323     4791   2899   3178    816    986    519       C  
ATOM   7471  O   ALA C 323      15.420  86.205  37.293  1.00 27.13           O  
ANISOU 7471  O   ALA C 323     4513   2809   2983    844    955    513       O  
ATOM   7472  CB  ALA C 323      13.103  86.457  34.872  1.00 23.76           C  
ANISOU 7472  CB  ALA C 323     4189   2208   2628    670    992    469       C  
ATOM   7473  N   ASP C 324      13.727  84.680  37.453  1.00 28.59           N  
ANISOU 7473  N   ASP C 324     4882   2829   3152    827   1010    538       N  
ATOM   7474  CA  ASP C 324      13.778  84.581  38.884  1.00 29.29           C  
ANISOU 7474  CA  ASP C 324     4973   2948   3206    872    997    559       C  
ATOM   7475  C   ASP C 324      15.114  84.002  39.323  1.00 30.41           C  
ANISOU 7475  C   ASP C 324     5102   3157   3292   1007    997    589       C  
ATOM   7476  O   ASP C 324      15.608  84.407  40.354  1.00 31.08           O  
ANISOU 7476  O   ASP C 324     5127   3331   3350   1051    960    590       O  
ATOM   7477  CB  ASP C 324      12.619  83.784  39.480  1.00 32.57           C  
ANISOU 7477  CB  ASP C 324     5500   3266   3607    848   1037    571       C  
ATOM   7478  CG  ASP C 324      11.352  84.597  39.688  1.00 36.51           C  
ANISOU 7478  CG  ASP C 324     5975   3749   4146    731   1018    538       C  
ATOM   7479  OD1 ASP C 324      11.446  85.848  39.712  1.00 39.61           O  
ANISOU 7479  OD1 ASP C 324     6270   4212   4567    687    968    515       O  
ATOM   7480  OD2 ASP C 324      10.277  83.984  39.821  1.00 42.63           O  
ANISOU 7480  OD2 ASP C 324     6831   4443   4923    683   1059    532       O  
ATOM   7481  N   LYS C 325      15.678  83.052  38.562  1.00 29.95           N  
ANISOU 7481  N   LYS C 325     5101   3065   3212   1079   1036    609       N  
ATOM   7482  CA  LYS C 325      16.959  82.473  38.934  1.00 31.78           C  
ANISOU 7482  CA  LYS C 325     5319   3372   3382   1227   1036    637       C  
ATOM   7483  C   LYS C 325      18.076  83.521  38.849  1.00 31.73           C  
ANISOU 7483  C   LYS C 325     5151   3515   3389   1232    983    603       C  
ATOM   7484  O   LYS C 325      19.044  83.453  39.559  1.00 33.38           O  
ANISOU 7484  O   LYS C 325     5301   3834   3547   1335    958    607       O  
ATOM   7485  CB  LYS C 325      17.285  81.261  38.059  1.00 32.79           C  
ANISOU 7485  CB  LYS C 325     5549   3425   3484   1301   1096    665       C  
ATOM   7486  CG  LYS C 325      16.553  79.982  38.451  1.00 34.04           C  
ANISOU 7486  CG  LYS C 325     5880   3449   3601   1339   1165    703       C  
ATOM   7487  CD  LYS C 325      16.737  78.893  37.455  1.00 36.72           C  
ANISOU 7487  CD  LYS C 325     6327   3698   3924   1384   1231    720       C  
ATOM   7488  CE  LYS C 325      15.866  77.695  37.728  1.00 39.02           C  
ANISOU 7488  CE  LYS C 325     6802   3837   4186   1384   1316    744       C  
ATOM   7489  NZ  LYS C 325      16.202  77.076  39.034  1.00 40.90           N  
ANISOU 7489  NZ  LYS C 325     7116   4080   4344   1517   1340    795       N  
ATOM   7490  N   LEU C 326      17.938  84.498  37.967  1.00 32.82           N  
ANISOU 7490  N   LEU C 326     5219   3659   3590   1122    970    565       N  
ATOM   7491  CA  LEU C 326      18.992  85.508  37.762  1.00 36.07           C  
ANISOU 7491  CA  LEU C 326     5487   4197   4019   1106    939    524       C  
ATOM   7492  C   LEU C 326      18.854  86.644  38.786  1.00 38.90           C  
ANISOU 7492  C   LEU C 326     5757   4630   4390   1043    892    490       C  
ATOM   7493  O   LEU C 326      19.810  87.370  38.993  1.00 44.45           O  
ANISOU 7493  O   LEU C 326     6339   5455   5092   1042    868    450       O  
ATOM   7494  CB  LEU C 326      18.912  86.026  36.321  1.00 32.60           C  
ANISOU 7494  CB  LEU C 326     5035   3715   3636   1022    961    503       C  
ATOM   7495  CG  LEU C 326      19.310  84.983  35.266  1.00 33.46           C  
ANISOU 7495  CG  LEU C 326     5210   3774   3728   1092   1005    528       C  
ATOM   7496  CD1 LEU C 326      19.265  85.551  33.854  1.00 32.65           C  
ANISOU 7496  CD1 LEU C 326     5093   3636   3673   1016   1026    506       C  
ATOM   7497  CD2 LEU C 326      20.682  84.395  35.565  1.00 34.36           C  
ANISOU 7497  CD2 LEU C 326     5273   3993   3787   1227   1004    539       C  
ATOM   7498  N   LEU C 327      17.677  86.773  39.414  1.00 39.50           N  
ANISOU 7498  N   LEU C 327     5895   4637   4476    988    885    500       N  
ATOM   7499  CA  LEU C 327      17.405  87.779  40.474  1.00 41.77           C  
ANISOU 7499  CA  LEU C 327     6117   4981   4769    932    844    472       C  
ATOM   7500  C   LEU C 327      17.951  87.312  41.829  1.00 44.51           C  
ANISOU 7500  C   LEU C 327     6448   5414   5048   1042    817    485       C  
ATOM   7501  O   LEU C 327      18.224  86.124  42.036  1.00 53.19           O  
ANISOU 7501  O   LEU C 327     7619   6497   6091   1162    837    528       O  
ATOM   7502  CB  LEU C 327      15.898  88.012  40.564  1.00 37.48           C  
ANISOU 7502  CB  LEU C 327     5650   4331   4259    841    851    479       C  
ATOM   7503  CG  LEU C 327      15.321  88.875  39.453  1.00 39.79           C  
ANISOU 7503  CG  LEU C 327     5934   4573   4611    732    862    453       C  
ATOM   7504  CD1 LEU C 327      13.818  88.672  39.323  1.00 39.35           C  
ANISOU 7504  CD1 LEU C 327     5965   4412   4572    674    876    463       C  
ATOM   7505  CD2 LEU C 327      15.642  90.345  39.692  1.00 42.01           C  
ANISOU 7505  CD2 LEU C 327     6117   4926   4917    660    837    409       C  
TER    7506      LEU C 327                                                      
HETATM 7507 CL    CL A 401      26.812  49.271  36.883  1.00 29.21          CL  
HETATM 7508 CL    CL A 402      24.353  56.064  35.575  1.00 42.71          CL  
HETATM 7509 CL    CL A 403       3.179  47.631  46.156  1.00 48.11          CL  
HETATM 7510 CL    CL A 404      21.597  56.729  29.551  1.00 43.30          CL  
HETATM 7511 CL    CL A 405      17.854  57.570  43.186  1.00 37.74          CL  
HETATM 7512 MG    MG B 401      55.696 116.450  -3.595  1.00 44.21          MG  
HETATM 7513 CL    CL B 402      39.541 101.156   9.455  1.00 33.66          CL  
HETATM 7514 CL    CL B 403      41.206  84.956   5.027  1.00 23.10          CL  
HETATM 7515 MG    MG C 401      12.084  80.712  27.034  1.00 55.53          MG  
HETATM 7516 CL    CL C 402      -0.057 100.739  54.709  1.00 41.13          CL  
HETATM 7517 CL    CL C 403       7.487 104.246  43.724  1.00 45.13          CL  
HETATM 7518 CL    CL C 404      -7.699  84.957  42.446  1.00 54.81          CL  
HETATM 7519  O   HOH A 501      27.502  31.586  53.005  1.00 40.66           O  
HETATM 7520  O   HOH A 502      12.970  51.928  46.302  1.00 19.94           O  
HETATM 7521  O   HOH A 503      23.118  55.210  47.752  1.00 40.62           O  
HETATM 7522  O   HOH A 504      17.236  45.368  26.805  1.00 33.58           O  
HETATM 7523  O   HOH A 505      25.475  48.309  55.085  1.00 29.29           O  
HETATM 7524  O   HOH A 506      23.196  42.321  19.318  1.00 45.46           O  
HETATM 7525  O   HOH A 507      40.090  34.742  39.014  1.00 36.34           O  
HETATM 7526  O   HOH A 508      24.120  32.908  13.766  1.00 55.47           O  
HETATM 7527  O   HOH A 509      33.255  46.587  30.770  1.00 38.01           O  
HETATM 7528  O   HOH A 510      17.908  59.663  41.031  1.00 23.63           O  
HETATM 7529  O   HOH A 511       4.804  61.772  48.135  1.00 49.51           O  
HETATM 7530  O   HOH A 512      24.620  71.895  27.042  1.00 30.79           O  
HETATM 7531  O   HOH A 513       4.761  62.289  23.953  1.00 41.64           O  
HETATM 7532  O   HOH A 514      48.445  55.169  28.077  1.00 49.20           O  
HETATM 7533  O   HOH A 515      21.748  69.584  27.003  1.00 26.15           O  
HETATM 7534  O   HOH A 516       5.785  42.267  34.366  1.00 36.28           O  
HETATM 7535  O   HOH A 517      43.452  44.436  38.704  1.00 33.96           O  
HETATM 7536  O   HOH A 518       5.485  69.155  36.337  1.00 24.87           O  
HETATM 7537  O   HOH A 519      33.044  50.862  42.466  1.00 41.40           O  
HETATM 7538  O   HOH A 520      21.491  67.671  33.032  1.00 40.63           O  
HETATM 7539  O   HOH A 521      12.617  72.520  19.829  1.00 38.89           O  
HETATM 7540  O   HOH A 522      28.914  28.195  46.196  1.00 37.07           O  
HETATM 7541  O   HOH A 523      14.728  35.286  45.485  1.00 37.79           O  
HETATM 7542  O   HOH A 524      17.592  73.181  35.744  1.00 24.16           O  
HETATM 7543  O   HOH A 525      18.739  49.993  51.918  1.00 46.39           O  
HETATM 7544  O   HOH A 526      10.323  70.910  36.201  1.00 36.90           O  
HETATM 7545  O   HOH A 527       8.601  69.714  34.573  1.00 30.23           O  
HETATM 7546  O   HOH A 528      20.267  63.557  29.952  1.00 28.02           O  
HETATM 7547  O   HOH A 529       7.524  45.924  34.785  1.00 25.85           O  
HETATM 7548  O   HOH A 530      25.792  66.540  14.823  1.00 38.93           O  
HETATM 7549  O   HOH A 531      30.124  26.255  48.016  1.00 38.92           O  
HETATM 7550  O   HOH A 532      37.035  43.737  52.932  1.00 42.09           O  
HETATM 7551  O   HOH A 533       9.487  52.452  23.110  1.00 34.32           O  
HETATM 7552  O   HOH A 534      17.598  27.694  35.128  1.00 47.42           O  
HETATM 7553  O   HOH A 535      15.690  63.222  42.996  1.00 42.25           O  
HETATM 7554  O   HOH A 536      13.055  69.946  19.208  1.00 29.22           O  
HETATM 7555  O   HOH A 537      19.437  75.157  38.076  1.00 39.13           O  
HETATM 7556  O   HOH A 538      40.547  49.014  41.055  1.00 43.97           O  
HETATM 7557  O   HOH A 539       4.675  44.662  33.838  1.00 33.93           O  
HETATM 7558  O   HOH A 540      -0.586  58.841  43.460  1.00 39.51           O  
HETATM 7559  O   HOH A 541      31.935  25.881  45.339  1.00 26.71           O  
HETATM 7560  O   HOH A 542      25.918  46.333  30.844  1.00 25.71           O  
HETATM 7561  O   HOH A 543      15.878  44.012  48.197  1.00 24.74           O  
HETATM 7562  O   HOH A 544      -1.422  51.765  41.287  1.00 40.16           O  
HETATM 7563  O   HOH A 545      16.767  30.485  38.975  1.00 24.33           O  
HETATM 7564  O   HOH A 546      20.001  61.651  27.688  1.00 35.95           O  
HETATM 7565  O   HOH A 547      15.782  36.334  53.388  1.00 46.11           O  
HETATM 7566  O   HOH A 548      24.322  51.989  49.385  1.00 31.74           O  
HETATM 7567  O   HOH A 549      26.908  56.131  38.319  1.00 42.03           O  
HETATM 7568  O   HOH A 550      35.488  26.980  47.231  1.00 49.89           O  
HETATM 7569  O   HOH A 551      25.265  40.888  55.521  1.00 44.20           O  
HETATM 7570  O   HOH A 552       3.091  63.920  31.117  1.00 48.37           O  
HETATM 7571  O   HOH A 553      13.502  49.030  45.912  1.00 29.42           O  
HETATM 7572  O   HOH A 554      28.976  42.735  40.101  1.00 23.38           O  
HETATM 7573  O   HOH A 555      30.203  19.871  35.297  1.00 48.38           O  
HETATM 7574  O   HOH A 556      35.510  32.311  47.732  1.00 36.39           O  
HETATM 7575  O   HOH A 557      34.474  31.888  43.145  1.00 21.13           O  
HETATM 7576  O   HOH A 558      33.295  24.734  34.770  1.00 43.31           O  
HETATM 7577  O   HOH A 559      29.501  35.407  50.568  1.00 39.96           O  
HETATM 7578  O   HOH A 560      43.618  36.244  34.851  1.00 45.45           O  
HETATM 7579  O   HOH A 561      18.133  39.958  49.155  1.00 45.55           O  
HETATM 7580  O   HOH A 562       9.151  57.689  23.176  1.00 48.52           O  
HETATM 7581  O   HOH A 563      20.020  66.223  28.797  1.00 46.09           O  
HETATM 7582  O   HOH A 564      33.676  22.218  30.409  1.00 38.47           O  
HETATM 7583  O   HOH A 565      23.026  44.283  25.196  1.00 35.35           O  
HETATM 7584  O   HOH A 566      26.602  49.978  50.019  1.00 23.51           O  
HETATM 7585  O   HOH A 567      23.367  25.290  32.138  1.00 35.15           O  
HETATM 7586  O   HOH A 568      39.048  34.978  15.507  1.00 31.52           O  
HETATM 7587  O   HOH A 569       8.233  57.568  28.651  1.00 32.03           O  
HETATM 7588  O   HOH A 570      13.430  74.654  20.265  1.00 35.07           O  
HETATM 7589  O   HOH A 571      15.394  44.223  28.333  1.00 46.82           O  
HETATM 7590  O   HOH A 572      31.863  41.294  25.721  1.00 32.09           O  
HETATM 7591  O   HOH A 573      31.773  32.631  50.086  1.00 42.87           O  
HETATM 7592  O   HOH A 574      10.015  62.936  36.042  1.00 24.61           O  
HETATM 7593  O   HOH A 575      26.977  65.664  26.870  1.00 35.60           O  
HETATM 7594  O   HOH A 576      32.858  26.131  31.958  1.00 28.86           O  
HETATM 7595  O   HOH A 577      16.096  75.143  41.746  1.00 51.90           O  
HETATM 7596  O   HOH A 578      35.510  46.897  29.448  1.00 57.68           O  
HETATM 7597  O   HOH A 579      24.150  37.751  55.056  1.00 46.54           O  
HETATM 7598  O   HOH A 580      17.989  31.111  48.970  1.00 49.71           O  
HETATM 7599  O   HOH A 581      11.434  33.411  40.204  1.00 39.03           O  
HETATM 7600  O   HOH A 582      32.669  49.376  49.942  1.00 48.53           O  
HETATM 7601  O   HOH A 583      38.230  45.977  48.078  1.00 42.42           O  
HETATM 7602  O   HOH A 584      37.475  26.842  39.436  1.00 29.56           O  
HETATM 7603  O   HOH A 585      11.995  35.297  42.534  1.00 49.40           O  
HETATM 7604  O   HOH A 586      28.260  46.248  29.411  1.00 44.12           O  
HETATM 7605  O   HOH A 587      14.135  77.341  21.539  1.00 36.44           O  
HETATM 7606  O   HOH A 588       4.927  66.505  40.607  1.00 31.61           O  
HETATM 7607  O   HOH A 589      14.527  49.183  22.498  1.00 54.36           O  
HETATM 7608  O   HOH A 590       5.494  39.029  33.434  1.00 57.44           O  
HETATM 7609  O   HOH A 591      18.830  54.956  42.568  1.00 21.38           O  
HETATM 7610  O   HOH A 592      28.152  40.481  28.812  1.00 37.83           O  
HETATM 7611  O   HOH A 593      28.083  75.162  19.956  1.00 55.17           O  
HETATM 7612  O   HOH A 594      40.336  26.230  38.962  1.00 54.55           O  
HETATM 7613  O   HOH A 595      30.634  69.471  21.701  1.00 41.68           O  
HETATM 7614  O   HOH A 596      38.472  44.635  22.979  1.00 53.30           O  
HETATM 7615  O   HOH A 597       8.937  47.991  29.114  1.00 36.89           O  
HETATM 7616  O   HOH A 598      39.398  43.398  11.641  1.00 55.94           O  
HETATM 7617  O   HOH A 599      29.700  72.542  14.906  1.00 48.83           O  
HETATM 7618  O   HOH A 600      19.180  75.378  35.267  1.00 23.02           O  
HETATM 7619  O   HOH A 601      24.365  51.368  26.747  1.00 56.35           O  
HETATM 7620  O   HOH A 602      23.612  37.340  14.841  1.00 47.16           O  
HETATM 7621  O   HOH A 603       9.736  74.623  39.267  1.00 41.85           O  
HETATM 7622  O   HOH A 604      15.361  68.986  45.625  1.00 36.84           O  
HETATM 7623  O   HOH A 605      27.965  61.185  32.997  1.00 47.61           O  
HETATM 7624  O   HOH A 606      27.936  76.430  27.268  1.00 45.68           O  
HETATM 7625  O   HOH A 607       0.927  64.281  33.429  1.00 37.68           O  
HETATM 7626  O   HOH A 608       7.040  39.421  37.862  1.00 44.38           O  
HETATM 7627  O   HOH A 609      25.577  53.864  42.531  1.00 28.42           O  
HETATM 7628  O   HOH A 610      13.800  28.848  35.676  1.00 50.47           O  
HETATM 7629  O   HOH A 611      -2.000  53.131  44.085  1.00 34.14           O  
HETATM 7630  O   HOH A 612      20.318  64.271  26.655  1.00 27.62           O  
HETATM 7631  O   HOH A 613      25.608  60.977  40.548  1.00 53.89           O  
HETATM 7632  O   HOH A 614      42.621  46.690  39.850  1.00 32.05           O  
HETATM 7633  O   HOH A 615      37.326  23.895  40.601  1.00 24.61           O  
HETATM 7634  O   HOH A 616      25.563  46.659  27.028  1.00 49.76           O  
HETATM 7635  O   HOH A 617      34.495  43.673  25.394  1.00 57.29           O  
HETATM 7636  O   HOH A 618      10.940  60.104  48.169  1.00 48.39           O  
HETATM 7637  O   HOH A 619      25.682  75.769  20.720  1.00 42.70           O  
HETATM 7638  O   HOH A 620      43.704  33.849  36.612  1.00 43.96           O  
HETATM 7639  O   HOH A 621      28.788  38.761  54.028  1.00 40.13           O  
HETATM 7640  O   HOH A 622      22.283  48.462  23.791  1.00 52.48           O  
HETATM 7641  O   HOH A 623      26.531  73.836  17.274  1.00 41.14           O  
HETATM 7642  O   HOH A 624      22.497  17.984  38.032  1.00 64.01           O  
HETATM 7643  O   HOH A 625      18.385  70.633  44.203  1.00 45.28           O  
HETATM 7644  O   HOH A 626      12.752  37.180  51.460  1.00 51.94           O  
HETATM 7645  O   HOH A 627      15.844  32.862  29.123  1.00 43.00           O  
HETATM 7646  O   HOH A 628       4.698  54.781  24.277  1.00 39.43           O  
HETATM 7647  O   HOH A 629      41.826  37.466  42.331  1.00 34.03           O  
HETATM 7648  O   HOH A 630       9.088  69.081  44.873  1.00 51.83           O  
HETATM 7649  O   HOH A 631      28.757  79.805  29.362  1.00 54.44           O  
HETATM 7650  O   HOH A 632      27.307  60.577  26.087  1.00 40.78           O  
HETATM 7651  O   HOH A 633      23.394  53.354  35.379  1.00 30.06           O  
HETATM 7652  O   HOH A 634      34.518  42.998  22.192  1.00 45.49           O  
HETATM 7653  O   HOH A 635      10.929  37.836  43.342  1.00 43.22           O  
HETATM 7654  O   HOH A 636      32.559  21.669  27.703  1.00 54.70           O  
HETATM 7655  O   HOH A 637      29.294  27.334  16.934  1.00 50.20           O  
HETATM 7656  O   HOH A 638      -0.695  57.920  36.557  1.00 26.46           O  
HETATM 7657  O   HOH A 639      22.956  23.780  34.448  1.00 30.76           O  
HETATM 7658  O   HOH A 640      14.430  27.425  30.897  1.00 60.89           O  
HETATM 7659  O   HOH A 641      33.957  25.131  47.104  1.00 29.56           O  
HETATM 7660  O   HOH A 642      18.217  56.261  16.233  1.00 49.95           O  
HETATM 7661  O   HOH A 643      31.911  35.941  51.584  1.00 43.60           O  
HETATM 7662  O   HOH A 644      29.906  43.543  17.623  1.00 46.03           O  
HETATM 7663  O   HOH A 645      24.420  73.807  12.642  1.00 22.59           O  
HETATM 7664  O   HOH A 646      26.496  23.764  24.359  1.00 44.90           O  
HETATM 7665  O   HOH A 647       9.639  41.341  29.571  1.00 50.59           O  
HETATM 7666  O   HOH A 648      35.192  55.709  36.691  1.00 60.57           O  
HETATM 7667  O   HOH A 649      18.207  37.866  20.016  1.00 29.13           O  
HETATM 7668  O   HOH A 650      23.327  25.886  47.431  1.00 48.02           O  
HETATM 7669  O   HOH A 651      30.035  22.074  47.990  1.00 35.34           O  
HETATM 7670  O   HOH A 652      12.371  64.429  14.953  1.00 41.83           O  
HETATM 7671  O   HOH A 653      25.878  21.282  38.926  1.00 46.57           O  
HETATM 7672  O   HOH A 654      26.231  57.335  26.525  1.00 54.46           O  
HETATM 7673  O   HOH A 655      13.380  43.239  50.015  1.00 40.52           O  
HETATM 7674  O   HOH A 656       7.245  66.051  15.538  1.00 47.28           O  
HETATM 7675  O   HOH A 657       5.028  65.550  23.417  1.00 35.30           O  
HETATM 7676  O   HOH A 658      31.601  57.203  40.325  1.00 50.40           O  
HETATM 7677  O   HOH A 659      10.768  58.958  21.090  1.00 42.96           O  
HETATM 7678  O   HOH A 660      24.685  50.822  32.389  1.00 54.46           O  
HETATM 7679  O   HOH A 661      40.274  43.615  46.183  1.00 25.79           O  
HETATM 7680  O   HOH A 662      27.683  41.200  55.629  1.00 28.98           O  
HETATM 7681  O   HOH A 663      22.930  60.254  44.048  1.00 65.03           O  
HETATM 7682  O   HOH A 664      17.070  63.652  46.793  1.00 49.44           O  
HETATM 7683  O   HOH A 665      29.843  23.757  23.371  1.00 44.16           O  
HETATM 7684  O   HOH A 666      14.400  42.433  15.591  1.00 58.25           O  
HETATM 7685  O   HOH A 667      27.169  56.381  41.728  1.00 27.08           O  
HETATM 7686  O   HOH A 668      32.174  41.647  22.796  1.00 43.74           O  
HETATM 7687  O   HOH A 669      46.557  35.201  30.599  1.00 50.38           O  
HETATM 7688  O   HOH A 670      29.521  23.029  31.580  1.00 41.81           O  
HETATM 7689  O   HOH A 671       8.694  44.993  32.324  1.00 41.64           O  
HETATM 7690  O   HOH A 672      24.257  63.348  16.073  1.00 59.03           O  
HETATM 7691  O   HOH A 673      43.921  28.989  33.163  1.00 47.92           O  
HETATM 7692  O   HOH A 674      16.900  58.892  49.429  1.00 56.83           O  
HETATM 7693  O   HOH A 675       7.119  76.307  24.679  1.00 58.23           O  
HETATM 7694  O   HOH A 676      35.712  31.071  52.291  1.00 52.21           O  
HETATM 7695  O   HOH A 677      26.811  28.840  12.933  1.00 59.33           O  
HETATM 7696  O   HOH A 678      38.709  36.363   9.520  1.00 52.49           O  
HETATM 7697  O   HOH A 679      15.570  29.439  41.299  1.00 47.26           O  
HETATM 7698  O   HOH A 680      32.538  25.224  49.719  1.00 45.96           O  
HETATM 7699  O   HOH A 681      26.998  66.090  24.338  1.00 43.70           O  
HETATM 7700  O   HOH A 682      30.064  41.231  21.116  1.00 51.49           O  
HETATM 7701  O   HOH A 683      16.102  28.315  36.800  1.00 41.61           O  
HETATM 7702  O   HOH A 684      17.827  61.678  43.126  1.00 34.24           O  
HETATM 7703  O   HOH A 685      26.858  72.323  28.996  1.00 54.03           O  
HETATM 7704  O   HOH A 686      10.672  70.084  16.634  1.00 47.00           O  
HETATM 7705  O   HOH A 687      20.797  79.283  38.561  1.00 45.48           O  
HETATM 7706  O   HOH A 688      30.016  26.087  50.784  1.00 60.28           O  
HETATM 7707  O   HOH A 689       0.525  66.785  38.566  1.00 50.13           O  
HETATM 7708  O   HOH A 690       8.526  65.039  47.471  1.00 48.11           O  
HETATM 7709  O   HOH A 691       3.380  69.768  26.323  1.00 62.31           O  
HETATM 7710  O   HOH A 692      25.921  64.533  38.702  1.00 64.17           O  
HETATM 7711  O   HOH A 693       6.741  46.859  30.161  1.00 40.56           O  
HETATM 7712  O   HOH A 694      30.456  61.617  36.775  1.00 48.23           O  
HETATM 7713  O   HOH A 695       1.608  66.737  41.454  1.00 50.23           O  
HETATM 7714  O   HOH A 696      27.404  60.273  22.579  1.00 51.73           O  
HETATM 7715  O   HOH A 697      40.940  25.385  34.234  1.00 47.85           O  
HETATM 7716  O   HOH A 698      31.952  72.044  14.670  1.00 40.51           O  
HETATM 7717  O   HOH A 699       7.275  45.775  23.882  1.00 59.15           O  
HETATM 7718  O   HOH A 700      29.957  49.827  33.548  1.00 53.02           O  
HETATM 7719  O   HOH A 701      33.210  47.505  26.022  1.00 57.35           O  
HETATM 7720  O   HOH A 702      46.472  27.838  34.252  1.00 65.97           O  
HETATM 7721  O   HOH A 703      21.216  28.115  21.211  1.00 59.10           O  
HETATM 7722  O   HOH A 704      43.252  38.152  37.370  1.00 48.80           O  
HETATM 7723  O   HOH A 705       6.565  68.561  46.584  1.00 63.99           O  
HETATM 7724  O   HOH A 706      40.095  49.972  24.908  1.00 62.37           O  
HETATM 7725  O   HOH A 707      25.298  59.364  42.651  1.00 53.48           O  
HETATM 7726  O   HOH A 708      23.303  18.522  33.833  1.00 52.00           O  
HETATM 7727  O   HOH A 709      48.017  29.046  18.461  1.00 48.88           O  
HETATM 7728  O   HOH B 501      13.096 103.073  27.529  1.00 47.72           O  
HETATM 7729  O   HOH B 502      23.045 102.797  10.726  1.00 43.23           O  
HETATM 7730  O   HOH B 503      24.913 104.017  -4.784  1.00 40.97           O  
HETATM 7731  O   HOH B 504      59.750  99.445  10.251  1.00 46.63           O  
HETATM 7732  O   HOH B 505      56.457  98.775  10.882  1.00 32.35           O  
HETATM 7733  O   HOH B 506      30.390  72.750   5.952  1.00 30.67           O  
HETATM 7734  O   HOH B 507      34.125 111.326   4.016  1.00 36.89           O  
HETATM 7735  O   HOH B 508      27.505  90.689  21.423  1.00 29.79           O  
HETATM 7736  O   HOH B 509      42.436 111.134 -12.977  1.00 41.76           O  
HETATM 7737  O   HOH B 510      52.082 122.191   4.561  1.00 38.48           O  
HETATM 7738  O   HOH B 511      31.730  72.794   2.513  1.00 39.73           O  
HETATM 7739  O   HOH B 512      33.133 117.149 -14.029  1.00 59.18           O  
HETATM 7740  O   HOH B 513      21.518  92.566  22.544  1.00 21.10           O  
HETATM 7741  O   HOH B 514      21.690  93.578  26.305  1.00 29.99           O  
HETATM 7742  O   HOH B 515      46.752  93.798  -8.368  1.00 37.30           O  
HETATM 7743  O   HOH B 516      22.241  88.040   4.851  1.00 21.94           O  
HETATM 7744  O   HOH B 517      45.535 118.096  -7.185  1.00 27.36           O  
HETATM 7745  O   HOH B 518      29.392  99.540  -1.773  1.00 28.61           O  
HETATM 7746  O   HOH B 519      47.914  84.741   1.578  1.00 32.39           O  
HETATM 7747  O   HOH B 520      16.736 101.613  15.754  1.00 45.92           O  
HETATM 7748  O   HOH B 521      36.131  87.720  13.672  1.00 18.76           O  
HETATM 7749  O   HOH B 522      56.741 110.700  -7.351  1.00 34.21           O  
HETATM 7750  O   HOH B 523      41.160 124.085  -9.071  1.00 32.69           O  
HETATM 7751  O   HOH B 524      31.661  90.782  -8.455  1.00 50.17           O  
HETATM 7752  O   HOH B 525      29.175  98.671  19.215  1.00 43.96           O  
HETATM 7753  O   HOH B 526      15.475  85.343   6.647  1.00 35.19           O  
HETATM 7754  O   HOH B 527      26.472  91.073  25.671  1.00 57.09           O  
HETATM 7755  O   HOH B 528      28.572 101.133   0.228  1.00 26.21           O  
HETATM 7756  O   HOH B 529      45.625 113.226  21.107  1.00 58.26           O  
HETATM 7757  O   HOH B 530      58.134  99.956  -0.630  1.00 45.92           O  
HETATM 7758  O   HOH B 531      37.819 110.042  10.249  1.00 41.15           O  
HETATM 7759  O   HOH B 532      55.346 103.635  13.151  1.00 53.75           O  
HETATM 7760  O   HOH B 533      50.251  94.492  10.797  1.00 23.30           O  
HETATM 7761  O   HOH B 534      47.278 123.805 -12.401  1.00 66.30           O  
HETATM 7762  O   HOH B 535      52.513  96.198  -9.369  1.00 43.62           O  
HETATM 7763  O   HOH B 536      49.707  85.423   3.210  1.00 43.65           O  
HETATM 7764  O   HOH B 537      55.999 118.263  -9.586  1.00 42.32           O  
HETATM 7765  O   HOH B 538      55.796 106.866  -6.481  1.00 42.21           O  
HETATM 7766  O   HOH B 539      31.280  89.488  -4.251  1.00 22.17           O  
HETATM 7767  O   HOH B 540      57.452  93.742   3.488  1.00 26.86           O  
HETATM 7768  O   HOH B 541      48.488 104.410  16.012  1.00 53.95           O  
HETATM 7769  O   HOH B 542      22.014  97.156  27.080  1.00 50.14           O  
HETATM 7770  O   HOH B 543      23.866  76.651  13.794  1.00 28.75           O  
HETATM 7771  O   HOH B 544      28.271  75.492  11.756  1.00 25.65           O  
HETATM 7772  O   HOH B 545      56.496 108.593  -4.763  1.00 38.90           O  
HETATM 7773  O   HOH B 546      46.664  89.272  -0.095  1.00 19.19           O  
HETATM 7774  O   HOH B 547      26.639  92.761  -1.944  1.00 35.56           O  
HETATM 7775  O   HOH B 548      54.326  90.284  -2.518  1.00 34.68           O  
HETATM 7776  O   HOH B 549      51.780 110.976  11.340  1.00 37.93           O  
HETATM 7777  O   HOH B 550      25.108  79.299  17.944  1.00 36.01           O  
HETATM 7778  O   HOH B 551      20.256  94.342   1.252  1.00 34.68           O  
HETATM 7779  O   HOH B 552      21.069 103.710   9.405  1.00 57.62           O  
HETATM 7780  O   HOH B 553      18.159  91.309   5.372  1.00 29.24           O  
HETATM 7781  O   HOH B 554      27.411  83.017  11.296  1.00 21.36           O  
HETATM 7782  O   HOH B 555      54.163 110.845  -0.442  1.00 18.24           O  
HETATM 7783  O   HOH B 556      48.484 122.202 -10.731  1.00 46.58           O  
HETATM 7784  O   HOH B 557      48.743 116.954 -10.246  1.00 49.33           O  
HETATM 7785  O   HOH B 558      51.439 115.904   4.850  1.00 26.28           O  
HETATM 7786  O   HOH B 559      44.352 129.866  -8.665  1.00 28.64           O  
HETATM 7787  O   HOH B 560      48.730 120.094   7.298  1.00 36.61           O  
HETATM 7788  O   HOH B 561      39.256  89.837  10.197  1.00 17.18           O  
HETATM 7789  O   HOH B 562      15.614 103.595   5.676  1.00 61.21           O  
HETATM 7790  O   HOH B 563      13.182 100.320  13.521  1.00 38.80           O  
HETATM 7791  O   HOH B 564      11.937  81.292  20.114  1.00 55.39           O  
HETATM 7792  O   HOH B 565      26.071  83.552  24.037  1.00 22.38           O  
HETATM 7793  O   HOH B 566      43.210  93.202  -9.828  1.00 43.00           O  
HETATM 7794  O   HOH B 567      20.799  93.589  31.903  1.00 35.92           O  
HETATM 7795  O   HOH B 568      35.302 105.089   5.915  1.00 31.94           O  
HETATM 7796  O   HOH B 569      41.787 118.769  11.431  1.00 55.83           O  
HETATM 7797  O   HOH B 570      48.894 110.374 -19.473  1.00 61.14           O  
HETATM 7798  O   HOH B 571      48.703  86.852   6.900  1.00 35.04           O  
HETATM 7799  O   HOH B 572      49.894  92.216  -2.246  1.00 31.82           O  
HETATM 7800  O   HOH B 573      24.139  92.052  18.987  1.00 40.33           O  
HETATM 7801  O   HOH B 574      29.896 103.636   9.425  1.00 46.80           O  
HETATM 7802  O   HOH B 575      38.392 118.721 -12.860  1.00 44.31           O  
HETATM 7803  O   HOH B 576      43.825 100.717 -11.681  1.00 26.05           O  
HETATM 7804  O   HOH B 577      47.647  91.997  10.962  1.00 21.93           O  
HETATM 7805  O   HOH B 578      40.659 131.179  -6.578  1.00 23.90           O  
HETATM 7806  O   HOH B 579      45.478 103.769   5.456  1.00 23.76           O  
HETATM 7807  O   HOH B 580      13.692 103.727  21.182  1.00 37.90           O  
HETATM 7808  O   HOH B 581      21.396  77.168   7.168  1.00 22.47           O  
HETATM 7809  O   HOH B 582      35.043  96.701  13.875  1.00 26.79           O  
HETATM 7810  O   HOH B 583      41.938  94.768 -11.749  1.00 37.45           O  
HETATM 7811  O   HOH B 584      14.906  99.447  15.120  1.00 30.73           O  
HETATM 7812  O   HOH B 585      50.132  90.507  16.893  1.00 32.04           O  
HETATM 7813  O   HOH B 586      25.687  93.127  17.030  1.00 25.02           O  
HETATM 7814  O   HOH B 587      57.950 115.750  -4.027  1.00 35.16           O  
HETATM 7815  O   HOH B 588      26.865  80.944  -2.367  1.00 32.21           O  
HETATM 7816  O   HOH B 589       3.234 102.011  14.786  1.00 38.63           O  
HETATM 7817  O   HOH B 590      25.251  84.015  26.649  1.00 24.16           O  
HETATM 7818  O   HOH B 591      25.831 101.540  18.725  1.00 38.44           O  
HETATM 7819  O   HOH B 592      42.079  86.758   2.736  1.00 18.85           O  
HETATM 7820  O   HOH B 593      24.815  94.768  15.346  1.00 34.10           O  
HETATM 7821  O   HOH B 594      11.698  88.167  11.325  1.00 38.30           O  
HETATM 7822  O   HOH B 595      31.255 122.518  11.170  1.00 54.97           O  
HETATM 7823  O   HOH B 596      35.667 132.965   4.099  1.00 44.66           O  
HETATM 7824  O   HOH B 597      23.515  79.594  15.992  1.00 28.57           O  
HETATM 7825  O   HOH B 598      36.242 110.016   2.189  1.00 38.54           O  
HETATM 7826  O   HOH B 599      18.237  89.342   0.631  1.00 35.57           O  
HETATM 7827  O   HOH B 600      52.853 101.245 -14.105  1.00 54.74           O  
HETATM 7828  O   HOH B 601      28.403  74.034   2.086  1.00 37.29           O  
HETATM 7829  O   HOH B 602      54.234 114.313   7.887  1.00 27.54           O  
HETATM 7830  O   HOH B 603      22.816  94.484  17.179  1.00 32.78           O  
HETATM 7831  O   HOH B 604      34.087 104.035 -10.942  1.00 43.64           O  
HETATM 7832  O   HOH B 605      10.785  87.714  20.633  1.00 30.49           O  
HETATM 7833  O   HOH B 606      17.641  97.428   8.814  1.00 26.08           O  
HETATM 7834  O   HOH B 607      23.157  84.071   1.393  1.00 48.45           O  
HETATM 7835  O   HOH B 608      20.267  79.655   7.782  1.00 48.52           O  
HETATM 7836  O   HOH B 609      32.172 101.165 -13.915  1.00 41.10           O  
HETATM 7837  O   HOH B 610       8.794 100.024  25.498  1.00 28.52           O  
HETATM 7838  O   HOH B 611      56.824 110.617  11.498  1.00 44.21           O  
HETATM 7839  O   HOH B 612      30.232  81.078  -7.443  1.00 48.00           O  
HETATM 7840  O   HOH B 613      49.134 117.364  -6.481  1.00 31.36           O  
HETATM 7841  O   HOH B 614      48.565  84.069   7.428  1.00 40.92           O  
HETATM 7842  O   HOH B 615      52.973  88.582   3.429  1.00 28.31           O  
HETATM 7843  O   HOH B 616      47.991 107.886  17.651  1.00 38.97           O  
HETATM 7844  O   HOH B 617      58.824 104.503  -0.683  1.00 42.56           O  
HETATM 7845  O   HOH B 618      48.785 119.969  -6.732  1.00 37.50           O  
HETATM 7846  O   HOH B 619      18.537  79.395  10.128  1.00 41.55           O  
HETATM 7847  O   HOH B 620      33.202  73.793   0.049  1.00 26.45           O  
HETATM 7848  O   HOH B 621      42.015  95.567  13.163  1.00 24.39           O  
HETATM 7849  O   HOH B 622      53.673 117.137  -3.640  1.00 34.31           O  
HETATM 7850  O   HOH B 623      27.339  91.464  28.907  1.00 58.32           O  
HETATM 7851  O   HOH B 624      28.778  97.796  12.460  1.00 18.25           O  
HETATM 7852  O   HOH B 625      24.477 117.967  -8.216  1.00 31.93           O  
HETATM 7853  O   HOH B 626      32.548  75.040  -3.278  1.00 29.88           O  
HETATM 7854  O   HOH B 627      22.359 102.596  -2.720  1.00 54.28           O  
HETATM 7855  O   HOH B 628      43.434  84.239   7.086  1.00 25.92           O  
HETATM 7856  O   HOH B 629      38.871  79.364  11.343  1.00 19.89           O  
HETATM 7857  O   HOH B 630      54.469 108.606  12.409  1.00 24.40           O  
HETATM 7858  O   HOH B 631      24.940  98.585  22.584  1.00 33.07           O  
HETATM 7859  O   HOH B 632      30.704 127.279   1.181  1.00 33.94           O  
HETATM 7860  O   HOH B 633      37.003  79.566  14.074  1.00 55.22           O  
HETATM 7861  O   HOH B 634      46.272  90.805  13.278  1.00 39.18           O  
HETATM 7862  O   HOH B 635      15.769  97.950  12.890  1.00 34.07           O  
HETATM 7863  O   HOH B 636      10.890  86.478  23.211  1.00 35.72           O  
HETATM 7864  O   HOH B 637      56.504 117.742  -5.697  1.00 38.41           O  
HETATM 7865  O   HOH B 638      21.150  87.435   1.200  1.00 47.26           O  
HETATM 7866  O   HOH B 639      50.290 105.519 -13.784  1.00 48.06           O  
HETATM 7867  O   HOH B 640       9.542  84.325  15.008  1.00 51.46           O  
HETATM 7868  O   HOH B 641      28.502  98.390  -5.722  1.00 35.55           O  
HETATM 7869  O   HOH B 642      22.014 102.127  13.156  1.00 57.61           O  
HETATM 7870  O   HOH B 643      51.087 120.138   5.838  1.00 30.48           O  
HETATM 7871  O   HOH B 644      15.825 105.309  24.625  1.00 52.68           O  
HETATM 7872  O   HOH B 645      25.776  77.019   1.379  1.00 35.53           O  
HETATM 7873  O   HOH B 646      35.718  79.423  20.232  1.00 41.18           O  
HETATM 7874  O   HOH B 647      38.712 121.386 -11.184  1.00 40.66           O  
HETATM 7875  O   HOH B 648      39.499  85.126  14.011  1.00 44.81           O  
HETATM 7876  O   HOH B 649      53.702 113.210 -13.662  1.00 56.51           O  
HETATM 7877  O   HOH B 650      59.675  95.403   7.295  1.00 17.27           O  
HETATM 7878  O   HOH B 651      27.531 110.261  -8.298  1.00 43.38           O  
HETATM 7879  O   HOH B 652      35.533  97.520  11.031  1.00 29.17           O  
HETATM 7880  O   HOH B 653      45.931 128.920  -0.014  1.00 38.63           O  
HETATM 7881  O   HOH B 654      29.458 124.614  -3.288  1.00 57.55           O  
HETATM 7882  O   HOH B 655       6.577 100.217  22.127  1.00 23.16           O  
HETATM 7883  O   HOH B 656      34.692  88.853  22.630  1.00 51.39           O  
HETATM 7884  O   HOH B 657      51.071  88.457   8.838  1.00 21.72           O  
HETATM 7885  O   HOH B 658      50.920  88.762  -7.272  1.00 38.07           O  
HETATM 7886  O   HOH B 659      14.027  89.095   3.368  1.00 51.68           O  
HETATM 7887  O   HOH B 660      20.452 101.876  26.808  1.00 44.74           O  
HETATM 7888  O   HOH B 661      29.775 117.378  17.653  1.00 64.20           O  
HETATM 7889  O   HOH B 662      34.985  81.417  23.099  1.00 39.33           O  
HETATM 7890  O   HOH B 663      35.839 108.697  17.229  1.00 54.98           O  
HETATM 7891  O   HOH B 664      50.779 119.019  -4.730  1.00 46.10           O  
HETATM 7892  O   HOH B 665      30.711  92.421  -4.205  1.00 40.32           O  
HETATM 7893  O   HOH B 666      23.593  73.223   7.659  1.00 44.99           O  
HETATM 7894  O   HOH B 667      25.833 108.528  -6.484  1.00 28.30           O  
HETATM 7895  O   HOH B 668      41.253  96.036  16.194  1.00 23.10           O  
HETATM 7896  O   HOH B 669      48.392 127.705   2.084  1.00  9.41           O  
HETATM 7897  O   HOH B 670       8.754  88.504  16.652  1.00 43.46           O  
HETATM 7898  O   HOH B 671      47.473  91.012  15.688  1.00 42.76           O  
HETATM 7899  O   HOH B 672      60.948 113.098  -3.988  1.00 56.28           O  
HETATM 7900  O   HOH B 673      57.554 116.989   1.117  1.00 59.85           O  
HETATM 7901  O   HOH B 674      10.382  83.359  19.332  1.00 54.96           O  
HETATM 7902  O   HOH B 675      42.511  90.254  -7.951  1.00 45.89           O  
HETATM 7903  O   HOH B 676      56.986 118.353  -2.516  1.00 46.23           O  
HETATM 7904  O   HOH B 677      54.806  89.600   4.797  1.00 43.46           O  
HETATM 7905  O   HOH B 678      29.219  91.106  23.096  1.00 52.60           O  
HETATM 7906  O   HOH B 679      35.013  78.485  17.796  1.00 50.18           O  
HETATM 7907  O   HOH B 680      28.642  87.031  -8.767  1.00 45.00           O  
HETATM 7908  O   HOH B 681      39.039 134.295   0.627  1.00 35.19           O  
HETATM 7909  O   HOH B 682      37.278  85.688  15.304  1.00 37.45           O  
HETATM 7910  O   HOH B 683      45.542 129.867   2.515  1.00 37.73           O  
HETATM 7911  O   HOH B 684      32.247 115.812   4.767  1.00 46.61           O  
HETATM 7912  O   HOH B 685      56.914 121.883   3.588  1.00 57.05           O  
HETATM 7913  O   HOH B 686      20.138 109.490   2.031  1.00 46.59           O  
HETATM 7914  O   HOH B 687      23.152  86.144   2.438  1.00 32.69           O  
HETATM 7915  O   HOH B 688      48.621 125.427   5.511  1.00 45.69           O  
HETATM 7916  O   HOH B 689      59.437 111.876   7.434  1.00 57.16           O  
HETATM 7917  O   HOH B 690      13.495  75.786  18.251  1.00 56.72           O  
HETATM 7918  O   HOH B 691      13.929  84.468   9.062  1.00 31.99           O  
HETATM 7919  O   HOH B 692      38.992  93.050 -11.383  1.00 41.39           O  
HETATM 7920  O   HOH B 693      15.169  79.567  12.511  1.00 54.47           O  
HETATM 7921  O   HOH B 694      28.997  92.889  26.508  1.00 59.37           O  
HETATM 7922  O   HOH B 695      23.272  94.100  28.129  1.00 45.48           O  
HETATM 7923  O   HOH B 696      35.968 113.922  24.004  1.00 49.99           O  
HETATM 7924  O   HOH B 697      30.949  83.448  -8.463  1.00 53.15           O  
HETATM 7925  O   HOH B 698      37.452 100.514  11.246  1.00 38.99           O  
HETATM 7926  O   HOH B 699      32.337 135.044  -1.323  1.00 40.32           O  
HETATM 7927  O   HOH B 700      42.829 127.124 -12.203  1.00 50.79           O  
HETATM 7928  O   HOH B 701      58.379  97.944  -7.620  1.00 47.58           O  
HETATM 7929  O   HOH B 702      15.632  80.603   8.111  1.00 49.58           O  
HETATM 7930  O   HOH B 703      29.581 105.724   5.765  1.00 58.64           O  
HETATM 7931  O   HOH B 704      35.583 104.998  15.412  1.00 50.43           O  
HETATM 7932  O   HOH B 705      49.610 112.917 -15.332  1.00 56.85           O  
HETATM 7933  O   HOH B 706      45.150 125.995   8.557  1.00 61.58           O  
HETATM 7934  O   HOH B 707      19.109  82.661   1.282  1.00 47.53           O  
HETATM 7935  O   HOH B 708      18.998  91.375  -1.692  1.00 58.25           O  
HETATM 7936  O   HOH B 709      27.876 118.452 -11.916  1.00 52.09           O  
HETATM 7937  O   HOH B 710      35.731  74.719  13.817  1.00 52.83           O  
HETATM 7938  O   HOH B 711      36.375  80.610  17.034  1.00 47.14           O  
HETATM 7939  O   HOH B 712      22.618  99.486  22.572  1.00 40.98           O  
HETATM 7940  O   HOH B 713      27.375  81.576  30.934  1.00 44.15           O  
HETATM 7941  O   HOH B 714      59.196 106.636  -6.967  1.00 50.07           O  
HETATM 7942  O   HOH B 715      34.527  99.989 -17.015  1.00 53.23           O  
HETATM 7943  O   HOH B 716      31.937 136.019   0.800  1.00 49.34           O  
HETATM 7944  O   HOH B 717      40.734  91.244  16.668  1.00 59.50           O  
HETATM 7945  O   HOH B 718      45.879 125.208 -13.503  1.00 68.25           O  
HETATM 7946  O   HOH B 719      38.410  87.623  11.882  1.00 11.88           O  
HETATM 7947  O   HOH B 720      20.751  93.805  -4.996  1.00 57.60           O  
HETATM 7948  O   HOH B 721      44.520 129.026 -11.424  1.00 47.30           O  
HETATM 7949  O   HOH B 722      49.250 105.947 -18.877  1.00 56.63           O  
HETATM 7950  O   HOH B 723      30.644 108.557   6.085  1.00 53.63           O  
HETATM 7951  O   HOH B 724      60.886 111.616   4.669  1.00 50.51           O  
HETATM 7952  O   HOH B 725      39.342  97.349  19.304  1.00 54.15           O  
HETATM 7953  O   HOH B 726      28.464 120.872  10.081  1.00 48.71           O  
HETATM 7954  O   HOH B 727      18.085 114.181  -0.573  1.00 50.18           O  
HETATM 7955  O   HOH B 728      45.818 118.046 -10.053  1.00 50.57           O  
HETATM 7956  O   HOH B 729      26.375 116.195   7.283  1.00 56.65           O  
HETATM 7957  O   HOH B 730      16.480 104.389  21.717  1.00 55.90           O  
HETATM 7958  O   HOH B 731      20.304 101.902  21.474  1.00 55.05           O  
HETATM 7959  O   HOH B 732      20.348 110.400   4.472  1.00 65.07           O  
HETATM 7960  O   HOH B 733      34.016 132.810  -9.879  1.00 60.17           O  
HETATM 7961  O   HOH B 734      37.617 105.544  11.084  1.00 45.01           O  
HETATM 7962  O   HOH B 735      59.224 116.504  -6.603  1.00 56.44           O  
HETATM 7963  O   HOH B 736      23.988 103.619  21.484  1.00 64.07           O  
HETATM 7964  O   HOH C 501     -11.967 111.723  74.318  1.00 41.15           O  
HETATM 7965  O   HOH C 502      -0.646  74.303  42.632  1.00 38.17           O  
HETATM 7966  O   HOH C 503     -19.493 113.780  55.590  1.00 41.71           O  
HETATM 7967  O   HOH C 504     -13.738  97.742  77.199  1.00 38.22           O  
HETATM 7968  O   HOH C 505     -21.887 110.686  61.216  1.00 34.25           O  
HETATM 7969  O   HOH C 506     -17.119 117.805  66.180  1.00 54.18           O  
HETATM 7970  O   HOH C 507      -3.410  94.875  67.059  1.00 35.39           O  
HETATM 7971  O   HOH C 508      -4.770  91.520  27.612  1.00 40.11           O  
HETATM 7972  O   HOH C 509      14.970  85.146  42.668  1.00 45.97           O  
HETATM 7973  O   HOH C 510       7.761  84.002  39.544  1.00 25.34           O  
HETATM 7974  O   HOH C 511      -9.427  93.101  51.263  1.00 56.92           O  
HETATM 7975  O   HOH C 512     -11.475 113.745  42.552  1.00 35.14           O  
HETATM 7976  O   HOH C 513      -9.161 107.257  38.658  1.00 26.55           O  
HETATM 7977  O   HOH C 514     -18.980 106.243  69.223  1.00 32.40           O  
HETATM 7978  O   HOH C 515     -12.559 100.458  45.410  1.00 32.05           O  
HETATM 7979  O   HOH C 516       8.169 112.392  63.578  1.00 51.54           O  
HETATM 7980  O   HOH C 517      -7.334  98.428  74.323  1.00 41.72           O  
HETATM 7981  O   HOH C 518      -7.866 110.060  29.940  1.00 49.33           O  
HETATM 7982  O   HOH C 519      -5.740  95.120  60.028  1.00 47.48           O  
HETATM 7983  O   HOH C 520     -19.111 105.392  48.767  1.00 38.48           O  
HETATM 7984  O   HOH C 521      -7.070 119.887  33.444  1.00 37.07           O  
HETATM 7985  O   HOH C 522      -0.026 116.046  48.703  1.00 23.88           O  
HETATM 7986  O   HOH C 523       1.083 121.471  60.078  1.00 51.13           O  
HETATM 7987  O   HOH C 524       8.084  97.626  26.925  1.00 27.12           O  
HETATM 7988  O   HOH C 525      -6.286  97.431  54.571  1.00 36.18           O  
HETATM 7989  O   HOH C 526     -10.374  91.889  74.360  1.00 33.88           O  
HETATM 7990  O   HOH C 527     -13.039  88.821  78.288  1.00 41.97           O  
HETATM 7991  O   HOH C 528       5.881 117.087  65.400  1.00 46.93           O  
HETATM 7992  O   HOH C 529       0.704  81.087  30.816  1.00 28.47           O  
HETATM 7993  O   HOH C 530       1.811  89.045  41.992  1.00 33.29           O  
HETATM 7994  O   HOH C 531      10.436  80.093  25.870  1.00 45.42           O  
HETATM 7995  O   HOH C 532     -25.468 102.367  70.660  1.00 41.99           O  
HETATM 7996  O   HOH C 533       9.761  89.591  41.567  1.00 35.51           O  
HETATM 7997  O   HOH C 534     -11.689  98.132  58.120  1.00 37.05           O  
HETATM 7998  O   HOH C 535      -2.645  96.631  52.367  1.00 49.92           O  
HETATM 7999  O   HOH C 536      -3.615 114.011  71.018  1.00 46.23           O  
HETATM 8000  O   HOH C 537      -0.960 119.226  63.660  1.00 46.32           O  
HETATM 8001  O   HOH C 538       8.521 102.330  28.298  1.00 31.86           O  
HETATM 8002  O   HOH C 539       5.336 104.952  45.686  1.00 22.63           O  
HETATM 8003  O   HOH C 540      -1.750 118.050  52.492  1.00 33.09           O  
HETATM 8004  O   HOH C 541      -7.247 109.163  76.610  1.00 51.83           O  
HETATM 8005  O   HOH C 542       7.776 101.551  42.636  1.00 29.79           O  
HETATM 8006  O   HOH C 543      -9.293 119.412  55.805  1.00 41.15           O  
HETATM 8007  O   HOH C 544       3.917 111.469  42.580  1.00 31.41           O  
HETATM 8008  O   HOH C 545       8.985 114.934  61.490  1.00 49.92           O  
HETATM 8009  O   HOH C 546      -3.543  74.879  33.363  1.00 54.92           O  
HETATM 8010  O   HOH C 547       8.563  94.820  29.253  1.00 27.90           O  
HETATM 8011  O   HOH C 548       4.504  98.587  33.505  1.00 24.31           O  
HETATM 8012  O   HOH C 549     -10.631 117.242  70.510  1.00 37.62           O  
HETATM 8013  O   HOH C 550      10.489  81.776  41.342  1.00 32.91           O  
HETATM 8014  O   HOH C 551       4.397  97.111  67.177  1.00 25.94           O  
HETATM 8015  O   HOH C 552      -8.603 118.616  51.258  1.00 28.56           O  
HETATM 8016  O   HOH C 553      10.087 107.356  50.180  1.00 44.87           O  
HETATM 8017  O   HOH C 554       9.261 114.106  51.781  1.00 44.14           O  
HETATM 8018  O   HOH C 555       6.750 112.830  41.571  1.00 54.15           O  
HETATM 8019  O   HOH C 556      -2.830 111.419  77.601  1.00 55.86           O  
HETATM 8020  O   HOH C 557      -1.336 105.815  26.606  1.00 37.14           O  
HETATM 8021  O   HOH C 558     -16.612  89.504  56.965  1.00 47.98           O  
HETATM 8022  O   HOH C 559       9.333  92.598  70.289  1.00 24.07           O  
HETATM 8023  O   HOH C 560      -1.447 117.115  64.608  1.00 43.07           O  
HETATM 8024  O   HOH C 561       1.579 112.418  43.979  1.00 25.38           O  
HETATM 8025  O   HOH C 562       8.285 110.164  56.564  1.00 30.60           O  
HETATM 8026  O   HOH C 563      -4.169 117.853  39.205  1.00 36.59           O  
HETATM 8027  O   HOH C 564      -4.384  96.215  33.511  1.00 29.09           O  
HETATM 8028  O   HOH C 565     -15.213 102.745  43.536  1.00 34.77           O  
HETATM 8029  O   HOH C 566     -21.625 120.766  62.589  1.00 46.82           O  
HETATM 8030  O   HOH C 567     -11.030  94.006  36.316  1.00 34.26           O  
HETATM 8031  O   HOH C 568     -15.489 115.506  54.037  1.00 31.27           O  
HETATM 8032  O   HOH C 569      -1.206  87.486  27.353  1.00 54.07           O  
HETATM 8033  O   HOH C 570      -5.858 113.486  29.985  1.00 39.81           O  
HETATM 8034  O   HOH C 571      -7.207  91.616  33.393  1.00 40.72           O  
HETATM 8035  O   HOH C 572       8.302 104.756  26.319  1.00 50.52           O  
HETATM 8036  O   HOH C 573     -18.468 107.238  72.582  1.00 37.11           O  
HETATM 8037  O   HOH C 574      14.276  90.557  35.423  1.00 26.65           O  
HETATM 8038  O   HOH C 575       5.857  96.771  62.997  1.00 27.39           O  
HETATM 8039  O   HOH C 576      -8.602 122.151  56.257  1.00 42.80           O  
HETATM 8040  O   HOH C 577       9.037 103.216  61.052  1.00 47.55           O  
HETATM 8041  O   HOH C 578       0.745  97.237  26.236  1.00 48.72           O  
HETATM 8042  O   HOH C 579      16.433 101.232  37.428  1.00 33.49           O  
HETATM 8043  O   HOH C 580      14.147  99.961  30.615  1.00 60.31           O  
HETATM 8044  O   HOH C 581       4.847 119.418  59.331  1.00 36.44           O  
HETATM 8045  O   HOH C 582      -6.213 104.278  72.880  1.00 25.24           O  
HETATM 8046  O   HOH C 583       4.385  89.808  41.415  1.00 31.01           O  
HETATM 8047  O   HOH C 584     -10.406  91.173  67.638  1.00 49.62           O  
HETATM 8048  O   HOH C 585      -5.501 106.925  29.606  1.00 34.87           O  
HETATM 8049  O   HOH C 586       6.467 103.107  51.897  1.00 25.13           O  
HETATM 8050  O   HOH C 587       7.814 103.464  66.547  1.00 28.10           O  
HETATM 8051  O   HOH C 588     -12.181  97.950  46.477  1.00 26.48           O  
HETATM 8052  O   HOH C 589       6.062 107.614  26.656  1.00 44.96           O  
HETATM 8053  O   HOH C 590      16.095  88.466  35.769  1.00 25.91           O  
HETATM 8054  O   HOH C 591     -10.859 101.185  38.550  1.00 37.76           O  
HETATM 8055  O   HOH C 592      -3.300 101.646  72.188  1.00 38.17           O  
HETATM 8056  O   HOH C 593     -22.894  87.068  67.393  1.00 33.77           O  
HETATM 8057  O   HOH C 594       9.809 103.459  46.738  1.00 47.07           O  
HETATM 8058  O   HOH C 595     -14.049 112.941  75.517  1.00 50.33           O  
HETATM 8059  O   HOH C 596      10.205  97.728  49.285  1.00 49.69           O  
HETATM 8060  O   HOH C 597      -8.358 112.222  31.215  1.00 52.84           O  
HETATM 8061  O   HOH C 598       1.603 102.903  70.280  1.00 40.09           O  
HETATM 8062  O   HOH C 599       3.076  86.654  40.612  1.00 30.55           O  
HETATM 8063  O   HOH C 600       2.572  80.126  29.158  1.00 39.64           O  
HETATM 8064  O   HOH C 601      10.668  95.061  30.451  1.00 28.77           O  
HETATM 8065  O   HOH C 602      -0.656  92.451  45.797  1.00 24.10           O  
HETATM 8066  O   HOH C 603       5.379  97.528  51.036  1.00 41.49           O  
HETATM 8067  O   HOH C 604       5.290 118.856  52.477  1.00 32.96           O  
HETATM 8068  O   HOH C 605      -7.108 111.270  69.699  1.00 28.05           O  
HETATM 8069  O   HOH C 606      17.873  90.847  35.996  1.00 51.24           O  
HETATM 8070  O   HOH C 607       6.927 101.760  24.671  1.00 41.22           O  
HETATM 8071  O   HOH C 608       5.618  87.976  40.024  1.00 39.98           O  
HETATM 8072  O   HOH C 609      -3.090 117.317  67.785  1.00 42.90           O  
HETATM 8073  O   HOH C 610     -21.029 103.234  50.364  1.00 44.51           O  
HETATM 8074  O   HOH C 611     -28.774  95.862  63.296  1.00 36.03           O  
HETATM 8075  O   HOH C 612      -7.620  92.894  62.632  1.00 54.92           O  
HETATM 8076  O   HOH C 613     -19.750  80.130  69.095  1.00 55.13           O  
HETATM 8077  O   HOH C 614       2.700 102.619  25.293  1.00 34.95           O  
HETATM 8078  O   HOH C 615      -2.967  90.607  69.152  1.00 35.87           O  
HETATM 8079  O   HOH C 616     -17.288 108.635  70.634  1.00 35.81           O  
HETATM 8080  O   HOH C 617     -18.935  97.705  78.703  1.00 30.53           O  
HETATM 8081  O   HOH C 618     -10.506 116.156  35.321  1.00 46.53           O  
HETATM 8082  O   HOH C 619      14.871  78.258  41.412  1.00 39.99           O  
HETATM 8083  O   HOH C 620      14.839  95.925  28.831  1.00 35.83           O  
HETATM 8084  O   HOH C 621       1.975  85.172  48.373  1.00 44.29           O  
HETATM 8085  O   HOH C 622       0.847 116.539  67.052  1.00 47.62           O  
HETATM 8086  O   HOH C 623      -1.187 114.008  27.981  1.00 44.15           O  
HETATM 8087  O   HOH C 624       1.799 108.414  25.614  1.00 46.54           O  
HETATM 8088  O   HOH C 625      -2.645 122.366  43.150  1.00 44.07           O  
HETATM 8089  O   HOH C 626      -7.661  97.743  31.591  1.00 47.44           O  
HETATM 8090  O   HOH C 627     -24.743  83.950  66.323  1.00 47.27           O  
HETATM 8091  O   HOH C 628     -28.249  93.680  55.497  1.00 37.92           O  
HETATM 8092  O   HOH C 629      -1.979 105.004  73.604  1.00 34.65           O  
HETATM 8093  O   HOH C 630      12.300 101.851  43.816  1.00 55.32           O  
HETATM 8094  O   HOH C 631       4.713  79.036  29.150  1.00 39.10           O  
HETATM 8095  O   HOH C 632       6.856  76.656  46.879  1.00 35.87           O  
HETATM 8096  O   HOH C 633       5.327 118.602  61.905  1.00 52.46           O  
HETATM 8097  O   HOH C 634       1.557  99.492  24.539  1.00 31.25           O  
HETATM 8098  O   HOH C 635      -0.345  70.269  36.421  1.00 36.39           O  
HETATM 8099  O   HOH C 636       3.062  81.455  25.323  1.00 63.35           O  
HETATM 8100  O   HOH C 637     -26.600 102.338  66.620  1.00 43.72           O  
HETATM 8101  O   HOH C 638       4.749 105.556  70.023  1.00 32.38           O  
HETATM 8102  O   HOH C 639      -3.266 121.808  46.472  1.00 53.49           O  
HETATM 8103  O   HOH C 640     -16.162 114.938  41.680  1.00 41.97           O  
HETATM 8104  O   HOH C 641       0.572  97.943  51.072  1.00 36.71           O  
HETATM 8105  O   HOH C 642     -20.644  78.381  64.426  1.00 65.58           O  
HETATM 8106  O   HOH C 643     -21.693  97.203  48.990  1.00 30.26           O  
HETATM 8107  O   HOH C 644     -12.552 121.638  63.401  1.00 52.56           O  
HETATM 8108  O   HOH C 645       5.988  83.685  46.160  1.00 38.15           O  
HETATM 8109  O   HOH C 646      11.764  93.059  61.501  1.00 57.83           O  
HETATM 8110  O   HOH C 647     -10.364  95.492  31.137  1.00 44.77           O  
HETATM 8111  O   HOH C 648      -2.337  89.572  26.197  1.00 37.28           O  
HETATM 8112  O   HOH C 649     -27.277 104.418  63.929  1.00 50.58           O  
HETATM 8113  O   HOH C 650      17.983  98.278  38.565  1.00 45.87           O  
HETATM 8114  O   HOH C 651      12.920  97.413  33.307  1.00 45.13           O  
HETATM 8115  O   HOH C 652      11.517  97.540  31.299  1.00 44.00           O  
HETATM 8116  O   HOH C 653      11.924 105.761  36.516  1.00 54.97           O  
HETATM 8117  O   HOH C 654     -25.209  87.255  66.093  1.00 38.46           O  
HETATM 8118  O   HOH C 655       8.513 100.864  51.669  1.00 23.21           O  
HETATM 8119  O   HOH C 656       6.533 118.922  55.107  1.00 47.50           O  
HETATM 8120  O   HOH C 657     -15.084 105.533  41.710  1.00 49.94           O  
HETATM 8121  O   HOH C 658       3.821  96.790  49.354  1.00 33.57           O  
HETATM 8122  O   HOH C 659       2.991  69.571  38.078  1.00 27.75           O  
HETATM 8123  O   HOH C 660       1.578  94.734  25.288  1.00 48.05           O  
HETATM 8124  O   HOH C 661     -22.798 109.138  51.959  1.00 57.11           O  
HETATM 8125  O   HOH C 662       7.229  78.519  28.553  1.00 30.71           O  
HETATM 8126  O   HOH C 663      -4.902  98.945  32.208  1.00 40.57           O  
HETATM 8127  O   HOH C 664     -10.027  96.212  76.935  1.00 43.44           O  
HETATM 8128  O   HOH C 665     -10.413 105.953  40.695  1.00 42.75           O  
HETATM 8129  O   HOH C 666      10.690 108.201  37.565  1.00 40.07           O  
HETATM 8130  O   HOH C 667      18.578  95.708  32.884  1.00 59.56           O  
HETATM 8131  O   HOH C 668       2.438 115.744  45.126  1.00 55.26           O  
HETATM 8132  O   HOH C 669      -2.374  77.771  43.735  1.00 51.93           O  
HETATM 8133  O   HOH C 670      13.450 101.188  54.604  1.00 52.20           O  
HETATM 8134  O   HOH C 671      -4.571 123.286  48.769  1.00 37.02           O  
HETATM 8135  O   HOH C 672       7.254  83.898  23.958  1.00 61.68           O  
HETATM 8136  O   HOH C 673     -25.870  83.465  62.271  1.00 67.30           O  
HETATM 8137  O   HOH C 674       5.225  90.670  50.171  1.00 53.11           O  
HETATM 8138  O   HOH C 675       0.276 109.766  74.737  1.00 45.57           O  
HETATM 8139  O   HOH C 676     -26.948  91.644  53.860  1.00 62.91           O  
HETATM 8140  O   HOH C 677      -0.622 115.194  35.790  1.00 26.28           O  
HETATM 8141  O   HOH C 678      -7.329 119.333  47.303  1.00 42.75           O  
HETATM 8142  O   HOH C 679     -10.357 121.654  68.545  1.00 54.92           O  
HETATM 8143  O   HOH C 680     -17.949 114.043  76.992  1.00 54.90           O  
HETATM 8144  O   HOH C 681     -17.917 115.595  54.502  1.00 44.35           O  
HETATM 8145  O   HOH C 682     -15.642  83.961  52.718  1.00 57.54           O  
HETATM 8146  O   HOH C 683       3.102  91.537  23.912  1.00 62.15           O  
HETATM 8147  O   HOH C 684      -6.768 125.471  49.424  1.00 52.60           O  
HETATM 8148  O   HOH C 685      -0.600  88.645  61.366  1.00 60.69           O  
HETATM 8149  O   HOH C 686      10.549 102.494  41.841  1.00 52.16           O  
HETATM 8150  O   HOH C 687     -13.027 125.055  58.523  1.00 59.75           O  
HETATM 8151  O   HOH C 688     -23.342  95.173  65.251  1.00 71.00           O  
HETATM 8152  O   HOH C 689       2.489 118.665  63.359  1.00 54.98           O  
HETATM 8153  O   HOH C 690      -9.219 107.555  30.117  1.00 56.10           O  
HETATM 8154  O   HOH C 691      -8.554 111.876  77.195  1.00 58.80           O  
HETATM 8155  O   HOH C 692     -26.031  99.925  52.886  1.00 61.93           O  
HETATM 8156  O   HOH C 693      11.837 107.682  44.844  1.00 53.75           O  
HETATM 8157  O   HOH C 694      -6.320  80.020  27.924  1.00 56.77           O  
HETATM 8158  O   HOH C 695      20.020  96.009  36.010  1.00 62.08           O  
HETATM 8159  O   HOH C 696       5.021  81.368  45.446  1.00 35.16           O  
HETATM 8160  O   HOH C 697      12.597  81.853  42.890  1.00 42.58           O  
HETATM 8161  O   HOH C 698      11.173  75.362  45.850  1.00 53.21           O  
HETATM 8162  O   HOH C 699      -8.007  83.830  45.617  1.00 52.44           O  
HETATM 8163  O   HOH C 700     -24.053  99.862  51.098  1.00 58.26           O  
HETATM 8164  O   HOH C 701     -11.987  92.055  32.060  1.00 60.52           O  
HETATM 8165  O   HOH C 702     -15.494 118.455  53.915  1.00 49.68           O  
HETATM 8166  O   HOH C 703     -19.251 121.482  63.457  1.00 59.46           O  
HETATM 8167  O   HOH C 704      12.039  99.636  28.885  1.00 48.13           O  
HETATM 8168  O   HOH C 705       6.409 112.481  34.084  1.00 53.90           O  
HETATM 8169  O   HOH C 706       7.464  98.264  51.770  1.00 43.20           O  
HETATM 8170  O   HOH C 707     -11.621 103.264  37.427  1.00 49.57           O  
HETATM 8171  O   HOH C 708       7.046  96.466  56.414  1.00 40.47           O  
HETATM 8172  O   HOH C 709     -22.443 116.652  75.121  1.00 57.09           O  
HETATM 8173  O   HOH C 710     -15.331  91.631  58.228  1.00 60.50           O  
HETATM 8174  O   HOH C 711      12.061  89.367  43.038  1.00 43.18           O  
HETATM 8175  O   HOH C 712      12.868 107.446  33.010  1.00 53.08           O  
HETATM 8176  O   HOH C 713     -22.361 114.283  45.911  1.00 50.72           O  
HETATM 8177  O   HOH C 714      10.134 115.826  53.712  1.00 57.01           O  
HETATM 8178  O   HOH C 715       1.697 115.486  39.428  1.00 47.88           O  
HETATM 8179  O   HOH C 716      11.054 110.920  34.243  1.00 52.65           O  
HETATM 8180  O   HOH C 717       7.734  95.170  61.263  1.00 24.53           O  
HETATM 8181  O   HOH C 718     -17.404 107.549  75.017  1.00 36.49           O  
HETATM 8182  O   HOH C 719      12.934 103.091  48.960  1.00 64.04           O  
HETATM 8183  O   HOH C 720      21.820  89.296  35.573  1.00 47.17           O  
HETATM 8184  O   HOH C 721      -1.437 117.262  40.930  1.00 62.46           O  
HETATM 8185  O   HOH C 722     -11.257 113.138  33.701  1.00 53.42           O  
HETATM 8186  O   HOH C 723      10.928 117.714  59.320  1.00 50.11           O  
HETATM 8187  O   HOH C 724     -28.083 107.777  73.144  1.00 57.52           O  
HETATM 8188  O   HOH C 725      -5.389 102.598  27.774  1.00 53.93           O  
HETATM 8189  O   HOH C 726      -7.092 101.503  30.668  1.00 57.82           O  
HETATM 8190  O   HOH C 727       3.456 122.769  52.865  1.00 44.27           O  
HETATM 8191  O   HOH C 728      -5.976  89.844  59.905  1.00 63.05           O  
HETATM 8192  O   HOH C 729      12.506 115.211  52.753  1.00 59.39           O  
HETATM 8193  O   HOH C 730     -11.264  85.252  55.504  1.00 49.09           O  
HETATM 8194  O   HOH C 731       5.735  93.518  58.930  1.00 51.91           O  
HETATM 8195  O   HOH C 732     -34.979  89.713  56.089  1.00 57.35           O  



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.