 |
| home | start a new run | job status | references&downloads | examples | help |
Should you encounter any unexpected behaviour, |
*** rhamnosidase_6gsz_2 ***elNémo ID: 2606190905412989214Job options:ID = 2606190905412989214 JOBID = rhamnosidase_6gsz_2 USERID = Mina 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:HEADER rhamnosidase_6gsz_2 CRYST1 90.260 106.248 119.832 90.00 90.00 90.00 P 21 21 21 0 ATOM 1 N ALA A 2 68.209 16.859 46.196 1.00 53.12 A N ANISOU 1 N ALA A 2 5874 5746 8562 991 -1465 -1348 A N ATOM 2 CA ALA A 2 67.087 17.819 46.192 1.00 41.10 A C ANISOU 2 CA ALA A 2 2399 6115 7100 -827 -1515 -821 A C ATOM 3 C ALA A 2 65.939 17.264 45.345 1.00 28.20 A C ANISOU 3 C ALA A 2 3377 3522 3816 -199 -1136 -558 A C ATOM 4 O ALA A 2 64.795 17.548 45.704 1.00 30.28 A O ANISOU 4 O ALA A 2 3568 3284 4650 -560 -56 -577 A O ATOM 5 CB ALA A 2 67.519 19.209 45.735 1.00 46.82 A C ANISOU 5 CB ALA A 2 3671 6097 8018 -1234 -485 -1035 A C ATOM 6 N LEU A 3 66.209 16.517 44.249 1.00 27.68 A N ANISOU 6 N LEU A 3 2424 3015 5075 -962 -540 -1033 A N ATOM 7 CA LEU A 3 65.101 15.993 43.442 1.00 22.22 A C ANISOU 7 CA LEU A 3 2251 2735 3454 -444 -352 -474 A C ATOM 8 C LEU A 3 65.493 14.798 42.570 1.00 20.09 A C ANISOU 8 C LEU A 3 2282 2130 3220 -652 -177 -76 A C ATOM 9 O LEU A 3 66.377 14.881 41.716 1.00 23.25 A O ANISOU 9 O LEU A 3 2272 2593 3969 -416 107 -252 A O ATOM 10 CB LEU A 3 64.565 17.090 42.531 1.00 24.13 A C ANISOU 10 CB LEU A 3 3029 2696 3442 -407 154 -188 A C ATOM 11 CG LEU A 3 63.345 16.682 41.710 1.00 25.27 A C ANISOU 11 CG LEU A 3 3758 2921 2919 161 -132 -775 A C ATOM 12 CD1 LEU A 3 62.162 16.372 42.608 1.00 27.12 A C ANISOU 12 CD1 LEU A 3 3240 2700 4363 -397 -211 -1022 A C ATOM 13 CD2 LEU A 3 63.007 17.769 40.720 1.00 32.19 A C ANISOU 13 CD2 LEU A 3 4762 3579 3887 957 -596 -316 A C ATOM 14 N SER A 4 64.729 13.708 42.713 1.00 17.37 A N ANISOU 14 N SER A 4 1855 2040 2703 -535 -376 -85 A N ATOM 15 CA SER A 4 64.910 12.528 41.882 1.00 18.34 A C ANISOU 15 CA SER A 4 1761 2335 2871 -346 -149 -165 A C ATOM 16 C SER A 4 63.572 11.830 41.643 1.00 16.22 A C ANISOU 16 C SER A 4 1660 1947 2554 -175 -131 -43 A C ATOM 17 O SER A 4 62.575 12.091 42.348 1.00 16.84 A O ANISOU 17 O SER A 4 1729 1970 2698 -334 -109 -371 A O ATOM 18 CB SER A 4 65.896 11.547 42.481 1.00 21.85 A C ANISOU 18 CB SER A 4 2160 2429 3711 -295 -536 -68 A C ATOM 19 OG SER A 4 65.399 10.977 43.679 1.00 25.59 A O ANISOU 19 OG SER A 4 3180 3070 3471 337 -995 338 A O ATOM 20 N ILE A 5 63.594 10.897 40.700 1.00 16.95 A N ANISOU 20 N ILE A 5 1538 2126 2776 -234 201 -327 A N ATOM 21 CA ILE A 5 62.453 9.999 40.474 1.00 16.52 A C ANISOU 21 CA ILE A 5 1569 1992 2715 -208 111 -41 A C ATOM 22 C ILE A 5 62.684 8.706 41.267 1.00 17.30 A C ANISOU 22 C ILE A 5 1963 2020 2589 -94 29 -59 A C ATOM 23 O ILE A 5 63.706 8.049 41.078 1.00 19.14 A O ANISOU 23 O ILE A 5 1960 2197 3114 55 -285 -124 A O ATOM 24 CB ILE A 5 62.233 9.721 38.974 1.00 16.59 A C ANISOU 24 CB ILE A 5 1565 1999 2736 -312 120 -274 A C ATOM 25 CG1 ILE A 5 61.715 10.988 38.280 1.00 18.51 A C ANISOU 25 CG1 ILE A 5 2193 2072 2768 -218 458 -96 A C ATOM 26 CG2 ILE A 5 61.284 8.546 38.777 1.00 16.76 A C ANISOU 26 CG2 ILE A 5 1528 1851 2988 -137 -182 -450 A C ATOM 27 CD1 ILE A 5 61.681 10.913 36.771 1.00 21.03 A C ANISOU 27 CD1 ILE A 5 2351 2619 3019 -222 476 0 A C ATOM 28 N SER A 6 61.730 8.388 42.150 1.00 16.89 A N ANISOU 28 N SER A 6 1776 2013 2625 -105 -92 7 A N ATOM 29 CA SER A 6 61.847 7.255 43.053 1.00 19.37 A C ANISOU 29 CA SER A 6 2414 2319 2625 24 -614 133 A C ATOM 30 C SER A 6 61.198 5.987 42.503 1.00 18.13 A C ANISOU 30 C SER A 6 2377 1999 2512 390 -491 45 A C ATOM 31 O SER A 6 61.539 4.922 42.985 1.00 23.62 A O ANISOU 31 O SER A 6 3528 2403 3040 505 -1155 479 A O ATOM 32 CB SER A 6 61.269 7.556 44.397 1.00 22.80 A C ANISOU 32 CB SER A 6 3234 2669 2757 -310 -566 -253 A C ATOM 33 OG SER A 6 59.932 7.982 44.291 1.00 26.79 A O ANISOU 33 OG SER A 6 3199 3257 3721 -28 135 -280 A O ATOM 34 N GLN A 7 60.236 6.109 41.581 1.00 17.70 A N ANISOU 34 N GLN A 7 2075 1803 2845 -78 -532 25 A N ATOM 35 CA GLN A 7 59.445 4.951 41.144 1.00 16.41 A C ANISOU 35 CA GLN A 7 2408 1503 2324 134 -316 -41 A C ATOM 36 C GLN A 7 58.927 5.309 39.765 1.00 14.91 A C ANISOU 36 C GLN A 7 1792 1706 2167 384 -215 -184 A C ATOM 37 O GLN A 7 58.484 6.435 39.569 1.00 18.14 A O ANISOU 37 O GLN A 7 2367 1647 2877 436 -426 189 A O ATOM 38 CB GLN A 7 58.222 4.709 42.065 1.00 19.38 A C ANISOU 38 CB GLN A 7 3189 1868 2306 -205 200 106 A C ATOM 39 CG GLN A 7 57.324 3.553 41.607 1.00 21.21 A C ANISOU 39 CG GLN A 7 2820 2049 3191 -219 371 211 A C ATOM 40 CD GLN A 7 55.977 3.393 42.285 1.00 25.74 A C ANISOU 40 CD GLN A 7 2542 3208 4029 -60 329 784 A C ATOM 41 NE2 GLN A 7 55.042 4.294 42.005 1.00 21.43 A N ANISOU 41 NE2 GLN A 7 2859 2483 2800 151 527 0 A N ATOM 42 OE1 GLN A 7 55.750 2.425 43.018 1.00 39.41 A O ANISOU 42 OE1 GLN A 7 4848 3741 6384 -344 374 1903 A O ATOM 43 N VAL A 8 59.034 4.378 38.833 1.00 14.04 A N ANISOU 43 N VAL A 8 1652 1329 2351 183 -75 -113 A N ATOM 44 CA VAL A 8 58.407 4.442 37.532 1.00 13.53 A C ANISOU 44 CA VAL A 8 1672 1267 2201 -271 -43 41 A C ATOM 45 C VAL A 8 57.497 3.224 37.439 1.00 14.66 A C ANISOU 45 C VAL A 8 1588 1180 2802 -157 -218 163 A C ATOM 46 O VAL A 8 57.983 2.080 37.648 1.00 16.28 A O ANISOU 46 O VAL A 8 1857 1386 2943 85 -170 347 A O ATOM 47 CB VAL A 8 59.422 4.461 36.375 1.00 13.70 A C ANISOU 47 CB VAL A 8 1854 1095 2254 -37 22 -69 A C ATOM 48 CG1 VAL A 8 58.703 4.436 35.053 1.00 13.75 A C ANISOU 48 CG1 VAL A 8 1841 1086 2296 -146 187 120 A C ATOM 49 CG2 VAL A 8 60.299 5.703 36.458 1.00 15.41 A C ANISOU 49 CG2 VAL A 8 1835 1285 2735 -121 -22 125 A C ATOM 50 N ALA A 9 56.199 3.455 37.170 1.00 12.37 A N ANISOU 50 N ALA A 9 1591 841 2269 -213 -387 56 A N ATOM 51 CA ALA A 9 55.248 2.390 37.176 1.00 11.85 A C ANISOU 51 CA ALA A 9 1602 934 1964 -245 -80 -15 A C ATOM 52 C ALA A 9 54.273 2.496 36.001 1.00 10.50 A C ANISOU 52 C ALA A 9 1213 837 1938 -95 41 206 A C ATOM 53 O ALA A 9 53.991 3.593 35.471 1.00 11.58 A O ANISOU 53 O ALA A 9 1608 781 2010 28 49 162 A O ATOM 54 CB ALA A 9 54.531 2.360 38.481 1.00 15.90 A C ANISOU 54 CB ALA A 9 2412 1930 1696 -647 -166 -13 A C ATOM 55 N PHE A 10 53.724 1.343 35.606 1.00 11.36 A N ANISOU 55 N PHE A 10 1577 964 1774 -121 7 -42 A N ATOM 56 CA PHE A 10 52.819 1.217 34.501 1.00 9.86 A C ANISOU 56 CA PHE A 10 1361 689 1697 103 99 112 A C ATOM 57 C PHE A 10 51.408 0.915 35.005 1.00 11.46 A C ANISOU 57 C PHE A 10 1410 978 1965 -8 116 299 A C ATOM 58 O PHE A 10 51.217 0.002 35.838 1.00 11.34 A O ANISOU 58 O PHE A 10 1750 738 1819 6 213 142 A O ATOM 59 CB PHE A 10 53.327 0.112 33.592 1.00 10.22 A C ANISOU 59 CB PHE A 10 1453 758 1672 90 1 52 A C ATOM 60 CG PHE A 10 54.722 0.391 33.107 1.00 11.84 A C ANISOU 60 CG PHE A 10 1568 1133 1795 -72 155 32 A C ATOM 61 CD1 PHE A 10 54.956 1.301 32.085 1.00 12.05 A C ANISOU 61 CD1 PHE A 10 1533 986 2059 81 -48 160 A C ATOM 62 CD2 PHE A 10 55.812 -0.133 33.782 1.00 12.24 A C ANISOU 62 CD2 PHE A 10 1594 849 2204 101 218 -41 A C ATOM 63 CE1 PHE A 10 56.245 1.645 31.726 1.00 13.22 A C ANISOU 63 CE1 PHE A 10 1732 1305 1986 -80 174 184 A C ATOM 64 CE2 PHE A 10 57.102 0.181 33.391 1.00 12.72 A C ANISOU 64 CE2 PHE A 10 1545 967 2320 94 44 130 A C ATOM 65 CZ PHE A 10 57.328 1.087 32.375 1.00 13.54 A C ANISOU 65 CZ PHE A 10 1684 1147 2310 -13 254 204 A C ATOM 66 N GLU A 11 50.410 1.663 34.496 1.00 11.50 A N ANISOU 66 N GLU A 11 1632 661 2074 -18 60 33 A N ATOM 67 CA GLU A 11 49.038 1.568 35.015 1.00 10.27 A C ANISOU 67 CA GLU A 11 1589 602 1712 -27 49 44 A C ATOM 68 C GLU A 11 49.117 1.652 36.540 1.00 10.59 A C ANISOU 68 C GLU A 11 1343 1030 1649 -194 133 -65 A C ATOM 69 O GLU A 11 49.754 2.550 37.091 1.00 11.50 A O ANISOU 69 O GLU A 11 1587 739 2042 -95 126 -132 A O ATOM 70 CB GLU A 11 48.320 0.340 34.435 1.00 10.19 A C ANISOU 70 CB GLU A 11 1590 673 1609 11 101 -45 A C ATOM 71 CG GLU A 11 48.199 0.420 32.916 1.00 10.71 A C ANISOU 71 CG GLU A 11 1589 842 1636 32 27 -113 A C ATOM 72 CD GLU A 11 47.163 1.407 32.382 1.00 11.10 A C ANISOU 72 CD GLU A 11 1702 1067 1449 147 235 64 A C ATOM 73 OE1 GLU A 11 46.052 1.416 32.963 1.00 11.75 A O ANISOU 73 OE1 GLU A 11 1637 978 1849 1 250 193 A O ATOM 74 OE2 GLU A 11 47.468 2.121 31.386 1.00 11.42 A O ANISOU 74 OE2 GLU A 11 1583 1109 1648 -84 66 242 A O ATOM 75 N HIS A 12 48.454 0.706 37.228 1.00 9.54 A N ANISOU 75 N HIS A 12 1426 686 1510 -187 74 -123 A N ATOM 76 CA HIS A 12 48.472 0.600 38.670 1.00 10.65 A C ANISOU 76 CA HIS A 12 1717 776 1554 -75 164 -58 A C ATOM 77 C HIS A 12 49.245 -0.646 39.133 1.00 12.23 A C ANISOU 77 C HIS A 12 1575 1037 2033 -24 92 107 A C ATOM 78 O HIS A 12 49.180 -1.024 40.327 1.00 13.28 A O ANISOU 78 O HIS A 12 1803 1199 2042 193 -37 36 A O ATOM 79 CB HIS A 12 47.070 0.644 39.261 1.00 10.77 A C ANISOU 79 CB HIS A 12 1514 808 1770 -266 22 102 A C ATOM 80 CG HIS A 12 46.392 1.936 38.946 1.00 11.23 A C ANISOU 80 CG HIS A 12 1606 852 1808 -113 254 86 A C ATOM 81 CD2 HIS A 12 45.487 2.210 37.994 1.00 10.42 A C ANISOU 81 CD2 HIS A 12 1551 609 1797 -129 197 -166 A C ATOM 82 ND1 HIS A 12 46.699 3.144 39.580 1.00 11.30 A N ANISOU 82 ND1 HIS A 12 1538 1070 1684 -85 5 -29 A N ATOM 83 CE1 HIS A 12 45.960 4.084 39.026 1.00 12.71 A C ANISOU 83 CE1 HIS A 12 1450 1539 1837 114 -9 50 A C ATOM 84 NE2 HIS A 12 45.245 3.567 38.038 1.00 11.25 A N ANISOU 84 NE2 HIS A 12 1652 667 1955 24 174 33 A N ATOM 85 N HIS A 13 50.089 -1.153 38.242 1.00 11.32 A N ANISOU 85 N HIS A 13 1674 775 1851 -65 144 343 A N ATOM 86 CA HIS A 13 50.901 -2.328 38.564 1.00 11.67 A C ANISOU 86 CA HIS A 13 1728 856 1848 21 -11 216 A C ATOM 87 C HIS A 13 52.119 -1.933 39.402 1.00 12.98 A C ANISOU 87 C HIS A 13 1711 1214 2004 -18 -55 98 A C ATOM 88 O HIS A 13 52.768 -0.913 39.116 1.00 13.75 A O ANISOU 88 O HIS A 13 1781 1113 2327 -97 -24 6 A O ATOM 89 CB HIS A 13 51.420 -2.960 37.283 1.00 12.06 A C ANISOU 89 CB HIS A 13 1951 678 1951 -176 88 217 A C ATOM 90 CG HIS A 13 50.386 -3.334 36.266 1.00 11.02 A C ANISOU 90 CG HIS A 13 1913 388 1886 -131 16 86 A C ATOM 91 CD2 HIS A 13 50.152 -2.885 35.019 1.00 12.06 A C ANISOU 91 CD2 HIS A 13 1624 1040 1917 -74 191 181 A C ATOM 92 ND1 HIS A 13 49.502 -4.395 36.457 1.00 11.88 A N ANISOU 92 ND1 HIS A 13 1749 704 2060 -238 -101 179 A N ATOM 93 CE1 HIS A 13 48.752 -4.500 35.360 1.00 10.71 A C ANISOU 93 CE1 HIS A 13 1539 815 1714 13 89 2 A C ATOM 94 NE2 HIS A 13 49.115 -3.560 34.473 1.00 12.43 A N ANISOU 94 NE2 HIS A 13 1507 1236 1981 -28 207 170 A N ATOM 95 N ARG A 14 52.495 -2.738 40.390 1.00 12.01 A N ANISOU 95 N ARG A 14 1682 998 1884 8 49 -27 A N ATOM 96 CA ARG A 14 53.722 -2.497 41.137 1.00 13.47 A C ANISOU 96 CA ARG A 14 1862 1345 1912 45 -76 -105 A C ATOM 97 C ARG A 14 54.943 -2.823 40.258 1.00 15.65 A C ANISOU 97 C ARG A 14 2047 1871 2028 5 152 -103 A C ATOM 98 O ARG A 14 55.980 -2.151 40.318 1.00 19.33 A O ANISOU 98 O ARG A 14 1858 2764 2721 -6 101 -174 A O ATOM 99 CB ARG A 14 53.780 -3.294 42.446 1.00 15.62 A C ANISOU 99 CB ARG A 14 2224 1585 2124 153 145 112 A C ATOM 100 CG ARG A 14 52.682 -2.964 43.446 1.00 17.43 A C ANISOU 100 CG ARG A 14 2330 2162 2129 185 28 11 A C ATOM 101 CD ARG A 14 52.939 -3.439 44.874 1.00 18.23 A C ANISOU 101 CD ARG A 14 2393 2720 1811 133 56 -364 A C ATOM 102 NE ARG A 14 54.106 -2.758 45.446 1.00 18.08 A N ANISOU 102 NE ARG A 14 2590 1613 2667 -69 -84 -57 A N ATOM 103 CZ ARG A 14 54.665 -3.047 46.616 1.00 15.87 A C ANISOU 103 CZ ARG A 14 1975 1913 2140 154 144 -371 A C ATOM 104 NH1 ARG A 14 54.147 -4.021 47.368 1.00 16.84 A N ANISOU 104 NH1 ARG A 14 1834 1893 2671 -13 -189 -52 A N ATOM 105 NH2 ARG A 14 55.727 -2.358 47.040 1.00 20.52 A N ANISOU 105 NH2 ARG A 14 2235 2749 2813 -140 -23 -696 A N ATOM 106 N THR A 15 54.828 -3.938 39.539 1.00 15.19 A N ANISOU 106 N THR A 15 2041 1528 2201 118 50 42 A N ATOM 107 CA THR A 15 55.765 -4.411 38.535 1.00 17.56 A C ANISOU 107 CA THR A 15 2371 2326 1972 370 -41 -269 A C ATOM 108 C THR A 15 54.945 -4.858 37.324 1.00 13.76 A C ANISOU 108 C THR A 15 1998 1247 1981 297 143 -59 A C ATOM 109 O THR A 15 53.780 -5.181 37.467 1.00 15.76 A O ANISOU 109 O THR A 15 1939 1570 2478 252 110 -167 A O ATOM 110 CB THR A 15 56.633 -5.580 39.034 1.00 20.54 A C ANISOU 110 CB THR A 15 2236 2730 2836 866 -123 -726 A C ATOM 111 CG2 THR A 15 57.361 -5.275 40.319 1.00 26.71 A C ANISOU 111 CG2 THR A 15 2750 4372 3026 1354 -585 -495 A C ATOM 112 OG1 THR A 15 55.822 -6.736 39.220 1.00 23.71 A O ANISOU 112 OG1 THR A 15 3048 3105 2856 764 137 -47 A O ATOM 113 N ALA A 16 55.568 -4.874 36.144 1.00 12.35 A N ANISOU 113 N ALA A 16 1789 840 2062 242 205 9 A N ATOM 114 CA ALA A 16 54.809 -5.006 34.906 1.00 11.70 A C ANISOU 114 CA ALA A 16 1583 844 2018 83 168 105 A C ATOM 115 C ALA A 16 55.341 -6.151 34.041 1.00 12.93 A C ANISOU 115 C ALA A 16 1936 952 2022 34 212 8 A C ATOM 116 O ALA A 16 55.885 -5.968 32.971 1.00 14.22 A O ANISOU 116 O ALA A 16 2481 946 1974 188 329 69 A O ATOM 117 CB ALA A 16 54.754 -3.663 34.202 1.00 12.83 A C ANISOU 117 CB ALA A 16 1770 1006 2095 -36 -9 228 A C ATOM 118 N LEU A 17 55.134 -7.378 34.519 1.00 11.74 A N ANISOU 118 N LEU A 17 1750 1183 1525 -137 103 132 A N ATOM 119 CA LEU A 17 55.463 -8.610 33.770 1.00 12.99 A C ANISOU 119 CA LEU A 17 1842 1416 1678 -143 -56 -147 A C ATOM 120 C LEU A 17 54.157 -9.361 33.474 1.00 10.67 A C ANISOU 120 C LEU A 17 1611 742 1701 210 99 18 A C ATOM 121 O LEU A 17 53.466 -9.802 34.407 1.00 13.01 A O ANISOU 121 O LEU A 17 1728 1271 1942 12 342 -78 A O ATOM 122 CB LEU A 17 56.465 -9.452 34.562 1.00 13.47 A C ANISOU 122 CB LEU A 17 1687 1077 2352 -124 62 -148 A C ATOM 123 CG LEU A 17 56.730 -10.831 33.951 1.00 13.90 A C ANISOU 123 CG LEU A 17 1753 987 2539 -202 58 -2 A C ATOM 124 CD1 LEU A 17 57.312 -10.706 32.551 1.00 15.93 A C ANISOU 124 CD1 LEU A 17 2359 1136 2557 218 97 -35 A C ATOM 125 CD2 LEU A 17 57.626 -11.677 34.848 1.00 17.17 A C ANISOU 125 CD2 LEU A 17 2280 1387 2856 72 114 307 A C ATOM 126 N GLY A 18 53.852 -9.514 32.187 1.00 10.81 A N ANISOU 126 N GLY A 18 1519 883 1704 80 126 43 A N ATOM 127 CA GLY A 18 52.700 -10.268 31.757 1.00 12.52 A C ANISOU 127 CA GLY A 18 1747 1064 1943 -196 232 -25 A C ATOM 128 C GLY A 18 51.391 -9.502 31.803 1.00 13.03 A C ANISOU 128 C GLY A 18 1823 1083 2042 -134 132 -229 A C ATOM 129 O GLY A 18 50.305 -10.071 31.958 1.00 12.83 A O ANISOU 129 O GLY A 18 1815 862 2197 78 -18 68 A O ATOM 130 N ILE A 19 51.492 -8.172 31.615 1.00 11.82 A N ANISOU 130 N ILE A 19 1625 1115 1752 -30 210 144 A N ATOM 131 CA ILE A 19 50.352 -7.276 31.738 1.00 11.10 A C ANISOU 131 CA ILE A 19 1599 937 1679 -106 176 14 A C ATOM 132 C ILE A 19 49.426 -7.386 30.516 1.00 10.44 A C ANISOU 132 C ILE A 19 1475 791 1701 -129 171 192 A C ATOM 133 O ILE A 19 49.768 -7.909 29.447 1.00 12.24 A O ANISOU 133 O ILE A 19 1727 1049 1873 -82 174 -27 A O ATOM 134 CB ILE A 19 50.796 -5.826 32.004 1.00 11.06 A C ANISOU 134 CB ILE A 19 1533 834 1834 42 149 -11 A C ATOM 135 CG1 ILE A 19 51.522 -5.207 30.820 1.00 11.79 A C ANISOU 135 CG1 ILE A 19 1847 753 1881 18 226 49 A C ATOM 136 CG2 ILE A 19 51.641 -5.770 33.274 1.00 11.97 A C ANISOU 136 CG2 ILE A 19 1849 732 1967 -18 79 55 A C ATOM 137 CD1 ILE A 19 51.719 -3.707 30.926 1.00 12.46 A C ANISOU 137 CD1 ILE A 19 1698 845 2189 -97 -111 -77 A C ATOM 138 N GLY A 20 48.239 -6.804 30.662 1.00 10.66 A N ANISOU 138 N GLY A 20 1553 770 1726 -98 182 -48 A N ATOM 139 CA GLY A 20 47.219 -6.830 29.632 1.00 11.32 A C ANISOU 139 CA GLY A 20 1468 873 1960 169 44 34 A C ATOM 140 C GLY A 20 47.274 -5.665 28.652 1.00 12.66 A C ANISOU 140 C GLY A 20 1674 1323 1812 -33 92 163 A C ATOM 141 O GLY A 20 46.612 -5.687 27.629 1.00 15.64 A O ANISOU 141 O GLY A 20 2554 1146 2242 -168 -314 214 A O ATOM 142 N GLU A 21 48.037 -4.632 28.970 1.00 11.66 A N ANISOU 142 N GLU A 21 1731 1325 1371 -111 -32 239 A N ATOM 143 CA GLU A 21 48.065 -3.380 28.178 1.00 12.56 A C ANISOU 143 CA GLU A 21 1924 1066 1780 -52 -28 182 A C ATOM 144 C GLU A 21 49.219 -3.436 27.171 1.00 12.21 A C ANISOU 144 C GLU A 21 1991 828 1818 -166 1 23 A C ATOM 145 O GLU A 21 50.347 -3.728 27.538 1.00 14.98 A O ANISOU 145 O GLU A 21 1886 1671 2134 5 229 237 A O ATOM 146 CB GLU A 21 48.255 -2.146 29.067 1.00 13.02 A C ANISOU 146 CB GLU A 21 1812 1142 1989 -42 146 46 A C ATOM 147 CG GLU A 21 47.130 -1.961 30.052 1.00 13.01 A C ANISOU 147 CG GLU A 21 2041 1120 1780 98 147 302 A C ATOM 148 CD GLU A 21 47.236 -2.742 31.364 1.00 12.05 A C ANISOU 148 CD GLU A 21 2020 766 1789 -134 91 142 A C ATOM 149 OE1 GLU A 21 48.377 -3.141 31.734 1.00 14.66 A O ANISOU 149 OE1 GLU A 21 2042 1308 2218 -60 -23 154 A O ATOM 150 OE2 GLU A 21 46.185 -2.835 32.045 1.00 15.09 A O ANISOU 150 OE2 GLU A 21 1988 1519 2227 -113 244 178 A O ATOM 151 N THR A 22 48.939 -3.091 25.920 1.00 13.50 A N ANISOU 151 N THR A 22 2291 1165 1672 -154 135 45 A N ATOM 152 CA THR A 22 49.999 -2.930 24.907 1.00 13.88 A C ANISOU 152 CA THR A 22 2505 1005 1763 81 270 192 A C ATOM 153 C THR A 22 50.454 -1.466 24.831 1.00 13.08 A C ANISOU 153 C THR A 22 2388 1033 1549 97 438 87 A C ATOM 154 O THR A 22 51.545 -1.206 24.279 1.00 14.83 A O ANISOU 154 O THR A 22 2322 1322 1988 -31 372 4 A O ATOM 155 CB THR A 22 49.499 -3.346 23.530 1.00 14.78 A C ANISOU 155 CB THR A 22 2493 1151 1969 -440 218 134 A C ATOM 156 CG2 THR A 22 49.130 -4.807 23.513 1.00 16.48 A C ANISOU 156 CG2 THR A 22 2802 1190 2267 -579 325 -47 A C ATOM 157 OG1 THR A 22 48.389 -2.535 23.157 1.00 17.18 A O ANISOU 157 OG1 THR A 22 2595 1981 1949 -222 145 65 A O ATOM 158 N GLN A 23 49.660 -0.544 25.402 1.00 11.58 A N ANISOU 158 N GLN A 23 1843 824 1733 -183 382 25 A N ATOM 159 CA GLN A 23 50.010 0.899 25.450 1.00 11.75 A C ANISOU 159 CA GLN A 23 1983 884 1596 -352 253 181 A C ATOM 160 C GLN A 23 49.853 1.337 26.906 1.00 10.94 A C ANISOU 160 C GLN A 23 1520 1017 1617 -13 195 68 A C ATOM 161 O GLN A 23 49.022 2.198 27.229 1.00 12.66 A O ANISOU 161 O GLN A 23 1860 1014 1933 176 193 172 A O ATOM 162 CB GLN A 23 49.139 1.710 24.485 1.00 14.44 A C ANISOU 162 CB GLN A 23 2308 1351 1828 -103 95 100 A C ATOM 163 CG GLN A 23 49.291 1.293 23.030 1.00 16.19 A C ANISOU 163 CG GLN A 23 2735 1623 1792 -96 -73 26 A C ATOM 164 CD GLN A 23 48.338 2.014 22.115 1.00 22.59 A C ANISOU 164 CD GLN A 23 3407 2483 2690 211 -399 351 A C ATOM 165 NE2 GLN A 23 47.172 1.466 21.943 1.00 30.90 A N ANISOU 165 NE2 GLN A 23 4026 3812 3901 -221 -1596 938 A N ATOM 166 OE1 GLN A 23 48.625 3.092 21.640 1.00 37.16 A O ANISOU 166 OE1 GLN A 23 5991 3588 4539 -127 -759 1836 A O ATOM 167 N PRO A 24 50.633 0.778 27.850 1.00 11.02 A N ANISOU 167 N PRO A 24 1666 831 1689 8 74 -62 A N ATOM 168 CA PRO A 24 50.436 1.065 29.273 1.00 10.44 A C ANISOU 168 CA PRO A 24 1641 709 1616 -81 53 203 A C ATOM 169 C PRO A 24 50.788 2.519 29.580 1.00 11.03 A C ANISOU 169 C PRO A 24 1660 846 1684 -160 248 -64 A C ATOM 170 O PRO A 24 51.834 3.023 29.112 1.00 12.04 A O ANISOU 170 O PRO A 24 1858 759 1955 -22 463 119 A O ATOM 171 CB PRO A 24 51.411 0.111 29.970 1.00 11.34 A C ANISOU 171 CB PRO A 24 1922 813 1572 -94 -94 177 A C ATOM 172 CG PRO A 24 52.471 -0.128 28.946 1.00 11.91 A C ANISOU 172 CG PRO A 24 1754 649 2121 77 33 -17 A C ATOM 173 CD PRO A 24 51.718 -0.192 27.628 1.00 12.71 A C ANISOU 173 CD PRO A 24 1886 812 2130 110 25 -171 A C ATOM 174 N ARG A 25 49.963 3.161 30.417 1.00 10.17 A N ANISOU 174 N ARG A 25 1528 544 1791 -249 308 192 A N ATOM 175 CA ARG A 25 50.266 4.514 30.876 1.00 9.27 A C ANISOU 175 CA ARG A 25 1407 438 1677 -207 134 349 A C ATOM 176 C ARG A 25 51.415 4.448 31.876 1.00 10.27 A C ANISOU 176 C ARG A 25 1302 820 1780 -70 122 115 A C ATOM 177 O ARG A 25 51.622 3.427 32.541 1.00 11.77 A O ANISOU 177 O ARG A 25 1467 795 2209 -32 223 227 A O ATOM 178 CB ARG A 25 48.994 5.148 31.462 1.00 11.60 A C ANISOU 178 CB ARG A 25 1366 1218 1823 -209 238 185 A C ATOM 179 CG ARG A 25 47.901 5.356 30.409 1.00 11.20 A C ANISOU 179 CG ARG A 25 1379 1013 1864 -265 278 21 A C ATOM 180 CD ARG A 25 46.599 5.776 31.028 1.00 11.07 A C ANISOU 180 CD ARG A 25 1455 1002 1747 -139 221 -27 A C ATOM 181 NE ARG A 25 46.053 4.733 31.866 1.00 10.74 A N ANISOU 181 NE ARG A 25 1418 804 1856 -49 178 73 A N ATOM 182 CZ ARG A 25 45.160 4.913 32.825 1.00 11.44 A C ANISOU 182 CZ ARG A 25 1557 1164 1625 -18 136 -153 A C ATOM 183 NH1 ARG A 25 44.682 6.134 33.051 1.00 10.91 A N ANISOU 183 NH1 ARG A 25 1350 1190 1602 25 -58 -236 A N ATOM 184 NH2 ARG A 25 44.747 3.894 33.586 1.00 11.98 A N ANISOU 184 NH2 ARG A 25 1611 1386 1555 -151 74 42 A N ATOM 185 N VAL A 26 52.128 5.581 32.001 1.00 10.31 A N ANISOU 185 N VAL A 26 1509 685 1720 -62 44 56 A N ATOM 186 CA VAL A 26 53.348 5.682 32.764 1.00 11.14 A C ANISOU 186 CA VAL A 26 1541 843 1849 13 91 77 A C ATOM 187 C VAL A 26 53.159 6.739 33.849 1.00 10.68 A C ANISOU 187 C VAL A 26 1251 1027 1777 -33 186 43 A C ATOM 188 O VAL A 26 52.611 7.808 33.598 1.00 11.61 A O ANISOU 188 O VAL A 26 1490 1004 1915 38 76 194 A O ATOM 189 CB VAL A 26 54.556 6.016 31.858 1.00 12.09 A C ANISOU 189 CB VAL A 26 1589 906 2095 -245 115 -122 A C ATOM 190 CG1 VAL A 26 55.855 5.913 32.632 1.00 12.60 A C ANISOU 190 CG1 VAL A 26 1641 1042 2102 -97 175 19 A C ATOM 191 CG2 VAL A 26 54.559 5.135 30.608 1.00 13.18 A C ANISOU 191 CG2 VAL A 26 1876 1068 2062 -98 210 -173 A C ATOM 192 N SER A 27 53.707 6.477 35.020 1.00 10.64 A N ANISOU 192 N SER A 27 1510 768 1765 33 97 -33 A N ATOM 193 CA SER A 27 53.714 7.406 36.155 1.00 11.01 A C ANISOU 193 CA SER A 27 1507 959 1715 64 -26 -83 A C ATOM 194 C SER A 27 55.085 7.398 36.828 1.00 11.67 A C ANISOU 194 C SER A 27 1334 972 2125 -16 -44 -33 A C ATOM 195 O SER A 27 55.749 6.372 36.842 1.00 13.27 A O ANISOU 195 O SER A 27 1522 960 2558 7 -125 -49 A O ATOM 196 CB SER A 27 52.679 7.043 37.198 1.00 11.30 A C ANISOU 196 CB SER A 27 1661 986 1646 72 39 -59 A C ATOM 197 OG SER A 27 51.379 6.938 36.660 1.00 11.95 A O ANISOU 197 OG SER A 27 1466 1016 2056 -79 129 35 A O ATOM 198 N TRP A 28 55.490 8.531 37.387 1.00 12.38 A N ANISOU 198 N TRP A 28 1540 878 2283 -27 -112 -18 A N ATOM 199 CA TRP A 28 56.695 8.553 38.180 1.00 13.79 A C ANISOU 199 CA TRP A 28 1996 1216 2028 -210 -218 -40 A C ATOM 200 C TRP A 28 56.442 9.332 39.452 1.00 14.43 A C ANISOU 200 C TRP A 28 2304 989 2187 90 -237 -114 A C ATOM 201 O TRP A 28 55.885 10.431 39.408 1.00 17.81 A O ANISOU 201 O TRP A 28 2660 1216 2888 449 -347 -298 A O ATOM 202 CB TRP A 28 57.882 9.110 37.381 1.00 13.45 A C ANISOU 202 CB TRP A 28 1667 1279 2164 18 -131 -177 A C ATOM 203 CG TRP A 28 57.590 10.361 36.599 1.00 12.84 A C ANISOU 203 CG TRP A 28 1723 1088 2067 -123 186 -254 A C ATOM 204 CD1 TRP A 28 57.886 11.661 36.921 1.00 13.90 A C ANISOU 204 CD1 TRP A 28 1779 1333 2167 -404 -92 -339 A C ATOM 205 CD2 TRP A 28 57.074 10.389 35.268 1.00 12.38 A C ANISOU 205 CD2 TRP A 28 1528 1133 2042 -143 126 174 A C ATOM 206 CE2 TRP A 28 57.031 11.740 34.859 1.00 12.35 A C ANISOU 206 CE2 TRP A 28 1354 1152 2186 61 76 120 A C ATOM 207 CE3 TRP A 28 56.638 9.387 34.380 1.00 13.61 A C ANISOU 207 CE3 TRP A 28 1459 1404 2307 -63 -48 -96 A C ATOM 208 NE1 TRP A 28 57.515 12.468 35.889 1.00 14.66 A N ANISOU 208 NE1 TRP A 28 1695 1527 2346 -30 204 -89 A N ATOM 209 CZ2 TRP A 28 56.561 12.103 33.613 1.00 13.82 A C ANISOU 209 CZ2 TRP A 28 1660 1548 2040 -153 21 169 A C ATOM 210 CZ3 TRP A 28 56.174 9.746 33.139 1.00 13.14 A C ANISOU 210 CZ3 TRP A 28 1706 1275 2010 -152 295 156 A C ATOM 211 CH2 TRP A 28 56.135 11.103 32.758 1.00 13.07 A C ANISOU 211 CH2 TRP A 28 1712 1277 1978 -188 134 210 A C ATOM 212 N ARG A 29 56.959 8.829 40.550 1.00 13.68 A N ANISOU 212 N ARG A 29 1896 968 2331 -200 -326 -29 A N ATOM 213 CA AARG A 29 56.923 9.511 41.821 0.50 15.45 A C ANISOU 213 CA AARG A 29 1925 1607 2336 -57 -108 -15 A C ATOM 214 CA BARG A 29 56.928 9.520 41.851 0.50 14.61 A C ANISOU 214 CA BARG A 29 1923 1415 2213 -56 -108 161 A C ATOM 215 C ARG A 29 58.270 10.205 42.074 1.00 15.49 A C ANISOU 215 C ARG A 29 2015 1547 2323 -94 -258 -45 A C ATOM 216 O ARG A 29 59.308 9.715 41.672 1.00 17.06 A O ANISOU 216 O ARG A 29 1722 2010 2748 -239 -413 -317 A O ATOM 217 CB AARG A 29 56.568 8.424 42.830 0.50 17.13 A C ANISOU 217 CB AARG A 29 2157 1911 2438 94 -48 263 A C ATOM 218 CB BARG A 29 56.748 8.563 43.031 0.50 16.55 A C ANISOU 218 CB BARG A 29 2052 1652 2581 -105 -225 542 A C ATOM 219 CG AARG A 29 56.158 8.924 44.196 0.50 18.90 A C ANISOU 219 CG AARG A 29 2305 2099 2774 119 -139 -598 A C ATOM 220 CG BARG A 29 55.325 8.144 43.344 0.50 15.76 A C ANISOU 220 CG BARG A 29 2072 1605 2309 22 1 345 A C ATOM 221 CD AARG A 29 55.657 7.705 44.944 0.50 23.34 A C ANISOU 221 CD AARG A 29 3011 2645 3211 544 393 2 A C ATOM 222 CD BARG A 29 55.270 7.710 44.803 0.50 15.57 A C ANISOU 222 CD BARG A 29 1745 1812 2358 100 67 534 A C ATOM 223 NE AARG A 29 54.217 7.530 44.795 0.50 24.56 A N ANISOU 223 NE AARG A 29 3018 2814 3499 908 127 -659 A N ATOM 224 NE BARG A 29 56.304 6.762 45.248 0.50 15.67 A N ANISOU 224 NE BARG A 29 2217 1170 2566 108 30 409 A N ATOM 225 CZ AARG A 29 53.548 6.425 45.061 0.50 26.92 A C ANISOU 225 CZ AARG A 29 3196 3426 3607 626 337 -288 A C ATOM 226 CZ BARG A 29 56.102 5.457 45.425 0.50 13.67 A C ANISOU 226 CZ BARG A 29 1808 1199 2186 113 190 385 A C ATOM 227 NH1AARG A 29 52.265 6.522 45.373 0.50 20.82 A N ANISOU 227 NH1AARG A 29 2910 1101 3898 881 -274 -1023 A N ATOM 228 NH1BARG A 29 54.894 4.986 45.231 0.50 14.42 A N ANISOU 228 NH1BARG A 29 1709 1219 2551 164 407 269 A N ATOM 229 NH2AARG A 29 54.147 5.247 45.000 0.50 30.29 A N ANISOU 229 NH2AARG A 29 4701 2865 3941 620 285 364 A N ATOM 230 NH2BARG A 29 57.109 4.649 45.749 0.50 18.56 A N ANISOU 230 NH2BARG A 29 2269 2139 2644 658 -227 132 A N ATOM 231 N PHE A 30 58.226 11.344 42.764 1.00 14.57 A N ANISOU 231 N PHE A 30 1576 1512 2445 -119 -83 -50 A N ATOM 232 CA PHE A 30 59.388 12.137 43.064 1.00 14.76 A C ANISOU 232 CA PHE A 30 1678 1549 2379 -305 123 -49 A C ATOM 233 C PHE A 30 59.826 11.951 44.511 1.00 17.65 A C ANISOU 233 C PHE A 30 2131 2166 2409 -190 18 -151 A C ATOM 234 O PHE A 30 59.000 11.669 45.416 1.00 20.89 A O ANISOU 234 O PHE A 30 2091 3495 2351 -421 -186 82 A O ATOM 235 CB PHE A 30 59.059 13.611 42.850 1.00 14.97 A C ANISOU 235 CB PHE A 30 1599 1695 2391 -136 -34 -95 A C ATOM 236 CG PHE A 30 58.677 13.983 41.444 1.00 13.74 A C ANISOU 236 CG PHE A 30 1760 1124 2333 -319 -35 -135 A C ATOM 237 CD1 PHE A 30 59.637 14.125 40.447 1.00 14.42 A C ANISOU 237 CD1 PHE A 30 1927 1284 2266 -172 39 -205 A C ATOM 238 CD2 PHE A 30 57.345 14.160 41.107 1.00 13.35 A C ANISOU 238 CD2 PHE A 30 1775 1022 2273 -381 -58 -332 A C ATOM 239 CE1 PHE A 30 59.278 14.516 39.169 1.00 14.19 A C ANISOU 239 CE1 PHE A 30 1942 1391 2059 -418 430 -145 A C ATOM 240 CE2 PHE A 30 56.989 14.485 39.811 1.00 14.25 A C ANISOU 240 CE2 PHE A 30 1878 1179 2354 -164 -91 -164 A C ATOM 241 CZ PHE A 30 57.953 14.694 38.852 1.00 14.84 A C ANISOU 241 CZ PHE A 30 2308 948 2382 -242 -1 -214 A C ATOM 242 N ASP A 31 61.123 12.166 44.732 1.00 18.78 A N ANISOU 242 N ASP A 31 2169 2551 2415 -464 11 -222 A N ATOM 243 CA ASP A 31 61.711 12.251 46.080 1.00 19.84 A C ANISOU 243 CA ASP A 31 2260 2301 2975 -200 -550 -248 A C ATOM 244 C ASP A 31 62.562 13.527 46.107 1.00 21.42 A C ANISOU 244 C ASP A 31 2808 2837 2492 -765 -304 -328 A C ATOM 245 O ASP A 31 63.222 13.852 45.167 1.00 24.59 A O ANISOU 245 O ASP A 31 3543 3281 2520 -1212 161 -612 A O ATOM 246 CB ASP A 31 62.498 10.978 46.410 1.00 22.65 A C ANISOU 246 CB ASP A 31 3156 2340 3107 121 -814 -201 A C ATOM 247 CG ASP A 31 63.021 10.830 47.825 1.00 34.89 A C ANISOU 247 CG ASP A 31 5121 4346 3786 659 -1292 571 A C ATOM 248 OD1 ASP A 31 62.706 11.667 48.720 1.00 45.48 A O ANISOU 248 OD1 ASP A 31 7000 6373 3904 1044 -1944 -19 A O ATOM 249 OD2 ASP A 31 63.740 9.852 48.027 1.00 52.88 A O ANISOU 249 OD2 ASP A 31 7070 5452 7568 1691 -1459 1317 A O ATOM 250 N GLY A 32 62.570 14.223 47.229 1.00 25.51 A N ANISOU 250 N GLY A 32 3348 3200 3145 -805 358 -877 A N ATOM 251 CA GLY A 32 63.394 15.399 47.342 1.00 25.12 A C ANISOU 251 CA GLY A 32 3598 2382 3566 -550 -77 -726 A C ATOM 252 C GLY A 32 62.674 16.511 48.070 1.00 22.87 A C ANISOU 252 C GLY A 32 2613 3112 2965 -482 -119 -814 A C ATOM 253 O GLY A 32 61.504 16.525 48.153 1.00 25.57 A O ANISOU 253 O GLY A 32 2763 2539 4411 -555 -163 -705 A O ATOM 254 N ASN A 33 63.437 17.469 48.576 1.00 26.02 A N ANISOU 254 N ASN A 33 3033 2751 4100 -542 -359 -791 A N ATOM 255 CA ASN A 33 62.900 18.520 49.435 1.00 25.29 A C ANISOU 255 CA ASN A 33 3122 2920 3566 303 -803 -643 A C ATOM 256 C ASN A 33 62.855 19.871 48.695 1.00 24.03 A C ANISOU 256 C ASN A 33 2743 3354 3032 -393 -733 -462 A C ATOM 257 O ASN A 33 62.638 20.906 49.322 1.00 28.42 A O ANISOU 257 O ASN A 33 3769 2996 4032 -688 -968 -702 A O ATOM 258 CB ASN A 33 63.684 18.608 50.758 1.00 29.62 A C ANISOU 258 CB ASN A 33 4426 3073 3756 410 -1347 -668 A C ATOM 259 CG ASN A 33 65.119 19.039 50.552 1.00 35.57 A C ANISOU 259 CG ASN A 33 4591 4004 4918 34 -933 -976 A C ATOM 260 ND2 ASN A 33 65.843 19.352 51.627 1.00 50.86 A N ANISOU 260 ND2 ASN A 33 8317 5343 5661 -306 -2146 -1383 A N ATOM 261 OD1 ASN A 33 65.581 19.073 49.418 1.00 39.18 A O ANISOU 261 OD1 ASN A 33 3847 6036 5001 -1295 -1417 -652 A O ATOM 262 N VAL A 34 62.981 19.856 47.363 1.00 21.99 A N ANISOU 262 N VAL A 34 2855 2299 3199 -500 -340 -572 A N ATOM 263 CA VAL A 34 62.942 21.064 46.553 1.00 22.87 A C ANISOU 263 CA VAL A 34 2286 2978 3425 -642 -416 -183 A C ATOM 264 C VAL A 34 61.661 21.879 46.839 1.00 21.16 A C ANISOU 264 C VAL A 34 2854 1890 3294 -642 -231 -426 A C ATOM 265 O VAL A 34 60.579 21.345 47.000 1.00 20.44 A O ANISOU 265 O VAL A 34 2513 2369 2885 -453 -320 -456 A O ATOM 266 CB VAL A 34 63.069 20.710 45.062 1.00 26.70 A C ANISOU 266 CB VAL A 34 3527 3020 3595 -880 -433 -646 A C ATOM 267 CG1 VAL A 34 61.912 19.836 44.556 1.00 21.89 A C ANISOU 267 CG1 VAL A 34 2869 2168 3280 -249 -312 -415 A C ATOM 268 CG2 VAL A 34 63.230 21.957 44.223 1.00 32.12 A C ANISOU 268 CG2 VAL A 34 4523 4013 3665 -673 -213 -157 A C ATOM 269 N SER A 35 61.819 23.201 46.808 1.00 22.50 A N ANISOU 269 N SER A 35 2953 1841 3755 -743 -177 -459 A N ATOM 270 CA SER A 35 60.794 24.185 47.095 1.00 20.89 A C ANISOU 270 CA SER A 35 2926 1908 3104 -900 -203 -639 A C ATOM 271 C SER A 35 60.073 24.633 45.821 1.00 18.70 A C ANISOU 271 C SER A 35 2677 1460 2968 -705 173 -740 A C ATOM 272 O SER A 35 60.711 24.985 44.831 1.00 23.93 A O ANISOU 272 O SER A 35 2641 2882 3566 -1278 444 -455 A O ATOM 273 CB SER A 35 61.391 25.400 47.784 1.00 24.28 A C ANISOU 273 CB SER A 35 2883 2843 3497 -1021 -1100 -1014 A C ATOM 274 OG SER A 35 61.735 25.110 49.128 1.00 33.56 A O ANISOU 274 OG SER A 35 4948 3682 4118 -396 -1486 -716 A O ATOM 275 N ASP A 36 58.739 24.678 45.898 1.00 18.40 A N ANISOU 275 N ASP A 36 2611 1633 2745 -775 101 -461 A N ATOM 276 CA ASP A 36 57.859 25.262 44.868 1.00 18.04 A C ANISOU 276 CA ASP A 36 2722 1029 3104 -949 -131 -515 A C ATOM 277 C ASP A 36 58.169 24.700 43.480 1.00 19.69 A C ANISOU 277 C ASP A 36 2813 1573 3092 -479 265 -424 A C ATOM 278 O ASP A 36 58.147 25.411 42.475 1.00 21.96 A O ANISOU 278 O ASP A 36 2991 1509 3843 -361 227 -247 A O ATOM 279 CB ASP A 36 58.000 26.787 44.827 1.00 20.82 A C ANISOU 279 CB ASP A 36 3548 1015 3347 -1102 -93 -480 A C ATOM 280 CG ASP A 36 57.408 27.465 46.023 1.00 31.47 A C ANISOU 280 CG ASP A 36 4893 1915 5149 -912 786 -1274 A C ATOM 281 OD1 ASP A 36 56.410 26.993 46.561 1.00 38.63 A O ANISOU 281 OD1 ASP A 36 4361 3019 7299 -872 1163 -1536 A O ATOM 282 OD2 ASP A 36 57.941 28.514 46.364 1.00 48.40 A O ANISOU 282 OD2 ASP A 36 7708 3087 7591 -2935 1545 -2022 A O ATOM 283 N TRP A 37 58.381 23.385 43.408 1.00 17.39 A N ANISOU 283 N TRP A 37 2442 1402 2761 -535 234 -165 A N ATOM 284 CA TRP A 37 58.794 22.777 42.163 1.00 18.03 A C ANISOU 284 CA TRP A 37 2244 2094 2512 -545 -101 -271 A C ATOM 285 C TRP A 37 57.584 22.222 41.406 1.00 14.83 A C ANISOU 285 C TRP A 37 1839 1490 2305 -218 164 -340 A C ATOM 286 O TRP A 37 56.755 21.507 41.993 1.00 15.61 A O ANISOU 286 O TRP A 37 2008 1617 2304 -416 216 -300 A O ATOM 287 CB TRP A 37 59.807 21.664 42.449 1.00 17.92 A C ANISOU 287 CB TRP A 37 2059 1749 3000 -706 131 -273 A C ATOM 288 CG TRP A 37 60.467 21.119 41.221 1.00 16.46 A C ANISOU 288 CG TRP A 37 2188 1405 2658 -314 -29 -156 A C ATOM 289 CD1 TRP A 37 61.650 21.521 40.681 1.00 18.42 A C ANISOU 289 CD1 TRP A 37 2159 2082 2757 -400 -53 -62 A C ATOM 290 CD2 TRP A 37 59.990 20.038 40.387 1.00 15.46 A C ANISOU 290 CD2 TRP A 37 2073 1393 2407 -316 75 -179 A C ATOM 291 CE2 TRP A 37 60.938 19.877 39.357 1.00 16.39 A C ANISOU 291 CE2 TRP A 37 2314 1373 2540 -467 273 -139 A C ATOM 292 CE3 TRP A 37 58.855 19.204 40.391 1.00 14.25 A C ANISOU 292 CE3 TRP A 37 1980 1344 2091 -235 249 -56 A C ATOM 293 NE1 TRP A 37 61.936 20.796 39.561 1.00 17.39 A N ANISOU 293 NE1 TRP A 37 1952 1747 2905 -448 229 -120 A N ATOM 294 CZ2 TRP A 37 60.786 18.927 38.349 1.00 15.28 A C ANISOU 294 CZ2 TRP A 37 1951 1374 2481 -219 115 -221 A C ATOM 295 CZ3 TRP A 37 58.727 18.252 39.404 1.00 15.86 A C ANISOU 295 CZ3 TRP A 37 2094 1358 2570 -225 31 -160 A C ATOM 296 CH2 TRP A 37 59.685 18.099 38.412 1.00 16.19 A C ANISOU 296 CH2 TRP A 37 2060 1183 2908 -196 160 61 A C ATOM 297 N GLU A 38 57.546 22.503 40.105 1.00 15.29 A N ANISOU 297 N GLU A 38 2152 1248 2406 -535 -226 -210 A N ATOM 298 CA GLU A 38 56.567 21.945 39.194 1.00 16.36 A C ANISOU 298 CA GLU A 38 2160 1928 2127 -791 -73 -136 A C ATOM 299 C GLU A 38 57.289 21.491 37.932 1.00 16.51 A C ANISOU 299 C GLU A 38 2275 1311 2684 -321 142 -310 A C ATOM 300 O GLU A 38 58.298 22.068 37.531 1.00 17.89 A O ANISOU 300 O GLU A 38 2392 1670 2733 -412 353 -305 A O ATOM 301 CB GLU A 38 55.476 22.970 38.862 1.00 23.63 A C ANISOU 301 CB GLU A 38 3191 2979 2808 191 -384 -276 A C ATOM 302 CG GLU A 38 54.569 23.245 40.043 1.00 28.67 A C ANISOU 302 CG GLU A 38 3747 3390 3754 444 158 -34 A C ATOM 303 CD GLU A 38 53.441 24.243 39.847 1.00 36.15 A C ANISOU 303 CD GLU A 38 4837 3450 5449 944 -401 777 A C ATOM 304 OE1 GLU A 38 53.739 25.429 39.574 1.00 43.48 A O ANISOU 304 OE1 GLU A 38 5134 2738 8645 640 -1180 -179 A O ATOM 305 OE2 GLU A 38 52.266 23.836 39.988 1.00 44.57 A O ANISOU 305 OE2 GLU A 38 5128 4876 6928 1167 107 1110 A O ATOM 306 N GLN A 39 56.767 20.435 37.311 1.00 14.32 A N ANISOU 306 N GLN A 39 1875 1212 2351 -319 270 -5 A N ATOM 307 CA GLN A 39 57.343 19.923 36.087 1.00 13.71 A C ANISOU 307 CA GLN A 39 1915 1091 2201 -409 306 101 A C ATOM 308 C GLN A 39 56.870 20.742 34.871 1.00 13.55 A C ANISOU 308 C GLN A 39 1835 1002 2308 -220 100 -136 A C ATOM 309 O GLN A 39 55.689 21.069 34.768 1.00 13.58 A O ANISOU 309 O GLN A 39 1851 1205 2103 -351 99 -126 A O ATOM 310 CB GLN A 39 56.856 18.466 35.942 1.00 12.68 A C ANISOU 310 CB GLN A 39 1732 1123 1963 -346 -22 -70 A C ATOM 311 CG GLN A 39 57.381 17.758 34.690 1.00 12.85 A C ANISOU 311 CG GLN A 39 1965 919 1995 -195 82 96 A C ATOM 312 CD GLN A 39 56.844 16.362 34.607 1.00 11.96 A C ANISOU 312 CD GLN A 39 1814 958 1771 -124 208 56 A C ATOM 313 NE2 GLN A 39 55.848 16.197 33.732 1.00 13.25 A N ANISOU 313 NE2 GLN A 39 1818 1280 1936 -91 87 -177 A N ATOM 314 OE1 GLN A 39 57.350 15.459 35.295 1.00 13.46 A O ANISOU 314 OE1 GLN A 39 1573 1153 2389 -24 -113 101 A O ATOM 315 N ARG A 40 57.791 21.025 33.930 1.00 13.47 A N ANISOU 315 N ARG A 40 1709 1047 2358 -230 58 -274 A N ATOM 316 CA AARG A 40 57.433 21.598 32.637 0.40 14.99 A C ANISOU 316 CA AARG A 40 2083 1108 2505 -180 194 -16 A C ATOM 317 CA BARG A 40 57.388 21.568 32.657 0.60 15.20 A C ANISOU 317 CA BARG A 40 2137 1165 2471 -71 234 -5 A C ATOM 318 C ARG A 40 57.488 20.561 31.506 1.00 13.96 A C ANISOU 318 C ARG A 40 1871 1083 2349 -187 174 96 A C ATOM 319 O ARG A 40 56.796 20.736 30.496 1.00 13.83 A O ANISOU 319 O ARG A 40 1777 1014 2461 -223 275 60 A O ATOM 320 CB AARG A 40 58.296 22.817 32.297 0.40 17.69 A C ANISOU 320 CB AARG A 40 2665 1056 2998 -444 222 -153 A C ATOM 321 CB BARG A 40 58.142 22.849 32.319 0.60 17.77 A C ANISOU 321 CB BARG A 40 2534 1187 3031 -311 335 -134 A C ATOM 322 CG AARG A 40 59.611 22.496 31.604 0.40 18.51 A C ANISOU 322 CG AARG A 40 2710 1114 3208 -770 426 -102 A C ATOM 323 CG BARG A 40 59.631 22.660 32.096 0.60 18.83 A C ANISOU 323 CG BARG A 40 2509 1599 3044 -536 449 -154 A C ATOM 324 CD AARG A 40 60.472 23.738 31.358 0.40 20.61 A C ANISOU 324 CD AARG A 40 3250 1100 3480 -894 454 130 A C ATOM 325 CD BARG A 40 60.274 23.960 31.592 0.60 23.08 A C ANISOU 325 CD BARG A 40 3525 1404 3840 -470 364 225 A C ATOM 326 NE AARG A 40 61.891 23.412 31.344 0.40 21.78 A N ANISOU 326 NE AARG A 40 3270 1387 3616 -1001 605 341 A N ATOM 327 NE BARG A 40 59.514 24.572 30.504 0.60 26.69 A N ANISOU 327 NE BARG A 40 3360 2105 4675 -377 3 711 A N ATOM 328 CZ AARG A 40 62.536 22.950 30.290 0.40 23.88 A C ANISOU 328 CZ AARG A 40 3414 2211 3448 -519 443 320 A C ATOM 329 CZ BARG A 40 58.741 25.671 30.593 0.60 28.64 A C ANISOU 329 CZ BARG A 40 4133 2445 4302 97 -392 860 A C ATOM 330 NH1AARG A 40 61.909 22.863 29.130 0.40 31.58 A N ANISOU 330 NH1AARG A 40 4049 3751 4196 -423 -221 242 A N ATOM 331 NH1BARG A 40 58.651 26.387 31.715 0.60 26.69 A N ANISOU 331 NH1BARG A 40 3359 1904 4874 -700 -1008 308 A N ATOM 332 NH2AARG A 40 63.799 22.583 30.393 0.40 21.11 A N ANISOU 332 NH2AARG A 40 3326 2185 2508 -454 405 483 A N ATOM 333 NH2BARG A 40 58.052 26.044 29.528 0.60 29.64 A N ANISOU 333 NH2BARG A 40 4000 3057 4202 -333 -270 1775 A N ATOM 334 N ALA A 41 58.314 19.510 31.655 1.00 12.85 A N ANISOU 334 N ALA A 41 1858 1111 1912 -123 191 131 A N ATOM 335 CA ALA A 41 58.513 18.584 30.547 1.00 14.04 A C ANISOU 335 CA ALA A 41 2075 1396 1862 -123 239 144 A C ATOM 336 C ALA A 41 59.075 17.293 31.111 1.00 12.38 A C ANISOU 336 C ALA A 41 1753 1173 1777 -281 196 24 A C ATOM 337 O ALA A 41 59.558 17.247 32.234 1.00 12.50 A O ANISOU 337 O ALA A 41 1922 829 1999 -41 -7 -14 A O ATOM 338 CB ALA A 41 59.464 19.135 29.509 1.00 14.23 A C ANISOU 338 CB ALA A 41 2010 1367 2028 -8 334 6 A C ATOM 339 N TYR A 42 58.996 16.243 30.305 1.00 12.82 A N ANISOU 339 N TYR A 42 1560 1206 2101 -64 82 -77 A N ATOM 340 CA TYR A 42 59.602 14.954 30.646 1.00 13.48 A C ANISOU 340 CA TYR A 42 1646 1182 2291 -182 -83 195 A C ATOM 341 C TYR A 42 60.157 14.324 29.373 1.00 13.88 A C ANISOU 341 C TYR A 42 1791 1121 2359 -357 31 232 A C ATOM 342 O TYR A 42 59.761 14.625 28.265 1.00 13.70 A O ANISOU 342 O TYR A 42 1876 934 2394 55 205 120 A O ATOM 343 CB TYR A 42 58.616 14.033 31.361 1.00 13.15 A C ANISOU 343 CB TYR A 42 1811 937 2246 25 115 13 A C ATOM 344 CG TYR A 42 57.399 13.641 30.574 1.00 12.23 A C ANISOU 344 CG TYR A 42 1495 1113 2036 -16 287 -42 A C ATOM 345 CD1 TYR A 42 57.448 12.593 29.662 1.00 12.87 A C ANISOU 345 CD1 TYR A 42 1446 1133 2309 62 118 -105 A C ATOM 346 CD2 TYR A 42 56.162 14.225 30.811 1.00 13.16 A C ANISOU 346 CD2 TYR A 42 1655 887 2458 9 306 87 A C ATOM 347 CE1 TYR A 42 56.319 12.176 28.975 1.00 12.60 A C ANISOU 347 CE1 TYR A 42 1799 869 2119 -86 -18 13 A C ATOM 348 CE2 TYR A 42 55.031 13.801 30.150 1.00 12.67 A C ANISOU 348 CE2 TYR A 42 1637 1230 1945 201 187 239 A C ATOM 349 CZ TYR A 42 55.084 12.734 29.266 1.00 12.82 A C ANISOU 349 CZ TYR A 42 1667 1028 2173 -227 159 297 A C ATOM 350 OH TYR A 42 53.930 12.331 28.610 1.00 14.85 A O ANISOU 350 OH TYR A 42 1930 1164 2548 -281 -105 372 A O ATOM 351 N GLU A 43 61.060 13.367 29.613 1.00 14.01 A N ANISOU 351 N GLU A 43 1853 1379 2091 20 172 65 A N ATOM 352 CA GLU A 43 61.585 12.481 28.589 1.00 14.34 A C ANISOU 352 CA GLU A 43 1916 1245 2287 -141 370 58 A C ATOM 353 C GLU A 43 61.393 11.040 29.072 1.00 13.46 A C ANISOU 353 C GLU A 43 1548 1224 2339 -85 190 5 A C ATOM 354 O GLU A 43 61.715 10.720 30.207 1.00 14.28 A O ANISOU 354 O GLU A 43 1649 1355 2419 -67 223 -55 A O ATOM 355 CB GLU A 43 63.058 12.781 28.284 1.00 16.12 A C ANISOU 355 CB GLU A 43 1936 1297 2892 164 691 -15 A C ATOM 356 CG GLU A 43 63.215 14.040 27.460 1.00 17.65 A C ANISOU 356 CG GLU A 43 2091 1494 3118 -130 272 125 A C ATOM 357 CD GLU A 43 64.647 14.396 27.123 1.00 22.12 A C ANISOU 357 CD GLU A 43 2118 2660 3625 -447 221 739 A C ATOM 358 OE1 GLU A 43 65.552 13.761 27.671 1.00 20.67 A O ANISOU 358 OE1 GLU A 43 2071 1918 3864 -381 347 351 A O ATOM 359 OE2 GLU A 43 64.832 15.384 26.365 1.00 30.76 A O ANISOU 359 OE2 GLU A 43 2649 3656 5381 -1013 1447 1667 A O ATOM 360 N ILE A 44 60.876 10.220 28.167 1.00 13.18 A N ANISOU 360 N ILE A 44 1742 1082 2183 152 76 52 A N ATOM 361 CA ILE A 44 60.767 8.763 28.390 1.00 13.52 A C ANISOU 361 CA ILE A 44 1844 1075 2216 129 171 136 A C ATOM 362 C ILE A 44 61.672 8.078 27.360 1.00 13.11 A C ANISOU 362 C ILE A 44 1648 1237 2096 -146 123 -5 A C ATOM 363 O ILE A 44 61.495 8.251 26.161 1.00 14.23 A O ANISOU 363 O ILE A 44 1991 1326 2088 143 332 -86 A O ATOM 364 CB ILE A 44 59.324 8.257 28.266 1.00 14.23 A C ANISOU 364 CB ILE A 44 1924 918 2563 106 330 -164 A C ATOM 365 CG1 ILE A 44 58.383 8.961 29.228 1.00 14.69 A C ANISOU 365 CG1 ILE A 44 1975 1089 2515 45 234 -347 A C ATOM 366 CG2 ILE A 44 59.317 6.742 28.487 1.00 14.24 A C ANISOU 366 CG2 ILE A 44 2054 1015 2340 110 520 96 A C ATOM 367 CD1 ILE A 44 56.908 8.593 29.116 1.00 16.40 A C ANISOU 367 CD1 ILE A 44 2091 1418 2722 131 -106 -94 A C ATOM 368 N GLU A 45 62.623 7.296 27.873 1.00 14.66 A N ANISOU 368 N GLU A 45 1725 1704 2138 148 191 57 A N ATOM 369 CA GLU A 45 63.525 6.452 27.072 1.00 15.63 A C ANISOU 369 CA GLU A 45 2125 1155 2656 109 356 82 A C ATOM 370 C GLU A 45 62.925 5.048 27.012 1.00 14.64 A C ANISOU 370 C GLU A 45 1906 1259 2395 116 160 -78 A C ATOM 371 O GLU A 45 62.659 4.443 28.056 1.00 16.27 A O ANISOU 371 O GLU A 45 2328 1347 2506 33 292 -130 A O ATOM 372 CB GLU A 45 64.909 6.422 27.715 1.00 16.36 A C ANISOU 372 CB GLU A 45 2214 1283 2716 176 330 -151 A C ATOM 373 CG GLU A 45 65.946 5.612 26.936 1.00 17.86 A C ANISOU 373 CG GLU A 45 2008 1493 3283 165 480 -240 A C ATOM 374 CD GLU A 45 67.181 5.390 27.790 1.00 20.26 A C ANISOU 374 CD GLU A 45 1949 2662 3086 -103 516 99 A C ATOM 375 OE1 GLU A 45 68.205 6.068 27.545 1.00 26.72 A O ANISOU 375 OE1 GLU A 45 2024 3674 4454 -646 354 565 A O ATOM 376 OE2 GLU A 45 67.077 4.611 28.766 1.00 20.64 A O ANISOU 376 OE2 GLU A 45 2149 2261 3432 336 177 155 A O ATOM 377 N VAL A 46 62.718 4.566 25.795 1.00 14.93 A N ANISOU 377 N VAL A 46 2349 1038 2285 -213 316 61 A N ATOM 378 CA VAL A 46 62.246 3.216 25.570 1.00 13.57 A C ANISOU 378 CA VAL A 46 2004 866 2284 15 582 16 A C ATOM 379 C VAL A 46 63.287 2.429 24.768 1.00 15.94 A C ANISOU 379 C VAL A 46 2210 1591 2254 383 571 14 A C ATOM 380 O VAL A 46 63.595 2.779 23.616 1.00 18.06 A O ANISOU 380 O VAL A 46 2696 1592 2573 172 950 49 A O ATOM 381 CB VAL A 46 60.891 3.229 24.847 1.00 14.67 A C ANISOU 381 CB VAL A 46 2241 1062 2268 139 287 32 A C ATOM 382 CG1 VAL A 46 60.353 1.808 24.664 1.00 15.59 A C ANISOU 382 CG1 VAL A 46 2296 1111 2517 92 282 -23 A C ATOM 383 CG2 VAL A 46 59.895 4.125 25.573 1.00 15.90 A C ANISOU 383 CG2 VAL A 46 2344 1441 2256 202 572 140 A C ATOM 384 N LYS A 47 63.791 1.347 25.381 1.00 15.88 A N ANISOU 384 N LYS A 47 1919 1557 2555 129 774 360 A N ATOM 385 CA LYS A 47 64.812 0.471 24.739 1.00 18.07 A C ANISOU 385 CA LYS A 47 2285 1964 2614 273 711 -141 A C ATOM 386 C LYS A 47 64.186 -0.880 24.382 1.00 20.25 A C ANISOU 386 C LYS A 47 2602 2122 2966 369 757 448 A C ATOM 387 O LYS A 47 63.616 -1.520 25.270 1.00 19.83 A O ANISOU 387 O LYS A 47 3198 1134 3201 120 790 -352 A O ATOM 388 CB LYS A 47 66.035 0.319 25.658 1.00 21.11 A C ANISOU 388 CB LYS A 47 2464 2537 3018 647 488 329 A C ATOM 389 CG LYS A 47 67.136 -0.595 25.146 1.00 26.96 A C ANISOU 389 CG LYS A 47 3310 3051 3881 962 858 36 A C ATOM 390 CD LYS A 47 67.865 -0.051 23.945 1.00 33.39 A C ANISOU 390 CD LYS A 47 3598 3356 5730 1307 1928 601 A C ATOM 391 CE LYS A 47 69.011 -0.942 23.506 1.00 39.36 A C ANISOU 391 CE LYS A 47 4290 4748 5914 1504 2428 -1051 A C ATOM 392 NZ LYS A 47 68.527 -2.078 22.691 1.00 42.94 A N ANISOU 392 NZ LYS A 47 5918 4420 5974 1497 2056 -360 A N ATOM 393 N ARG A 48 64.282 -1.292 23.117 1.00 21.85 A N ANISOU 393 N ARG A 48 3276 1798 3227 92 747 -192 A N ATOM 394 CA ARG A 48 63.883 -2.585 22.631 1.00 25.26 A C ANISOU 394 CA ARG A 48 3470 2434 3694 8 637 35 A C ATOM 395 C ARG A 48 65.150 -3.317 22.223 1.00 30.27 A C ANISOU 395 C ARG A 48 4860 1996 4642 508 2356 -471 A C ATOM 396 O ARG A 48 66.012 -2.679 21.655 1.00 35.11 A O ANISOU 396 O ARG A 48 6180 2331 4828 -398 2217 3 A O ATOM 397 CB ARG A 48 62.980 -2.402 21.410 1.00 29.37 A C ANISOU 397 CB ARG A 48 3151 3722 4284 -468 273 -438 A C ATOM 398 CG ARG A 48 61.532 -2.289 21.798 1.00 20.25 A C ANISOU 398 CG ARG A 48 2843 1791 3059 -772 522 -462 A C ATOM 399 CD ARG A 48 60.632 -2.171 20.572 1.00 21.89 A C ANISOU 399 CD ARG A 48 2658 2530 3127 -445 517 -472 A C ATOM 400 NE ARG A 48 59.231 -2.195 20.972 1.00 22.11 A N ANISOU 400 NE ARG A 48 2384 2556 3459 -70 345 47 A N ATOM 401 CZ ARG A 48 58.474 -1.133 21.118 1.00 20.73 A C ANISOU 401 CZ ARG A 48 2611 2203 3063 -280 393 -621 A C ATOM 402 NH1 ARG A 48 59.031 0.068 21.255 1.00 21.22 A N ANISOU 402 NH1 ARG A 48 3176 1992 2893 -304 232 78 A N ATOM 403 NH2 ARG A 48 57.168 -1.263 21.085 1.00 22.51 A N ANISOU 403 NH2 ARG A 48 2336 3611 2603 231 314 319 A N ATOM 404 N ALA A 49 65.230 -4.615 22.554 1.00 33.80 A N ANISOU 404 N ALA A 49 5283 2363 5196 718 2121 321 A N ATOM 405 CA ALA A 49 66.395 -5.418 22.211 1.00 37.68 A C ANISOU 405 CA ALA A 49 5748 2206 6362 856 2348 -262 A C ATOM 406 C ALA A 49 66.708 -5.193 20.715 1.00 43.67 A C ANISOU 406 C ALA A 49 5716 4629 6245 -436 2061 -828 A C ATOM 407 O ALA A 49 65.702 -5.184 19.864 1.00 51.91 A O ANISOU 407 O ALA A 49 8272 4819 6630 -349 -271 -1359 A O ATOM 408 CB ALA A 49 66.133 -6.872 22.582 1.00 43.74 A C ANISOU 408 CB ALA A 49 7136 2494 6989 440 2107 390 A C ATOM 409 N GLY A 50 68.036 -5.051 20.412 1.00 42.76 A N ANISOU 409 N GLY A 50 6437 2806 7001 -3 2258 -377 A N ATOM 410 CA GLY A 50 68.507 -4.949 19.024 1.00 48.92 A C ANISOU 410 CA GLY A 50 6040 4906 7639 1188 3225 -596 A C ATOM 411 C GLY A 50 68.339 -3.562 18.416 1.00 55.15 A C ANISOU 411 C GLY A 50 8415 5191 7349 2068 3742 -663 A C ATOM 412 O GLY A 50 68.795 -3.355 17.285 1.00 69.77 A O ANISOU 412 O GLY A 50 10985 7708 7814 413 4933 -1880 A O ATOM 413 N HIS A 51 67.695 -2.630 19.140 1.00 46.26 A N ANISOU 413 N HIS A 51 7720 4008 5847 1549 3518 37 A N ATOM 414 CA HIS A 51 67.465 -1.269 18.632 1.00 44.69 A C ANISOU 414 CA HIS A 51 6834 4150 5996 -117 2900 226 A C ATOM 415 C HIS A 51 68.102 -0.249 19.577 1.00 45.49 A C ANISOU 415 C HIS A 51 7632 4164 5485 -67 2860 506 A C ATOM 416 O HIS A 51 68.160 -0.450 20.789 1.00 36.91 A O ANISOU 416 O HIS A 51 5465 3337 5220 585 2395 90 A O ATOM 417 CB HIS A 51 65.969 -0.960 18.447 1.00 40.87 A C ANISOU 417 CB HIS A 51 6523 4274 4729 373 2697 -602 A C ATOM 418 CG HIS A 51 65.250 -1.936 17.568 1.00 56.55 A C ANISOU 418 CG HIS A 51 8002 7807 5675 -1268 2571 -1860 A C ATOM 419 CD2 HIS A 51 65.696 -2.930 16.763 1.00 60.71 A C ANISOU 419 CD2 HIS A 51 7108 7701 8256 132 1758 -1865 A C ATOM 420 ND1 HIS A 51 63.869 -1.956 17.470 1.00 69.31 A N ANISOU 420 ND1 HIS A 51 8800 8968 8567 -626 1732 -2588 A N ATOM 421 CE1 HIS A 51 63.497 -2.912 16.642 1.00 74.64 A C ANISOU 421 CE1 HIS A 51 9746 9965 8647 -673 1305 -3094 A C ATOM 422 NE2 HIS A 51 64.603 -3.527 16.189 1.00 67.33 A N ANISOU 422 NE2 HIS A 51 9817 7040 8726 -1880 2013 -2739 A N ATOM 423 N ASP A 52 68.605 0.844 18.991 1.00 41.87 A N ANISOU 423 N ASP A 52 6514 3919 5475 74 2758 279 A N ATOM 424 CA ASP A 52 68.917 2.031 19.756 1.00 35.62 A C ANISOU 424 CA ASP A 52 3884 3931 5717 919 2784 -425 A C ATOM 425 C ASP A 52 67.654 2.444 20.539 1.00 28.88 A C ANISOU 425 C ASP A 52 3555 3466 3951 1304 1797 -161 A C ATOM 426 O ASP A 52 66.530 2.362 20.059 1.00 30.78 A O ANISOU 426 O ASP A 52 4381 3219 4092 412 1159 361 A O ATOM 427 CB ASP A 52 69.352 3.186 18.851 1.00 40.22 A C ANISOU 427 CB ASP A 52 4017 5528 5737 1007 2917 887 A C ATOM 428 N ALA A 53 67.869 2.864 21.781 1.00 28.38 A N ANISOU 428 N ALA A 53 3798 3275 3709 582 1989 822 A N ATOM 429 CA ALA A 53 66.883 3.494 22.543 1.00 27.70 A C ANISOU 429 CA ALA A 53 3529 2441 4552 833 1301 158 A C ATOM 430 C ALA A 53 66.253 4.650 21.751 1.00 25.61 A C ANISOU 430 C ALA A 53 2707 2249 4773 -151 1203 560 A C ATOM 431 O ALA A 53 66.935 5.406 21.026 1.00 29.19 A O ANISOU 431 O ALA A 53 2999 2185 5905 13 2123 323 A O ATOM 432 CB ALA A 53 67.525 3.978 23.817 1.00 32.81 A C ANISOU 432 CB ALA A 53 3928 3779 4758 726 598 180 A C ATOM 433 N ASP A 54 64.930 4.801 21.902 1.00 21.11 A N ANISOU 433 N ASP A 54 2736 1281 4001 -34 1272 -252 A N ATOM 434 CA ASP A 54 64.233 6.022 21.495 1.00 18.31 A C ANISOU 434 CA ASP A 54 2414 1819 2723 95 1465 -4 A C ATOM 435 C ASP A 54 63.970 6.869 22.743 1.00 18.41 A C ANISOU 435 C ASP A 54 2453 2038 2503 -182 1083 -122 A C ATOM 436 O ASP A 54 63.672 6.330 23.763 1.00 18.86 A O ANISOU 436 O ASP A 54 2787 1694 2684 231 933 13 A O ATOM 437 CB ASP A 54 62.895 5.743 20.820 1.00 23.86 A C ANISOU 437 CB ASP A 54 3136 2820 3110 -513 942 23 A C ATOM 438 CG ASP A 54 62.988 5.098 19.462 1.00 29.50 A C ANISOU 438 CG ASP A 54 3800 4404 3005 -749 757 -249 A C ATOM 439 OD1 ASP A 54 63.982 5.363 18.756 1.00 34.88 A O ANISOU 439 OD1 ASP A 54 4509 4606 4135 -780 1499 -78 A O ATOM 440 OD2 ASP A 54 62.058 4.334 19.142 1.00 31.76 A O ANISOU 440 OD2 ASP A 54 4557 4539 2969 -1080 681 -511 A O ATOM 441 N VAL A 55 64.106 8.207 22.610 1.00 18.15 A N ANISOU 441 N VAL A 55 2210 1920 2765 -48 760 84 A N ATOM 442 CA VAL A 55 63.759 9.142 23.671 1.00 17.83 A C ANISOU 442 CA VAL A 55 1851 2023 2899 139 605 143 A C ATOM 443 C VAL A 55 62.619 10.011 23.138 1.00 17.12 A C ANISOU 443 C VAL A 55 2134 2116 2254 169 595 381 A C ATOM 444 O VAL A 55 62.724 10.622 22.084 1.00 19.74 A O ANISOU 444 O VAL A 55 2800 2252 2448 363 963 592 A O ATOM 445 CB VAL A 55 64.964 9.977 24.162 1.00 20.11 A C ANISOU 445 CB VAL A 55 2325 2204 3109 -210 464 143 A C ATOM 446 CG1 VAL A 55 64.548 11.014 25.197 1.00 22.21 A C ANISOU 446 CG1 VAL A 55 2387 2202 3849 55 274 23 A C ATOM 447 CG2 VAL A 55 66.069 9.063 24.712 1.00 22.72 A C ANISOU 447 CG2 VAL A 55 2177 2182 4273 -266 433 129 A C ATOM 448 N PHE A 56 61.535 10.060 23.907 1.00 15.56 A N ANISOU 448 N PHE A 56 2307 1364 2240 72 675 193 A N ATOM 449 CA PHE A 56 60.347 10.820 23.567 1.00 14.83 A C ANISOU 449 CA PHE A 56 2098 1550 1986 -4 692 258 A C ATOM 450 C PHE A 56 60.197 11.960 24.578 1.00 14.58 A C ANISOU 450 C PHE A 56 1954 1227 2359 57 623 160 A C ATOM 451 O PHE A 56 60.094 11.735 25.798 1.00 16.95 A O ANISOU 451 O PHE A 56 2860 1134 2444 7 213 180 A O ATOM 452 CB PHE A 56 59.114 9.923 23.663 1.00 15.43 A C ANISOU 452 CB PHE A 56 2020 1501 2340 20 323 -9 A C ATOM 453 CG PHE A 56 59.186 8.753 22.717 1.00 14.95 A C ANISOU 453 CG PHE A 56 2032 1386 2260 134 505 123 A C ATOM 454 CD1 PHE A 56 58.807 8.886 21.388 1.00 17.02 A C ANISOU 454 CD1 PHE A 56 2471 1448 2547 125 229 195 A C ATOM 455 CD2 PHE A 56 59.638 7.517 23.152 1.00 14.32 A C ANISOU 455 CD2 PHE A 56 1800 1495 2142 49 675 269 A C ATOM 456 CE1 PHE A 56 58.886 7.817 20.513 1.00 20.26 A C ANISOU 456 CE1 PHE A 56 2960 1824 2914 230 444 8 A C ATOM 457 CE2 PHE A 56 59.708 6.446 22.283 1.00 17.25 A C ANISOU 457 CE2 PHE A 56 2479 1480 2593 -303 502 126 A C ATOM 458 CZ PHE A 56 59.312 6.584 20.978 1.00 17.68 A C ANISOU 458 CZ PHE A 56 2544 1682 2492 201 431 -75 A C ATOM 459 N ARG A 57 60.205 13.190 24.085 1.00 15.88 A N ANISOU 459 N ARG A 57 2314 1236 2481 116 690 255 A N ATOM 460 CA ARG A 57 60.038 14.384 24.959 1.00 14.88 A C ANISOU 460 CA ARG A 57 1910 1564 2178 164 782 131 A C ATOM 461 C ARG A 57 58.610 14.914 24.827 1.00 13.80 A C ANISOU 461 C ARG A 57 2044 892 2304 -100 470 226 A C ATOM 462 O ARG A 57 58.058 15.001 23.727 1.00 16.79 A O ANISOU 462 O ARG A 57 2587 1265 2525 69 270 -68 A O ATOM 463 CB ARG A 57 61.005 15.504 24.556 1.00 18.88 A C ANISOU 463 CB ARG A 57 1923 1860 3391 -170 379 253 A C ATOM 464 CG ARG A 57 60.960 16.705 25.501 1.00 24.47 A C ANISOU 464 CG ARG A 57 3121 1574 4601 366 1235 -65 A C ATOM 465 CD ARG A 57 62.037 17.767 25.341 1.00 32.99 A C ANISOU 465 CD ARG A 57 3938 3040 5555 -685 809 -291 A C ATOM 466 NE ARG A 57 61.879 18.823 26.349 1.00 31.08 A N ANISOU 466 NE ARG A 57 3754 3293 4761 -177 590 15 A N ATOM 467 CZ ARG A 57 62.775 19.128 27.299 1.00 31.50 A C ANISOU 467 CZ ARG A 57 4021 3780 4166 674 610 -52 A C ATOM 468 NH1 ARG A 57 63.825 18.345 27.511 1.00 31.35 A N ANISOU 468 NH1 ARG A 57 3007 3417 5486 55 376 819 A N ATOM 469 NH2 ARG A 57 62.642 20.239 28.007 1.00 31.93 A N ANISOU 469 NH2 ARG A 57 4179 2986 4966 -548 691 -74 A N ATOM 470 N SER A 58 58.040 15.274 25.977 1.00 14.27 A N ANISOU 470 N SER A 58 1962 1407 2051 -50 209 159 A N ATOM 471 CA ASER A 58 56.729 15.917 26.077 0.50 12.66 A C ANISOU 471 CA ASER A 58 1833 1165 1809 -222 255 159 A C ATOM 472 CA BSER A 58 56.768 15.963 25.989 0.50 13.27 A C ANISOU 472 CA BSER A 58 1993 1279 1767 -46 238 153 A C ATOM 473 C SER A 58 56.875 17.204 26.871 1.00 12.39 A C ANISOU 473 C SER A 58 1663 1125 1917 -362 237 225 A C ATOM 474 O SER A 58 57.409 17.168 27.958 1.00 14.95 A O ANISOU 474 O SER A 58 2150 1193 2336 191 23 95 A O ATOM 475 CB ASER A 58 55.739 15.043 26.791 0.50 12.66 A C ANISOU 475 CB ASER A 58 1860 523 2426 -283 97 165 A C ATOM 476 CB BSER A 58 55.661 15.039 26.424 0.50 16.32 A C ANISOU 476 CB BSER A 58 2110 1636 2452 -148 411 371 A C ATOM 477 OG ASER A 58 55.400 13.890 26.036 0.50 12.86 A O ANISOU 477 OG ASER A 58 1699 672 2514 -260 221 -92 A O ATOM 478 OG BSER A 58 54.402 15.702 26.422 0.50 18.60 A O ANISOU 478 OG BSER A 58 2223 1634 3209 -115 303 224 A O ATOM 479 N GLU A 59 56.322 18.287 26.331 1.00 13.43 A N ANISOU 479 N GLU A 59 1841 1380 1879 -4 402 237 A N ATOM 480 CA GLU A 59 56.011 19.504 27.104 1.00 14.82 A C ANISOU 480 CA GLU A 59 1871 1301 2457 154 399 144 A C ATOM 481 C GLU A 59 54.712 19.213 27.838 1.00 13.44 A C ANISOU 481 C GLU A 59 1991 1075 2040 279 225 270 A C ATOM 482 O GLU A 59 53.685 19.024 27.185 1.00 15.66 A O ANISOU 482 O GLU A 59 2026 1348 2576 62 175 18 A O ATOM 483 CB GLU A 59 55.862 20.689 26.163 1.00 14.86 A C ANISOU 483 CB GLU A 59 1923 1200 2520 108 353 101 A C ATOM 484 CG GLU A 59 55.829 22.011 26.852 1.00 17.29 A C ANISOU 484 CG GLU A 59 2519 1234 2816 212 269 54 A C ATOM 485 CD GLU A 59 57.139 22.490 27.445 1.00 23.75 A C ANISOU 485 CD GLU A 59 3009 2127 3886 -493 252 -437 A C ATOM 486 OE1 GLU A 59 58.232 21.891 27.139 1.00 22.93 A O ANISOU 486 OE1 GLU A 59 2916 2161 3634 -267 387 754 A O ATOM 487 OE2 GLU A 59 57.053 23.538 28.194 1.00 23.10 A O ANISOU 487 OE2 GLU A 59 3225 2033 3518 -188 639 -325 A O ATOM 488 N SER A 60 54.830 19.016 29.148 1.00 11.45 A N ANISOU 488 N SER A 60 1429 1097 1822 -171 86 140 A N ATOM 489 CA SER A 60 53.721 18.568 29.973 1.00 11.11 A C ANISOU 489 CA SER A 60 1671 609 1941 7 282 81 A C ATOM 490 C SER A 60 54.105 18.688 31.437 1.00 11.81 A C ANISOU 490 C SER A 60 1628 880 1977 -334 295 209 A C ATOM 491 O SER A 60 55.218 18.291 31.803 1.00 13.05 A O ANISOU 491 O SER A 60 1732 1143 2081 -124 227 76 A O ATOM 492 CB SER A 60 53.400 17.126 29.676 1.00 11.89 A C ANISOU 492 CB SER A 60 1935 620 1960 17 54 -13 A C ATOM 493 OG SER A 60 52.385 16.644 30.556 1.00 13.12 A O ANISOU 493 OG SER A 60 1783 1160 2040 -96 21 101 A O ATOM 494 N SER A 61 53.148 19.122 32.266 1.00 11.64 A N ANISOU 494 N SER A 61 1622 861 1937 -247 175 32 A N ATOM 495 CA ASER A 61 53.344 19.067 33.703 0.50 11.44 A C ANISOU 495 CA ASER A 61 1452 895 1999 42 18 -12 A C ATOM 496 CA BSER A 61 53.301 19.093 33.698 0.50 13.15 A C ANISOU 496 CA BSER A 61 1875 1089 2031 -131 69 83 A C ATOM 497 C SER A 61 52.879 17.735 34.292 1.00 13.04 A C ANISOU 497 C SER A 61 1932 1103 1917 -119 -128 120 A C ATOM 498 O SER A 61 53.035 17.551 35.462 1.00 12.55 A O ANISOU 498 O SER A 61 1930 968 1868 -505 4 -34 A O ATOM 499 CB ASER A 61 52.622 20.175 34.388 0.50 11.14 A C ANISOU 499 CB ASER A 61 1529 680 2023 7 38 81 A C ATOM 500 CB BSER A 61 52.515 20.232 34.296 0.50 16.76 A C ANISOU 500 CB BSER A 61 2712 1191 2463 79 249 -75 A C ATOM 501 OG ASER A 61 51.225 19.934 34.383 0.50 10.12 A O ANISOU 501 OG ASER A 61 1389 408 2048 225 -104 -108 A O ATOM 502 OG BSER A 61 52.893 21.490 33.707 0.50 23.25 A O ANISOU 502 OG BSER A 61 3911 1627 3296 -642 276 110 A O ATOM 503 N ASP A 62 52.314 16.845 33.482 1.00 12.04 A N ANISOU 503 N ASP A 62 1764 1112 1698 -220 109 133 A N ATOM 504 CA ASP A 62 51.725 15.601 34.036 1.00 11.99 A C ANISOU 504 CA ASP A 62 1712 1015 1828 -150 206 125 A C ATOM 505 C ASP A 62 52.808 14.555 34.326 1.00 12.09 A C ANISOU 505 C ASP A 62 1960 910 1721 -131 61 -158 A C ATOM 506 O ASP A 62 53.676 14.287 33.481 1.00 11.17 A O ANISOU 506 O ASP A 62 1766 660 1815 -136 189 139 A O ATOM 507 CB ASP A 62 50.707 15.039 33.061 1.00 12.50 A C ANISOU 507 CB ASP A 62 1883 849 2013 135 18 -25 A C ATOM 508 CG ASP A 62 49.684 14.081 33.642 1.00 13.37 A C ANISOU 508 CG ASP A 62 1876 1218 1983 34 211 -2 A C ATOM 509 OD1 ASP A 62 49.642 13.879 34.856 1.00 12.87 A O ANISOU 509 OD1 ASP A 62 1981 787 2119 -196 92 -13 A O ATOM 510 OD2 ASP A 62 48.883 13.602 32.887 1.00 13.19 A O ANISOU 510 OD2 ASP A 62 1811 1047 2150 -262 141 81 A O ATOM 511 N SER A 63 52.769 14.041 35.560 1.00 11.85 A N ANISOU 511 N SER A 63 1675 1089 1738 -109 -12 34 A N ATOM 512 CA SER A 63 53.674 12.955 35.969 1.00 10.98 A C ANISOU 512 CA SER A 63 1758 850 1563 -180 115 27 A C ATOM 513 C SER A 63 52.916 11.675 36.348 1.00 10.94 A C ANISOU 513 C SER A 63 1545 877 1733 -104 -16 171 A C ATOM 514 O SER A 63 53.548 10.716 36.817 1.00 11.77 A O ANISOU 514 O SER A 63 1655 795 2018 -19 -177 -22 A O ATOM 515 CB SER A 63 54.547 13.451 37.140 1.00 11.87 A C ANISOU 515 CB SER A 63 1697 996 1817 -215 -32 -21 A C ATOM 516 OG SER A 63 53.751 13.968 38.197 1.00 11.79 A O ANISOU 516 OG SER A 63 1783 977 1716 -204 -53 -129 A O ATOM 517 N VAL A 64 51.583 11.643 36.112 1.00 10.96 A N ANISOU 517 N VAL A 64 1551 702 1910 -100 198 195 A N ATOM 518 CA VAL A 64 50.758 10.515 36.537 1.00 11.31 A C ANISOU 518 CA VAL A 64 1827 747 1721 -286 77 148 A C ATOM 519 C VAL A 64 49.889 10.054 35.376 1.00 11.06 A C ANISOU 519 C VAL A 64 1411 1065 1725 -146 264 35 A C ATOM 520 O VAL A 64 49.071 10.804 34.843 1.00 12.01 A O ANISOU 520 O VAL A 64 1802 741 2021 -236 98 78 A O ATOM 521 CB VAL A 64 49.870 10.910 37.738 1.00 12.68 A C ANISOU 521 CB VAL A 64 2078 1122 1617 -335 248 177 A C ATOM 522 CG1 VAL A 64 48.935 9.753 38.121 1.00 16.45 A C ANISOU 522 CG1 VAL A 64 2821 1516 1913 -827 913 -231 A C ATOM 523 CG2 VAL A 64 50.708 11.336 38.924 1.00 14.56 A C ANISOU 523 CG2 VAL A 64 2648 976 1906 -200 43 54 A C ATOM 524 N LEU A 65 50.052 8.767 35.047 1.00 10.97 A N ANISOU 524 N LEU A 65 1438 1027 1702 -150 156 -5 A N ATOM 525 CA LEU A 65 49.216 8.105 34.018 1.00 10.64 A C ANISOU 525 CA LEU A 65 1489 1089 1464 -136 227 32 A C ATOM 526 C LEU A 65 49.276 8.857 32.671 1.00 9.64 A C ANISOU 526 C LEU A 65 1467 727 1466 -100 163 -72 A C ATOM 527 O LEU A 65 48.236 9.050 31.990 1.00 11.38 A O ANISOU 527 O LEU A 65 1471 953 1898 -67 79 137 A O ATOM 528 CB LEU A 65 47.793 7.917 34.547 1.00 11.07 A C ANISOU 528 CB LEU A 65 1531 973 1699 -185 286 -99 A C ATOM 529 CG LEU A 65 47.689 6.996 35.777 1.00 11.01 A C ANISOU 529 CG LEU A 65 1429 920 1835 -293 39 57 A C ATOM 530 CD1 LEU A 65 46.318 7.147 36.442 1.00 11.99 A C ANISOU 530 CD1 LEU A 65 1719 1008 1826 -244 204 37 A C ATOM 531 CD2 LEU A 65 47.942 5.520 35.465 1.00 11.10 A C ANISOU 531 CD2 LEU A 65 1589 1050 1579 -346 93 -203 A C ATOM 532 N VAL A 66 50.508 9.165 32.252 1.00 10.25 A N ANISOU 532 N VAL A 66 1290 886 1718 12 44 -162 A N ATOM 533 CA VAL A 66 50.733 9.800 30.954 1.00 11.17 A C ANISOU 533 CA VAL A 66 1297 1185 1760 189 47 -119 A C ATOM 534 C VAL A 66 50.742 8.720 29.880 1.00 10.10 A C ANISOU 534 C VAL A 66 1461 642 1734 93 6 113 A C ATOM 535 O VAL A 66 50.863 7.528 30.191 1.00 10.97 A O ANISOU 535 O VAL A 66 1803 630 1732 100 101 206 A O ATOM 536 CB VAL A 66 52.040 10.616 30.922 1.00 12.17 A C ANISOU 536 CB VAL A 66 1692 925 2006 -83 156 10 A C ATOM 537 CG1 VAL A 66 52.148 11.555 32.135 1.00 13.19 A C ANISOU 537 CG1 VAL A 66 1783 1066 2160 50 201 -88 A C ATOM 538 CG2 VAL A 66 53.267 9.737 30.806 1.00 12.00 A C ANISOU 538 CG2 VAL A 66 1422 1260 1875 -263 74 45 A C ATOM 539 N PRO A 67 50.563 9.061 28.591 1.00 11.04 A N ANISOU 539 N PRO A 67 1721 692 1779 114 83 189 A N ATOM 540 CA PRO A 67 50.503 8.044 27.558 1.00 12.47 A C ANISOU 540 CA PRO A 67 1708 1305 1723 17 -50 28 A C ATOM 541 C PRO A 67 51.788 7.258 27.307 1.00 11.74 A C ANISOU 541 C PRO A 67 1830 596 2033 -11 99 299 A C ATOM 542 O PRO A 67 52.891 7.735 27.522 1.00 12.78 A O ANISOU 542 O PRO A 67 1703 1025 2126 67 60 -84 A O ATOM 543 CB PRO A 67 50.132 8.824 26.293 1.00 12.69 A C ANISOU 543 CB PRO A 67 1890 1012 1919 379 12 62 A C ATOM 544 CG PRO A 67 49.533 10.114 26.808 1.00 12.36 A C ANISOU 544 CG PRO A 67 2052 715 1929 267 11 213 A C ATOM 545 CD PRO A 67 50.329 10.410 28.069 1.00 11.64 A C ANISOU 545 CD PRO A 67 1721 748 1952 165 78 232 A C ATOM 546 N TRP A 68 51.597 5.972 26.961 1.00 10.93 A N ANISOU 546 N TRP A 68 1701 694 1757 -108 317 218 A N ATOM 547 CA TRP A 68 52.713 5.211 26.401 1.00 11.16 A C ANISOU 547 CA TRP A 68 1387 1026 1826 -107 110 171 A C ATOM 548 C TRP A 68 53.213 5.936 25.152 1.00 11.66 A C ANISOU 548 C TRP A 68 1874 640 1913 92 158 121 A C ATOM 549 O TRP A 68 52.406 6.220 24.282 1.00 12.72 A O ANISOU 549 O TRP A 68 2051 986 1794 -11 90 82 A O ATOM 550 CB TRP A 68 52.217 3.809 26.063 1.00 12.10 A C ANISOU 550 CB TRP A 68 1814 932 1850 -234 427 175 A C ATOM 551 CG TRP A 68 53.257 2.939 25.422 1.00 11.82 A C ANISOU 551 CG TRP A 68 1571 965 1952 -86 203 199 A C ATOM 552 CD1 TRP A 68 53.292 2.523 24.111 1.00 12.56 A C ANISOU 552 CD1 TRP A 68 1647 1078 2045 103 247 130 A C ATOM 553 CD2 TRP A 68 54.425 2.403 26.058 1.00 11.66 A C ANISOU 553 CD2 TRP A 68 1786 792 1850 -100 189 19 A C ATOM 554 CE2 TRP A 68 55.120 1.668 25.063 1.00 12.76 A C ANISOU 554 CE2 TRP A 68 1812 1055 1980 31 255 -37 A C ATOM 555 CE3 TRP A 68 54.952 2.490 27.347 1.00 12.10 A C ANISOU 555 CE3 TRP A 68 1682 1096 1817 77 339 120 A C ATOM 556 NE1 TRP A 68 54.418 1.769 23.889 1.00 12.50 A N ANISOU 556 NE1 TRP A 68 2000 972 1777 193 411 -118 A N ATOM 557 CZ2 TRP A 68 56.330 1.045 25.342 1.00 13.48 A C ANISOU 557 CZ2 TRP A 68 2028 1033 2058 164 360 112 A C ATOM 558 CZ3 TRP A 68 56.141 1.857 27.615 1.00 12.87 A C ANISOU 558 CZ3 TRP A 68 1790 1340 1760 81 -79 77 A C ATOM 559 CH2 TRP A 68 56.821 1.147 26.618 1.00 14.11 A C ANISOU 559 CH2 TRP A 68 1878 1358 2123 32 269 119 A C ATOM 560 N PRO A 69 54.502 6.265 25.060 1.00 12.75 A N ANISOU 560 N PRO A 69 1875 941 2029 -163 131 122 A N ATOM 561 CA PRO A 69 54.969 7.106 23.946 1.00 14.34 A C ANISOU 561 CA PRO A 69 1959 1598 1890 -49 287 146 A C ATOM 562 C PRO A 69 55.454 6.385 22.687 1.00 14.18 A C ANISOU 562 C PRO A 69 1998 1198 2189 -4 463 80 A C ATOM 563 O PRO A 69 55.732 6.988 21.684 1.00 18.40 A O ANISOU 563 O PRO A 69 2935 1511 2544 28 836 194 A O ATOM 564 CB PRO A 69 56.169 7.835 24.578 1.00 15.86 A C ANISOU 564 CB PRO A 69 1820 1666 2537 -18 331 223 A C ATOM 565 CG PRO A 69 56.737 6.789 25.532 1.00 15.07 A C ANISOU 565 CG PRO A 69 1878 1431 2415 71 347 14 A C ATOM 566 CD PRO A 69 55.508 6.116 26.125 1.00 13.63 A C ANISOU 566 CD PRO A 69 1909 1091 2179 -22 191 99 A C ATOM 567 N SER A 70 55.580 5.062 22.762 1.00 16.12 A N ANISOU 567 N SER A 70 2367 1058 2700 -224 567 -160 A N ATOM 568 CA SER A 70 56.202 4.294 21.665 1.00 16.26 A C ANISOU 568 CA SER A 70 2406 1547 2224 -61 384 22 A C ATOM 569 C SER A 70 55.101 3.528 20.906 1.00 16.41 A C ANISOU 569 C SER A 70 2650 1412 2170 -75 519 14 A C ATOM 570 O SER A 70 53.889 3.721 21.123 1.00 16.61 A O ANISOU 570 O SER A 70 2650 1314 2346 46 276 -54 A O ATOM 571 CB SER A 70 57.309 3.415 22.250 1.00 16.78 A C ANISOU 571 CB SER A 70 2308 1748 2320 138 435 -202 A C ATOM 572 OG SER A 70 57.989 2.630 21.273 1.00 18.79 A O ANISOU 572 OG SER A 70 2746 1597 2793 225 585 -362 A O ATOM 573 N SER A 71 55.513 2.690 19.948 1.00 17.55 A N ANISOU 573 N SER A 71 2932 1670 2065 -146 810 -75 A N ATOM 574 CA SER A 71 54.561 1.820 19.286 1.00 17.76 A C ANISOU 574 CA SER A 71 3073 1485 2191 -250 670 56 A C ATOM 575 C SER A 71 54.057 0.783 20.302 1.00 15.32 A C ANISOU 575 C SER A 71 2761 975 2082 112 343 15 A C ATOM 576 O SER A 71 54.712 0.503 21.306 1.00 15.06 A O ANISOU 576 O SER A 71 2511 1168 2042 65 295 -98 A O ATOM 577 CB SER A 71 55.182 1.137 18.094 1.00 20.47 A C ANISOU 577 CB SER A 71 3293 2092 2392 -7 582 -349 A C ATOM 578 OG SER A 71 56.365 0.501 18.500 1.00 23.82 A O ANISOU 578 OG SER A 71 3797 2501 2751 245 861 -391 A O ATOM 579 N PRO A 72 52.858 0.239 20.091 1.00 17.14 A N ANISOU 579 N PRO A 72 2714 1237 2559 -149 457 218 A N ATOM 580 CA PRO A 72 52.315 -0.786 21.005 1.00 15.96 A C ANISOU 580 CA PRO A 72 2650 1311 2100 -6 328 228 A C ATOM 581 C PRO A 72 53.246 -1.983 21.202 1.00 15.29 A C ANISOU 581 C PRO A 72 2545 1380 1883 -19 446 227 A C ATOM 582 O PRO A 72 53.923 -2.415 20.267 1.00 17.05 A O ANISOU 582 O PRO A 72 2888 1330 2259 40 644 19 A O ATOM 583 CB PRO A 72 51.002 -1.212 20.348 1.00 17.33 A C ANISOU 583 CB PRO A 72 2503 1609 2471 -132 425 168 A C ATOM 584 CG PRO A 72 50.631 -0.038 19.454 1.00 20.21 A C ANISOU 584 CG PRO A 72 2735 1790 3152 35 -23 325 A C ATOM 585 CD PRO A 72 51.950 0.520 18.967 1.00 20.80 A C ANISOU 585 CD PRO A 72 3367 1667 2868 -74 369 262 A C ATOM 586 N LEU A 73 53.338 -2.434 22.441 1.00 15.07 A N ANISOU 586 N LEU A 73 2607 1339 1779 131 689 23 A N ATOM 587 CA LEU A 73 54.085 -3.649 22.756 1.00 14.38 A C ANISOU 587 CA LEU A 73 2320 1121 2023 -61 502 208 A C ATOM 588 C LEU A 73 53.301 -4.884 22.293 1.00 15.89 A C ANISOU 588 C LEU A 73 2379 1507 2150 -120 549 -49 A C ATOM 589 O LEU A 73 52.095 -4.946 22.373 1.00 17.38 A O ANISOU 589 O LEU A 73 2497 1599 2504 -256 170 -69 A O ATOM 590 CB LEU A 73 54.348 -3.711 24.262 1.00 14.87 A C ANISOU 590 CB LEU A 73 2317 1288 2043 -282 421 354 A C ATOM 591 CG LEU A 73 55.219 -2.588 24.815 1.00 15.83 A C ANISOU 591 CG LEU A 73 2507 1431 2074 -398 302 327 A C ATOM 592 CD1 LEU A 73 55.073 -2.489 26.315 1.00 18.27 A C ANISOU 592 CD1 LEU A 73 3434 1371 2134 -205 24 181 A C ATOM 593 CD2 LEU A 73 56.671 -2.799 24.428 1.00 18.89 A C ANISOU 593 CD2 LEU A 73 2664 1649 2863 -251 337 466 A C ATOM 594 N GLN A 74 54.043 -5.854 21.774 1.00 15.74 A N ANISOU 594 N GLN A 74 2524 1293 2163 -108 688 78 A N ATOM 595 CA GLN A 74 53.460 -7.159 21.393 1.00 16.43 A C ANISOU 595 CA GLN A 74 2569 1294 2377 -99 393 148 A C ATOM 596 C GLN A 74 53.414 -8.114 22.607 1.00 15.24 A C ANISOU 596 C GLN A 74 2766 980 2044 70 123 -149 A C ATOM 597 O GLN A 74 54.147 -7.955 23.596 1.00 14.73 A O ANISOU 597 O GLN A 74 2643 1047 1905 208 238 -2 A O ATOM 598 CB GLN A 74 54.299 -7.705 20.226 1.00 19.39 A C ANISOU 598 CB GLN A 74 3625 1602 2137 -227 434 -356 A C ATOM 599 CG GLN A 74 54.199 -6.833 18.981 1.00 24.43 A C ANISOU 599 CG GLN A 74 4561 2168 2550 -416 854 133 A C ATOM 600 CD GLN A 74 54.915 -7.420 17.792 1.00 34.45 A C ANISOU 600 CD GLN A 74 6071 4209 2809 -187 1295 -257 A C ATOM 601 NE2 GLN A 74 55.359 -6.570 16.892 1.00 48.06 A N ANISOU 601 NE2 GLN A 74 7701 6320 4240 -662 1017 1243 A N ATOM 602 OE1 GLN A 74 55.064 -8.624 17.679 1.00 49.14 A O ANISOU 602 OE1 GLN A 74 8903 5482 4285 1478 1065 -891 A O ATOM 603 N SER A 75 52.663 -9.217 22.461 1.00 17.08 A N ANISOU 603 N SER A 75 2862 1407 2218 -140 147 -182 A N ATOM 604 CA SER A 75 52.646 -10.279 23.461 1.00 16.51 A C ANISOU 604 CA SER A 75 2703 1620 1950 18 400 -285 A C ATOM 605 C SER A 75 54.071 -10.784 23.689 1.00 14.70 A C ANISOU 605 C SER A 75 2748 1012 1822 -164 281 7 A C ATOM 606 O SER A 75 54.784 -11.119 22.706 1.00 16.97 A O ANISOU 606 O SER A 75 2984 1192 2271 -60 623 -167 A O ATOM 607 CB SER A 75 51.756 -11.404 22.962 1.00 17.99 A C ANISOU 607 CB SER A 75 3154 1506 2172 -104 471 -268 A C ATOM 608 OG SER A 75 51.863 -12.520 23.846 1.00 17.76 A O ANISOU 608 OG SER A 75 3061 1595 2091 -252 494 -137 A O ATOM 609 N GLY A 76 54.497 -10.850 24.956 1.00 14.24 A N ANISOU 609 N GLY A 76 2511 1044 1853 41 435 -60 A N ATOM 610 CA GLY A 76 55.824 -11.339 25.286 1.00 16.51 A C ANISOU 610 CA GLY A 76 2505 1536 2230 -89 338 -145 A C ATOM 611 C GLY A 76 56.971 -10.395 24.964 1.00 15.20 A C ANISOU 611 C GLY A 76 2161 1284 2331 145 332 -79 A C ATOM 612 O GLY A 76 58.140 -10.767 25.151 1.00 18.16 A O ANISOU 612 O GLY A 76 2002 1708 3188 74 564 112 A O ATOM 613 N GLU A 77 56.685 -9.146 24.557 1.00 15.68 A N ANISOU 613 N GLU A 77 2259 1242 2454 59 467 33 A N ATOM 614 CA GLU A 77 57.746 -8.214 24.156 1.00 16.86 A C ANISOU 614 CA GLU A 77 2166 2066 2174 -150 520 -1 A C ATOM 615 C GLU A 77 58.109 -7.316 25.333 1.00 16.38 A C ANISOU 615 C GLU A 77 2235 1720 2269 63 254 39 A C ATOM 616 O GLU A 77 57.248 -6.569 25.844 1.00 17.37 A O ANISOU 616 O GLU A 77 2088 1886 2626 -61 599 -6 A O ATOM 617 CB GLU A 77 57.298 -7.324 23.001 1.00 17.83 A C ANISOU 617 CB GLU A 77 2426 1847 2502 83 476 -16 A C ATOM 618 CG GLU A 77 58.414 -6.406 22.507 1.00 18.45 A C ANISOU 618 CG GLU A 77 2718 2002 2288 -363 397 -58 A C ATOM 619 CD GLU A 77 58.028 -5.420 21.418 1.00 20.39 A C ANISOU 619 CD GLU A 77 2558 1929 3257 32 561 264 A C ATOM 620 OE1 GLU A 77 56.819 -5.302 21.104 1.00 20.44 A O ANISOU 620 OE1 GLU A 77 2669 1866 3229 28 810 136 A O ATOM 621 OE2 GLU A 77 58.979 -4.805 20.851 1.00 21.30 A O ANISOU 621 OE2 GLU A 77 2854 2253 2985 25 957 278 A O ATOM 622 N GLU A 78 59.366 -7.391 25.764 1.00 15.46 A N ANISOU 622 N GLU A 78 2066 1298 2507 59 609 -95 A N ATOM 623 CA GLU A 78 59.855 -6.549 26.863 1.00 15.48 A C ANISOU 623 CA GLU A 78 1858 1785 2236 -162 287 46 A C ATOM 624 C GLU A 78 60.439 -5.242 26.319 1.00 16.84 A C ANISOU 624 C GLU A 78 2297 1400 2701 156 701 -183 A C ATOM 625 O GLU A 78 61.228 -5.240 25.352 1.00 20.36 A O ANISOU 625 O GLU A 78 2948 1694 3093 40 1101 -252 A O ATOM 626 CB GLU A 78 60.962 -7.261 27.639 1.00 16.15 A C ANISOU 626 CB GLU A 78 1821 1696 2618 101 473 30 A C ATOM 627 CG GLU A 78 61.450 -6.566 28.881 1.00 18.11 A C ANISOU 627 CG GLU A 78 1922 1769 3190 -96 103 -39 A C ATOM 628 CD GLU A 78 62.634 -7.252 29.535 1.00 20.20 A C ANISOU 628 CD GLU A 78 2507 2293 2874 651 383 8 A C ATOM 629 OE1 GLU A 78 63.763 -7.117 28.995 1.00 26.15 A O ANISOU 629 OE1 GLU A 78 2707 3310 3916 567 701 445 A O ATOM 630 OE2 GLU A 78 62.439 -7.850 30.608 1.00 20.96 A O ANISOU 630 OE2 GLU A 78 2475 2003 3484 69 11 463 A O ATOM 631 N ALA A 79 60.088 -4.156 27.010 1.00 13.92 A N ANISOU 631 N ALA A 79 1732 1195 2362 -112 383 -157 A N ATOM 632 CA ALA A 79 60.800 -2.875 26.859 1.00 14.37 A C ANISOU 632 CA ALA A 79 1658 1332 2468 -196 364 -91 A C ATOM 633 C ALA A 79 61.441 -2.490 28.192 1.00 15.06 A C ANISOU 633 C ALA A 79 1960 1254 2506 230 419 -219 A C ATOM 634 O ALA A 79 60.889 -2.768 29.295 1.00 14.90 A O ANISOU 634 O ALA A 79 1900 1421 2341 -15 239 -64 A O ATOM 635 CB ALA A 79 59.865 -1.797 26.383 1.00 17.82 A C ANISOU 635 CB ALA A 79 2259 1752 2760 -180 -154 176 A C ATOM 636 N THR A 80 62.558 -1.753 28.088 1.00 15.19 A N ANISOU 636 N THR A 80 2007 1384 2380 81 632 32 A N ATOM 637 CA THR A 80 63.210 -1.194 29.259 1.00 14.97 A C ANISOU 637 CA THR A 80 1596 1392 2699 -104 333 116 A C ATOM 638 C THR A 80 63.018 0.319 29.197 1.00 14.74 A C ANISOU 638 C THR A 80 1821 1466 2312 -54 287 -90 A C ATOM 639 O THR A 80 63.254 0.893 28.166 1.00 15.77 A O ANISOU 639 O THR A 80 2004 1510 2476 175 452 -79 A O ATOM 640 CB THR A 80 64.694 -1.588 29.314 1.00 14.64 A C ANISOU 640 CB THR A 80 1723 1080 2758 -11 210 52 A C ATOM 641 CG2 THR A 80 65.411 -1.043 30.520 1.00 18.38 A C ANISOU 641 CG2 THR A 80 1964 1803 3216 -104 -114 7 A C ATOM 642 OG1 THR A 80 64.736 -3.015 29.336 1.00 17.40 A O ANISOU 642 OG1 THR A 80 2316 1077 3216 170 246 -11 A O ATOM 643 N VAL A 81 62.590 0.908 30.320 1.00 12.79 A N ANISOU 643 N VAL A 81 1801 856 2202 187 418 344 A N ATOM 644 CA VAL A 81 62.130 2.292 30.338 1.00 13.27 A C ANISOU 644 CA VAL A 81 1863 882 2295 247 232 227 A C ATOM 645 C VAL A 81 62.874 3.068 31.398 1.00 14.23 A C ANISOU 645 C VAL A 81 1664 1432 2310 -68 416 322 A C ATOM 646 O VAL A 81 63.058 2.586 32.515 1.00 13.79 A O ANISOU 646 O VAL A 81 1916 1062 2261 12 86 173 A O ATOM 647 CB VAL A 81 60.613 2.328 30.590 1.00 12.35 A C ANISOU 647 CB VAL A 81 1878 837 1977 132 268 344 A C ATOM 648 CG1 VAL A 81 60.150 3.765 30.785 1.00 14.24 A C ANISOU 648 CG1 VAL A 81 1732 911 2766 184 408 343 A C ATOM 649 CG2 VAL A 81 59.870 1.700 29.415 1.00 15.16 A C ANISOU 649 CG2 VAL A 81 1746 1579 2435 15 171 17 A C ATOM 650 N ARG A 82 63.269 4.312 31.042 1.00 13.86 A N ANISOU 650 N ARG A 82 1544 1469 2251 -216 437 251 A N ATOM 651 CA ARG A 82 63.713 5.284 32.038 1.00 14.78 A C ANISOU 651 CA ARG A 82 1529 1456 2630 25 221 10 A C ATOM 652 C ARG A 82 62.980 6.599 31.757 1.00 13.82 A C ANISOU 652 C ARG A 82 1501 1559 2190 -9 275 117 A C ATOM 653 O ARG A 82 62.555 6.820 30.636 1.00 13.59 A O ANISOU 653 O ARG A 82 1635 1322 2203 -135 211 -9 A O ATOM 654 CB ARG A 82 65.225 5.510 31.984 1.00 15.54 A C ANISOU 654 CB ARG A 82 1564 1329 3012 78 -38 -8 A C ATOM 655 CG ARG A 82 66.068 4.277 32.260 1.00 17.19 A C ANISOU 655 CG ARG A 82 1474 1529 3524 148 275 273 A C ATOM 656 CD ARG A 82 67.535 4.649 32.447 1.00 18.90 A C ANISOU 656 CD ARG A 82 1493 1925 3762 227 197 169 A C ATOM 657 NE ARG A 82 68.108 5.171 31.226 1.00 20.15 A N ANISOU 657 NE ARG A 82 1611 2292 3751 -148 410 -21 A N ATOM 658 CZ ARG A 82 69.254 5.884 31.185 1.00 22.41 A C ANISOU 658 CZ ARG A 82 1579 3073 3860 -314 486 147 A C ATOM 659 NH1 ARG A 82 69.934 6.112 32.302 1.00 24.58 A N ANISOU 659 NH1 ARG A 82 2182 3119 4036 59 253 -108 A N ATOM 660 NH2 ARG A 82 69.685 6.388 30.033 1.00 25.90 A N ANISOU 660 NH2 ARG A 82 2416 3443 3982 240 626 650 A N ATOM 661 N VAL A 83 62.844 7.422 32.800 1.00 13.46 A N ANISOU 661 N VAL A 83 1608 1287 2216 9 35 191 A N ATOM 662 CA VAL A 83 62.214 8.723 32.705 1.00 13.51 A C ANISOU 662 CA VAL A 83 1717 1294 2120 71 -28 143 A C ATOM 663 C VAL A 83 63.121 9.756 33.340 1.00 13.45 A C ANISOU 663 C VAL A 83 1373 1615 2122 -51 75 205 A C ATOM 664 O VAL A 83 63.771 9.498 34.328 1.00 14.36 A O ANISOU 664 O VAL A 83 1727 1270 2459 54 -172 19 A O ATOM 665 CB VAL A 83 60.835 8.710 33.393 1.00 14.23 A C ANISOU 665 CB VAL A 83 1855 1142 2407 30 282 -128 A C ATOM 666 CG1 VAL A 83 60.146 10.069 33.312 1.00 15.65 A C ANISOU 666 CG1 VAL A 83 1853 1473 2620 153 134 -10 A C ATOM 667 CG2 VAL A 83 59.963 7.591 32.829 1.00 14.75 A C ANISOU 667 CG2 VAL A 83 1693 1561 2347 -30 136 93 A C ATOM 668 N ARG A 84 63.055 10.985 32.824 1.00 13.67 A N ANISOU 668 N ARG A 84 1682 1392 2119 120 -88 -82 A N ATOM 669 CA ARG A 84 63.588 12.138 33.558 1.00 14.93 A C ANISOU 669 CA ARG A 84 1677 1613 2380 -62 -189 -55 A C ATOM 670 C ARG A 84 62.631 13.305 33.352 1.00 13.92 A C ANISOU 670 C ARG A 84 1679 1410 2198 -170 262 152 A C ATOM 671 O ARG A 84 61.942 13.388 32.377 1.00 14.22 A O ANISOU 671 O ARG A 84 1826 1198 2377 -182 147 -29 A O ATOM 672 CB ARG A 84 65.032 12.474 33.177 1.00 17.68 A C ANISOU 672 CB ARG A 84 1988 1365 3362 -78 340 -52 A C ATOM 673 CG ARG A 84 65.230 12.854 31.730 1.00 19.46 A C ANISOU 673 CG ARG A 84 2014 2021 3359 -75 417 -53 A C ATOM 674 CD ARG A 84 66.702 13.210 31.498 1.00 20.32 A C ANISOU 674 CD ARG A 84 1955 2524 3240 -114 286 187 A C ATOM 675 NE ARG A 84 66.914 13.609 30.129 1.00 22.32 A N ANISOU 675 NE ARG A 84 2145 2581 3754 -631 847 257 A N ATOM 676 CZ ARG A 84 68.044 14.134 29.672 1.00 27.94 A C ANISOU 676 CZ ARG A 84 2020 4264 4330 -1081 759 497 A C ATOM 677 NH1 ARG A 84 69.080 14.318 30.487 1.00 39.86 A N ANISOU 677 NH1 ARG A 84 3020 6736 5387 -1404 -208 486 A N ATOM 678 NH2 ARG A 84 68.110 14.478 28.401 1.00 32.53 A N ANISOU 678 NH2 ARG A 84 2596 5711 4053 -1195 572 600 A N ATOM 679 N SER A 85 62.641 14.166 34.350 1.00 14.94 A N ANISOU 679 N SER A 85 1665 1640 2372 -36 -38 -74 A N ATOM 680 CA SER A 85 61.684 15.237 34.483 1.00 14.50 A C ANISOU 680 CA SER A 85 1644 1378 2487 -51 -162 -109 A C ATOM 681 C SER A 85 62.437 16.575 34.602 1.00 16.21 A C ANISOU 681 C SER A 85 2100 1360 2698 -81 -149 -162 A C ATOM 682 O SER A 85 63.451 16.665 35.284 1.00 17.85 A O ANISOU 682 O SER A 85 2335 1364 3082 -65 -394 -74 A O ATOM 683 CB SER A 85 60.798 14.949 35.666 1.00 15.87 A C ANISOU 683 CB SER A 85 2249 1333 2445 90 -34 -225 A C ATOM 684 OG SER A 85 59.922 16.024 35.899 1.00 16.32 A O ANISOU 684 OG SER A 85 2197 1180 2822 -133 109 -284 A O ATOM 685 N PHE A 86 61.899 17.599 33.927 1.00 14.70 A N ANISOU 685 N PHE A 86 1646 1412 2528 -368 -193 34 A N ATOM 686 CA PHE A 86 62.457 18.938 33.855 1.00 14.84 A C ANISOU 686 CA PHE A 86 1582 1416 2639 -355 71 -134 A C ATOM 687 C PHE A 86 61.569 19.946 34.598 1.00 15.17 A C ANISOU 687 C PHE A 86 1768 1424 2572 -379 178 16 A C ATOM 688 O PHE A 86 60.369 20.027 34.350 1.00 14.70 A O ANISOU 688 O PHE A 86 1704 1221 2660 -248 101 -137 A O ATOM 689 CB PHE A 86 62.591 19.320 32.384 1.00 15.76 A C ANISOU 689 CB PHE A 86 1864 1377 2745 -318 230 -145 A C ATOM 690 CG PHE A 86 63.474 18.407 31.579 1.00 15.20 A C ANISOU 690 CG PHE A 86 1571 1659 2543 -285 362 -24 A C ATOM 691 CD1 PHE A 86 62.947 17.255 30.999 1.00 17.46 A C ANISOU 691 CD1 PHE A 86 1798 1979 2855 -475 370 -139 A C ATOM 692 CD2 PHE A 86 64.834 18.664 31.435 1.00 20.68 A C ANISOU 692 CD2 PHE A 86 1803 2389 3663 -560 465 -276 A C ATOM 693 CE1 PHE A 86 63.751 16.405 30.260 1.00 23.35 A C ANISOU 693 CE1 PHE A 86 2563 2611 3698 -170 625 -508 A C ATOM 694 CE2 PHE A 86 65.635 17.800 30.714 1.00 23.34 A C ANISOU 694 CE2 PHE A 86 1752 3011 4103 -78 398 -275 A C ATOM 695 CZ PHE A 86 65.091 16.681 30.122 1.00 23.48 A C ANISOU 695 CZ PHE A 86 2262 2825 3835 282 175 -431 A C ATOM 696 N GLY A 87 62.205 20.774 35.442 1.00 15.54 A N ANISOU 696 N GLY A 87 1679 1530 2692 -402 241 -137 A N ATOM 697 CA GLY A 87 61.479 21.750 36.265 1.00 16.60 A C ANISOU 697 CA GLY A 87 2037 1592 2677 -461 198 -236 A C ATOM 698 C GLY A 87 61.103 23.001 35.498 1.00 18.55 A C ANISOU 698 C GLY A 87 2200 1924 2923 -434 61 -88 A C ATOM 699 O GLY A 87 61.768 23.398 34.550 1.00 19.10 A O ANISOU 699 O GLY A 87 2274 1918 3064 -357 301 23 A O ATOM 700 N SER A 88 59.984 23.593 35.919 1.00 20.65 A N ANISOU 700 N SER A 88 2662 1575 3610 -122 459 181 A N ATOM 701 CA SER A 88 59.453 24.785 35.259 1.00 19.99 A C ANISOU 701 CA SER A 88 2576 1903 3113 -206 262 249 A C ATOM 702 C SER A 88 60.397 25.969 35.402 1.00 26.34 A C ANISOU 702 C SER A 88 3173 2591 4243 -799 139 181 A C ATOM 703 O SER A 88 60.297 26.880 34.594 1.00 34.05 A O ANISOU 703 O SER A 88 4478 2255 6205 -416 596 927 A O ATOM 704 CB SER A 88 58.067 25.118 35.734 1.00 23.27 A C ANISOU 704 CB SER A 88 2764 2640 3436 383 129 -428 A C ATOM 705 OG SER A 88 58.091 25.459 37.087 1.00 27.47 A O ANISOU 705 OG SER A 88 3587 3397 3453 392 399 -222 A O ATOM 706 N ASP A 89 61.243 25.977 36.436 1.00 26.16 A N ANISOU 706 N ASP A 89 3795 1680 4461 -192 -96 -749 A N ATOM 707 CA ASP A 89 62.113 27.157 36.693 1.00 36.67 A C ANISOU 707 CA ASP A 89 4464 3163 6305 -1088 -171 -1430 A C ATOM 708 C ASP A 89 63.385 27.053 35.852 1.00 37.08 A C ANISOU 708 C ASP A 89 4959 3165 5965 -817 214 -812 A C ATOM 709 O ASP A 89 64.255 27.905 35.938 1.00 47.63 A O ANISOU 709 O ASP A 89 4671 4682 8742 -1452 -601 247 A O ATOM 710 CB ASP A 89 62.458 27.311 38.183 1.00 43.80 A C ANISOU 710 CB ASP A 89 4411 6288 5943 -596 -17 -2061 A C ATOM 711 CG ASP A 89 63.064 26.070 38.835 1.00 49.97 A C ANISOU 711 CG ASP A 89 5927 7561 5496 523 -41 -2565 A C ATOM 712 OD1 ASP A 89 63.638 25.222 38.106 1.00 54.01 A O ANISOU 712 OD1 ASP A 89 5847 9228 5447 3440 -1553 -2591 A O ATOM 713 OD2 ASP A 89 62.946 25.944 40.082 1.00 68.68 A O ANISOU 713 OD2 ASP A 89 9155 11131 5810 -1546 788 -2325 A O ATOM 714 N GLY A 90 63.537 25.922 35.155 1.00 37.00 A N ANISOU 714 N GLY A 90 4077 3884 6096 -482 -197 -1148 A N ATOM 715 CA GLY A 90 64.699 25.669 34.308 1.00 40.39 A C ANISOU 715 CA GLY A 90 4694 3838 6812 -604 352 -283 A C ATOM 716 C GLY A 90 65.968 25.426 35.108 1.00 43.61 A C ANISOU 716 C GLY A 90 4186 5093 7291 -658 461 215 A C ATOM 717 O GLY A 90 67.044 25.417 34.529 1.00 60.13 A O ANISOU 717 O GLY A 90 4435 7825 10586 -879 1700 234 A O ATOM 718 N GLN A 91 65.836 25.232 36.431 1.00 43.82 A N ANISOU 718 N GLN A 91 5377 3836 7436 -982 -415 914 A N ATOM 719 CA GLN A 91 66.988 25.104 37.362 1.00 44.78 A C ANISOU 719 CA GLN A 91 4981 3310 8723 -1667 -716 408 A C ATOM 720 C GLN A 91 67.060 23.719 38.030 1.00 45.66 A C ANISOU 720 C GLN A 91 3940 3963 9444 -1102 401 1257 A C ATOM 721 O GLN A 91 68.192 23.262 38.302 1.00 58.95 A O ANISOU 721 O GLN A 91 4024 5797 12576 -798 -1147 868 A O ATOM 722 CB GLN A 91 66.945 26.206 38.422 1.00 56.32 A C ANISOU 722 CB GLN A 91 7223 3661 10514 -1782 -299 -607 A C ATOM 723 CG GLN A 91 67.195 27.594 37.847 1.00 67.42 A C ANISOU 723 CG GLN A 91 10727 4192 10695 -1013 -301 505 A C ATOM 724 CD GLN A 91 67.258 28.662 38.912 1.00 74.22 A C ANISOU 724 CD GLN A 91 11381 5325 11492 -3575 -390 304 A C ATOM 725 NE2 GLN A 91 67.995 29.719 38.622 1.00 77.19 A N ANISOU 725 NE2 GLN A 91 9331 9281 10714 -4306 2506 2185 A N ATOM 726 OE1 GLN A 91 66.652 28.548 39.979 1.00 92.03 A O ANISOU 726 OE1 GLN A 91 12363 10807 11796 -801 438 -346 A O ATOM 727 N HIS A 92 65.919 23.073 38.341 1.00 34.64 A N ANISOU 727 N HIS A 92 3317 1796 8045 -1569 -929 -1392 A N ATOM 728 CA HIS A 92 66.016 21.739 38.963 1.00 27.51 A C ANISOU 728 CA HIS A 92 2709 3385 4357 -1205 -539 -663 A C ATOM 729 C HIS A 92 65.387 20.668 38.056 1.00 21.42 A C ANISOU 729 C HIS A 92 2098 2163 3876 -596 223 -604 A C ATOM 730 O HIS A 92 64.159 20.634 37.871 1.00 20.72 A O ANISOU 730 O HIS A 92 2062 2098 3712 -335 146 -570 A O ATOM 731 CB HIS A 92 65.347 21.682 40.332 1.00 34.01 A C ANISOU 731 CB HIS A 92 3397 4797 4725 -1551 -126 -1289 A C ATOM 732 CG HIS A 92 65.948 22.535 41.382 1.00 36.95 A C ANISOU 732 CG HIS A 92 4034 5213 4791 -1862 -125 -1391 A C ATOM 733 CD2 HIS A 92 66.962 22.295 42.242 1.00 41.92 A C ANISOU 733 CD2 HIS A 92 5074 5408 5446 -1427 -933 -1240 A C ATOM 734 ND1 HIS A 92 65.448 23.796 41.678 1.00 47.19 A N ANISOU 734 ND1 HIS A 92 5568 6198 6162 -1053 -139 -2061 A N ATOM 735 CE1 HIS A 92 66.162 24.321 42.663 1.00 52.02 A C ANISOU 735 CE1 HIS A 92 6649 6120 6995 -382 -563 -3392 A C ATOM 736 NE2 HIS A 92 67.098 23.412 43.033 1.00 48.58 A N ANISOU 736 NE2 HIS A 92 5592 6367 6496 -1463 -720 -2178 A N ATOM 737 N ASP A 93 66.234 19.811 37.478 1.00 19.71 A N ANISOU 737 N ASP A 93 1721 2364 3403 -631 141 -602 A N ATOM 738 CA ASP A 93 65.816 18.655 36.665 1.00 18.91 A C ANISOU 738 CA ASP A 93 2176 1963 3045 -612 -142 -222 A C ATOM 739 C ASP A 93 66.256 17.378 37.379 1.00 19.46 A C ANISOU 739 C ASP A 93 2072 2169 3151 -368 -559 -321 A C ATOM 740 O ASP A 93 67.237 17.399 38.142 1.00 21.38 A O ANISOU 740 O ASP A 93 2337 2038 3746 -502 -823 -158 A O ATOM 741 CB ASP A 93 66.477 18.681 35.286 1.00 21.43 A C ANISOU 741 CB ASP A 93 1870 2693 3578 -42 194 -158 A C ATOM 742 CG ASP A 93 66.222 19.948 34.489 1.00 24.80 A C ANISOU 742 CG ASP A 93 2836 2643 3942 -88 471 -73 A C ATOM 743 OD1 ASP A 93 65.149 20.542 34.678 1.00 22.28 A O ANISOU 743 OD1 ASP A 93 2203 1532 4728 -932 545 0 A O ATOM 744 OD2 ASP A 93 67.098 20.324 33.686 1.00 29.71 A O ANISOU 744 OD2 ASP A 93 2408 3657 5222 -204 571 496 A O ATOM 745 N THR A 94 65.531 16.268 37.165 1.00 18.58 A N ANISOU 745 N THR A 94 1735 2029 3296 -172 -487 -184 A N ATOM 746 CA THR A 94 65.933 14.994 37.733 1.00 18.46 A C ANISOU 746 CA THR A 94 2122 2180 2710 -126 -202 -238 A C ATOM 747 C THR A 94 67.012 14.343 36.881 1.00 17.44 A C ANISOU 747 C THR A 94 1739 1952 2932 -411 -161 -29 A C ATOM 748 O THR A 94 67.056 14.510 35.659 1.00 17.50 A O ANISOU 748 O THR A 94 1885 1796 2967 -194 -18 -101 A O ATOM 749 CB THR A 94 64.759 14.017 37.884 1.00 18.49 A C ANISOU 749 CB THR A 94 2214 2030 2780 -31 -57 65 A C ATOM 750 CG2 THR A 94 63.550 14.655 38.550 1.00 19.56 A C ANISOU 750 CG2 THR A 94 2483 2132 2817 111 -232 -613 A C ATOM 751 OG1 THR A 94 64.428 13.471 36.603 1.00 16.35 A O ANISOU 751 OG1 THR A 94 1670 1699 2841 -48 -53 -74 A O ATOM 752 N PRO A 95 67.879 13.520 37.510 1.00 18.87 A N ANISOU 752 N PRO A 95 2111 2020 3035 -253 -349 -149 A N ATOM 753 CA PRO A 95 68.610 12.517 36.751 1.00 19.15 A C ANISOU 753 CA PRO A 95 1705 2247 3323 -312 -19 -48 A C ATOM 754 C PRO A 95 67.626 11.534 36.096 1.00 17.81 A C ANISOU 754 C PRO A 95 1982 1781 3003 75 -193 -88 A C ATOM 755 O PRO A 95 66.445 11.467 36.455 1.00 17.27 A O ANISOU 755 O PRO A 95 1997 1630 2933 -30 -50 -206 A O ATOM 756 CB PRO A 95 69.442 11.781 37.812 1.00 22.95 A C ANISOU 756 CB PRO A 95 2208 2471 4038 143 -572 -292 A C ATOM 757 CG PRO A 95 69.430 12.665 39.038 1.00 24.18 A C ANISOU 757 CG PRO A 95 2661 2748 3778 257 -671 27 A C ATOM 758 CD PRO A 95 68.139 13.445 38.954 1.00 21.49 A C ANISOU 758 CD PRO A 95 2435 2406 3323 104 -305 -32 A C ATOM 759 N TRP A 96 68.129 10.738 35.160 1.00 17.66 A N ANISOU 759 N TRP A 96 1683 2015 3009 -214 80 -234 A N ATOM 760 CA TRP A 96 67.359 9.594 34.684 1.00 16.93 A C ANISOU 760 CA TRP A 96 1546 2063 2822 -99 6 -184 A C ATOM 761 C TRP A 96 67.030 8.679 35.853 1.00 18.13 A C ANISOU 761 C TRP A 96 1865 1934 3090 188 -144 25 A C ATOM 762 O TRP A 96 67.874 8.430 36.730 1.00 17.48 A O ANISOU 762 O TRP A 96 1679 1801 3159 -224 -44 -62 A O ATOM 763 CB TRP A 96 68.143 8.800 33.641 1.00 17.56 A C ANISOU 763 CB TRP A 96 1630 2298 2740 93 -195 -234 A C ATOM 764 CG TRP A 96 68.238 9.443 32.299 1.00 19.54 A C ANISOU 764 CG TRP A 96 2048 2634 2743 -67 548 -115 A C ATOM 765 CD1 TRP A 96 69.353 9.988 31.732 1.00 23.96 A C ANISOU 765 CD1 TRP A 96 2190 3250 3660 -723 373 -55 A C ATOM 766 CD2 TRP A 96 67.210 9.507 31.299 1.00 18.22 A C ANISOU 766 CD2 TRP A 96 1907 1868 3146 -242 354 -148 A C ATOM 767 CE2 TRP A 96 67.762 10.142 30.172 1.00 21.43 A C ANISOU 767 CE2 TRP A 96 2207 3018 2917 -179 512 -212 A C ATOM 768 CE3 TRP A 96 65.871 9.127 31.251 1.00 15.94 A C ANISOU 768 CE3 TRP A 96 1865 1443 2746 -178 480 -186 A C ATOM 769 NE1 TRP A 96 69.067 10.426 30.467 1.00 25.43 A N ANISOU 769 NE1 TRP A 96 2189 3820 3653 -441 786 -1 A N ATOM 770 CZ2 TRP A 96 67.014 10.393 29.020 1.00 20.14 A C ANISOU 770 CZ2 TRP A 96 2440 2241 2968 -459 508 219 A C ATOM 771 CZ3 TRP A 96 65.140 9.358 30.117 1.00 16.46 A C ANISOU 771 CZ3 TRP A 96 1977 1576 2701 36 415 -296 A C ATOM 772 CH2 TRP A 96 65.700 9.980 29.007 1.00 18.83 A C ANISOU 772 CH2 TRP A 96 2161 2019 2974 -64 381 75 A C ATOM 773 N SER A 97 65.795 8.194 35.840 1.00 15.96 A N ANISOU 773 N SER A 97 1791 1442 2831 222 -325 50 A N ATOM 774 CA SER A 97 65.344 7.204 36.776 1.00 16.92 A C ANISOU 774 CA SER A 97 1747 1617 3063 -62 -265 69 A C ATOM 775 C SER A 97 66.140 5.902 36.629 1.00 17.32 A C ANISOU 775 C SER A 97 1727 2118 2733 149 -251 -261 A C ATOM 776 O SER A 97 66.759 5.651 35.613 1.00 17.99 A O ANISOU 776 O SER A 97 1897 1663 3276 96 74 -226 A O ATOM 777 CB SER A 97 63.872 6.910 36.552 1.00 16.03 A C ANISOU 777 CB SER A 97 1824 1486 2781 -37 -274 9 A C ATOM 778 OG SER A 97 63.685 6.217 35.352 1.00 15.72 A O ANISOU 778 OG SER A 97 1784 1690 2498 -175 37 55 A O ATOM 779 N ASP A 98 66.063 5.070 37.665 1.00 17.24 A N ANISOU 779 N ASP A 98 1967 1684 2900 325 -135 -176 A N ATOM 780 CA ASP A 98 66.466 3.681 37.514 1.00 18.05 A C ANISOU 780 CA ASP A 98 2048 1710 3100 182 48 -204 A C ATOM 781 C ASP A 98 65.564 3.051 36.454 1.00 19.72 A C ANISOU 781 C ASP A 98 2134 1989 3369 56 -51 -387 A C ATOM 782 O ASP A 98 64.400 3.408 36.346 1.00 22.64 A O ANISOU 782 O ASP A 98 2142 2901 3558 129 -135 -672 A O ATOM 783 CB ASP A 98 66.361 2.916 38.828 1.00 22.06 A C ANISOU 783 CB ASP A 98 2870 2455 3057 97 -308 70 A C ATOM 784 CG ASP A 98 67.306 3.403 39.894 1.00 30.49 A C ANISOU 784 CG ASP A 98 4338 3586 3657 -204 -577 -880 A C ATOM 785 OD1 ASP A 98 68.340 4.028 39.534 1.00 34.25 A O ANISOU 785 OD1 ASP A 98 4195 4450 4367 -477 -1257 -500 A O ATOM 786 OD2 ASP A 98 66.982 3.185 41.085 1.00 43.47 A O ANISOU 786 OD2 ASP A 98 5791 7126 3597 -713 -660 -1105 A O ATOM 787 N ALA A 99 66.136 2.146 35.657 1.00 16.44 A N ANISOU 787 N ALA A 99 1745 1656 2843 -131 -81 -51 A N ATOM 788 CA ALA A 99 65.423 1.477 34.614 1.00 16.38 A C ANISOU 788 CA ALA A 99 1745 1678 2800 -174 -143 76 A C ATOM 789 C ALA A 99 64.424 0.467 35.206 1.00 15.30 A C ANISOU 789 C ALA A 99 1774 1729 2307 -130 -107 148 A C ATOM 790 O ALA A 99 64.668 -0.183 36.236 1.00 18.38 A O ANISOU 790 O ALA A 99 2059 2086 2837 -395 -478 548 A O ATOM 791 CB ALA A 99 66.407 0.772 33.692 1.00 19.52 A C ANISOU 791 CB ALA A 99 2161 2021 3232 29 -27 -251 A C ATOM 792 N VAL A 100 63.286 0.358 34.528 1.00 14.17 A N ANISOU 792 N VAL A 100 1758 927 2699 -25 -159 46 A N ATOM 793 CA VAL A 100 62.271 -0.643 34.832 1.00 14.11 A C ANISOU 793 CA VAL A 100 1776 1168 2416 -54 -1 199 A C ATOM 794 C VAL A 100 61.869 -1.316 33.518 1.00 14.77 A C ANISOU 794 C VAL A 100 1769 1514 2325 2 223 146 A C ATOM 795 O VAL A 100 62.061 -0.788 32.453 1.00 16.48 A O ANISOU 795 O VAL A 100 2509 1331 2421 -103 216 182 A O ATOM 796 CB VAL A 100 61.038 0.017 35.483 1.00 15.63 A C ANISOU 796 CB VAL A 100 1768 1622 2548 -226 290 232 A C ATOM 797 CG1 VAL A 100 61.348 0.592 36.850 1.00 18.85 A C ANISOU 797 CG1 VAL A 100 2455 1914 2792 -85 111 -19 A C ATOM 798 CG2 VAL A 100 60.408 1.091 34.609 1.00 16.78 A C ANISOU 798 CG2 VAL A 100 2142 1552 2682 -151 186 159 A C ATOM 799 N THR A 101 61.267 -2.504 33.635 1.00 16.08 A N ANISOU 799 N THR A 101 1902 1567 2639 -180 183 140 A N ATOM 800 CA THR A 101 60.818 -3.251 32.466 1.00 14.45 A C ANISOU 800 CA THR A 101 1621 1474 2394 39 300 132 A C ATOM 801 C THR A 101 59.280 -3.318 32.421 1.00 11.69 A C ANISOU 801 C THR A 101 1733 691 2016 -180 132 174 A C ATOM 802 O THR A 101 58.573 -3.226 33.442 1.00 13.86 A O ANISOU 802 O THR A 101 1704 1302 2261 -100 296 86 A O ATOM 803 CB THR A 101 61.418 -4.668 32.451 1.00 16.25 A C ANISOU 803 CB THR A 101 1857 1648 2669 263 199 -78 A C ATOM 804 CG2 THR A 101 62.923 -4.612 32.297 1.00 17.92 A C ANISOU 804 CG2 THR A 101 1979 1447 3381 -47 611 -121 A C ATOM 805 OG1 THR A 101 61.079 -5.344 33.662 1.00 18.34 A O ANISOU 805 OG1 THR A 101 2301 1713 2954 66 104 147 A O ATOM 806 N VAL A 102 58.778 -3.491 31.210 1.00 13.27 A N ANISOU 806 N VAL A 102 1870 1134 2037 -15 -3 56 A N ATOM 807 CA VAL A 102 57.354 -3.666 30.958 1.00 12.51 A C ANISOU 807 CA VAL A 102 1800 934 2018 -56 280 -43 A C ATOM 808 C VAL A 102 57.172 -4.672 29.818 1.00 12.35 A C ANISOU 808 C VAL A 102 1760 901 2029 -210 318 -20 A C ATOM 809 O VAL A 102 57.894 -4.632 28.848 1.00 13.72 A O ANISOU 809 O VAL A 102 2259 952 2000 -192 405 98 A O ATOM 810 CB VAL A 102 56.685 -2.309 30.675 1.00 12.88 A C ANISOU 810 CB VAL A 102 2038 941 1915 103 192 -99 A C ATOM 811 CG1 VAL A 102 57.330 -1.577 29.509 1.00 14.78 A C ANISOU 811 CG1 VAL A 102 2136 1248 2229 27 109 174 A C ATOM 812 CG2 VAL A 102 55.193 -2.463 30.447 1.00 13.61 A C ANISOU 812 CG2 VAL A 102 2150 1017 2001 197 145 26 A C ATOM 813 N GLU A 103 56.245 -5.622 29.998 1.00 11.93 A N ANISOU 813 N GLU A 103 1687 1070 1773 -234 421 22 A N ATOM 814 CA GLU A 103 56.107 -6.727 29.037 1.00 13.37 A C ANISOU 814 CA GLU A 103 1859 1400 1818 -71 266 -106 A C ATOM 815 C GLU A 103 54.680 -7.246 29.085 1.00 11.39 A C ANISOU 815 C GLU A 103 1686 951 1690 288 231 -54 A C ATOM 816 O GLU A 103 54.228 -7.701 30.144 1.00 12.89 A O ANISOU 816 O GLU A 103 1872 1151 1874 -122 329 21 A O ATOM 817 CB GLU A 103 57.056 -7.837 29.482 1.00 14.14 A C ANISOU 817 CB GLU A 103 1820 1247 2303 -289 145 206 A C ATOM 818 CG GLU A 103 57.019 -9.051 28.595 1.00 15.23 A C ANISOU 818 CG GLU A 103 2002 1429 2356 -140 64 39 A C ATOM 819 CD GLU A 103 58.014 -10.122 29.027 1.00 15.51 A C ANISOU 819 CD GLU A 103 2331 1038 2523 -239 197 93 A C ATOM 820 OE1 GLU A 103 59.124 -9.770 29.491 1.00 16.00 A O ANISOU 820 OE1 GLU A 103 2157 1177 2743 102 263 -18 A O ATOM 821 OE2 GLU A 103 57.664 -11.341 28.919 1.00 15.22 A O ANISOU 821 OE2 GLU A 103 2171 878 2733 -200 566 48 A O ATOM 822 N PRO A 104 53.921 -7.192 27.988 1.00 11.77 A N ANISOU 822 N PRO A 104 1938 921 1612 -35 177 -70 A N ATOM 823 CA PRO A 104 52.598 -7.797 27.983 1.00 11.65 A C ANISOU 823 CA PRO A 104 1721 844 1859 111 97 -51 A C ATOM 824 C PRO A 104 52.664 -9.324 28.058 1.00 11.28 A C ANISOU 824 C PRO A 104 1653 885 1748 14 258 128 A C ATOM 825 O PRO A 104 53.639 -9.949 27.614 1.00 13.47 A O ANISOU 825 O PRO A 104 1877 1006 2233 -49 412 -177 A O ATOM 826 CB PRO A 104 51.995 -7.363 26.650 1.00 12.84 A C ANISOU 826 CB PRO A 104 1910 985 1983 -150 60 -33 A C ATOM 827 CG PRO A 104 52.796 -6.133 26.273 1.00 13.34 A C ANISOU 827 CG PRO A 104 2245 1009 1812 -202 97 95 A C ATOM 828 CD PRO A 104 54.202 -6.478 26.719 1.00 13.11 A C ANISOU 828 CD PRO A 104 2017 1113 1851 -166 346 119 A C ATOM 829 N GLY A 105 51.556 -9.887 28.546 1.00 10.46 A N ANISOU 829 N GLY A 105 1660 689 1623 -69 183 -7 A N ATOM 830 CA GLY A 105 51.353 -11.332 28.613 1.00 11.49 A C ANISOU 830 CA GLY A 105 2095 636 1632 19 159 186 A C ATOM 831 C GLY A 105 50.803 -11.897 27.312 1.00 12.94 A C ANISOU 831 C GLY A 105 2026 1209 1678 -88 220 194 A C ATOM 832 O GLY A 105 51.177 -11.498 26.220 1.00 12.92 A O ANISOU 832 O GLY A 105 2153 1255 1499 -134 266 -84 A O ATOM 833 N LEU A 106 49.982 -12.931 27.466 1.00 12.25 A N ANISOU 833 N LEU A 106 2019 1049 1585 -132 155 76 A N ATOM 834 CA LEU A 106 49.344 -13.628 26.361 1.00 11.41 A C ANISOU 834 CA LEU A 106 1870 941 1522 -82 257 56 A C ATOM 835 C LEU A 106 47.983 -12.980 26.099 1.00 14.38 A C ANISOU 835 C LEU A 106 2054 1231 2179 -19 170 -5 A C ATOM 836 O LEU A 106 47.070 -13.074 26.931 1.00 16.22 A O ANISOU 836 O LEU A 106 2394 1255 2511 54 393 26 A O ATOM 837 CB LEU A 106 49.206 -15.118 26.726 1.00 13.37 A C ANISOU 837 CB LEU A 106 2166 936 1976 31 104 82 A C ATOM 838 CG LEU A 106 50.493 -15.837 27.081 1.00 11.98 A C ANISOU 838 CG LEU A 106 2245 637 1669 -7 -135 -7 A C ATOM 839 CD1 LEU A 106 50.229 -17.316 27.286 1.00 11.26 A C ANISOU 839 CD1 LEU A 106 1980 689 1609 -49 10 -36 A C ATOM 840 CD2 LEU A 106 51.548 -15.680 25.999 1.00 13.35 A C ANISOU 840 CD2 LEU A 106 2102 1131 1836 6 -194 59 A C ATOM 841 N LEU A 107 47.902 -12.224 25.001 1.00 14.93 A N ANISOU 841 N LEU A 107 2269 1481 1919 368 156 -120 A N ATOM 842 CA LEU A 107 46.808 -11.268 24.856 1.00 15.51 A C ANISOU 842 CA LEU A 107 2282 1272 2336 263 14 80 A C ATOM 843 C LEU A 107 45.570 -11.820 24.140 1.00 16.98 A C ANISOU 843 C LEU A 107 2153 1637 2660 67 81 37 A C ATOM 844 O LEU A 107 44.492 -11.271 24.278 1.00 21.11 A O ANISOU 844 O LEU A 107 2537 1851 3631 217 -174 -207 A O ATOM 845 CB LEU A 107 47.313 -10.040 24.103 1.00 16.57 A C ANISOU 845 CB LEU A 107 2745 1215 2333 207 -108 219 A C ATOM 846 CG LEU A 107 48.523 -9.337 24.696 1.00 17.78 A C ANISOU 846 CG LEU A 107 2653 1629 2470 47 113 -31 A C ATOM 847 CD1 LEU A 107 49.059 -8.281 23.741 1.00 19.44 A C ANISOU 847 CD1 LEU A 107 3004 1456 2925 -100 358 -123 A C ATOM 848 CD2 LEU A 107 48.131 -8.713 26.011 1.00 22.86 A C ANISOU 848 CD2 LEU A 107 3577 2437 2670 -367 402 -514 A C ATOM 849 N THR A 108 45.723 -12.915 23.394 1.00 18.08 A N ANISOU 849 N THR A 108 2470 1853 2546 26 -194 -90 A N ATOM 850 CA THR A 108 44.652 -13.539 22.700 1.00 18.41 A C ANISOU 850 CA THR A 108 2335 1968 2692 -18 -329 213 A C ATOM 851 C THR A 108 44.688 -15.039 22.956 1.00 17.23 A C ANISOU 851 C THR A 108 1980 1991 2574 -43 -9 193 A C ATOM 852 O THR A 108 45.720 -15.565 23.344 1.00 15.15 A O ANISOU 852 O THR A 108 2175 1505 2074 -25 -79 -49 A O ATOM 853 CB THR A 108 44.785 -13.351 21.182 1.00 21.49 A C ANISOU 853 CB THR A 108 3293 2150 2721 -624 -269 276 A C ATOM 854 CG2 THR A 108 44.958 -11.914 20.765 1.00 24.67 A C ANISOU 854 CG2 THR A 108 3817 2486 3070 -1320 -479 511 A C ATOM 855 OG1 THR A 108 45.910 -14.094 20.702 1.00 23.83 A O ANISOU 855 OG1 THR A 108 3612 3257 2184 -422 -76 57 A O ATOM 856 N PRO A 109 43.577 -15.782 22.744 1.00 17.63 A N ANISOU 856 N PRO A 109 2252 1553 2891 7 -425 74 A N ATOM 857 CA PRO A 109 43.633 -17.242 22.835 1.00 16.68 A C ANISOU 857 CA PRO A 109 2673 1562 2101 117 -234 -47 A C ATOM 858 C PRO A 109 44.755 -17.876 22.016 1.00 17.70 A C ANISOU 858 C PRO A 109 2507 2028 2188 -218 -232 -225 A C ATOM 859 O PRO A 109 45.388 -18.803 22.506 1.00 17.85 A O ANISOU 859 O PRO A 109 2819 1760 2204 -125 -34 -91 A O ATOM 860 CB PRO A 109 42.237 -17.653 22.374 1.00 19.94 A C ANISOU 860 CB PRO A 109 2998 2387 2191 -335 -126 -20 A C ATOM 861 CG PRO A 109 41.369 -16.504 22.846 1.00 20.07 A C ANISOU 861 CG PRO A 109 2517 2347 2761 -293 -291 307 A C ATOM 862 CD PRO A 109 42.209 -15.295 22.488 1.00 20.94 A C ANISOU 862 CD PRO A 109 2364 1941 3649 -118 -569 237 A C ATOM 863 N ASP A 110 45.004 -17.369 20.809 1.00 17.71 A N ANISOU 863 N ASP A 110 2753 1759 2216 -54 -510 -23 A N ATOM 864 CA ASP A 110 46.028 -17.949 19.944 1.00 18.29 A C ANISOU 864 CA ASP A 110 2771 2102 2075 -304 -176 357 A C ATOM 865 C ASP A 110 47.406 -17.869 20.614 1.00 15.83 A C ANISOU 865 C ASP A 110 2502 1649 1862 -198 65 -69 A C ATOM 866 O ASP A 110 48.270 -18.672 20.334 1.00 17.81 A O ANISOU 866 O ASP A 110 3132 1518 2117 45 143 115 A O ATOM 867 CB ASP A 110 46.041 -17.263 18.576 1.00 21.86 A C ANISOU 867 CB ASP A 110 3419 2959 1925 222 -128 392 A C ATOM 868 CG ASP A 110 44.948 -17.772 17.636 1.00 32.72 A C ANISOU 868 CG ASP A 110 4644 4472 3314 -488 -914 -54 A C ATOM 869 OD1 ASP A 110 44.280 -18.797 17.957 1.00 36.55 A O ANISOU 869 OD1 ASP A 110 4962 5286 3639 -1141 -1013 -465 A O ATOM 870 OD2 ASP A 110 44.769 -17.154 16.596 1.00 42.07 A O ANISOU 870 OD2 ASP A 110 6395 6394 3194 -780 -1260 157 A O ATOM 871 N ASP A 111 47.627 -16.846 21.455 1.00 15.55 A N ANISOU 871 N ASP A 111 2558 1328 2020 -266 -95 28 A N ATOM 872 CA ASP A 111 48.929 -16.667 22.089 1.00 14.76 A C ANISOU 872 CA ASP A 111 2270 1500 1838 -185 184 -36 A C ATOM 873 C ASP A 111 49.241 -17.800 23.084 1.00 13.71 A C ANISOU 873 C ASP A 111 1960 1536 1711 -200 232 -94 A C ATOM 874 O ASP A 111 50.375 -17.941 23.506 1.00 15.25 A O ANISOU 874 O ASP A 111 2235 1324 2234 -195 59 136 A O ATOM 875 CB ASP A 111 49.008 -15.305 22.809 1.00 14.76 A C ANISOU 875 CB ASP A 111 2438 1362 1806 -210 199 0 A C ATOM 876 CG ASP A 111 49.149 -14.115 21.876 1.00 17.54 A C ANISOU 876 CG ASP A 111 2852 1636 2176 -29 475 209 A C ATOM 877 OD1 ASP A 111 49.749 -14.268 20.775 1.00 20.84 A O ANISOU 877 OD1 ASP A 111 3631 1932 2355 -122 704 125 A O ATOM 878 OD2 ASP A 111 48.655 -13.058 22.265 1.00 20.14 A O ANISOU 878 OD2 ASP A 111 3449 1683 2517 309 364 423 A O ATOM 879 N TRP A 112 48.216 -18.572 23.479 1.00 13.50 A N ANISOU 879 N TRP A 112 2082 1133 1914 -183 213 34 A N ATOM 880 CA TRP A 112 48.411 -19.767 24.342 1.00 12.27 A C ANISOU 880 CA TRP A 112 1924 1102 1635 -225 222 -62 A C ATOM 881 C TRP A 112 48.897 -20.994 23.569 1.00 15.56 A C ANISOU 881 C TRP A 112 2931 1151 1829 -429 202 -216 A C ATOM 882 O TRP A 112 49.154 -22.018 24.199 1.00 15.54 A O ANISOU 882 O TRP A 112 2697 1347 1859 -140 410 55 A O ATOM 883 CB TRP A 112 47.121 -20.081 25.125 1.00 12.62 A C ANISOU 883 CB TRP A 112 1840 1271 1681 -240 138 -116 A C ATOM 884 CG TRP A 112 46.817 -19.107 26.214 1.00 12.16 A C ANISOU 884 CG TRP A 112 1898 1112 1608 -175 47 -36 A C ATOM 885 CD1 TRP A 112 46.155 -17.916 26.144 1.00 13.77 A C ANISOU 885 CD1 TRP A 112 2079 1266 1884 -149 3 202 A C ATOM 886 CD2 TRP A 112 47.302 -19.220 27.565 1.00 11.54 A C ANISOU 886 CD2 TRP A 112 2054 787 1543 22 89 -67 A C ATOM 887 CE2 TRP A 112 46.872 -18.058 28.259 1.00 12.52 A C ANISOU 887 CE2 TRP A 112 2055 928 1773 -116 -17 -362 A C ATOM 888 CE3 TRP A 112 48.051 -20.196 28.235 1.00 11.10 A C ANISOU 888 CE3 TRP A 112 1904 884 1427 -127 68 13 A C ATOM 889 NE1 TRP A 112 46.133 -17.325 27.374 1.00 14.04 A N ANISOU 889 NE1 TRP A 112 1817 1549 1969 -116 123 -60 A N ATOM 890 CZ2 TRP A 112 47.125 -17.886 29.612 1.00 13.43 A C ANISOU 890 CZ2 TRP A 112 2092 1292 1719 7 151 -280 A C ATOM 891 CZ3 TRP A 112 48.324 -19.997 29.573 1.00 11.49 A C ANISOU 891 CZ3 TRP A 112 2027 959 1378 -143 103 -114 A C ATOM 892 CH2 TRP A 112 47.899 -18.833 30.232 1.00 12.52 A C ANISOU 892 CH2 TRP A 112 1965 1217 1575 -130 28 -404 A C ATOM 893 N HIS A 113 48.988 -20.886 22.237 1.00 16.86 A N ANISOU 893 N HIS A 113 3226 1342 1835 -107 297 -157 A N ATOM 894 CA HIS A 113 49.507 -21.958 21.411 1.00 20.03 A C ANISOU 894 CA HIS A 113 3739 1628 2242 -248 795 -264 A C ATOM 895 C HIS A 113 48.659 -23.205 21.696 1.00 19.24 A C ANISOU 895 C HIS A 113 3458 1850 2002 -302 419 -201 A C ATOM 896 O HIS A 113 47.409 -23.157 21.714 1.00 22.19 A O ANISOU 896 O HIS A 113 3824 1859 2748 -548 227 -298 A O ATOM 897 CB HIS A 113 51.038 -22.016 21.605 1.00 21.35 A C ANISOU 897 CB HIS A 113 3842 1537 2732 243 851 -107 A C ATOM 898 CG HIS A 113 51.737 -20.893 20.893 1.00 27.30 A C ANISOU 898 CG HIS A 113 4245 2498 3628 191 1229 718 A C ATOM 899 CD2 HIS A 113 51.830 -19.561 21.160 1.00 30.56 A C ANISOU 899 CD2 HIS A 113 4657 3027 3927 -56 1791 -41 A C ATOM 900 ND1 HIS A 113 52.464 -21.089 19.735 1.00 31.65 A N ANISOU 900 ND1 HIS A 113 4368 4476 3179 -968 1060 69 A N ATOM 901 CE1 HIS A 113 52.941 -19.927 19.304 1.00 30.21 A C ANISOU 901 CE1 HIS A 113 3978 4128 3369 -1031 672 115 A C ATOM 902 NE2 HIS A 113 52.555 -18.965 20.152 1.00 31.55 A N ANISOU 902 NE2 HIS A 113 4381 3273 4332 86 1288 1103 A N ATOM 903 N ASP A 114 49.268 -24.326 21.958 1.00 20.86 A N ANISOU 903 N ASP A 114 4431 1669 1826 -229 312 -1 A N ATOM 904 CA AASP A 114 48.397 -25.526 22.070 0.50 21.79 A C ANISOU 904 CA AASP A 114 4135 1804 2340 -378 408 -56 A C ATOM 905 CA BASP A 114 48.473 -25.560 22.078 0.50 21.25 A C ANISOU 905 CA BASP A 114 4145 1657 2273 -295 396 -145 A C ATOM 906 C ASP A 114 48.079 -25.845 23.540 1.00 19.08 A C ANISOU 906 C ASP A 114 3444 1583 2220 -335 497 -488 A C ATOM 907 O ASP A 114 47.626 -26.916 23.863 1.00 18.72 A O ANISOU 907 O ASP A 114 3236 1501 2373 -298 546 -181 A O ATOM 908 CB AASP A 114 48.966 -26.736 21.317 0.50 24.44 A C ANISOU 908 CB AASP A 114 4491 2250 2544 -62 467 -368 A C ATOM 909 CB BASP A 114 49.234 -26.740 21.464 0.50 23.94 A C ANISOU 909 CB BASP A 114 4632 1868 2595 -34 192 -604 A C ATOM 910 CG AASP A 114 50.431 -27.044 21.573 0.50 28.46 A C ANISOU 910 CG AASP A 114 4515 2802 3494 150 492 277 A C ATOM 911 CG BASP A 114 49.267 -26.708 19.943 0.50 27.90 A C ANISOU 911 CG BASP A 114 5007 2976 2618 87 136 -161 A C ATOM 912 OD1AASP A 114 51.162 -26.116 21.983 0.50 29.13 A O ANISOU 912 OD1AASP A 114 5383 2359 3325 862 -8 -105 A O ATOM 913 OD1BASP A 114 48.478 -25.927 19.355 0.50 31.30 A O ANISOU 913 OD1BASP A 114 5045 3178 3667 -112 -1113 -588 A O ATOM 914 OD2AASP A 114 50.840 -28.218 21.333 0.50 28.47 A O ANISOU 914 OD2AASP A 114 5232 2595 2988 -68 281 154 A O ATOM 915 OD2BASP A 114 50.076 -27.471 19.357 0.50 34.62 A O ANISOU 915 OD2BASP A 114 5839 4068 3246 1693 -13 456 A O ATOM 916 N ALA A 115 48.290 -24.906 24.442 1.00 15.03 A N ANISOU 916 N ALA A 115 2512 1307 1890 -224 540 -285 A N ATOM 917 CA ALA A 115 48.019 -25.158 25.865 1.00 13.47 A C ANISOU 917 CA ALA A 115 2158 943 2014 56 251 -58 A C ATOM 918 C ALA A 115 46.516 -25.287 26.071 1.00 13.63 A C ANISOU 918 C ALA A 115 2184 1442 1552 -53 324 129 A C ATOM 919 O ALA A 115 45.725 -24.476 25.558 1.00 15.30 A O ANISOU 919 O ALA A 115 2006 1492 2311 31 35 33 A O ATOM 920 CB ALA A 115 48.604 -24.101 26.730 1.00 15.05 A C ANISOU 920 CB ALA A 115 2240 1307 2171 -14 325 -269 A C ATOM 921 N VAL A 116 46.140 -26.344 26.795 1.00 13.13 A N ANISOU 921 N VAL A 116 2017 1152 1817 -60 125 131 A N ATOM 922 CA VAL A 116 44.744 -26.590 27.159 1.00 12.49 A C ANISOU 922 CA VAL A 116 2111 970 1665 -220 227 -162 A C ATOM 923 C VAL A 116 44.654 -26.884 28.664 1.00 11.11 A C ANISOU 923 C VAL A 116 1684 888 1648 -452 -26 -180 A C ATOM 924 O VAL A 116 45.643 -27.204 29.346 1.00 12.01 A O ANISOU 924 O VAL A 116 1768 987 1807 -143 -50 -116 A O ATOM 925 CB VAL A 116 44.125 -27.744 26.354 1.00 13.73 A C ANISOU 925 CB VAL A 116 2297 1159 1759 -282 8 -135 A C ATOM 926 CG1 VAL A 116 44.155 -27.442 24.864 1.00 15.92 A C ANISOU 926 CG1 VAL A 116 2594 1758 1695 -193 312 -213 A C ATOM 927 CG2 VAL A 116 44.769 -29.081 26.669 1.00 15.49 A C ANISOU 927 CG2 VAL A 116 2346 1295 2244 11 88 -427 A C ATOM 928 N VAL A 117 43.449 -26.713 29.196 1.00 12.11 A N ANISOU 928 N VAL A 117 1776 1112 1710 -94 89 23 A N ATOM 929 CA VAL A 117 43.221 -27.069 30.586 1.00 12.05 A C ANISOU 929 CA VAL A 117 1961 991 1624 -246 49 -47 A C ATOM 930 C VAL A 117 43.260 -28.595 30.701 1.00 11.42 A C ANISOU 930 C VAL A 117 1791 1058 1489 -174 80 -109 A C ATOM 931 O VAL A 117 42.533 -29.259 29.952 1.00 11.98 A O ANISOU 931 O VAL A 117 1825 997 1728 -165 -65 -52 A O ATOM 932 CB VAL A 117 41.897 -26.510 31.133 1.00 12.89 A C ANISOU 932 CB VAL A 117 2104 742 2049 -167 143 -31 A C ATOM 933 CG1 VAL A 117 41.644 -26.967 32.560 1.00 13.45 A C ANISOU 933 CG1 VAL A 117 2063 1080 1966 -49 269 -316 A C ATOM 934 CG2 VAL A 117 41.843 -24.996 31.037 1.00 13.38 A C ANISOU 934 CG2 VAL A 117 1989 736 2357 -197 -40 -145 A C ATOM 935 N ILE A 118 44.063 -29.097 31.652 1.00 10.27 A N ANISOU 935 N ILE A 118 1931 596 1373 -224 60 -74 A N ATOM 936 CA ILE A 118 44.103 -30.523 31.870 1.00 11.03 A C ANISOU 936 CA ILE A 118 1980 586 1625 -191 46 -177 A C ATOM 937 C ILE A 118 43.636 -30.859 33.278 1.00 11.15 A C ANISOU 937 C ILE A 118 1785 914 1535 -81 -19 -147 A C ATOM 938 O ILE A 118 43.738 -30.079 34.213 1.00 11.64 A O ANISOU 938 O ILE A 118 1887 952 1584 -138 84 -164 A O ATOM 939 CB ILE A 118 45.489 -31.091 31.594 1.00 12.18 A C ANISOU 939 CB ILE A 118 2075 811 1741 -34 -4 -16 A C ATOM 940 CG1 ILE A 118 46.541 -30.512 32.536 1.00 11.68 A C ANISOU 940 CG1 ILE A 118 1825 1083 1530 111 21 -43 A C ATOM 941 CG2 ILE A 118 45.825 -30.923 30.121 1.00 13.46 A C ANISOU 941 CG2 ILE A 118 2280 1101 1733 -227 79 -92 A C ATOM 942 CD1 ILE A 118 47.898 -31.168 32.398 1.00 12.34 A C ANISOU 942 CD1 ILE A 118 1955 912 1821 76 188 -22 A C ATOM 943 N ALA A 119 43.192 -32.120 33.390 1.00 11.87 A N ANISOU 943 N ALA A 119 1992 913 1605 -213 130 -277 A N ATOM 944 CA ALA A 119 42.761 -32.725 34.593 1.00 12.32 A C ANISOU 944 CA ALA A 119 1915 977 1787 -115 147 -221 A C ATOM 945 C ALA A 119 43.325 -34.140 34.675 1.00 12.23 A C ANISOU 945 C ALA A 119 1712 1213 1722 -3 77 -28 A C ATOM 946 O ALA A 119 43.639 -34.761 33.663 1.00 13.02 A O ANISOU 946 O ALA A 119 2140 1097 1710 -4 31 -38 A O ATOM 947 CB ALA A 119 41.251 -32.762 34.660 1.00 12.27 A C ANISOU 947 CB ALA A 119 1937 718 2005 -92 102 -41 A C ATOM 948 N SER A 120 43.357 -34.660 35.909 1.00 10.79 A N ANISOU 948 N SER A 120 1870 557 1669 -57 187 -84 A N ATOM 949 CA SER A 120 43.765 -36.056 36.128 1.00 10.98 A C ANISOU 949 CA SER A 120 1677 697 1795 75 81 63 A C ATOM 950 C SER A 120 42.752 -37.070 35.591 1.00 12.38 A C ANISOU 950 C SER A 120 1818 1064 1820 26 -77 -39 A C ATOM 951 O SER A 120 41.547 -36.869 35.645 1.00 12.59 A O ANISOU 951 O SER A 120 1910 777 2093 -55 5 -182 A O ATOM 952 CB SER A 120 43.975 -36.289 37.617 1.00 10.81 A C ANISOU 952 CB SER A 120 1947 443 1718 -137 0 -2 A C ATOM 953 OG SER A 120 44.413 -37.596 37.876 1.00 12.32 A O ANISOU 953 OG SER A 120 2145 449 2084 -30 147 3 A O ATOM 954 N ASP A 121 43.295 -38.219 35.168 1.00 11.98 A N ANISOU 954 N ASP A 121 1718 1105 1729 -60 116 -7 A N ATOM 955 CA ASP A 121 42.469 -39.379 34.921 1.00 11.62 A C ANISOU 955 CA ASP A 121 1693 1181 1540 -124 217 -238 A C ATOM 956 C ASP A 121 41.888 -39.958 36.212 1.00 12.04 A C ANISOU 956 C ASP A 121 1951 932 1691 -67 232 -244 A C ATOM 957 O ASP A 121 40.999 -40.811 36.142 1.00 14.68 A O ANISOU 957 O ASP A 121 2489 1159 1927 -511 319 -297 A O ATOM 958 CB ASP A 121 43.261 -40.427 34.152 1.00 12.94 A C ANISOU 958 CB ASP A 121 1834 1214 1868 -31 424 -189 A C ATOM 959 CG ASP A 121 43.271 -40.243 32.634 1.00 14.59 A C ANISOU 959 CG ASP A 121 1856 1720 1968 68 187 61 A C ATOM 960 OD1 ASP A 121 42.568 -39.333 32.108 1.00 16.63 A O ANISOU 960 OD1 ASP A 121 2409 1410 2498 66 30 -12 A O ATOM 961 OD2 ASP A 121 43.932 -41.051 31.957 1.00 18.13 A O ANISOU 961 OD2 ASP A 121 2282 2310 2296 271 487 -199 A O ATOM 962 N ARG A 122 42.380 -39.544 37.375 1.00 12.61 A N ANISOU 962 N ARG A 122 2101 960 1727 -54 122 -92 A N ATOM 963 CA ARG A 122 41.711 -39.933 38.631 1.00 13.09 A C ANISOU 963 CA ARG A 122 2094 995 1883 23 143 -75 A C ATOM 964 C ARG A 122 40.319 -39.328 38.652 1.00 12.32 A C ANISOU 964 C ARG A 122 1986 948 1745 -55 146 -3 A C ATOM 965 O ARG A 122 40.176 -38.151 38.393 1.00 14.32 A O ANISOU 965 O ARG A 122 2297 867 2277 128 284 -26 A O ATOM 966 CB ARG A 122 42.502 -39.434 39.821 1.00 14.15 A C ANISOU 966 CB ARG A 122 2522 1042 1810 56 4 -107 A C ATOM 967 CG ARG A 122 41.979 -39.833 41.182 1.00 13.82 A C ANISOU 967 CG ARG A 122 2339 896 2015 -4 216 -157 A C ATOM 968 CD ARG A 122 42.846 -39.206 42.256 1.00 15.38 A C ANISOU 968 CD ARG A 122 2290 1448 2103 -229 170 -72 A C ATOM 969 NE ARG A 122 42.505 -39.545 43.627 1.00 16.75 A N ANISOU 969 NE ARG A 122 2642 1646 2075 -450 121 4 A N ATOM 970 CZ ARG A 122 41.762 -38.817 44.439 1.00 19.86 A C ANISOU 970 CZ ARG A 122 2734 2577 2234 -329 321 -60 A C ATOM 971 NH1 ARG A 122 41.152 -37.720 44.006 1.00 19.96 A N ANISOU 971 NH1 ARG A 122 2529 1771 3284 -150 166 -887 A N ATOM 972 NH2 ARG A 122 41.620 -39.221 45.698 1.00 24.56 A N ANISOU 972 NH2 ARG A 122 3885 3341 2104 -1398 204 -256 A N ATOM 973 N PRO A 123 39.252 -40.063 38.989 1.00 12.86 A N ANISOU 973 N PRO A 123 1897 674 2314 -90 156 -245 A N ATOM 974 CA PRO A 123 37.926 -39.462 39.011 1.00 14.20 A C ANISOU 974 CA PRO A 123 1917 1295 2183 -54 93 -139 A C ATOM 975 C PRO A 123 37.819 -38.375 40.083 1.00 13.94 A C ANISOU 975 C PRO A 123 2078 1040 2177 -2 -123 -16 A C ATOM 976 O PRO A 123 38.368 -38.510 41.162 1.00 13.51 A O ANISOU 976 O PRO A 123 2195 1021 1917 103 45 -199 A O ATOM 977 CB PRO A 123 36.952 -40.613 39.320 1.00 17.60 A C ANISOU 977 CB PRO A 123 2226 1359 3103 -263 162 -403 A C ATOM 978 CG PRO A 123 37.792 -41.766 39.656 1.00 21.30 A C ANISOU 978 CG PRO A 123 2338 1843 3910 -135 379 156 A C ATOM 979 CD PRO A 123 39.223 -41.498 39.294 1.00 14.68 A C ANISOU 979 CD PRO A 123 2335 611 2629 -29 231 -396 A C ATOM 980 N THR A 124 37.092 -37.297 39.761 1.00 11.93 A N ANISOU 980 N THR A 124 1993 1030 1510 36 179 -78 A N ATOM 981 CA THR A 124 36.846 -36.264 40.760 1.00 13.02 A C ANISOU 981 CA THR A 124 2031 1291 1622 32 357 -227 A C ATOM 982 C THR A 124 35.897 -36.829 41.846 1.00 13.26 A C ANISOU 982 C THR A 124 1979 1319 1739 -263 188 -80 A C ATOM 983 O THR A 124 35.041 -37.705 41.614 1.00 14.82 A O ANISOU 983 O THR A 124 2220 1283 2128 -303 116 -78 A O ATOM 984 CB THR A 124 36.306 -34.995 40.123 1.00 13.34 A C ANISOU 984 CB THR A 124 1821 1203 2045 -86 140 -170 A C ATOM 985 CG2 THR A 124 34.839 -35.065 39.777 1.00 13.66 A C ANISOU 985 CG2 THR A 124 1900 757 2531 -28 243 -22 A C ATOM 986 OG1 THR A 124 36.561 -33.933 41.040 1.00 12.87 A O ANISOU 986 OG1 THR A 124 1918 1094 1878 -112 240 -78 A O ATOM 987 N GLU A 125 36.031 -36.299 43.050 1.00 12.42 A N ANISOU 987 N GLU A 125 1878 1104 1733 -104 243 -37 A N ATOM 988 CA GLU A 125 35.193 -36.689 44.138 1.00 12.97 A C ANISOU 988 CA GLU A 125 1864 1114 1947 -263 347 -70 A C ATOM 989 C GLU A 125 33.770 -36.162 43.921 1.00 12.89 A C ANISOU 989 C GLU A 125 1733 1516 1647 -292 194 146 A C ATOM 990 O GLU A 125 33.567 -35.025 43.412 1.00 14.21 A O ANISOU 990 O GLU A 125 1868 1268 2262 -251 131 29 A O ATOM 991 CB GLU A 125 35.714 -36.136 45.461 1.00 14.24 A C ANISOU 991 CB GLU A 125 1967 1659 1782 -140 382 49 A C ATOM 992 CG GLU A 125 37.101 -36.628 45.844 1.00 14.56 A C ANISOU 992 CG GLU A 125 2064 1482 1985 -183 202 100 A C ATOM 993 CD GLU A 125 38.310 -35.868 45.321 1.00 14.38 A C ANISOU 993 CD GLU A 125 2106 1565 1791 -80 238 105 A C ATOM 994 OE1 GLU A 125 38.151 -35.060 44.353 1.00 13.33 A O ANISOU 994 OE1 GLU A 125 1866 1064 2133 -173 41 104 A O ATOM 995 OE2 GLU A 125 39.418 -36.074 45.924 1.00 14.07 A O ANISOU 995 OE2 GLU A 125 2126 778 2440 -30 122 78 A O ATOM 996 N VAL A 126 32.802 -36.936 44.404 1.00 15.13 A N ANISOU 996 N VAL A 126 1830 1420 2499 -351 331 121 A N ATOM 997 CA VAL A 126 31.378 -36.615 44.350 1.00 16.96 A C ANISOU 997 CA VAL A 126 1960 1719 2765 -416 216 -26 A C ATOM 998 C VAL A 126 30.918 -36.208 45.754 1.00 16.20 A C ANISOU 998 C VAL A 126 2050 1538 2565 -525 88 -183 A C ATOM 999 O VAL A 126 31.155 -36.892 46.756 1.00 19.15 A O ANISOU 999 O VAL A 126 2849 1854 2573 -405 441 -43 A O ATOM 1000 CB VAL A 126 30.557 -37.810 43.842 1.00 20.50 A C ANISOU 1000 CB VAL A 126 2386 2376 3026 -764 320 -554 A C ATOM 1001 CG1 VAL A 126 29.063 -37.504 43.877 1.00 23.22 A C ANISOU 1001 CG1 VAL A 126 2520 2718 3583 -510 180 -452 A C ATOM 1002 CG2 VAL A 126 30.990 -38.189 42.430 1.00 23.82 A C ANISOU 1002 CG2 VAL A 126 2825 3192 3031 -603 228 -741 A C ATOM 1003 N ASP A 127 30.341 -35.004 45.823 1.00 16.57 A N ANISOU 1003 N ASP A 127 1987 1800 2509 -215 360 3 A N ATOM 1004 CA ASP A 127 29.695 -34.473 47.053 1.00 18.33 A C ANISOU 1004 CA ASP A 127 2388 1933 2643 -510 370 -297 A C ATOM 1005 C ASP A 127 30.740 -34.440 48.171 1.00 17.45 A C ANISOU 1005 C ASP A 127 2262 2007 2359 -632 482 -100 A C ATOM 1006 O ASP A 127 30.454 -34.767 49.312 1.00 19.31 A O ANISOU 1006 O ASP A 127 2578 2114 2643 -553 591 84 A O ATOM 1007 CB ASP A 127 28.456 -35.299 47.415 1.00 23.81 A C ANISOU 1007 CB ASP A 127 2587 3012 3448 -927 649 -205 A C ATOM 1008 CG ASP A 127 27.299 -35.165 46.423 1.00 34.82 A C ANISOU 1008 CG ASP A 127 3962 4573 4695 -892 -266 -264 A C ATOM 1009 OD1 ASP A 127 27.111 -34.052 45.860 1.00 40.28 A O ANISOU 1009 OD1 ASP A 127 4289 4963 6051 -601 -624 275 A O ATOM 1010 OD2 ASP A 127 26.571 -36.175 46.219 1.00 45.92 A O ANISOU 1010 OD2 ASP A 127 4434 6347 6665 -2319 377 -1171 A O ATOM 1011 N ALA A 128 31.974 -34.030 47.829 1.00 16.29 A N ANISOU 1011 N ALA A 128 2154 1502 2533 -498 418 -201 A N ATOM 1012 CA ALA A 128 33.067 -34.041 48.823 1.00 14.20 A C ANISOU 1012 CA ALA A 128 2122 982 2289 -355 340 -198 A C ATOM 1013 C ALA A 128 34.204 -33.119 48.386 1.00 13.00 A C ANISOU 1013 C ALA A 128 1875 1099 1965 -124 134 103 A C ATOM 1014 O ALA A 128 34.351 -32.816 47.202 1.00 14.22 A O ANISOU 1014 O ALA A 128 2345 999 2058 -66 45 145 A O ATOM 1015 CB ALA A 128 33.574 -35.454 49.089 1.00 15.38 A C ANISOU 1015 CB ALA A 128 2554 1221 2067 -421 258 224 A C ATOM 1016 N THR A 129 35.058 -32.773 49.351 1.00 12.40 A N ANISOU 1016 N THR A 129 1896 1058 1756 -237 240 60 A N ATOM 1017 CA THR A 129 36.207 -31.956 49.066 1.00 12.91 A C ANISOU 1017 CA THR A 129 1943 1107 1853 -223 280 198 A C ATOM 1018 C THR A 129 37.155 -32.669 48.103 1.00 13.51 A C ANISOU 1018 C THR A 129 2128 1067 1936 -117 242 35 A C ATOM 1019 O THR A 129 37.222 -33.900 48.035 1.00 13.24 A O ANISOU 1019 O THR A 129 2185 958 1887 4 234 87 A O ATOM 1020 CB THR A 129 36.903 -31.541 50.371 1.00 14.06 A C ANISOU 1020 CB THR A 129 2167 1207 1968 -281 167 52 A C ATOM 1021 CG2 THR A 129 37.628 -32.650 51.092 1.00 16.59 A C ANISOU 1021 CG2 THR A 129 2446 1489 2367 -64 -98 174 A C ATOM 1022 OG1 THR A 129 37.861 -30.533 50.102 1.00 12.81 A O ANISOU 1022 OG1 THR A 129 1832 997 2039 -71 126 -75 A O ATOM 1023 N HIS A 130 37.916 -31.900 47.345 1.00 11.73 A N ANISOU 1023 N HIS A 130 1649 972 1833 73 319 32 A N ATOM 1024 CA HIS A 130 38.812 -32.410 46.327 1.00 10.55 A C ANISOU 1024 CA HIS A 130 1586 725 1696 -74 108 9 A C ATOM 1025 C HIS A 130 40.234 -32.501 46.858 1.00 11.27 A C ANISOU 1025 C HIS A 130 1614 1022 1642 -29 -6 34 A C ATOM 1026 O HIS A 130 40.881 -31.504 47.190 1.00 13.50 A O ANISOU 1026 O HIS A 130 1887 1185 2056 -185 -36 -82 A O ATOM 1027 CB HIS A 130 38.768 -31.548 45.073 1.00 10.74 A C ANISOU 1027 CB HIS A 130 1687 669 1724 -148 36 33 A C ATOM 1028 CG HIS A 130 37.417 -31.495 44.466 1.00 11.43 A C ANISOU 1028 CG HIS A 130 1773 992 1576 -73 -88 -39 A C ATOM 1029 CD2 HIS A 130 36.530 -30.501 44.319 1.00 13.93 A C ANISOU 1029 CD2 HIS A 130 2178 946 2167 4 -70 120 A C ATOM 1030 ND1 HIS A 130 36.775 -32.635 44.019 1.00 13.13 A N ANISOU 1030 ND1 HIS A 130 1736 1246 2005 -368 172 -174 A N ATOM 1031 CE1 HIS A 130 35.582 -32.327 43.560 1.00 12.98 A C ANISOU 1031 CE1 HIS A 130 1978 938 2014 -25 -38 -276 A C ATOM 1032 NE2 HIS A 130 35.417 -30.988 43.710 1.00 13.01 A N ANISOU 1032 NE2 HIS A 130 2024 865 2054 115 -49 -2 A N ATOM 1033 N ARG A 131 40.763 -33.709 46.870 1.00 12.06 A N ANISOU 1033 N ARG A 131 1795 1002 1783 -4 143 149 A N ATOM 1034 CA ARG A 131 42.159 -33.913 47.213 1.00 11.82 A C ANISOU 1034 CA ARG A 131 1923 830 1735 -92 107 22 A C ATOM 1035 C ARG A 131 43.040 -33.263 46.141 1.00 12.48 A C ANISOU 1035 C ARG A 131 1887 1187 1667 -44 163 44 A C ATOM 1036 O ARG A 131 42.787 -33.436 44.951 1.00 11.80 A O ANISOU 1036 O ARG A 131 2046 727 1710 108 44 87 A O ATOM 1037 CB ARG A 131 42.451 -35.410 47.291 1.00 12.67 A C ANISOU 1037 CB ARG A 131 2008 847 1959 -53 147 232 A C ATOM 1038 CG ARG A 131 43.886 -35.665 47.720 1.00 12.56 A C ANISOU 1038 CG ARG A 131 2101 643 2028 121 65 119 A C ATOM 1039 CD ARG A 131 44.033 -37.084 48.192 1.00 13.76 A C ANISOU 1039 CD ARG A 131 2165 726 2335 275 44 208 A C ATOM 1040 NE ARG A 131 45.426 -37.365 48.560 1.00 13.77 A N ANISOU 1040 NE ARG A 131 2044 858 2326 249 213 72 A N ATOM 1041 CZ ARG A 131 45.852 -38.602 48.810 1.00 16.45 A C ANISOU 1041 CZ ARG A 131 2461 912 2877 287 46 359 A C ATOM 1042 NH1 ARG A 131 44.976 -39.601 48.833 1.00 19.18 A N ANISOU 1042 NH1 ARG A 131 2535 1841 2910 -276 146 544 A N ATOM 1043 NH2 ARG A 131 47.145 -38.812 49.048 1.00 16.28 A N ANISOU 1043 NH2 ARG A 131 2475 1266 2446 208 -218 332 A N ATOM 1044 N PRO A 132 44.070 -32.469 46.498 1.00 11.12 A N ANISOU 1044 N PRO A 132 1608 1043 1572 250 11 162 A N ATOM 1045 CA PRO A 132 44.898 -31.838 45.478 1.00 10.72 A C ANISOU 1045 CA PRO A 132 1411 1232 1430 199 127 -128 A C ATOM 1046 C PRO A 132 45.551 -32.849 44.541 1.00 9.97 A C ANISOU 1046 C PRO A 132 1397 866 1525 214 47 -38 A C ATOM 1047 O PRO A 132 45.837 -34.018 44.947 1.00 11.75 A O ANISOU 1047 O PRO A 132 1835 830 1799 117 93 147 A O ATOM 1048 CB PRO A 132 45.934 -31.080 46.312 1.00 11.43 A C ANISOU 1048 CB PRO A 132 1701 1138 1504 -15 51 30 A C ATOM 1049 CG PRO A 132 45.140 -30.711 47.539 1.00 10.41 A C ANISOU 1049 CG PRO A 132 1693 881 1382 177 -69 92 A C ATOM 1050 CD PRO A 132 44.398 -31.983 47.856 1.00 11.96 A C ANISOU 1050 CD PRO A 132 1770 1288 1487 -43 100 279 A C ATOM 1051 N ILE A 133 45.788 -32.426 43.307 1.00 11.35 A N ANISOU 1051 N ILE A 133 1666 1151 1496 185 97 -3 A N ATOM 1052 CA ILE A 133 46.388 -33.236 42.277 1.00 11.55 A C ANISOU 1052 CA ILE A 133 1712 885 1790 123 254 -47 A C ATOM 1053 C ILE A 133 47.739 -32.652 41.881 1.00 12.01 A C ANISOU 1053 C ILE A 133 1769 843 1950 -34 234 -127 A C ATOM 1054 O ILE A 133 47.836 -31.421 41.681 1.00 12.12 A O ANISOU 1054 O ILE A 133 1865 802 1935 -125 204 -12 A O ATOM 1055 CB ILE A 133 45.463 -33.345 41.059 1.00 13.21 A C ANISOU 1055 CB ILE A 133 1818 1404 1795 25 166 -75 A C ATOM 1056 CG1 ILE A 133 44.148 -34.029 41.442 1.00 14.68 A C ANISOU 1056 CG1 ILE A 133 1871 1383 2324 -18 164 -289 A C ATOM 1057 CG2 ILE A 133 46.201 -33.970 39.898 1.00 14.41 A C ANISOU 1057 CG2 ILE A 133 2321 1316 1837 189 -84 -377 A C ATOM 1058 CD1 ILE A 133 44.262 -35.469 41.760 1.00 18.20 A C ANISOU 1058 CD1 ILE A 133 2851 1443 2618 -509 420 -46 A C ATOM 1059 N GLN A 134 48.767 -33.486 41.797 1.00 11.42 A N ANISOU 1059 N GLN A 134 1924 742 1671 47 359 41 A N ATOM 1060 CA GLN A 134 50.051 -33.181 41.258 1.00 11.73 A C ANISOU 1060 CA GLN A 134 1902 821 1732 -4 164 -82 A C ATOM 1061 C GLN A 134 50.031 -33.481 39.765 1.00 11.38 A C ANISOU 1061 C GLN A 134 1795 889 1637 -123 126 -156 A C ATOM 1062 O GLN A 134 49.636 -34.570 39.372 1.00 13.38 A O ANISOU 1062 O GLN A 134 2394 724 1962 -30 171 -252 A O ATOM 1063 CB GLN A 134 51.153 -33.972 41.960 1.00 12.12 A C ANISOU 1063 CB GLN A 134 1707 1111 1784 81 321 95 A C ATOM 1064 CG GLN A 134 51.276 -33.678 43.457 1.00 13.76 A C ANISOU 1064 CG GLN A 134 2081 1281 1865 46 29 29 A C ATOM 1065 CD GLN A 134 52.234 -34.586 44.192 1.00 16.20 A C ANISOU 1065 CD GLN A 134 2820 1096 2236 327 -127 111 A C ATOM 1066 NE2 GLN A 134 52.329 -35.854 43.793 1.00 20.29 A N ANISOU 1066 NE2 GLN A 134 3534 1262 2910 414 9 -211 A N ATOM 1067 OE1 GLN A 134 52.833 -34.200 45.174 1.00 18.09 A O ANISOU 1067 OE1 GLN A 134 2588 1555 2728 306 -296 -112 A O ATOM 1068 N PHE A 135 50.538 -32.561 38.955 1.00 11.23 A N ANISOU 1068 N PHE A 135 1802 988 1476 95 186 -94 A N ATOM 1069 CA PHE A 135 50.670 -32.692 37.529 1.00 10.10 A C ANISOU 1069 CA PHE A 135 1755 484 1596 202 161 -51 A C ATOM 1070 C PHE A 135 52.140 -32.532 37.180 1.00 12.03 A C ANISOU 1070 C PHE A 135 1725 1177 1670 171 214 -291 A C ATOM 1071 O PHE A 135 52.805 -31.668 37.731 1.00 11.95 A O ANISOU 1071 O PHE A 135 1762 975 1804 113 176 -211 A O ATOM 1072 CB PHE A 135 49.920 -31.574 36.814 1.00 10.90 A C ANISOU 1072 CB PHE A 135 1721 586 1833 214 90 73 A C ATOM 1073 CG PHE A 135 48.420 -31.606 36.958 1.00 11.64 A C ANISOU 1073 CG PHE A 135 1651 981 1790 19 167 53 A C ATOM 1074 CD1 PHE A 135 47.632 -32.279 36.042 1.00 13.17 A C ANISOU 1074 CD1 PHE A 135 1784 1183 2037 -31 256 -200 A C ATOM 1075 CD2 PHE A 135 47.776 -30.916 37.977 1.00 12.63 A C ANISOU 1075 CD2 PHE A 135 1725 1239 1833 -141 98 -244 A C ATOM 1076 CE1 PHE A 135 46.249 -32.328 36.169 1.00 14.13 A C ANISOU 1076 CE1 PHE A 135 1749 1662 1958 -302 148 -208 A C ATOM 1077 CE2 PHE A 135 46.389 -30.956 38.111 1.00 13.27 A C ANISOU 1077 CE2 PHE A 135 1803 1132 2106 -218 401 -260 A C ATOM 1078 CZ PHE A 135 45.620 -31.638 37.188 1.00 13.00 A C ANISOU 1078 CZ PHE A 135 1438 1433 2066 -4 136 -44 A C ATOM 1079 N ARG A 136 52.659 -33.380 36.274 1.00 10.75 A N ANISOU 1079 N ARG A 136 1749 731 1604 91 353 -90 A N ATOM 1080 CA ARG A 136 54.049 -33.239 35.933 1.00 11.45 A C ANISOU 1080 CA ARG A 136 1720 835 1794 145 306 -172 A C ATOM 1081 C ARG A 136 54.298 -33.493 34.438 1.00 11.66 A C ANISOU 1081 C ARG A 136 1602 1161 1666 97 133 -91 A C ATOM 1082 O ARG A 136 53.575 -34.211 33.761 1.00 12.75 A O ANISOU 1082 O ARG A 136 1841 1163 1838 67 83 -147 A O ATOM 1083 CB ARG A 136 54.949 -34.160 36.765 1.00 11.56 A C ANISOU 1083 CB ARG A 136 1764 944 1685 173 363 -53 A C ATOM 1084 CG ARG A 136 54.958 -35.621 36.349 1.00 11.73 A C ANISOU 1084 CG ARG A 136 1864 938 1651 68 233 -47 A C ATOM 1085 CD ARG A 136 55.783 -36.492 37.297 1.00 13.72 A C ANISOU 1085 CD ARG A 136 2159 1417 1637 183 124 -31 A C ATOM 1086 NE ARG A 136 57.151 -36.057 37.471 1.00 13.91 A N ANISOU 1086 NE ARG A 136 2146 1250 1888 282 105 -38 A N ATOM 1087 CZ ARG A 136 58.171 -36.289 36.660 1.00 14.81 A C ANISOU 1087 CZ ARG A 136 2098 1658 1870 226 99 86 A C ATOM 1088 NH1 ARG A 136 58.023 -37.100 35.608 1.00 14.40 A N ANISOU 1088 NH1 ARG A 136 2214 1397 1859 463 246 31 A N ATOM 1089 NH2 ARG A 136 59.355 -35.745 36.955 1.00 14.49 A N ANISOU 1089 NH2 ARG A 136 1905 1330 2270 364 -55 82 A N ATOM 1090 N LYS A 137 55.392 -32.892 33.977 1.00 11.96 A N ANISOU 1090 N LYS A 137 1613 1134 1796 72 212 -158 A N ATOM 1091 CA LYS A 137 55.866 -32.973 32.593 1.00 11.73 A C ANISOU 1091 CA LYS A 137 1678 1014 1764 197 169 -92 A C ATOM 1092 C LYS A 137 57.391 -32.824 32.589 1.00 13.63 A C ANISOU 1092 C LYS A 137 1711 1446 2021 231 258 -399 A C ATOM 1093 O LYS A 137 57.947 -31.974 33.287 1.00 14.14 A O ANISOU 1093 O LYS A 137 1680 1589 2100 130 102 -332 A O ATOM 1094 CB LYS A 137 55.191 -31.851 31.790 1.00 13.86 A C ANISOU 1094 CB LYS A 137 2022 1111 2134 317 196 114 A C ATOM 1095 CG LYS A 137 55.690 -31.638 30.367 1.00 16.86 A C ANISOU 1095 CG LYS A 137 1977 2081 2346 408 255 46 A C ATOM 1096 CD LYS A 137 55.314 -32.691 29.397 1.00 19.33 A C ANISOU 1096 CD LYS A 137 2462 2290 2593 174 606 -244 A C ATOM 1097 CE LYS A 137 55.464 -32.226 27.962 1.00 25.12 A C ANISOU 1097 CE LYS A 137 3405 3286 2852 -250 477 14 A C ATOM 1098 NZ LYS A 137 55.176 -33.303 26.995 1.00 25.32 A N ANISOU 1098 NZ LYS A 137 2839 4095 2684 -352 596 -275 A N ATOM 1099 N GLU A 138 58.064 -33.650 31.803 1.00 12.76 A N ANISOU 1099 N GLU A 138 1726 1279 1841 195 165 -370 A N ATOM 1100 CA GLU A 138 59.490 -33.479 31.516 1.00 13.89 A C ANISOU 1100 CA GLU A 138 1843 1120 2314 70 262 -373 A C ATOM 1101 C GLU A 138 59.648 -33.034 30.062 1.00 15.92 A C ANISOU 1101 C GLU A 138 1682 1997 2368 77 247 -269 A C ATOM 1102 O GLU A 138 58.801 -33.353 29.188 1.00 17.42 A O ANISOU 1102 O GLU A 138 1702 2831 2083 -108 275 -297 A O ATOM 1103 CB GLU A 138 60.288 -34.757 31.780 1.00 14.26 A C ANISOU 1103 CB GLU A 138 1835 1308 2274 245 457 -272 A C ATOM 1104 CG GLU A 138 60.185 -35.222 33.227 1.00 15.55 A C ANISOU 1104 CG GLU A 138 2199 1489 2220 193 86 -294 A C ATOM 1105 CD GLU A 138 61.068 -36.407 33.600 1.00 16.51 A C ANISOU 1105 CD GLU A 138 2083 1803 2387 270 127 -83 A C ATOM 1106 OE1 GLU A 138 61.997 -36.707 32.816 1.00 20.11 A O ANISOU 1106 OE1 GLU A 138 2494 2572 2575 947 243 -292 A O ATOM 1107 OE2 GLU A 138 60.855 -36.999 34.693 1.00 16.79 A O ANISOU 1107 OE2 GLU A 138 2054 1990 2335 319 304 -191 A O ATOM 1108 N PHE A 139 60.702 -32.234 29.828 1.00 14.62 A N ANISOU 1108 N PHE A 139 1487 2010 2057 140 230 -115 A N ATOM 1109 CA PHE A 139 60.941 -31.636 28.499 1.00 15.70 A C ANISOU 1109 CA PHE A 139 1813 1924 2224 77 363 -3 A C ATOM 1110 C PHE A 139 62.433 -31.370 28.381 1.00 16.43 A C ANISOU 1110 C PHE A 139 1972 2188 2082 -23 363 -43 A C ATOM 1111 O PHE A 139 63.156 -31.452 29.358 1.00 19.16 A O ANISOU 1111 O PHE A 139 1824 3312 2144 -178 204 18 A O ATOM 1112 CB PHE A 139 60.120 -30.351 28.312 1.00 17.98 A C ANISOU 1112 CB PHE A 139 2097 1996 2737 99 329 316 A C ATOM 1113 CG PHE A 139 60.390 -29.261 29.321 1.00 17.16 A C ANISOU 1113 CG PHE A 139 1937 2072 2511 219 142 450 A C ATOM 1114 CD1 PHE A 139 59.765 -29.283 30.552 1.00 17.02 A C ANISOU 1114 CD1 PHE A 139 1975 2211 2279 286 -50 230 A C ATOM 1115 CD2 PHE A 139 61.237 -28.194 29.025 1.00 17.12 A C ANISOU 1115 CD2 PHE A 139 1983 1886 2635 268 205 132 A C ATOM 1116 CE1 PHE A 139 59.974 -28.279 31.468 1.00 16.22 A C ANISOU 1116 CE1 PHE A 139 1766 2134 2263 331 489 214 A C ATOM 1117 CE2 PHE A 139 61.449 -27.183 29.956 1.00 16.79 A C ANISOU 1117 CE2 PHE A 139 1970 1835 2571 140 482 150 A C ATOM 1118 CZ PHE A 139 60.812 -27.230 31.170 1.00 18.77 A C ANISOU 1118 CZ PHE A 139 2362 1999 2767 240 535 232 A C ATOM 1119 N SER A 140 62.833 -30.987 27.179 1.00 15.63 A N ANISOU 1119 N SER A 140 2212 1805 1921 79 295 29 A N ATOM 1120 CA SER A 140 64.210 -30.761 26.840 1.00 17.75 A C ANISOU 1120 CA SER A 140 1967 2308 2468 90 218 38 A C ATOM 1121 C SER A 140 64.395 -29.345 26.330 1.00 17.99 A C ANISOU 1121 C SER A 140 2088 2378 2369 -43 232 119 A C ATOM 1122 O SER A 140 63.595 -28.882 25.513 1.00 21.62 A O ANISOU 1122 O SER A 140 2366 3071 2775 -322 22 591 A O ATOM 1123 CB SER A 140 64.608 -31.693 25.739 1.00 24.02 A C ANISOU 1123 CB SER A 140 3034 3041 3051 -16 873 -150 A C ATOM 1124 OG SER A 140 64.586 -32.997 26.213 1.00 27.86 A O ANISOU 1124 OG SER A 140 2668 2511 5404 288 630 -478 A O ATOM 1125 N VAL A 141 65.492 -28.726 26.750 1.00 16.90 A N ANISOU 1125 N VAL A 141 2098 1962 2361 146 242 193 A N ATOM 1126 CA VAL A 141 65.961 -27.482 26.175 1.00 17.31 A C ANISOU 1126 CA VAL A 141 1971 1968 2637 33 358 203 A C ATOM 1127 C VAL A 141 67.360 -27.771 25.638 1.00 18.93 A C ANISOU 1127 C VAL A 141 2179 1926 3085 -83 607 86 A C ATOM 1128 O VAL A 141 68.329 -27.744 26.372 1.00 21.62 A O ANISOU 1128 O VAL A 141 2176 2767 3270 -103 594 400 A O ATOM 1129 CB VAL A 141 65.933 -26.348 27.209 1.00 20.38 A C ANISOU 1129 CB VAL A 141 2433 2112 3196 -323 401 -32 A C ATOM 1130 CG1 VAL A 141 66.407 -25.047 26.588 1.00 20.91 A C ANISOU 1130 CG1 VAL A 141 2394 2086 3465 -185 576 -22 A C ATOM 1131 CG2 VAL A 141 64.550 -26.163 27.791 1.00 20.97 A C ANISOU 1131 CG2 VAL A 141 2617 2091 3256 -6 468 -262 A C ATOM 1132 N ASP A 142 67.434 -28.134 24.362 1.00 19.37 A N ANISOU 1132 N ASP A 142 2159 1826 3373 -186 860 -323 A N ATOM 1133 CA ASP A 142 68.717 -28.646 23.812 1.00 21.53 A C ANISOU 1133 CA ASP A 142 2585 2215 3380 309 1266 -132 A C ATOM 1134 C ASP A 142 69.463 -27.628 22.936 1.00 24.07 A C ANISOU 1134 C ASP A 142 3060 2018 4066 167 1015 230 A C ATOM 1135 O ASP A 142 70.356 -27.966 22.165 1.00 34.46 A O ANISOU 1135 O ASP A 142 3743 3990 5360 -107 1814 -284 A O ATOM 1136 CB ASP A 142 68.481 -29.931 23.036 1.00 27.77 A C ANISOU 1136 CB ASP A 142 3498 2837 4215 -125 1336 -721 A C ATOM 1137 CG ASP A 142 67.841 -31.029 23.867 1.00 27.45 A C ANISOU 1137 CG ASP A 142 3286 3207 3937 381 1183 -342 A C ATOM 1138 OD1 ASP A 142 68.341 -31.319 25.021 1.00 27.28 A O ANISOU 1138 OD1 ASP A 142 4417 1982 3965 -361 891 48 A O ATOM 1139 OD2 ASP A 142 66.864 -31.590 23.354 1.00 31.38 A O ANISOU 1139 OD2 ASP A 142 3737 3929 4255 -393 1417 -1201 A O ATOM 1140 N ASP A 143 69.078 -26.372 23.051 1.00 21.60 A N ANISOU 1140 N ASP A 143 3025 1954 3225 77 1584 89 A N ATOM 1141 CA ASP A 143 69.683 -25.220 22.362 1.00 26.66 A C ANISOU 1141 CA ASP A 143 3669 2831 3629 -880 1511 193 A C ATOM 1142 C ASP A 143 70.034 -24.190 23.436 1.00 27.01 A C ANISOU 1142 C ASP A 143 2749 3434 4077 -363 1393 -180 A C ATOM 1143 O ASP A 143 69.415 -24.171 24.510 1.00 25.42 A O ANISOU 1143 O ASP A 143 3572 2198 3889 -57 1390 -161 A O ATOM 1144 CB ASP A 143 68.694 -24.664 21.330 1.00 36.82 A C ANISOU 1144 CB ASP A 143 5947 2930 5111 293 685 -191 A C ATOM 1145 CG ASP A 143 68.217 -25.669 20.278 1.00 44.32 A C ANISOU 1145 CG ASP A 143 6043 5315 5479 -234 1298 -1422 A C ATOM 1146 OD1 ASP A 143 69.027 -26.040 19.421 1.00 45.79 A O ANISOU 1146 OD1 ASP A 143 5907 5814 5675 -669 2243 -775 A O ATOM 1147 OD2 ASP A 143 67.023 -26.063 20.320 1.00 49.52 A O ANISOU 1147 OD2 ASP A 143 7058 3987 7768 -1474 1149 -1151 A O ATOM 1148 N SER A 144 70.995 -23.316 23.150 1.00 25.91 A N ANISOU 1148 N SER A 144 2929 2760 4154 -3 1920 -167 A N ATOM 1149 CA SER A 144 71.262 -22.196 24.049 1.00 27.96 A C ANISOU 1149 CA SER A 144 3216 3063 4342 0 1627 -238 A C ATOM 1150 C SER A 144 70.035 -21.273 24.079 1.00 25.27 A C ANISOU 1150 C SER A 144 3068 2687 3845 -129 1150 160 A C ATOM 1151 O SER A 144 69.351 -21.073 23.058 1.00 25.11 A O ANISOU 1151 O SER A 144 2943 2542 4052 -29 1418 -214 A O ATOM 1152 CB SER A 144 72.497 -21.458 23.651 1.00 31.40 A C ANISOU 1152 CB SER A 144 3934 3352 4644 -439 1923 -182 A C ATOM 1153 OG SER A 144 72.321 -20.938 22.365 1.00 42.62 A O ANISOU 1153 OG SER A 144 5241 5298 5652 -13 2122 1441 A O ATOM 1154 N TYR A 145 69.743 -20.735 25.265 1.00 23.62 A N ANISOU 1154 N TYR A 145 2394 2655 3923 -241 720 -15 A N ATOM 1155 CA TYR A 145 68.557 -19.895 25.450 1.00 22.49 A C ANISOU 1155 CA TYR A 145 2278 2583 3684 -215 579 -285 A C ATOM 1156 C TYR A 145 68.927 -18.632 26.228 1.00 21.17 A C ANISOU 1156 C TYR A 145 2274 2428 3341 -275 489 -13 A C ATOM 1157 O TYR A 145 69.924 -18.596 26.941 1.00 22.72 A O ANISOU 1157 O TYR A 145 2136 2754 3741 -281 558 -219 A O ATOM 1158 CB TYR A 145 67.432 -20.660 26.170 1.00 23.61 A C ANISOU 1158 CB TYR A 145 2124 3238 3608 -450 617 -462 A C ATOM 1159 CG TYR A 145 67.796 -21.172 27.545 1.00 21.99 A C ANISOU 1159 CG TYR A 145 2250 2519 3585 -589 711 -317 A C ATOM 1160 CD1 TYR A 145 68.467 -22.369 27.669 1.00 24.69 A C ANISOU 1160 CD1 TYR A 145 3106 2508 3767 -499 504 3 A C ATOM 1161 CD2 TYR A 145 67.444 -20.505 28.716 1.00 29.11 A C ANISOU 1161 CD2 TYR A 145 3409 3851 3798 -906 875 -736 A C ATOM 1162 CE1 TYR A 145 68.842 -22.862 28.897 1.00 26.91 A C ANISOU 1162 CE1 TYR A 145 3409 2843 3969 -445 729 128 A C ATOM 1163 CE2 TYR A 145 67.813 -20.992 29.969 1.00 25.43 A C ANISOU 1163 CE2 TYR A 145 3353 2160 4148 -284 589 -804 A C ATOM 1164 CZ TYR A 145 68.529 -22.175 30.045 1.00 26.01 A C ANISOU 1164 CZ TYR A 145 3173 2828 3881 -260 859 289 A C ATOM 1165 OH TYR A 145 68.927 -22.750 31.217 1.00 30.68 A O ANISOU 1165 OH TYR A 145 4445 2872 4337 434 13 19 A O ATOM 1166 N VAL A 146 68.070 -17.617 26.103 1.00 20.69 A N ANISOU 1166 N VAL A 146 2186 2599 3073 -129 582 -258 A N ATOM 1167 CA VAL A 146 68.324 -16.309 26.699 1.00 21.80 A C ANISOU 1167 CA VAL A 146 2067 2798 3415 -504 877 -434 A C ATOM 1168 C VAL A 146 67.255 -15.903 27.720 1.00 21.94 A C ANISOU 1168 C VAL A 146 2443 2787 3104 -461 906 -506 A C ATOM 1169 O VAL A 146 67.560 -15.097 28.613 1.00 20.72 A O ANISOU 1169 O VAL A 146 2112 2397 3360 -282 850 -439 A O ATOM 1170 CB VAL A 146 68.492 -15.225 25.623 1.00 23.61 A C ANISOU 1170 CB VAL A 146 2707 3165 3097 -573 1065 -313 A C ATOM 1171 CG1 VAL A 146 69.726 -15.506 24.759 1.00 27.73 A C ANISOU 1171 CG1 VAL A 146 2719 3558 4258 -424 1403 -338 A C ATOM 1172 CG2 VAL A 146 67.238 -15.021 24.780 1.00 24.52 A C ANISOU 1172 CG2 VAL A 146 3204 3201 2908 -252 1015 14 A C ATOM 1173 N SER A 147 66.029 -16.412 27.588 1.00 19.58 A N ANISOU 1173 N SER A 147 2340 2140 2959 -182 719 -293 A N ATOM 1174 CA SER A 147 64.950 -16.038 28.520 1.00 17.04 A C ANISOU 1174 CA SER A 147 2202 1446 2826 -428 761 165 A C ATOM 1175 C SER A 147 63.864 -17.101 28.485 1.00 15.81 A C ANISOU 1175 C SER A 147 1895 1802 2307 -376 650 -249 A C ATOM 1176 O SER A 147 63.763 -17.842 27.510 1.00 17.00 A O ANISOU 1176 O SER A 147 2001 2285 2172 -314 527 -271 A O ATOM 1177 CB SER A 147 64.394 -14.641 28.238 1.00 19.45 A C ANISOU 1177 CB SER A 147 3033 1339 3014 -684 402 528 A C ATOM 1178 OG SER A 147 63.763 -14.605 26.980 1.00 22.12 A O ANISOU 1178 OG SER A 147 2693 2479 3232 272 638 79 A O ATOM 1179 N ALA A 148 63.062 -17.148 29.559 1.00 14.66 A N ANISOU 1179 N ALA A 148 2072 1260 2236 -99 606 56 A N ATOM 1180 CA ALA A 148 61.953 -18.066 29.574 1.00 14.24 A C ANISOU 1180 CA ALA A 148 1778 1399 2232 57 745 -43 A C ATOM 1181 C ALA A 148 60.836 -17.498 30.442 1.00 13.28 A C ANISOU 1181 C ALA A 148 1609 1510 1927 52 426 -250 A C ATOM 1182 O ALA A 148 61.096 -16.799 31.435 1.00 13.10 A O ANISOU 1182 O ALA A 148 1957 1157 1862 99 255 -51 A O ATOM 1183 CB ALA A 148 62.392 -19.446 30.034 1.00 14.69 A C ANISOU 1183 CB ALA A 148 1643 1471 2466 54 507 80 A C ATOM 1184 N ARG A 149 59.607 -17.860 30.058 1.00 12.99 A N ANISOU 1184 N ARG A 149 1632 1318 1984 114 254 -168 A N ATOM 1185 CA ARG A 149 58.410 -17.441 30.771 1.00 12.62 A C ANISOU 1185 CA ARG A 149 1746 1020 2028 -12 534 53 A C ATOM 1186 C ARG A 149 57.498 -18.631 31.056 1.00 12.07 A C ANISOU 1186 C ARG A 149 1453 1222 1911 -92 494 -221 A C ATOM 1187 O ARG A 149 57.403 -19.541 30.257 1.00 13.57 A O ANISOU 1187 O ARG A 149 1895 1495 1766 -122 425 -341 A O ATOM 1188 CB ARG A 149 57.597 -16.434 29.948 1.00 15.25 A C ANISOU 1188 CB ARG A 149 2238 1166 2388 195 156 -84 A C ATOM 1189 CG ARG A 149 58.338 -15.148 29.604 1.00 14.29 A C ANISOU 1189 CG ARG A 149 1642 1466 2322 156 249 38 A C ATOM 1190 CD ARG A 149 58.596 -14.276 30.822 1.00 13.05 A C ANISOU 1190 CD ARG A 149 1656 916 2384 103 429 119 A C ATOM 1191 NE ARG A 149 59.287 -13.058 30.480 1.00 14.20 A N ANISOU 1191 NE ARG A 149 2071 686 2635 225 336 254 A N ATOM 1192 CZ ARG A 149 60.615 -12.857 30.573 1.00 16.10 A C ANISOU 1192 CZ ARG A 149 2091 1041 2982 39 440 395 A C ATOM 1193 NH1 ARG A 149 61.429 -13.778 31.073 1.00 16.17 A N ANISOU 1193 NH1 ARG A 149 2081 1506 2555 360 333 287 A N ATOM 1194 NH2 ARG A 149 61.101 -11.674 30.209 1.00 15.65 A N ANISOU 1194 NH2 ARG A 149 2068 985 2893 -49 769 145 A N ATOM 1195 N LEU A 150 56.842 -18.590 32.223 1.00 11.35 A N ANISOU 1195 N LEU A 150 1638 940 1733 77 372 -149 A N ATOM 1196 CA LEU A 150 55.750 -19.516 32.536 1.00 12.02 A C ANISOU 1196 CA LEU A 150 1642 1178 1743 -30 355 -94 A C ATOM 1197 C LEU A 150 54.477 -18.695 32.673 1.00 10.78 A C ANISOU 1197 C LEU A 150 1539 1164 1393 -22 131 -240 A C ATOM 1198 O LEU A 150 54.460 -17.724 33.464 1.00 12.16 A O ANISOU 1198 O LEU A 150 1882 1002 1733 -72 96 -318 A O ATOM 1199 CB LEU A 150 56.003 -20.284 33.830 1.00 12.29 A C ANISOU 1199 CB LEU A 150 1541 1229 1897 164 217 -132 A C ATOM 1200 CG LEU A 150 54.913 -21.294 34.173 1.00 12.19 A C ANISOU 1200 CG LEU A 150 1600 1055 1974 112 161 -233 A C ATOM 1201 CD1 LEU A 150 54.866 -22.441 33.158 1.00 13.49 A C ANISOU 1201 CD1 LEU A 150 2323 969 1831 -49 -8 -57 A C ATOM 1202 CD2 LEU A 150 55.121 -21.841 35.565 1.00 13.54 A C ANISOU 1202 CD2 LEU A 150 1647 1430 2066 -46 7 -111 A C ATOM 1203 N TYR A 151 53.453 -19.073 31.916 1.00 10.11 A N ANISOU 1203 N TYR A 151 1428 832 1578 104 86 -70 A N ATOM 1204 CA TYR A 151 52.132 -18.495 31.968 1.00 10.26 A C ANISOU 1204 CA TYR A 151 1421 954 1522 28 193 -222 A C ATOM 1205 C TYR A 151 51.200 -19.555 32.536 1.00 9.89 A C ANISOU 1205 C TYR A 151 1529 727 1502 33 147 -154 A C ATOM 1206 O TYR A 151 51.223 -20.711 32.044 1.00 11.17 A O ANISOU 1206 O TYR A 151 1766 745 1730 -38 299 -269 A O ATOM 1207 CB TYR A 151 51.691 -18.112 30.570 1.00 10.74 A C ANISOU 1207 CB TYR A 151 1513 987 1579 -7 34 -211 A C ATOM 1208 CG TYR A 151 52.638 -17.175 29.885 1.00 10.50 A C ANISOU 1208 CG TYR A 151 1732 828 1428 126 107 70 A C ATOM 1209 CD1 TYR A 151 52.611 -15.825 30.172 1.00 10.20 A C ANISOU 1209 CD1 TYR A 151 1509 841 1525 -129 90 -7 A C ATOM 1210 CD2 TYR A 151 53.547 -17.597 28.932 1.00 11.70 A C ANISOU 1210 CD2 TYR A 151 1617 1049 1780 28 168 53 A C ATOM 1211 CE1 TYR A 151 53.450 -14.936 29.519 1.00 11.46 A C ANISOU 1211 CE1 TYR A 151 1498 1081 1773 -311 154 -19 A C ATOM 1212 CE2 TYR A 151 54.376 -16.704 28.267 1.00 12.33 A C ANISOU 1212 CE2 TYR A 151 1548 1302 1835 -27 268 16 A C ATOM 1213 CZ TYR A 151 54.333 -15.354 28.565 1.00 12.80 A C ANISOU 1213 CZ TYR A 151 1532 1266 2063 -54 331 187 A C ATOM 1214 OH TYR A 151 55.177 -14.516 27.860 1.00 13.49 A O ANISOU 1214 OH TYR A 151 1710 1487 1928 -36 582 229 A O ATOM 1215 N ILE A 152 50.475 -19.273 33.622 1.00 9.34 A N ANISOU 1215 N ILE A 152 1560 552 1437 -122 128 -136 A N ATOM 1216 CA ILE A 152 49.836 -20.362 34.342 1.00 9.72 A C ANISOU 1216 CA ILE A 152 1282 912 1497 -193 203 -24 A C ATOM 1217 C ILE A 152 48.623 -19.878 35.110 1.00 9.14 A C ANISOU 1217 C ILE A 152 1357 884 1229 -164 177 -76 A C ATOM 1218 O ILE A 152 48.622 -18.775 35.685 1.00 9.96 A O ANISOU 1218 O ILE A 152 1550 788 1446 -48 85 -119 A O ATOM 1219 CB ILE A 152 50.874 -21.027 35.264 1.00 9.75 A C ANISOU 1219 CB ILE A 152 1332 819 1553 -97 152 -162 A C ATOM 1220 CG1 ILE A 152 50.275 -22.197 36.047 1.00 10.36 A C ANISOU 1220 CG1 ILE A 152 1601 866 1468 -44 192 -86 A C ATOM 1221 CG2 ILE A 152 51.570 -20.025 36.164 1.00 10.48 A C ANISOU 1221 CG2 ILE A 152 1622 726 1633 87 -113 -115 A C ATOM 1222 CD1 ILE A 152 51.306 -23.145 36.644 1.00 11.20 A C ANISOU 1222 CD1 ILE A 152 1588 949 1718 5 213 -154 A C ATOM 1223 N THR A 153 47.607 -20.723 35.157 1.00 8.95 A N ANISOU 1223 N THR A 153 1400 810 1187 -153 79 -70 A N ATOM 1224 CA THR A 153 46.502 -20.562 36.055 1.00 9.34 A C ANISOU 1224 CA THR A 153 1362 798 1386 -28 149 91 A C ATOM 1225 C THR A 153 45.920 -21.927 36.390 1.00 8.72 A C ANISOU 1225 C THR A 153 1119 669 1526 84 137 -45 A C ATOM 1226 O THR A 153 46.366 -22.953 35.896 1.00 10.65 A O ANISOU 1226 O THR A 153 1687 804 1555 223 242 -157 A O ATOM 1227 CB THR A 153 45.417 -19.629 35.503 1.00 10.59 A C ANISOU 1227 CB THR A 153 1482 1009 1532 70 90 194 A C ATOM 1228 CG2 THR A 153 44.605 -20.219 34.375 1.00 12.12 A C ANISOU 1228 CG2 THR A 153 1503 1438 1661 116 -10 139 A C ATOM 1229 OG1 THR A 153 44.551 -19.246 36.571 1.00 11.12 A O ANISOU 1229 OG1 THR A 153 1240 1150 1834 22 133 -97 A O ATOM 1230 N ALA A 154 44.917 -21.932 37.266 1.00 9.76 A N ANISOU 1230 N ALA A 154 1464 583 1660 -105 328 -98 A N ATOM 1231 CA ALA A 154 44.259 -23.175 37.634 1.00 9.25 A C ANISOU 1231 CA ALA A 154 1294 643 1578 -204 70 -85 A C ATOM 1232 C ALA A 154 42.761 -22.968 37.725 1.00 10.26 A C ANISOU 1232 C ALA A 154 1346 1089 1459 23 111 -185 A C ATOM 1233 O ALA A 154 42.276 -21.840 38.000 1.00 12.22 A O ANISOU 1233 O ALA A 154 1578 1014 2050 265 213 96 A O ATOM 1234 CB ALA A 154 44.754 -23.634 38.986 1.00 11.93 A C ANISOU 1234 CB ALA A 154 1618 1074 1841 -8 -174 83 A C ATOM 1235 N LEU A 155 42.044 -24.066 37.529 1.00 11.15 A N ANISOU 1235 N LEU A 155 1369 1173 1692 -36 103 -165 A N ATOM 1236 CA LEU A 155 40.661 -24.168 37.942 1.00 10.65 A C ANISOU 1236 CA LEU A 155 1413 1145 1486 -59 124 -162 A C ATOM 1237 C LEU A 155 40.718 -24.676 39.384 1.00 9.89 A C ANISOU 1237 C LEU A 155 1455 826 1476 -275 63 -97 A C ATOM 1238 O LEU A 155 40.681 -25.899 39.645 1.00 11.23 A O ANISOU 1238 O LEU A 155 1736 760 1770 -134 35 -17 A O ATOM 1239 CB LEU A 155 39.903 -25.088 36.996 1.00 11.51 A C ANISOU 1239 CB LEU A 155 1528 1004 1839 -36 -101 -184 A C ATOM 1240 CG LEU A 155 39.461 -24.488 35.669 1.00 14.64 A C ANISOU 1240 CG LEU A 155 1848 2016 1698 -174 -176 -312 A C ATOM 1241 CD1 LEU A 155 40.611 -23.935 34.861 1.00 17.53 A C ANISOU 1241 CD1 LEU A 155 2599 2052 2007 -553 -53 -230 A C ATOM 1242 CD2 LEU A 155 38.656 -25.540 34.905 1.00 14.48 A C ANISOU 1242 CD2 LEU A 155 1679 1783 2039 -230 -101 -222 A C ATOM 1243 N GLY A 156 40.953 -23.760 40.297 1.00 10.05 A N ANISOU 1243 N GLY A 156 1468 991 1357 -31 -38 -139 A N ATOM 1244 CA GLY A 156 41.412 -24.020 41.637 1.00 10.08 A C ANISOU 1244 CA GLY A 156 1405 979 1445 65 31 -71 A C ATOM 1245 C GLY A 156 42.492 -23.053 41.993 1.00 9.49 A C ANISOU 1245 C GLY A 156 1471 859 1276 -43 191 149 A C ATOM 1246 O GLY A 156 42.369 -21.841 41.697 1.00 11.19 A O ANISOU 1246 O GLY A 156 1690 797 1763 141 189 133 A O ATOM 1247 N LEU A 157 43.526 -23.535 42.674 1.00 10.42 A N ANISOU 1247 N LEU A 157 1475 735 1749 29 58 47 A N ATOM 1248 CA LEU A 157 44.719 -22.762 43.049 1.00 9.76 A C ANISOU 1248 CA LEU A 157 1319 946 1441 92 122 79 A C ATOM 1249 C LEU A 157 45.939 -23.598 42.713 1.00 9.60 A C ANISOU 1249 C LEU A 157 1452 526 1669 173 -34 221 A C ATOM 1250 O LEU A 157 45.834 -24.853 42.749 1.00 10.81 A O ANISOU 1250 O LEU A 157 1793 508 1805 65 301 103 A O ATOM 1251 CB LEU A 157 44.684 -22.453 44.540 1.00 10.94 A C ANISOU 1251 CB LEU A 157 1753 910 1491 -119 -47 -29 A C ATOM 1252 CG LEU A 157 43.499 -21.597 45.017 1.00 10.89 A C ANISOU 1252 CG LEU A 157 1646 824 1667 -219 84 -121 A C ATOM 1253 CD1 LEU A 157 43.451 -21.524 46.561 1.00 13.60 A C ANISOU 1253 CD1 LEU A 157 1966 1328 1871 -226 238 -333 A C ATOM 1254 CD2 LEU A 157 43.491 -20.191 44.395 1.00 10.84 A C ANISOU 1254 CD2 LEU A 157 1515 922 1679 -179 20 -70 A C ATOM 1255 N TYR A 158 47.078 -23.001 42.425 1.00 10.20 A N ANISOU 1255 N TYR A 158 1568 826 1481 116 83 -108 A N ATOM 1256 CA TYR A 158 48.240 -23.759 42.004 1.00 10.23 A C ANISOU 1256 CA TYR A 158 1508 582 1796 131 19 43 A C ATOM 1257 C TYR A 158 49.495 -23.344 42.766 1.00 10.12 A C ANISOU 1257 C TYR A 158 1565 756 1524 132 -6 -154 A C ATOM 1258 O TYR A 158 49.668 -22.188 43.185 1.00 11.29 A O ANISOU 1258 O TYR A 158 1664 696 1927 -20 0 -157 A O ATOM 1259 CB TYR A 158 48.490 -23.685 40.487 1.00 10.07 A C ANISOU 1259 CB TYR A 158 1479 709 1636 35 -120 -186 A C ATOM 1260 CG TYR A 158 48.947 -22.317 40.088 1.00 10.63 A C ANISOU 1260 CG TYR A 158 1595 750 1693 138 31 -47 A C ATOM 1261 CD1 TYR A 158 48.043 -21.315 39.780 1.00 9.85 A C ANISOU 1261 CD1 TYR A 158 1399 776 1567 -44 -186 -80 A C ATOM 1262 CD2 TYR A 158 50.315 -22.000 40.087 1.00 10.30 A C ANISOU 1262 CD2 TYR A 158 1472 854 1586 158 -139 -160 A C ATOM 1263 CE1 TYR A 158 48.481 -20.030 39.486 1.00 9.97 A C ANISOU 1263 CE1 TYR A 158 1523 782 1481 -124 44 -120 A C ATOM 1264 CE2 TYR A 158 50.754 -20.710 39.828 1.00 11.13 A C ANISOU 1264 CE2 TYR A 158 1458 1174 1596 -39 -63 119 A C ATOM 1265 CZ TYR A 158 49.831 -19.735 39.532 1.00 10.16 A C ANISOU 1265 CZ TYR A 158 1454 896 1509 -133 151 76 A C ATOM 1266 OH TYR A 158 50.304 -18.459 39.342 1.00 10.81 A O ANISOU 1266 OH TYR A 158 1631 901 1572 -246 193 34 A O ATOM 1267 N GLU A 159 50.448 -24.272 42.829 1.00 10.20 A N ANISOU 1267 N GLU A 159 1333 927 1615 111 139 -46 A N ATOM 1268 CA GLU A 159 51.821 -24.023 43.224 1.00 11.08 A C ANISOU 1268 CA GLU A 159 1511 997 1700 93 109 -239 A C ATOM 1269 C GLU A 159 52.708 -24.779 42.243 1.00 10.69 A C ANISOU 1269 C GLU A 159 1588 895 1577 122 104 -215 A C ATOM 1270 O GLU A 159 52.621 -26.018 42.182 1.00 11.32 A O ANISOU 1270 O GLU A 159 1805 774 1718 172 69 -164 A O ATOM 1271 CB GLU A 159 52.116 -24.508 44.635 1.00 13.79 A C ANISOU 1271 CB GLU A 159 2125 1423 1692 195 7 -240 A C ATOM 1272 CG GLU A 159 53.521 -24.271 45.097 1.00 17.70 A C ANISOU 1272 CG GLU A 159 2298 1868 2557 37 -105 -184 A C ATOM 1273 CD GLU A 159 53.710 -24.496 46.600 1.00 29.87 A C ANISOU 1273 CD GLU A 159 3805 4563 2980 -125 -846 1049 A C ATOM 1274 OE1 GLU A 159 52.769 -24.994 47.270 1.00 36.91 A O ANISOU 1274 OE1 GLU A 159 5518 4809 3694 -1511 -1354 1827 A O ATOM 1275 OE2 GLU A 159 54.771 -24.143 47.106 1.00 32.86 A O ANISOU 1275 OE2 GLU A 159 4088 4095 4302 -730 -397 880 A O ATOM 1276 N ALA A 160 53.553 -24.090 41.490 1.00 11.05 A N ANISOU 1276 N ALA A 160 1432 965 1801 73 100 -231 A N ATOM 1277 CA ALA A 160 54.411 -24.661 40.470 1.00 11.25 A C ANISOU 1277 CA ALA A 160 1787 973 1515 108 -47 -354 A C ATOM 1278 C ALA A 160 55.870 -24.710 40.915 1.00 11.93 A C ANISOU 1278 C ALA A 160 1674 1196 1661 288 37 -308 A C ATOM 1279 O ALA A 160 56.355 -23.861 41.659 1.00 11.53 A O ANISOU 1279 O ALA A 160 1436 1184 1759 41 108 -220 A O ATOM 1280 CB ALA A 160 54.317 -23.898 39.171 1.00 12.44 A C ANISOU 1280 CB ALA A 160 1791 1224 1709 70 96 -27 A C ATOM 1281 N ARG A 161 56.549 -25.772 40.464 1.00 11.45 A N ANISOU 1281 N ARG A 161 1552 955 1841 185 -77 -297 A N ATOM 1282 CA ARG A 161 57.981 -25.967 40.709 1.00 11.75 A C ANISOU 1282 CA ARG A 161 1531 957 1975 186 21 -69 A C ATOM 1283 C ARG A 161 58.635 -26.342 39.376 1.00 12.52 A C ANISOU 1283 C ARG A 161 1715 1214 1827 -14 52 -44 A C ATOM 1284 O ARG A 161 58.094 -27.164 38.612 1.00 13.73 A O ANISOU 1284 O ARG A 161 1600 1472 2144 -85 254 -425 A O ATOM 1285 CB ARG A 161 58.236 -27.090 41.721 1.00 14.59 A C ANISOU 1285 CB ARG A 161 2054 1264 2225 519 81 152 A C ATOM 1286 CG ARG A 161 57.500 -26.937 43.045 1.00 18.96 A C ANISOU 1286 CG ARG A 161 3085 1817 2299 845 177 183 A C ATOM 1287 CD ARG A 161 57.830 -27.955 44.119 1.00 19.84 A C ANISOU 1287 CD ARG A 161 3209 1881 2447 433 10 354 A C ATOM 1288 NE ARG A 161 59.143 -27.634 44.671 1.00 23.91 A N ANISOU 1288 NE ARG A 161 3473 2449 3162 256 -173 -66 A N ATOM 1289 CZ ARG A 161 59.386 -26.687 45.585 1.00 25.73 A C ANISOU 1289 CZ ARG A 161 4202 2987 2586 446 -29 -97 A C ATOM 1290 NH1 ARG A 161 58.392 -25.969 46.082 1.00 27.60 A N ANISOU 1290 NH1 ARG A 161 4259 2760 3465 1094 -117 496 A N ATOM 1291 NH2 ARG A 161 60.628 -26.472 46.000 1.00 28.01 A N ANISOU 1291 NH2 ARG A 161 4297 3492 2851 186 -21 668 A N ATOM 1292 N ILE A 162 59.831 -25.816 39.113 1.00 11.87 A N ANISOU 1292 N ILE A 162 1568 1058 1883 87 5 -391 A N ATOM 1293 CA ILE A 162 60.596 -26.207 37.960 1.00 11.81 A C ANISOU 1293 CA ILE A 162 1691 1129 1667 -75 7 -263 A C ATOM 1294 C ILE A 162 61.943 -26.709 38.468 1.00 12.39 A C ANISOU 1294 C ILE A 162 1781 1204 1722 344 93 -279 A C ATOM 1295 O ILE A 162 62.653 -25.985 39.185 1.00 13.70 A O ANISOU 1295 O ILE A 162 1664 1413 2125 253 -30 -272 A O ATOM 1296 CB ILE A 162 60.785 -25.069 36.957 1.00 12.99 A C ANISOU 1296 CB ILE A 162 1794 1186 1955 147 123 -46 A C ATOM 1297 CG1 ILE A 162 59.456 -24.759 36.275 1.00 13.27 A C ANISOU 1297 CG1 ILE A 162 1717 1301 2021 124 87 -164 A C ATOM 1298 CG2 ILE A 162 61.859 -25.425 35.926 1.00 13.80 A C ANISOU 1298 CG2 ILE A 162 1680 1473 2088 -1 133 -46 A C ATOM 1299 CD1 ILE A 162 59.500 -23.462 35.432 1.00 14.37 A C ANISOU 1299 CD1 ILE A 162 2006 1524 1927 168 385 -15 A C ATOM 1300 N ASN A 163 62.267 -27.983 38.186 1.00 12.24 A N ANISOU 1300 N ASN A 163 1724 1028 1898 202 -55 -127 A N ATOM 1301 CA ASN A 163 63.486 -28.602 38.725 1.00 14.37 A C ANISOU 1301 CA ASN A 163 1954 1441 2064 538 -35 -193 A C ATOM 1302 C ASN A 163 63.589 -28.421 40.254 1.00 14.34 A C ANISOU 1302 C ASN A 163 2112 1176 2158 398 2 -123 A C ATOM 1303 O ASN A 163 64.647 -28.042 40.775 1.00 16.72 A O ANISOU 1303 O ASN A 163 2025 1810 2518 492 -294 -130 A O ATOM 1304 CB ASN A 163 64.714 -28.081 37.982 1.00 14.03 A C ANISOU 1304 CB ASN A 163 1807 1208 2316 499 -139 -207 A C ATOM 1305 CG ASN A 163 64.625 -28.275 36.483 1.00 14.04 A C ANISOU 1305 CG ASN A 163 1813 1402 2118 287 38 -58 A C ATOM 1306 ND2 ASN A 163 65.001 -27.287 35.684 1.00 14.77 A N ANISOU 1306 ND2 ASN A 163 1712 1379 2518 228 284 12 A N ATOM 1307 OD1 ASN A 163 64.257 -29.362 36.025 1.00 15.16 A O ANISOU 1307 OD1 ASN A 163 1802 1344 2613 204 50 -321 A O ATOM 1308 N ASP A 164 62.468 -28.675 40.955 1.00 14.65 A N ANISOU 1308 N ASP A 164 2289 1059 2217 283 130 16 A N ATOM 1309 CA ASP A 164 62.318 -28.547 42.424 1.00 16.08 A C ANISOU 1309 CA ASP A 164 1985 1843 2278 426 60 -82 A C ATOM 1310 C ASP A 164 62.630 -27.146 42.966 1.00 17.55 A C ANISOU 1310 C ASP A 164 2755 1947 1965 194 -105 15 A C ATOM 1311 O ASP A 164 62.975 -27.016 44.142 1.00 21.89 A O ANISOU 1311 O ASP A 164 4036 2119 2161 459 -619 -198 A O ATOM 1312 CB ASP A 164 63.135 -29.586 43.203 1.00 19.18 A C ANISOU 1312 CB ASP A 164 3098 1837 2352 782 -58 -107 A C ATOM 1313 CG ASP A 164 62.641 -29.760 44.645 1.00 23.02 A C ANISOU 1313 CG ASP A 164 3606 2569 2570 10 -80 -96 A C ATOM 1314 OD1 ASP A 164 61.387 -29.567 44.927 1.00 23.82 A O ANISOU 1314 OD1 ASP A 164 3696 2632 2722 -349 30 -106 A O ATOM 1315 OD2 ASP A 164 63.488 -30.069 45.488 1.00 31.29 A O ANISOU 1315 OD2 ASP A 164 4545 3444 3899 1038 -1038 -192 A O ATOM 1316 N GLN A 165 62.470 -26.115 42.152 1.00 13.54 A N ANISOU 1316 N GLN A 165 1969 1571 1602 483 -219 -409 A N ATOM 1317 CA GLN A 165 62.534 -24.737 42.628 1.00 15.28 A C ANISOU 1317 CA GLN A 165 1994 1611 2199 448 -346 -511 A C ATOM 1318 C GLN A 165 61.138 -24.134 42.493 1.00 12.70 A C ANISOU 1318 C GLN A 165 1897 1042 1883 204 -80 -99 A C ATOM 1319 O GLN A 165 60.551 -24.162 41.389 1.00 13.43 A O ANISOU 1319 O GLN A 165 2053 1250 1798 340 -79 -323 A O ATOM 1320 CB GLN A 165 63.529 -23.965 41.781 1.00 16.21 A C ANISOU 1320 CB GLN A 165 1888 1523 2747 389 -280 -279 A C ATOM 1321 CG GLN A 165 64.928 -24.545 41.817 1.00 18.98 A C ANISOU 1321 CG GLN A 165 1995 1905 3312 479 132 -81 A C ATOM 1322 CD GLN A 165 65.674 -24.257 40.534 1.00 24.55 A C ANISOU 1322 CD GLN A 165 2783 2695 3848 -452 347 83 A C ATOM 1323 NE2 GLN A 165 66.663 -23.406 40.669 1.00 24.99 A N ANISOU 1323 NE2 GLN A 165 2610 3156 3729 -676 -471 -9 A N ATOM 1324 OE1 GLN A 165 65.363 -24.786 39.435 1.00 32.08 A O ANISOU 1324 OE1 GLN A 165 4177 3093 4918 243 52 -774 A O ATOM 1325 N ARG A 166 60.634 -23.535 43.572 1.00 13.99 A N ANISOU 1325 N ARG A 166 1914 1474 1927 437 -155 -281 A N ATOM 1326 CA ARG A 166 59.328 -22.912 43.508 1.00 13.32 A C ANISOU 1326 CA ARG A 166 1815 1369 1876 322 32 -106 A C ATOM 1327 C ARG A 166 59.325 -21.809 42.445 1.00 13.19 A C ANISOU 1327 C ARG A 166 1700 1356 1956 109 -63 -13 A C ATOM 1328 O ARG A 166 60.230 -20.989 42.409 1.00 14.48 A O ANISOU 1328 O ARG A 166 1711 1617 2172 100 -86 -236 A O ATOM 1329 CB ARG A 166 58.896 -22.356 44.869 1.00 14.20 A C ANISOU 1329 CB ARG A 166 2114 1333 1946 245 159 -162 A C ATOM 1330 CG ARG A 166 57.395 -22.050 44.886 1.00 15.29 A C ANISOU 1330 CG ARG A 166 2212 1396 2198 355 297 149 A C ATOM 1331 CD ARG A 166 56.964 -21.354 46.143 1.00 17.29 A C ANISOU 1331 CD ARG A 166 2491 1670 2405 481 75 139 A C ATOM 1332 NE ARG A 166 55.527 -21.467 46.331 1.00 17.74 A N ANISOU 1332 NE ARG A 166 2333 1670 2738 605 519 317 A N ATOM 1333 CZ ARG A 166 54.628 -20.605 45.826 1.00 15.25 A C ANISOU 1333 CZ ARG A 166 2009 1111 2672 74 252 233 A C ATOM 1334 NH1 ARG A 166 55.005 -19.635 44.977 1.00 13.74 A N ANISOU 1334 NH1 ARG A 166 1946 1232 2042 65 167 97 A N ATOM 1335 NH2 ARG A 166 53.365 -20.714 46.210 1.00 15.77 A N ANISOU 1335 NH2 ARG A 166 2069 1250 2672 248 489 122 A N ATOM 1336 N VAL A 167 58.270 -21.753 41.635 1.00 12.34 A N ANISOU 1336 N VAL A 167 1614 998 2074 100 12 36 A N ATOM 1337 CA VAL A 167 58.087 -20.692 40.659 1.00 12.12 A C ANISOU 1337 CA VAL A 167 1401 1265 1938 182 -8 101 A C ATOM 1338 C VAL A 167 57.371 -19.530 41.334 1.00 12.37 A C ANISOU 1338 C VAL A 167 1586 1139 1973 -41 167 10 A C ATOM 1339 O VAL A 167 56.240 -19.643 41.705 1.00 13.12 A O ANISOU 1339 O VAL A 167 1583 1000 2400 124 176 -151 A O ATOM 1340 CB VAL A 167 57.311 -21.127 39.416 1.00 11.78 A C ANISOU 1340 CB VAL A 167 1516 1138 1819 213 110 -100 A C ATOM 1341 CG1 VAL A 167 57.077 -19.981 38.453 1.00 13.91 A C ANISOU 1341 CG1 VAL A 167 2089 1341 1855 140 -139 -37 A C ATOM 1342 CG2 VAL A 167 57.997 -22.320 38.751 1.00 12.38 A C ANISOU 1342 CG2 VAL A 167 1514 1338 1850 147 157 -279 A C ATOM 1343 N GLY A 168 58.098 -18.413 41.441 1.00 11.60 A N ANISOU 1343 N GLY A 168 1436 1093 1877 56 241 -215 A N ATOM 1344 CA GLY A 168 57.570 -17.204 42.033 1.00 12.29 A C ANISOU 1344 CA GLY A 168 1740 1000 1927 254 71 -32 A C ATOM 1345 C GLY A 168 57.318 -17.318 43.520 1.00 12.16 A C ANISOU 1345 C GLY A 168 1318 1418 1884 169 12 -17 A C ATOM 1346 O GLY A 168 57.592 -18.340 44.147 1.00 13.41 A O ANISOU 1346 O GLY A 168 1969 1415 1710 -15 72 81 A O ATOM 1347 N ASP A 169 56.700 -16.275 44.060 1.00 13.07 A N ANISOU 1347 N ASP A 169 1573 1381 2011 133 112 -127 A N ATOM 1348 CA ASP A 169 56.387 -16.158 45.490 1.00 14.54 A C ANISOU 1348 CA ASP A 169 1755 1641 2127 97 115 -195 A C ATOM 1349 C ASP A 169 54.913 -15.803 45.723 1.00 12.10 A C ANISOU 1349 C ASP A 169 1711 1261 1623 104 82 -27 A C ATOM 1350 O ASP A 169 54.532 -15.271 46.782 1.00 14.15 A O ANISOU 1350 O ASP A 169 2053 1565 1758 252 -32 -292 A O ATOM 1351 CB ASP A 169 57.303 -15.155 46.166 1.00 15.63 A C ANISOU 1351 CB ASP A 169 1832 1923 2182 -27 -60 -163 A C ATOM 1352 CG ASP A 169 57.216 -13.751 45.604 1.00 16.19 A C ANISOU 1352 CG ASP A 169 1832 1854 2463 111 119 -254 A C ATOM 1353 OD1 ASP A 169 56.397 -13.531 44.705 1.00 16.06 A O ANISOU 1353 OD1 ASP A 169 2179 1579 2344 18 103 -303 A O ATOM 1354 OD2 ASP A 169 57.981 -12.898 46.088 1.00 19.88 A O ANISOU 1354 OD2 ASP A 169 2272 2154 3125 43 -296 -452 A O ATOM 1355 N HIS A 170 54.064 -16.067 44.726 1.00 11.32 A N ANISOU 1355 N HIS A 170 1501 1004 1793 68 155 -170 A N ATOM 1356 CA HIS A 170 52.647 -15.872 44.885 1.00 11.42 A C ANISOU 1356 CA HIS A 170 1536 1136 1665 182 101 -98 A C ATOM 1357 C HIS A 170 52.029 -17.071 45.604 1.00 12.21 A C ANISOU 1357 C HIS A 170 1695 1019 1924 146 42 -61 A C ATOM 1358 O HIS A 170 52.312 -18.251 45.236 1.00 13.66 A O ANISOU 1358 O HIS A 170 1801 996 2392 140 334 -128 A O ATOM 1359 CB HIS A 170 51.915 -15.698 43.549 1.00 12.23 A C ANISOU 1359 CB HIS A 170 1888 1158 1599 279 20 -271 A C ATOM 1360 CG HIS A 170 52.423 -14.633 42.640 1.00 14.37 A C ANISOU 1360 CG HIS A 170 2171 1246 2040 437 82 -15 A C ATOM 1361 CD2 HIS A 170 53.591 -13.949 42.591 1.00 16.29 A C ANISOU 1361 CD2 HIS A 170 2215 1665 2309 587 199 113 A C ATOM 1362 ND1 HIS A 170 51.691 -14.271 41.536 1.00 14.81 A N ANISOU 1362 ND1 HIS A 170 2641 921 2064 466 9 -66 A N ATOM 1363 CE1 HIS A 170 52.369 -13.332 40.869 1.00 14.74 A C ANISOU 1363 CE1 HIS A 170 2331 1081 2187 576 72 219 A C ATOM 1364 NE2 HIS A 170 53.545 -13.135 41.478 1.00 15.45 A N ANISOU 1364 NE2 HIS A 170 2418 1347 2105 558 158 -127 A N ATOM 1365 N VAL A 171 51.129 -16.824 46.548 1.00 10.15 A N ANISOU 1365 N VAL A 171 1536 537 1782 -21 -74 -51 A N ATOM 1366 CA VAL A 171 50.400 -17.885 47.222 1.00 10.27 A C ANISOU 1366 CA VAL A 171 1597 798 1505 -81 -94 49 A C ATOM 1367 C VAL A 171 48.914 -17.657 46.989 1.00 10.66 A C ANISOU 1367 C VAL A 171 1498 1128 1421 98 126 47 A C ATOM 1368 O VAL A 171 48.486 -16.582 46.535 1.00 10.94 A O ANISOU 1368 O VAL A 171 1541 896 1716 115 -64 -143 A O ATOM 1369 CB VAL A 171 50.738 -17.994 48.714 1.00 10.47 A C ANISOU 1369 CB VAL A 171 1614 860 1502 124 -122 75 A C ATOM 1370 CG1 VAL A 171 52.190 -18.370 48.899 1.00 12.58 A C ANISOU 1370 CG1 VAL A 171 1701 1304 1773 55 -294 -123 A C ATOM 1371 CG2 VAL A 171 50.386 -16.727 49.459 1.00 12.93 A C ANISOU 1371 CG2 VAL A 171 1979 992 1939 117 -86 -148 A C ATOM 1372 N MET A 172 48.098 -18.660 47.278 1.00 10.69 A N ANISOU 1372 N MET A 172 1519 1011 1529 22 -51 -27 A N ATOM 1373 CA MET A 172 46.655 -18.621 46.995 1.00 11.18 A C ANISOU 1373 CA MET A 172 1679 877 1691 -1 -149 -228 A C ATOM 1374 C MET A 172 46.376 -18.112 45.569 1.00 10.91 A C ANISOU 1374 C MET A 172 1355 1258 1531 -70 -41 -178 A C ATOM 1375 O MET A 172 45.452 -17.335 45.318 1.00 12.00 A O ANISOU 1375 O MET A 172 1495 1510 1553 102 84 -48 A O ATOM 1376 CB MET A 172 45.892 -17.824 48.052 1.00 12.94 A C ANISOU 1376 CB MET A 172 1872 1383 1658 106 -124 -240 A C ATOM 1377 CG MET A 172 46.119 -18.356 49.471 1.00 12.40 A C ANISOU 1377 CG MET A 172 2003 988 1718 324 -143 -243 A C ATOM 1378 SD MET A 172 45.631 -20.039 49.734 1.00 16.06 A S ANISOU 1378 SD MET A 172 2715 1232 2154 295 122 88 A S ATOM 1379 CE MET A 172 43.860 -19.847 49.839 1.00 16.47 A C ANISOU 1379 CE MET A 172 2726 1576 1954 40 358 -192 A C ATOM 1380 N ALA A 173 47.182 -18.581 44.605 1.00 10.29 A N ANISOU 1380 N ALA A 173 1631 975 1301 2 -28 -31 A N ATOM 1381 CA ALA A 173 47.172 -18.108 43.236 1.00 10.05 A C ANISOU 1381 CA ALA A 173 1485 1014 1317 33 -92 -22 A C ATOM 1382 C ALA A 173 46.250 -18.961 42.388 1.00 9.15 A C ANISOU 1382 C ALA A 173 1506 689 1279 19 48 -3 A C ATOM 1383 O ALA A 173 46.277 -20.199 42.521 1.00 10.04 A O ANISOU 1383 O ALA A 173 1567 670 1577 33 83 -3 A O ATOM 1384 CB ALA A 173 48.578 -18.154 42.686 1.00 11.04 A C ANISOU 1384 CB ALA A 173 1591 1024 1577 40 -8 -11 A C ATOM 1385 N PRO A 174 45.451 -18.402 41.465 1.00 9.49 A N ANISOU 1385 N PRO A 174 1658 607 1337 -52 -40 17 A N ATOM 1386 CA PRO A 174 45.441 -16.996 41.035 1.00 10.03 A C ANISOU 1386 CA PRO A 174 1550 588 1672 -75 172 -2 A C ATOM 1387 C PRO A 174 44.517 -16.060 41.795 1.00 10.18 A C ANISOU 1387 C PRO A 174 1648 781 1438 60 159 19 A C ATOM 1388 O PRO A 174 44.391 -14.896 41.394 1.00 11.56 A O ANISOU 1388 O PRO A 174 1658 858 1873 -23 74 238 A O ATOM 1389 CB PRO A 174 44.950 -17.154 39.574 1.00 11.96 A C ANISOU 1389 CB PRO A 174 1615 1094 1836 114 14 -20 A C ATOM 1390 CG PRO A 174 43.915 -18.258 39.676 1.00 11.80 A C ANISOU 1390 CG PRO A 174 1821 1150 1513 -13 -112 -86 A C ATOM 1391 CD PRO A 174 44.594 -19.220 40.610 1.00 10.42 A C ANISOU 1391 CD PRO A 174 1442 979 1535 -94 -60 -164 A C ATOM 1392 N GLY A 175 43.934 -16.506 42.903 1.00 9.91 A N ANISOU 1392 N GLY A 175 1445 895 1423 114 62 2 A N ATOM 1393 CA GLY A 175 43.035 -15.660 43.670 1.00 9.45 A C ANISOU 1393 CA GLY A 175 1591 770 1228 32 17 -94 A C ATOM 1394 C GLY A 175 41.590 -15.898 43.243 1.00 10.31 A C ANISOU 1394 C GLY A 175 1516 1027 1373 34 23 -142 A C ATOM 1395 O GLY A 175 41.311 -16.860 42.482 1.00 11.15 A O ANISOU 1395 O GLY A 175 1478 1052 1705 28 -94 -262 A O ATOM 1396 N TRP A 176 40.675 -15.084 43.747 1.00 9.86 A N ANISOU 1396 N TRP A 176 1316 864 1567 34 -60 -61 A N ATOM 1397 CA TRP A 176 39.257 -15.251 43.544 1.00 9.32 A C ANISOU 1397 CA TRP A 176 1309 773 1459 146 1 -180 A C ATOM 1398 C TRP A 176 38.692 -14.177 42.608 1.00 10.22 A C ANISOU 1398 C TRP A 176 1565 868 1448 219 33 -68 A C ATOM 1399 O TRP A 176 38.517 -13.018 43.030 1.00 11.04 A O ANISOU 1399 O TRP A 176 1772 844 1579 64 -40 -140 A O ATOM 1400 CB TRP A 176 38.487 -15.279 44.864 1.00 9.29 A C ANISOU 1400 CB TRP A 176 1415 677 1436 100 22 -225 A C ATOM 1401 CG TRP A 176 37.069 -15.725 44.709 1.00 9.41 A C ANISOU 1401 CG TRP A 176 1465 661 1446 91 67 98 A C ATOM 1402 CD1 TRP A 176 36.467 -16.221 43.588 1.00 10.33 A C ANISOU 1402 CD1 TRP A 176 1500 710 1712 120 9 -89 A C ATOM 1403 CD2 TRP A 176 36.062 -15.722 45.732 1.00 9.09 A C ANISOU 1403 CD2 TRP A 176 1324 642 1488 26 78 -117 A C ATOM 1404 CE2 TRP A 176 34.886 -16.261 45.156 1.00 9.77 A C ANISOU 1404 CE2 TRP A 176 1397 782 1532 6 6 -26 A C ATOM 1405 CE3 TRP A 176 36.049 -15.337 47.074 1.00 10.20 A C ANISOU 1405 CE3 TRP A 176 1545 821 1506 75 121 -217 A C ATOM 1406 NE1 TRP A 176 35.164 -16.564 43.851 1.00 10.44 A N ANISOU 1406 NE1 TRP A 176 1580 739 1647 -55 50 -115 A N ATOM 1407 CZ2 TRP A 176 33.723 -16.445 45.889 1.00 9.99 A C ANISOU 1407 CZ2 TRP A 176 1385 774 1634 -115 37 -115 A C ATOM 1408 CZ3 TRP A 176 34.889 -15.487 47.796 1.00 10.67 A C ANISOU 1408 CZ3 TRP A 176 1498 849 1706 148 135 -151 A C ATOM 1409 CH2 TRP A 176 33.750 -16.065 47.213 1.00 11.63 A C ANISOU 1409 CH2 TRP A 176 1600 1156 1663 -139 254 -185 A C ATOM 1410 N GLN A 177 38.455 -14.534 41.343 1.00 9.90 A N ANISOU 1410 N GLN A 177 1416 829 1515 200 11 -117 A N ATOM 1411 CA GLN A 177 37.752 -13.694 40.366 1.00 9.87 A C ANISOU 1411 CA GLN A 177 1439 766 1543 93 -67 -182 A C ATOM 1412 C GLN A 177 36.330 -14.256 40.202 1.00 9.38 A C ANISOU 1412 C GLN A 177 1331 870 1361 40 29 32 A C ATOM 1413 O GLN A 177 36.074 -15.422 40.541 1.00 9.82 A O ANISOU 1413 O GLN A 177 1446 810 1471 -94 48 -98 A O ATOM 1414 CB GLN A 177 38.495 -13.638 39.023 1.00 11.00 A C ANISOU 1414 CB GLN A 177 1539 1106 1533 116 -46 -111 A C ATOM 1415 CG GLN A 177 39.900 -13.035 39.152 1.00 11.51 A C ANISOU 1415 CG GLN A 177 1505 1243 1624 140 -97 263 A C ATOM 1416 CD GLN A 177 40.975 -14.047 39.507 1.00 11.64 A C ANISOU 1416 CD GLN A 177 1646 1040 1735 242 17 32 A C ATOM 1417 NE2 GLN A 177 41.825 -13.772 40.498 1.00 10.99 A N ANISOU 1417 NE2 GLN A 177 1697 882 1597 13 53 241 A N ATOM 1418 OE1 GLN A 177 41.082 -15.110 38.852 1.00 11.07 A O ANISOU 1418 OE1 GLN A 177 1560 1083 1564 -142 165 -75 A O ATOM 1419 N SER A 178 35.477 -13.499 39.526 1.00 10.22 A N ANISOU 1419 N SER A 178 1402 867 1611 64 -93 30 A N ATOM 1420 CA SER A 178 34.205 -13.970 39.021 1.00 10.49 A C ANISOU 1420 CA SER A 178 1421 1174 1389 53 -73 98 A C ATOM 1421 C SER A 178 34.575 -14.786 37.777 1.00 10.32 A C ANISOU 1421 C SER A 178 1585 715 1621 -373 8 -1 A C ATOM 1422 O SER A 178 34.441 -14.335 36.650 1.00 11.26 A O ANISOU 1422 O SER A 178 1791 954 1532 -9 -91 -179 A O ATOM 1423 CB SER A 178 33.261 -12.830 38.711 1.00 10.88 A C ANISOU 1423 CB SER A 178 1458 1205 1470 80 -57 -13 A C ATOM 1424 OG SER A 178 32.896 -12.144 39.907 1.00 11.56 A O ANISOU 1424 OG SER A 178 1572 984 1833 -173 201 -251 A O ATOM 1425 N TYR A 179 34.967 -16.056 38.029 1.00 10.48 A N ANISOU 1425 N TYR A 179 1705 766 1510 -146 64 39 A N ATOM 1426 CA TYR A 179 35.726 -16.837 37.036 1.00 10.62 A C ANISOU 1426 CA TYR A 179 1583 1053 1398 -41 52 120 A C ATOM 1427 C TYR A 179 34.945 -17.076 35.745 1.00 11.26 A C ANISOU 1427 C TYR A 179 1761 757 1760 234 -170 -2 A C ATOM 1428 O TYR A 179 35.585 -17.241 34.694 1.00 14.73 A O ANISOU 1428 O TYR A 179 2032 1887 1678 83 -50 -246 A O ATOM 1429 CB TYR A 179 36.093 -18.212 37.583 1.00 10.66 A C ANISOU 1429 CB TYR A 179 1579 1055 1415 -43 9 39 A C ATOM 1430 CG TYR A 179 36.935 -18.206 38.822 1.00 9.36 A C ANISOU 1430 CG TYR A 179 1507 566 1482 -21 -106 -97 A C ATOM 1431 CD1 TYR A 179 38.242 -17.741 38.820 1.00 10.05 A C ANISOU 1431 CD1 TYR A 179 1499 841 1478 11 139 71 A C ATOM 1432 CD2 TYR A 179 36.447 -18.713 40.016 1.00 9.46 A C ANISOU 1432 CD2 TYR A 179 1378 557 1657 -66 -13 -122 A C ATOM 1433 CE1 TYR A 179 39.049 -17.843 39.942 1.00 9.55 A C ANISOU 1433 CE1 TYR A 179 1408 769 1449 -26 139 -157 A C ATOM 1434 CE2 TYR A 179 37.224 -18.811 41.152 1.00 9.08 A C ANISOU 1434 CE2 TYR A 179 1523 454 1472 44 83 27 A C ATOM 1435 CZ TYR A 179 38.534 -18.361 41.135 1.00 9.51 A C ANISOU 1435 CZ TYR A 179 1495 705 1411 80 93 -115 A C ATOM 1436 OH TYR A 179 39.300 -18.493 42.273 1.00 10.63 A O ANISOU 1436 OH TYR A 179 1614 886 1536 79 -65 -71 A O ATOM 1437 N GLN A 180 33.610 -17.126 35.804 1.00 11.42 A N ANISOU 1437 N GLN A 180 1785 843 1708 -97 -234 15 A N ATOM 1438 CA GLN A 180 32.858 -17.374 34.553 1.00 13.20 A C ANISOU 1438 CA GLN A 180 1699 1390 1926 182 -409 -43 A C ATOM 1439 C GLN A 180 32.953 -16.197 33.574 1.00 13.07 A C ANISOU 1439 C GLN A 180 1681 1458 1825 -283 -337 -42 A C ATOM 1440 O GLN A 180 32.577 -16.355 32.400 1.00 15.58 A O ANISOU 1440 O GLN A 180 2521 1430 1966 185 -567 -193 A O ATOM 1441 CB GLN A 180 31.398 -17.752 34.804 1.00 13.79 A C ANISOU 1441 CB GLN A 180 1851 1466 1921 -145 -170 -123 A C ATOM 1442 CG GLN A 180 30.447 -16.649 35.248 1.00 14.01 A C ANISOU 1442 CG GLN A 180 1600 1641 2079 -179 -282 -168 A C ATOM 1443 CD GLN A 180 30.417 -16.362 36.722 1.00 13.13 A C ANISOU 1443 CD GLN A 180 1877 914 2196 -273 0 17 A C ATOM 1444 NE2 GLN A 180 29.184 -16.210 37.204 1.00 14.19 A N ANISOU 1444 NE2 GLN A 180 1846 1180 2362 -97 125 138 A N ATOM 1445 OE1 GLN A 180 31.465 -16.274 37.421 1.00 13.19 A O ANISOU 1445 OE1 GLN A 180 1968 1054 1989 -44 -168 -11 A O ATOM 1446 N TYR A 181 33.341 -15.014 34.078 1.00 11.74 A N ANISOU 1446 N TYR A 181 1526 1356 1575 -207 -286 -10 A N ATOM 1447 CA TYR A 181 33.530 -13.806 33.275 1.00 12.04 A C ANISOU 1447 CA TYR A 181 1687 1325 1560 169 71 -50 A C ATOM 1448 C TYR A 181 35.011 -13.479 33.070 1.00 11.50 A C ANISOU 1448 C TYR A 181 1737 1128 1501 197 -8 -252 A C ATOM 1449 O TYR A 181 35.404 -13.087 31.971 1.00 15.77 A O ANISOU 1449 O TYR A 181 1843 2549 1599 -97 -80 258 A O ATOM 1450 CB TYR A 181 32.833 -12.621 33.934 1.00 12.28 A C ANISOU 1450 CB TYR A 181 1563 1329 1774 219 -21 -65 A C ATOM 1451 CG TYR A 181 31.362 -12.816 34.128 1.00 12.54 A C ANISOU 1451 CG TYR A 181 1631 914 2218 84 -41 -20 A C ATOM 1452 CD1 TYR A 181 30.531 -12.928 33.028 1.00 15.41 A C ANISOU 1452 CD1 TYR A 181 2047 1627 2181 -7 -170 63 A C ATOM 1453 CD2 TYR A 181 30.797 -12.888 35.392 1.00 14.00 A C ANISOU 1453 CD2 TYR A 181 1986 1087 2245 126 -72 -37 A C ATOM 1454 CE1 TYR A 181 29.174 -13.098 33.181 1.00 16.04 A C ANISOU 1454 CE1 TYR A 181 1974 1865 2255 -148 -40 -165 A C ATOM 1455 CE2 TYR A 181 29.438 -13.116 35.549 1.00 13.66 A C ANISOU 1455 CE2 TYR A 181 2107 809 2275 9 139 89 A C ATOM 1456 CZ TYR A 181 28.625 -13.175 34.442 1.00 15.27 A C ANISOU 1456 CZ TYR A 181 2035 1557 2208 27 46 66 A C ATOM 1457 OH TYR A 181 27.286 -13.399 34.533 1.00 19.40 A O ANISOU 1457 OH TYR A 181 1994 2360 3016 -53 147 -58 A O ATOM 1458 N ARG A 182 35.806 -13.630 34.118 1.00 11.12 A N ANISOU 1458 N ARG A 182 1570 982 1672 -30 -63 5 A N ATOM 1459 CA ARG A 182 37.199 -13.148 34.121 1.00 10.99 A C ANISOU 1459 CA ARG A 182 1545 980 1648 173 -38 -79 A C ATOM 1460 C ARG A 182 37.989 -14.108 34.998 1.00 10.72 A C ANISOU 1460 C ARG A 182 1380 1126 1566 59 -91 -34 A C ATOM 1461 O ARG A 182 37.570 -14.380 36.122 1.00 11.96 A O ANISOU 1461 O ARG A 182 1877 1220 1447 162 -38 -14 A O ATOM 1462 CB ARG A 182 37.264 -11.713 34.646 1.00 11.40 A C ANISOU 1462 CB ARG A 182 1688 854 1786 299 63 -7 A C ATOM 1463 CG ARG A 182 38.645 -11.070 34.576 1.00 12.35 A C ANISOU 1463 CG ARG A 182 1801 900 1989 158 95 14 A C ATOM 1464 CD ARG A 182 38.630 -9.649 35.086 1.00 11.44 A C ANISOU 1464 CD ARG A 182 1639 913 1795 195 -189 18 A C ATOM 1465 NE ARG A 182 38.413 -9.621 36.529 1.00 11.26 A N ANISOU 1465 NE ARG A 182 1729 667 1882 37 -150 -35 A N ATOM 1466 CZ ARG A 182 39.355 -9.705 37.492 1.00 10.33 A C ANISOU 1466 CZ ARG A 182 1502 717 1703 147 -18 -73 A C ATOM 1467 NH1 ARG A 182 40.660 -9.543 37.198 1.00 11.53 A N ANISOU 1467 NH1 ARG A 182 1582 847 1950 153 174 -214 A N ATOM 1468 NH2 ARG A 182 38.944 -9.939 38.752 1.00 10.77 A N ANISOU 1468 NH2 ARG A 182 1938 436 1717 107 -30 -113 A N ATOM 1469 N HIS A 183 39.096 -14.594 34.443 1.00 10.00 A N ANISOU 1469 N HIS A 183 1419 998 1379 -62 60 87 A N ATOM 1470 CA HIS A 183 39.888 -15.592 35.166 1.00 9.96 A C ANISOU 1470 CA HIS A 183 1414 746 1624 35 84 -80 A C ATOM 1471 C HIS A 183 41.356 -15.202 35.022 1.00 8.60 A C ANISOU 1471 C HIS A 183 1423 370 1472 36 -73 -6 A C ATOM 1472 O HIS A 183 41.887 -15.165 33.908 1.00 10.94 A O ANISOU 1472 O HIS A 183 1745 895 1514 -108 45 -149 A O ATOM 1473 CB HIS A 183 39.591 -16.976 34.615 1.00 10.75 A C ANISOU 1473 CB HIS A 183 1655 890 1537 6 -118 -192 A C ATOM 1474 CG HIS A 183 40.115 -18.150 35.373 1.00 10.11 A C ANISOU 1474 CG HIS A 183 1253 847 1740 -146 91 33 A C ATOM 1475 CD2 HIS A 183 41.282 -18.336 36.021 1.00 10.78 A C ANISOU 1475 CD2 HIS A 183 1669 589 1838 -82 -137 142 A C ATOM 1476 ND1 HIS A 183 39.368 -19.304 35.516 1.00 11.11 A N ANISOU 1476 ND1 HIS A 183 1376 1015 1828 -313 -27 -69 A N ATOM 1477 CE1 HIS A 183 40.075 -20.152 36.242 1.00 12.65 A C ANISOU 1477 CE1 HIS A 183 1669 1085 2050 -6 -5 -63 A C ATOM 1478 NE2 HIS A 183 41.266 -19.622 36.525 1.00 11.27 A N ANISOU 1478 NE2 HIS A 183 1847 460 1975 -93 67 -7 A N ATOM 1479 N GLU A 184 41.976 -14.818 36.150 1.00 9.37 A N ANISOU 1479 N GLU A 184 1445 917 1198 33 24 0 A N ATOM 1480 CA GLU A 184 43.345 -14.283 36.055 1.00 10.27 A C ANISOU 1480 CA GLU A 184 1351 1147 1403 29 76 -11 A C ATOM 1481 C GLU A 184 44.338 -15.412 35.827 1.00 9.98 A C ANISOU 1481 C GLU A 184 1400 968 1420 -40 84 -5 A C ATOM 1482 O GLU A 184 44.128 -16.565 36.302 1.00 10.82 A O ANISOU 1482 O GLU A 184 1579 891 1637 -48 117 -29 A O ATOM 1483 CB GLU A 184 43.792 -13.488 37.288 1.00 10.06 A C ANISOU 1483 CB GLU A 184 1577 762 1481 74 21 87 A C ATOM 1484 CG GLU A 184 43.154 -12.105 37.335 1.00 10.76 A C ANISOU 1484 CG GLU A 184 1577 711 1799 8 -100 -28 A C ATOM 1485 CD GLU A 184 43.459 -11.301 38.573 1.00 10.88 A C ANISOU 1485 CD GLU A 184 1447 959 1726 -18 42 -84 A C ATOM 1486 OE1 GLU A 184 44.435 -11.616 39.287 1.00 12.04 A O ANISOU 1486 OE1 GLU A 184 1637 904 2031 -10 -102 -77 A O ATOM 1487 OE2 GLU A 184 42.747 -10.278 38.803 1.00 11.59 A O ANISOU 1487 OE2 GLU A 184 1620 998 1782 227 -74 -81 A O ATOM 1488 N TYR A 185 45.386 -15.125 35.057 1.00 10.48 A N ANISOU 1488 N TYR A 185 1429 786 1764 -7 133 114 A N ATOM 1489 CA TYR A 185 46.526 -16.013 34.920 1.00 10.22 A C ANISOU 1489 CA TYR A 185 1217 1065 1600 -7 181 -59 A C ATOM 1490 C TYR A 185 47.784 -15.219 35.250 1.00 8.39 A C ANISOU 1490 C TYR A 185 1274 550 1362 37 294 -98 A C ATOM 1491 O TYR A 185 47.801 -13.965 35.147 1.00 9.74 A O ANISOU 1491 O TYR A 185 1484 508 1708 -6 6 -116 A O ATOM 1492 CB TYR A 185 46.674 -16.647 33.523 1.00 10.40 A C ANISOU 1492 CB TYR A 185 1572 829 1549 35 -10 -28 A C ATOM 1493 CG TYR A 185 47.121 -15.642 32.497 1.00 11.34 A C ANISOU 1493 CG TYR A 185 1646 940 1722 -92 90 -29 A C ATOM 1494 CD1 TYR A 185 46.222 -14.814 31.856 1.00 11.58 A C ANISOU 1494 CD1 TYR A 185 1478 1340 1580 91 183 -26 A C ATOM 1495 CD2 TYR A 185 48.448 -15.563 32.153 1.00 11.66 A C ANISOU 1495 CD2 TYR A 185 1703 927 1797 -9 156 -95 A C ATOM 1496 CE1 TYR A 185 46.677 -13.830 30.984 1.00 11.55 A C ANISOU 1496 CE1 TYR A 185 1739 903 1745 102 17 -71 A C ATOM 1497 CE2 TYR A 185 48.909 -14.597 31.276 1.00 12.10 A C ANISOU 1497 CE2 TYR A 185 1533 1233 1830 21 293 51 A C ATOM 1498 CZ TYR A 185 48.016 -13.742 30.676 1.00 13.43 A C ANISOU 1498 CZ TYR A 185 1882 1464 1756 22 122 112 A C ATOM 1499 OH TYR A 185 48.515 -12.807 29.806 1.00 14.30 A O ANISOU 1499 OH TYR A 185 2267 1180 1986 -68 394 43 A O ATOM 1500 N ASN A 186 48.829 -15.890 35.684 1.00 9.79 A N ANISOU 1500 N ASN A 186 1278 742 1699 97 129 1 A N ATOM 1501 CA ASN A 186 50.063 -15.293 36.145 1.00 9.15 A C ANISOU 1501 CA ASN A 186 1373 539 1562 240 149 -171 A C ATOM 1502 C ASN A 186 51.217 -15.535 35.188 1.00 9.96 A C ANISOU 1502 C ASN A 186 1375 648 1761 38 279 -183 A C ATOM 1503 O ASN A 186 51.243 -16.548 34.493 1.00 10.29 A O ANISOU 1503 O ASN A 186 1677 625 1608 30 304 -180 A O ATOM 1504 CB ASN A 186 50.408 -15.691 37.569 1.00 10.18 A C ANISOU 1504 CB ASN A 186 1513 720 1634 118 -34 -138 A C ATOM 1505 CG ASN A 186 49.238 -15.458 38.498 1.00 10.77 A C ANISOU 1505 CG ASN A 186 1595 673 1821 122 107 -25 A C ATOM 1506 ND2 ASN A 186 48.745 -14.227 38.522 1.00 11.98 A N ANISOU 1506 ND2 ASN A 186 1666 881 2005 469 10 -86 A N ATOM 1507 OD1 ASN A 186 48.736 -16.389 39.160 1.00 12.45 A O ANISOU 1507 OD1 ASN A 186 1815 890 2026 -106 102 77 A O ATOM 1508 N THR A 187 52.182 -14.625 35.191 1.00 10.21 A N ANISOU 1508 N THR A 187 1506 728 1643 -134 339 -85 A N ATOM 1509 CA THR A 187 53.360 -14.689 34.368 1.00 9.80 A C ANISOU 1509 CA THR A 187 1438 654 1629 37 146 60 A C ATOM 1510 C THR A 187 54.603 -14.641 35.259 1.00 10.90 A C ANISOU 1510 C THR A 187 1473 1025 1642 97 39 -195 A C ATOM 1511 O THR A 187 54.723 -13.759 36.143 1.00 12.13 A O ANISOU 1511 O THR A 187 1693 1107 1806 -66 25 -296 A O ATOM 1512 CB THR A 187 53.397 -13.522 33.375 1.00 10.09 A C ANISOU 1512 CB THR A 187 1502 718 1611 -21 185 101 A C ATOM 1513 CG2 THR A 187 54.622 -13.619 32.482 1.00 11.62 A C ANISOU 1513 CG2 THR A 187 1525 928 1960 -95 353 128 A C ATOM 1514 OG1 THR A 187 52.223 -13.547 32.569 1.00 11.09 A O ANISOU 1514 OG1 THR A 187 1669 770 1775 -33 13 7 A O ATOM 1515 N TYR A 188 55.556 -15.556 35.014 1.00 10.86 A N ANISOU 1515 N TYR A 188 1459 940 1725 95 52 35 A N ATOM 1516 CA TYR A 188 56.783 -15.616 35.786 1.00 10.37 A C ANISOU 1516 CA TYR A 188 1502 598 1839 81 11 -218 A C ATOM 1517 C TYR A 188 57.982 -15.673 34.838 1.00 12.20 A C ANISOU 1517 C TYR A 188 1502 1285 1847 85 -47 -19 A C ATOM 1518 O TYR A 188 57.956 -16.369 33.806 1.00 12.66 A O ANISOU 1518 O TYR A 188 1744 1143 1920 -187 202 -126 A O ATOM 1519 CB TYR A 188 56.796 -16.871 36.653 1.00 10.98 A C ANISOU 1519 CB TYR A 188 1496 801 1873 160 277 -104 A C ATOM 1520 CG TYR A 188 55.645 -16.940 37.623 1.00 10.53 A C ANISOU 1520 CG TYR A 188 1257 1144 1600 45 92 -29 A C ATOM 1521 CD1 TYR A 188 55.678 -16.259 38.839 1.00 11.34 A C ANISOU 1521 CD1 TYR A 188 1479 1056 1771 160 62 -125 A C ATOM 1522 CD2 TYR A 188 54.510 -17.693 37.344 1.00 9.77 A C ANISOU 1522 CD2 TYR A 188 1382 871 1460 88 40 -170 A C ATOM 1523 CE1 TYR A 188 54.614 -16.300 39.734 1.00 11.35 A C ANISOU 1523 CE1 TYR A 188 1459 1138 1715 123 14 -334 A C ATOM 1524 CE2 TYR A 188 53.469 -17.788 38.258 1.00 10.03 A C ANISOU 1524 CE2 TYR A 188 1414 731 1664 -71 18 -96 A C ATOM 1525 CZ TYR A 188 53.514 -17.124 39.476 1.00 10.44 A C ANISOU 1525 CZ TYR A 188 1428 1005 1534 78 84 -142 A C ATOM 1526 OH TYR A 188 52.507 -17.244 40.387 1.00 11.31 A O ANISOU 1526 OH TYR A 188 1459 1083 1753 93 54 -213 A O ATOM 1527 N ASP A 189 59.065 -15.025 35.262 1.00 11.46 A N ANISOU 1527 N ASP A 189 1484 884 1983 97 76 -212 A N ATOM 1528 CA ASP A 189 60.347 -15.145 34.584 1.00 12.52 A C ANISOU 1528 CA ASP A 189 1519 1136 2099 -50 229 -51 A C ATOM 1529 C ASP A 189 61.092 -16.348 35.174 1.00 13.84 A C ANISOU 1529 C ASP A 189 1762 1457 2039 243 343 -63 A C ATOM 1530 O ASP A 189 61.545 -16.317 36.315 1.00 14.44 A O ANISOU 1530 O ASP A 189 1919 1274 2294 255 97 -201 A O ATOM 1531 CB ASP A 189 61.147 -13.866 34.721 1.00 13.65 A C ANISOU 1531 CB ASP A 189 1804 1128 2250 -83 140 -176 A C ATOM 1532 CG ASP A 189 62.543 -13.936 34.130 1.00 16.90 A C ANISOU 1532 CG ASP A 189 1947 1617 2858 -254 523 -327 A C ATOM 1533 OD1 ASP A 189 62.927 -15.022 33.645 1.00 16.19 A O ANISOU 1533 OD1 ASP A 189 1624 1608 2918 -40 476 -273 A O ATOM 1534 OD2 ASP A 189 63.241 -12.880 34.162 1.00 20.82 A O ANISOU 1534 OD2 ASP A 189 2123 1826 3961 -407 1045 -266 A O ATOM 1535 N VAL A 190 61.110 -17.441 34.420 1.00 13.44 A N ANISOU 1535 N VAL A 190 1564 1456 2084 79 55 -123 A N ATOM 1536 CA VAL A 190 61.690 -18.701 34.896 1.00 13.60 A C ANISOU 1536 CA VAL A 190 1649 1342 2175 -40 373 231 A C ATOM 1537 C VAL A 190 63.045 -18.983 34.227 1.00 13.66 A C ANISOU 1537 C VAL A 190 1462 1307 2418 220 140 25 A C ATOM 1538 O VAL A 190 63.555 -20.108 34.297 1.00 14.06 A O ANISOU 1538 O VAL A 190 1493 1266 2583 273 155 -148 A O ATOM 1539 CB VAL A 190 60.713 -19.874 34.736 1.00 14.21 A C ANISOU 1539 CB VAL A 190 1749 1393 2257 -20 42 162 A C ATOM 1540 CG1 VAL A 190 59.450 -19.622 35.515 1.00 14.90 A C ANISOU 1540 CG1 VAL A 190 1758 1248 2654 186 98 183 A C ATOM 1541 CG2 VAL A 190 60.410 -20.192 33.294 1.00 14.03 A C ANISOU 1541 CG2 VAL A 190 1836 1305 2189 169 312 -15 A C ATOM 1542 N THR A 191 63.673 -17.974 33.639 1.00 14.91 A N ANISOU 1542 N THR A 191 1549 1566 2547 -87 222 -125 A N ATOM 1543 CA THR A 191 64.959 -18.102 32.955 1.00 15.11 A C ANISOU 1543 CA THR A 191 1548 1543 2649 57 124 -214 A C ATOM 1544 C THR A 191 65.971 -18.871 33.816 1.00 15.05 A C ANISOU 1544 C THR A 191 1514 1746 2457 208 316 -171 A C ATOM 1545 O THR A 191 66.652 -19.771 33.294 1.00 17.80 A O ANISOU 1545 O THR A 191 2009 1488 3264 476 166 -240 A O ATOM 1546 CB THR A 191 65.536 -16.720 32.635 1.00 15.79 A C ANISOU 1546 CB THR A 191 1668 1844 2485 -47 270 134 A C ATOM 1547 CG2 THR A 191 66.842 -16.785 31.868 1.00 19.92 A C ANISOU 1547 CG2 THR A 191 1541 2366 3661 -55 505 263 A C ATOM 1548 OG1 THR A 191 64.567 -16.043 31.830 1.00 15.32 A O ANISOU 1548 OG1 THR A 191 1499 1660 2660 -24 176 -91 A O ATOM 1549 N ASP A 192 66.083 -18.509 35.102 1.00 15.60 A N ANISOU 1549 N ASP A 192 1868 1535 2524 78 -119 -12 A N ATOM 1550 CA ASP A 192 67.160 -19.000 35.947 1.00 17.00 A C ANISOU 1550 CA ASP A 192 1833 1735 2890 16 -236 56 A C ATOM 1551 C ASP A 192 66.802 -20.355 36.585 1.00 16.88 A C ANISOU 1551 C ASP A 192 1756 1846 2810 -93 -377 103 A C ATOM 1552 O ASP A 192 67.670 -20.958 37.237 1.00 18.97 A O ANISOU 1552 O ASP A 192 2072 2118 3016 52 -227 642 A O ATOM 1553 CB ASP A 192 67.515 -17.949 36.991 1.00 21.50 A C ANISOU 1553 CB ASP A 192 2644 2397 3128 -179 -295 -261 A C ATOM 1554 CG ASP A 192 68.231 -16.723 36.429 1.00 27.95 A C ANISOU 1554 CG ASP A 192 3522 2913 4183 -321 -204 276 A C ATOM 1555 OD1 ASP A 192 68.729 -16.765 35.245 1.00 29.45 A O ANISOU 1555 OD1 ASP A 192 3135 3408 4646 -847 -431 450 A O ATOM 1556 OD2 ASP A 192 68.308 -15.736 37.185 1.00 34.27 A O ANISOU 1556 OD2 ASP A 192 3996 3339 5684 -582 365 -833 A O ATOM 1557 N LEU A 193 65.556 -20.826 36.427 1.00 15.04 A N ANISOU 1557 N LEU A 193 1578 1583 2553 158 -196 52 A N ATOM 1558 CA LEU A 193 65.155 -22.122 37.003 1.00 14.32 A C ANISOU 1558 CA LEU A 193 1754 1361 2326 193 -150 -101 A C ATOM 1559 C LEU A 193 65.444 -23.259 36.027 1.00 15.41 A C ANISOU 1559 C LEU A 193 1932 1355 2565 299 -129 -58 A C ATOM 1560 O LEU A 193 65.529 -24.419 36.450 1.00 15.26 A O ANISOU 1560 O LEU A 193 1751 1201 2846 301 -85 -47 A O ATOM 1561 CB LEU A 193 63.658 -22.103 37.344 1.00 14.44 A C ANISOU 1561 CB LEU A 193 1959 965 2563 246 114 15 A C ATOM 1562 CG LEU A 193 63.185 -20.982 38.256 1.00 15.32 A C ANISOU 1562 CG LEU A 193 1964 1366 2491 152 232 -141 A C ATOM 1563 CD1 LEU A 193 61.745 -21.192 38.666 1.00 15.89 A C ANISOU 1563 CD1 LEU A 193 2102 1582 2352 24 196 -160 A C ATOM 1564 CD2 LEU A 193 64.031 -20.834 39.491 1.00 18.41 A C ANISOU 1564 CD2 LEU A 193 2431 1762 2802 285 -37 39 A C ATOM 1565 N LEU A 194 65.540 -22.954 34.726 1.00 16.46 A N ANISOU 1565 N LEU A 194 2431 1208 2614 160 156 -292 A N ATOM 1566 CA LEU A 194 65.840 -23.976 33.738 1.00 16.91 A C ANISOU 1566 CA LEU A 194 2251 1571 2601 -81 134 -479 A C ATOM 1567 C LEU A 194 67.311 -24.380 33.811 1.00 18.69 A C ANISOU 1567 C LEU A 194 2324 1860 2917 60 -6 -660 A C ATOM 1568 O LEU A 194 68.187 -23.670 34.350 1.00 20.62 A O ANISOU 1568 O LEU A 194 2226 2298 3308 -1 101 -780 A O ATOM 1569 CB LEU A 194 65.534 -23.471 32.338 1.00 18.10 A C ANISOU 1569 CB LEU A 194 2534 1318 3024 -325 140 8 A C ATOM 1570 CG LEU A 194 64.090 -23.106 32.037 1.00 20.69 A C ANISOU 1570 CG LEU A 194 2929 1826 3106 280 -296 -26 A C ATOM 1571 CD1 LEU A 194 63.993 -22.539 30.610 1.00 22.92 A C ANISOU 1571 CD1 LEU A 194 3596 1820 3291 581 216 80 A C ATOM 1572 CD2 LEU A 194 63.230 -24.332 32.142 1.00 20.18 A C ANISOU 1572 CD2 LEU A 194 2143 2365 3159 190 -169 122 A C ATOM 1573 N LYS A 195 67.576 -25.541 33.221 1.00 20.60 A N ANISOU 1573 N LYS A 195 1976 2329 3522 162 -93 -1200 A N ATOM 1574 CA LYS A 195 68.939 -25.936 32.941 1.00 23.75 A C ANISOU 1574 CA LYS A 195 2134 3134 3754 379 59 -774 A C ATOM 1575 C LYS A 195 69.006 -26.453 31.506 1.00 19.71 A C ANISOU 1575 C LYS A 195 1735 1893 3859 -1 458 -598 A C ATOM 1576 O LYS A 195 67.999 -26.716 30.818 1.00 19.05 A O ANISOU 1576 O LYS A 195 1870 2070 3298 -309 478 -458 A O ATOM 1577 CB LYS A 195 69.433 -26.914 34.010 1.00 32.90 A C ANISOU 1577 CB LYS A 195 3117 3726 5654 1066 -100 39 A C ATOM 1578 CG LYS A 195 68.484 -28.054 34.316 1.00 38.99 A C ANISOU 1578 CG LYS A 195 3945 4219 6647 630 -573 1061 A C ATOM 1579 CD LYS A 195 68.888 -28.928 35.501 1.00 48.03 A C ANISOU 1579 CD LYS A 195 5000 6585 6665 480 -1867 1579 A C ATOM 1580 CE LYS A 195 67.904 -30.066 35.692 1.00 54.61 A C ANISOU 1580 CE LYS A 195 4418 8645 7683 213 -52 2747 A C ATOM 1581 NZ LYS A 195 68.332 -31.004 36.758 1.00 65.57 A N ANISOU 1581 NZ LYS A 195 5035 9408 10469 2462 -563 2842 A N ATOM 1582 N GLN A 196 70.232 -26.508 31.013 1.00 24.93 A N ANISOU 1582 N GLN A 196 1827 3127 4516 -355 763 -1401 A N ATOM 1583 CA GLN A 196 70.486 -27.019 29.702 1.00 23.87 A C ANISOU 1583 CA GLN A 196 2272 2880 3917 -668 906 -573 A C ATOM 1584 C GLN A 196 70.152 -28.510 29.684 1.00 20.63 A C ANISOU 1584 C GLN A 196 2260 2439 3139 157 348 -444 A C ATOM 1585 O GLN A 196 70.518 -29.238 30.589 1.00 24.20 A O ANISOU 1585 O GLN A 196 2887 2959 3349 192 217 -165 A O ATOM 1586 CB GLN A 196 71.975 -26.817 29.397 1.00 26.57 A C ANISOU 1586 CB GLN A 196 2197 3352 4545 -518 910 -438 A C ATOM 1587 CG GLN A 196 72.273 -26.830 27.922 1.00 30.67 A C ANISOU 1587 CG GLN A 196 3242 4049 4362 -358 120 -283 A C ATOM 1588 CD GLN A 196 71.614 -25.656 27.246 1.00 33.90 A C ANISOU 1588 CD GLN A 196 3144 3706 6030 -146 166 -248 A C ATOM 1589 NE2 GLN A 196 70.668 -25.935 26.370 1.00 32.77 A N ANISOU 1589 NE2 GLN A 196 3388 4247 4814 -1425 1067 -100 A N ATOM 1590 OE1 GLN A 196 71.953 -24.513 27.500 1.00 44.04 A O ANISOU 1590 OE1 GLN A 196 5181 3991 7558 -988 -489 -541 A O ATOM 1591 N GLY A 197 69.442 -28.941 28.650 1.00 17.54 A N ANISOU 1591 N GLY A 197 2011 1766 2886 90 612 -86 A N ATOM 1592 CA GLY A 197 69.133 -30.347 28.519 1.00 17.14 A C ANISOU 1592 CA GLY A 197 1962 1731 2819 8 444 -482 A C ATOM 1593 C GLY A 197 67.796 -30.675 29.183 1.00 15.59 A C ANISOU 1593 C GLY A 197 1811 1580 2531 75 249 -198 A C ATOM 1594 O GLY A 197 66.795 -29.990 28.997 1.00 16.65 A O ANISOU 1594 O GLY A 197 1906 1687 2733 166 278 -30 A O ATOM 1595 N PRO A 198 67.732 -31.751 29.977 1.00 14.97 A N ANISOU 1595 N PRO A 198 1695 1669 2322 170 554 -230 A N ATOM 1596 CA PRO A 198 66.454 -32.212 30.544 1.00 15.00 A C ANISOU 1596 CA PRO A 198 1661 1473 2564 144 491 -178 A C ATOM 1597 C PRO A 198 65.964 -31.325 31.683 1.00 14.15 A C ANISOU 1597 C PRO A 198 1512 1622 2242 71 92 -143 A C ATOM 1598 O PRO A 198 66.773 -30.903 32.501 1.00 15.13 A O ANISOU 1598 O PRO A 198 1710 1679 2358 69 120 -593 A O ATOM 1599 CB PRO A 198 66.759 -33.658 31.006 1.00 16.38 A C ANISOU 1599 CB PRO A 198 2058 1318 2845 122 324 -349 A C ATOM 1600 CG PRO A 198 68.228 -33.685 31.198 1.00 19.56 A C ANISOU 1600 CG PRO A 198 2201 1825 3406 476 90 101 A C ATOM 1601 CD PRO A 198 68.852 -32.642 30.307 1.00 17.31 A C ANISOU 1601 CD PRO A 198 1895 1874 2808 290 216 -339 A C ATOM 1602 N ASN A 199 64.648 -31.104 31.717 1.00 12.41 A N ANISOU 1602 N ASN A 199 1528 1306 1879 176 77 -112 A N ATOM 1603 CA ASN A 199 63.987 -30.279 32.731 1.00 13.63 A C ANISOU 1603 CA ASN A 199 1769 1295 2113 153 132 -219 A C ATOM 1604 C ASN A 199 62.673 -30.954 33.136 1.00 13.64 A C ANISOU 1604 C ASN A 199 1719 1699 1762 101 138 -169 A C ATOM 1605 O ASN A 199 62.101 -31.730 32.352 1.00 13.53 A O ANISOU 1605 O ASN A 199 1732 1536 1871 22 245 -147 A O ATOM 1606 CB ASN A 199 63.671 -28.870 32.225 1.00 13.20 A C ANISOU 1606 CB ASN A 199 1819 1310 1887 245 130 -258 A C ATOM 1607 CG ASN A 199 64.901 -28.005 32.024 1.00 14.72 A C ANISOU 1607 CG ASN A 199 1970 1354 2266 176 341 -289 A C ATOM 1608 ND2 ASN A 199 65.550 -28.134 30.858 1.00 15.48 A N ANISOU 1608 ND2 ASN A 199 2117 1455 2309 -4 511 40 A N ATOM 1609 OD1 ASN A 199 65.262 -27.217 32.918 1.00 15.75 A O ANISOU 1609 OD1 ASN A 199 2123 1369 2491 -60 277 -378 A O ATOM 1610 N ALA A 200 62.162 -30.576 34.309 1.00 13.28 A N ANISOU 1610 N ALA A 200 1681 1405 1958 199 186 -308 A N ATOM 1611 CA ALA A 200 60.844 -31.001 34.708 1.00 13.12 A C ANISOU 1611 CA ALA A 200 1742 1203 2037 222 201 -191 A C ATOM 1612 C ALA A 200 60.075 -29.831 35.305 1.00 12.39 A C ANISOU 1612 C ALA A 200 1598 1348 1760 199 106 -292 A C ATOM 1613 O ALA A 200 60.682 -28.969 35.927 1.00 13.49 A O ANISOU 1613 O ALA A 200 1626 1419 2078 21 177 -353 A O ATOM 1614 CB ALA A 200 60.912 -32.133 35.711 1.00 13.94 A C ANISOU 1614 CB ALA A 200 1960 1052 2283 116 277 -156 A C ATOM 1615 N ILE A 201 58.754 -29.867 35.109 1.00 11.83 A N ANISOU 1615 N ILE A 201 1642 955 1896 162 222 -114 A N ATOM 1616 CA ILE A 201 57.812 -28.956 35.777 1.00 13.14 A C ANISOU 1616 CA ILE A 201 1596 1453 1943 138 271 -349 A C ATOM 1617 C ILE A 201 56.811 -29.823 36.523 1.00 12.52 A C ANISOU 1617 C ILE A 201 1665 1399 1692 -24 97 -389 A C ATOM 1618 O ILE A 201 56.312 -30.836 35.972 1.00 13.52 A O ANISOU 1618 O ILE A 201 1910 1029 2195 -6 257 -418 A O ATOM 1619 CB ILE A 201 57.155 -27.974 34.798 1.00 14.80 A C ANISOU 1619 CB ILE A 201 1806 1687 2127 53 267 -167 A C ATOM 1620 CG1 ILE A 201 56.163 -27.078 35.526 1.00 14.10 A C ANISOU 1620 CG1 ILE A 201 1843 1355 2155 124 65 -79 A C ATOM 1621 CG2 ILE A 201 56.485 -28.668 33.641 1.00 13.79 A C ANISOU 1621 CG2 ILE A 201 1582 1161 2494 356 85 -274 A C ATOM 1622 CD1 ILE A 201 55.819 -25.806 34.777 1.00 14.83 A C ANISOU 1622 CD1 ILE A 201 2012 1140 2481 81 88 -85 A C ATOM 1623 N GLY A 202 56.550 -29.460 37.776 1.00 12.13 A N ANISOU 1623 N GLY A 202 1841 1098 1669 -63 182 -187 A N ATOM 1624 CA GLY A 202 55.500 -30.077 38.570 1.00 12.18 A C ANISOU 1624 CA GLY A 202 1621 1168 1837 213 363 -276 A C ATOM 1625 C GLY A 202 54.583 -28.997 39.129 1.00 11.79 A C ANISOU 1625 C GLY A 202 1567 833 2077 29 227 -431 A C ATOM 1626 O GLY A 202 55.058 -27.934 39.571 1.00 13.98 A O ANISOU 1626 O GLY A 202 1751 1024 2535 -142 322 -640 A O ATOM 1627 N VAL A 203 53.276 -29.228 39.114 1.00 11.15 A N ANISOU 1627 N VAL A 203 1603 967 1665 83 98 -133 A N ATOM 1628 CA VAL A 203 52.329 -28.245 39.633 1.00 10.78 A C ANISOU 1628 CA VAL A 203 1539 879 1676 43 9 -239 A C ATOM 1629 C VAL A 203 51.329 -28.982 40.527 1.00 10.33 A C ANISOU 1629 C VAL A 203 1673 682 1567 74 29 -97 A C ATOM 1630 O VAL A 203 50.768 -30.036 40.116 1.00 12.01 A O ANISOU 1630 O VAL A 203 2172 635 1755 -1 107 -262 A O ATOM 1631 CB VAL A 203 51.558 -27.511 38.517 1.00 10.48 A C ANISOU 1631 CB VAL A 203 1805 808 1368 -60 3 -309 A C ATOM 1632 CG1 VAL A 203 50.716 -26.387 39.133 1.00 11.51 A C ANISOU 1632 CG1 VAL A 203 2036 760 1576 168 -50 -175 A C ATOM 1633 CG2 VAL A 203 52.501 -26.938 37.462 1.00 12.20 A C ANISOU 1633 CG2 VAL A 203 1843 1114 1678 159 323 -174 A C ATOM 1634 N THR A 204 51.099 -28.482 41.726 1.00 11.25 A N ANISOU 1634 N THR A 204 1716 862 1694 33 39 -127 A N ATOM 1635 CA THR A 204 50.053 -28.981 42.572 1.00 10.62 A C ANISOU 1635 CA THR A 204 1609 811 1614 259 105 -120 A C ATOM 1636 C THR A 204 48.852 -28.066 42.472 1.00 10.44 A C ANISOU 1636 C THR A 204 1566 624 1774 140 48 47 A C ATOM 1637 O THR A 204 49.025 -26.826 42.565 1.00 10.98 A O ANISOU 1637 O THR A 204 1864 622 1684 -30 112 13 A O ATOM 1638 CB THR A 204 50.474 -29.103 44.034 1.00 12.23 A C ANISOU 1638 CB THR A 204 1880 1138 1629 361 51 -96 A C ATOM 1639 CG2 THR A 204 49.370 -29.721 44.871 1.00 12.99 A C ANISOU 1639 CG2 THR A 204 2023 1290 1621 253 -9 1 A C ATOM 1640 OG1 THR A 204 51.659 -29.896 44.141 1.00 13.71 A O ANISOU 1640 OG1 THR A 204 1937 1278 1993 402 255 65 A O ATOM 1641 N VAL A 205 47.662 -28.616 42.263 1.00 10.59 A N ANISOU 1641 N VAL A 205 1516 857 1651 103 214 5 A N ATOM 1642 CA VAL A 205 46.420 -27.888 42.164 1.00 10.18 A C ANISOU 1642 CA VAL A 205 1591 584 1690 108 166 -59 A C ATOM 1643 C VAL A 205 45.493 -28.291 43.292 1.00 10.03 A C ANISOU 1643 C VAL A 205 1531 741 1537 162 65 -36 A C ATOM 1644 O VAL A 205 45.256 -29.463 43.482 1.00 11.80 A O ANISOU 1644 O VAL A 205 1891 847 1742 -102 175 195 A O ATOM 1645 CB VAL A 205 45.726 -28.044 40.808 1.00 10.91 A C ANISOU 1645 CB VAL A 205 1513 792 1838 8 49 37 A C ATOM 1646 CG1 VAL A 205 44.369 -27.334 40.747 1.00 10.47 A C ANISOU 1646 CG1 VAL A 205 1635 757 1584 85 23 -20 A C ATOM 1647 CG2 VAL A 205 46.633 -27.560 39.690 1.00 11.22 A C ANISOU 1647 CG2 VAL A 205 1633 824 1805 60 142 18 A C ATOM 1648 N GLY A 206 44.963 -27.309 44.007 1.00 10.58 A N ANISOU 1648 N GLY A 206 1489 766 1762 168 87 -119 A N ATOM 1649 CA GLY A 206 43.946 -27.439 45.039 1.00 10.44 A C ANISOU 1649 CA GLY A 206 1481 924 1558 -6 -75 44 A C ATOM 1650 C GLY A 206 42.642 -26.765 44.663 1.00 9.91 A C ANISOU 1650 C GLY A 206 1439 891 1436 -28 22 14 A C ATOM 1651 O GLY A 206 42.591 -26.065 43.651 1.00 10.46 A O ANISOU 1651 O GLY A 206 1615 945 1412 29 98 81 A O ATOM 1652 N GLU A 207 41.577 -27.002 45.458 1.00 10.02 A N ANISOU 1652 N GLU A 207 1663 654 1489 23 83 111 A N ATOM 1653 CA GLU A 207 40.229 -26.609 45.010 1.00 10.71 A C ANISOU 1653 CA GLU A 207 1474 954 1640 -115 138 -56 A C ATOM 1654 C GLU A 207 40.011 -25.084 45.115 1.00 10.42 A C ANISOU 1654 C GLU A 207 1533 981 1445 -84 114 37 A C ATOM 1655 O GLU A 207 39.244 -24.543 44.333 1.00 11.28 A O ANISOU 1655 O GLU A 207 1789 887 1608 -137 -23 64 A O ATOM 1656 CB GLU A 207 39.177 -27.397 45.791 1.00 10.84 A C ANISOU 1656 CB GLU A 207 1668 814 1635 7 214 20 A C ATOM 1657 CG GLU A 207 39.127 -27.087 47.260 1.00 10.77 A C ANISOU 1657 CG GLU A 207 1662 832 1595 85 70 -64 A C ATOM 1658 CD GLU A 207 38.142 -27.877 48.076 1.00 13.67 A C ANISOU 1658 CD GLU A 207 1517 1622 2055 46 256 -82 A C ATOM 1659 OE1 GLU A 207 37.708 -28.960 47.597 1.00 14.43 A O ANISOU 1659 OE1 GLU A 207 1867 1089 2524 -137 428 252 A O ATOM 1660 OE2 GLU A 207 37.851 -27.436 49.240 1.00 15.65 A O ANISOU 1660 OE2 GLU A 207 2269 1832 1846 205 428 350 A O ATOM 1661 N GLY A 208 40.565 -24.446 46.141 1.00 9.59 A N ANISOU 1661 N GLY A 208 1441 664 1536 172 -130 205 A N ATOM 1662 CA GLY A 208 40.316 -23.031 46.353 1.00 9.41 A C ANISOU 1662 CA GLY A 208 1506 566 1503 44 67 251 A C ATOM 1663 C GLY A 208 38.838 -22.694 46.368 1.00 10.54 A C ANISOU 1663 C GLY A 208 1527 724 1750 33 88 110 A C ATOM 1664 O GLY A 208 37.998 -23.358 46.983 1.00 11.74 A O ANISOU 1664 O GLY A 208 1538 1037 1886 -2 225 -10 A O ATOM 1665 N TRP A 209 38.560 -21.509 45.824 1.00 10.13 A N ANISOU 1665 N TRP A 209 1481 600 1766 -95 -50 0 A N ATOM 1666 CA TRP A 209 37.226 -20.994 45.636 1.00 10.30 A C ANISOU 1666 CA TRP A 209 1602 893 1417 96 -119 50 A C ATOM 1667 C TRP A 209 36.517 -21.614 44.431 1.00 10.01 A C ANISOU 1667 C TRP A 209 1491 864 1445 -1 20 32 A C ATOM 1668 O TRP A 209 35.286 -21.601 44.354 1.00 11.09 A O ANISOU 1668 O TRP A 209 1560 765 1886 -104 5 -122 A O ATOM 1669 CB TRP A 209 37.300 -19.459 45.459 1.00 9.99 A C ANISOU 1669 CB TRP A 209 1439 813 1542 159 224 -136 A C ATOM 1670 CG TRP A 209 37.866 -18.702 46.621 1.00 11.02 A C ANISOU 1670 CG TRP A 209 1509 924 1753 -4 59 27 A C ATOM 1671 CD1 TRP A 209 37.185 -18.264 47.720 1.00 11.83 A C ANISOU 1671 CD1 TRP A 209 1709 1008 1775 -9 51 -185 A C ATOM 1672 CD2 TRP A 209 39.231 -18.282 46.808 1.00 10.01 A C ANISOU 1672 CD2 TRP A 209 1497 668 1636 40 -19 -234 A C ATOM 1673 CE2 TRP A 209 39.272 -17.536 48.006 1.00 10.05 A C ANISOU 1673 CE2 TRP A 209 1372 807 1640 110 -44 -277 A C ATOM 1674 CE3 TRP A 209 40.396 -18.377 46.038 1.00 11.34 A C ANISOU 1674 CE3 TRP A 209 1640 575 2091 94 184 -217 A C ATOM 1675 NE1 TRP A 209 38.021 -17.569 48.558 1.00 12.06 A N ANISOU 1675 NE1 TRP A 209 1541 1140 1899 44 125 -324 A N ATOM 1676 CZ2 TRP A 209 40.441 -16.954 48.475 1.00 10.92 A C ANISOU 1676 CZ2 TRP A 209 1457 947 1744 75 -175 -271 A C ATOM 1677 CZ3 TRP A 209 41.550 -17.767 46.490 1.00 12.39 A C ANISOU 1677 CZ3 TRP A 209 1476 1449 1781 138 158 -177 A C ATOM 1678 CH2 TRP A 209 41.564 -17.047 47.688 1.00 11.95 A C ANISOU 1678 CH2 TRP A 209 1564 1108 1868 -36 -26 -160 A C ATOM 1679 N TYR A 210 37.307 -22.058 43.427 1.00 10.02 A N ANISOU 1679 N TYR A 210 1327 1066 1413 -22 88 110 A N ATOM 1680 CA TYR A 210 36.733 -22.541 42.154 1.00 10.29 A C ANISOU 1680 CA TYR A 210 1415 909 1583 -31 -2 101 A C ATOM 1681 C TYR A 210 35.768 -23.725 42.391 1.00 10.14 A C ANISOU 1681 C TYR A 210 1320 929 1602 54 93 163 A C ATOM 1682 O TYR A 210 34.667 -23.783 41.838 1.00 11.15 A O ANISOU 1682 O TYR A 210 1665 802 1767 129 -125 -48 A O ATOM 1683 CB TYR A 210 37.872 -22.910 41.182 1.00 10.07 A C ANISOU 1683 CB TYR A 210 1580 747 1495 -43 129 219 A C ATOM 1684 CG TYR A 210 37.436 -22.987 39.739 1.00 10.83 A C ANISOU 1684 CG TYR A 210 1680 964 1470 253 86 41 A C ATOM 1685 CD1 TYR A 210 36.902 -24.158 39.206 1.00 12.89 A C ANISOU 1685 CD1 TYR A 210 1666 1443 1789 174 -82 -164 A C ATOM 1686 CD2 TYR A 210 37.508 -21.872 38.930 1.00 13.00 A C ANISOU 1686 CD2 TYR A 210 1848 1357 1733 375 88 338 A C ATOM 1687 CE1 TYR A 210 36.452 -24.203 37.896 1.00 14.15 A C ANISOU 1687 CE1 TYR A 210 1721 1765 1889 72 -103 -194 A C ATOM 1688 CE2 TYR A 210 37.097 -21.921 37.619 1.00 13.62 A C ANISOU 1688 CE2 TYR A 210 1836 1724 1613 264 239 158 A C ATOM 1689 CZ TYR A 210 36.573 -23.078 37.099 1.00 14.59 A C ANISOU 1689 CZ TYR A 210 1732 2017 1793 322 60 -41 A C ATOM 1690 OH TYR A 210 36.115 -23.100 35.813 1.00 20.24 A O ANISOU 1690 OH TYR A 210 2068 3856 1763 275 47 -307 A O ATOM 1691 N SER A 211 36.204 -24.667 43.220 1.00 10.02 A N ANISOU 1691 N SER A 211 1399 901 1505 -8 -49 121 A N ATOM 1692 CA SER A 211 35.405 -25.860 43.532 1.00 9.63 A C ANISOU 1692 CA SER A 211 1487 768 1402 -77 -78 -75 A C ATOM 1693 C SER A 211 35.241 -26.135 45.032 1.00 10.77 A C ANISOU 1693 C SER A 211 1651 944 1495 -133 46 30 A C ATOM 1694 O SER A 211 34.544 -27.103 45.355 1.00 11.26 A O ANISOU 1694 O SER A 211 1847 790 1639 -208 212 -102 A O ATOM 1695 CB SER A 211 35.870 -27.091 42.795 1.00 11.64 A C ANISOU 1695 CB SER A 211 1806 1013 1601 110 85 -163 A C ATOM 1696 OG SER A 211 37.201 -27.408 43.142 1.00 11.93 A O ANISOU 1696 OG SER A 211 1780 904 1846 16 0 -108 A O ATOM 1697 N GLY A 212 35.890 -25.398 45.935 1.00 10.54 A N ANISOU 1697 N GLY A 212 1300 1112 1591 -126 220 -43 A N ATOM 1698 CA GLY A 212 35.742 -25.630 47.331 1.00 11.59 A C ANISOU 1698 CA GLY A 212 1724 913 1764 -64 190 90 A C ATOM 1699 C GLY A 212 34.388 -25.244 47.899 1.00 10.43 A C ANISOU 1699 C GLY A 212 1542 933 1486 -211 112 128 A C ATOM 1700 O GLY A 212 33.563 -24.604 47.259 1.00 11.19 A O ANISOU 1700 O GLY A 212 1663 1075 1510 -46 145 29 A O ATOM 1701 N ARG A 213 34.182 -25.604 49.163 1.00 10.84 A N ANISOU 1701 N ARG A 213 1692 1054 1372 -98 84 -9 A N ATOM 1702 CA ARG A 213 32.960 -25.259 49.898 1.00 11.43 A C ANISOU 1702 CA ARG A 213 1541 1162 1637 -296 210 81 A C ATOM 1703 C ARG A 213 33.036 -23.786 50.357 1.00 11.91 A C ANISOU 1703 C ARG A 213 1624 1192 1706 97 87 50 A C ATOM 1704 O ARG A 213 33.838 -23.464 51.199 1.00 12.86 A O ANISOU 1704 O ARG A 213 1824 1205 1855 112 111 -156 A O ATOM 1705 CB ARG A 213 32.725 -26.200 51.079 1.00 12.32 A C ANISOU 1705 CB ARG A 213 1904 1004 1772 -224 214 75 A C ATOM 1706 CG ARG A 213 31.368 -26.029 51.745 1.00 12.97 A C ANISOU 1706 CG ARG A 213 1823 1309 1797 9 95 154 A C ATOM 1707 CD ARG A 213 31.179 -27.022 52.898 1.00 14.27 A C ANISOU 1707 CD ARG A 213 2336 1377 1709 -45 209 82 A C ATOM 1708 NE ARG A 213 32.174 -26.873 53.950 1.00 14.00 A N ANISOU 1708 NE ARG A 213 1878 1455 1986 -181 343 106 A N ATOM 1709 CZ ARG A 213 32.149 -25.961 54.929 1.00 13.06 A C ANISOU 1709 CZ ARG A 213 1810 1333 1818 -141 241 250 A C ATOM 1710 NH1 ARG A 213 31.065 -25.214 55.104 1.00 14.19 A N ANISOU 1710 NH1 ARG A 213 2097 1492 1801 217 388 242 A N ATOM 1711 NH2 ARG A 213 33.200 -25.884 55.752 1.00 14.12 A N ANISOU 1711 NH2 ARG A 213 2214 1417 1733 -141 2 51 A N ATOM 1712 N ILE A 214 32.171 -22.951 49.772 1.00 10.28 A N ANISOU 1712 N ILE A 214 1523 847 1533 33 26 -103 A N ATOM 1713 CA ILE A 214 32.197 -21.518 50.033 1.00 10.55 A C ANISOU 1713 CA ILE A 214 1587 876 1545 -141 234 -103 A C ATOM 1714 C ILE A 214 30.770 -21.100 50.399 1.00 10.48 A C ANISOU 1714 C ILE A 214 1525 958 1498 -109 191 -95 A C ATOM 1715 O ILE A 214 29.792 -21.551 49.811 1.00 12.10 A O ANISOU 1715 O ILE A 214 1699 1083 1813 -48 114 -213 A O ATOM 1716 CB ILE A 214 32.783 -20.724 48.839 1.00 11.53 A C ANISOU 1716 CB ILE A 214 1727 832 1819 -132 241 153 A C ATOM 1717 CG1 ILE A 214 34.187 -21.178 48.431 1.00 14.13 A C ANISOU 1717 CG1 ILE A 214 1955 1328 2084 -180 578 -27 A C ATOM 1718 CG2 ILE A 214 32.768 -19.218 49.055 1.00 12.58 A C ANISOU 1718 CG2 ILE A 214 1936 817 2025 52 234 177 A C ATOM 1719 CD1 ILE A 214 35.231 -20.955 49.503 1.00 17.61 A C ANISOU 1719 CD1 ILE A 214 1941 1996 2752 -67 307 446 A C ATOM 1720 N GLY A 215 30.685 -20.125 51.310 1.00 10.92 A N ANISOU 1720 N GLY A 215 1503 796 1849 -368 268 -150 A N ATOM 1721 CA GLY A 215 29.397 -19.643 51.813 1.00 12.12 A C ANISOU 1721 CA GLY A 215 1698 1125 1780 6 331 104 A C ATOM 1722 C GLY A 215 29.070 -20.115 53.214 1.00 12.68 A C ANISOU 1722 C GLY A 215 1698 1427 1691 -48 219 40 A C ATOM 1723 O GLY A 215 29.572 -21.147 53.655 1.00 13.07 A O ANISOU 1723 O GLY A 215 1884 1283 1797 -126 281 21 A O ATOM 1724 N TYR A 216 28.130 -19.418 53.861 1.00 13.97 A N ANISOU 1724 N TYR A 216 1837 1471 1997 -16 212 -143 A N ATOM 1725 CA TYR A 216 27.697 -19.719 55.194 1.00 15.45 A C ANISOU 1725 CA TYR A 216 1908 2004 1959 -125 154 -246 A C ATOM 1726 C TYR A 216 26.484 -20.658 55.134 1.00 16.34 A C ANISOU 1726 C TYR A 216 1862 2278 2067 -102 -16 37 A C ATOM 1727 O TYR A 216 25.991 -21.010 54.057 1.00 15.51 A O ANISOU 1727 O TYR A 216 1663 2297 1934 -246 450 -212 A O ATOM 1728 CB TYR A 216 27.414 -18.421 55.966 1.00 16.61 A C ANISOU 1728 CB TYR A 216 1558 2144 2607 -104 399 -362 A C ATOM 1729 CG TYR A 216 26.648 -17.364 55.226 1.00 16.68 A C ANISOU 1729 CG TYR A 216 1887 1778 2671 -347 484 -245 A C ATOM 1730 CD1 TYR A 216 25.273 -17.391 55.123 1.00 20.21 A C ANISOU 1730 CD1 TYR A 216 1826 2322 3528 101 391 -32 A C ATOM 1731 CD2 TYR A 216 27.299 -16.279 54.687 1.00 18.36 A C ANISOU 1731 CD2 TYR A 216 2068 1504 3402 -340 862 -468 A C ATOM 1732 CE1 TYR A 216 24.565 -16.407 54.445 1.00 23.69 A C ANISOU 1732 CE1 TYR A 216 1862 2708 4431 -39 635 796 A C ATOM 1733 CE2 TYR A 216 26.616 -15.310 53.979 1.00 22.94 A C ANISOU 1733 CE2 TYR A 216 2435 1942 4337 -75 612 12 A C ATOM 1734 CZ TYR A 216 25.240 -15.339 53.902 1.00 23.17 A C ANISOU 1734 CZ TYR A 216 2414 2111 4277 307 892 526 A C ATOM 1735 OH TYR A 216 24.571 -14.348 53.232 1.00 31.12 A O ANISOU 1735 OH TYR A 216 3441 2647 5736 601 719 1112 A O ATOM 1736 N ASP A 217 26.001 -21.053 56.304 1.00 16.48 A N ANISOU 1736 N ASP A 217 2015 2166 2078 -329 369 -386 A N ATOM 1737 CA ASP A 217 24.835 -21.966 56.420 1.00 19.11 A C ANISOU 1737 CA ASP A 217 2353 2338 2570 -545 466 -85 A C ATOM 1738 C ASP A 217 25.127 -23.281 55.690 1.00 18.00 A C ANISOU 1738 C ASP A 217 2111 2566 2160 -452 185 -124 A C ATOM 1739 O ASP A 217 24.210 -23.951 55.178 1.00 21.65 A O ANISOU 1739 O ASP A 217 2331 2569 3323 -510 149 -645 A O ATOM 1740 CB ASP A 217 23.568 -21.271 55.928 1.00 20.40 A C ANISOU 1740 CB ASP A 217 2116 2447 3189 -650 546 -215 A C ATOM 1741 CG ASP A 217 23.149 -20.103 56.813 1.00 20.87 A C ANISOU 1741 CG ASP A 217 2451 2419 3059 -269 399 -129 A C ATOM 1742 OD1 ASP A 217 23.445 -20.142 58.017 1.00 23.36 A O ANISOU 1742 OD1 ASP A 217 2230 3484 3162 -119 201 -614 A O ATOM 1743 OD2 ASP A 217 22.518 -19.172 56.273 1.00 20.56 A O ANISOU 1743 OD2 ASP A 217 2010 2643 3157 -528 829 326 A O ATOM 1744 N GLY A 218 26.398 -23.691 55.772 1.00 17.10 A N ANISOU 1744 N GLY A 218 2174 2119 2202 -271 511 -192 A N ATOM 1745 CA GLY A 218 26.895 -24.939 55.194 1.00 17.84 A C ANISOU 1745 CA GLY A 218 2649 1961 2167 -366 191 -319 A C ATOM 1746 C GLY A 218 27.638 -24.715 53.893 1.00 16.64 A C ANISOU 1746 C GLY A 218 2249 1892 2182 -72 220 -96 A C ATOM 1747 O GLY A 218 28.485 -25.519 53.495 1.00 18.33 A O ANISOU 1747 O GLY A 218 2339 1662 2962 -9 114 -88 A O ATOM 1748 N GLY A 219 27.297 -23.634 53.192 1.00 14.87 A N ANISOU 1748 N GLY A 219 1957 1806 1884 -164 427 -106 A N ATOM 1749 CA GLY A 219 27.917 -23.327 51.907 1.00 14.24 A C ANISOU 1749 CA GLY A 219 2116 1663 1631 -127 306 -370 A C ATOM 1750 C GLY A 219 27.560 -24.303 50.806 1.00 14.26 A C ANISOU 1750 C GLY A 219 2317 1358 1742 -330 597 -377 A C ATOM 1751 O GLY A 219 26.708 -25.183 50.970 1.00 17.84 A O ANISOU 1751 O GLY A 219 2696 1684 2398 -740 621 -375 A O ATOM 1752 N LYS A 220 28.229 -24.121 49.674 1.00 12.89 A N ANISOU 1752 N LYS A 220 1957 1016 1921 -184 625 -323 A N ATOM 1753 CA LYS A 220 28.057 -24.935 48.486 1.00 13.42 A C ANISOU 1753 CA LYS A 220 1965 1297 1836 -240 300 -280 A C ATOM 1754 C LYS A 220 29.442 -25.171 47.904 1.00 12.63 A C ANISOU 1754 C LYS A 220 1715 1131 1951 -200 74 -19 A C ATOM 1755 O LYS A 220 30.301 -24.307 47.956 1.00 12.42 A O ANISOU 1755 O LYS A 220 1767 1070 1879 -195 280 -44 A O ATOM 1756 CB LYS A 220 27.196 -24.235 47.427 1.00 19.05 A C ANISOU 1756 CB LYS A 220 2102 2345 2788 37 -26 121 A C ATOM 1757 CG LYS A 220 25.772 -23.926 47.868 1.00 23.85 A C ANISOU 1757 CG LYS A 220 2286 3328 3448 141 -10 -117 A C ATOM 1758 CD LYS A 220 24.913 -23.229 46.810 1.00 30.05 A C ANISOU 1758 CD LYS A 220 3010 3842 4562 756 -214 511 A C ATOM 1759 CE LYS A 220 23.498 -22.980 47.296 1.00 41.33 A C ANISOU 1759 CE LYS A 220 2876 5901 6924 388 -98 568 A C ATOM 1760 NZ LYS A 220 22.874 -21.841 46.581 1.00 52.48 A N ANISOU 1760 NZ LYS A 220 4823 6938 8178 1236 278 1576 A N ATOM 1761 N ARG A 221 29.664 -26.382 47.377 1.00 12.97 A N ANISOU 1761 N ARG A 221 1841 1191 1894 -171 249 -49 A N ATOM 1762 CA ARG A 221 30.906 -26.667 46.713 1.00 12.64 A C ANISOU 1762 CA ARG A 221 1926 1166 1710 -114 255 -19 A C ATOM 1763 C ARG A 221 30.681 -26.775 45.203 1.00 10.71 A C ANISOU 1763 C ARG A 221 1628 720 1720 -7 105 47 A C ATOM 1764 O ARG A 221 29.537 -26.735 44.707 1.00 12.17 A O ANISOU 1764 O ARG A 221 1592 1004 2026 -126 -9 -93 A O ATOM 1765 CB ARG A 221 31.629 -27.876 47.289 1.00 14.55 A C ANISOU 1765 CB ARG A 221 2200 1412 1915 -4 403 63 A C ATOM 1766 CG ARG A 221 30.897 -29.181 47.089 1.00 15.90 A C ANISOU 1766 CG ARG A 221 2312 1302 2424 -9 379 55 A C ATOM 1767 CD ARG A 221 31.712 -30.423 47.514 1.00 18.05 A C ANISOU 1767 CD ARG A 221 2611 1071 3174 103 453 -83 A C ATOM 1768 NE ARG A 221 31.734 -30.587 48.969 1.00 21.71 A N ANISOU 1768 NE ARG A 221 3599 1166 3483 178 -46 -203 A N ATOM 1769 CZ ARG A 221 32.659 -30.116 49.791 1.00 19.52 A C ANISOU 1769 CZ ARG A 221 2769 1232 3415 312 170 327 A C ATOM 1770 NH1 ARG A 221 33.760 -29.537 49.325 1.00 23.66 A N ANISOU 1770 NH1 ARG A 221 3184 1461 4345 609 1404 515 A N ATOM 1771 NH2 ARG A 221 32.465 -30.174 51.089 1.00 24.42 A N ANISOU 1771 NH2 ARG A 221 4443 1784 3051 385 221 485 A N ATOM 1772 N ASN A 222 31.796 -26.911 44.466 1.00 11.40 A N ANISOU 1772 N ASN A 222 1621 946 1764 -224 94 -111 A N ATOM 1773 CA ASN A 222 31.747 -27.087 43.004 1.00 11.95 A C ANISOU 1773 CA ASN A 222 1412 1523 1603 -344 292 58 A C ATOM 1774 C ASN A 222 30.992 -25.944 42.329 1.00 11.61 A C ANISOU 1774 C ASN A 222 1705 1188 1517 -435 67 -124 A C ATOM 1775 O ASN A 222 30.231 -26.159 41.370 1.00 11.88 A O ANISOU 1775 O ASN A 222 1696 844 1971 -222 -140 -111 A O ATOM 1776 CB ASN A 222 31.159 -28.456 42.631 1.00 13.31 A C ANISOU 1776 CB ASN A 222 1784 1346 1925 -121 200 -66 A C ATOM 1777 CG ASN A 222 31.978 -29.582 43.201 1.00 13.34 A C ANISOU 1777 CG ASN A 222 2017 1216 1834 -275 185 60 A C ATOM 1778 ND2 ASN A 222 31.306 -30.625 43.701 1.00 12.86 A N ANISOU 1778 ND2 ASN A 222 1709 1143 2034 -321 198 -27 A N ATOM 1779 OD1 ASN A 222 33.204 -29.519 43.143 1.00 13.76 A O ANISOU 1779 OD1 ASN A 222 2135 776 2317 -152 80 -26 A O ATOM 1780 N ILE A 223 31.249 -24.705 42.797 1.00 10.92 A N ANISOU 1780 N ILE A 223 1469 1100 1580 -257 -6 -119 A N ATOM 1781 CA ILE A 223 30.439 -23.581 42.338 1.00 11.97 A C ANISOU 1781 CA ILE A 223 1584 1457 1507 38 120 -69 A C ATOM 1782 C ILE A 223 30.740 -23.269 40.854 1.00 9.55 A C ANISOU 1782 C ILE A 223 1563 559 1505 -22 29 -77 A C ATOM 1783 O ILE A 223 29.817 -23.002 40.045 1.00 12.29 A O ANISOU 1783 O ILE A 223 1500 1290 1878 63 -82 151 A O ATOM 1784 CB ILE A 223 30.655 -22.342 43.234 1.00 12.07 A C ANISOU 1784 CB ILE A 223 1629 1177 1778 76 25 -70 A C ATOM 1785 CG1 ILE A 223 30.085 -22.620 44.634 1.00 12.47 A C ANISOU 1785 CG1 ILE A 223 1789 1215 1735 246 101 -318 A C ATOM 1786 CG2 ILE A 223 30.008 -21.106 42.637 1.00 12.08 A C ANISOU 1786 CG2 ILE A 223 1832 1071 1684 5 110 -109 A C ATOM 1787 CD1 ILE A 223 30.439 -21.582 45.684 1.00 13.99 A C ANISOU 1787 CD1 ILE A 223 2278 1322 1714 -104 218 -308 A C ATOM 1788 N TYR A 224 32.029 -23.257 40.510 1.00 11.24 A N ANISOU 1788 N TYR A 224 1405 963 1902 -58 -100 -81 A N ATOM 1789 CA TYR A 224 32.474 -22.868 39.171 1.00 10.83 A C ANISOU 1789 CA TYR A 224 1549 853 1710 -56 -172 -202 A C ATOM 1790 C TYR A 224 32.764 -24.073 38.272 1.00 11.02 A C ANISOU 1790 C TYR A 224 1568 945 1671 -22 -65 -178 A C ATOM 1791 O TYR A 224 32.752 -23.978 37.040 1.00 13.64 A O ANISOU 1791 O TYR A 224 2261 1270 1649 -19 -4 -170 A O ATOM 1792 CB TYR A 224 33.702 -21.963 39.244 1.00 10.77 A C ANISOU 1792 CB TYR A 224 1509 1000 1583 -66 7 -107 A C ATOM 1793 CG TYR A 224 33.409 -20.678 39.963 1.00 10.78 A C ANISOU 1793 CG TYR A 224 1533 941 1619 85 40 -37 A C ATOM 1794 CD1 TYR A 224 32.888 -19.588 39.276 1.00 10.47 A C ANISOU 1794 CD1 TYR A 224 1728 771 1479 -108 -114 -146 A C ATOM 1795 CD2 TYR A 224 33.611 -20.544 41.328 1.00 10.72 A C ANISOU 1795 CD2 TYR A 224 1582 904 1584 -120 20 29 A C ATOM 1796 CE1 TYR A 224 32.618 -18.393 39.922 1.00 11.10 A C ANISOU 1796 CE1 TYR A 224 1720 700 1798 -40 -92 -152 A C ATOM 1797 CE2 TYR A 224 33.322 -19.349 41.981 1.00 10.87 A C ANISOU 1797 CE2 TYR A 224 1526 990 1612 -85 -207 -38 A C ATOM 1798 CZ TYR A 224 32.824 -18.272 41.277 1.00 10.66 A C ANISOU 1798 CZ TYR A 224 1537 758 1754 124 -105 -274 A C ATOM 1799 OH TYR A 224 32.610 -17.073 41.931 1.00 11.88 A O ANISOU 1799 OH TYR A 224 1805 712 1996 22 -34 -332 A O ATOM 1800 N GLY A 225 32.985 -25.235 38.892 1.00 11.64 A N ANISOU 1800 N GLY A 225 1979 848 1595 -95 54 -127 A N ATOM 1801 CA GLY A 225 33.324 -26.508 38.246 1.00 12.48 A C ANISOU 1801 CA GLY A 225 1892 1247 1603 -208 107 -487 A C ATOM 1802 C GLY A 225 33.503 -27.515 39.345 1.00 11.73 A C ANISOU 1802 C GLY A 225 1573 1090 1793 -113 55 -404 A C ATOM 1803 O GLY A 225 33.527 -27.188 40.505 1.00 12.37 A O ANISOU 1803 O GLY A 225 2181 691 1825 -127 179 -53 A O ATOM 1804 N ASP A 226 33.631 -28.790 38.949 1.00 12.20 A N ANISOU 1804 N ASP A 226 1771 967 1895 -61 -17 -214 A N ATOM 1805 CA ASP A 226 33.721 -29.864 39.940 1.00 13.36 A C ANISOU 1805 CA ASP A 226 1646 1311 2118 -38 178 27 A C ATOM 1806 C ASP A 226 35.024 -30.628 39.819 1.00 10.97 A C ANISOU 1806 C ASP A 226 1516 700 1949 -220 203 95 A C ATOM 1807 O ASP A 226 35.147 -31.684 40.481 1.00 13.09 A O ANISOU 1807 O ASP A 226 2063 665 2245 -107 410 203 A O ATOM 1808 CB ASP A 226 32.543 -30.830 39.834 1.00 14.65 A C ANISOU 1808 CB ASP A 226 1971 1298 2296 -165 411 -176 A C ATOM 1809 CG ASP A 226 32.463 -31.651 38.570 1.00 18.65 A C ANISOU 1809 CG ASP A 226 2880 1091 3114 -935 582 -535 A C ATOM 1810 OD1 ASP A 226 33.311 -31.498 37.682 1.00 15.60 A O ANISOU 1810 OD1 ASP A 226 1927 1418 2580 -120 -68 -402 A O ATOM 1811 OD2 ASP A 226 31.575 -32.520 38.549 1.00 27.47 A O ANISOU 1811 OD2 ASP A 226 3080 2425 4932 -1694 1091 -1542 A O ATOM 1812 N THR A 227 35.964 -30.174 38.991 1.00 11.34 A N ANISOU 1812 N THR A 227 1671 768 1867 -62 288 102 A N ATOM 1813 CA THR A 227 37.179 -30.932 38.651 1.00 11.57 A C ANISOU 1813 CA THR A 227 1530 1025 1838 -55 -13 42 A C ATOM 1814 C THR A 227 38.414 -30.010 38.718 1.00 11.84 A C ANISOU 1814 C THR A 227 1825 1002 1671 -246 49 -27 A C ATOM 1815 O THR A 227 38.410 -28.912 38.153 1.00 13.54 A O ANISOU 1815 O THR A 227 1982 1045 2117 -112 148 221 A O ATOM 1816 CB THR A 227 37.043 -31.601 37.280 1.00 13.78 A C ANISOU 1816 CB THR A 227 1707 1607 1919 -216 165 -258 A C ATOM 1817 CG2 THR A 227 38.271 -32.434 36.946 1.00 14.68 A C ANISOU 1817 CG2 THR A 227 2127 1259 2190 3 193 -192 A C ATOM 1818 OG1 THR A 227 35.899 -32.456 37.299 1.00 13.66 A O ANISOU 1818 OG1 THR A 227 1854 1213 2122 -280 294 -221 A O ATOM 1819 N LEU A 228 39.465 -30.401 39.465 1.00 10.99 A N ANISOU 1819 N LEU A 228 1841 684 1649 -222 160 1 A N ATOM 1820 CA LEU A 228 40.687 -29.612 39.503 1.00 10.99 A C ANISOU 1820 CA LEU A 228 1839 783 1550 -242 164 -156 A C ATOM 1821 C LEU A 228 41.346 -29.596 38.120 1.00 11.56 A C ANISOU 1821 C LEU A 228 2042 849 1500 -126 207 -175 A C ATOM 1822 O LEU A 228 41.442 -30.610 37.461 1.00 12.29 A O ANISOU 1822 O LEU A 228 2162 1015 1493 -48 169 -271 A O ATOM 1823 CB LEU A 228 41.672 -30.194 40.513 1.00 12.31 A C ANISOU 1823 CB LEU A 228 2045 988 1642 -129 -47 -257 A C ATOM 1824 CG LEU A 228 41.170 -30.289 41.941 1.00 14.09 A C ANISOU 1824 CG LEU A 228 2041 1395 1917 64 47 -55 A C ATOM 1825 CD1 LEU A 228 42.224 -30.846 42.878 1.00 15.73 A C ANISOU 1825 CD1 LEU A 228 2167 1971 1838 -213 -202 408 A C ATOM 1826 CD2 LEU A 228 40.683 -28.976 42.441 1.00 14.21 A C ANISOU 1826 CD2 LEU A 228 2531 1273 1593 42 145 -61 A C ATOM 1827 N GLY A 229 41.768 -28.411 37.671 1.00 11.73 A N ANISOU 1827 N GLY A 229 1863 909 1682 -64 136 22 A N ATOM 1828 CA GLY A 229 42.343 -28.236 36.362 1.00 11.74 A C ANISOU 1828 CA GLY A 229 1759 1021 1680 -126 28 -47 A C ATOM 1829 C GLY A 229 43.549 -27.314 36.348 1.00 10.85 A C ANISOU 1829 C GLY A 229 1781 944 1395 -161 166 14 A C ATOM 1830 O GLY A 229 43.644 -26.419 37.191 1.00 10.98 A O ANISOU 1830 O GLY A 229 1668 858 1644 72 153 -183 A O ATOM 1831 N LEU A 230 44.429 -27.519 35.371 1.00 10.24 A N ANISOU 1831 N LEU A 230 1715 732 1443 -196 147 -60 A N ATOM 1832 CA LEU A 230 45.671 -26.737 35.228 1.00 10.31 A C ANISOU 1832 CA LEU A 230 1602 920 1392 -78 324 -192 A C ATOM 1833 C LEU A 230 45.756 -26.240 33.777 1.00 10.46 A C ANISOU 1833 C LEU A 230 1756 721 1495 26 214 13 A C ATOM 1834 O LEU A 230 45.566 -26.997 32.833 1.00 11.31 A O ANISOU 1834 O LEU A 230 1790 938 1568 21 103 -53 A O ATOM 1835 CB LEU A 230 46.869 -27.664 35.483 1.00 11.90 A C ANISOU 1835 CB LEU A 230 1874 898 1747 123 185 -149 A C ATOM 1836 CG LEU A 230 48.244 -27.070 35.190 1.00 12.49 A C ANISOU 1836 CG LEU A 230 1617 1215 1911 220 13 -196 A C ATOM 1837 CD1 LEU A 230 48.541 -25.890 36.094 1.00 13.12 A C ANISOU 1837 CD1 LEU A 230 1753 1029 2202 94 -107 -128 A C ATOM 1838 CD2 LEU A 230 49.316 -28.120 35.264 1.00 13.40 A C ANISOU 1838 CD2 LEU A 230 1602 1107 2381 61 -336 -83 A C ATOM 1839 N LEU A 231 46.086 -24.953 33.603 1.00 9.96 A N ANISOU 1839 N LEU A 231 1601 646 1535 23 125 -103 A N ATOM 1840 CA LEU A 231 46.478 -24.422 32.295 1.00 11.03 A C ANISOU 1840 CA LEU A 231 1615 886 1688 8 227 -146 A C ATOM 1841 C LEU A 231 47.884 -23.844 32.443 1.00 11.12 A C ANISOU 1841 C LEU A 231 1688 1043 1490 -114 229 -190 A C ATOM 1842 O LEU A 231 48.094 -22.956 33.302 1.00 11.49 A O ANISOU 1842 O LEU A 231 1748 846 1771 -137 91 -193 A O ATOM 1843 CB LEU A 231 45.496 -23.324 31.879 1.00 10.78 A C ANISOU 1843 CB LEU A 231 1666 905 1523 47 157 -210 A C ATOM 1844 CG LEU A 231 45.815 -22.639 30.532 1.00 11.93 A C ANISOU 1844 CG LEU A 231 1934 717 1881 -103 404 -104 A C ATOM 1845 CD1 LEU A 231 45.707 -23.644 29.368 1.00 12.53 A C ANISOU 1845 CD1 LEU A 231 2047 792 1922 58 155 -133 A C ATOM 1846 CD2 LEU A 231 44.902 -21.440 30.305 1.00 12.64 A C ANISOU 1846 CD2 LEU A 231 2149 975 1676 98 292 -98 A C ATOM 1847 N SER A 232 48.805 -24.222 31.553 1.00 10.97 A N ANISOU 1847 N SER A 232 1661 882 1625 -75 203 -227 A N ATOM 1848 CA ASER A 232 50.217 -23.840 31.688 0.50 11.18 A C ANISOU 1848 CA ASER A 232 1734 819 1694 -103 488 -410 A C ATOM 1849 CA BSER A 232 50.127 -23.657 31.634 0.50 11.34 A C ANISOU 1849 CA BSER A 232 1735 900 1672 -153 411 -343 A C ATOM 1850 C SER A 232 50.834 -23.721 30.289 1.00 12.31 A C ANISOU 1850 C SER A 232 2028 1116 1532 -261 392 -377 A C ATOM 1851 O SER A 232 50.623 -24.603 29.474 1.00 14.00 A O ANISOU 1851 O SER A 232 2386 1097 1837 -200 422 -544 A O ATOM 1852 CB ASER A 232 50.939 -24.857 32.555 0.50 12.93 A C ANISOU 1852 CB ASER A 232 1921 1500 1490 -12 396 -239 A C ATOM 1853 CB BSER A 232 50.955 -24.306 32.680 0.50 11.32 A C ANISOU 1853 CB BSER A 232 1690 1026 1581 -193 260 -487 A C ATOM 1854 OG ASER A 232 52.306 -24.529 32.794 0.50 14.29 A O ANISOU 1854 OG ASER A 232 1957 1535 1935 -49 305 -141 A O ATOM 1855 OG BSER A 232 51.247 -25.637 32.295 0.50 12.79 A O ANISOU 1855 OG BSER A 232 1959 890 2009 43 176 -136 A O ATOM 1856 N LEU A 233 51.640 -22.698 30.059 1.00 11.42 A N ANISOU 1856 N LEU A 233 1818 893 1624 -47 345 -172 A N ATOM 1857 CA LEU A 233 52.476 -22.632 28.883 1.00 10.82 A C ANISOU 1857 CA LEU A 233 1745 767 1599 147 250 -110 A C ATOM 1858 C LEU A 233 53.851 -22.125 29.312 1.00 11.42 A C ANISOU 1858 C LEU A 233 1745 906 1687 -20 203 -120 A C ATOM 1859 O LEU A 233 53.953 -21.002 29.849 1.00 11.72 A O ANISOU 1859 O LEU A 233 1687 984 1782 58 286 -257 A O ATOM 1860 CB LEU A 233 51.865 -21.702 27.829 1.00 10.54 A C ANISOU 1860 CB LEU A 233 1742 791 1471 35 118 -117 A C ATOM 1861 CG LEU A 233 52.666 -21.601 26.524 1.00 11.74 A C ANISOU 1861 CG LEU A 233 1930 917 1612 116 247 18 A C ATOM 1862 CD1 LEU A 233 52.677 -22.958 25.814 1.00 13.48 A C ANISOU 1862 CD1 LEU A 233 2335 1230 1555 241 429 -166 A C ATOM 1863 CD2 LEU A 233 52.138 -20.449 25.647 1.00 13.52 A C ANISOU 1863 CD2 LEU A 233 2358 1111 1669 40 270 162 A C ATOM 1864 N LEU A 234 54.891 -22.905 29.037 1.00 12.71 A N ANISOU 1864 N LEU A 234 1809 965 2055 86 198 -43 A N ATOM 1865 CA ALEU A 234 56.279 -22.506 29.199 0.50 12.66 A C ANISOU 1865 CA ALEU A 234 1816 1030 1964 313 195 -286 A C ATOM 1866 CA BLEU A 234 56.272 -22.476 29.209 0.50 13.26 A C ANISOU 1866 CA BLEU A 234 1785 1289 1961 227 249 -347 A C ATOM 1867 C LEU A 234 56.812 -22.110 27.823 1.00 13.90 A C ANISOU 1867 C LEU A 234 2064 1274 1943 -55 190 -147 A C ATOM 1868 O LEU A 234 56.662 -22.851 26.865 1.00 15.88 A O ANISOU 1868 O LEU A 234 2565 1334 2131 -66 860 -519 A O ATOM 1869 CB ALEU A 234 57.098 -23.661 29.770 0.50 16.92 A C ANISOU 1869 CB ALEU A 234 2563 998 2867 496 -66 -129 A C ATOM 1870 CB BLEU A 234 57.103 -23.566 29.893 0.50 16.39 A C ANISOU 1870 CB BLEU A 234 1924 1454 2848 401 49 -265 A C ATOM 1871 CG ALEU A 234 58.560 -23.322 30.046 0.50 21.62 A C ANISOU 1871 CG ALEU A 234 2768 1745 3701 974 -511 -65 A C ATOM 1872 CG BLEU A 234 58.390 -23.071 30.561 0.50 22.51 A C ANISOU 1872 CG BLEU A 234 2358 2947 3248 657 -587 -647 A C ATOM 1873 CD1ALEU A 234 58.680 -22.480 31.288 0.50 24.30 A C ANISOU 1873 CD1ALEU A 234 4077 1740 3416 800 -1605 185 A C ATOM 1874 CD1BLEU A 234 58.737 -23.935 31.763 0.50 21.46 A C ANISOU 1874 CD1BLEU A 234 2557 3504 2091 433 -420 -1211 A C ATOM 1875 CD2ALEU A 234 59.384 -24.586 30.191 0.50 23.30 A C ANISOU 1875 CD2ALEU A 234 3685 848 4319 699 -587 -548 A C ATOM 1876 CD2BLEU A 234 59.538 -23.056 29.563 0.50 28.89 A C ANISOU 1876 CD2BLEU A 234 2373 4206 4396 -45 192 436 A C ATOM 1877 N VAL A 235 57.343 -20.887 27.716 1.00 13.44 A N ANISOU 1877 N VAL A 235 1870 1251 1983 -19 395 -233 A N ATOM 1878 CA VAL A 235 57.894 -20.379 26.472 1.00 14.63 A C ANISOU 1878 CA VAL A 235 1982 1489 2087 104 401 -234 A C ATOM 1879 C VAL A 235 59.377 -20.094 26.718 1.00 14.48 A C ANISOU 1879 C VAL A 235 1903 1868 1730 -12 312 -227 A C ATOM 1880 O VAL A 235 59.713 -19.237 27.563 1.00 15.60 A O ANISOU 1880 O VAL A 235 2184 1769 1972 -128 545 -357 A O ATOM 1881 CB VAL A 235 57.159 -19.108 26.014 1.00 14.69 A C ANISOU 1881 CB VAL A 235 2059 1477 2042 -78 337 -18 A C ATOM 1882 CG1 VAL A 235 57.687 -18.674 24.657 1.00 17.36 A C ANISOU 1882 CG1 VAL A 235 2421 2317 1856 102 305 -31 A C ATOM 1883 CG2 VAL A 235 55.656 -19.305 25.938 1.00 14.37 A C ANISOU 1883 CG2 VAL A 235 2025 1391 2041 272 437 -246 A C ATOM 1884 N VAL A 236 60.254 -20.741 25.958 1.00 15.62 A N ANISOU 1884 N VAL A 236 1997 1773 2162 -6 427 -317 A N ATOM 1885 CA VAL A 236 61.683 -20.535 26.054 1.00 15.04 A C ANISOU 1885 CA VAL A 236 2121 1451 2139 178 367 -258 A C ATOM 1886 C VAL A 236 62.148 -19.836 24.772 1.00 17.13 A C ANISOU 1886 C VAL A 236 2147 1959 2403 -89 385 6 A C ATOM 1887 O VAL A 236 61.810 -20.267 23.674 1.00 18.50 A O ANISOU 1887 O VAL A 236 2214 2399 2414 -247 720 -68 A O ATOM 1888 CB VAL A 236 62.432 -21.882 26.229 1.00 15.04 A C ANISOU 1888 CB VAL A 236 2137 1259 2318 84 270 -170 A C ATOM 1889 CG1 VAL A 236 63.925 -21.662 26.353 1.00 17.70 A C ANISOU 1889 CG1 VAL A 236 2090 2038 2595 315 203 -78 A C ATOM 1890 CG2 VAL A 236 61.903 -22.690 27.403 1.00 16.51 A C ANISOU 1890 CG2 VAL A 236 2281 1297 2693 31 187 17 A C ATOM 1891 N THR A 237 62.806 -18.688 24.940 1.00 16.44 A N ANISOU 1891 N THR A 237 2422 1815 2009 -176 915 -186 A N ATOM 1892 CA THR A 237 63.360 -17.953 23.810 1.00 17.32 A C ANISOU 1892 CA THR A 237 2485 1626 2470 -86 802 218 A C ATOM 1893 C THR A 237 64.828 -18.347 23.647 1.00 19.31 A C ANISOU 1893 C THR A 237 2369 2186 2781 -171 435 329 A C ATOM 1894 O THR A 237 65.633 -18.168 24.538 1.00 19.11 A O ANISOU 1894 O THR A 237 2147 2454 2658 -61 636 -169 A O ATOM 1895 CB THR A 237 63.257 -16.441 24.026 1.00 19.06 A C ANISOU 1895 CB THR A 237 2560 1589 3092 -256 596 210 A C ATOM 1896 CG2 THR A 237 63.839 -15.657 22.867 1.00 20.79 A C ANISOU 1896 CG2 THR A 237 2863 2119 2917 -86 732 267 A C ATOM 1897 OG1 THR A 237 61.870 -16.149 24.203 1.00 21.39 A O ANISOU 1897 OG1 THR A 237 2676 2291 3160 293 864 165 A O ATOM 1898 N LYS A 238 65.129 -18.910 22.486 1.00 22.10 A N ANISOU 1898 N LYS A 238 2427 2555 3413 -3 931 -44 A N ATOM 1899 CA LYS A 238 66.457 -19.352 22.162 1.00 21.26 A C ANISOU 1899 CA LYS A 238 2240 2434 3401 -168 869 -312 A C ATOM 1900 C LYS A 238 67.314 -18.163 21.714 1.00 24.73 A C ANISOU 1900 C LYS A 238 2741 2807 3845 -252 1198 352 A C ATOM 1901 O LYS A 238 66.810 -17.068 21.408 1.00 24.92 A O ANISOU 1901 O LYS A 238 3268 2598 3599 -353 1181 -221 A O ATOM 1902 CB LYS A 238 66.371 -20.441 21.096 1.00 24.52 A C ANISOU 1902 CB LYS A 238 2824 2935 3555 -185 1138 -689 A C ATOM 1903 CG LYS A 238 65.828 -21.762 21.617 1.00 28.66 A C ANISOU 1903 CG LYS A 238 3484 2938 4468 -221 908 -485 A C ATOM 1904 CD LYS A 238 65.616 -22.758 20.515 1.00 31.03 A C ANISOU 1904 CD LYS A 238 3846 3186 4758 -226 880 -852 A C ATOM 1905 CE LYS A 238 64.325 -22.539 19.756 1.00 36.54 A C ANISOU 1905 CE LYS A 238 4266 4424 5191 203 665 -798 A C ATOM 1906 NZ LYS A 238 64.351 -23.179 18.415 1.00 42.46 A N ANISOU 1906 NZ LYS A 238 5240 5073 5817 -496 846 -1590 A N ATOM 1907 N SER A 239 68.620 -18.415 21.651 1.00 27.03 A N ANISOU 1907 N SER A 239 2907 3019 4340 -370 1286 -106 A N ATOM 1908 CA SER A 239 69.632 -17.425 21.325 1.00 30.61 A C ANISOU 1908 CA SER A 239 3259 3276 5095 -754 912 303 A C ATOM 1909 C SER A 239 69.374 -16.769 19.957 1.00 31.58 A C ANISOU 1909 C SER A 239 3800 3508 4691 -1084 895 10 A C ATOM 1910 O SER A 239 69.709 -15.621 19.775 1.00 36.17 A O ANISOU 1910 O SER A 239 5120 3435 5187 -1331 2383 134 A O ATOM 1911 CB SER A 239 71.020 -18.048 21.397 1.00 34.47 A C ANISOU 1911 CB SER A 239 3252 4108 5735 -660 -682 533 A C ATOM 1912 OG SER A 239 71.351 -18.351 22.749 1.00 37.41 A O ANISOU 1912 OG SER A 239 4243 4180 5791 -875 555 977 A O ATOM 1913 N ASP A 240 68.780 -17.508 19.017 1.00 32.68 A N ANISOU 1913 N ASP A 240 3738 4645 4032 -1085 1608 -388 A N ATOM 1914 CA ASP A 240 68.503 -17.027 17.663 1.00 33.72 A C ANISOU 1914 CA ASP A 240 4759 4026 4025 -780 1888 110 A C ATOM 1915 C ASP A 240 67.138 -16.314 17.569 1.00 34.30 A C ANISOU 1915 C ASP A 240 4577 4845 3608 -1105 1166 819 A C ATOM 1916 O ASP A 240 66.763 -15.842 16.471 1.00 34.17 A O ANISOU 1916 O ASP A 240 5099 4601 3283 -1070 1703 1143 A O ATOM 1917 CB ASP A 240 68.623 -18.187 16.671 1.00 36.43 A C ANISOU 1917 CB ASP A 240 4437 5734 3669 -908 2066 -885 A C ATOM 1918 CG ASP A 240 67.513 -19.229 16.748 1.00 41.48 A C ANISOU 1918 CG ASP A 240 5094 6120 4543 -1140 2743 -1057 A C ATOM 1919 OD1 ASP A 240 66.595 -19.055 17.555 1.00 37.62 A O ANISOU 1919 OD1 ASP A 240 4759 5387 4148 -1079 2517 -676 A O ATOM 1920 OD2 ASP A 240 67.574 -20.212 15.976 1.00 46.93 A O ANISOU 1920 OD2 ASP A 240 5758 6103 5969 -362 2758 -1738 A O ATOM 1921 N GLY A 241 66.406 -16.229 18.694 1.00 32.68 A N ANISOU 1921 N GLY A 241 3632 3990 4792 -528 1469 734 A N ATOM 1922 CA GLY A 241 65.129 -15.503 18.787 1.00 31.19 A C ANISOU 1922 CA GLY A 241 3837 3369 4643 -613 902 1245 A C ATOM 1923 C GLY A 241 63.902 -16.384 18.541 1.00 29.24 A C ANISOU 1923 C GLY A 241 3834 3373 3900 -648 1340 753 A C ATOM 1924 O GLY A 241 62.777 -15.921 18.716 1.00 31.19 A O ANISOU 1924 O GLY A 241 3891 3692 4265 -434 1013 749 A O ATOM 1925 N SER A 242 64.112 -17.634 18.096 1.00 28.92 A N ANISOU 1925 N SER A 242 4279 3708 2998 -645 1551 123 A N ATOM 1926 CA SER A 242 63.041 -18.584 17.936 1.00 29.91 A C ANISOU 1926 CA SER A 242 4120 3933 3309 -400 1125 439 A C ATOM 1927 C SER A 242 62.653 -19.113 19.316 1.00 25.00 A C ANISOU 1927 C SER A 242 3440 3298 2761 -270 745 -85 A C ATOM 1928 O SER A 242 63.399 -18.954 20.296 1.00 23.81 A O ANISOU 1928 O SER A 242 3330 3449 2267 -295 976 419 A O ATOM 1929 CB SER A 242 63.411 -19.706 17.007 1.00 30.51 A C ANISOU 1929 CB SER A 242 4397 4466 2729 -814 756 135 A C ATOM 1930 OG SER A 242 64.417 -20.531 17.568 1.00 33.32 A O ANISOU 1930 OG SER A 242 4340 4968 3352 -199 1221 -436 A O ATOM 1931 N LYS A 243 61.485 -19.749 19.373 1.00 24.55 A N ANISOU 1931 N LYS A 243 3409 3076 2843 -393 986 151 A N ATOM 1932 CA LYS A 243 60.889 -20.118 20.654 1.00 22.73 A C ANISOU 1932 CA LYS A 243 3214 2658 2761 -418 836 263 A C ATOM 1933 C LYS A 243 60.528 -21.605 20.700 1.00 20.42 A C ANISOU 1933 C LYS A 243 2943 2505 2312 -243 398 347 A C ATOM 1934 O LYS A 243 60.056 -22.198 19.707 1.00 24.71 A O ANISOU 1934 O LYS A 243 3372 3579 2435 -714 554 87 A O ATOM 1935 CB LYS A 243 59.665 -19.238 20.951 1.00 22.81 A C ANISOU 1935 CB LYS A 243 3356 2857 2453 -483 1086 405 A C ATOM 1936 CG LYS A 243 60.004 -17.768 21.121 1.00 26.51 A C ANISOU 1936 CG LYS A 243 3873 2785 3414 -186 1134 540 A C ATOM 1937 CD LYS A 243 58.884 -16.811 21.472 1.00 31.02 A C ANISOU 1937 CD LYS A 243 4641 3374 3768 428 1023 608 A C ATOM 1938 CE LYS A 243 59.416 -15.391 21.418 1.00 36.26 A C ANISOU 1938 CE LYS A 243 5175 3571 5029 386 1330 448 A C ATOM 1939 NZ LYS A 243 58.626 -14.458 22.259 1.00 42.66 A N ANISOU 1939 NZ LYS A 243 5898 5015 5294 -143 2757 -30 A N ATOM 1940 N LEU A 244 60.662 -22.152 21.908 1.00 17.98 A N ANISOU 1940 N LEU A 244 2646 2030 2155 37 645 -86 A N ATOM 1941 CA ALEU A 244 60.141 -23.466 22.284 0.50 17.54 A C ANISOU 1941 CA ALEU A 244 2230 2068 2364 -286 859 -509 A C ATOM 1942 CA BLEU A 244 60.133 -23.469 22.295 0.50 17.71 A C ANISOU 1942 CA BLEU A 244 2229 2033 2464 -291 906 -483 A C ATOM 1943 C LEU A 244 58.900 -23.261 23.167 1.00 16.52 A C ANISOU 1943 C LEU A 244 2150 2113 2014 -123 689 -370 A C ATOM 1944 O LEU A 244 58.914 -22.422 24.062 1.00 18.15 A O ANISOU 1944 O LEU A 244 2439 2068 2386 -248 742 -530 A O ATOM 1945 CB ALEU A 244 61.280 -24.201 23.009 0.50 20.54 A C ANISOU 1945 CB ALEU A 244 2829 2277 2697 119 348 -687 A C ATOM 1946 CB BLEU A 244 61.143 -24.255 23.139 0.50 19.10 A C ANISOU 1946 CB BLEU A 244 2665 1651 2939 -102 652 -387 A C ATOM 1947 CG ALEU A 244 60.972 -25.498 23.762 0.50 25.26 A C ANISOU 1947 CG ALEU A 244 3440 2982 3173 13 286 -98 A C ATOM 1948 CG BLEU A 244 62.549 -24.431 22.580 0.50 22.45 A C ANISOU 1948 CG BLEU A 244 2783 2196 3549 -178 972 -4 A C ATOM 1949 CD1ALEU A 244 60.527 -26.614 22.824 0.50 27.72 A C ANISOU 1949 CD1ALEU A 244 3131 3404 3995 127 -347 -369 A C ATOM 1950 CD1BLEU A 244 63.408 -25.176 23.589 0.50 25.16 A C ANISOU 1950 CD1BLEU A 244 2429 2818 4310 116 606 -298 A C ATOM 1951 CD2ALEU A 244 62.207 -25.949 24.541 0.50 25.41 A C ANISOU 1951 CD2ALEU A 244 3896 2461 3295 59 -130 -419 A C ATOM 1952 CD2BLEU A 244 62.517 -25.149 21.244 0.50 24.05 A C ANISOU 1952 CD2BLEU A 244 3025 2343 3770 -35 1018 -272 A C ATOM 1953 N TYR A 245 57.847 -24.024 22.892 1.00 17.03 A N ANISOU 1953 N TYR A 245 2347 1787 2335 -120 626 -593 A N ATOM 1954 CA TYR A 245 56.558 -23.985 23.620 1.00 16.30 A C ANISOU 1954 CA TYR A 245 2171 1950 2068 -175 435 -259 A C ATOM 1955 C TYR A 245 56.299 -25.320 24.309 1.00 15.28 A C ANISOU 1955 C TYR A 245 2305 1593 1907 -256 332 -490 A C ATOM 1956 O TYR A 245 56.258 -26.348 23.645 1.00 20.64 A O ANISOU 1956 O TYR A 245 3422 2087 2330 -698 703 -901 A O ATOM 1957 CB TYR A 245 55.404 -23.688 22.670 1.00 17.67 A C ANISOU 1957 CB TYR A 245 2103 2558 2052 -74 381 -242 A C ATOM 1958 CG TYR A 245 55.559 -22.356 21.997 1.00 20.55 A C ANISOU 1958 CG TYR A 245 2227 3066 2512 -88 47 249 A C ATOM 1959 CD1 TYR A 245 56.239 -22.230 20.789 1.00 24.00 A C ANISOU 1959 CD1 TYR A 245 2747 3704 2665 174 209 385 A C ATOM 1960 CD2 TYR A 245 55.023 -21.231 22.573 1.00 22.89 A C ANISOU 1960 CD2 TYR A 245 3055 2856 2786 -127 201 250 A C ATOM 1961 CE1 TYR A 245 56.397 -20.996 20.190 1.00 27.70 A C ANISOU 1961 CE1 TYR A 245 3807 4164 2554 -62 268 601 A C ATOM 1962 CE2 TYR A 245 55.178 -19.986 21.991 1.00 27.18 A C ANISOU 1962 CE2 TYR A 245 3897 3224 3204 -21 -198 808 A C ATOM 1963 CZ TYR A 245 55.876 -19.872 20.804 1.00 25.45 A C ANISOU 1963 CZ TYR A 245 3409 2961 3298 79 -247 1196 A C ATOM 1964 OH TYR A 245 56.001 -18.660 20.216 1.00 32.79 A O ANISOU 1964 OH TYR A 245 4705 3367 4384 -148 -803 1994 A O ATOM 1965 N ILE A 246 56.092 -25.310 25.626 1.00 14.29 A N ANISOU 1965 N ILE A 246 2157 1301 1970 -48 297 -252 A N ATOM 1966 CA ILE A 246 55.814 -26.535 26.356 1.00 13.57 A C ANISOU 1966 CA ILE A 246 2045 1251 1858 -97 401 -346 A C ATOM 1967 C ILE A 246 54.452 -26.332 26.995 1.00 13.60 A C ANISOU 1967 C ILE A 246 1816 1507 1842 -23 227 -10 A C ATOM 1968 O ILE A 246 54.335 -25.646 28.043 1.00 15.70 A O ANISOU 1968 O ILE A 246 2303 1438 2223 23 310 -367 A O ATOM 1969 CB ILE A 246 56.859 -26.853 27.448 1.00 15.53 A C ANISOU 1969 CB ILE A 246 2245 1478 2178 -81 129 -196 A C ATOM 1970 CG1 ILE A 246 58.296 -26.838 26.933 1.00 20.33 A C ANISOU 1970 CG1 ILE A 246 2428 2144 3152 333 218 -12 A C ATOM 1971 CG2 ILE A 246 56.515 -28.199 28.102 1.00 16.82 A C ANISOU 1971 CG2 ILE A 246 2483 1341 2566 89 272 -265 A C ATOM 1972 CD1 ILE A 246 58.548 -27.836 25.859 1.00 26.27 A C ANISOU 1972 CD1 ILE A 246 2885 3692 3402 22 592 -681 A C ATOM 1973 N PRO A 247 53.387 -26.825 26.346 1.00 14.16 A N ANISOU 1973 N PRO A 247 2201 1299 1878 -72 222 -237 A N ATOM 1974 CA PRO A 247 52.036 -26.620 26.838 1.00 13.52 A C ANISOU 1974 CA PRO A 247 2013 1090 2032 -205 326 21 A C ATOM 1975 C PRO A 247 51.578 -27.656 27.853 1.00 11.83 A C ANISOU 1975 C PRO A 247 1874 698 1922 -10 284 -102 A C ATOM 1976 O PRO A 247 52.018 -28.828 27.801 1.00 13.49 A O ANISOU 1976 O PRO A 247 2517 811 1795 238 459 -74 A O ATOM 1977 CB PRO A 247 51.195 -26.730 25.555 1.00 14.90 A C ANISOU 1977 CB PRO A 247 2192 1313 2155 -129 103 53 A C ATOM 1978 CG PRO A 247 51.913 -27.824 24.788 1.00 18.08 A C ANISOU 1978 CG PRO A 247 2584 2112 2172 -94 72 -296 A C ATOM 1979 CD PRO A 247 53.380 -27.531 25.053 1.00 18.38 A C ANISOU 1979 CD PRO A 247 2610 2267 2106 -77 194 -659 A C ATOM 1980 N SER A 248 50.580 -27.299 28.667 1.00 12.26 A N ANISOU 1980 N SER A 248 1966 932 1758 -86 309 -48 A N ATOM 1981 CA SER A 248 49.751 -28.284 29.343 1.00 12.26 A C ANISOU 1981 CA SER A 248 1668 1201 1789 -114 280 60 A C ATOM 1982 C SER A 248 48.935 -29.009 28.286 1.00 12.82 A C ANISOU 1982 C SER A 248 1962 1097 1811 33 203 -52 A C ATOM 1983 O SER A 248 48.264 -28.402 27.454 1.00 13.87 A O ANISOU 1983 O SER A 248 2288 1027 1955 -69 -61 -128 A O ATOM 1984 CB SER A 248 48.865 -27.642 30.380 1.00 12.35 A C ANISOU 1984 CB SER A 248 1780 1341 1570 -20 215 105 A C ATOM 1985 OG SER A 248 48.170 -26.504 29.868 1.00 11.97 A O ANISOU 1985 OG SER A 248 1889 864 1794 -112 9 -170 A O ATOM 1986 N ASP A 249 48.938 -30.354 28.350 1.00 12.87 A N ANISOU 1986 N ASP A 249 2184 1034 1668 -70 318 -132 A N ATOM 1987 CA ASP A 249 48.159 -31.187 27.408 1.00 13.31 A C ANISOU 1987 CA ASP A 249 2050 1303 1701 -1 197 -179 A C ATOM 1988 C ASP A 249 48.139 -32.610 27.974 1.00 13.93 A C ANISOU 1988 C ASP A 249 2231 1307 1752 -93 143 -288 A C ATOM 1989 O ASP A 249 48.656 -32.841 29.075 1.00 14.04 A O ANISOU 1989 O ASP A 249 2615 913 1803 -69 77 -497 A O ATOM 1990 CB ASP A 249 48.713 -31.109 25.988 1.00 14.29 A C ANISOU 1990 CB ASP A 249 2551 989 1889 -22 287 -82 A C ATOM 1991 CG ASP A 249 50.091 -31.705 25.802 1.00 15.25 A C ANISOU 1991 CG ASP A 249 2407 1475 1912 -98 215 -93 A C ATOM 1992 OD1 ASP A 249 50.543 -32.463 26.698 1.00 15.78 A O ANISOU 1992 OD1 ASP A 249 2831 1355 1810 -25 262 -64 A O ATOM 1993 OD2 ASP A 249 50.741 -31.396 24.751 1.00 19.96 A O ANISOU 1993 OD2 ASP A 249 3356 1565 2663 179 1042 23 A O ATOM 1994 N SER A 250 47.555 -33.538 27.203 1.00 14.56 A N ANISOU 1994 N SER A 250 2725 1277 1528 -310 17 -121 A N ATOM 1995 CA ASER A 250 47.279 -34.913 27.635 0.50 15.29 A C ANISOU 1995 CA ASER A 250 2717 1234 1857 -91 -34 3 A C ATOM 1996 CA BSER A 250 47.268 -34.876 27.740 0.50 14.64 A C ANISOU 1996 CA BSER A 250 2588 1257 1717 -107 -35 11 A C ATOM 1997 C SER A 250 48.553 -35.754 27.717 1.00 15.30 A C ANISOU 1997 C SER A 250 2823 947 2044 -65 100 4 A C ATOM 1998 O SER A 250 48.495 -36.970 28.006 1.00 17.61 A O ANISOU 1998 O SER A 250 3218 824 2646 -6 123 12 A O ATOM 1999 CB ASER A 250 46.330 -35.572 26.675 0.50 17.49 A C ANISOU 1999 CB ASER A 250 3169 992 2484 -164 -218 -293 A C ATOM 2000 CB BSER A 250 46.024 -35.489 27.027 0.50 14.95 A C ANISOU 2000 CB BSER A 250 2410 1090 2180 146 -106 -97 A C ATOM 2001 OG ASER A 250 47.038 -36.014 25.523 0.50 19.75 A O ANISOU 2001 OG ASER A 250 2903 1584 3014 -5 -192 -841 A O ATOM 2002 OG BSER A 250 44.810 -34.694 27.163 0.50 14.30 A O ANISOU 2002 OG BSER A 250 1949 1032 2452 -192 -198 228 A O ATOM 2003 N SER A 251 49.729 -35.177 27.408 1.00 14.86 A N ANISOU 2003 N SER A 251 2650 1264 1729 -2 136 -348 A N ATOM 2004 CA SER A 251 51.033 -35.835 27.618 1.00 15.40 A C ANISOU 2004 CA SER A 251 2723 932 2196 -139 84 -305 A C ATOM 2005 C SER A 251 51.533 -35.788 29.075 1.00 15.52 A C ANISOU 2005 C SER A 251 2519 1306 2070 136 333 -420 A C ATOM 2006 O SER A 251 52.518 -36.459 29.404 1.00 17.76 A O ANISOU 2006 O SER A 251 2603 1452 2691 329 600 -329 A O ATOM 2007 CB SER A 251 52.119 -35.350 26.682 1.00 18.81 A C ANISOU 2007 CB SER A 251 2850 1783 2512 -79 377 -229 A C ATOM 2008 OG SER A 251 52.516 -34.023 27.028 1.00 17.58 A O ANISOU 2008 OG SER A 251 2998 1607 2073 -100 433 -2 A O ATOM 2009 N TRP A 252 50.905 -34.962 29.923 1.00 13.01 A N ANISOU 2009 N TRP A 252 2418 723 1801 270 23 -212 A N ATOM 2010 CA TRP A 252 51.305 -34.874 31.307 1.00 12.75 A C ANISOU 2010 CA TRP A 252 2173 690 1980 323 14 -18 A C ATOM 2011 C TRP A 252 50.808 -36.100 32.073 1.00 12.41 A C ANISOU 2011 C TRP A 252 1991 930 1794 244 126 -83 A C ATOM 2012 O TRP A 252 49.886 -36.776 31.637 1.00 14.11 A O ANISOU 2012 O TRP A 252 2211 1104 2047 73 -5 -131 A O ATOM 2013 CB TRP A 252 50.770 -33.553 31.880 1.00 12.28 A C ANISOU 2013 CB TRP A 252 1995 796 1873 242 151 -126 A C ATOM 2014 CG TRP A 252 51.376 -32.282 31.380 1.00 12.93 A C ANISOU 2014 CG TRP A 252 2137 1101 1672 231 192 90 A C ATOM 2015 CD1 TRP A 252 51.607 -31.902 30.084 1.00 11.87 A C ANISOU 2015 CD1 TRP A 252 2120 547 1843 158 272 -33 A C ATOM 2016 CD2 TRP A 252 51.805 -31.213 32.217 1.00 12.32 A C ANISOU 2016 CD2 TRP A 252 1784 1156 1741 246 256 87 A C ATOM 2017 CE2 TRP A 252 52.274 -30.211 31.344 1.00 12.48 A C ANISOU 2017 CE2 TRP A 252 2191 835 1715 154 176 -8 A C ATOM 2018 CE3 TRP A 252 51.889 -31.010 33.605 1.00 12.92 A C ANISOU 2018 CE3 TRP A 252 2258 830 1818 254 171 -83 A C ATOM 2019 NE1 TRP A 252 52.121 -30.637 30.051 1.00 12.41 A N ANISOU 2019 NE1 TRP A 252 2096 674 1942 67 152 0 A N ATOM 2020 CZ2 TRP A 252 52.747 -28.992 31.826 1.00 11.21 A C ANISOU 2020 CZ2 TRP A 252 1787 665 1806 161 133 247 A C ATOM 2021 CZ3 TRP A 252 52.348 -29.790 34.066 1.00 12.65 A C ANISOU 2021 CZ3 TRP A 252 1818 1123 1864 162 105 -176 A C ATOM 2022 CH2 TRP A 252 52.819 -28.826 33.179 1.00 13.17 A C ANISOU 2022 CH2 TRP A 252 2019 1189 1793 121 133 -136 A C ATOM 2023 N LYS A 253 51.409 -36.295 33.229 1.00 12.19 A N ANISOU 2023 N LYS A 253 2010 931 1691 103 222 -101 A N ATOM 2024 CA LYS A 253 50.971 -37.325 34.173 1.00 12.51 A C ANISOU 2024 CA LYS A 253 1871 1311 1569 12 281 -5 A C ATOM 2025 C LYS A 253 50.529 -36.684 35.476 1.00 11.82 A C ANISOU 2025 C LYS A 253 2060 841 1588 -239 235 -162 A C ATOM 2026 O LYS A 253 50.846 -35.516 35.754 1.00 12.11 A O ANISOU 2026 O LYS A 253 2042 757 1799 -128 204 -193 A O ATOM 2027 CB LYS A 253 52.075 -38.332 34.458 1.00 15.00 A C ANISOU 2027 CB LYS A 253 2321 1518 1858 338 257 90 A C ATOM 2028 CG LYS A 253 52.518 -39.133 33.230 1.00 17.07 A C ANISOU 2028 CG LYS A 253 2597 1441 2446 473 288 -201 A C ATOM 2029 CD LYS A 253 53.350 -40.342 33.632 1.00 25.73 A C ANISOU 2029 CD LYS A 253 4170 2259 3344 1310 309 237 A C ATOM 2030 CE LYS A 253 54.025 -41.046 32.496 1.00 33.49 A C ANISOU 2030 CE LYS A 253 4770 3739 4213 1636 572 -457 A C ATOM 2031 NZ LYS A 253 54.644 -42.266 33.050 1.00 44.89 A N ANISOU 2031 NZ LYS A 253 6984 4505 5564 2719 514 -148 A N ATOM 2032 N SER A 254 49.750 -37.406 36.263 1.00 11.39 A N ANISOU 2032 N SER A 254 1951 627 1749 12 296 -9 A N ATOM 2033 CA SER A 254 49.139 -36.869 37.474 1.00 12.08 A C ANISOU 2033 CA SER A 254 2033 1152 1403 -116 186 16 A C ATOM 2034 C SER A 254 49.113 -37.905 38.596 1.00 11.73 A C ANISOU 2034 C SER A 254 2142 660 1654 220 361 -46 A C ATOM 2035 O SER A 254 49.161 -39.135 38.384 1.00 12.50 A O ANISOU 2035 O SER A 254 2351 608 1790 165 82 21 A O ATOM 2036 CB SER A 254 47.718 -36.386 37.195 1.00 13.28 A C ANISOU 2036 CB SER A 254 2221 831 1993 -12 68 -37 A C ATOM 2037 OG SER A 254 46.899 -37.465 36.774 1.00 13.31 A O ANISOU 2037 OG SER A 254 2099 929 2030 48 207 -37 A O ATOM 2038 N SER A 255 49.034 -37.440 39.822 1.00 11.91 A N ANISOU 2038 N SER A 255 2105 832 1586 55 140 -63 A N ATOM 2039 CA SER A 255 48.962 -38.310 41.024 1.00 12.64 A C ANISOU 2039 CA SER A 255 2300 1020 1482 106 267 -184 A C ATOM 2040 C SER A 255 48.487 -37.480 42.201 1.00 11.82 A C ANISOU 2040 C SER A 255 2110 631 1748 73 278 -263 A C ATOM 2041 O SER A 255 48.762 -36.276 42.264 1.00 14.28 A O ANISOU 2041 O SER A 255 3034 542 1849 112 472 -170 A O ATOM 2042 CB SER A 255 50.336 -38.837 41.347 1.00 15.73 A C ANISOU 2042 CB SER A 255 2235 1642 2100 153 432 135 A C ATOM 2043 OG SER A 255 50.326 -39.666 42.483 1.00 17.63 A O ANISOU 2043 OG SER A 255 2997 1314 2385 320 317 197 A O ATOM 2044 N THR A 256 47.858 -38.094 43.191 1.00 13.27 A N ANISOU 2044 N THR A 256 2119 1112 1810 214 191 -26 A N ATOM 2045 CA THR A 256 47.755 -37.512 44.479 1.00 14.48 A C ANISOU 2045 CA THR A 256 2243 1409 1849 215 227 -90 A C ATOM 2046 C THR A 256 49.129 -37.463 45.139 1.00 13.83 A C ANISOU 2046 C THR A 256 2208 1375 1669 288 122 -147 A C ATOM 2047 O THR A 256 50.077 -38.129 44.707 1.00 14.35 A O ANISOU 2047 O THR A 256 2266 1353 1833 306 285 -148 A O ATOM 2048 CB THR A 256 46.773 -38.278 45.365 1.00 14.79 A C ANISOU 2048 CB THR A 256 2249 1709 1662 330 398 44 A C ATOM 2049 CG2 THR A 256 45.367 -38.198 44.827 1.00 18.76 A C ANISOU 2049 CG2 THR A 256 2459 2543 2124 -291 187 9 A C ATOM 2050 OG1 THR A 256 47.257 -39.624 45.470 1.00 17.11 A O ANISOU 2050 OG1 THR A 256 2557 1484 2460 24 8 234 A O ATOM 2051 N GLY A 257 49.218 -36.668 46.207 1.00 14.22 A N ANISOU 2051 N GLY A 257 2363 1149 1890 371 -167 -100 A N ATOM 2052 CA GLY A 257 50.440 -36.532 46.949 1.00 13.74 A C ANISOU 2052 CA GLY A 257 2196 1191 1832 346 -82 -215 A C ATOM 2053 C GLY A 257 50.177 -36.403 48.443 1.00 13.46 A C ANISOU 2053 C GLY A 257 1929 1271 1912 521 29 31 A C ATOM 2054 O GLY A 257 49.154 -36.872 48.936 1.00 14.24 A O ANISOU 2054 O GLY A 257 2183 1218 2006 79 -20 -154 A O ATOM 2055 N PRO A 258 51.087 -35.759 49.203 1.00 13.95 A N ANISOU 2055 N PRO A 258 2063 1351 1887 481 -130 23 A N ATOM 2056 CA PRO A 258 50.922 -35.714 50.645 1.00 14.37 A C ANISOU 2056 CA PRO A 258 2312 1099 2046 319 61 -132 A C ATOM 2057 C PRO A 258 49.721 -34.909 51.142 1.00 12.93 A C ANISOU 2057 C PRO A 258 2171 1314 1428 434 -44 185 A C ATOM 2058 O PRO A 258 49.282 -35.107 52.290 1.00 12.89 A O ANISOU 2058 O PRO A 258 2153 1149 1593 456 152 119 A O ATOM 2059 CB PRO A 258 52.245 -35.118 51.145 1.00 14.69 A C ANISOU 2059 CB PRO A 258 2103 1413 2063 442 -211 119 A C ATOM 2060 CG PRO A 258 52.726 -34.264 49.955 1.00 14.53 A C ANISOU 2060 CG PRO A 258 1875 1436 2209 99 -76 31 A C ATOM 2061 CD PRO A 258 52.298 -35.072 48.741 1.00 15.03 A C ANISOU 2061 CD PRO A 258 2133 1326 2251 445 -133 -37 A C ATOM 2062 N ILE A 259 49.243 -33.950 50.334 1.00 12.88 A N ANISOU 2062 N ILE A 259 2064 1258 1569 279 136 387 A N ATOM 2063 CA ILE A 259 48.061 -33.230 50.811 1.00 12.66 A C ANISOU 2063 CA ILE A 259 1966 1136 1706 120 -14 160 A C ATOM 2064 C ILE A 259 46.850 -34.144 50.640 1.00 12.87 A C ANISOU 2064 C ILE A 259 1859 1166 1863 251 46 93 A C ATOM 2065 O ILE A 259 46.474 -34.466 49.514 1.00 14.47 A O ANISOU 2065 O ILE A 259 2157 1555 1784 209 151 222 A O ATOM 2066 CB ILE A 259 47.868 -31.859 50.128 1.00 13.70 A C ANISOU 2066 CB ILE A 259 2074 1251 1878 350 33 261 A C ATOM 2067 CG1 ILE A 259 49.126 -30.984 50.125 1.00 14.40 A C ANISOU 2067 CG1 ILE A 259 2013 1405 2051 304 -184 279 A C ATOM 2068 CG2 ILE A 259 46.695 -31.144 50.793 1.00 14.53 A C ANISOU 2068 CG2 ILE A 259 2194 1410 1914 529 -54 -87 A C ATOM 2069 CD1 ILE A 259 49.063 -29.816 49.167 1.00 14.66 A C ANISOU 2069 CD1 ILE A 259 2145 1288 2134 296 -268 325 A C ATOM 2070 N ILE A 260 46.204 -34.467 51.776 1.00 13.43 A N ANISOU 2070 N ILE A 260 2086 1147 1870 367 86 144 A N ATOM 2071 CA ILE A 260 44.993 -35.269 51.770 1.00 14.27 A C ANISOU 2071 CA ILE A 260 2189 1342 1890 80 -72 92 A C ATOM 2072 C ILE A 260 43.776 -34.405 51.449 1.00 13.09 A C ANISOU 2072 C ILE A 260 1852 1284 1835 -118 126 30 A C ATOM 2073 O ILE A 260 42.899 -34.790 50.670 1.00 12.97 A O ANISOU 2073 O ILE A 260 2099 842 1985 104 -3 -28 A O ATOM 2074 CB ILE A 260 44.813 -35.996 53.119 1.00 15.89 A C ANISOU 2074 CB ILE A 260 2385 1466 2187 361 143 351 A C ATOM 2075 CG1 ILE A 260 46.050 -36.819 53.479 1.00 16.96 A C ANISOU 2075 CG1 ILE A 260 2238 1787 2420 420 334 272 A C ATOM 2076 CG2 ILE A 260 43.565 -36.852 53.101 1.00 17.66 A C ANISOU 2076 CG2 ILE A 260 2560 1348 2800 337 101 600 A C ATOM 2077 CD1 ILE A 260 46.475 -37.818 52.422 1.00 19.66 A C ANISOU 2077 CD1 ILE A 260 2925 1644 2901 852 -32 60 A C ATOM 2078 N SER A 261 43.718 -33.226 52.101 1.00 12.39 A N ANISOU 2078 N SER A 261 1729 1334 1642 110 139 72 A N ATOM 2079 CA SER A 261 42.664 -32.265 51.845 1.00 13.24 A C ANISOU 2079 CA SER A 261 1785 1278 1965 43 105 6 A C ATOM 2080 C SER A 261 43.228 -30.881 52.142 1.00 11.59 A C ANISOU 2080 C SER A 261 1849 1107 1445 122 140 280 A C ATOM 2081 O SER A 261 44.084 -30.749 52.995 1.00 12.50 A O ANISOU 2081 O SER A 261 2017 915 1815 338 -68 224 A O ATOM 2082 CB SER A 261 41.411 -32.533 52.646 1.00 12.90 A C ANISOU 2082 CB SER A 261 2054 834 2012 185 238 66 A C ATOM 2083 OG SER A 261 41.697 -32.485 54.016 1.00 14.15 A O ANISOU 2083 OG SER A 261 2225 1299 1849 161 212 308 A O ATOM 2084 N SER A 262 42.725 -29.880 51.433 1.00 11.31 A N ANISOU 2084 N SER A 262 1977 981 1338 91 -40 164 A N ATOM 2085 CA SER A 262 43.125 -28.480 51.726 1.00 11.62 A C ANISOU 2085 CA SER A 262 1818 964 1633 196 34 53 A C ATOM 2086 C SER A 262 42.000 -27.547 51.299 1.00 10.93 A C ANISOU 2086 C SER A 262 1717 873 1564 126 89 8 A C ATOM 2087 O SER A 262 41.700 -27.489 50.118 1.00 11.73 A O ANISOU 2087 O SER A 262 1943 958 1555 222 50 -47 A O ATOM 2088 CB SER A 262 44.451 -28.165 51.043 1.00 12.07 A C ANISOU 2088 CB SER A 262 1925 789 1873 19 109 89 A C ATOM 2089 OG SER A 262 44.989 -26.950 51.541 1.00 12.44 A O ANISOU 2089 OG SER A 262 1903 895 1926 -167 101 105 A O ATOM 2090 N GLU A 263 41.358 -26.941 52.293 1.00 11.27 A N ANISOU 2090 N GLU A 263 1772 1203 1303 18 93 52 A N ATOM 2091 CA GLU A 263 40.074 -26.246 52.127 1.00 12.24 A C ANISOU 2091 CA GLU A 263 1864 1097 1690 -18 44 -65 A C ATOM 2092 C GLU A 263 40.207 -24.878 52.787 1.00 11.72 A C ANISOU 2092 C GLU A 263 1812 1030 1612 194 76 -8 A C ATOM 2093 O GLU A 263 40.772 -24.772 53.851 1.00 12.43 A O ANISOU 2093 O GLU A 263 1966 1073 1683 79 20 -34 A O ATOM 2094 CB GLU A 263 38.944 -27.015 52.812 1.00 11.52 A C ANISOU 2094 CB GLU A 263 1806 837 1733 77 55 -191 A C ATOM 2095 CG GLU A 263 38.826 -28.447 52.372 1.00 12.42 A C ANISOU 2095 CG GLU A 263 1984 896 1836 74 107 -310 A C ATOM 2096 CD GLU A 263 37.723 -29.124 53.133 1.00 14.44 A C ANISOU 2096 CD GLU A 263 1981 1369 2134 -3 -35 78 A C ATOM 2097 OE1 GLU A 263 36.536 -28.722 52.954 1.00 14.56 A O ANISOU 2097 OE1 GLU A 263 1912 1161 2459 -74 -51 14 A O ATOM 2098 OE2 GLU A 263 38.055 -30.117 53.869 1.00 16.51 A O ANISOU 2098 OE2 GLU A 263 2460 1274 2539 58 155 336 A O ATOM 2099 N ILE A 264 39.646 -23.862 52.118 1.00 10.10 A N ANISOU 2099 N ILE A 264 1692 990 1155 39 -13 -109 A N ATOM 2100 CA AILE A 264 39.666 -22.469 52.603 0.50 10.59 A C ANISOU 2100 CA AILE A 264 1652 908 1464 -23 138 -94 A C ATOM 2101 CA BILE A 264 39.773 -22.522 52.650 0.50 10.54 A C ANISOU 2101 CA BILE A 264 1715 821 1468 35 169 -16 A C ATOM 2102 C ILE A 264 39.182 -22.457 54.061 1.00 10.59 A C ANISOU 2102 C ILE A 264 1665 918 1440 79 130 122 A C ATOM 2103 O ILE A 264 39.842 -21.919 54.972 1.00 11.38 A O ANISOU 2103 O ILE A 264 1810 927 1584 70 166 -32 A O ATOM 2104 CB AILE A 264 38.801 -21.552 51.701 0.50 10.12 A C ANISOU 2104 CB AILE A 264 1607 524 1711 -208 117 -16 A C ATOM 2105 CB BILE A 264 39.159 -21.512 51.676 0.50 10.15 A C ANISOU 2105 CB BILE A 264 1781 647 1428 -112 103 -30 A C ATOM 2106 CG1AILE A 264 39.331 -21.450 50.262 0.50 11.25 A C ANISOU 2106 CG1AILE A 264 1683 862 1730 -146 57 -10 A C ATOM 2107 CG1BILE A 264 40.052 -21.418 50.442 0.50 10.69 A C ANISOU 2107 CG1BILE A 264 1769 810 1480 6 114 61 A C ATOM 2108 CG2AILE A 264 38.627 -20.177 52.316 0.50 9.77 A C ANISOU 2108 CG2AILE A 264 1486 542 1681 -153 26 11 A C ATOM 2109 CG2BILE A 264 38.960 -20.153 52.311 0.50 10.06 A C ANISOU 2109 CG2BILE A 264 1703 686 1434 122 138 38 A C ATOM 2110 CD1AILE A 264 40.735 -20.898 50.117 0.50 12.94 A C ANISOU 2110 CD1AILE A 264 1786 1244 1885 -242 227 19 A C ATOM 2111 CD1BILE A 264 39.443 -20.652 49.346 0.50 10.98 A C ANISOU 2111 CD1BILE A 264 1909 956 1303 -36 258 229 A C ATOM 2112 N TYR A 265 37.967 -23.005 54.275 1.00 10.11 A N ANISOU 2112 N TYR A 265 1652 770 1418 62 102 -57 A N ATOM 2113 CA TYR A 265 37.343 -22.909 55.612 1.00 11.42 A C ANISOU 2113 CA TYR A 265 1802 1058 1477 171 200 -5 A C ATOM 2114 C TYR A 265 37.872 -23.943 56.597 1.00 11.36 A C ANISOU 2114 C TYR A 265 1609 1216 1490 361 232 -34 A C ATOM 2115 O TYR A 265 38.247 -23.640 57.752 1.00 13.10 A O ANISOU 2115 O TYR A 265 2190 1064 1722 7 -64 109 A O ATOM 2116 CB TYR A 265 35.821 -23.018 55.574 1.00 11.64 A C ANISOU 2116 CB TYR A 265 1834 1036 1553 189 132 -91 A C ATOM 2117 CG TYR A 265 35.091 -21.919 54.835 1.00 11.07 A C ANISOU 2117 CG TYR A 265 1595 1050 1561 174 137 -76 A C ATOM 2118 CD1 TYR A 265 35.637 -20.654 54.586 1.00 11.25 A C ANISOU 2118 CD1 TYR A 265 1663 1132 1479 21 97 -165 A C ATOM 2119 CD2 TYR A 265 33.822 -22.174 54.359 1.00 11.17 A C ANISOU 2119 CD2 TYR A 265 1617 1071 1554 177 141 -297 A C ATOM 2120 CE1 TYR A 265 34.895 -19.696 53.905 1.00 11.61 A C ANISOU 2120 CE1 TYR A 265 1520 1276 1616 -31 -33 -49 A C ATOM 2121 CE2 TYR A 265 33.074 -21.227 53.703 1.00 10.85 A C ANISOU 2121 CE2 TYR A 265 1330 1156 1635 -125 138 -3 A C ATOM 2122 CZ TYR A 265 33.612 -19.963 53.468 1.00 10.34 A C ANISOU 2122 CZ TYR A 265 1468 1011 1449 -29 4 128 A C ATOM 2123 OH TYR A 265 32.857 -19.054 52.770 1.00 11.25 A O ANISOU 2123 OH TYR A 265 1624 984 1667 99 -198 -30 A O ATOM 2124 N ASP A 266 37.889 -25.217 56.186 1.00 12.06 A N ANISOU 2124 N ASP A 266 1893 1253 1435 267 245 -108 A N ATOM 2125 CA ASP A 266 38.152 -26.247 57.183 1.00 12.50 A C ANISOU 2125 CA ASP A 266 1800 1395 1553 -15 217 86 A C ATOM 2126 C ASP A 266 39.634 -26.482 57.489 1.00 11.18 A C ANISOU 2126 C ASP A 266 1949 984 1314 3 147 -186 A C ATOM 2127 O ASP A 266 39.946 -26.930 58.584 1.00 14.33 A O ANISOU 2127 O ASP A 266 2351 1694 1398 229 81 218 A O ATOM 2128 CB ASP A 266 37.431 -27.550 56.862 1.00 13.47 A C ANISOU 2128 CB ASP A 266 2166 1014 1937 32 269 76 A C ATOM 2129 CG ASP A 266 35.934 -27.530 57.168 1.00 15.50 A C ANISOU 2129 CG ASP A 266 2064 1751 2072 -134 30 -218 A C ATOM 2130 OD1 ASP A 266 35.459 -26.582 57.872 1.00 15.27 A O ANISOU 2130 OD1 ASP A 266 2123 1493 2183 16 167 39 A O ATOM 2131 OD2 ASP A 266 35.219 -28.451 56.657 1.00 17.60 A O ANISOU 2131 OD2 ASP A 266 2151 1760 2776 -297 207 -399 A O ATOM 2132 N GLY A 267 40.538 -26.161 56.566 1.00 11.56 A N ANISOU 2132 N GLY A 267 2005 1033 1353 96 151 217 A N ATOM 2133 CA GLY A 267 41.959 -26.303 56.763 1.00 11.60 A C ANISOU 2133 CA GLY A 267 2083 888 1434 28 -90 -7 A C ATOM 2134 C GLY A 267 42.543 -27.424 55.906 1.00 12.32 A C ANISOU 2134 C GLY A 267 1792 912 1976 -102 108 -63 A C ATOM 2135 O GLY A 267 41.940 -27.901 54.957 1.00 12.26 A O ANISOU 2135 O GLY A 267 1965 910 1781 98 -6 106 A O ATOM 2136 N GLU A 268 43.753 -27.809 56.266 1.00 11.96 A N ANISOU 2136 N GLU A 268 1880 1023 1641 133 88 119 A N ATOM 2137 CA GLU A 268 44.568 -28.734 55.472 1.00 12.73 A C ANISOU 2137 CA GLU A 268 2072 1408 1357 383 88 199 A C ATOM 2138 C GLU A 268 44.985 -29.941 56.327 1.00 12.37 A C ANISOU 2138 C GLU A 268 1828 1125 1744 441 -140 22 A C ATOM 2139 O GLU A 268 45.485 -29.765 57.456 1.00 14.23 A O ANISOU 2139 O GLU A 268 2566 1095 1744 315 -423 277 A O ATOM 2140 CB GLU A 268 45.835 -28.056 54.950 1.00 13.16 A C ANISOU 2140 CB GLU A 268 2103 1108 1787 355 191 59 A C ATOM 2141 CG GLU A 268 46.748 -29.021 54.220 1.00 12.80 A C ANISOU 2141 CG GLU A 268 2015 1423 1426 305 5 -103 A C ATOM 2142 CD GLU A 268 47.804 -28.381 53.335 1.00 14.10 A C ANISOU 2142 CD GLU A 268 2003 1330 2023 38 -70 -65 A C ATOM 2143 OE1 GLU A 268 47.427 -27.432 52.570 1.00 13.47 A O ANISOU 2143 OE1 GLU A 268 2156 1069 1891 -131 130 72 A O ATOM 2144 OE2 GLU A 268 49.006 -28.747 53.503 1.00 14.19 A O ANISOU 2144 OE2 GLU A 268 2045 1207 2139 257 123 84 A O ATOM 2145 N GLU A 269 44.814 -31.147 55.749 1.00 12.62 A N ANISOU 2145 N GLU A 269 2072 1181 1543 383 -77 0 A N ATOM 2146 CA GLU A 269 45.353 -32.418 56.277 1.00 14.40 A C ANISOU 2146 CA GLU A 269 2328 1449 1694 491 49 235 A C ATOM 2147 C GLU A 269 46.501 -32.824 55.338 1.00 13.34 A C ANISOU 2147 C GLU A 269 2233 699 2137 439 -53 38 A C ATOM 2148 O GLU A 269 46.283 -33.001 54.132 1.00 14.65 A O ANISOU 2148 O GLU A 269 2515 1122 1929 316 -29 57 A O ATOM 2149 CB GLU A 269 44.281 -33.488 56.358 1.00 14.77 A C ANISOU 2149 CB GLU A 269 2056 1689 1867 419 47 51 A C ATOM 2150 CG GLU A 269 44.845 -34.823 56.791 1.00 18.72 A C ANISOU 2150 CG GLU A 269 3394 1767 1951 774 322 62 A C ATOM 2151 CD GLU A 269 43.854 -35.959 56.961 1.00 24.70 A C ANISOU 2151 CD GLU A 269 3629 2163 3592 519 443 868 A C ATOM 2152 OE1 GLU A 269 42.640 -35.745 56.946 1.00 24.88 A O ANISOU 2152 OE1 GLU A 269 3667 2325 3457 -10 389 331 A O ATOM 2153 OE2 GLU A 269 44.333 -37.100 57.144 1.00 33.60 A O ANISOU 2153 OE2 GLU A 269 6264 1755 4745 699 2015 1373 A O ATOM 2154 N TYR A 270 47.704 -32.910 55.912 1.00 13.02 A N ANISOU 2154 N TYR A 270 2116 1120 1708 262 -107 243 A N ATOM 2155 CA TYR A 270 48.920 -33.233 55.170 1.00 13.26 A C ANISOU 2155 CA TYR A 270 2211 1166 1660 90 -64 298 A C ATOM 2156 C TYR A 270 49.542 -34.474 55.803 1.00 14.38 A C ANISOU 2156 C TYR A 270 2233 1351 1880 369 -41 225 A C ATOM 2157 O TYR A 270 49.849 -34.453 56.992 1.00 15.44 A O ANISOU 2157 O TYR A 270 2817 1088 1960 445 -275 63 A O ATOM 2158 CB TYR A 270 49.869 -32.037 55.249 1.00 14.25 A C ANISOU 2158 CB TYR A 270 1897 1358 2160 120 -89 160 A C ATOM 2159 CG TYR A 270 51.113 -32.134 54.419 1.00 12.89 A C ANISOU 2159 CG TYR A 270 2027 946 1923 131 -35 138 A C ATOM 2160 CD1 TYR A 270 52.257 -32.755 54.903 1.00 14.69 A C ANISOU 2160 CD1 TYR A 270 2319 1558 1703 374 -99 346 A C ATOM 2161 CD2 TYR A 270 51.176 -31.586 53.152 1.00 13.45 A C ANISOU 2161 CD2 TYR A 270 1908 1279 1923 332 -191 202 A C ATOM 2162 CE1 TYR A 270 53.425 -32.813 54.151 1.00 14.76 A C ANISOU 2162 CE1 TYR A 270 2096 1258 2251 674 -239 43 A C ATOM 2163 CE2 TYR A 270 52.330 -31.635 52.394 1.00 14.63 A C ANISOU 2163 CE2 TYR A 270 2235 1414 1907 388 12 227 A C ATOM 2164 CZ TYR A 270 53.468 -32.258 52.884 1.00 14.63 A C ANISOU 2164 CZ TYR A 270 2084 1370 2102 128 -276 -19 A C ATOM 2165 OH TYR A 270 54.587 -32.323 52.111 1.00 15.72 A O ANISOU 2165 OH TYR A 270 2246 1450 2277 370 -203 92 A O ATOM 2166 N ASP A 271 49.835 -35.463 54.966 1.00 14.50 A N ANISOU 2166 N ASP A 271 2460 1392 1655 540 -95 260 A N ATOM 2167 CA ASP A 271 50.492 -36.714 55.421 1.00 14.00 A C ANISOU 2167 CA ASP A 271 2279 1431 1608 529 -175 156 A C ATOM 2168 C ASP A 271 51.872 -36.762 54.785 1.00 13.91 A C ANISOU 2168 C ASP A 271 2197 1166 1922 443 -240 368 A C ATOM 2169 O ASP A 271 51.996 -37.157 53.622 1.00 14.04 A O ANISOU 2169 O ASP A 271 2126 1357 1851 333 -182 188 A O ATOM 2170 CB ASP A 271 49.661 -37.956 55.126 1.00 14.93 A C ANISOU 2170 CB ASP A 271 2403 1567 1699 453 108 164 A C ATOM 2171 CG ASP A 271 50.254 -39.225 55.707 1.00 16.03 A C ANISOU 2171 CG ASP A 271 2412 1611 2068 309 113 329 A C ATOM 2172 OD1 ASP A 271 51.430 -39.175 56.189 1.00 16.38 A O ANISOU 2172 OD1 ASP A 271 2454 1336 2433 392 2 374 A O ATOM 2173 OD2 ASP A 271 49.511 -40.254 55.667 1.00 19.69 A O ANISOU 2173 OD2 ASP A 271 3029 1528 2923 -52 -114 534 A O ATOM 2174 N SER A 272 52.902 -36.380 55.547 1.00 13.89 A N ANISOU 2174 N SER A 272 2282 1119 1876 277 -320 232 A N ATOM 2175 CA SER A 272 54.243 -36.256 54.975 1.00 15.63 A C ANISOU 2175 CA SER A 272 2228 1609 2100 802 -162 353 A C ATOM 2176 C SER A 272 54.831 -37.622 54.564 1.00 16.28 A C ANISOU 2176 C SER A 272 2260 1680 2243 608 -229 35 A C ATOM 2177 O SER A 272 55.796 -37.677 53.802 1.00 17.20 A O ANISOU 2177 O SER A 272 2408 1797 2327 543 -90 417 A O ATOM 2178 CB SER A 272 55.190 -35.542 55.934 1.00 16.84 A C ANISOU 2178 CB SER A 272 2077 2140 2180 568 -226 526 A C ATOM 2179 OG SER A 272 55.473 -36.324 57.091 1.00 16.22 A O ANISOU 2179 OG SER A 272 2541 1605 2017 490 -303 354 A O ATOM 2180 N ARG A 273 54.231 -38.717 55.037 1.00 15.20 A N ANISOU 2180 N ARG A 273 2213 1576 1986 685 -149 -181 A N ATOM 2181 CA ARG A 273 54.650 -40.039 54.641 1.00 15.79 A C ANISOU 2181 CA ARG A 273 2666 1442 1890 804 -222 -4 A C ATOM 2182 C ARG A 273 54.406 -40.278 53.147 1.00 16.98 A C ANISOU 2182 C ARG A 273 2671 1945 1833 616 -16 45 A C ATOM 2183 O ARG A 273 55.005 -41.191 52.547 1.00 18.62 A O ANISOU 2183 O ARG A 273 3009 1778 2286 756 120 139 A O ATOM 2184 CB ARG A 273 53.947 -41.124 55.468 1.00 16.28 A C ANISOU 2184 CB ARG A 273 2549 1423 2212 692 -215 -37 A C ATOM 2185 CG ARG A 273 54.283 -41.066 56.947 1.00 17.94 A C ANISOU 2185 CG ARG A 273 2901 1732 2183 527 -103 53 A C ATOM 2186 CD ARG A 273 53.409 -41.982 57.757 1.00 19.57 A C ANISOU 2186 CD ARG A 273 3048 2075 2310 454 -156 390 A C ATOM 2187 NE ARG A 273 51.996 -41.626 57.676 1.00 18.17 A N ANISOU 2187 NE ARG A 273 2866 1516 2519 182 -207 356 A N ATOM 2188 CZ ARG A 273 51.000 -42.270 58.254 1.00 18.53 A C ANISOU 2188 CZ ARG A 273 3084 1289 2665 575 104 561 A C ATOM 2189 NH1 ARG A 273 51.242 -43.375 58.962 1.00 20.32 A N ANISOU 2189 NH1 ARG A 273 3645 1296 2779 415 -7 736 A N ATOM 2190 NH2 ARG A 273 49.763 -41.850 58.053 1.00 20.71 A N ANISOU 2190 NH2 ARG A 273 2960 1775 3131 481 -143 584 A N ATOM 2191 N LEU A 274 53.512 -39.486 52.558 1.00 16.31 A N ANISOU 2191 N LEU A 274 2808 1565 1825 414 -202 71 A N ATOM 2192 CA LEU A 274 53.141 -39.641 51.148 1.00 15.70 A C ANISOU 2192 CA LEU A 274 2661 1325 1979 208 -201 -30 A C ATOM 2193 C LEU A 274 53.899 -38.681 50.224 1.00 17.03 A C ANISOU 2193 C LEU A 274 2631 1739 2098 292 -8 92 A C ATOM 2194 O LEU A 274 53.579 -38.641 49.051 1.00 20.13 A O ANISOU 2194 O LEU A 274 3369 2003 2275 -73 -119 146 A O ATOM 2195 CB LEU A 274 51.621 -39.502 51.012 1.00 17.43 A C ANISOU 2195 CB LEU A 274 2580 1624 2415 263 -363 -18 A C ATOM 2196 CG LEU A 274 50.811 -40.559 51.745 1.00 19.60 A C ANISOU 2196 CG LEU A 274 2987 2103 2355 378 47 165 A C ATOM 2197 CD1 LEU A 274 49.316 -40.317 51.628 1.00 20.80 A C ANISOU 2197 CD1 LEU A 274 2991 2415 2497 66 -68 11 A C ATOM 2198 CD2 LEU A 274 51.174 -41.946 51.219 1.00 25.26 A C ANISOU 2198 CD2 LEU A 274 3423 2225 3947 468 170 -327 A C ATOM 2199 N GLU A 275 54.933 -37.993 50.720 1.00 16.44 A N ANISOU 2199 N GLU A 275 2488 1636 2123 364 30 188 A N ATOM 2200 CA GLU A 275 55.766 -37.180 49.869 1.00 16.10 A C ANISOU 2200 CA GLU A 275 2241 1704 2171 484 -31 212 A C ATOM 2201 C GLU A 275 56.487 -38.075 48.870 1.00 17.72 A C ANISOU 2201 C GLU A 275 2850 1762 2121 698 137 290 A C ATOM 2202 O GLU A 275 57.000 -39.142 49.243 1.00 20.34 A O ANISOU 2202 O GLU A 275 3496 1784 2446 884 309 410 A O ATOM 2203 CB GLU A 275 56.789 -36.393 50.691 1.00 16.96 A C ANISOU 2203 CB GLU A 275 2269 1880 2295 363 59 80 A C ATOM 2204 CG GLU A 275 56.167 -35.253 51.472 1.00 15.98 A C ANISOU 2204 CG GLU A 275 2018 1724 2328 320 19 200 A C ATOM 2205 CD GLU A 275 57.023 -34.618 52.562 1.00 18.69 A C ANISOU 2205 CD GLU A 275 2260 2358 2482 356 -148 -245 A C ATOM 2206 OE1 GLU A 275 58.164 -35.079 52.806 1.00 21.31 A O ANISOU 2206 OE1 GLU A 275 2622 2247 3227 769 -245 31 A O ATOM 2207 OE2 GLU A 275 56.518 -33.706 53.224 1.00 18.25 A O ANISOU 2207 OE2 GLU A 275 2268 2117 2547 377 -171 -74 A O ATOM 2208 N GLN A 276 56.531 -37.643 47.618 1.00 17.44 A N ANISOU 2208 N GLN A 276 2402 1996 2227 470 -22 319 A N ATOM 2209 CA GLN A 276 57.282 -38.315 46.553 1.00 19.10 A C ANISOU 2209 CA GLN A 276 2726 1769 2761 590 116 207 A C ATOM 2210 C GLN A 276 58.476 -37.452 46.151 1.00 20.05 A C ANISOU 2210 C GLN A 276 2843 2356 2419 510 304 186 A C ATOM 2211 O GLN A 276 58.382 -36.613 45.262 1.00 19.38 A O ANISOU 2211 O GLN A 276 2849 1845 2668 519 -34 66 A O ATOM 2212 CB GLN A 276 56.362 -38.571 45.365 1.00 22.82 A C ANISOU 2212 CB GLN A 276 3636 2489 2544 -195 233 -171 A C ATOM 2213 CG GLN A 276 55.203 -39.526 45.680 1.00 25.00 A C ANISOU 2213 CG GLN A 276 3802 3620 2077 -699 -186 614 A C ATOM 2214 CD GLN A 276 54.338 -39.692 44.449 1.00 23.88 A C ANISOU 2214 CD GLN A 276 3131 3395 2544 358 -123 -510 A C ATOM 2215 NE2 GLN A 276 53.087 -39.222 44.484 1.00 25.97 A N ANISOU 2215 NE2 GLN A 276 2799 4675 2391 419 -229 1059 A N ATOM 2216 OE1 GLN A 276 54.840 -40.175 43.455 1.00 19.76 A O ANISOU 2216 OE1 GLN A 276 2826 2053 2629 326 234 -240 A O ATOM 2217 N LYS A 277 59.588 -37.619 46.855 1.00 21.55 A N ANISOU 2217 N LYS A 277 3493 2588 2105 447 -11 166 A N ATOM 2218 CA LYS A 277 60.738 -36.771 46.635 1.00 22.13 A C ANISOU 2218 CA LYS A 277 3084 2611 2713 507 -241 31 A C ATOM 2219 C LYS A 277 61.199 -36.906 45.171 1.00 20.75 A C ANISOU 2219 C LYS A 277 2993 2090 2799 554 -2 443 A C ATOM 2220 O LYS A 277 61.265 -37.990 44.623 1.00 23.18 A O ANISOU 2220 O LYS A 277 3178 2547 3081 1013 79 14 A O ATOM 2221 CB LYS A 277 61.849 -37.074 47.644 1.00 29.04 A C ANISOU 2221 CB LYS A 277 3060 4146 3826 486 -735 343 A C ATOM 2222 CG LYS A 277 62.997 -36.078 47.542 1.00 37.43 A C ANISOU 2222 CG LYS A 277 3092 6262 4864 -398 -1211 140 A C ATOM 2223 CD LYS A 277 63.819 -35.869 48.796 1.00 50.52 A C ANISOU 2223 CD LYS A 277 4550 8484 6160 -580 -2458 -1071 A C ATOM 2224 CE LYS A 277 64.640 -34.591 48.694 1.00 64.70 A C ANISOU 2224 CE LYS A 277 6134 9169 9278 -1046 -1904 -2056 A C ATOM 2225 NZ LYS A 277 65.674 -34.471 49.755 1.00 68.62 A N ANISOU 2225 NZ LYS A 277 6895 10391 8786 466 -1742 -3531 A N ATOM 2226 N GLY A 278 61.465 -35.774 44.526 1.00 19.90 A N ANISOU 2226 N GLY A 278 2804 2033 2721 250 -2 283 A N ATOM 2227 CA GLY A 278 61.948 -35.742 43.158 1.00 20.81 A C ANISOU 2227 CA GLY A 278 2678 2417 2811 236 -30 231 A C ATOM 2228 C GLY A 278 60.854 -35.607 42.101 1.00 16.67 A C ANISOU 2228 C GLY A 278 2217 1702 2415 430 279 -84 A C ATOM 2229 O GLY A 278 61.171 -35.607 40.923 1.00 17.32 A O ANISOU 2229 O GLY A 278 2318 1609 2651 588 579 172 A O ATOM 2230 N TRP A 279 59.573 -35.492 42.487 1.00 14.66 A N ANISOU 2230 N TRP A 279 2048 1485 2035 602 -1 3 A N ATOM 2231 CA TRP A 279 58.520 -35.479 41.489 1.00 14.90 A C ANISOU 2231 CA TRP A 279 2156 1414 2091 309 60 -30 A C ATOM 2232 C TRP A 279 58.603 -34.281 40.541 1.00 14.51 A C ANISOU 2232 C TRP A 279 1950 1389 2172 311 104 -29 A C ATOM 2233 O TRP A 279 58.007 -34.336 39.466 1.00 15.29 A O ANISOU 2233 O TRP A 279 2398 1160 2249 368 201 -66 A O ATOM 2234 CB TRP A 279 57.145 -35.610 42.155 1.00 13.94 A C ANISOU 2234 CB TRP A 279 1966 1294 2037 309 -166 65 A C ATOM 2235 CG TRP A 279 56.672 -34.378 42.851 1.00 15.81 A C ANISOU 2235 CG TRP A 279 2225 1711 2071 626 -213 -125 A C ATOM 2236 CD1 TRP A 279 56.955 -34.006 44.133 1.00 18.06 A C ANISOU 2236 CD1 TRP A 279 3252 1444 2165 958 -595 81 A C ATOM 2237 CD2 TRP A 279 55.801 -33.378 42.321 1.00 14.61 A C ANISOU 2237 CD2 TRP A 279 1847 1541 2162 350 12 73 A C ATOM 2238 CE2 TRP A 279 55.597 -32.440 43.352 1.00 18.64 A C ANISOU 2238 CE2 TRP A 279 3196 1691 2193 892 -373 5 A C ATOM 2239 CE3 TRP A 279 55.136 -33.210 41.110 1.00 14.73 A C ANISOU 2239 CE3 TRP A 279 2374 1012 2210 50 -66 181 A C ATOM 2240 NE1 TRP A 279 56.332 -32.822 44.436 1.00 20.44 A N ANISOU 2240 NE1 TRP A 279 3354 2071 2340 1439 -545 -281 A N ATOM 2241 CZ2 TRP A 279 54.772 -31.335 43.198 1.00 19.25 A C ANISOU 2241 CZ2 TRP A 279 3058 1968 2288 1096 -379 -174 A C ATOM 2242 CZ3 TRP A 279 54.275 -32.141 40.977 1.00 14.53 A C ANISOU 2242 CZ3 TRP A 279 2219 1254 2045 81 -270 418 A C ATOM 2243 CH2 TRP A 279 54.130 -31.200 41.990 1.00 17.09 A C ANISOU 2243 CH2 TRP A 279 2613 1680 2200 581 -259 252 A C ATOM 2244 N SER A 280 59.220 -33.171 40.967 1.00 15.11 A N ANISOU 2244 N SER A 280 2136 1857 1749 149 66 -152 A N ATOM 2245 CA SER A 280 59.375 -32.017 40.102 1.00 15.82 A C ANISOU 2245 CA SER A 280 2119 1601 2288 506 451 -125 A C ATOM 2246 C SER A 280 60.770 -31.941 39.475 1.00 14.40 A C ANISOU 2246 C SER A 280 1847 1237 2386 160 73 -149 A C ATOM 2247 O SER A 280 61.200 -30.878 39.075 1.00 14.63 A O ANISOU 2247 O SER A 280 1963 1334 2262 102 171 -78 A O ATOM 2248 CB SER A 280 59.007 -30.728 40.813 1.00 15.27 A C ANISOU 2248 CB SER A 280 1699 1687 2414 612 93 -202 A C ATOM 2249 OG SER A 280 59.956 -30.371 41.799 1.00 16.00 A O ANISOU 2249 OG SER A 280 2322 1478 2277 340 -172 -303 A O ATOM 2250 N GLN A 281 61.475 -33.086 39.401 1.00 14.81 A N ANISOU 2250 N GLN A 281 1979 1443 2201 450 171 84 A N ATOM 2251 CA GLN A 281 62.786 -33.177 38.807 1.00 15.90 A C ANISOU 2251 CA GLN A 281 2040 1696 2303 293 260 -41 A C ATOM 2252 C GLN A 281 62.836 -34.330 37.803 1.00 15.25 A C ANISOU 2252 C GLN A 281 2076 1789 1928 281 -22 26 A C ATOM 2253 O GLN A 281 62.019 -35.247 37.810 1.00 16.08 A O ANISOU 2253 O GLN A 281 2115 1702 2290 318 112 -151 A O ATOM 2254 CB GLN A 281 63.849 -33.409 39.870 1.00 15.92 A C ANISOU 2254 CB GLN A 281 2260 1699 2088 222 238 -176 A C ATOM 2255 CG GLN A 281 64.014 -32.195 40.757 1.00 21.13 A C ANISOU 2255 CG GLN A 281 2905 2095 3025 269 -264 -601 A C ATOM 2256 CD GLN A 281 64.617 -32.541 42.090 1.00 24.46 A C ANISOU 2256 CD GLN A 281 2965 2768 3559 426 -452 -137 A C ATOM 2257 NE2 GLN A 281 65.908 -32.316 42.176 1.00 29.23 A N ANISOU 2257 NE2 GLN A 281 2535 5086 3484 799 -644 -353 A N ATOM 2258 OE1 GLN A 281 63.928 -32.985 43.025 1.00 30.03 A O ANISOU 2258 OE1 GLN A 281 4081 2473 4856 47 31 334 A O ATOM 2259 N VAL A 282 63.796 -34.245 36.900 1.00 16.10 A N ANISOU 2259 N VAL A 282 1881 1917 2318 242 -4 82 A N ATOM 2260 CA VAL A 282 63.967 -35.331 35.906 1.00 18.14 A C ANISOU 2260 CA VAL A 282 2179 2380 2333 325 58 -67 A C ATOM 2261 C VAL A 282 64.483 -36.606 36.569 1.00 19.46 A C ANISOU 2261 C VAL A 282 2251 2272 2871 342 269 105 A C ATOM 2262 O VAL A 282 64.938 -36.609 37.701 1.00 20.46 A O ANISOU 2262 O VAL A 282 2639 2050 3083 786 94 -109 A O ATOM 2263 CB VAL A 282 64.866 -34.911 34.740 1.00 19.48 A C ANISOU 2263 CB VAL A 282 2962 1684 2753 549 534 196 A C ATOM 2264 CG1 VAL A 282 64.284 -33.705 34.078 1.00 20.57 A C ANISOU 2264 CG1 VAL A 282 2694 2116 3004 890 814 524 A C ATOM 2265 CG2 VAL A 282 66.302 -34.664 35.168 1.00 21.87 A C ANISOU 2265 CG2 VAL A 282 2805 2294 3211 422 453 532 A C ATOM 2266 N GLY A 283 64.344 -37.707 35.840 1.00 19.27 A N ANISOU 2266 N GLY A 283 2758 2200 2362 592 99 453 A N ATOM 2267 CA GLY A 283 64.825 -38.993 36.330 1.00 24.60 A C ANISOU 2267 CA GLY A 283 3928 2162 3257 1086 404 424 A C ATOM 2268 C GLY A 283 63.933 -39.575 37.407 1.00 24.85 A C ANISOU 2268 C GLY A 283 3029 2477 3933 905 394 725 A C ATOM 2269 O GLY A 283 64.335 -40.504 38.126 1.00 28.97 A O ANISOU 2269 O GLY A 283 3970 3194 3840 1981 1236 1146 A O ATOM 2270 N PHE A 284 62.688 -39.102 37.477 1.00 22.39 A N ANISOU 2270 N PHE A 284 3024 2433 3048 890 248 434 A N ATOM 2271 CA PHE A 284 61.747 -39.507 38.496 1.00 19.10 A C ANISOU 2271 CA PHE A 284 2599 1969 2688 808 23 -86 A C ATOM 2272 C PHE A 284 61.080 -40.826 38.125 1.00 19.90 A C ANISOU 2272 C PHE A 284 2464 2230 2864 688 134 -37 A C ATOM 2273 O PHE A 284 60.773 -41.042 36.950 1.00 23.58 A O ANISOU 2273 O PHE A 284 3238 2472 3247 895 -153 -682 A O ATOM 2274 CB PHE A 284 60.683 -38.414 38.623 1.00 18.63 A C ANISOU 2274 CB PHE A 284 2685 1675 2716 662 369 332 A C ATOM 2275 CG PHE A 284 59.595 -38.709 39.621 1.00 16.26 A C ANISOU 2275 CG PHE A 284 2350 1319 2507 686 229 -184 A C ATOM 2276 CD1 PHE A 284 59.898 -38.756 40.979 1.00 15.71 A C ANISOU 2276 CD1 PHE A 284 2505 1067 2395 631 265 -176 A C ATOM 2277 CD2 PHE A 284 58.285 -38.902 39.211 1.00 16.43 A C ANISOU 2277 CD2 PHE A 284 2714 1023 2505 689 -50 121 A C ATOM 2278 CE1 PHE A 284 58.907 -39.029 41.907 1.00 17.98 A C ANISOU 2278 CE1 PHE A 284 2801 1224 2805 548 353 -229 A C ATOM 2279 CE2 PHE A 284 57.298 -39.144 40.143 1.00 17.38 A C ANISOU 2279 CE2 PHE A 284 2868 1157 2579 692 105 -5 A C ATOM 2280 CZ PHE A 284 57.616 -39.204 41.487 1.00 17.43 A C ANISOU 2280 CZ PHE A 284 2863 1277 2483 238 46 82 A C ATOM 2281 N ASN A 285 60.775 -41.635 39.145 1.00 21.31 A N ANISOU 2281 N ASN A 285 3438 1751 2907 510 -232 -177 A N ATOM 2282 CA ASN A 285 60.006 -42.872 38.986 1.00 25.27 A C ANISOU 2282 CA ASN A 285 3852 1961 3788 234 -643 244 A C ATOM 2283 C ASN A 285 58.518 -42.518 38.972 1.00 20.96 A C ANISOU 2283 C ASN A 285 3681 1370 2910 164 -181 80 A C ATOM 2284 O ASN A 285 57.928 -42.386 40.019 1.00 25.51 A O ANISOU 2284 O ASN A 285 4750 1591 3352 82 371 358 A O ATOM 2285 CB ASN A 285 60.238 -43.867 40.140 1.00 32.31 A C ANISOU 2285 CB ASN A 285 5755 2358 4163 -35 -1356 539 A C ATOM 2286 CG ASN A 285 59.365 -45.105 40.044 1.00 36.67 A C ANISOU 2286 CG ASN A 285 6392 3242 4297 -996 -971 768 A C ATOM 2287 ND2 ASN A 285 59.246 -45.848 41.146 1.00 40.55 A N ANISOU 2287 ND2 ASN A 285 5731 4023 5650 -546 -1378 1826 A N ATOM 2288 OD1 ASN A 285 58.824 -45.406 38.972 1.00 31.07 A O ANISOU 2288 OD1 ASN A 285 5353 1572 4881 543 -1345 333 A O ATOM 2289 N SER A 286 57.918 -42.429 37.791 1.00 20.45 A N ANISOU 2289 N SER A 286 3324 1518 2926 442 -191 -41 A N ATOM 2290 CA SER A 286 56.520 -42.040 37.686 1.00 21.45 A C ANISOU 2290 CA SER A 286 3118 2414 2617 350 71 -398 A C ATOM 2291 C SER A 286 55.614 -43.264 37.523 1.00 24.59 A C ANISOU 2291 C SER A 286 3301 1473 4567 779 -154 -545 A C ATOM 2292 O SER A 286 54.478 -43.126 37.073 1.00 25.84 A O ANISOU 2292 O SER A 286 3631 1411 4775 907 -288 -927 A O ATOM 2293 CB SER A 286 56.323 -41.087 36.555 1.00 23.53 A C ANISOU 2293 CB SER A 286 2587 3091 3260 506 -36 335 A C ATOM 2294 OG SER A 286 56.503 -41.755 35.330 1.00 30.37 A O ANISOU 2294 OG SER A 286 4049 3683 3807 998 -106 -230 A O ATOM 2295 N THR A 287 56.127 -44.455 37.878 1.00 25.78 A N ANISOU 2295 N THR A 287 3060 1612 5122 857 381 -270 A N ATOM 2296 CA THR A 287 55.323 -45.628 37.991 1.00 31.28 A C ANISOU 2296 CA THR A 287 3619 2231 6033 496 624 -19 A C ATOM 2297 C THR A 287 54.170 -45.350 38.936 1.00 25.83 A C ANISOU 2297 C THR A 287 3553 1080 5182 312 460 158 A C ATOM 2298 O THR A 287 54.342 -44.769 40.045 1.00 34.24 A O ANISOU 2298 O THR A 287 4780 3885 4342 959 226 383 A O ATOM 2299 CB THR A 287 56.117 -46.830 38.512 1.00 32.67 A C ANISOU 2299 CB THR A 287 4114 882 7416 293 122 -515 A C ATOM 2300 CG2 THR A 287 55.281 -48.080 38.748 1.00 34.60 A C ANISOU 2300 CG2 THR A 287 3021 2621 7504 -71 480 231 A C ATOM 2301 OG1 THR A 287 57.083 -46.975 37.466 1.00 45.99 A O ANISOU 2301 OG1 THR A 287 5261 4553 7659 -901 1089 732 A O ATOM 2302 N GLY A 288 52.993 -45.743 38.483 1.00 26.33 A N ANISOU 2302 N GLY A 288 3886 1536 4579 975 -164 404 A N ATOM 2303 CA GLY A 288 51.826 -45.561 39.287 1.00 26.75 A C ANISOU 2303 CA GLY A 288 3687 2163 4311 742 -181 184 A C ATOM 2304 C GLY A 288 51.148 -44.228 39.061 1.00 21.89 A C ANISOU 2304 C GLY A 288 3627 1446 3242 199 33 62 A C ATOM 2305 O GLY A 288 50.021 -44.085 39.517 1.00 25.09 A O ANISOU 2305 O GLY A 288 3462 1811 4257 98 -82 674 A O ATOM 2306 N TRP A 289 51.799 -43.283 38.366 1.00 18.60 A N ANISOU 2306 N TRP A 289 2714 1544 2810 475 -21 -60 A N ATOM 2307 CA TRP A 289 51.127 -42.051 38.001 1.00 15.03 A C ANISOU 2307 CA TRP A 289 2378 1189 2144 286 52 -414 A C ATOM 2308 C TRP A 289 50.117 -42.344 36.894 1.00 15.32 A C ANISOU 2308 C TRP A 289 2555 1248 2017 560 -79 -296 A C ATOM 2309 O TRP A 289 50.276 -43.272 36.076 1.00 18.88 A O ANISOU 2309 O TRP A 289 2943 1494 2736 357 -393 -943 A O ATOM 2310 CB TRP A 289 52.113 -40.933 37.630 1.00 14.57 A C ANISOU 2310 CB TRP A 289 2088 1339 2107 420 -26 -113 A C ATOM 2311 CG TRP A 289 52.828 -40.340 38.800 1.00 14.44 A C ANISOU 2311 CG TRP A 289 2183 1182 2121 120 80 -158 A C ATOM 2312 CD1 TRP A 289 53.430 -40.988 39.828 1.00 17.27 A C ANISOU 2312 CD1 TRP A 289 2775 1240 2545 410 -276 -134 A C ATOM 2313 CD2 TRP A 289 52.951 -38.935 39.120 1.00 13.51 A C ANISOU 2313 CD2 TRP A 289 2199 1019 1915 165 3 -29 A C ATOM 2314 CE2 TRP A 289 53.643 -38.853 40.354 1.00 13.83 A C ANISOU 2314 CE2 TRP A 289 2159 1278 1815 311 16 -29 A C ATOM 2315 CE3 TRP A 289 52.530 -37.732 38.530 1.00 12.07 A C ANISOU 2315 CE3 TRP A 289 1866 1047 1674 102 -51 -117 A C ATOM 2316 NE1 TRP A 289 53.932 -40.125 40.756 1.00 15.83 A N ANISOU 2316 NE1 TRP A 289 2372 1495 2147 413 -348 131 A N ATOM 2317 CZ2 TRP A 289 53.928 -37.629 40.973 1.00 14.65 A C ANISOU 2317 CZ2 TRP A 289 1953 1414 2199 -13 135 -67 A C ATOM 2318 CZ3 TRP A 289 52.792 -36.534 39.152 1.00 14.43 A C ANISOU 2318 CZ3 TRP A 289 2113 1097 2272 57 102 -323 A C ATOM 2319 CH2 TRP A 289 53.489 -36.485 40.356 1.00 14.55 A C ANISOU 2319 CH2 TRP A 289 2049 1370 2108 90 245 -143 A C ATOM 2320 N LEU A 290 49.063 -41.558 36.898 1.00 13.31 A N ANISOU 2320 N LEU A 290 2164 799 2091 130 -10 -429 A N ATOM 2321 CA LEU A 290 47.970 -41.671 35.960 1.00 14.15 A C ANISOU 2321 CA LEU A 290 2199 1182 1992 59 -4 -151 A C ATOM 2322 C LEU A 290 48.178 -40.723 34.790 1.00 13.74 A C ANISOU 2322 C LEU A 290 1926 1163 2131 91 135 -215 A C ATOM 2323 O LEU A 290 48.976 -39.777 34.875 1.00 14.10 A O ANISOU 2323 O LEU A 290 2278 1019 2060 -14 -10 -418 A O ATOM 2324 CB LEU A 290 46.668 -41.341 36.690 1.00 16.51 A C ANISOU 2324 CB LEU A 290 2281 1794 2196 262 99 85 A C ATOM 2325 CG LEU A 290 46.370 -42.185 37.915 1.00 18.76 A C ANISOU 2325 CG LEU A 290 2942 1756 2427 298 228 257 A C ATOM 2326 CD1 LEU A 290 45.062 -41.766 38.546 1.00 24.47 A C ANISOU 2326 CD1 LEU A 290 3337 3229 2730 613 544 739 A C ATOM 2327 CD2 LEU A 290 46.351 -43.661 37.574 1.00 22.22 A C ANISOU 2327 CD2 LEU A 290 3448 1928 3065 -253 319 136 A C ATOM 2328 N GLY A 291 47.331 -40.893 33.769 1.00 13.93 A N ANISOU 2328 N GLY A 291 2164 964 2161 88 94 -64 A N ATOM 2329 CA GLY A 291 47.286 -39.934 32.697 1.00 14.90 A C ANISOU 2329 CA GLY A 291 2731 895 2035 -131 -19 -209 A C ATOM 2330 C GLY A 291 46.528 -38.665 33.061 1.00 13.54 A C ANISOU 2330 C GLY A 291 2428 924 1792 -165 57 -191 A C ATOM 2331 O GLY A 291 46.091 -38.458 34.215 1.00 12.95 A O ANISOU 2331 O GLY A 291 2019 1146 1752 -121 -37 -138 A O ATOM 2332 N THR A 292 46.373 -37.858 32.014 1.00 13.85 A N ANISOU 2332 N THR A 292 2374 1232 1656 157 178 -191 A N ATOM 2333 CA THR A 292 45.660 -36.585 32.067 1.00 12.28 A C ANISOU 2333 CA THR A 292 2003 986 1675 -136 173 -238 A C ATOM 2334 C THR A 292 44.803 -36.463 30.805 1.00 13.66 A C ANISOU 2334 C THR A 292 2238 1434 1515 260 308 137 A C ATOM 2335 O THR A 292 45.029 -37.179 29.816 1.00 15.88 A O ANISOU 2335 O THR A 292 2600 1632 1798 228 3 -201 A O ATOM 2336 CB THR A 292 46.604 -35.371 32.212 1.00 13.97 A C ANISOU 2336 CB THR A 292 2169 971 2168 -157 -59 0 A C ATOM 2337 CG2 THR A 292 47.376 -35.359 33.514 1.00 13.36 A C ANISOU 2337 CG2 THR A 292 2172 993 1909 157 79 -169 A C ATOM 2338 OG1 THR A 292 47.510 -35.332 31.099 1.00 14.62 A O ANISOU 2338 OG1 THR A 292 2454 1083 2017 -44 36 143 A O ATOM 2339 N HIS A 293 43.819 -35.557 30.859 1.00 12.65 A N ANISOU 2339 N HIS A 293 2108 1065 1631 14 -81 -155 A N ATOM 2340 CA HIS A 293 42.900 -35.309 29.729 1.00 12.56 A C ANISOU 2340 CA HIS A 293 2088 1063 1619 -77 -16 18 A C ATOM 2341 C HIS A 293 42.542 -33.824 29.697 1.00 13.16 A C ANISOU 2341 C HIS A 293 2234 1090 1677 -126 -196 -151 A C ATOM 2342 O HIS A 293 42.756 -33.157 30.706 1.00 13.31 A O ANISOU 2342 O HIS A 293 2124 1234 1697 -325 -92 -86 A O ATOM 2343 CB HIS A 293 41.676 -36.241 29.821 1.00 13.16 A C ANISOU 2343 CB HIS A 293 2096 1031 1873 -157 -338 134 A C ATOM 2344 CG HIS A 293 40.876 -36.068 31.059 1.00 14.34 A C ANISOU 2344 CG HIS A 293 2094 1033 2321 -307 124 90 A C ATOM 2345 CD2 HIS A 293 39.914 -35.170 31.385 1.00 15.20 A C ANISOU 2345 CD2 HIS A 293 2147 1044 2582 -27 -175 -108 A C ATOM 2346 ND1 HIS A 293 40.999 -36.910 32.141 1.00 16.73 A N ANISOU 2346 ND1 HIS A 293 2619 1440 2295 -246 13 93 A N ATOM 2347 CE1 HIS A 293 40.170 -36.525 33.091 1.00 17.29 A C ANISOU 2347 CE1 HIS A 293 2403 1649 2517 -30 199 256 A C ATOM 2348 NE2 HIS A 293 39.490 -35.462 32.652 1.00 16.51 A N ANISOU 2348 NE2 HIS A 293 2397 1270 2604 -199 -202 -87 A N ATOM 2349 N GLU A 294 41.961 -33.366 28.586 1.00 12.92 A N ANISOU 2349 N GLU A 294 2236 779 1894 -156 -208 -130 A N ATOM 2350 CA GLU A 294 41.609 -31.971 28.408 1.00 13.37 A C ANISOU 2350 CA GLU A 294 2244 739 2094 -209 -14 -102 A C ATOM 2351 C GLU A 294 40.234 -31.677 29.021 1.00 13.80 A C ANISOU 2351 C GLU A 294 2078 1392 1774 -462 -180 -94 A C ATOM 2352 O GLU A 294 39.316 -32.541 28.942 1.00 15.32 A O ANISOU 2352 O GLU A 294 2100 1600 2121 -456 -152 -33 A O ATOM 2353 CB GLU A 294 41.646 -31.587 26.928 1.00 13.85 A C ANISOU 2353 CB GLU A 294 2412 1142 1706 -156 -258 -339 A C ATOM 2354 CG GLU A 294 41.479 -30.099 26.697 1.00 18.64 A C ANISOU 2354 CG GLU A 294 2899 1439 2744 244 55 -10 A C ATOM 2355 CD GLU A 294 41.140 -29.669 25.285 1.00 27.43 A C ANISOU 2355 CD GLU A 294 3703 3880 2838 546 -997 -152 A C ATOM 2356 OE1 GLU A 294 41.157 -30.516 24.419 1.00 37.24 A O ANISOU 2356 OE1 GLU A 294 6308 5381 2460 2106 -429 -421 A O ATOM 2357 OE2 GLU A 294 40.847 -28.459 25.096 1.00 29.85 A O ANISOU 2357 OE2 GLU A 294 3606 4187 3547 -338 -402 714 A O ATOM 2358 N LEU A 295 40.069 -30.490 29.590 1.00 13.63 A N ANISOU 2358 N LEU A 295 1758 1293 2126 -266 -240 -107 A N ATOM 2359 CA LEU A 295 38.777 -29.948 30.062 1.00 14.20 A C ANISOU 2359 CA LEU A 295 1731 1490 2174 -494 -115 220 A C ATOM 2360 C LEU A 295 38.391 -28.786 29.146 1.00 15.20 A C ANISOU 2360 C LEU A 295 2037 1084 2653 -186 -282 78 A C ATOM 2361 O LEU A 295 39.195 -27.872 28.973 1.00 16.44 A O ANISOU 2361 O LEU A 295 1873 1547 2823 -358 -376 398 A O ATOM 2362 CB LEU A 295 38.967 -29.397 31.481 1.00 17.01 A C ANISOU 2362 CB LEU A 295 2205 1899 2356 -71 -91 -203 A C ATOM 2363 CG LEU A 295 39.176 -30.419 32.566 1.00 16.07 A C ANISOU 2363 CG LEU A 295 2258 1824 2024 -77 97 -34 A C ATOM 2364 CD1 LEU A 295 39.013 -29.767 33.937 1.00 16.94 A C ANISOU 2364 CD1 LEU A 295 2169 1860 2405 -97 347 -106 A C ATOM 2365 CD2 LEU A 295 38.222 -31.567 32.403 1.00 18.26 A C ANISOU 2365 CD2 LEU A 295 2483 1416 3039 -197 -62 -54 A C ATOM 2366 N SER A 296 37.160 -28.803 28.624 1.00 15.32 A N ANISOU 2366 N SER A 296 2117 1174 2530 -377 -320 19 A N ATOM 2367 CA SER A 296 36.678 -27.679 27.808 1.00 15.54 A C ANISOU 2367 CA SER A 296 2104 1428 2373 -191 -54 180 A C ATOM 2368 C SER A 296 36.729 -26.377 28.613 1.00 14.77 A C ANISOU 2368 C SER A 296 1685 1628 2297 -445 -138 71 A C ATOM 2369 O SER A 296 36.289 -26.323 29.753 1.00 15.96 A O ANISOU 2369 O SER A 296 2483 1313 2267 -176 -220 292 A O ATOM 2370 CB SER A 296 35.292 -27.968 27.333 1.00 18.20 A C ANISOU 2370 CB SER A 296 2363 2192 2359 -393 -487 241 A C ATOM 2371 OG SER A 296 34.764 -26.902 26.585 1.00 22.61 A O ANISOU 2371 OG SER A 296 2961 2386 3241 -72 -513 291 A O ATOM 2372 N PHE A 297 37.304 -25.330 28.003 1.00 14.21 A N ANISOU 2372 N PHE A 297 1960 1383 2055 -327 -163 -16 A N ATOM 2373 CA PHE A 297 37.491 -24.046 28.730 1.00 13.82 A C ANISOU 2373 CA PHE A 297 1801 1262 2187 -306 -67 3 A C ATOM 2374 C PHE A 297 37.630 -22.890 27.747 1.00 14.94 A C ANISOU 2374 C PHE A 297 2037 1440 2199 133 -21 225 A C ATOM 2375 O PHE A 297 38.464 -22.951 26.839 1.00 15.92 A O ANISOU 2375 O PHE A 297 2564 1251 2232 -127 61 -123 A O ATOM 2376 CB PHE A 297 38.749 -24.108 29.596 1.00 13.06 A C ANISOU 2376 CB PHE A 297 1753 1182 2027 -4 -9 -177 A C ATOM 2377 CG PHE A 297 38.966 -22.854 30.392 1.00 13.08 A C ANISOU 2377 CG PHE A 297 1695 1133 2139 121 67 -197 A C ATOM 2378 CD1 PHE A 297 38.349 -22.724 31.618 1.00 15.03 A C ANISOU 2378 CD1 PHE A 297 2430 1173 2108 99 139 -146 A C ATOM 2379 CD2 PHE A 297 39.815 -21.854 29.950 1.00 15.17 A C ANISOU 2379 CD2 PHE A 297 2409 1340 2013 -146 -169 148 A C ATOM 2380 CE1 PHE A 297 38.555 -21.613 32.399 1.00 18.13 A C ANISOU 2380 CE1 PHE A 297 2834 1762 2293 -136 351 -640 A C ATOM 2381 CE2 PHE A 297 40.010 -20.733 30.730 1.00 17.52 A C ANISOU 2381 CE2 PHE A 297 2617 1543 2496 -228 -236 -179 A C ATOM 2382 CZ PHE A 297 39.373 -20.614 31.937 1.00 18.25 A C ANISOU 2382 CZ PHE A 297 2559 1617 2757 -137 -251 -498 A C ATOM 2383 N PRO A 298 36.832 -21.811 27.899 1.00 14.64 A N ANISOU 2383 N PRO A 298 1781 1504 2275 -55 108 287 A N ATOM 2384 CA PRO A 298 36.969 -20.667 26.999 1.00 14.78 A C ANISOU 2384 CA PRO A 298 2021 1287 2307 -321 -12 166 A C ATOM 2385 C PRO A 298 38.079 -19.687 27.381 1.00 13.52 A C ANISOU 2385 C PRO A 298 2042 1028 2064 -144 17 -15 A C ATOM 2386 O PRO A 298 37.946 -18.956 28.388 1.00 13.32 A O ANISOU 2386 O PRO A 298 1900 1480 1679 -13 77 -1 A O ATOM 2387 CB PRO A 298 35.583 -20.020 27.065 1.00 17.00 A C ANISOU 2387 CB PRO A 298 2231 1683 2544 -8 -244 178 A C ATOM 2388 CG PRO A 298 35.029 -20.394 28.400 1.00 20.89 A C ANISOU 2388 CG PRO A 298 2659 2169 3108 790 472 395 A C ATOM 2389 CD PRO A 298 35.700 -21.676 28.827 1.00 14.83 A C ANISOU 2389 CD PRO A 298 2204 1419 2009 31 187 203 A C ATOM 2390 N LYS A 299 39.150 -19.669 26.577 1.00 14.20 A N ANISOU 2390 N LYS A 299 2003 1365 2027 -210 3 -222 A N ATOM 2391 CA LYS A 299 40.349 -18.823 26.847 1.00 13.75 A C ANISOU 2391 CA LYS A 299 2087 1320 1816 -353 109 -74 A C ATOM 2392 C LYS A 299 40.039 -17.327 26.732 1.00 13.36 A C ANISOU 2392 C LYS A 299 1699 1616 1760 -345 338 288 A C ATOM 2393 O LYS A 299 40.903 -16.534 27.071 1.00 15.17 A O ANISOU 2393 O LYS A 299 2199 1424 2142 -197 -37 -39 A O ATOM 2394 CB LYS A 299 41.490 -19.193 25.893 1.00 13.99 A C ANISOU 2394 CB LYS A 299 2332 1002 1981 -226 337 -50 A C ATOM 2395 CG LYS A 299 42.129 -20.546 26.172 1.00 16.01 A C ANISOU 2395 CG LYS A 299 2393 946 2744 -147 64 -20 A C ATOM 2396 CD LYS A 299 43.385 -20.749 25.374 1.00 21.40 A C ANISOU 2396 CD LYS A 299 2349 1991 3791 -175 616 178 A C ATOM 2397 CE LYS A 299 44.092 -22.034 25.681 1.00 19.77 A C ANISOU 2397 CE LYS A 299 2347 1740 3422 -73 215 157 A C ATOM 2398 NZ LYS A 299 43.332 -23.192 25.163 1.00 20.81 A N ANISOU 2398 NZ LYS A 299 2707 2088 3112 -186 -449 118 A N ATOM 2399 N GLU A 300 38.816 -16.965 26.305 1.00 13.88 A N ANISOU 2399 N GLU A 300 2214 1227 1831 -48 48 -231 A N ATOM 2400 CA GLU A 300 38.414 -15.551 26.204 1.00 14.13 A C ANISOU 2400 CA GLU A 300 2250 1452 1666 -84 -43 -28 A C ATOM 2401 C GLU A 300 38.290 -14.919 27.592 1.00 13.75 A C ANISOU 2401 C GLU A 300 2447 1208 1569 11 -176 35 A C ATOM 2402 O GLU A 300 38.353 -13.702 27.687 1.00 15.49 A O ANISOU 2402 O GLU A 300 2740 1090 2054 26 -102 -197 A O ATOM 2403 CB GLU A 300 37.093 -15.405 25.424 1.00 18.29 A C ANISOU 2403 CB GLU A 300 3047 1689 2214 519 -715 124 A C ATOM 2404 CG GLU A 300 37.268 -15.695 23.943 1.00 24.23 A C ANISOU 2404 CG GLU A 300 3524 3132 2550 380 -421 -27 A C ATOM 2405 CD GLU A 300 37.292 -17.164 23.525 1.00 28.79 A C ANISOU 2405 CD GLU A 300 5093 3054 2792 70 -1 361 A C ATOM 2406 OE1 GLU A 300 36.991 -18.081 24.389 1.00 24.02 A O ANISOU 2406 OE1 GLU A 300 3611 3008 2506 -847 -1163 533 A O ATOM 2407 OE2 GLU A 300 37.608 -17.407 22.323 1.00 34.95 A O ANISOU 2407 OE2 GLU A 300 5253 5083 2943 -380 -65 -738 A O ATOM 2408 N ARG A 301 38.127 -15.725 28.660 1.00 13.04 A N ANISOU 2408 N ARG A 301 2070 1016 1868 20 -66 14 A N ATOM 2409 CA ARG A 301 37.981 -15.149 30.002 1.00 13.39 A C ANISOU 2409 CA ARG A 301 1858 1673 1555 172 -195 80 A C ATOM 2410 C ARG A 301 39.336 -14.828 30.640 1.00 11.62 A C ANISOU 2410 C ARG A 301 1740 1420 1254 125 -146 401 A C ATOM 2411 O ARG A 301 39.353 -14.179 31.711 1.00 13.36 A O ANISOU 2411 O ARG A 301 2117 1321 1635 29 123 -37 A O ATOM 2412 CB ARG A 301 37.186 -16.047 30.948 1.00 17.67 A C ANISOU 2412 CB ARG A 301 2456 2449 1808 -226 -95 9 A C ATOM 2413 CG ARG A 301 36.212 -17.002 30.292 1.00 16.75 A C ANISOU 2413 CG ARG A 301 2433 1244 2685 195 102 -2 A C ATOM 2414 CD ARG A 301 35.912 -18.166 31.222 1.00 18.92 A C ANISOU 2414 CD ARG A 301 2494 2369 2323 -258 402 -32 A C ATOM 2415 NE ARG A 301 34.515 -18.590 31.137 1.00 18.42 A N ANISOU 2415 NE ARG A 301 2626 1625 2746 -19 526 122 A N ATOM 2416 CZ ARG A 301 34.031 -19.709 31.633 1.00 18.33 A C ANISOU 2416 CZ ARG A 301 2194 2040 2729 -161 -153 9 A C ATOM 2417 NH1 ARG A 301 34.801 -20.494 32.375 1.00 17.31 A N ANISOU 2417 NH1 ARG A 301 2539 1636 2400 -321 -241 -150 A N ATOM 2418 NH2 ARG A 301 32.782 -20.084 31.387 1.00 22.67 A N ANISOU 2418 NH2 ARG A 301 2392 2816 3404 -436 -60 -133 A N ATOM 2419 N LEU A 302 40.436 -15.293 30.033 1.00 11.43 A N ANISOU 2419 N LEU A 302 1706 908 1726 -6 -31 16 A N ATOM 2420 CA LEU A 302 41.731 -15.146 30.683 1.00 11.57 A C ANISOU 2420 CA LEU A 302 1889 1140 1365 -198 -140 -133 A C ATOM 2421 C LEU A 302 42.183 -13.675 30.685 1.00 12.64 A C ANISOU 2421 C LEU A 302 2027 1170 1605 -296 -74 74 A C ATOM 2422 O LEU A 302 42.087 -13.013 29.652 1.00 16.86 A O ANISOU 2422 O LEU A 302 3153 1347 1904 -565 -419 93 A O ATOM 2423 CB LEU A 302 42.770 -16.065 30.037 1.00 11.96 A C ANISOU 2423 CB LEU A 302 1931 1135 1477 -351 20 75 A C ATOM 2424 CG LEU A 302 42.511 -17.555 30.239 1.00 12.55 A C ANISOU 2424 CG LEU A 302 1893 982 1890 -278 -15 -213 A C ATOM 2425 CD1 LEU A 302 43.328 -18.368 29.277 1.00 13.08 A C ANISOU 2425 CD1 LEU A 302 1818 1290 1859 84 -63 -22 A C ATOM 2426 CD2 LEU A 302 42.737 -17.979 31.669 1.00 13.06 A C ANISOU 2426 CD2 LEU A 302 1825 1123 2011 -182 -39 -79 A C ATOM 2427 N ALA A 303 42.667 -13.227 31.852 1.00 9.82 A N ANISOU 2427 N ALA A 303 1493 577 1658 -147 2 129 A N ATOM 2428 CA ALA A 303 43.057 -11.840 32.023 1.00 10.00 A C ANISOU 2428 CA ALA A 303 1641 559 1598 -97 -141 62 A C ATOM 2429 C ALA A 303 44.340 -11.755 32.853 1.00 10.67 A C ANISOU 2429 C ALA A 303 1400 1165 1489 -172 126 -205 A C ATOM 2430 O ALA A 303 44.555 -12.505 33.803 1.00 12.06 A O ANISOU 2430 O ALA A 303 1533 1074 1974 6 110 8 A O ATOM 2431 CB ALA A 303 41.970 -11.061 32.730 1.00 12.65 A C ANISOU 2431 CB ALA A 303 1754 1307 1743 -1 -99 -188 A C ATOM 2432 N SER A 304 45.151 -10.719 32.568 1.00 10.78 A N ANISOU 2432 N SER A 304 1652 968 1476 -150 -35 115 A N ATOM 2433 CA SER A 304 46.248 -10.337 33.433 1.00 10.41 A C ANISOU 2433 CA SER A 304 1658 937 1357 -119 45 38 A C ATOM 2434 C SER A 304 45.682 -9.684 34.695 1.00 10.11 A C ANISOU 2434 C SER A 304 1374 1084 1381 -156 69 -31 A C ATOM 2435 O SER A 304 44.683 -8.964 34.624 1.00 11.57 A O ANISOU 2435 O SER A 304 1565 1135 1696 -16 -87 -35 A O ATOM 2436 CB SER A 304 47.139 -9.335 32.727 1.00 11.54 A C ANISOU 2436 CB SER A 304 1534 1222 1625 -315 96 -15 A C ATOM 2437 OG SER A 304 47.725 -9.924 31.578 1.00 15.25 A O ANISOU 2437 OG SER A 304 2117 1616 2060 -261 430 -309 A O ATOM 2438 N PRO A 305 46.325 -9.846 35.851 1.00 9.68 A N ANISOU 2438 N PRO A 305 1546 713 1419 -44 34 -82 A N ATOM 2439 CA PRO A 305 45.984 -9.061 37.038 1.00 10.04 A C ANISOU 2439 CA PRO A 305 1563 895 1354 -302 183 -117 A C ATOM 2440 C PRO A 305 46.129 -7.560 36.795 1.00 10.51 A C ANISOU 2440 C PRO A 305 1549 860 1583 51 95 -82 A C ATOM 2441 O PRO A 305 47.069 -7.148 36.095 1.00 12.53 A O ANISOU 2441 O PRO A 305 1712 775 2271 55 413 -146 A O ATOM 2442 CB PRO A 305 46.973 -9.522 38.085 1.00 10.95 A C ANISOU 2442 CB PRO A 305 1934 653 1573 -211 53 -141 A C ATOM 2443 CG PRO A 305 47.395 -10.893 37.646 1.00 12.27 A C ANISOU 2443 CG PRO A 305 1971 789 1902 136 -3 -102 A C ATOM 2444 CD PRO A 305 47.397 -10.816 36.138 1.00 11.30 A C ANISOU 2444 CD PRO A 305 1611 826 1854 65 -86 -251 A C ATOM 2445 N ASP A 306 45.264 -6.783 37.449 1.00 9.54 A N ANISOU 2445 N ASP A 306 1303 657 1663 -202 177 33 A N ATOM 2446 CA ASP A 306 45.407 -5.333 37.507 1.00 9.29 A C ANISOU 2446 CA ASP A 306 1444 633 1449 -180 170 108 A C ATOM 2447 C ASP A 306 46.223 -4.917 38.710 1.00 10.24 A C ANISOU 2447 C ASP A 306 1444 905 1541 25 135 -88 A C ATOM 2448 O ASP A 306 46.731 -3.767 38.715 1.00 12.27 A O ANISOU 2448 O ASP A 306 1803 901 1956 -123 136 -150 A O ATOM 2449 CB ASP A 306 44.042 -4.681 37.526 1.00 9.97 A C ANISOU 2449 CB ASP A 306 1402 910 1475 -149 137 47 A C ATOM 2450 CG ASP A 306 43.227 -4.987 36.286 1.00 11.85 A C ANISOU 2450 CG ASP A 306 1585 1245 1669 19 79 -280 A C ATOM 2451 OD1 ASP A 306 43.671 -4.607 35.188 1.00 14.13 A O ANISOU 2451 OD1 ASP A 306 2348 1214 1807 -105 -5 135 A O ATOM 2452 OD2 ASP A 306 42.183 -5.683 36.402 1.00 14.29 A O ANISOU 2452 OD2 ASP A 306 1717 1674 2039 -306 70 -227 A O ATOM 2453 N GLY A 307 46.266 -5.731 39.753 1.00 11.55 A N ANISOU 2453 N GLY A 307 1586 1033 1769 54 -137 59 A N ATOM 2454 CA GLY A 307 46.915 -5.416 40.971 1.00 11.68 A C ANISOU 2454 CA GLY A 307 1657 985 1795 245 -117 170 A C ATOM 2455 C GLY A 307 47.886 -6.493 41.414 1.00 11.23 A C ANISOU 2455 C GLY A 307 1584 989 1694 288 -94 -65 A C ATOM 2456 O GLY A 307 48.219 -7.365 40.651 1.00 11.75 A O ANISOU 2456 O GLY A 307 1533 1139 1791 231 -103 -187 A O ATOM 2457 N PRO A 308 48.357 -6.407 42.660 1.00 12.34 A N ANISOU 2457 N PRO A 308 1857 950 1879 398 -290 -359 A N ATOM 2458 CA PRO A 308 49.424 -7.272 43.115 1.00 12.33 A C ANISOU 2458 CA PRO A 308 1829 1085 1769 200 -316 49 A C ATOM 2459 C PRO A 308 48.854 -8.594 43.585 1.00 12.38 A C ANISOU 2459 C PRO A 308 1681 1183 1837 161 -142 -32 A C ATOM 2460 O PRO A 308 47.666 -8.715 43.860 1.00 14.03 A O ANISOU 2460 O PRO A 308 1772 1536 2020 325 212 241 A O ATOM 2461 CB PRO A 308 50.002 -6.499 44.304 1.00 16.58 A C ANISOU 2461 CB PRO A 308 3025 1478 1797 760 -507 -414 A C ATOM 2462 CG PRO A 308 48.810 -5.771 44.864 1.00 18.74 A C ANISOU 2462 CG PRO A 308 3235 2082 1802 1025 -620 -862 A C ATOM 2463 CD PRO A 308 47.937 -5.409 43.672 1.00 18.34 A C ANISOU 2463 CD PRO A 308 3292 1681 1993 971 -668 -802 A C ATOM 2464 N PRO A 309 49.721 -9.618 43.664 1.00 11.55 A N ANISOU 2464 N PRO A 309 1613 1024 1750 136 -57 218 A N ATOM 2465 CA PRO A 309 49.304 -10.939 44.113 1.00 11.14 A C ANISOU 2465 CA PRO A 309 1656 995 1581 127 8 52 A C ATOM 2466 C PRO A 309 49.218 -11.026 45.629 1.00 10.74 A C ANISOU 2466 C PRO A 309 1511 1038 1530 -119 42 -59 A C ATOM 2467 O PRO A 309 49.684 -10.165 46.360 1.00 11.26 A O ANISOU 2467 O PRO A 309 1836 1019 1421 93 -84 -185 A O ATOM 2468 CB PRO A 309 50.445 -11.839 43.600 1.00 12.13 A C ANISOU 2468 CB PRO A 309 1617 1299 1691 32 196 -281 A C ATOM 2469 CG PRO A 309 51.649 -10.967 43.681 1.00 10.82 A C ANISOU 2469 CG PRO A 309 1456 896 1758 295 146 -83 A C ATOM 2470 CD PRO A 309 51.145 -9.585 43.326 1.00 11.61 A C ANISOU 2470 CD PRO A 309 1736 849 1825 92 -158 16 A C ATOM 2471 N VAL A 310 48.660 -12.146 46.079 1.00 11.09 A N ANISOU 2471 N VAL A 310 1733 933 1547 -171 4 -105 A N ATOM 2472 CA VAL A 310 48.726 -12.532 47.493 1.00 10.34 A C ANISOU 2472 CA VAL A 310 1551 814 1563 85 -120 -123 A C ATOM 2473 C VAL A 310 50.117 -13.122 47.728 1.00 9.74 A C ANISOU 2473 C VAL A 310 1492 901 1305 29 -15 -36 A C ATOM 2474 O VAL A 310 50.573 -13.986 46.953 1.00 11.74 A O ANISOU 2474 O VAL A 310 1836 868 1755 224 -141 -308 A O ATOM 2475 CB VAL A 310 47.593 -13.505 47.872 1.00 12.01 A C ANISOU 2475 CB VAL A 310 1720 883 1957 67 36 -108 A C ATOM 2476 CG1 VAL A 310 47.701 -13.938 49.329 1.00 12.28 A C ANISOU 2476 CG1 VAL A 310 1894 731 2041 340 116 -66 A C ATOM 2477 CG2 VAL A 310 46.228 -12.844 47.611 1.00 12.28 A C ANISOU 2477 CG2 VAL A 310 1723 1224 1716 124 -136 122 A C ATOM 2478 N ARG A 311 50.780 -12.678 48.793 1.00 10.16 A N ANISOU 2478 N ARG A 311 1644 898 1316 352 -113 -214 A N ATOM 2479 CA ARG A 311 52.095 -13.145 49.169 1.00 11.91 A C ANISOU 2479 CA ARG A 311 1611 1141 1770 212 -115 62 A C ATOM 2480 C ARG A 311 52.139 -13.395 50.670 1.00 11.59 A C ANISOU 2480 C ARG A 311 1521 1164 1715 122 -146 -203 A C ATOM 2481 O ARG A 311 51.296 -12.935 51.441 1.00 11.30 A O ANISOU 2481 O ARG A 311 1528 1185 1580 156 -105 -35 A O ATOM 2482 CB ARG A 311 53.178 -12.130 48.824 1.00 11.84 A C ANISOU 2482 CB ARG A 311 1339 1388 1769 181 -175 -154 A C ATOM 2483 CG ARG A 311 53.379 -11.921 47.330 1.00 11.57 A C ANISOU 2483 CG ARG A 311 1703 894 1797 259 -86 -250 A C ATOM 2484 CD ARG A 311 54.773 -11.373 47.015 1.00 14.45 A C ANISOU 2484 CD ARG A 311 1998 1440 2049 -20 124 -72 A C ATOM 2485 NE ARG A 311 55.027 -11.157 45.607 1.00 14.53 A N ANISOU 2485 NE ARG A 311 2040 1388 2094 28 93 97 A N ATOM 2486 CZ ARG A 311 54.774 -10.038 44.929 1.00 14.84 A C ANISOU 2486 CZ ARG A 311 1908 1615 2115 214 41 110 A C ATOM 2487 NH1 ARG A 311 54.310 -8.960 45.560 1.00 14.76 A N ANISOU 2487 NH1 ARG A 311 1578 1525 2504 -72 -124 -211 A N ATOM 2488 NH2 ARG A 311 55.010 -10.025 43.617 1.00 15.74 A N ANISOU 2488 NH2 ARG A 311 2089 1671 2218 30 479 -97 A N ATOM 2489 N ARG A 312 53.189 -14.145 51.043 1.00 12.20 A N ANISOU 2489 N ARG A 312 1558 1372 1702 372 120 -43 A N ATOM 2490 CA ARG A 312 53.644 -14.223 52.394 1.00 12.96 A C ANISOU 2490 CA ARG A 312 1729 1331 1863 167 -131 172 A C ATOM 2491 C ARG A 312 54.404 -12.924 52.669 1.00 13.14 A C ANISOU 2491 C ARG A 312 1858 1691 1443 -112 -38 66 A C ATOM 2492 O ARG A 312 55.554 -12.774 52.280 1.00 13.85 A O ANISOU 2492 O ARG A 312 1676 1575 2008 87 -197 -159 A O ATOM 2493 CB ARG A 312 54.540 -15.448 52.585 1.00 12.90 A C ANISOU 2493 CB ARG A 312 1740 1373 1788 173 -86 145 A C ATOM 2494 CG ARG A 312 53.905 -16.788 52.213 1.00 13.47 A C ANISOU 2494 CG ARG A 312 2046 1298 1772 249 -283 -20 A C ATOM 2495 CD ARG A 312 54.941 -17.865 51.894 1.00 15.05 A C ANISOU 2495 CD ARG A 312 2219 1498 1998 346 -114 148 A C ATOM 2496 NE ARG A 312 55.656 -18.357 53.075 1.00 16.35 A N ANISOU 2496 NE ARG A 312 2272 1723 2217 355 -337 255 A N ATOM 2497 CZ ARG A 312 56.902 -18.020 53.429 1.00 16.60 A C ANISOU 2497 CZ ARG A 312 2259 1806 2240 439 -267 376 A C ATOM 2498 NH1 ARG A 312 57.599 -17.131 52.699 1.00 19.46 A N ANISOU 2498 NH1 ARG A 312 2700 1720 2970 311 21 445 A N ATOM 2499 NH2 ARG A 312 57.437 -18.587 54.512 1.00 17.97 A N ANISOU 2499 NH2 ARG A 312 2310 2230 2286 397 -664 256 A N ATOM 2500 N VAL A 313 53.701 -11.967 53.270 1.00 13.46 A N ANISOU 2500 N VAL A 313 1556 1766 1790 -113 -86 113 A N ATOM 2501 CA VAL A 313 54.216 -10.609 53.350 1.00 13.67 A C ANISOU 2501 CA VAL A 313 1620 1717 1854 -113 -37 93 A C ATOM 2502 C VAL A 313 55.184 -10.458 54.524 1.00 13.84 A C ANISOU 2502 C VAL A 313 1568 1840 1847 20 -44 109 A C ATOM 2503 O VAL A 313 56.158 -9.682 54.422 1.00 16.41 A O ANISOU 2503 O VAL A 313 1925 1875 2434 -133 -203 177 A O ATOM 2504 CB VAL A 313 53.057 -9.598 53.402 1.00 15.00 A C ANISOU 2504 CB VAL A 313 2157 1359 2184 121 -263 -94 A C ATOM 2505 CG1 VAL A 313 53.508 -8.182 53.600 1.00 17.87 A C ANISOU 2505 CG1 VAL A 313 2631 1669 2487 -158 133 -152 A C ATOM 2506 CG2 VAL A 313 52.280 -9.670 52.112 1.00 15.04 A C ANISOU 2506 CG2 VAL A 313 2359 1148 2205 285 -183 36 A C ATOM 2507 N ALA A 314 54.929 -11.159 55.636 1.00 13.96 A N ANISOU 2507 N ALA A 314 1922 1694 1687 28 -194 -41 A N ATOM 2508 CA ALA A 314 55.741 -11.035 56.837 1.00 14.91 A C ANISOU 2508 CA ALA A 314 1764 1786 2114 -87 -385 -135 A C ATOM 2509 C ALA A 314 55.634 -12.306 57.674 1.00 16.36 A C ANISOU 2509 C ALA A 314 1840 2187 2188 -143 -437 -2 A C ATOM 2510 O ALA A 314 54.721 -13.067 57.533 1.00 16.96 A O ANISOU 2510 O ALA A 314 1803 2037 2603 -49 -742 -28 A O ATOM 2511 CB ALA A 314 55.290 -9.835 57.646 1.00 17.01 A C ANISOU 2511 CB ALA A 314 2460 1616 2386 -290 -403 -126 A C ATOM 2512 N GLU A 315 56.598 -12.448 58.569 1.00 18.12 A N ANISOU 2512 N GLU A 315 2102 2557 2225 -175 -679 -147 A N ATOM 2513 CA AGLU A 315 56.568 -13.338 59.687 0.70 19.70 A C ANISOU 2513 CA AGLU A 315 2497 2554 2433 -123 -569 -196 A C ATOM 2514 CA BGLU A 315 56.521 -13.373 59.687 0.30 19.08 A C ANISOU 2514 CA BGLU A 315 2525 2386 2339 59 -673 -191 A C ATOM 2515 C GLU A 315 56.005 -12.598 60.904 1.00 18.21 A C ANISOU 2515 C GLU A 315 2420 2036 2459 122 -354 45 A C ATOM 2516 O GLU A 315 56.253 -11.377 61.055 1.00 20.64 A O ANISOU 2516 O GLU A 315 3591 2204 2047 -300 -231 -115 A O ATOM 2517 CB AGLU A 315 58.010 -13.753 59.986 0.70 25.56 A C ANISOU 2517 CB AGLU A 315 2859 3455 3396 901 -268 384 A C ATOM 2518 CB BGLU A 315 57.888 -13.998 60.000 0.30 21.36 A C ANISOU 2518 CB BGLU A 315 2941 2626 2547 622 -644 -54 A C ATOM 2519 CG AGLU A 315 58.090 -14.820 61.024 0.70 27.86 A C ANISOU 2519 CG AGLU A 315 2706 4044 3835 593 -215 765 A C ATOM 2520 CG BGLU A 315 58.403 -14.958 58.937 0.30 24.35 A C ANISOU 2520 CG BGLU A 315 3323 3393 2535 498 -890 -647 A C ATOM 2521 CD AGLU A 315 59.474 -15.351 61.365 0.70 30.16 A C ANISOU 2521 CD AGLU A 315 2549 4793 4118 366 -813 580 A C ATOM 2522 CD BGLU A 315 59.917 -15.133 58.905 0.30 26.84 A C ANISOU 2522 CD BGLU A 315 3389 3807 3002 590 -837 -763 A C ATOM 2523 OE1AGLU A 315 60.419 -15.121 60.586 0.70 35.57 A O ANISOU 2523 OE1AGLU A 315 3117 5538 4858 1358 31 1502 A O ATOM 2524 OE1BGLU A 315 60.612 -14.479 59.714 0.30 28.35 A O ANISOU 2524 OE1BGLU A 315 3314 4170 3284 542 -1733 -54 A O ATOM 2525 OE2AGLU A 315 59.587 -16.000 62.417 0.70 35.40 A O ANISOU 2525 OE2AGLU A 315 3715 5168 4565 -1 -642 1139 A O ATOM 2526 OE2BGLU A 315 60.405 -15.907 58.059 0.30 29.71 A O ANISOU 2526 OE2BGLU A 315 3118 4481 3688 1035 -185 -669 A O ATOM 2527 N HIS A 316 55.306 -13.303 61.777 1.00 17.87 A N ANISOU 2527 N HIS A 316 2834 1992 1962 168 -423 -258 A N ATOM 2528 CA HIS A 316 54.926 -12.763 63.078 1.00 17.73 A C ANISOU 2528 CA HIS A 316 2738 2109 1890 30 -521 -147 A C ATOM 2529 C HIS A 316 55.288 -13.799 64.136 1.00 18.28 A C ANISOU 2529 C HIS A 316 2705 2147 2093 -75 -758 -36 A C ATOM 2530 O HIS A 316 54.794 -14.928 64.123 1.00 18.87 A O ANISOU 2530 O HIS A 316 2831 1934 2405 -1 -685 -273 A O ATOM 2531 CB HIS A 316 53.456 -12.389 63.134 1.00 18.73 A C ANISOU 2531 CB HIS A 316 2577 2045 2493 -145 -392 13 A C ATOM 2532 CG HIS A 316 53.146 -11.416 64.198 1.00 19.16 A C ANISOU 2532 CG HIS A 316 2470 2194 2612 -99 -512 -132 A C ATOM 2533 CD2 HIS A 316 52.861 -11.583 65.506 1.00 22.06 A C ANISOU 2533 CD2 HIS A 316 2967 2252 3163 -255 -203 224 A C ATOM 2534 ND1 HIS A 316 53.170 -10.058 63.968 1.00 22.84 A N ANISOU 2534 ND1 HIS A 316 3161 2331 3186 244 -581 158 A N ATOM 2535 CE1 HIS A 316 52.896 -9.425 65.098 1.00 24.52 A C ANISOU 2535 CE1 HIS A 316 3265 2838 3214 2 -541 -26 A C ATOM 2536 NE2 HIS A 316 52.701 -10.336 66.059 1.00 22.55 A N ANISOU 2536 NE2 HIS A 316 2736 2959 2872 232 -302 -330 A N ATOM 2537 N LYS A 317 56.178 -13.389 65.049 1.00 19.19 A N ANISOU 2537 N LYS A 317 2718 2295 2275 -65 -851 -38 A N ATOM 2538 CA LYS A 317 56.745 -14.340 66.009 1.00 20.02 A C ANISOU 2538 CA LYS A 317 2653 2349 2605 501 -708 -104 A C ATOM 2539 C LYS A 317 55.739 -14.720 67.097 1.00 20.08 A C ANISOU 2539 C LYS A 317 2292 2346 2991 165 -717 -25 A C ATOM 2540 O LYS A 317 54.855 -13.949 67.475 1.00 20.32 A O ANISOU 2540 O LYS A 317 2648 2730 2342 260 -296 -130 A O ATOM 2541 CB LYS A 317 58.020 -13.757 66.617 1.00 24.85 A C ANISOU 2541 CB LYS A 317 2665 3377 3400 -136 -972 363 A C ATOM 2542 CG LYS A 317 59.173 -13.717 65.625 1.00 34.63 A C ANISOU 2542 CG LYS A 317 3806 5070 4280 -776 -490 1624 A C ATOM 2543 CD LYS A 317 60.497 -13.251 66.205 1.00 49.97 A C ANISOU 2543 CD LYS A 317 3329 8776 6879 -759 -846 1374 A C ATOM 2544 CE LYS A 317 61.535 -12.987 65.132 1.00 64.66 A C ANISOU 2544 CE LYS A 317 4894 10597 9077 -2027 651 2607 A C ATOM 2545 NZ LYS A 317 62.790 -12.449 65.712 1.00 79.78 A N ANISOU 2545 NZ LYS A 317 6889 13333 10089 -2966 -512 1239 A N ATOM 2546 N LEU A 318 55.934 -15.937 67.609 1.00 20.22 A N ANISOU 2546 N LEU A 318 2473 2353 2855 202 -512 -54 A N ATOM 2547 CA LEU A 318 55.224 -16.422 68.752 1.00 21.36 A C ANISOU 2547 CA LEU A 318 2819 2530 2763 249 -880 166 A C ATOM 2548 C LEU A 318 55.527 -15.502 69.938 1.00 24.26 A C ANISOU 2548 C LEU A 318 3129 3346 2740 -138 -847 -53 A C ATOM 2549 O LEU A 318 56.680 -15.165 70.178 1.00 27.05 A O ANISOU 2549 O LEU A 318 3137 4563 2576 -414 -832 -59 A O ATOM 2550 CB LEU A 318 55.703 -17.859 68.994 1.00 22.44 A C ANISOU 2550 CB LEU A 318 2888 2906 2732 655 -860 157 A C ATOM 2551 CG LEU A 318 55.092 -18.635 70.137 1.00 24.00 A C ANISOU 2551 CG LEU A 318 2938 2873 3307 420 -662 203 A C ATOM 2552 CD1 LEU A 318 53.646 -18.974 69.869 1.00 23.87 A C ANISOU 2552 CD1 LEU A 318 2841 2688 3540 510 -698 -30 A C ATOM 2553 CD2 LEU A 318 55.903 -19.899 70.343 1.00 24.69 A C ANISOU 2553 CD2 LEU A 318 3751 2535 3094 481 -986 -222 A C ATOM 2554 N ALA A 319 54.476 -15.106 70.663 1.00 23.88 A N ANISOU 2554 N ALA A 319 3314 3182 2575 2 -937 122 A N ATOM 2555 CA ALA A 319 54.611 -14.249 71.834 1.00 24.33 A C ANISOU 2555 CA ALA A 319 3520 3273 2449 -424 -646 80 A C ATOM 2556 C ALA A 319 54.602 -15.051 73.146 1.00 24.72 A C ANISOU 2556 C ALA A 319 3684 3456 2253 -632 -893 -27 A C ATOM 2557 O ALA A 319 55.219 -14.656 74.102 1.00 25.31 A O ANISOU 2557 O ALA A 319 3065 4013 2538 -144 -1242 -112 A O ATOM 2558 CB ALA A 319 53.525 -13.220 71.845 1.00 25.31 A C ANISOU 2558 CB ALA A 319 3606 3468 2542 -434 -806 69 A C ATOM 2559 N ASN A 320 53.861 -16.162 73.191 1.00 21.02 A N ANISOU 2559 N ASN A 320 3339 2893 1755 -194 -888 -28 A N ATOM 2560 CA ASN A 320 53.707 -16.908 74.420 1.00 24.38 A C ANISOU 2560 CA ASN A 320 3887 3270 2106 327 -992 373 A C ATOM 2561 C ASN A 320 53.121 -18.285 74.091 1.00 24.59 A C ANISOU 2561 C ASN A 320 3052 3520 2770 110 -1118 315 A C ATOM 2562 O ASN A 320 52.398 -18.453 73.110 1.00 23.72 A O ANISOU 2562 O ASN A 320 3540 3267 2204 547 -962 131 A O ATOM 2563 CB ASN A 320 52.800 -16.160 75.412 1.00 27.58 A C ANISOU 2563 CB ASN A 320 4450 3767 2259 289 -655 386 A C ATOM 2564 CG ASN A 320 52.907 -16.655 76.838 1.00 27.17 A C ANISOU 2564 CG ASN A 320 4096 3928 2299 915 -663 324 A C ATOM 2565 ND2 ASN A 320 51.849 -16.480 77.618 1.00 31.64 A N ANISOU 2565 ND2 ASN A 320 5022 4666 2332 799 311 407 A N ATOM 2566 OD1 ASN A 320 53.912 -17.240 77.212 1.00 28.86 A O ANISOU 2566 OD1 ASN A 320 4025 4735 2204 1227 -1077 307 A O ATOM 2567 N VAL A 321 53.446 -19.249 74.949 1.00 24.28 A N ANISOU 2567 N VAL A 321 3269 3490 2466 353 -1076 127 A N ATOM 2568 CA VAL A 321 52.848 -20.552 74.980 1.00 23.57 A C ANISOU 2568 CA VAL A 321 3195 3644 2115 148 -769 -163 A C ATOM 2569 C VAL A 321 52.300 -20.743 76.390 1.00 23.71 A C ANISOU 2569 C VAL A 321 3708 3176 2124 -185 -647 -100 A C ATOM 2570 O VAL A 321 52.997 -20.455 77.361 1.00 27.85 A O ANISOU 2570 O VAL A 321 4281 4228 2072 293 -1028 -166 A O ATOM 2571 CB VAL A 321 53.835 -21.689 74.671 1.00 25.23 A C ANISOU 2571 CB VAL A 321 3419 3808 2360 366 -469 -205 A C ATOM 2572 CG1 VAL A 321 53.100 -23.026 74.629 1.00 25.98 A C ANISOU 2572 CG1 VAL A 321 3723 3903 2246 469 -615 -78 A C ATOM 2573 CG2 VAL A 321 54.622 -21.424 73.407 1.00 26.56 A C ANISOU 2573 CG2 VAL A 321 4153 3851 2086 588 -699 -139 A C ATOM 2574 N PHE A 322 51.039 -21.168 76.492 1.00 22.13 A N ANISOU 2574 N PHE A 322 3538 2912 1956 160 -537 121 A N ATOM 2575 CA PHE A 322 50.399 -21.261 77.808 1.00 25.68 A C ANISOU 2575 CA PHE A 322 4079 3549 2127 293 -174 65 A C ATOM 2576 C PHE A 322 49.470 -22.472 77.853 1.00 25.12 A C ANISOU 2576 C PHE A 322 4044 3487 2011 317 -227 181 A C ATOM 2577 O PHE A 322 49.173 -23.071 76.829 1.00 24.28 A O ANISOU 2577 O PHE A 322 4452 2971 1801 387 -425 423 A O ATOM 2578 CB PHE A 322 49.683 -19.957 78.170 1.00 25.64 A C ANISOU 2578 CB PHE A 322 3845 3898 1999 492 -302 -342 A C ATOM 2579 CG PHE A 322 48.484 -19.607 77.336 1.00 25.92 A C ANISOU 2579 CG PHE A 322 3787 3450 2611 597 -168 -77 A C ATOM 2580 CD1 PHE A 322 48.629 -18.818 76.208 1.00 28.66 A C ANISOU 2580 CD1 PHE A 322 3798 3919 3171 767 -489 591 A C ATOM 2581 CD2 PHE A 322 47.215 -20.019 77.706 1.00 26.71 A C ANISOU 2581 CD2 PHE A 322 3668 3882 2599 983 -41 371 A C ATOM 2582 CE1 PHE A 322 47.527 -18.493 75.437 1.00 27.17 A C ANISOU 2582 CE1 PHE A 322 3481 4062 2780 260 -409 856 A C ATOM 2583 CE2 PHE A 322 46.108 -19.690 76.938 1.00 26.17 A C ANISOU 2583 CE2 PHE A 322 3765 3362 2815 242 -367 251 A C ATOM 2584 CZ PHE A 322 46.261 -18.911 75.813 1.00 22.75 A C ANISOU 2584 CZ PHE A 322 3331 2890 2423 168 -499 93 A C ATOM 2585 N SER A 323 49.031 -22.795 79.071 1.00 25.97 A N ANISOU 2585 N SER A 323 4738 3184 1942 215 -599 616 A N ATOM 2586 CA SER A 323 48.150 -23.881 79.302 1.00 25.60 A C ANISOU 2586 CA SER A 323 4256 3638 1833 305 -260 725 A C ATOM 2587 C SER A 323 46.715 -23.358 79.422 1.00 23.83 A C ANISOU 2587 C SER A 323 4310 2651 2093 136 -290 104 A C ATOM 2588 O SER A 323 46.483 -22.396 80.127 1.00 27.43 A O ANISOU 2588 O SER A 323 4694 3243 2485 607 -344 -340 A O ATOM 2589 CB SER A 323 48.594 -24.617 80.552 1.00 33.82 A C ANISOU 2589 CB SER A 323 6193 4614 2040 -151 -137 1636 A C ATOM 2590 OG SER A 323 47.607 -25.539 80.947 1.00 41.77 A O ANISOU 2590 OG SER A 323 7738 5239 2891 -652 100 761 A O ATOM 2591 N SER A 324 45.767 -23.988 78.722 1.00 24.23 A N ANISOU 2591 N SER A 324 4040 3287 1877 295 -127 -59 A N ATOM 2592 CA SER A 324 44.354 -23.650 78.828 1.00 23.66 A C ANISOU 2592 CA SER A 324 4188 2709 2090 426 177 562 A C ATOM 2593 C SER A 324 43.808 -24.086 80.190 1.00 25.89 A C ANISOU 2593 C SER A 324 4165 3677 1995 617 -33 938 A C ATOM 2594 O SER A 324 44.511 -24.753 80.950 1.00 27.21 A O ANISOU 2594 O SER A 324 5138 3744 1455 880 -158 795 A O ATOM 2595 CB SER A 324 43.544 -24.248 77.710 1.00 24.04 A C ANISOU 2595 CB SER A 324 4233 2805 2094 369 365 491 A C ATOM 2596 OG SER A 324 43.269 -25.601 77.940 1.00 23.94 A O ANISOU 2596 OG SER A 324 4056 2806 2234 640 349 572 A O ATOM 2597 N ALA A 325 42.537 -23.755 80.472 1.00 25.84 A N ANISOU 2597 N ALA A 325 4159 3575 2082 500 231 994 A N ATOM 2598 CA ALA A 325 41.910 -24.137 81.756 1.00 29.52 A C ANISOU 2598 CA ALA A 325 4967 3786 2461 86 515 1135 A C ATOM 2599 C ALA A 325 41.986 -25.653 81.962 1.00 29.61 A C ANISOU 2599 C ALA A 325 5624 3815 1811 336 48 928 A C ATOM 2600 O ALA A 325 42.167 -26.118 83.079 1.00 32.97 A O ANISOU 2600 O ALA A 325 6236 4737 1551 435 -92 844 A O ATOM 2601 CB ALA A 325 40.483 -23.650 81.833 1.00 30.77 A C ANISOU 2601 CB ALA A 325 4759 4439 2492 21 612 774 A C ATOM 2602 N SER A 326 41.863 -26.418 80.872 1.00 29.46 A N ANISOU 2602 N SER A 326 5587 3612 1994 95 211 720 A N ATOM 2603 CA SER A 326 41.842 -27.912 80.957 1.00 28.83 A C ANISOU 2603 CA SER A 326 5190 3563 2199 292 -222 1402 A C ATOM 2604 C SER A 326 43.212 -28.529 80.640 1.00 28.26 A C ANISOU 2604 C SER A 326 5160 2914 2661 130 -139 866 A C ATOM 2605 O SER A 326 43.312 -29.743 80.501 1.00 33.75 A O ANISOU 2605 O SER A 326 6096 3014 3711 1004 184 1268 A O ATOM 2606 CB SER A 326 40.791 -28.448 80.017 1.00 31.41 A C ANISOU 2606 CB SER A 326 5746 3891 2297 139 -112 858 A C ATOM 2607 OG SER A 326 41.128 -28.125 78.673 1.00 31.97 A O ANISOU 2607 OG SER A 326 5224 4471 2452 147 110 1267 A O ATOM 2608 N GLY A 327 44.250 -27.702 80.512 1.00 25.53 A N ANISOU 2608 N GLY A 327 4509 3114 2077 493 -210 684 A N ATOM 2609 CA GLY A 327 45.616 -28.145 80.325 1.00 28.88 A C ANISOU 2609 CA GLY A 327 4757 3978 2238 685 -132 585 A C ATOM 2610 C GLY A 327 46.009 -28.329 78.862 1.00 28.07 A C ANISOU 2610 C GLY A 327 4442 4090 2132 878 -689 -368 A C ATOM 2611 O GLY A 327 47.045 -28.931 78.596 1.00 26.90 A O ANISOU 2611 O GLY A 327 4564 3600 2054 848 77 696 A O ATOM 2612 N LYS A 328 45.229 -27.784 77.920 1.00 26.19 A N ANISOU 2612 N LYS A 328 4707 3452 1791 872 141 697 A N ATOM 2613 CA LYS A 328 45.619 -27.848 76.499 1.00 24.59 A C ANISOU 2613 CA LYS A 328 4211 3419 1711 350 -196 186 A C ATOM 2614 C LYS A 328 46.776 -26.860 76.248 1.00 22.77 A C ANISOU 2614 C LYS A 328 4246 2698 1707 581 -420 160 A C ATOM 2615 O LYS A 328 46.896 -25.810 76.909 1.00 25.01 A O ANISOU 2615 O LYS A 328 4701 2417 2384 397 -259 -22 A O ATOM 2616 CB LYS A 328 44.432 -27.537 75.580 1.00 23.26 A C ANISOU 2616 CB LYS A 328 3487 3112 2236 358 7 -175 A C ATOM 2617 CG LYS A 328 43.187 -28.400 75.748 1.00 24.58 A C ANISOU 2617 CG LYS A 328 3433 3590 2316 224 -409 277 A C ATOM 2618 CD LYS A 328 43.429 -29.892 75.645 1.00 29.85 A C ANISOU 2618 CD LYS A 328 4409 3614 3318 311 -572 760 A C ATOM 2619 CE LYS A 328 42.249 -30.709 76.153 1.00 41.58 A C ANISOU 2619 CE LYS A 328 5562 4195 6039 -427 154 539 A C ATOM 2620 NZ LYS A 328 42.491 -32.167 76.002 1.00 53.20 A N ANISOU 2620 NZ LYS A 328 8120 4620 7473 -822 963 509 A N ATOM 2621 N THR A 329 47.597 -27.148 75.238 1.00 22.03 A N ANISOU 2621 N THR A 329 3733 2455 2179 733 -413 264 A N ATOM 2622 CA THR A 329 48.703 -26.275 74.863 1.00 21.61 A C ANISOU 2622 CA THR A 329 3556 2817 1835 774 -662 332 A C ATOM 2623 C THR A 329 48.204 -25.239 73.858 1.00 20.97 A C ANISOU 2623 C THR A 329 3652 2148 2168 569 -655 329 A C ATOM 2624 O THR A 329 47.648 -25.625 72.832 1.00 19.41 A O ANISOU 2624 O THR A 329 3132 2286 1955 352 -225 232 A O ATOM 2625 CB THR A 329 49.851 -27.074 74.242 1.00 21.37 A C ANISOU 2625 CB THR A 329 3472 2803 1843 796 -623 285 A C ATOM 2626 CG2 THR A 329 50.989 -26.209 73.773 1.00 23.92 A C ANISOU 2626 CG2 THR A 329 3744 2752 2589 671 -826 219 A C ATOM 2627 OG1 THR A 329 50.318 -27.981 75.242 1.00 25.77 A O ANISOU 2627 OG1 THR A 329 4287 3263 2239 1254 -504 657 A O ATOM 2628 N VAL A 330 48.433 -23.951 74.165 1.00 20.37 A N ANISOU 2628 N VAL A 330 3814 2321 1603 666 -375 231 A N ATOM 2629 CA VAL A 330 47.963 -22.841 73.326 1.00 19.90 A C ANISOU 2629 CA VAL A 330 3293 2499 1767 608 -289 486 A C ATOM 2630 C VAL A 330 49.117 -21.886 73.003 1.00 20.12 A C ANISOU 2630 C VAL A 330 3599 2184 1860 684 -402 -61 A C ATOM 2631 O VAL A 330 49.858 -21.425 73.876 1.00 21.19 A O ANISOU 2631 O VAL A 330 3928 2885 1235 388 -299 55 A O ATOM 2632 CB VAL A 330 46.795 -22.085 73.976 1.00 19.50 A C ANISOU 2632 CB VAL A 330 3258 2613 1536 421 -180 204 A C ATOM 2633 CG1 VAL A 330 46.223 -21.035 73.034 1.00 20.30 A C ANISOU 2633 CG1 VAL A 330 3205 2894 1613 220 -96 457 A C ATOM 2634 CG2 VAL A 330 45.694 -23.021 74.446 1.00 22.99 A C ANISOU 2634 CG2 VAL A 330 3931 2870 1932 119 -315 -98 A C ATOM 2635 N LEU A 331 49.245 -21.604 71.705 1.00 18.40 A N ANISOU 2635 N LEU A 331 3227 2097 1665 337 -694 -153 A N ATOM 2636 CA LEU A 331 50.105 -20.558 71.182 1.00 17.72 A C ANISOU 2636 CA LEU A 331 2506 2329 1898 622 -441 13 A C ATOM 2637 C LEU A 331 49.340 -19.231 71.177 1.00 17.72 A C ANISOU 2637 C LEU A 331 2628 2186 1917 404 -174 -239 A C ATOM 2638 O LEU A 331 48.161 -19.184 70.830 1.00 17.96 A O ANISOU 2638 O LEU A 331 2734 1972 2115 242 -259 -202 A O ATOM 2639 CB LEU A 331 50.493 -20.905 69.746 1.00 19.23 A C ANISOU 2639 CB LEU A 331 3019 2343 1944 538 -598 -211 A C ATOM 2640 CG LEU A 331 51.057 -22.295 69.481 1.00 18.13 A C ANISOU 2640 CG LEU A 331 2684 2072 2132 355 -276 -36 A C ATOM 2641 CD1 LEU A 331 51.493 -22.407 68.038 1.00 18.18 A C ANISOU 2641 CD1 LEU A 331 2533 2130 2243 302 -363 -227 A C ATOM 2642 CD2 LEU A 331 52.214 -22.611 70.429 1.00 19.35 A C ANISOU 2642 CD2 LEU A 331 3018 2339 1992 508 -314 -1 A C ATOM 2643 N ASP A 332 50.054 -18.168 71.542 1.00 16.86 A N ANISOU 2643 N ASP A 332 2433 2263 1708 416 -598 -209 A N ATOM 2644 CA ASP A 332 49.587 -16.789 71.451 1.00 18.36 A C ANISOU 2644 CA ASP A 332 2750 2192 2031 332 -559 142 A C ATOM 2645 C ASP A 332 50.589 -16.037 70.572 1.00 16.80 A C ANISOU 2645 C ASP A 332 2459 1838 2085 573 -616 -92 A C ATOM 2646 O ASP A 332 51.763 -15.886 70.943 1.00 18.45 A O ANISOU 2646 O ASP A 332 2530 2742 1737 509 -753 29 A O ATOM 2647 CB ASP A 332 49.409 -16.196 72.861 1.00 19.05 A C ANISOU 2647 CB ASP A 332 2662 2287 2287 295 -590 -167 A C ATOM 2648 CG ASP A 332 48.984 -14.735 72.878 1.00 20.07 A C ANISOU 2648 CG ASP A 332 3486 2168 1972 264 -491 -326 A C ATOM 2649 OD1 ASP A 332 48.660 -14.221 71.787 1.00 19.02 A O ANISOU 2649 OD1 ASP A 332 3160 1858 2207 475 -304 -56 A O ATOM 2650 OD2 ASP A 332 48.927 -14.135 73.995 1.00 22.80 A O ANISOU 2650 OD2 ASP A 332 4113 2602 1946 539 -442 -438 A O ATOM 2651 N PHE A 333 50.102 -15.519 69.431 1.00 16.59 A N ANISOU 2651 N PHE A 333 2443 1937 1920 428 -488 95 A N ATOM 2652 CA PHE A 333 50.950 -14.708 68.536 1.00 16.68 A C ANISOU 2652 CA PHE A 333 2529 1973 1835 273 -560 -18 A C ATOM 2653 C PHE A 333 50.893 -13.199 68.849 1.00 16.82 A C ANISOU 2653 C PHE A 333 2342 2032 2014 319 -620 -44 A C ATOM 2654 O PHE A 333 51.591 -12.425 68.183 1.00 19.25 A O ANISOU 2654 O PHE A 333 2710 2083 2520 397 -205 184 A O ATOM 2655 CB PHE A 333 50.581 -15.010 67.087 1.00 16.04 A C ANISOU 2655 CB PHE A 333 2456 2033 1603 475 -369 200 A C ATOM 2656 CG PHE A 333 51.151 -16.352 66.729 1.00 15.69 A C ANISOU 2656 CG PHE A 333 2541 2051 1369 418 -526 51 A C ATOM 2657 CD1 PHE A 333 52.482 -16.492 66.397 1.00 18.18 A C ANISOU 2657 CD1 PHE A 333 2631 2226 2049 -142 -250 273 A C ATOM 2658 CD2 PHE A 333 50.360 -17.479 66.832 1.00 16.64 A C ANISOU 2658 CD2 PHE A 333 2473 2403 1447 213 -315 107 A C ATOM 2659 CE1 PHE A 333 52.997 -17.749 66.126 1.00 17.11 A C ANISOU 2659 CE1 PHE A 333 2673 2347 1479 137 -257 185 A C ATOM 2660 CE2 PHE A 333 50.870 -18.745 66.580 1.00 16.93 A C ANISOU 2660 CE2 PHE A 333 2498 2407 1526 107 -247 -114 A C ATOM 2661 CZ PHE A 333 52.187 -18.865 66.218 1.00 17.15 A C ANISOU 2661 CZ PHE A 333 2586 2017 1913 365 -75 -56 A C ATOM 2662 N GLY A 334 50.067 -12.786 69.819 1.00 17.01 A N ANISOU 2662 N GLY A 334 2426 2112 1924 294 -536 54 A N ATOM 2663 CA GLY A 334 50.022 -11.378 70.262 1.00 17.30 A C ANISOU 2663 CA GLY A 334 2721 1944 1908 402 -500 -6 A C ATOM 2664 C GLY A 334 49.257 -10.437 69.343 1.00 18.34 A C ANISOU 2664 C GLY A 334 2963 2124 1880 411 -598 -10 A C ATOM 2665 O GLY A 334 49.087 -9.248 69.659 1.00 20.30 A O ANISOU 2665 O GLY A 334 3320 2135 2257 347 -576 -319 A O ATOM 2666 N GLN A 335 48.773 -10.956 68.231 1.00 16.82 A N ANISOU 2666 N GLN A 335 2749 1714 1924 544 -599 -49 A N ATOM 2667 CA GLN A 335 48.131 -10.195 67.163 1.00 14.49 A C ANISOU 2667 CA GLN A 335 2357 1677 1470 223 -378 -148 A C ATOM 2668 C GLN A 335 47.144 -11.144 66.502 1.00 14.73 A C ANISOU 2668 C GLN A 335 2162 1703 1731 157 -278 -130 A C ATOM 2669 O GLN A 335 47.516 -12.281 66.235 1.00 15.28 A O ANISOU 2669 O GLN A 335 2450 1610 1745 356 -255 -92 A O ATOM 2670 CB GLN A 335 49.164 -9.702 66.153 1.00 15.44 A C ANISOU 2670 CB GLN A 335 2305 1501 2058 139 -211 -114 A C ATOM 2671 CG GLN A 335 48.544 -9.056 64.918 1.00 15.82 A C ANISOU 2671 CG GLN A 335 2486 1504 2019 213 -198 -8 A C ATOM 2672 CD GLN A 335 47.784 -7.774 65.196 1.00 14.07 A C ANISOU 2672 CD GLN A 335 2003 1667 1675 124 -228 -107 A C ATOM 2673 NE2 GLN A 335 46.545 -7.702 64.676 1.00 13.30 A N ANISOU 2673 NE2 GLN A 335 2047 1468 1538 -12 -284 159 A N ATOM 2674 OE1 GLN A 335 48.311 -6.856 65.862 1.00 15.91 A O ANISOU 2674 OE1 GLN A 335 2241 1729 2075 109 -253 -220 A O ATOM 2675 N ASN A 336 45.936 -10.649 66.233 1.00 13.17 A N ANISOU 2675 N ASN A 336 1943 1458 1600 97 14 -250 A N ATOM 2676 CA ASN A 336 44.960 -11.357 65.431 1.00 14.13 A C ANISOU 2676 CA ASN A 336 2126 1412 1828 2 -218 80 A C ATOM 2677 C ASN A 336 45.341 -11.115 63.968 1.00 13.03 A C ANISOU 2677 C ASN A 336 1977 1236 1738 78 -90 -90 A C ATOM 2678 O ASN A 336 45.181 -9.994 63.458 1.00 13.25 A O ANISOU 2678 O ASN A 336 2283 1198 1552 126 -201 -110 A O ATOM 2679 CB ASN A 336 43.551 -10.861 65.751 1.00 13.27 A C ANISOU 2679 CB ASN A 336 2185 1252 1602 17 77 109 A C ATOM 2680 CG ASN A 336 42.448 -11.668 65.107 1.00 14.46 A C ANISOU 2680 CG ASN A 336 2152 1470 1870 101 -108 -102 A C ATOM 2681 ND2 ASN A 336 41.253 -11.108 65.011 1.00 13.69 A N ANISOU 2681 ND2 ASN A 336 2249 1382 1569 220 86 -55 A N ATOM 2682 OD1 ASN A 336 42.661 -12.838 64.757 1.00 14.14 A O ANISOU 2682 OD1 ASN A 336 2228 1233 1911 158 -264 -23 A O ATOM 2683 N LEU A 337 45.900 -12.138 63.334 1.00 13.02 A N ANISOU 2683 N LEU A 337 1902 1489 1556 175 14 -177 A N ATOM 2684 CA LEU A 337 46.481 -12.057 62.024 1.00 12.83 A C ANISOU 2684 CA LEU A 337 2060 1157 1657 -42 23 -46 A C ATOM 2685 C LEU A 337 45.792 -13.023 61.075 1.00 12.78 A C ANISOU 2685 C LEU A 337 1864 1501 1489 -32 -70 0 A C ATOM 2686 O LEU A 337 44.976 -13.854 61.471 1.00 13.23 A O ANISOU 2686 O LEU A 337 2110 1470 1446 -86 -55 15 A O ATOM 2687 CB LEU A 337 47.996 -12.258 62.082 1.00 15.98 A C ANISOU 2687 CB LEU A 337 2121 1971 1979 0 -323 -40 A C ATOM 2688 CG LEU A 337 48.507 -13.514 62.780 1.00 18.79 A C ANISOU 2688 CG LEU A 337 2470 2340 2328 376 -78 42 A C ATOM 2689 CD1 LEU A 337 48.507 -14.646 61.821 1.00 20.20 A C ANISOU 2689 CD1 LEU A 337 2798 1735 3141 218 -1313 -52 A C ATOM 2690 CD2 LEU A 337 49.916 -13.299 63.312 1.00 20.56 A C ANISOU 2690 CD2 LEU A 337 2805 3156 1849 659 -479 -437 A C ATOM 2691 N VAL A 338 46.149 -12.892 59.808 1.00 11.00 A N ANISOU 2691 N VAL A 338 1589 1099 1490 -22 -25 -188 A N ATOM 2692 CA VAL A 338 45.563 -13.682 58.727 1.00 11.19 A C ANISOU 2692 CA VAL A 338 1608 1269 1373 -68 -195 -31 A C ATOM 2693 C VAL A 338 46.684 -14.303 57.913 1.00 10.73 A C ANISOU 2693 C VAL A 338 1673 1092 1310 -12 -175 107 A C ATOM 2694 O VAL A 338 47.590 -13.617 57.472 1.00 12.17 A O ANISOU 2694 O VAL A 338 1797 1273 1555 -128 59 -101 A O ATOM 2695 CB VAL A 338 44.618 -12.844 57.843 1.00 11.57 A C ANISOU 2695 CB VAL A 338 1663 1215 1515 104 -148 -40 A C ATOM 2696 CG1 VAL A 338 44.081 -13.670 56.695 1.00 12.12 A C ANISOU 2696 CG1 VAL A 338 1583 1241 1781 63 -246 -5 A C ATOM 2697 CG2 VAL A 338 43.469 -12.325 58.682 1.00 12.05 A C ANISOU 2697 CG2 VAL A 338 1770 1072 1734 -106 -99 -165 A C ATOM 2698 N GLY A 339 46.622 -15.640 57.788 1.00 10.96 A N ANISOU 2698 N GLY A 339 1688 1044 1431 47 -206 142 A N ATOM 2699 CA GLY A 339 47.596 -16.441 57.083 1.00 12.46 A C ANISOU 2699 CA GLY A 339 1966 1383 1384 176 -87 206 A C ATOM 2700 C GLY A 339 47.600 -17.850 57.658 1.00 11.71 A C ANISOU 2700 C GLY A 339 1673 1365 1408 227 41 178 A C ATOM 2701 O GLY A 339 46.586 -18.489 57.664 1.00 12.23 A O ANISOU 2701 O GLY A 339 1819 1168 1659 263 -93 -47 A O ATOM 2702 N TRP A 340 48.762 -18.297 58.129 1.00 11.11 A N ANISOU 2702 N TRP A 340 1696 1054 1469 46 -169 142 A N ATOM 2703 CA TRP A 340 48.895 -19.693 58.547 1.00 11.02 A C ANISOU 2703 CA TRP A 340 1591 955 1640 309 -98 15 A C ATOM 2704 C TRP A 340 50.191 -19.848 59.339 1.00 12.82 A C ANISOU 2704 C TRP A 340 1870 1111 1887 294 -404 83 A C ATOM 2705 O TRP A 340 50.940 -18.892 59.513 1.00 13.91 A O ANISOU 2705 O TRP A 340 2085 1285 1913 15 -379 128 A O ATOM 2706 CB TRP A 340 48.850 -20.630 57.354 1.00 11.79 A C ANISOU 2706 CB TRP A 340 1721 1181 1574 359 -313 46 A C ATOM 2707 CG TRP A 340 49.796 -20.339 56.243 1.00 12.37 A C ANISOU 2707 CG TRP A 340 1926 997 1778 150 -216 51 A C ATOM 2708 CD1 TRP A 340 51.149 -20.465 56.213 1.00 12.54 A C ANISOU 2708 CD1 TRP A 340 2052 832 1877 381 -263 -16 A C ATOM 2709 CD2 TRP A 340 49.417 -19.833 54.953 1.00 11.89 A C ANISOU 2709 CD2 TRP A 340 1741 1115 1660 51 -209 66 A C ATOM 2710 CE2 TRP A 340 50.607 -19.717 54.203 1.00 12.23 A C ANISOU 2710 CE2 TRP A 340 1895 979 1772 116 -108 297 A C ATOM 2711 CE3 TRP A 340 48.202 -19.477 54.366 1.00 11.99 A C ANISOU 2711 CE3 TRP A 340 1767 1071 1715 16 -81 101 A C ATOM 2712 NE1 TRP A 340 51.652 -20.111 54.998 1.00 12.92 A N ANISOU 2712 NE1 TRP A 340 1670 1263 1975 250 -123 -30 A N ATOM 2713 CZ2 TRP A 340 50.597 -19.349 52.873 1.00 12.66 A C ANISOU 2713 CZ2 TRP A 340 1716 1500 1594 171 191 174 A C ATOM 2714 CZ3 TRP A 340 48.201 -19.093 53.045 1.00 12.08 A C ANISOU 2714 CZ3 TRP A 340 1656 1253 1679 163 -158 263 A C ATOM 2715 CH2 TRP A 340 49.378 -19.047 52.320 1.00 13.04 A C ANISOU 2715 CH2 TRP A 340 1877 1557 1519 113 5 205 A C ATOM 2716 N LEU A 341 50.448 -21.070 59.800 1.00 13.26 A N ANISOU 2716 N LEU A 341 2091 949 1996 143 -182 132 A N ATOM 2717 CA LEU A 341 51.697 -21.374 60.513 1.00 13.81 A C ANISOU 2717 CA LEU A 341 2177 1459 1612 34 -237 12 A C ATOM 2718 C LEU A 341 52.768 -21.948 59.582 1.00 13.39 A C ANISOU 2718 C LEU A 341 2060 1124 1903 195 -177 415 A C ATOM 2719 O LEU A 341 52.462 -22.540 58.570 1.00 14.16 A O ANISOU 2719 O LEU A 341 2054 1352 1972 340 -399 148 A O ATOM 2720 CB LEU A 341 51.432 -22.427 61.595 1.00 14.91 A C ANISOU 2720 CB LEU A 341 2232 1679 1752 -82 -375 220 A C ATOM 2721 CG LEU A 341 50.446 -22.015 62.675 1.00 16.09 A C ANISOU 2721 CG LEU A 341 2294 1723 2096 231 -155 254 A C ATOM 2722 CD1 LEU A 341 50.224 -23.168 63.635 1.00 16.98 A C ANISOU 2722 CD1 LEU A 341 2270 2165 2015 363 -86 462 A C ATOM 2723 CD2 LEU A 341 50.934 -20.752 63.400 1.00 16.66 A C ANISOU 2723 CD2 LEU A 341 2432 2220 1676 167 -377 129 A C ATOM 2724 N ARG A 342 54.013 -21.741 59.976 1.00 14.51 A N ANISOU 2724 N ARG A 342 1940 1780 1791 131 -339 49 A N ATOM 2725 CA ARG A 342 55.172 -22.474 59.456 1.00 15.47 A C ANISOU 2725 CA ARG A 342 2066 1674 2137 341 -369 -151 A C ATOM 2726 C ARG A 342 55.792 -23.216 60.634 1.00 16.47 A C ANISOU 2726 C ARG A 342 2595 1638 2022 159 -201 -60 A C ATOM 2727 O ARG A 342 56.041 -22.618 61.688 1.00 16.51 A O ANISOU 2727 O ARG A 342 2586 1808 1875 562 -542 106 A O ATOM 2728 CB ARG A 342 56.225 -21.525 58.858 1.00 17.16 A C ANISOU 2728 CB ARG A 342 2255 1922 2341 178 -295 78 A C ATOM 2729 CG ARG A 342 57.474 -22.252 58.339 1.00 19.33 A C ANISOU 2729 CG ARG A 342 2654 2210 2481 666 -132 342 A C ATOM 2730 CD ARG A 342 58.583 -21.338 57.871 1.00 24.36 A C ANISOU 2730 CD ARG A 342 3773 2805 2678 11 -115 638 A C ATOM 2731 NE ARG A 342 59.271 -20.725 58.996 1.00 38.13 A N ANISOU 2731 NE ARG A 342 5173 4226 5088 -574 -427 -161 A N ATOM 2732 CZ ARG A 342 60.043 -19.627 58.934 1.00 47.32 A C ANISOU 2732 CZ ARG A 342 6875 4923 6182 -1774 -131 -200 A C ATOM 2733 NH1 ARG A 342 60.647 -19.175 60.025 1.00 42.40 A N ANISOU 2733 NH1 ARG A 342 5851 5192 5065 -1956 1111 -866 A N ATOM 2734 NH2 ARG A 342 60.203 -18.989 57.783 1.00 51.51 A N ANISOU 2734 NH2 ARG A 342 5570 6502 7498 -1124 1343 900 A N ATOM 2735 N ILE A 343 55.993 -24.527 60.467 1.00 15.37 A N ANISOU 2735 N ILE A 343 2263 1595 1980 296 -673 -113 A N ATOM 2736 CA ILE A 343 56.528 -25.364 61.541 1.00 17.14 A C ANISOU 2736 CA ILE A 343 2369 2318 1823 150 -556 224 A C ATOM 2737 C ILE A 343 57.843 -25.968 61.057 1.00 16.77 A C ANISOU 2737 C ILE A 343 2523 1711 2137 345 -667 343 A C ATOM 2738 O ILE A 343 58.033 -26.156 59.846 1.00 16.98 A O ANISOU 2738 O ILE A 343 2070 2077 2302 600 -519 197 A O ATOM 2739 CB ILE A 343 55.531 -26.458 61.993 1.00 17.10 A C ANISOU 2739 CB ILE A 343 2351 2192 1952 274 -509 335 A C ATOM 2740 CG1 ILE A 343 55.279 -27.532 60.926 1.00 17.15 A C ANISOU 2740 CG1 ILE A 343 2201 2097 2215 252 -341 177 A C ATOM 2741 CG2 ILE A 343 54.260 -25.802 62.512 1.00 19.07 A C ANISOU 2741 CG2 ILE A 343 2437 2350 2457 209 -417 143 A C ATOM 2742 CD1 ILE A 343 54.280 -28.602 61.318 1.00 18.52 A C ANISOU 2742 CD1 ILE A 343 2831 2258 1945 132 -255 357 A C ATOM 2743 N ARG A 344 58.740 -26.202 62.028 1.00 16.44 A N ANISOU 2743 N ARG A 344 2022 2018 2204 367 -561 -29 A N ATOM 2744 CA AARG A 344 59.978 -26.913 61.813 0.40 18.23 A C ANISOU 2744 CA AARG A 344 2388 1951 2586 679 -637 -37 A C ATOM 2745 CA BARG A 344 59.966 -26.910 61.818 0.60 18.30 A C ANISOU 2745 CA BARG A 344 2406 2061 2483 663 -564 -21 A C ATOM 2746 C ARG A 344 60.090 -27.911 62.961 1.00 20.06 A C ANISOU 2746 C ARG A 344 2726 2177 2715 444 -839 140 A C ATOM 2747 O ARG A 344 60.261 -27.506 64.113 1.00 21.84 A O ANISOU 2747 O ARG A 344 3281 2147 2869 1221 -1041 -59 A O ATOM 2748 CB AARG A 344 61.166 -25.945 61.774 0.40 20.00 A C ANISOU 2748 CB AARG A 344 2363 2103 3130 580 -731 -119 A C ATOM 2749 CB BARG A 344 61.137 -25.924 61.786 0.60 21.90 A C ANISOU 2749 CB BARG A 344 2836 2449 3033 185 -752 -19 A C ATOM 2750 CG AARG A 344 62.529 -26.596 61.570 0.40 22.91 A C ANISOU 2750 CG AARG A 344 2659 2279 3764 852 -486 -487 A C ATOM 2751 CG BARG A 344 61.096 -24.983 60.590 0.60 24.42 A C ANISOU 2751 CG BARG A 344 3321 2835 3120 440 -520 160 A C ATOM 2752 CD AARG A 344 63.608 -25.584 61.223 0.40 24.91 A C ANISOU 2752 CD AARG A 344 2820 2335 4308 685 -737 -398 A C ATOM 2753 CD BARG A 344 61.966 -23.747 60.649 0.60 29.66 A C ANISOU 2753 CD BARG A 344 4154 3407 3706 -196 -336 -80 A C ATOM 2754 NE AARG A 344 64.938 -26.175 61.115 0.40 28.74 A N ANISOU 2754 NE AARG A 344 2744 3064 5111 515 -373 -864 A N ATOM 2755 NE BARG A 344 61.969 -23.008 59.384 0.60 32.82 A N ANISOU 2755 NE BARG A 344 4852 3908 3709 -787 -919 36 A N ATOM 2756 CZ AARG A 344 65.424 -26.744 60.020 0.40 32.90 A C ANISOU 2756 CZ AARG A 344 3196 4022 5281 398 358 -743 A C ATOM 2757 CZ BARG A 344 62.752 -21.957 59.139 0.60 35.88 A C ANISOU 2757 CZ BARG A 344 5327 3912 4394 -1039 -1671 -3 A C ATOM 2758 NH1AARG A 344 64.727 -26.720 58.899 0.40 39.56 A N ANISOU 2758 NH1AARG A 344 4190 5154 5686 467 -101 -553 A N ATOM 2759 NH1BARG A 344 63.439 -21.411 60.129 0.60 36.26 A N ANISOU 2759 NH1BARG A 344 4425 4117 5233 -1151 -1609 -582 A N ATOM 2760 NH2AARG A 344 66.599 -27.346 60.046 0.40 35.67 A N ANISOU 2760 NH2AARG A 344 3175 4115 6261 327 693 -863 A N ATOM 2761 NH2BARG A 344 62.863 -21.471 57.914 0.60 34.82 A N ANISOU 2761 NH2BARG A 344 4246 4955 4027 -938 -1810 -313 A N ATOM 2762 N VAL A 345 59.941 -29.199 62.645 1.00 19.36 A N ANISOU 2762 N VAL A 345 2618 2153 2585 699 -553 -147 A N ATOM 2763 CA VAL A 345 59.649 -30.147 63.687 1.00 20.62 A C ANISOU 2763 CA VAL A 345 3045 2391 2397 273 -985 -75 A C ATOM 2764 C VAL A 345 60.143 -31.533 63.270 1.00 21.33 A C ANISOU 2764 C VAL A 345 3104 2681 2318 889 -930 92 A C ATOM 2765 O VAL A 345 60.068 -31.895 62.112 1.00 19.80 A O ANISOU 2765 O VAL A 345 3009 2216 2296 976 -835 346 A O ATOM 2766 CB VAL A 345 58.135 -30.162 63.975 1.00 21.49 A C ANISOU 2766 CB VAL A 345 3354 2105 2704 323 -214 139 A C ATOM 2767 CG1 VAL A 345 57.321 -30.550 62.737 1.00 22.97 A C ANISOU 2767 CG1 VAL A 345 2808 2772 3146 473 -414 254 A C ATOM 2768 CG2 VAL A 345 57.787 -31.050 65.162 1.00 24.02 A C ANISOU 2768 CG2 VAL A 345 4088 2475 2562 829 -58 186 A C ATOM 2769 N LYS A 346 60.596 -32.308 64.264 1.00 20.15 A N ANISOU 2769 N LYS A 346 3044 2411 2201 988 -855 -47 A N ATOM 2770 CA LYS A 346 60.928 -33.721 64.104 1.00 22.59 A C ANISOU 2770 CA LYS A 346 3142 2617 2823 1085 -320 -83 A C ATOM 2771 C LYS A 346 60.071 -34.530 65.081 1.00 19.53 A C ANISOU 2771 C LYS A 346 2661 2277 2482 931 -650 -82 A C ATOM 2772 O LYS A 346 59.875 -34.157 66.227 1.00 22.51 A O ANISOU 2772 O LYS A 346 3418 2879 2255 1192 -808 10 A O ATOM 2773 CB LYS A 346 62.418 -33.992 64.378 1.00 27.70 A C ANISOU 2773 CB LYS A 346 3218 3266 4038 1350 -383 656 A C ATOM 2774 CG LYS A 346 62.768 -35.474 64.413 1.00 32.82 A C ANISOU 2774 CG LYS A 346 3933 3494 5043 1675 -349 342 A C ATOM 2775 CD LYS A 346 64.232 -35.774 64.262 1.00 40.81 A C ANISOU 2775 CD LYS A 346 3880 4900 6722 1344 8 899 A C ATOM 2776 CE LYS A 346 64.443 -37.245 63.944 1.00 44.81 A C ANISOU 2776 CE LYS A 346 4350 5209 7465 2112 499 956 A C ATOM 2777 NZ LYS A 346 65.827 -37.681 64.209 1.00 47.79 A N ANISOU 2777 NZ LYS A 346 4131 6415 7612 2107 1291 1792 A N ATOM 2778 N GLY A 347 59.575 -35.674 64.640 1.00 20.14 A N ANISOU 2778 N GLY A 347 3036 2425 2188 654 -433 135 A N ATOM 2779 CA GLY A 347 58.816 -36.489 65.544 1.00 21.36 A C ANISOU 2779 CA GLY A 347 3315 2748 2051 655 -330 172 A C ATOM 2780 C GLY A 347 58.544 -37.862 64.963 1.00 22.06 A C ANISOU 2780 C GLY A 347 3378 2308 2693 718 -152 380 A C ATOM 2781 O GLY A 347 58.935 -38.144 63.832 1.00 23.13 A O ANISOU 2781 O GLY A 347 3368 2609 2812 927 -354 479 A O ATOM 2782 N PRO A 348 57.848 -38.728 65.723 1.00 22.25 A N ANISOU 2782 N PRO A 348 3334 2858 2260 393 -545 338 A N ATOM 2783 CA PRO A 348 57.611 -40.099 65.301 1.00 24.53 A C ANISOU 2783 CA PRO A 348 3707 2791 2821 636 -668 134 A C ATOM 2784 C PRO A 348 56.782 -40.246 64.014 1.00 23.85 A C ANISOU 2784 C PRO A 348 3941 2448 2671 900 -614 158 A C ATOM 2785 O PRO A 348 55.744 -39.589 63.827 1.00 22.86 A O ANISOU 2785 O PRO A 348 3681 2278 2725 473 -648 645 A O ATOM 2786 CB PRO A 348 56.833 -40.682 66.486 1.00 24.79 A C ANISOU 2786 CB PRO A 348 3857 2811 2750 250 -613 287 A C ATOM 2787 CG PRO A 348 57.268 -39.845 67.660 1.00 25.26 A C ANISOU 2787 CG PRO A 348 4245 2322 3029 688 -699 369 A C ATOM 2788 CD PRO A 348 57.284 -38.455 67.065 1.00 23.13 A C ANISOU 2788 CD PRO A 348 3817 2611 2361 1113 -584 607 A C ATOM 2789 N LYS A 349 57.243 -41.161 63.155 1.00 23.95 A N ANISOU 2789 N LYS A 349 4242 2228 2627 1290 -611 285 A N ATOM 2790 CA LYS A 349 56.529 -41.509 61.955 1.00 22.84 A C ANISOU 2790 CA LYS A 349 3788 1928 2962 936 -451 153 A C ATOM 2791 C LYS A 349 55.079 -41.891 62.291 1.00 21.62 A C ANISOU 2791 C LYS A 349 3624 1777 2813 1039 -181 865 A C ATOM 2792 O LYS A 349 54.828 -42.764 63.126 1.00 23.16 A O ANISOU 2792 O LYS A 349 4312 1929 2559 725 -193 873 A O ATOM 2793 CB LYS A 349 57.233 -42.683 61.264 1.00 24.05 A C ANISOU 2793 CB LYS A 349 3879 1985 3273 1015 -273 47 A C ATOM 2794 CG LYS A 349 56.621 -43.084 59.926 1.00 23.08 A C ANISOU 2794 CG LYS A 349 3765 1773 3229 973 -116 117 A C ATOM 2795 CD LYS A 349 57.447 -44.147 59.198 1.00 24.49 A C ANISOU 2795 CD LYS A 349 4290 1577 3438 1126 -195 -56 A C ATOM 2796 CE LYS A 349 56.818 -44.502 57.868 1.00 31.73 A C ANISOU 2796 CE LYS A 349 5201 2684 4169 1016 -711 -329 A C ATOM 2797 NZ LYS A 349 57.674 -45.408 57.067 1.00 35.22 A N ANISOU 2797 NZ LYS A 349 4722 4057 4600 1181 -583 -516 A N ATOM 2798 N GLY A 350 54.123 -41.228 61.618 1.00 18.55 A N ANISOU 2798 N GLY A 350 3075 1472 2498 709 -181 499 A N ATOM 2799 CA GLY A 350 52.690 -41.507 61.742 1.00 20.30 A C ANISOU 2799 CA GLY A 350 3392 1755 2563 422 87 389 A C ATOM 2800 C GLY A 350 52.000 -40.781 62.876 1.00 19.19 A C ANISOU 2800 C GLY A 350 3039 1558 2693 322 91 440 A C ATOM 2801 O GLY A 350 50.780 -40.891 63.013 1.00 21.42 A O ANISOU 2801 O GLY A 350 3333 2098 2705 486 403 473 A O ATOM 2802 N GLN A 351 52.754 -40.018 63.677 1.00 19.07 A N ANISOU 2802 N GLN A 351 3280 1512 2451 872 -277 369 A N ATOM 2803 CA GLN A 351 52.153 -39.149 64.688 1.00 19.79 A C ANISOU 2803 CA GLN A 351 3279 1965 2272 649 32 338 A C ATOM 2804 C GLN A 351 51.604 -37.877 64.033 1.00 18.87 A C ANISOU 2804 C GLN A 351 2631 2050 2488 334 -362 498 A C ATOM 2805 O GLN A 351 52.302 -37.209 63.249 1.00 19.18 A O ANISOU 2805 O GLN A 351 3207 1638 2440 619 -209 504 A O ATOM 2806 CB GLN A 351 53.178 -38.788 65.758 1.00 19.36 A C ANISOU 2806 CB GLN A 351 3212 1581 2562 1006 -210 295 A C ATOM 2807 CG GLN A 351 52.591 -37.913 66.858 1.00 21.81 A C ANISOU 2807 CG GLN A 351 3818 2100 2367 1100 -10 335 A C ATOM 2808 CD GLN A 351 53.411 -37.987 68.106 1.00 23.79 A C ANISOU 2808 CD GLN A 351 4611 2368 2059 1271 -111 100 A C ATOM 2809 NE2 GLN A 351 53.496 -36.883 68.837 1.00 27.47 A N ANISOU 2809 NE2 GLN A 351 5053 2177 3205 1084 -622 139 A N ATOM 2810 OE1 GLN A 351 53.941 -39.050 68.426 1.00 28.15 A O ANISOU 2810 OE1 GLN A 351 5322 2842 2529 1367 -395 811 A O ATOM 2811 N THR A 352 50.361 -37.534 64.380 1.00 18.91 A N ANISOU 2811 N THR A 352 3289 1353 2541 574 -27 715 A N ATOM 2812 CA THR A 352 49.687 -36.387 63.822 1.00 18.04 A C ANISOU 2812 CA THR A 352 3270 1608 1974 707 133 827 A C ATOM 2813 C THR A 352 49.623 -35.241 64.841 1.00 20.16 A C ANISOU 2813 C THR A 352 3435 2009 2212 536 51 486 A C ATOM 2814 O THR A 352 49.164 -35.410 65.981 1.00 20.78 A O ANISOU 2814 O THR A 352 3860 1809 2226 522 179 327 A O ATOM 2815 CB THR A 352 48.273 -36.769 63.351 1.00 19.96 A C ANISOU 2815 CB THR A 352 3304 1647 2629 553 -56 217 A C ATOM 2816 CG2 THR A 352 47.524 -35.625 62.683 1.00 19.24 A C ANISOU 2816 CG2 THR A 352 3060 1761 2488 494 -153 204 A C ATOM 2817 OG1 THR A 352 48.369 -37.879 62.460 1.00 20.20 A O ANISOU 2817 OG1 THR A 352 3253 1976 2446 594 -180 71 A O ATOM 2818 N ILE A 353 50.034 -34.053 64.381 1.00 17.11 A N ANISOU 2818 N ILE A 353 2907 1832 1761 512 -13 151 A N ATOM 2819 CA ILE A 353 49.861 -32.811 65.097 1.00 16.69 A C ANISOU 2819 CA ILE A 353 2767 2040 1533 594 -456 -51 A C ATOM 2820 C ILE A 353 48.618 -32.091 64.557 1.00 17.06 A C ANISOU 2820 C ILE A 353 2818 1855 1806 545 -238 244 A C ATOM 2821 O ILE A 353 48.459 -31.977 63.343 1.00 18.02 A O ANISOU 2821 O ILE A 353 3224 1932 1690 735 -135 223 A O ATOM 2822 CB ILE A 353 51.092 -31.900 64.917 1.00 18.12 A C ANISOU 2822 CB ILE A 353 2896 2048 1939 608 -90 153 A C ATOM 2823 CG1 ILE A 353 52.419 -32.657 64.947 1.00 18.82 A C ANISOU 2823 CG1 ILE A 353 2852 2350 1947 762 -439 224 A C ATOM 2824 CG2 ILE A 353 51.047 -30.762 65.918 1.00 18.48 A C ANISOU 2824 CG2 ILE A 353 2943 2403 1672 475 -526 18 A C ATOM 2825 CD1 ILE A 353 53.639 -31.778 64.719 1.00 19.77 A C ANISOU 2825 CD1 ILE A 353 3323 1960 2228 686 -240 166 A C ATOM 2826 N ARG A 354 47.801 -31.563 65.475 1.00 17.18 A N ANISOU 2826 N ARG A 354 2914 2038 1574 590 -73 473 A N ATOM 2827 CA ARG A 354 46.612 -30.806 65.121 1.00 17.59 A C ANISOU 2827 CA ARG A 354 2735 1909 2037 571 -41 26 A C ATOM 2828 C ARG A 354 46.769 -29.363 65.609 1.00 18.89 A C ANISOU 2828 C ARG A 354 3296 1927 1952 696 -226 193 A C ATOM 2829 O ARG A 354 47.256 -29.130 66.744 1.00 17.69 A O ANISOU 2829 O ARG A 354 3226 1591 1903 511 -98 458 A O ATOM 2830 CB ARG A 354 45.365 -31.431 65.751 1.00 17.70 A C ANISOU 2830 CB ARG A 354 2888 2058 1776 370 -142 241 A C ATOM 2831 CG ARG A 354 44.058 -30.788 65.312 1.00 17.69 A C ANISOU 2831 CG ARG A 354 2812 1805 2104 117 -100 189 A C ATOM 2832 CD ARG A 354 42.827 -31.366 65.974 1.00 18.29 A C ANISOU 2832 CD ARG A 354 3098 1818 2033 278 70 507 A C ATOM 2833 NE ARG A 354 42.814 -31.059 67.393 1.00 19.92 A N ANISOU 2833 NE ARG A 354 3403 2164 1999 223 153 277 A N ATOM 2834 CZ ARG A 354 41.945 -31.554 68.261 1.00 26.75 A C ANISOU 2834 CZ ARG A 354 3910 3666 2586 -807 353 216 A C ATOM 2835 NH1 ARG A 354 40.978 -32.359 67.846 1.00 27.89 A N ANISOU 2835 NH1 ARG A 354 3749 3758 3090 -837 326 737 A N ATOM 2836 NH2 ARG A 354 42.027 -31.210 69.538 1.00 30.14 A N ANISOU 2836 NH2 ARG A 354 4439 4352 2658 -501 235 -203 A N ATOM 2837 N PHE A 355 46.349 -28.430 64.732 1.00 15.13 A N ANISOU 2837 N PHE A 355 2637 1708 1402 201 -189 93 A N ATOM 2838 CA PHE A 355 46.418 -26.988 64.995 1.00 15.75 A C ANISOU 2838 CA PHE A 355 2463 1595 1924 197 -105 47 A C ATOM 2839 C PHE A 355 45.033 -26.385 64.817 1.00 15.60 A C ANISOU 2839 C PHE A 355 2625 1459 1841 125 123 275 A C ATOM 2840 O PHE A 355 44.506 -26.415 63.707 1.00 14.97 A O ANISOU 2840 O PHE A 355 2490 1353 1845 268 64 86 A O ATOM 2841 CB PHE A 355 47.396 -26.331 64.026 1.00 14.72 A C ANISOU 2841 CB PHE A 355 2163 1657 1771 317 -123 -134 A C ATOM 2842 CG PHE A 355 48.792 -26.894 64.017 1.00 15.08 A C ANISOU 2842 CG PHE A 355 2175 1530 2023 204 48 -99 A C ATOM 2843 CD1 PHE A 355 49.744 -26.453 64.899 1.00 15.79 A C ANISOU 2843 CD1 PHE A 355 2411 1499 2088 73 -172 106 A C ATOM 2844 CD2 PHE A 355 49.150 -27.916 63.145 1.00 16.01 A C ANISOU 2844 CD2 PHE A 355 2481 1719 1880 396 13 -109 A C ATOM 2845 CE1 PHE A 355 51.027 -26.971 64.889 1.00 17.76 A C ANISOU 2845 CE1 PHE A 355 2710 1902 2135 461 -447 -33 A C ATOM 2846 CE2 PHE A 355 50.442 -28.403 63.114 1.00 16.55 A C ANISOU 2846 CE2 PHE A 355 2498 1808 1982 336 -9 -141 A C ATOM 2847 CZ PHE A 355 51.370 -27.955 64.000 1.00 16.67 A C ANISOU 2847 CZ PHE A 355 2370 1563 2397 339 -157 208 A C ATOM 2848 N VAL A 356 44.430 -25.923 65.927 1.00 15.03 A N ANISOU 2848 N VAL A 356 2396 1807 1506 360 -98 206 A N ATOM 2849 CA VAL A 356 43.101 -25.336 65.887 1.00 15.55 A C ANISOU 2849 CA VAL A 356 2299 1717 1890 225 216 -37 A C ATOM 2850 C VAL A 356 43.247 -23.824 66.101 1.00 15.98 A C ANISOU 2850 C VAL A 356 2651 1692 1729 382 -214 138 A C ATOM 2851 O VAL A 356 43.703 -23.399 67.183 1.00 16.29 A O ANISOU 2851 O VAL A 356 2871 1555 1764 185 -400 410 A O ATOM 2852 CB VAL A 356 42.168 -25.968 66.946 1.00 16.22 A C ANISOU 2852 CB VAL A 356 2629 1685 1847 225 77 211 A C ATOM 2853 CG1 VAL A 356 40.802 -25.313 66.972 1.00 16.98 A C ANISOU 2853 CG1 VAL A 356 2544 1735 2172 101 214 257 A C ATOM 2854 CG2 VAL A 356 42.000 -27.472 66.727 1.00 15.73 A C ANISOU 2854 CG2 VAL A 356 2443 1750 1783 -179 -115 181 A C ATOM 2855 N HIS A 357 42.873 -23.050 65.071 1.00 13.74 A N ANISOU 2855 N HIS A 357 2410 1300 1510 203 -107 21 A N ATOM 2856 CA HIS A 357 43.166 -21.600 65.063 1.00 14.69 A C ANISOU 2856 CA HIS A 357 2582 1360 1638 152 -8 0 A C ATOM 2857 C HIS A 357 41.930 -20.788 65.465 1.00 14.36 A C ANISOU 2857 C HIS A 357 2222 1631 1600 29 63 339 A C ATOM 2858 O HIS A 357 40.864 -20.988 64.903 1.00 14.59 A O ANISOU 2858 O HIS A 357 2223 1585 1735 432 -48 15 A O ATOM 2859 CB HIS A 357 43.610 -21.192 63.644 1.00 13.65 A C ANISOU 2859 CB HIS A 357 2224 1364 1599 101 61 -24 A C ATOM 2860 CG HIS A 357 44.767 -21.959 63.072 1.00 12.73 A C ANISOU 2860 CG HIS A 357 2428 889 1519 285 -114 182 A C ATOM 2861 CD2 HIS A 357 46.065 -21.621 62.859 1.00 14.05 A C ANISOU 2861 CD2 HIS A 357 2326 1372 1640 399 -261 84 A C ATOM 2862 ND1 HIS A 357 44.632 -23.259 62.621 1.00 13.81 A N ANISOU 2862 ND1 HIS A 357 2690 838 1718 202 -81 149 A N ATOM 2863 CE1 HIS A 357 45.793 -23.659 62.124 1.00 16.30 A C ANISOU 2863 CE1 HIS A 357 2355 1367 2472 71 -74 571 A C ATOM 2864 NE2 HIS A 357 46.702 -22.705 62.283 1.00 14.23 A N ANISOU 2864 NE2 HIS A 357 2504 1309 1591 232 -58 197 A N ATOM 2865 N THR A 358 42.089 -19.848 66.420 1.00 15.30 A N ANISOU 2865 N THR A 358 2262 1930 1619 205 -231 256 A N ATOM 2866 CA THR A 358 40.961 -18.996 66.849 1.00 14.33 A C ANISOU 2866 CA THR A 358 2316 1573 1552 100 -175 117 A C ATOM 2867 C THR A 358 41.422 -17.543 67.031 1.00 14.40 A C ANISOU 2867 C THR A 358 2368 1688 1415 126 9 161 A C ATOM 2868 O THR A 358 42.589 -17.260 67.234 1.00 14.55 A O ANISOU 2868 O THR A 358 2269 1445 1812 366 -195 200 A O ATOM 2869 CB THR A 358 40.289 -19.509 68.131 1.00 15.36 A C ANISOU 2869 CB THR A 358 2406 1559 1871 66 -18 83 A C ATOM 2870 CG2 THR A 358 39.938 -20.978 68.038 1.00 16.19 A C ANISOU 2870 CG2 THR A 358 3067 1509 1572 176 182 95 A C ATOM 2871 OG1 THR A 358 41.151 -19.282 69.245 1.00 16.16 A O ANISOU 2871 OG1 THR A 358 2780 1743 1617 -32 -109 361 A O ATOM 2872 N GLU A 359 40.441 -16.638 67.001 1.00 13.99 A N ANISOU 2872 N GLU A 359 2141 1683 1491 42 -41 -51 A N ATOM 2873 CA GLU A 359 40.709 -15.196 67.194 1.00 14.96 A C ANISOU 2873 CA GLU A 359 2434 1565 1684 -47 -22 -34 A C ATOM 2874 C GLU A 359 40.897 -14.850 68.668 1.00 15.95 A C ANISOU 2874 C GLU A 359 2130 2277 1651 135 -228 149 A C ATOM 2875 O GLU A 359 41.678 -13.949 69.020 1.00 17.81 A O ANISOU 2875 O GLU A 359 2797 2134 1834 103 -175 -227 A O ATOM 2876 CB GLU A 359 39.552 -14.385 66.624 1.00 15.36 A C ANISOU 2876 CB GLU A 359 2478 1553 1804 -124 -254 -261 A C ATOM 2877 CG GLU A 359 39.497 -14.455 65.134 1.00 15.12 A C ANISOU 2877 CG GLU A 359 2547 1395 1803 -43 -239 -74 A C ATOM 2878 CD GLU A 359 38.515 -13.430 64.587 1.00 14.92 A C ANISOU 2878 CD GLU A 359 2502 1477 1690 28 -38 -84 A C ATOM 2879 OE1 GLU A 359 37.302 -13.504 64.936 1.00 14.96 A O ANISOU 2879 OE1 GLU A 359 2419 1267 1996 136 19 -372 A O ATOM 2880 OE2 GLU A 359 38.974 -12.541 63.856 1.00 15.20 A O ANISOU 2880 OE2 GLU A 359 2329 1301 2144 76 -85 183 A O ATOM 2881 N VAL A 360 40.138 -15.540 69.519 1.00 15.72 A N ANISOU 2881 N VAL A 360 2606 1819 1545 272 229 -75 A N ATOM 2882 CA VAL A 360 40.020 -15.198 70.937 1.00 17.77 A C ANISOU 2882 CA VAL A 360 3034 2185 1532 165 243 59 A C ATOM 2883 C VAL A 360 39.940 -16.481 71.753 1.00 17.86 A C ANISOU 2883 C VAL A 360 3047 2066 1672 49 56 28 A C ATOM 2884 O VAL A 360 39.720 -17.585 71.227 1.00 17.24 A O ANISOU 2884 O VAL A 360 3051 2131 1368 362 -168 -23 A O ATOM 2885 CB VAL A 360 38.784 -14.330 71.223 1.00 17.50 A C ANISOU 2885 CB VAL A 360 3209 1581 1857 68 482 -92 A C ATOM 2886 CG1 VAL A 360 38.867 -12.995 70.494 1.00 16.73 A C ANISOU 2886 CG1 VAL A 360 2991 1491 1873 142 380 -211 A C ATOM 2887 CG2 VAL A 360 37.491 -15.060 70.914 1.00 20.41 A C ANISOU 2887 CG2 VAL A 360 3238 1861 2654 145 507 195 A C ATOM 2888 N MET A 361 40.113 -16.287 73.059 1.00 20.29 A N ANISOU 2888 N MET A 361 3830 2203 1676 643 17 -55 A N ATOM 2889 CA MET A 361 39.843 -17.269 74.056 1.00 21.57 A C ANISOU 2889 CA MET A 361 3765 2403 2026 458 382 14 A C ATOM 2890 C MET A 361 38.476 -16.950 74.680 1.00 23.41 A C ANISOU 2890 C MET A 361 3578 2886 2429 509 347 -106 A C ATOM 2891 O MET A 361 38.043 -15.781 74.730 1.00 23.14 A O ANISOU 2891 O MET A 361 4073 3016 1701 741 332 -19 A O ATOM 2892 CB MET A 361 40.898 -17.218 75.166 1.00 23.45 A C ANISOU 2892 CB MET A 361 3812 2725 2370 611 -23 53 A C ATOM 2893 CG MET A 361 42.321 -17.348 74.723 1.00 22.79 A C ANISOU 2893 CG MET A 361 3838 2413 2407 577 -111 267 A C ATOM 2894 SD MET A 361 42.665 -19.025 74.163 1.00 23.61 A S ANISOU 2894 SD MET A 361 3826 2523 2620 367 78 248 A S ATOM 2895 CE MET A 361 42.691 -19.944 75.710 1.00 27.84 A C ANISOU 2895 CE MET A 361 4352 3530 2695 818 -67 695 A C ATOM 2896 N GLU A 362 37.817 -17.977 75.191 1.00 23.64 A N ANISOU 2896 N GLU A 362 3647 3145 2188 563 209 200 A N ATOM 2897 CA GLU A 362 36.602 -17.797 75.957 1.00 24.35 A C ANISOU 2897 CA GLU A 362 3700 2773 2775 327 240 9 A C ATOM 2898 C GLU A 362 36.484 -18.940 76.968 1.00 26.49 A C ANISOU 2898 C GLU A 362 4581 2999 2482 670 114 130 A C ATOM 2899 O GLU A 362 36.653 -20.101 76.621 1.00 24.72 A O ANISOU 2899 O GLU A 362 4373 2763 2256 866 567 369 A O ATOM 2900 CB GLU A 362 35.385 -17.792 75.027 1.00 25.12 A C ANISOU 2900 CB GLU A 362 3841 3139 2564 294 123 208 A C ATOM 2901 CG GLU A 362 34.117 -17.341 75.722 1.00 26.00 A C ANISOU 2901 CG GLU A 362 4089 3083 2704 517 312 160 A C ATOM 2902 CD GLU A 362 32.792 -17.462 74.984 1.00 23.65 A C ANISOU 2902 CD GLU A 362 3733 2505 2747 316 614 179 A C ATOM 2903 OE1 GLU A 362 32.670 -18.307 74.026 1.00 26.38 A O ANISOU 2903 OE1 GLU A 362 4828 2760 2435 856 11 49 A O ATOM 2904 OE2 GLU A 362 31.855 -16.667 75.369 1.00 23.41 A O ANISOU 2904 OE2 GLU A 362 3381 2008 3504 203 685 285 A O ATOM 2905 N ASN A 363 36.174 -18.605 78.223 1.00 28.57 A N ANISOU 2905 N ASN A 363 5216 3149 2488 701 484 565 A N ATOM 2906 CA ASN A 363 35.976 -19.654 79.221 1.00 30.55 A C ANISOU 2906 CA ASN A 363 4900 3785 2920 411 106 1084 A C ATOM 2907 C ASN A 363 37.250 -20.504 79.352 1.00 28.62 A C ANISOU 2907 C ASN A 363 4494 3877 2500 337 499 518 A C ATOM 2908 O ASN A 363 37.174 -21.704 79.667 1.00 33.34 A O ANISOU 2908 O ASN A 363 6164 3880 2621 242 610 846 A O ATOM 2909 CB ASN A 363 34.747 -20.516 78.876 1.00 32.08 A C ANISOU 2909 CB ASN A 363 5047 3733 3409 404 -339 494 A C ATOM 2910 CG ASN A 363 33.462 -19.722 78.954 1.00 38.18 A C ANISOU 2910 CG ASN A 363 5057 4964 4485 453 -374 -677 A C ATOM 2911 ND2 ASN A 363 32.416 -20.183 78.290 1.00 40.82 A N ANISOU 2911 ND2 ASN A 363 3921 5401 6189 340 -238 -696 A N ATOM 2912 OD1 ASN A 363 33.423 -18.677 79.603 1.00 48.35 A O ANISOU 2912 OD1 ASN A 363 6606 6012 5752 1688 -707 -1834 A O ATOM 2913 N GLY A 364 38.418 -19.870 79.161 1.00 26.65 A N ANISOU 2913 N GLY A 364 4260 3972 1891 515 -11 316 A N ATOM 2914 CA GLY A 364 39.717 -20.505 79.414 1.00 28.80 A C ANISOU 2914 CA GLY A 364 4658 3847 2435 1112 115 440 A C ATOM 2915 C GLY A 364 40.174 -21.450 78.304 1.00 27.05 A C ANISOU 2915 C GLY A 364 3850 4167 2259 1115 -139 357 A C ATOM 2916 O GLY A 364 41.169 -22.133 78.484 1.00 26.24 A O ANISOU 2916 O GLY A 364 3882 4014 2073 1168 363 761 A O ATOM 2917 N GLU A 365 39.461 -21.501 77.167 1.00 23.94 A N ANISOU 2917 N GLU A 365 3969 2950 2175 1018 -97 284 A N ATOM 2918 CA GLU A 365 39.852 -22.338 76.012 1.00 23.02 A C ANISOU 2918 CA GLU A 365 3791 3235 1717 734 249 651 A C ATOM 2919 C GLU A 365 39.742 -21.520 74.715 1.00 21.95 A C ANISOU 2919 C GLU A 365 3724 2738 1877 727 227 648 A C ATOM 2920 O GLU A 365 39.019 -20.514 74.635 1.00 21.12 A O ANISOU 2920 O GLU A 365 3602 2633 1788 634 273 345 A O ATOM 2921 CB GLU A 365 38.938 -23.557 75.853 1.00 26.22 A C ANISOU 2921 CB GLU A 365 4666 2640 2657 496 619 1169 A C ATOM 2922 CG GLU A 365 38.777 -24.388 77.122 1.00 26.42 A C ANISOU 2922 CG GLU A 365 4563 3073 2402 725 -285 1205 A C ATOM 2923 CD GLU A 365 39.995 -25.211 77.520 1.00 25.43 A C ANISOU 2923 CD GLU A 365 4320 2702 2639 890 411 1156 A C ATOM 2924 OE1 GLU A 365 40.889 -25.412 76.664 1.00 26.68 A O ANISOU 2924 OE1 GLU A 365 4245 3509 2383 750 398 1047 A O ATOM 2925 OE2 GLU A 365 40.037 -25.652 78.694 1.00 32.17 A O ANISOU 2925 OE2 GLU A 365 5934 3662 2624 742 185 1316 A O ATOM 2926 N VAL A 366 40.398 -22.003 73.665 1.00 21.01 A N ANISOU 2926 N VAL A 366 3493 2463 2027 588 208 640 A N ATOM 2927 CA VAL A 366 40.281 -21.372 72.365 1.00 19.00 A C ANISOU 2927 CA VAL A 366 2954 2364 1898 274 37 504 A C ATOM 2928 C VAL A 366 38.799 -21.378 71.953 1.00 18.76 A C ANISOU 2928 C VAL A 366 2714 2221 2190 435 319 195 A C ATOM 2929 O VAL A 366 38.075 -22.298 72.261 1.00 22.31 A O ANISOU 2929 O VAL A 366 3213 2340 2923 438 93 802 A O ATOM 2930 CB VAL A 366 41.210 -22.003 71.316 1.00 18.18 A C ANISOU 2930 CB VAL A 366 2871 2172 1863 -83 110 538 A C ATOM 2931 CG1 VAL A 366 42.668 -21.893 71.719 1.00 18.69 A C ANISOU 2931 CG1 VAL A 366 3090 1811 2198 319 -62 503 A C ATOM 2932 CG2 VAL A 366 40.857 -23.438 70.987 1.00 20.01 A C ANISOU 2932 CG2 VAL A 366 3304 2183 2116 54 59 170 A C ATOM 2933 N ALA A 367 38.340 -20.285 71.321 1.00 17.33 A N ANISOU 2933 N ALA A 367 2901 1957 1725 19 75 59 A N ATOM 2934 CA ALA A 367 36.925 -20.139 71.005 1.00 16.48 A C ANISOU 2934 CA ALA A 367 2866 1508 1887 60 144 -30 A C ATOM 2935 C ALA A 367 36.642 -20.466 69.536 1.00 17.29 A C ANISOU 2935 C ALA A 367 2757 1911 1901 -247 44 54 A C ATOM 2936 O ALA A 367 36.838 -19.632 68.670 1.00 18.14 A O ANISOU 2936 O ALA A 367 2906 1694 2293 212 352 218 A O ATOM 2937 CB ALA A 367 36.516 -18.730 71.320 1.00 17.97 A C ANISOU 2937 CB ALA A 367 3004 1813 2011 381 22 -313 A C ATOM 2938 N THR A 368 36.169 -21.687 69.252 1.00 17.26 A N ANISOU 2938 N THR A 368 3046 1714 1798 -192 86 212 A N ATOM 2939 CA THR A 368 35.845 -22.082 67.895 1.00 17.64 A C ANISOU 2939 CA THR A 368 2937 1851 1912 -67 358 -117 A C ATOM 2940 C THR A 368 34.388 -21.764 67.553 1.00 16.72 A C ANISOU 2940 C THR A 368 2798 1551 2004 -187 469 -289 A C ATOM 2941 O THR A 368 34.005 -21.732 66.396 1.00 17.53 A O ANISOU 2941 O THR A 368 2840 1950 1868 286 576 -203 A O ATOM 2942 CB THR A 368 36.142 -23.573 67.692 1.00 17.42 A C ANISOU 2942 CB THR A 368 2798 1797 2022 -101 268 -151 A C ATOM 2943 CG2 THR A 368 37.607 -23.889 67.866 1.00 19.19 A C ANISOU 2943 CG2 THR A 368 2719 2235 2336 13 -21 67 A C ATOM 2944 OG1 THR A 368 35.362 -24.295 68.638 1.00 19.50 A O ANISOU 2944 OG1 THR A 368 2939 1840 2626 50 476 287 A O ATOM 2945 N ARG A 369 33.535 -21.585 68.575 1.00 16.40 A N ANISOU 2945 N ARG A 369 2953 1609 1669 227 329 64 A N ATOM 2946 CA ARG A 369 32.109 -21.413 68.328 1.00 17.20 A C ANISOU 2946 CA ARG A 369 2763 1596 2173 -37 774 -2 A C ATOM 2947 C ARG A 369 31.828 -20.366 67.237 1.00 16.36 A C ANISOU 2947 C ARG A 369 2655 1627 1933 96 378 -110 A C ATOM 2948 O ARG A 369 31.064 -20.652 66.313 1.00 16.39 A O ANISOU 2948 O ARG A 369 2487 1627 2113 -6 298 320 A O ATOM 2949 CB ARG A 369 31.391 -21.078 69.639 1.00 17.69 A C ANISOU 2949 CB ARG A 369 2900 1877 1940 191 745 326 A C ATOM 2950 CG ARG A 369 29.882 -21.025 69.495 1.00 17.49 A C ANISOU 2950 CG ARG A 369 2932 1890 1823 198 583 -61 A C ATOM 2951 CD ARG A 369 29.409 -19.652 69.063 1.00 22.14 A C ANISOU 2951 CD ARG A 369 3773 2046 2591 467 601 10 A C ATOM 2952 NE ARG A 369 29.524 -18.643 70.105 1.00 22.19 A N ANISOU 2952 NE ARG A 369 3891 1991 2548 207 550 143 A N ATOM 2953 CZ ARG A 369 29.042 -17.406 70.001 1.00 23.69 A C ANISOU 2953 CZ ARG A 369 4082 2135 2783 521 -112 35 A C ATOM 2954 NH1 ARG A 369 28.576 -16.966 68.827 1.00 21.07 A N ANISOU 2954 NH1 ARG A 369 2908 2065 3032 -12 18 243 A N ATOM 2955 NH2 ARG A 369 29.052 -16.648 71.086 1.00 21.35 A N ANISOU 2955 NH2 ARG A 369 3332 2180 2600 -44 795 45 A N ATOM 2956 N PRO A 370 32.369 -19.116 67.272 1.00 15.48 A N ANISOU 2956 N PRO A 370 2820 1527 1536 127 368 113 A N ATOM 2957 CA PRO A 370 31.984 -18.115 66.270 1.00 16.93 A C ANISOU 2957 CA PRO A 370 3159 1749 1525 60 259 166 A C ATOM 2958 C PRO A 370 32.503 -18.331 64.838 1.00 14.98 A C ANISOU 2958 C PRO A 370 2399 1533 1759 250 290 -1 A C ATOM 2959 O PRO A 370 32.147 -17.615 63.931 1.00 14.80 A O ANISOU 2959 O PRO A 370 2595 1477 1552 69 438 0 A O ATOM 2960 CB PRO A 370 32.531 -16.815 66.843 1.00 18.76 A C ANISOU 2960 CB PRO A 370 3373 1575 2179 83 516 -276 A C ATOM 2961 CG PRO A 370 33.611 -17.187 67.805 1.00 20.91 A C ANISOU 2961 CG PRO A 370 3155 1381 3406 73 14 -26 A C ATOM 2962 CD PRO A 370 33.304 -18.589 68.285 1.00 17.29 A C ANISOU 2962 CD PRO A 370 2837 1828 1903 111 232 240 A C ATOM 2963 N LEU A 371 33.292 -19.381 64.641 1.00 14.14 A N ANISOU 2963 N LEU A 371 2189 1492 1689 282 164 95 A N ATOM 2964 CA LEU A 371 33.763 -19.787 63.310 1.00 15.29 A C ANISOU 2964 CA LEU A 371 2231 1743 1833 -67 353 32 A C ATOM 2965 C LEU A 371 32.644 -20.475 62.537 1.00 13.75 A C ANISOU 2965 C LEU A 371 1947 1567 1710 146 431 150 A C ATOM 2966 O LEU A 371 32.758 -20.639 61.323 1.00 13.95 A O ANISOU 2966 O LEU A 371 2200 1435 1665 -73 340 40 A O ATOM 2967 CB LEU A 371 34.982 -20.702 63.427 1.00 15.59 A C ANISOU 2967 CB LEU A 371 2486 1738 1697 163 287 -76 A C ATOM 2968 CG LEU A 371 36.213 -20.081 64.085 1.00 16.88 A C ANISOU 2968 CG LEU A 371 2451 1989 1972 46 170 388 A C ATOM 2969 CD1 LEU A 371 37.334 -21.107 64.161 1.00 20.40 A C ANISOU 2969 CD1 LEU A 371 2920 2664 2164 607 243 141 A C ATOM 2970 CD2 LEU A 371 36.671 -18.817 63.374 1.00 19.22 A C ANISOU 2970 CD2 LEU A 371 2743 2392 2165 -222 440 627 A C ATOM 2971 N ARG A 372 31.594 -20.907 63.250 1.00 13.80 A N ANISOU 2971 N ARG A 372 2166 1477 1600 -52 517 29 A N ATOM 2972 CA ARG A 372 30.456 -21.581 62.597 1.00 14.40 A C ANISOU 2972 CA ARG A 372 2045 1805 1622 -74 635 63 A C ATOM 2973 C ARG A 372 30.976 -22.828 61.865 1.00 16.09 A C ANISOU 2973 C ARG A 372 2592 1558 1963 -205 390 148 A C ATOM 2974 O ARG A 372 31.688 -23.592 62.480 1.00 17.84 A O ANISOU 2974 O ARG A 372 2918 1746 2113 13 187 23 A O ATOM 2975 CB ARG A 372 29.664 -20.615 61.709 1.00 15.02 A C ANISOU 2975 CB ARG A 372 2375 1478 1853 3 266 -102 A C ATOM 2976 CG ARG A 372 29.111 -19.389 62.437 1.00 15.36 A C ANISOU 2976 CG ARG A 372 2308 1868 1660 197 398 -138 A C ATOM 2977 CD ARG A 372 28.140 -18.582 61.603 1.00 15.19 A C ANISOU 2977 CD ARG A 372 2282 1610 1878 -85 197 -161 A C ATOM 2978 NE ARG A 372 28.720 -18.139 60.351 1.00 14.51 A N ANISOU 2978 NE ARG A 372 2143 1444 1925 28 459 7 A N ATOM 2979 CZ ARG A 372 28.507 -16.966 59.778 1.00 14.01 A C ANISOU 2979 CZ ARG A 372 2127 1360 1835 151 250 -198 A C ATOM 2980 NH1 ARG A 372 27.716 -16.061 60.367 1.00 16.04 A N ANISOU 2980 NH1 ARG A 372 2408 1813 1872 227 463 -319 A N ATOM 2981 NH2 ARG A 372 29.090 -16.716 58.621 1.00 13.79 A N ANISOU 2981 NH2 ARG A 372 2016 1408 1814 -101 252 -49 A N ATOM 2982 N GLN A 373 30.605 -23.011 60.588 1.00 14.71 A N ANISOU 2982 N GLN A 373 2288 1249 2052 67 394 78 A N ATOM 2983 CA GLN A 373 30.997 -24.241 59.833 1.00 14.28 A C ANISOU 2983 CA GLN A 373 2153 1198 2072 224 350 315 A C ATOM 2984 C GLN A 373 32.328 -23.984 59.099 1.00 14.88 A C ANISOU 2984 C GLN A 373 2109 1458 2084 243 144 26 A C ATOM 2985 O GLN A 373 32.396 -24.164 57.869 1.00 17.80 A O ANISOU 2985 O GLN A 373 2570 2053 2138 -223 278 -335 A O ATOM 2986 CB GLN A 373 29.880 -24.664 58.878 1.00 25.18 A C ANISOU 2986 CB GLN A 373 3419 2926 3220 -51 -79 -152 A C ATOM 2987 CG GLN A 373 28.643 -25.155 59.614 1.00 27.74 A C ANISOU 2987 CG GLN A 373 3886 3229 3423 -80 92 -81 A C ATOM 2988 CD GLN A 373 27.661 -25.853 58.708 1.00 28.52 A C ANISOU 2988 CD GLN A 373 3578 3815 3443 -211 -11 255 A C ATOM 2989 NE2 GLN A 373 28.116 -26.919 58.069 1.00 29.03 A N ANISOU 2989 NE2 GLN A 373 3913 3480 3634 -226 -257 125 A N ATOM 2990 OE1 GLN A 373 26.522 -25.426 58.580 1.00 29.94 A O ANISOU 2990 OE1 GLN A 373 3653 3934 3789 -231 179 263 A O ATOM 2991 N ALA A 374 33.352 -23.558 59.843 1.00 14.65 A N ANISOU 2991 N ALA A 374 2141 1763 1662 109 234 188 A N ATOM 2992 CA ALA A 374 34.738 -23.440 59.386 1.00 12.91 A C ANISOU 2992 CA ALA A 374 2193 952 1757 84 210 -98 A C ATOM 2993 C ALA A 374 35.632 -24.031 60.479 1.00 15.20 A C ANISOU 2993 C ALA A 374 2581 1382 1811 226 145 34 A C ATOM 2994 O ALA A 374 35.772 -23.411 61.546 1.00 17.20 A O ANISOU 2994 O ALA A 374 3033 1757 1742 399 190 60 A O ATOM 2995 CB ALA A 374 35.077 -21.986 59.140 1.00 13.32 A C ANISOU 2995 CB ALA A 374 2283 926 1849 175 309 -95 A C ATOM 2996 N LYS A 375 36.216 -25.207 60.231 1.00 14.12 A N ANISOU 2996 N LYS A 375 2446 1285 1631 85 91 -71 A N ATOM 2997 CA LYS A 375 37.000 -25.842 61.299 1.00 15.29 A C ANISOU 2997 CA LYS A 375 2299 1565 1945 345 204 135 A C ATOM 2998 C LYS A 375 38.305 -25.100 61.597 1.00 15.51 A C ANISOU 2998 C LYS A 375 2243 1603 2047 467 295 -19 A C ATOM 2999 O LYS A 375 38.807 -25.208 62.705 1.00 15.84 A O ANISOU 2999 O LYS A 375 2677 1570 1770 89 340 191 A O ATOM 3000 CB LYS A 375 37.285 -27.303 60.987 1.00 16.57 A C ANISOU 3000 CB LYS A 375 2770 1364 2161 332 35 388 A C ATOM 3001 CG LYS A 375 36.038 -28.168 60.919 1.00 20.90 A C ANISOU 3001 CG LYS A 375 2805 1985 3151 82 278 7 A C ATOM 3002 CD LYS A 375 36.343 -29.625 60.654 1.00 24.66 A C ANISOU 3002 CD LYS A 375 3169 1948 4250 210 225 261 A C ATOM 3003 CE LYS A 375 35.083 -30.403 60.341 1.00 29.86 A C ANISOU 3003 CE LYS A 375 4269 2102 4974 -433 69 -955 A C ATOM 3004 NZ LYS A 375 35.415 -31.770 59.874 1.00 36.80 A N ANISOU 3004 NZ LYS A 375 6547 1867 5566 128 434 -141 A N ATOM 3005 N ALA A 376 38.893 -24.424 60.587 1.00 14.13 A N ANISOU 3005 N ALA A 376 2275 1329 1763 275 132 -148 A N ATOM 3006 CA ALA A 376 40.188 -23.705 60.738 1.00 14.98 A C ANISOU 3006 CA ALA A 376 2324 1437 1930 126 -25 -189 A C ATOM 3007 C ALA A 376 41.211 -24.574 61.477 1.00 13.83 A C ANISOU 3007 C ALA A 376 2403 1205 1643 160 179 -290 A C ATOM 3008 O ALA A 376 41.869 -24.110 62.407 1.00 14.60 A O ANISOU 3008 O ALA A 376 2443 1340 1764 98 -50 108 A O ATOM 3009 CB ALA A 376 40.004 -22.347 61.422 1.00 15.31 A C ANISOU 3009 CB ALA A 376 2345 1522 1948 166 83 -250 A C ATOM 3010 N THR A 377 41.272 -25.855 61.060 1.00 13.02 A N ANISOU 3010 N THR A 377 2559 1195 1192 268 -130 -239 A N ATOM 3011 CA THR A 377 42.081 -26.874 61.718 1.00 14.52 A C ANISOU 3011 CA THR A 377 2269 1465 1784 369 40 -78 A C ATOM 3012 C THR A 377 42.975 -27.561 60.691 1.00 13.12 A C ANISOU 3012 C THR A 377 2319 1010 1657 284 37 259 A C ATOM 3013 O THR A 377 42.468 -28.083 59.694 1.00 15.05 A O ANISOU 3013 O THR A 377 2107 1711 1898 309 -99 -123 A O ATOM 3014 CB THR A 377 41.185 -27.871 62.443 1.00 15.96 A C ANISOU 3014 CB THR A 377 2572 1733 1759 331 -8 405 A C ATOM 3015 CG2 THR A 377 41.948 -29.026 63.060 1.00 17.23 A C ANISOU 3015 CG2 THR A 377 2789 1835 1923 505 -89 319 A C ATOM 3016 OG1 THR A 377 40.455 -27.201 63.473 1.00 17.50 A O ANISOU 3016 OG1 THR A 377 2574 1978 2094 308 197 337 A O ATOM 3017 N ASP A 378 44.280 -27.536 60.971 1.00 13.82 A N ANISOU 3017 N ASP A 378 2197 1344 1709 155 60 309 A N ATOM 3018 CA ASP A 378 45.243 -28.221 60.137 1.00 14.64 A C ANISOU 3018 CA ASP A 378 2139 1851 1569 136 41 308 A C ATOM 3019 C ASP A 378 45.783 -29.441 60.882 1.00 15.33 A C ANISOU 3019 C ASP A 378 2363 1515 1945 366 6 -28 A C ATOM 3020 O ASP A 378 45.944 -29.405 62.102 1.00 16.00 A O ANISOU 3020 O ASP A 378 2949 1172 1956 443 -59 135 A O ATOM 3021 CB ASP A 378 46.370 -27.292 59.725 1.00 13.01 A C ANISOU 3021 CB ASP A 378 2123 1112 1710 368 168 24 A C ATOM 3022 CG ASP A 378 45.895 -26.070 58.959 1.00 11.94 A C ANISOU 3022 CG ASP A 378 1765 1160 1610 179 182 139 A C ATOM 3023 OD1 ASP A 378 44.835 -26.163 58.240 1.00 13.57 A O ANISOU 3023 OD1 ASP A 378 2197 858 2098 118 -153 27 A O ATOM 3024 OD2 ASP A 378 46.582 -25.037 59.090 1.00 14.07 A O ANISOU 3024 OD2 ASP A 378 2045 1335 1964 28 -109 -53 A O ATOM 3025 N HIS A 379 46.053 -30.506 60.127 1.00 13.39 A N ANISOU 3025 N HIS A 379 2457 1422 1208 405 -88 246 A N ATOM 3026 CA HIS A 379 46.655 -31.722 60.654 1.00 14.40 A C ANISOU 3026 CA HIS A 379 2374 1360 1735 330 -138 302 A C ATOM 3027 C HIS A 379 47.928 -32.003 59.874 1.00 14.40 A C ANISOU 3027 C HIS A 379 2533 1116 1820 397 -223 -76 A C ATOM 3028 O HIS A 379 47.868 -32.034 58.635 1.00 15.91 A O ANISOU 3028 O HIS A 379 2759 1500 1783 613 -423 36 A O ATOM 3029 CB HIS A 379 45.728 -32.924 60.516 1.00 15.75 A C ANISOU 3029 CB HIS A 379 2699 1307 1978 225 -44 437 A C ATOM 3030 CG HIS A 379 44.516 -32.901 61.388 1.00 17.36 A C ANISOU 3030 CG HIS A 379 2675 1504 2415 -14 109 275 A C ATOM 3031 CD2 HIS A 379 44.266 -33.503 62.570 1.00 20.52 A C ANISOU 3031 CD2 HIS A 379 3051 2296 2450 267 176 574 A C ATOM 3032 ND1 HIS A 379 43.373 -32.229 61.048 1.00 21.19 A N ANISOU 3032 ND1 HIS A 379 2921 2020 3110 419 207 -241 A N ATOM 3033 CE1 HIS A 379 42.448 -32.433 61.974 1.00 20.88 A C ANISOU 3033 CE1 HIS A 379 2690 2206 3035 419 151 -41 A C ATOM 3034 NE2 HIS A 379 42.971 -33.214 62.930 1.00 21.22 A N ANISOU 3034 NE2 HIS A 379 2916 2605 2542 10 188 131 A N ATOM 3035 N PHE A 380 49.022 -32.276 60.590 1.00 14.67 A N ANISOU 3035 N PHE A 380 2376 1541 1656 311 -110 290 A N ATOM 3036 CA PHE A 380 50.267 -32.609 59.947 1.00 15.14 A C ANISOU 3036 CA PHE A 380 2318 1574 1860 458 -185 680 A C ATOM 3037 C PHE A 380 50.749 -33.941 60.510 1.00 16.01 A C ANISOU 3037 C PHE A 380 3275 1151 1654 352 -97 393 A C ATOM 3038 O PHE A 380 51.018 -34.031 61.707 1.00 16.55 A O ANISOU 3038 O PHE A 380 3132 1548 1606 653 -285 191 A O ATOM 3039 CB PHE A 380 51.322 -31.523 60.180 1.00 16.38 A C ANISOU 3039 CB PHE A 380 2254 1860 2110 334 -179 323 A C ATOM 3040 CG PHE A 380 52.669 -31.806 59.584 1.00 15.48 A C ANISOU 3040 CG PHE A 380 2329 1448 2103 423 -332 352 A C ATOM 3041 CD1 PHE A 380 52.939 -31.523 58.254 1.00 14.58 A C ANISOU 3041 CD1 PHE A 380 2077 1368 2096 191 -374 256 A C ATOM 3042 CD2 PHE A 380 53.643 -32.430 60.343 1.00 17.02 A C ANISOU 3042 CD2 PHE A 380 2314 2453 1696 458 -299 624 A C ATOM 3043 CE1 PHE A 380 54.160 -31.828 57.689 1.00 14.56 A C ANISOU 3043 CE1 PHE A 380 2206 1667 1655 203 -279 350 A C ATOM 3044 CE2 PHE A 380 54.873 -32.713 59.793 1.00 16.55 A C ANISOU 3044 CE2 PHE A 380 2219 1925 2144 290 -289 529 A C ATOM 3045 CZ PHE A 380 55.128 -32.430 58.463 1.00 16.69 A C ANISOU 3045 CZ PHE A 380 2149 2050 2141 429 -246 512 A C ATOM 3046 N THR A 381 50.855 -34.936 59.633 1.00 14.46 A N ANISOU 3046 N THR A 381 2433 1525 1536 429 -190 244 A N ATOM 3047 CA THR A 381 51.370 -36.246 60.066 1.00 14.88 A C ANISOU 3047 CA THR A 381 2277 1680 1695 551 -238 380 A C ATOM 3048 C THR A 381 52.865 -36.315 59.731 1.00 14.39 A C ANISOU 3048 C THR A 381 2314 1278 1874 481 -64 311 A C ATOM 3049 O THR A 381 53.292 -36.146 58.550 1.00 15.00 A O ANISOU 3049 O THR A 381 2512 1308 1878 593 10 412 A O ATOM 3050 CB THR A 381 50.603 -37.415 59.481 1.00 14.52 A C ANISOU 3050 CB THR A 381 2490 1275 1751 309 2 690 A C ATOM 3051 CG2 THR A 381 51.189 -38.753 59.911 1.00 16.99 A C ANISOU 3051 CG2 THR A 381 3102 1240 2111 546 -69 442 A C ATOM 3052 OG1 THR A 381 49.241 -37.296 59.884 1.00 17.60 A O ANISOU 3052 OG1 THR A 381 2638 1557 2490 234 109 320 A O ATOM 3053 N LEU A 382 53.654 -36.565 60.784 1.00 16.14 A N ANISOU 3053 N LEU A 382 2522 1969 1639 366 -180 207 A N ATOM 3054 CA LEU A 382 55.120 -36.599 60.744 1.00 16.32 A C ANISOU 3054 CA LEU A 382 2408 1856 1936 257 -242 308 A C ATOM 3055 C LEU A 382 55.605 -37.874 60.037 1.00 16.98 A C ANISOU 3055 C LEU A 382 2577 2070 1803 126 -185 90 A C ATOM 3056 O LEU A 382 54.903 -38.907 60.003 1.00 17.21 A O ANISOU 3056 O LEU A 382 2355 1734 2449 594 -152 588 A O ATOM 3057 CB LEU A 382 55.649 -36.598 62.182 1.00 19.17 A C ANISOU 3057 CB LEU A 382 3176 2030 2076 748 -417 -34 A C ATOM 3058 CG LEU A 382 55.402 -35.303 62.948 1.00 18.00 A C ANISOU 3058 CG LEU A 382 2959 1900 1979 472 -710 56 A C ATOM 3059 CD1 LEU A 382 55.133 -35.576 64.421 1.00 22.09 A C ANISOU 3059 CD1 LEU A 382 3560 2763 2069 554 -492 158 A C ATOM 3060 CD2 LEU A 382 56.569 -34.360 62.768 1.00 19.37 A C ANISOU 3060 CD2 LEU A 382 2760 2482 2114 391 -547 31 A C ATOM 3061 N SER A 383 56.822 -37.813 59.501 1.00 17.43 A N ANISOU 3061 N SER A 383 2556 1790 2274 696 -414 175 A N ATOM 3062 CA SER A 383 57.428 -38.940 58.782 1.00 19.43 A C ANISOU 3062 CA SER A 383 2670 2193 2517 980 -372 43 A C ATOM 3063 C SER A 383 58.543 -39.619 59.592 1.00 21.61 A C ANISOU 3063 C SER A 383 3296 2373 2541 966 -728 269 A C ATOM 3064 O SER A 383 58.957 -40.712 59.197 1.00 23.60 A O ANISOU 3064 O SER A 383 3678 2279 3008 952 -384 58 A O ATOM 3065 CB SER A 383 57.998 -38.501 57.468 1.00 20.37 A C ANISOU 3065 CB SER A 383 2461 2502 2775 964 -280 281 A C ATOM 3066 OG SER A 383 59.148 -37.705 57.690 1.00 21.71 A O ANISOU 3066 OG SER A 383 2657 2278 3310 945 -137 262 A O ATOM 3067 N GLY A 384 59.016 -38.963 60.660 1.00 22.18 A N ANISOU 3067 N GLY A 384 2690 2990 2746 1297 -1050 90 A N ATOM 3068 CA GLY A 384 60.228 -39.330 61.490 1.00 25.71 A C ANISOU 3068 CA GLY A 384 2992 3836 2941 2140 -822 780 A C ATOM 3069 C GLY A 384 61.520 -39.371 60.713 1.00 31.65 A C ANISOU 3069 C GLY A 384 2938 4814 4271 1396 -777 674 A C ATOM 3070 O GLY A 384 62.512 -39.957 61.217 1.00 46.43 A O ANISOU 3070 O GLY A 384 4567 8176 4899 3447 -1618 -110 A O ATOM 3071 N AGLU A 385 61.496 -38.802 59.493 0.50 30.95 A N ANISOU 3071 N AGLU A 385 3404 4752 3601 1274 -260 -225 A N ATOM 3072 N BGLU A 385 61.580 -38.758 59.529 0.50 31.22 A N ANISOU 3072 N BGLU A 385 3655 4635 3572 1330 -215 -275 A N ATOM 3073 CA AGLU A 385 62.663 -38.668 58.610 0.50 31.43 A C ANISOU 3073 CA AGLU A 385 3483 4738 3720 1082 -138 -439 A C ATOM 3074 CA BGLU A 385 62.735 -38.975 58.649 0.50 29.09 A C ANISOU 3074 CA BGLU A 385 3194 4182 3675 1043 -463 -756 A C ATOM 3075 C AGLU A 385 63.269 -37.284 58.836 0.50 34.44 A C ANISOU 3075 C AGLU A 385 4254 4684 4147 1102 12 -529 A C ATOM 3076 C BGLU A 385 63.868 -38.028 59.035 0.50 29.53 A C ANISOU 3076 C BGLU A 385 4060 3954 3205 742 -777 -735 A C ATOM 3077 O AGLU A 385 63.263 -36.420 57.936 0.50 39.89 A O ANISOU 3077 O AGLU A 385 3463 7664 4028 43 1441 437 A O ATOM 3078 O BGLU A 385 65.029 -38.338 58.861 0.50 33.95 A O ANISOU 3078 O BGLU A 385 3720 5435 3744 -72 -486 -657 A O ATOM 3079 CB AGLU A 385 62.293 -38.785 57.130 0.50 29.92 A C ANISOU 3079 CB AGLU A 385 3567 4079 3721 1030 -264 -354 A C ATOM 3080 CB BGLU A 385 62.302 -38.826 57.197 0.50 29.49 A C ANISOU 3080 CB BGLU A 385 3555 4036 3612 1086 -373 -418 A C ATOM 3081 CG GLU A 385 61.602 -40.082 56.753 1.00 28.39 A C ANISOU 3081 CG GLU A 385 3162 3912 3711 1146 -254 -332 A C ATOM 3082 CD GLU A 385 61.058 -40.169 55.337 1.00 25.11 A C ANISOU 3082 CD GLU A 385 2997 3137 3403 1410 -288 279 A C ATOM 3083 OE1 GLU A 385 61.231 -39.261 54.484 1.00 28.38 A O ANISOU 3083 OE1 GLU A 385 3611 4058 3114 851 -952 541 A O ATOM 3084 OE2 GLU A 385 60.377 -41.146 55.107 1.00 29.50 A O ANISOU 3084 OE2 GLU A 385 4434 3263 3510 1328 -1259 140 A O ATOM 3085 N AGLY A 386 63.708 -37.059 60.078 0.50 27.39 A N ANISOU 3085 N AGLY A 386 3034 2928 4443 2409 -1032 196 A N ATOM 3086 N BGLY A 386 63.472 -36.891 59.597 0.50 31.31 A N ANISOU 3086 N BGLY A 386 3439 4377 4080 1438 -1123 -1079 A N ATOM 3087 CA AGLY A 386 64.440 -35.877 60.431 0.50 29.99 A C ANISOU 3087 CA AGLY A 386 3173 3873 4348 1527 -965 -111 A C ATOM 3088 CA BGLY A 386 64.345 -35.854 60.076 0.50 28.30 A C ANISOU 3088 CA BGLY A 386 2535 4466 3748 1542 -1597 -615 A C ATOM 3089 C AGLY A 386 63.528 -34.679 60.622 0.50 25.62 A C ANISOU 3089 C AGLY A 386 2861 3362 3511 1106 -1050 31 A C ATOM 3090 C BGLY A 386 63.520 -34.675 60.567 0.50 25.65 A C ANISOU 3090 C BGLY A 386 2816 3514 3414 1049 -1299 -219 A C ATOM 3091 O AGLY A 386 62.309 -34.824 60.780 0.50 23.21 A O ANISOU 3091 O AGLY A 386 3021 2764 3030 584 -974 -179 A O ATOM 3092 O BGLY A 386 62.341 -34.836 60.903 0.50 24.76 A O ANISOU 3092 O BGLY A 386 3234 3004 3170 668 -848 -348 A O ATOM 3093 N VAL A 387 64.143 -33.495 60.600 1.00 23.87 A N ANISOU 3093 N VAL A 387 2642 3379 3047 1089 -1208 -206 A N ATOM 3094 CA VAL A 387 63.437 -32.267 60.837 1.00 24.31 A C ANISOU 3094 CA VAL A 387 2942 3241 3052 1135 -1267 31 A C ATOM 3095 C VAL A 387 62.640 -31.914 59.577 1.00 25.63 A C ANISOU 3095 C VAL A 387 2503 4754 2480 713 -831 253 A C ATOM 3096 O VAL A 387 63.176 -31.870 58.486 1.00 28.19 A O ANISOU 3096 O VAL A 387 2594 5345 2772 630 -523 626 A O ATOM 3097 CB VAL A 387 64.403 -31.138 61.194 1.00 27.58 A C ANISOU 3097 CB VAL A 387 2770 4026 3680 674 -921 -50 A C ATOM 3098 CG1 VAL A 387 63.671 -29.804 61.330 1.00 28.11 A C ANISOU 3098 CG1 VAL A 387 2490 3984 4205 723 -1477 668 A C ATOM 3099 CG2 VAL A 387 65.157 -31.474 62.466 1.00 25.62 A C ANISOU 3099 CG2 VAL A 387 2768 3392 3572 905 -1009 -244 A C ATOM 3100 N GLN A 388 61.355 -31.653 59.749 1.00 20.47 A N ANISOU 3100 N GLN A 388 2425 2855 2496 439 -666 -190 A N ATOM 3101 CA GLN A 388 60.479 -31.355 58.607 1.00 18.42 A C ANISOU 3101 CA GLN A 388 2376 2142 2480 344 -675 61 A C ATOM 3102 C GLN A 388 60.029 -29.891 58.706 1.00 17.10 A C ANISOU 3102 C GLN A 388 1913 2294 2290 233 -121 69 A C ATOM 3103 O GLN A 388 59.856 -29.396 59.784 1.00 19.88 A O ANISOU 3103 O GLN A 388 3143 2327 2080 422 -562 179 A O ATOM 3104 CB GLN A 388 59.273 -32.288 58.638 1.00 18.67 A C ANISOU 3104 CB GLN A 388 2462 2207 2424 542 -453 138 A C ATOM 3105 CG GLN A 388 59.663 -33.766 58.602 1.00 19.17 A C ANISOU 3105 CG GLN A 388 2380 2132 2769 583 -638 99 A C ATOM 3106 CD GLN A 388 58.450 -34.662 58.651 1.00 18.77 A C ANISOU 3106 CD GLN A 388 2627 1904 2600 455 -470 66 A C ATOM 3107 NE2 GLN A 388 57.727 -34.730 57.534 1.00 17.88 A N ANISOU 3107 NE2 GLN A 388 2534 1967 2289 790 -367 319 A N ATOM 3108 OE1 GLN A 388 58.148 -35.258 59.697 1.00 20.21 A O ANISOU 3108 OE1 GLN A 388 2759 2435 2485 304 -901 119 A O ATOM 3109 N GLU A 389 59.868 -29.226 57.554 1.00 18.49 A N ANISOU 3109 N GLU A 389 2309 2319 2396 593 -300 167 A N ATOM 3110 CA AGLU A 389 59.317 -27.871 57.488 0.30 18.27 A C ANISOU 3110 CA AGLU A 389 2113 2525 2303 758 -467 -29 A C ATOM 3111 CA BGLU A 389 59.302 -27.904 57.507 0.70 18.20 A C ANISOU 3111 CA BGLU A 389 2168 2583 2163 766 -431 -95 A C ATOM 3112 C GLU A 389 58.004 -27.953 56.700 1.00 18.49 A C ANISOU 3112 C GLU A 389 2026 2596 2400 608 -431 19 A C ATOM 3113 O GLU A 389 57.946 -28.597 55.642 1.00 21.37 A O ANISOU 3113 O GLU A 389 2545 2943 2628 945 -528 -166 A O ATOM 3114 CB AGLU A 389 60.312 -26.878 56.874 0.30 19.68 A C ANISOU 3114 CB AGLU A 389 1982 2802 2692 586 -571 42 A C ATOM 3115 CB BGLU A 389 60.280 -26.924 56.891 0.70 20.95 A C ANISOU 3115 CB BGLU A 389 2289 2341 3328 678 -397 195 A C ATOM 3116 CG AGLU A 389 59.840 -25.422 56.904 0.30 20.17 A C ANISOU 3116 CG AGLU A 389 2174 2874 2615 692 -585 145 A C ATOM 3117 CG BGLU A 389 61.510 -26.736 57.734 0.70 26.63 A C ANISOU 3117 CG BGLU A 389 2651 3324 4142 -115 -636 458 A C ATOM 3118 CD AGLU A 389 60.833 -24.375 56.415 0.30 22.70 A C ANISOU 3118 CD AGLU A 389 2383 3399 2843 790 -217 606 A C ATOM 3119 CD BGLU A 389 62.428 -25.638 57.252 0.70 34.59 A C ANISOU 3119 CD BGLU A 389 3598 4200 5343 -915 -830 1275 A C ATOM 3120 OE1AGLU A 389 61.936 -24.319 56.966 0.30 30.55 A O ANISOU 3120 OE1AGLU A 389 2924 5924 2758 -817 -696 -66 A O ATOM 3121 OE1BGLU A 389 62.368 -25.303 56.057 0.70 50.82 A O ANISOU 3121 OE1BGLU A 389 6452 7925 4930 -2499 -201 1221 A O ATOM 3122 OE2AGLU A 389 60.496 -23.613 55.471 0.30 29.82 A O ANISOU 3122 OE2AGLU A 389 3034 5750 2543 539 -627 1395 A O ATOM 3123 OE2BGLU A 389 63.179 -25.116 58.079 0.70 52.56 A O ANISOU 3123 OE2BGLU A 389 4542 7576 7852 -2090 -1996 501 A O ATOM 3124 N TRP A 390 56.977 -27.266 57.206 1.00 15.90 A N ANISOU 3124 N TRP A 390 2041 1740 2258 493 -644 -186 A N ATOM 3125 CA TRP A 390 55.664 -27.294 56.551 1.00 13.76 A C ANISOU 3125 CA TRP A 390 2003 1322 1904 302 -468 23 A C ATOM 3126 C TRP A 390 54.962 -25.964 56.746 1.00 13.76 A C ANISOU 3126 C TRP A 390 1691 1632 1902 390 -228 -48 A C ATOM 3127 O TRP A 390 54.989 -25.367 57.819 1.00 14.74 A O ANISOU 3127 O TRP A 390 2193 1776 1629 364 -560 193 A O ATOM 3128 CB TRP A 390 54.835 -28.464 57.080 1.00 16.10 A C ANISOU 3128 CB TRP A 390 2288 1656 2171 352 -156 299 A C ATOM 3129 CG TRP A 390 53.398 -28.508 56.646 1.00 15.26 A C ANISOU 3129 CG TRP A 390 2301 1363 2135 11 24 425 A C ATOM 3130 CD1 TRP A 390 52.904 -29.072 55.507 1.00 16.99 A C ANISOU 3130 CD1 TRP A 390 2526 1448 2480 385 -420 312 A C ATOM 3131 CD2 TRP A 390 52.268 -27.954 57.333 1.00 15.77 A C ANISOU 3131 CD2 TRP A 390 2119 1768 2103 206 -240 588 A C ATOM 3132 CE2 TRP A 390 51.127 -28.237 56.555 1.00 16.80 A C ANISOU 3132 CE2 TRP A 390 2471 1643 2267 86 -340 615 A C ATOM 3133 CE3 TRP A 390 52.116 -27.191 58.500 1.00 17.67 A C ANISOU 3133 CE3 TRP A 390 2304 2270 2138 705 -350 467 A C ATOM 3134 NE1 TRP A 390 51.541 -28.942 55.455 1.00 16.34 A N ANISOU 3134 NE1 TRP A 390 2512 1373 2321 -94 -592 374 A N ATOM 3135 CZ2 TRP A 390 49.854 -27.846 56.955 1.00 17.84 A C ANISOU 3135 CZ2 TRP A 390 2355 1950 2472 -39 -444 465 A C ATOM 3136 CZ3 TRP A 390 50.854 -26.800 58.890 1.00 19.18 A C ANISOU 3136 CZ3 TRP A 390 2275 2713 2297 355 -151 464 A C ATOM 3137 CH2 TRP A 390 49.741 -27.126 58.122 1.00 18.34 A C ANISOU 3137 CH2 TRP A 390 2093 2443 2429 288 -41 552 A C ATOM 3138 N GLU A 391 54.233 -25.623 55.684 1.00 13.77 A N ANISOU 3138 N GLU A 391 2146 1125 1962 372 -348 -67 A N ATOM 3139 CA GLU A 391 53.179 -24.629 55.688 1.00 12.48 A C ANISOU 3139 CA GLU A 391 1657 1376 1706 287 -346 108 A C ATOM 3140 C GLU A 391 52.052 -25.215 54.848 1.00 13.53 A C ANISOU 3140 C GLU A 391 1633 1683 1823 298 -399 15 A C ATOM 3141 O GLU A 391 52.333 -25.937 53.872 1.00 13.69 A O ANISOU 3141 O GLU A 391 1815 1480 1905 453 -408 -17 A O ATOM 3142 CB GLU A 391 53.585 -23.295 55.037 1.00 14.57 A C ANISOU 3142 CB GLU A 391 1762 1104 2668 280 -230 51 A C ATOM 3143 CG GLU A 391 54.633 -22.524 55.796 1.00 14.78 A C ANISOU 3143 CG GLU A 391 2048 1417 2151 238 -199 2 A C ATOM 3144 CD GLU A 391 55.135 -21.243 55.126 1.00 15.58 A C ANISOU 3144 CD GLU A 391 2009 1701 2210 224 -292 298 A C ATOM 3145 OE1 GLU A 391 54.391 -20.595 54.323 1.00 15.76 A O ANISOU 3145 OE1 GLU A 391 1834 1623 2529 313 -358 256 A O ATOM 3146 OE2 GLU A 391 56.277 -20.883 55.448 1.00 17.73 A O ANISOU 3146 OE2 GLU A 391 1968 1878 2888 318 -531 395 A O ATOM 3147 N PRO A 392 50.779 -24.913 55.162 1.00 12.11 A N ANISOU 3147 N PRO A 392 1815 924 1862 229 -117 -53 A N ATOM 3148 CA PRO A 392 49.692 -25.360 54.295 1.00 13.25 A C ANISOU 3148 CA PRO A 392 1985 1073 1975 31 -184 108 A C ATOM 3149 C PRO A 392 49.767 -24.653 52.946 1.00 13.04 A C ANISOU 3149 C PRO A 392 1682 1528 1742 200 -231 100 A C ATOM 3150 O PRO A 392 50.379 -23.563 52.830 1.00 13.76 A O ANISOU 3150 O PRO A 392 1858 1464 1907 234 -163 19 A O ATOM 3151 CB PRO A 392 48.423 -25.016 55.069 1.00 13.88 A C ANISOU 3151 CB PRO A 392 1979 1180 2115 186 -269 -23 A C ATOM 3152 CG PRO A 392 48.861 -23.831 55.937 1.00 14.60 A C ANISOU 3152 CG PRO A 392 1774 1204 2568 437 -40 -400 A C ATOM 3153 CD PRO A 392 50.322 -24.071 56.281 1.00 13.18 A C ANISOU 3153 CD PRO A 392 1758 1350 1897 332 -119 -172 A C ATOM 3154 N SER A 393 49.061 -25.209 51.969 1.00 12.16 A N ANISOU 3154 N SER A 393 1703 1172 1744 53 100 -91 A N ATOM 3155 CA SER A 393 49.123 -24.736 50.588 1.00 12.08 A C ANISOU 3155 CA SER A 393 1561 1388 1639 -32 -157 -39 A C ATOM 3156 C SER A 393 47.864 -24.030 50.112 1.00 12.20 A C ANISOU 3156 C SER A 393 1734 1115 1787 41 4 111 A C ATOM 3157 O SER A 393 47.968 -23.007 49.403 1.00 13.12 A O ANISOU 3157 O SER A 393 1824 1156 2002 131 0 313 A O ATOM 3158 CB SER A 393 49.404 -25.903 49.651 1.00 13.24 A C ANISOU 3158 CB SER A 393 2037 1681 1310 175 -178 -143 A C ATOM 3159 OG SER A 393 50.716 -26.402 49.834 1.00 16.13 A O ANISOU 3159 OG SER A 393 2337 2056 1736 815 198 159 A O ATOM 3160 N PHE A 394 46.686 -24.503 50.490 1.00 10.94 A N ANISOU 3160 N PHE A 394 1591 1041 1524 57 -22 142 A N ATOM 3161 CA PHE A 394 45.442 -23.989 49.859 1.00 10.44 A C ANISOU 3161 CA PHE A 394 1423 1023 1519 -25 -40 -99 A C ATOM 3162 C PHE A 394 44.373 -23.629 50.892 1.00 10.32 A C ANISOU 3162 C PHE A 394 1724 657 1538 107 19 -50 A C ATOM 3163 O PHE A 394 43.152 -23.673 50.593 1.00 12.60 A O ANISOU 3163 O PHE A 394 1787 1254 1747 136 60 -315 A O ATOM 3164 CB PHE A 394 44.899 -24.991 48.843 1.00 10.07 A C ANISOU 3164 CB PHE A 394 1590 1054 1180 7 44 0 A C ATOM 3165 CG PHE A 394 45.928 -25.414 47.821 1.00 10.49 A C ANISOU 3165 CG PHE A 394 1511 1060 1412 62 155 -16 A C ATOM 3166 CD1 PHE A 394 46.498 -24.494 46.954 1.00 11.67 A C ANISOU 3166 CD1 PHE A 394 1764 1181 1488 143 99 90 A C ATOM 3167 CD2 PHE A 394 46.372 -26.743 47.756 1.00 11.17 A C ANISOU 3167 CD2 PHE A 394 1881 1001 1360 37 166 8 A C ATOM 3168 CE1 PHE A 394 47.448 -24.891 46.022 1.00 11.64 A C ANISOU 3168 CE1 PHE A 394 1883 966 1572 106 149 -56 A C ATOM 3169 CE2 PHE A 394 47.341 -27.127 46.837 1.00 12.64 A C ANISOU 3169 CE2 PHE A 394 1839 1131 1833 131 149 -256 A C ATOM 3170 CZ PHE A 394 47.864 -26.206 45.958 1.00 11.99 A C ANISOU 3170 CZ PHE A 394 1878 1048 1629 284 -50 -157 A C ATOM 3171 N THR A 395 44.818 -23.219 52.078 1.00 10.56 A N ANISOU 3171 N THR A 395 1454 1055 1503 130 -79 -10 A N ATOM 3172 CA THR A 395 43.894 -22.749 53.107 1.00 10.78 A C ANISOU 3172 CA THR A 395 1552 1097 1448 14 36 -2 A C ATOM 3173 C THR A 395 44.427 -21.424 53.656 1.00 11.38 A C ANISOU 3173 C THR A 395 1585 1096 1642 318 -49 -219 A C ATOM 3174 O THR A 395 45.575 -21.074 53.448 1.00 13.14 A O ANISOU 3174 O THR A 395 2021 1165 1805 -1 177 -176 A O ATOM 3175 CB THR A 395 43.725 -23.792 54.229 1.00 12.03 A C ANISOU 3175 CB THR A 395 1737 1130 1703 45 123 107 A C ATOM 3176 CG2 THR A 395 44.977 -23.947 55.054 1.00 13.11 A C ANISOU 3176 CG2 THR A 395 1714 1387 1879 224 229 257 A C ATOM 3177 OG1 THR A 395 42.675 -23.405 55.115 1.00 11.86 A O ANISOU 3177 OG1 THR A 395 1860 1053 1591 5 0 53 A O ATOM 3178 N TYR A 396 43.603 -20.755 54.476 1.00 10.57 A N ANISOU 3178 N TYR A 396 1544 982 1487 177 42 -125 A N ATOM 3179 CA TYR A 396 44.135 -19.681 55.299 1.00 10.84 A C ANISOU 3179 CA TYR A 396 1643 902 1571 -3 125 -102 A C ATOM 3180 C TYR A 396 43.225 -19.533 56.511 1.00 11.60 A C ANISOU 3180 C TYR A 396 1632 1264 1510 376 -12 167 A C ATOM 3181 O TYR A 396 42.076 -19.968 56.457 1.00 10.72 A O ANISOU 3181 O TYR A 396 1639 1057 1376 255 139 -38 A O ATOM 3182 CB TYR A 396 44.297 -18.358 54.518 1.00 11.92 A C ANISOU 3182 CB TYR A 396 1937 1067 1522 170 -69 53 A C ATOM 3183 CG TYR A 396 43.052 -17.586 54.156 1.00 10.83 A C ANISOU 3183 CG TYR A 396 1888 731 1494 -2 98 -88 A C ATOM 3184 CD1 TYR A 396 42.243 -17.833 53.060 1.00 11.28 A C ANISOU 3184 CD1 TYR A 396 1784 896 1603 78 20 -162 A C ATOM 3185 CD2 TYR A 396 42.739 -16.457 54.899 1.00 11.47 A C ANISOU 3185 CD2 TYR A 396 1812 831 1712 235 -146 -214 A C ATOM 3186 CE1 TYR A 396 41.216 -16.976 52.692 1.00 11.88 A C ANISOU 3186 CE1 TYR A 396 1818 1288 1408 133 -61 -174 A C ATOM 3187 CE2 TYR A 396 41.687 -15.622 54.571 1.00 10.97 A C ANISOU 3187 CE2 TYR A 396 1764 551 1851 91 -7 -152 A C ATOM 3188 CZ TYR A 396 40.937 -15.856 53.449 1.00 11.91 A C ANISOU 3188 CZ TYR A 396 1777 1063 1685 124 -95 -70 A C ATOM 3189 OH TYR A 396 39.946 -14.993 53.051 1.00 13.09 A O ANISOU 3189 OH TYR A 396 2150 1178 1645 275 40 33 A O ATOM 3190 N HIS A 397 43.747 -18.887 57.558 1.00 11.42 A N ANISOU 3190 N HIS A 397 1612 1148 1576 88 41 51 A N ATOM 3191 CA HIS A 397 43.006 -18.740 58.801 1.00 11.29 A C ANISOU 3191 CA HIS A 397 1782 1003 1504 215 116 -27 A C ATOM 3192 C HIS A 397 43.157 -17.310 59.332 1.00 11.36 A C ANISOU 3192 C HIS A 397 1748 1097 1467 71 -62 -25 A C ATOM 3193 O HIS A 397 44.158 -16.666 59.081 1.00 12.59 A O ANISOU 3193 O HIS A 397 1908 1216 1659 98 154 -86 A O ATOM 3194 CB HIS A 397 43.513 -19.728 59.849 1.00 12.29 A C ANISOU 3194 CB HIS A 397 1844 998 1827 110 104 112 A C ATOM 3195 CG HIS A 397 43.835 -21.095 59.360 1.00 12.43 A C ANISOU 3195 CG HIS A 397 2180 1196 1344 31 159 -119 A C ATOM 3196 CD2 HIS A 397 45.021 -21.717 59.356 1.00 13.18 A C ANISOU 3196 CD2 HIS A 397 2132 950 1925 -117 166 -15 A C ATOM 3197 ND1 HIS A 397 42.915 -21.937 58.770 1.00 12.83 A N ANISOU 3197 ND1 HIS A 397 2314 877 1684 211 -113 -163 A N ATOM 3198 CE1 HIS A 397 43.544 -23.089 58.498 1.00 12.75 A C ANISOU 3198 CE1 HIS A 397 2042 913 1886 236 19 49 A C ATOM 3199 NE2 HIS A 397 44.826 -22.989 58.859 1.00 12.41 A N ANISOU 3199 NE2 HIS A 397 2040 695 1980 30 19 74 A N ATOM 3200 N GLY A 398 42.189 -16.921 60.147 1.00 10.80 A N ANISOU 3200 N GLY A 398 1789 795 1518 -104 -93 -43 A N ATOM 3201 CA GLY A 398 42.238 -15.656 60.872 1.00 12.41 A C ANISOU 3201 CA GLY A 398 2158 950 1605 180 -13 -270 A C ATOM 3202 C GLY A 398 42.322 -15.984 62.356 1.00 13.26 A C ANISOU 3202 C GLY A 398 2145 1194 1699 95 27 -98 A C ATOM 3203 O GLY A 398 41.441 -16.631 62.868 1.00 13.37 A O ANISOU 3203 O GLY A 398 2344 1436 1297 7 61 139 A O ATOM 3204 N PHE A 399 43.416 -15.602 63.035 1.00 12.21 A N ANISOU 3204 N PHE A 399 2218 1091 1327 152 -52 -211 A N ATOM 3205 CA PHE A 399 43.668 -16.105 64.377 1.00 12.92 A C ANISOU 3205 CA PHE A 399 2306 1128 1472 145 -373 -67 A C ATOM 3206 C PHE A 399 44.724 -15.298 65.129 1.00 13.65 A C ANISOU 3206 C PHE A 399 2036 1507 1641 130 -265 -76 A C ATOM 3207 O PHE A 399 45.620 -14.717 64.523 1.00 13.18 A O ANISOU 3207 O PHE A 399 2227 1236 1542 187 -351 -122 A O ATOM 3208 CB PHE A 399 44.138 -17.561 64.281 1.00 13.15 A C ANISOU 3208 CB PHE A 399 2247 1178 1570 105 -30 100 A C ATOM 3209 CG PHE A 399 45.491 -17.774 63.643 1.00 12.95 A C ANISOU 3209 CG PHE A 399 2056 1130 1731 187 -216 -10 A C ATOM 3210 CD1 PHE A 399 45.630 -17.758 62.269 1.00 12.70 A C ANISOU 3210 CD1 PHE A 399 1978 1167 1680 78 -304 210 A C ATOM 3211 CD2 PHE A 399 46.639 -17.996 64.386 1.00 12.75 A C ANISOU 3211 CD2 PHE A 399 2137 1054 1652 224 -224 124 A C ATOM 3212 CE1 PHE A 399 46.858 -17.916 61.659 1.00 13.03 A C ANISOU 3212 CE1 PHE A 399 2201 1376 1373 133 -149 -94 A C ATOM 3213 CE2 PHE A 399 47.874 -18.193 63.776 1.00 13.94 A C ANISOU 3213 CE2 PHE A 399 1973 1745 1576 118 -365 -95 A C ATOM 3214 CZ PHE A 399 47.985 -18.165 62.403 1.00 13.73 A C ANISOU 3214 CZ PHE A 399 2052 1520 1643 213 -82 -16 A C ATOM 3215 N ARG A 400 44.634 -15.369 66.473 1.00 15.08 A N ANISOU 3215 N ARG A 400 2444 1544 1738 298 -133 -26 A N ATOM 3216 CA ARG A 400 45.710 -14.978 67.375 1.00 14.27 A C ANISOU 3216 CA ARG A 400 2288 1245 1888 188 -141 37 A C ATOM 3217 C ARG A 400 46.242 -16.196 68.173 1.00 13.70 A C ANISOU 3217 C ARG A 400 2127 1587 1489 352 -50 -16 A C ATOM 3218 O ARG A 400 47.413 -16.234 68.529 1.00 15.35 A O ANISOU 3218 O ARG A 400 2249 1792 1790 406 -257 31 A O ATOM 3219 CB ARG A 400 45.201 -13.893 68.338 1.00 15.90 A C ANISOU 3219 CB ARG A 400 2597 1665 1780 331 -72 -8 A C ATOM 3220 CG ARG A 400 46.180 -13.558 69.454 1.00 16.66 A C ANISOU 3220 CG ARG A 400 2755 1678 1895 345 -127 -145 A C ATOM 3221 CD ARG A 400 45.812 -12.318 70.236 1.00 18.37 A C ANISOU 3221 CD ARG A 400 2751 2085 2141 640 -504 -500 A C ATOM 3222 NE ARG A 400 46.711 -12.224 71.374 1.00 17.87 A N ANISOU 3222 NE ARG A 400 2939 1907 1940 192 -471 -256 A N ATOM 3223 CZ ARG A 400 46.816 -11.160 72.173 1.00 17.96 A C ANISOU 3223 CZ ARG A 400 3064 1934 1826 389 -519 -348 A C ATOM 3224 NH1 ARG A 400 46.050 -10.100 71.934 1.00 18.10 A N ANISOU 3224 NH1 ARG A 400 2934 1974 1968 505 -270 -471 A N ATOM 3225 NH2 ARG A 400 47.693 -11.175 73.173 1.00 20.61 A N ANISOU 3225 NH2 ARG A 400 3220 2618 1990 246 -628 -376 A N ATOM 3226 N TYR A 401 45.341 -17.155 68.439 1.00 14.50 A N ANISOU 3226 N TYR A 401 2309 1739 1459 198 -186 254 A N ATOM 3227 CA TYR A 401 45.628 -18.322 69.268 1.00 16.11 A C ANISOU 3227 CA TYR A 401 2796 1457 1866 243 -211 180 A C ATOM 3228 C TYR A 401 45.561 -19.606 68.442 1.00 15.63 A C ANISOU 3228 C TYR A 401 2416 1811 1711 334 -282 -55 A C ATOM 3229 O TYR A 401 44.757 -19.735 67.538 1.00 14.85 A O ANISOU 3229 O TYR A 401 2463 1565 1612 373 -267 212 A O ATOM 3230 CB TYR A 401 44.628 -18.377 70.425 1.00 17.50 A C ANISOU 3230 CB TYR A 401 3031 1793 1822 134 -22 -10 A C ATOM 3231 CG TYR A 401 44.615 -17.131 71.284 1.00 16.82 A C ANISOU 3231 CG TYR A 401 2610 2012 1765 375 -188 -133 A C ATOM 3232 CD1 TYR A 401 45.552 -16.968 72.291 1.00 17.14 A C ANISOU 3232 CD1 TYR A 401 2845 1979 1688 225 -273 -213 A C ATOM 3233 CD2 TYR A 401 43.684 -16.117 71.076 1.00 17.45 A C ANISOU 3233 CD2 TYR A 401 2984 2269 1376 622 -207 -244 A C ATOM 3234 CE1 TYR A 401 45.560 -15.823 73.067 1.00 18.83 A C ANISOU 3234 CE1 TYR A 401 3229 2069 1856 284 -818 -205 A C ATOM 3235 CE2 TYR A 401 43.699 -14.961 71.840 1.00 20.98 A C ANISOU 3235 CE2 TYR A 401 3671 2274 2025 323 -254 -422 A C ATOM 3236 CZ TYR A 401 44.646 -14.814 72.832 1.00 18.67 A C ANISOU 3236 CZ TYR A 401 3211 1873 2009 293 -143 -339 A C ATOM 3237 OH TYR A 401 44.669 -13.718 73.655 1.00 22.91 A O ANISOU 3237 OH TYR A 401 4450 2197 2058 202 -398 -642 A O ATOM 3238 N VAL A 402 46.360 -20.581 68.866 1.00 15.97 A N ANISOU 3238 N VAL A 402 2839 1735 1493 380 -411 -140 A N ATOM 3239 CA VAL A 402 46.329 -21.907 68.255 1.00 15.60 A C ANISOU 3239 CA VAL A 402 2560 1629 1738 481 -327 25 A C ATOM 3240 C VAL A 402 46.426 -22.947 69.369 1.00 15.33 A C ANISOU 3240 C VAL A 402 2454 1590 1778 277 -33 109 A C ATOM 3241 O VAL A 402 47.414 -22.976 70.093 1.00 18.22 A O ANISOU 3241 O VAL A 402 2827 2245 1848 543 -270 301 A O ATOM 3242 CB VAL A 402 47.464 -22.104 67.245 1.00 15.65 A C ANISOU 3242 CB VAL A 402 2502 1504 1940 346 -227 205 A C ATOM 3243 CG1 VAL A 402 47.247 -23.425 66.520 1.00 16.73 A C ANISOU 3243 CG1 VAL A 402 2705 1352 2298 275 -225 219 A C ATOM 3244 CG2 VAL A 402 47.541 -20.947 66.282 1.00 16.57 A C ANISOU 3244 CG2 VAL A 402 3088 1578 1628 -40 -367 32 A C ATOM 3245 N GLN A 403 45.419 -23.816 69.454 1.00 14.86 A N ANISOU 3245 N GLN A 403 2538 1596 1511 270 -162 322 A N ATOM 3246 CA GLN A 403 45.528 -25.006 70.308 1.00 17.52 A C ANISOU 3246 CA GLN A 403 3252 1525 1879 423 -404 363 A C ATOM 3247 C GLN A 403 46.279 -26.078 69.520 1.00 18.31 A C ANISOU 3247 C GLN A 403 3042 1800 2116 359 -527 87 A C ATOM 3248 O GLN A 403 45.911 -26.373 68.373 1.00 16.99 A O ANISOU 3248 O GLN A 403 2952 1636 1868 334 -313 350 A O ATOM 3249 CB GLN A 403 44.170 -25.537 70.736 1.00 17.49 A C ANISOU 3249 CB GLN A 403 3185 1684 1776 460 -41 410 A C ATOM 3250 CG GLN A 403 44.311 -26.718 71.694 1.00 19.82 A C ANISOU 3250 CG GLN A 403 3250 2026 2254 439 -21 790 A C ATOM 3251 CD GLN A 403 42.990 -27.266 72.172 1.00 20.55 A C ANISOU 3251 CD GLN A 403 3077 2146 2584 330 -18 526 A C ATOM 3252 NE2 GLN A 403 42.868 -28.587 72.101 1.00 22.36 A N ANISOU 3252 NE2 GLN A 403 3764 2218 2512 78 -154 590 A N ATOM 3253 OE1 GLN A 403 42.096 -26.523 72.606 1.00 22.14 A O ANISOU 3253 OE1 GLN A 403 3886 2307 2217 600 587 779 A O ATOM 3254 N VAL A 404 47.305 -26.653 70.156 1.00 17.14 A N ANISOU 3254 N VAL A 404 2944 1968 1601 506 -375 30 A N ATOM 3255 CA VAL A 404 48.177 -27.613 69.492 1.00 17.99 A C ANISOU 3255 CA VAL A 404 3175 2147 1512 639 -9 374 A C ATOM 3256 C VAL A 404 48.089 -28.939 70.227 1.00 20.45 A C ANISOU 3256 C VAL A 404 3752 2063 1955 157 -478 344 A C ATOM 3257 O VAL A 404 48.353 -28.951 71.441 1.00 20.71 A O ANISOU 3257 O VAL A 404 3611 2355 1903 855 -442 354 A O ATOM 3258 CB VAL A 404 49.633 -27.125 69.471 1.00 18.39 A C ANISOU 3258 CB VAL A 404 3024 2104 1859 733 -178 692 A C ATOM 3259 CG1 VAL A 404 50.513 -28.125 68.763 1.00 20.73 A C ANISOU 3259 CG1 VAL A 404 3267 2013 2594 683 -214 424 A C ATOM 3260 CG2 VAL A 404 49.761 -25.748 68.835 1.00 18.60 A C ANISOU 3260 CG2 VAL A 404 2848 1943 2272 319 -389 534 A C ATOM 3261 N ASP A 405 47.680 -29.998 69.508 1.00 17.21 A N ANISOU 3261 N ASP A 405 3257 1947 1333 359 -340 410 A N ATOM 3262 CA ASP A 405 47.618 -31.354 70.084 1.00 18.99 A C ANISOU 3262 CA ASP A 405 3509 1956 1749 551 -214 509 A C ATOM 3263 C ASP A 405 48.551 -32.260 69.300 1.00 20.20 A C ANISOU 3263 C ASP A 405 3450 2079 2145 759 -436 491 A C ATOM 3264 O ASP A 405 48.621 -32.189 68.070 1.00 22.03 A O ANISOU 3264 O ASP A 405 4037 2132 2200 590 -291 789 A O ATOM 3265 CB ASP A 405 46.179 -31.887 70.090 1.00 20.20 A C ANISOU 3265 CB ASP A 405 3692 1755 2226 481 246 454 A C ATOM 3266 CG ASP A 405 45.318 -31.231 71.159 1.00 24.81 A C ANISOU 3266 CG ASP A 405 3827 3039 2560 1129 503 567 A C ATOM 3267 OD1 ASP A 405 45.415 -31.648 72.351 1.00 33.18 A O ANISOU 3267 OD1 ASP A 405 5802 4202 2603 696 339 675 A O ATOM 3268 OD2 ASP A 405 44.623 -30.280 70.827 1.00 26.53 A O ANISOU 3268 OD2 ASP A 405 4115 2440 3524 757 384 897 A O ATOM 3269 N GLY A 406 49.220 -33.168 70.014 1.00 21.08 A N ANISOU 3269 N GLY A 406 3580 2279 2149 711 -568 594 A N ATOM 3270 CA GLY A 406 50.077 -34.148 69.361 1.00 22.13 A C ANISOU 3270 CA GLY A 406 3490 2273 2642 611 -373 405 A C ATOM 3271 C GLY A 406 51.468 -33.644 69.030 1.00 21.51 A C ANISOU 3271 C GLY A 406 3731 1996 2445 751 -343 738 A C ATOM 3272 O GLY A 406 52.205 -34.310 68.305 1.00 22.59 A O ANISOU 3272 O GLY A 406 3834 2460 2286 897 -356 403 A O ATOM 3273 N TRP A 407 51.838 -32.439 69.492 1.00 22.58 A N ANISOU 3273 N TRP A 407 3858 2272 2449 585 -548 539 A N ATOM 3274 CA TRP A 407 53.184 -31.926 69.236 1.00 19.91 A C ANISOU 3274 CA TRP A 407 3358 1843 2362 967 -396 399 A C ATOM 3275 C TRP A 407 54.213 -32.867 69.847 1.00 22.67 A C ANISOU 3275 C TRP A 407 3640 2740 2232 1112 -394 928 A C ATOM 3276 O TRP A 407 54.061 -33.280 70.994 1.00 25.99 A O ANISOU 3276 O TRP A 407 4565 3039 2269 1083 -398 1103 A O ATOM 3277 CB TRP A 407 53.344 -30.487 69.754 1.00 22.19 A C ANISOU 3277 CB TRP A 407 3562 2101 2768 804 -404 157 A C ATOM 3278 CG TRP A 407 54.669 -29.894 69.394 1.00 20.52 A C ANISOU 3278 CG TRP A 407 3329 2347 2121 719 -398 276 A C ATOM 3279 CD1 TRP A 407 55.843 -30.033 70.071 1.00 23.31 A C ANISOU 3279 CD1 TRP A 407 3482 3166 2209 803 -417 349 A C ATOM 3280 CD2 TRP A 407 54.964 -29.116 68.213 1.00 21.33 A C ANISOU 3280 CD2 TRP A 407 3010 2789 2304 813 -515 492 A C ATOM 3281 CE2 TRP A 407 56.336 -28.800 68.269 1.00 19.08 A C ANISOU 3281 CE2 TRP A 407 2998 2220 2029 774 -508 -34 A C ATOM 3282 CE3 TRP A 407 54.202 -28.646 67.137 1.00 20.03 A C ANISOU 3282 CE3 TRP A 407 3011 2380 2217 646 -533 175 A C ATOM 3283 NE1 TRP A 407 56.847 -29.375 69.419 1.00 22.90 A N ANISOU 3283 NE1 TRP A 407 3093 3226 2382 928 -554 441 A N ATOM 3284 CZ2 TRP A 407 56.958 -28.032 67.295 1.00 21.67 A C ANISOU 3284 CZ2 TRP A 407 3240 2772 2219 717 -621 75 A C ATOM 3285 CZ3 TRP A 407 54.821 -27.898 66.163 1.00 21.53 A C ANISOU 3285 CZ3 TRP A 407 2937 2329 2914 561 -271 393 A C ATOM 3286 CH2 TRP A 407 56.184 -27.606 66.234 1.00 21.53 A C ANISOU 3286 CH2 TRP A 407 3069 2505 2603 245 -728 528 A C ATOM 3287 N PRO A 408 55.263 -33.264 69.099 1.00 23.03 A N ANISOU 3287 N PRO A 408 3132 2637 2980 1010 -578 642 A N ATOM 3288 CA PRO A 408 56.189 -34.281 69.583 1.00 26.07 A C ANISOU 3288 CA PRO A 408 3635 3077 3192 1244 -581 1068 A C ATOM 3289 C PRO A 408 57.151 -33.768 70.662 1.00 27.99 A C ANISOU 3289 C PRO A 408 3971 3196 3468 1072 -884 1161 A C ATOM 3290 O PRO A 408 57.659 -32.644 70.604 1.00 30.10 A O ANISOU 3290 O PRO A 408 4515 3208 3713 1016 -773 1047 A O ATOM 3291 CB PRO A 408 56.937 -34.737 68.320 1.00 29.24 A C ANISOU 3291 CB PRO A 408 4142 3651 3315 944 -336 694 A C ATOM 3292 CG PRO A 408 56.871 -33.546 67.392 1.00 25.90 A C ANISOU 3292 CG PRO A 408 3442 2868 3530 592 -486 351 A C ATOM 3293 CD PRO A 408 55.587 -32.826 67.732 1.00 24.06 A C ANISOU 3293 CD PRO A 408 3448 2865 2828 627 -366 379 A C ATOM 3294 N ALA A 409 57.370 -34.626 71.651 1.00 35.15 A N ANISOU 3294 N ALA A 409 5820 3841 3693 699 -1536 1523 A N ATOM 3295 CA ALA A 409 58.345 -34.402 72.706 1.00 40.98 A C ANISOU 3295 CA ALA A 409 5822 5783 3964 810 -1852 1695 A C ATOM 3296 C ALA A 409 59.747 -34.151 72.118 1.00 34.41 A C ANISOU 3296 C ALA A 409 5695 4291 3088 1003 -1482 928 A C ATOM 3297 O ALA A 409 60.548 -33.418 72.711 1.00 37.18 A O ANISOU 3297 O ALA A 409 6526 3969 3632 1205 -1740 136 A O ATOM 3298 CB ALA A 409 58.318 -35.596 73.623 1.00 47.02 A C ANISOU 3298 CB ALA A 409 7029 6719 4115 622 -1725 2312 A C ATOM 3299 N ASP A 410 60.036 -34.744 70.946 1.00 35.81 A N ANISOU 3299 N ASP A 410 5762 4945 2898 1527 -1828 1087 A N ATOM 3300 CA ASP A 410 61.365 -34.652 70.303 1.00 37.66 A C ANISOU 3300 CA ASP A 410 5981 4701 3625 957 -1033 357 A C ATOM 3301 C ASP A 410 61.756 -33.198 69.984 1.00 34.44 A C ANISOU 3301 C ASP A 410 3797 4689 4597 1275 -1337 251 A C ATOM 3302 O ASP A 410 62.942 -32.906 69.907 1.00 36.82 A O ANISOU 3302 O ASP A 410 3910 5296 4782 710 -1569 1267 A O ATOM 3303 CB ASP A 410 61.430 -35.444 68.989 1.00 50.93 A C ANISOU 3303 CB ASP A 410 7548 6142 5662 839 -446 -1537 A C ATOM 3304 CG ASP A 410 60.953 -36.899 69.101 1.00 62.69 A C ANISOU 3304 CG ASP A 410 9010 6333 8477 -745 -1322 -1290 A C ATOM 3305 OD1 ASP A 410 61.875 -37.771 69.483 1.00 85.87 A O ANISOU 3305 OD1 ASP A 410 10631 9958 12036 2473 -919 -904 A O ATOM 3306 OD2 ASP A 410 59.700 -37.147 68.977 1.00 79.32 A O ANISOU 3306 OD2 ASP A 410 11984 7533 10621 -1564 -3100 2197 A O ATOM 3307 N THR A 411 60.780 -32.308 69.739 1.00 34.04 A N ANISOU 3307 N THR A 411 4558 3902 4472 1193 -1658 607 A N ATOM 3308 CA THR A 411 61.055 -30.923 69.376 1.00 31.72 A C ANISOU 3308 CA THR A 411 3996 4397 3658 206 -1197 761 A C ATOM 3309 C THR A 411 60.426 -29.977 70.404 1.00 32.04 A C ANISOU 3309 C THR A 411 3788 4020 4364 -299 -301 1025 A C ATOM 3310 O THR A 411 59.234 -30.059 70.719 1.00 33.19 A O ANISOU 3310 O THR A 411 3584 5866 3159 331 -736 1151 A O ATOM 3311 CB THR A 411 60.505 -30.590 67.982 1.00 31.56 A C ANISOU 3311 CB THR A 411 4539 3639 3813 1258 -1437 269 A C ATOM 3312 CG2 THR A 411 60.794 -29.159 67.582 1.00 32.85 A C ANISOU 3312 CG2 THR A 411 4736 3594 4149 1046 -1149 -263 A C ATOM 3313 OG1 THR A 411 61.090 -31.457 66.995 1.00 44.90 A O ANISOU 3313 OG1 THR A 411 7280 5488 4291 677 -1094 -1599 A O ATOM 3314 N PRO A 412 61.182 -29.015 70.968 1.00 32.00 A N ANISOU 3314 N PRO A 412 4061 4596 3499 676 -1630 655 A N ATOM 3315 CA PRO A 412 60.581 -28.000 71.836 1.00 32.33 A C ANISOU 3315 CA PRO A 412 3754 4906 3622 1277 -985 1040 A C ATOM 3316 C PRO A 412 59.643 -27.078 71.039 1.00 31.80 A C ANISOU 3316 C PRO A 412 4224 4801 3056 1180 -985 1087 A C ATOM 3317 O PRO A 412 59.945 -26.705 69.935 1.00 30.13 A O ANISOU 3317 O PRO A 412 4076 4425 2947 754 -1332 895 A O ATOM 3318 CB PRO A 412 61.792 -27.233 72.387 1.00 35.34 A C ANISOU 3318 CB PRO A 412 4665 4876 3883 799 -1243 926 A C ATOM 3319 CG PRO A 412 62.972 -28.138 72.122 1.00 38.30 A C ANISOU 3319 CG PRO A 412 5142 5385 4024 931 -1139 -175 A C ATOM 3320 CD PRO A 412 62.638 -28.834 70.828 1.00 34.18 A C ANISOU 3320 CD PRO A 412 4151 4612 4223 736 -883 -83 A C ATOM 3321 N LEU A 413 58.484 -26.773 71.609 1.00 32.88 A N ANISOU 3321 N LEU A 413 4521 5151 2818 1056 -1111 346 A N ATOM 3322 CA LEU A 413 57.516 -25.911 70.974 1.00 29.66 A C ANISOU 3322 CA LEU A 413 4095 4597 2575 1203 -344 23 A C ATOM 3323 C LEU A 413 57.788 -24.455 71.363 1.00 29.13 A C ANISOU 3323 C LEU A 413 3764 4830 2474 1150 -291 -604 A C ATOM 3324 O LEU A 413 57.480 -24.031 72.476 1.00 34.26 A O ANISOU 3324 O LEU A 413 5007 5704 2305 1174 -17 -499 A O ATOM 3325 CB LEU A 413 56.131 -26.384 71.403 1.00 30.99 A C ANISOU 3325 CB LEU A 413 4427 3889 3457 1300 -260 367 A C ATOM 3326 CG LEU A 413 54.961 -25.613 70.829 1.00 28.13 A C ANISOU 3326 CG LEU A 413 4489 3309 2888 1107 -412 447 A C ATOM 3327 CD1 LEU A 413 54.989 -25.559 69.305 1.00 27.41 A C ANISOU 3327 CD1 LEU A 413 5051 2371 2990 1258 -583 -17 A C ATOM 3328 CD2 LEU A 413 53.696 -26.239 71.321 1.00 30.55 A C ANISOU 3328 CD2 LEU A 413 4175 2926 4507 908 -594 548 A C ATOM 3329 N ASP A 414 58.395 -23.703 70.440 1.00 29.07 A N ANISOU 3329 N ASP A 414 3951 4020 3073 788 -1353 -264 A N ATOM 3330 CA ASP A 414 58.874 -22.344 70.734 1.00 26.87 A C ANISOU 3330 CA ASP A 414 3297 3558 3354 1355 -1419 -494 A C ATOM 3331 C ASP A 414 59.134 -21.581 69.428 1.00 25.72 A C ANISOU 3331 C ASP A 414 2873 3714 3184 729 -1776 -627 A C ATOM 3332 O ASP A 414 58.786 -22.023 68.327 1.00 25.66 A O ANISOU 3332 O ASP A 414 3726 2875 3148 885 -2076 -455 A O ATOM 3333 CB ASP A 414 60.108 -22.394 71.652 1.00 31.20 A C ANISOU 3333 CB ASP A 414 3970 4254 3628 868 -1936 -377 A C ATOM 3334 CG ASP A 414 61.357 -22.980 71.016 1.00 34.82 A C ANISOU 3334 CG ASP A 414 4125 5129 3976 799 -1732 30 A C ATOM 3335 OD1 ASP A 414 61.442 -23.006 69.772 1.00 32.10 A O ANISOU 3335 OD1 ASP A 414 4005 4122 4067 1449 -1349 -24 A O ATOM 3336 OD2 ASP A 414 62.242 -23.419 71.781 1.00 40.27 A O ANISOU 3336 OD2 ASP A 414 5725 6371 3204 1340 -2358 -261 A O ATOM 3337 N GLU A 415 59.744 -20.400 69.550 1.00 29.04 A N ANISOU 3337 N GLU A 415 4116 3470 3445 724 -2067 -900 A N ATOM 3338 CA GLU A 415 59.894 -19.509 68.410 1.00 30.18 A C ANISOU 3338 CA GLU A 415 4045 3083 4336 558 -1559 -428 A C ATOM 3339 C GLU A 415 60.802 -20.107 67.324 1.00 29.82 A C ANISOU 3339 C GLU A 415 4094 3424 3812 366 -1652 120 A C ATOM 3340 O GLU A 415 60.761 -19.653 66.194 1.00 30.94 A O ANISOU 3340 O GLU A 415 3896 3736 4124 265 -2019 665 A O ATOM 3341 CB GLU A 415 60.343 -18.111 68.851 1.00 36.02 A C ANISOU 3341 CB GLU A 415 5696 3335 4652 344 -2056 -1022 A C ATOM 3342 CG GLU A 415 61.589 -18.072 69.719 1.00 44.47 A C ANISOU 3342 CG GLU A 415 5868 5897 5129 278 -2148 -1282 A C ATOM 3343 CD GLU A 415 61.359 -18.093 71.232 1.00 53.34 A C ANISOU 3343 CD GLU A 415 7348 7866 5052 -1285 -1583 -1758 A C ATOM 3344 OE1 GLU A 415 60.404 -18.759 71.712 1.00 44.93 A O ANISOU 3344 OE1 GLU A 415 5912 6327 4829 249 -1015 -1871 A O ATOM 3345 OE2 GLU A 415 62.145 -17.452 71.940 1.00 61.31 A O ANISOU 3345 OE2 GLU A 415 8884 8449 5961 -2903 -1515 -1754 A O ATOM 3346 N ASN A 416 61.605 -21.133 67.647 1.00 28.43 A N ANISOU 3346 N ASN A 416 3406 3472 3924 352 -1911 -227 A N ATOM 3347 CA ASN A 416 62.457 -21.806 66.647 1.00 30.37 A C ANISOU 3347 CA ASN A 416 3801 3917 3818 15 -1451 -290 A C ATOM 3348 C ASN A 416 61.718 -22.929 65.898 1.00 25.04 A C ANISOU 3348 C ASN A 416 2890 3616 3006 90 -1079 187 A C ATOM 3349 O ASN A 416 62.215 -23.421 64.883 1.00 30.59 A O ANISOU 3349 O ASN A 416 3492 3836 4291 600 -746 -517 A O ATOM 3350 CB ASN A 416 63.718 -22.388 67.288 1.00 33.03 A C ANISOU 3350 CB ASN A 416 3448 4921 4180 -364 -1685 -332 A C ATOM 3351 CG ASN A 416 64.639 -21.312 67.821 1.00 36.39 A C ANISOU 3351 CG ASN A 416 3530 5274 5020 -952 -1106 -392 A C ATOM 3352 ND2 ASN A 416 64.887 -20.284 67.031 1.00 36.87 A N ANISOU 3352 ND2 ASN A 416 4096 4276 5635 -525 -1606 -208 A N ATOM 3353 OD1 ASN A 416 65.115 -21.402 68.949 1.00 52.04 A O ANISOU 3353 OD1 ASN A 416 5116 8882 5772 -252 -1965 -1446 A O ATOM 3354 N SER A 417 60.569 -23.368 66.386 1.00 20.77 A N ANISOU 3354 N SER A 417 2880 2339 2671 613 -1066 -148 A N ATOM 3355 CA SER A 417 59.847 -24.477 65.733 1.00 20.02 A C ANISOU 3355 CA SER A 417 2538 2504 2561 452 -995 -88 A C ATOM 3356 C SER A 417 58.478 -24.050 65.176 1.00 20.65 A C ANISOU 3356 C SER A 417 2697 2478 2670 601 -1084 70 A C ATOM 3357 O SER A 417 57.906 -24.801 64.431 1.00 19.61 A O ANISOU 3357 O SER A 417 2762 2139 2548 697 -703 -28 A O ATOM 3358 CB SER A 417 59.706 -25.624 66.677 1.00 21.46 A C ANISOU 3358 CB SER A 417 2878 2525 2749 570 -722 58 A C ATOM 3359 OG SER A 417 59.013 -25.243 67.851 1.00 21.50 A O ANISOU 3359 OG SER A 417 2954 2876 2339 633 -660 234 A O ATOM 3360 N VAL A 418 57.973 -22.863 65.549 1.00 19.21 A N ANISOU 3360 N VAL A 418 2587 2496 2216 640 -789 15 A N ATOM 3361 CA VAL A 418 56.686 -22.392 65.019 1.00 18.14 A C ANISOU 3361 CA VAL A 418 2586 2031 2274 764 -508 -149 A C ATOM 3362 C VAL A 418 56.739 -20.869 64.890 1.00 17.56 A C ANISOU 3362 C VAL A 418 2560 2193 1919 711 -883 203 A C ATOM 3363 O VAL A 418 57.216 -20.176 65.769 1.00 20.96 A O ANISOU 3363 O VAL A 418 3191 2344 2427 465 -891 -215 A O ATOM 3364 CB VAL A 418 55.460 -22.874 65.836 1.00 19.95 A C ANISOU 3364 CB VAL A 418 2533 2637 2409 387 -601 -284 A C ATOM 3365 CG1 VAL A 418 55.434 -22.312 67.245 1.00 21.80 A C ANISOU 3365 CG1 VAL A 418 2921 2754 2605 173 -375 -315 A C ATOM 3366 CG2 VAL A 418 54.131 -22.590 65.132 1.00 20.71 A C ANISOU 3366 CG2 VAL A 418 2841 2381 2647 554 -652 -151 A C ATOM 3367 N THR A 419 56.187 -20.390 63.767 1.00 16.41 A N ANISOU 3367 N THR A 419 2600 1791 1843 593 -1059 -47 A N ATOM 3368 CA ATHR A 419 55.999 -18.971 63.546 0.50 15.57 A C ANISOU 3368 CA ATHR A 419 2327 1718 1871 526 -652 -66 A C ATOM 3369 CA BTHR A 419 56.001 -18.983 63.529 0.50 16.78 A C ANISOU 3369 CA BTHR A 419 2409 1761 2205 488 -813 -5 A C ATOM 3370 C THR A 419 54.718 -18.786 62.720 1.00 15.02 A C ANISOU 3370 C THR A 419 2155 1623 1926 247 -587 49 A C ATOM 3371 O THR A 419 54.237 -19.715 62.085 1.00 17.43 A O ANISOU 3371 O THR A 419 2398 1993 2232 410 -1091 -223 A O ATOM 3372 CB ATHR A 419 57.251 -18.393 62.882 0.50 16.69 A C ANISOU 3372 CB ATHR A 419 2346 1822 2173 516 -819 142 A C ATOM 3373 CB BTHR A 419 57.137 -18.379 62.707 0.50 21.77 A C ANISOU 3373 CB BTHR A 419 2576 2351 3344 137 -915 386 A C ATOM 3374 CG2ATHR A 419 57.286 -18.632 61.387 0.50 14.62 A C ANISOU 3374 CG2ATHR A 419 1595 1919 2037 589 -638 69 A C ATOM 3375 CG2BTHR A 419 57.015 -16.876 62.719 0.50 22.45 A C ANISOU 3375 CG2BTHR A 419 2485 2264 3782 9 -1002 421 A C ATOM 3376 OG1ATHR A 419 57.298 -16.999 63.199 0.50 20.97 A O ANISOU 3376 OG1ATHR A 419 3128 1771 3066 680 -632 -41 A O ATOM 3377 OG1BTHR A 419 58.427 -18.748 63.201 0.50 30.27 A O ANISOU 3377 OG1BTHR A 419 3014 4684 3803 632 -1411 259 A O ATOM 3378 N ALA A 420 54.165 -17.571 62.746 1.00 15.85 A N ANISOU 3378 N ALA A 420 2340 1597 2083 390 -669 -66 A N ATOM 3379 CA ALA A 420 53.001 -17.239 61.939 1.00 13.82 A C ANISOU 3379 CA ALA A 420 2170 1519 1562 59 -372 27 A C ATOM 3380 C ALA A 420 53.480 -16.532 60.673 1.00 13.97 A C ANISOU 3380 C ALA A 420 1918 1628 1759 172 -172 94 A C ATOM 3381 O ALA A 420 54.414 -15.732 60.707 1.00 15.96 A O ANISOU 3381 O ALA A 420 2255 1732 2076 -20 -647 -34 A O ATOM 3382 CB ALA A 420 51.990 -16.408 62.673 1.00 16.38 A C ANISOU 3382 CB ALA A 420 2076 2047 2100 258 -380 -67 A C ATOM 3383 N ILE A 421 52.765 -16.813 59.588 1.00 13.11 A N ANISOU 3383 N ILE A 421 1953 1280 1747 94 -191 26 A N ATOM 3384 CA ILE A 421 53.009 -16.203 58.307 1.00 14.22 A C ANISOU 3384 CA ILE A 421 1940 1803 1659 52 -132 -10 A C ATOM 3385 C ILE A 421 51.790 -15.348 58.000 1.00 13.15 A C ANISOU 3385 C ILE A 421 1783 1504 1708 -144 52 138 A C ATOM 3386 O ILE A 421 50.694 -15.832 57.955 1.00 12.37 A O ANISOU 3386 O ILE A 421 1670 1145 1885 126 -229 92 A O ATOM 3387 CB ILE A 421 53.223 -17.262 57.220 1.00 13.80 A C ANISOU 3387 CB ILE A 421 1832 1590 1821 246 -336 -45 A C ATOM 3388 CG1 ILE A 421 54.273 -18.312 57.620 1.00 14.53 A C ANISOU 3388 CG1 ILE A 421 2204 1472 1844 450 -130 -75 A C ATOM 3389 CG2 ILE A 421 53.540 -16.618 55.873 1.00 14.02 A C ANISOU 3389 CG2 ILE A 421 1838 1658 1829 442 -148 -176 A C ATOM 3390 CD1 ILE A 421 55.660 -17.783 57.876 1.00 15.26 A C ANISOU 3390 CD1 ILE A 421 2249 1816 1730 350 -201 9 A C ATOM 3391 N VAL A 422 52.049 -14.054 57.780 1.00 12.20 A N ANISOU 3391 N VAL A 422 1754 1243 1639 230 -93 178 A N ATOM 3392 CA VAL A 422 51.049 -13.041 57.475 1.00 11.63 A C ANISOU 3392 CA VAL A 422 1769 1244 1405 122 -297 107 A C ATOM 3393 C VAL A 422 50.881 -12.978 55.956 1.00 10.81 A C ANISOU 3393 C VAL A 422 1735 960 1412 154 -183 -143 A C ATOM 3394 O VAL A 422 51.865 -12.759 55.266 1.00 12.64 A O ANISOU 3394 O VAL A 422 1765 1493 1545 -35 -208 -108 A O ATOM 3395 CB VAL A 422 51.420 -11.669 58.047 1.00 14.02 A C ANISOU 3395 CB VAL A 422 2159 1311 1856 92 -337 -15 A C ATOM 3396 CG1 VAL A 422 50.308 -10.660 57.707 1.00 14.50 A C ANISOU 3396 CG1 VAL A 422 2199 1551 1758 282 -250 -92 A C ATOM 3397 CG2 VAL A 422 51.675 -11.760 59.561 1.00 15.69 A C ANISOU 3397 CG2 VAL A 422 2468 1594 1897 300 -326 -174 A C ATOM 3398 N VAL A 423 49.640 -13.241 55.483 1.00 10.30 A N ANISOU 3398 N VAL A 423 1545 917 1450 276 -52 -142 A N ATOM 3399 CA VAL A 423 49.372 -13.436 54.061 1.00 10.36 A C ANISOU 3399 CA VAL A 423 1539 906 1489 32 20 -59 A C ATOM 3400 C VAL A 423 48.257 -12.458 53.659 1.00 10.83 A C ANISOU 3400 C VAL A 423 1613 1025 1477 14 -51 -5 A C ATOM 3401 O VAL A 423 47.218 -12.434 54.288 1.00 11.32 A O ANISOU 3401 O VAL A 423 1688 946 1666 50 18 -120 A O ATOM 3402 CB VAL A 423 48.973 -14.902 53.810 1.00 10.65 A C ANISOU 3402 CB VAL A 423 1545 823 1677 86 139 15 A C ATOM 3403 CG1 VAL A 423 48.603 -15.136 52.350 1.00 11.81 A C ANISOU 3403 CG1 VAL A 423 1706 960 1818 289 -43 -2 A C ATOM 3404 CG2 VAL A 423 50.034 -15.898 54.252 1.00 12.76 A C ANISOU 3404 CG2 VAL A 423 1760 1235 1851 390 14 -131 A C ATOM 3405 N HIS A 424 48.495 -11.715 52.563 1.00 9.95 A N ANISOU 3405 N HIS A 424 1410 968 1403 176 -34 -5 A N ATOM 3406 CA HIS A 424 47.472 -10.846 52.001 1.00 10.51 A C ANISOU 3406 CA HIS A 424 1628 890 1474 200 -126 2 A C ATOM 3407 C HIS A 424 47.931 -10.334 50.637 1.00 9.57 A C ANISOU 3407 C HIS A 424 1284 801 1550 -9 -147 34 A C ATOM 3408 O HIS A 424 49.098 -10.538 50.232 1.00 10.28 A O ANISOU 3408 O HIS A 424 1457 865 1582 63 81 -91 A O ATOM 3409 CB HIS A 424 47.095 -9.656 52.914 1.00 11.24 A C ANISOU 3409 CB HIS A 424 1702 1012 1557 253 -97 -100 A C ATOM 3410 CG HIS A 424 48.204 -8.744 53.321 1.00 11.81 A C ANISOU 3410 CG HIS A 424 1737 970 1779 264 9 -216 A C ATOM 3411 CD2 HIS A 424 48.929 -8.677 54.465 1.00 12.45 A C ANISOU 3411 CD2 HIS A 424 1734 1125 1871 329 -42 -303 A C ATOM 3412 ND1 HIS A 424 48.657 -7.723 52.495 1.00 13.43 A N ANISOU 3412 ND1 HIS A 424 2025 1040 2038 -28 -118 -225 A N ATOM 3413 CE1 HIS A 424 49.633 -7.047 53.142 1.00 14.27 A C ANISOU 3413 CE1 HIS A 424 1855 1313 2252 -3 -70 -239 A C ATOM 3414 NE2 HIS A 424 49.803 -7.580 54.375 1.00 13.80 A N ANISOU 3414 NE2 HIS A 424 1932 1489 1820 27 -108 -557 A N ATOM 3415 N SER A 425 47.009 -9.617 49.958 1.00 9.80 A N ANISOU 3415 N SER A 425 1362 836 1522 180 -130 -79 A N ATOM 3416 CA SER A 425 47.370 -8.957 48.709 1.00 10.04 A C ANISOU 3416 CA SER A 425 1320 1099 1393 -28 -149 -79 A C ATOM 3417 C SER A 425 48.475 -7.930 48.969 1.00 9.94 A C ANISOU 3417 C SER A 425 1366 1070 1340 11 -111 -63 A C ATOM 3418 O SER A 425 48.327 -7.059 49.839 1.00 11.17 A O ANISOU 3418 O SER A 425 1530 868 1846 -18 -105 -286 A O ATOM 3419 CB SER A 425 46.139 -8.307 48.091 1.00 10.49 A C ANISOU 3419 CB SER A 425 1506 802 1677 158 -40 -49 A C ATOM 3420 OG SER A 425 45.233 -9.311 47.642 1.00 10.52 A O ANISOU 3420 OG SER A 425 1487 960 1548 -10 -29 -11 A O ATOM 3421 N ASP A 426 49.563 -8.023 48.202 1.00 10.01 A N ANISOU 3421 N ASP A 426 1427 736 1639 57 -42 -86 A N ATOM 3422 CA ASP A 426 50.820 -7.342 48.561 1.00 10.65 A C ANISOU 3422 CA ASP A 426 1201 1197 1648 31 -51 -38 A C ATOM 3423 C ASP A 426 50.885 -5.933 47.950 1.00 11.01 A C ANISOU 3423 C ASP A 426 1595 988 1597 -105 52 -347 A C ATOM 3424 O ASP A 426 51.677 -5.656 47.086 1.00 11.84 A O ANISOU 3424 O ASP A 426 1642 1032 1823 65 145 -210 A O ATOM 3425 CB ASP A 426 52.028 -8.195 48.186 1.00 12.09 A C ANISOU 3425 CB ASP A 426 1239 1062 2292 80 -182 -97 A C ATOM 3426 CG ASP A 426 53.357 -7.740 48.763 1.00 12.88 A C ANISOU 3426 CG ASP A 426 1353 1334 2205 69 -225 -364 A C ATOM 3427 OD1 ASP A 426 53.361 -6.881 49.659 1.00 14.15 A O ANISOU 3427 OD1 ASP A 426 1706 1361 2309 -21 -117 -470 A O ATOM 3428 OD2 ASP A 426 54.379 -8.213 48.246 1.00 15.93 A O ANISOU 3428 OD2 ASP A 426 1595 1812 2646 246 -100 -621 A O ATOM 3429 N MET A 427 49.980 -5.085 48.426 1.00 10.46 A N ANISOU 3429 N MET A 427 1411 910 1651 -41 8 -28 A N ATOM 3430 CA MET A 427 49.877 -3.709 47.983 1.00 10.60 A C ANISOU 3430 CA MET A 427 1486 839 1700 -101 50 -27 A C ATOM 3431 C MET A 427 51.013 -2.878 48.585 1.00 10.13 A C ANISOU 3431 C MET A 427 1487 910 1451 80 50 -205 A C ATOM 3432 O MET A 427 51.511 -3.151 49.652 1.00 11.44 A O ANISOU 3432 O MET A 427 1668 1043 1636 17 -197 -259 A O ATOM 3433 CB MET A 427 48.522 -3.147 48.437 1.00 11.43 A C ANISOU 3433 CB MET A 427 1489 978 1875 24 13 3 A C ATOM 3434 CG MET A 427 47.310 -3.843 47.787 1.00 11.67 A C ANISOU 3434 CG MET A 427 1617 919 1897 43 -79 48 A C ATOM 3435 SD MET A 427 45.768 -3.344 48.560 1.00 13.27 A S ANISOU 3435 SD MET A 427 1746 1066 2230 69 0 -92 A S ATOM 3436 CE MET A 427 45.996 -3.966 50.216 1.00 12.29 A C ANISOU 3436 CE MET A 427 1773 936 1961 -7 562 -468 A C ATOM 3437 N GLU A 428 51.337 -1.771 47.905 1.00 11.62 A N ANISOU 3437 N GLU A 428 1794 1027 1591 86 -221 80 A N ATOM 3438 CA GLU A 428 52.355 -0.852 48.420 1.00 12.22 A C ANISOU 3438 CA GLU A 428 1245 1497 1898 143 -140 -175 A C ATOM 3439 C GLU A 428 51.757 -0.048 49.584 1.00 10.78 A C ANISOU 3439 C GLU A 428 1534 863 1697 -148 -221 -108 A C ATOM 3440 O GLU A 428 50.696 0.564 49.426 1.00 11.86 A O ANISOU 3440 O GLU A 428 1466 1321 1717 -17 -245 -188 A O ATOM 3441 CB GLU A 428 52.813 0.086 47.316 1.00 12.69 A C ANISOU 3441 CB GLU A 428 1471 1368 1980 21 -109 -217 A C ATOM 3442 CG GLU A 428 53.928 1.000 47.752 1.00 13.95 A C ANISOU 3442 CG GLU A 428 1688 1463 2148 -199 67 -216 A C ATOM 3443 CD GLU A 428 54.505 1.870 46.641 1.00 19.01 A C ANISOU 3443 CD GLU A 428 2588 1725 2908 -357 134 253 A C ATOM 3444 OE1 GLU A 428 53.813 2.098 45.605 1.00 23.48 A O ANISOU 3444 OE1 GLU A 428 3521 1887 3512 -417 -81 903 A O ATOM 3445 OE2 GLU A 428 55.674 2.304 46.806 1.00 26.26 A O ANISOU 3445 OE2 GLU A 428 2779 2458 4737 -865 638 129 A O ATOM 3446 N ARG A 429 52.409 -0.097 50.735 1.00 11.77 A N ANISOU 3446 N ARG A 429 1653 1140 1677 147 -194 -283 A N ATOM 3447 CA ARG A 429 52.020 0.707 51.879 1.00 10.52 A C ANISOU 3447 CA ARG A 429 1519 1039 1437 -216 -194 -245 A C ATOM 3448 C ARG A 429 52.245 2.199 51.590 1.00 11.33 A C ANISOU 3448 C ARG A 429 1452 1118 1734 -96 -115 -141 A C ATOM 3449 O ARG A 429 53.319 2.594 51.103 1.00 12.73 A O ANISOU 3449 O ARG A 429 1606 1188 2043 -118 188 -201 A O ATOM 3450 CB ARG A 429 52.833 0.310 53.113 1.00 11.67 A C ANISOU 3450 CB ARG A 429 1553 1208 1672 -11 -294 -228 A C ATOM 3451 CG ARG A 429 52.432 1.007 54.398 1.00 11.62 A C ANISOU 3451 CG ARG A 429 1673 1250 1491 -18 -251 -101 A C ATOM 3452 CD ARG A 429 51.078 0.579 54.935 1.00 11.78 A C ANISOU 3452 CD ARG A 429 1621 1254 1599 130 -170 -300 A C ATOM 3453 NE ARG A 429 50.730 1.406 56.089 1.00 12.08 A N ANISOU 3453 NE ARG A 429 1894 838 1856 40 -85 -276 A N ATOM 3454 CZ ARG A 429 51.204 1.261 57.316 1.00 12.70 A C ANISOU 3454 CZ ARG A 429 1923 969 1933 -40 -289 -239 A C ATOM 3455 NH1 ARG A 429 50.856 2.124 58.282 1.00 13.62 A N ANISOU 3455 NH1 ARG A 429 2214 1381 1580 -215 180 -176 A N ATOM 3456 NH2 ARG A 429 51.986 0.205 57.572 1.00 13.58 A N ANISOU 3456 NH2 ARG A 429 1810 1070 2280 -125 -558 22 A N ATOM 3457 N THR A 430 51.210 2.992 51.895 1.00 10.54 A N ANISOU 3457 N THR A 430 1306 976 1720 -112 -167 53 A N ATOM 3458 CA THR A 430 51.248 4.430 51.612 1.00 10.43 A C ANISOU 3458 CA THR A 430 1379 916 1665 -169 36 -68 A C ATOM 3459 C THR A 430 50.938 5.298 52.830 1.00 10.30 A C ANISOU 3459 C THR A 430 1352 898 1660 21 -82 -59 A C ATOM 3460 O THR A 430 51.377 6.472 52.819 1.00 12.74 A O ANISOU 3460 O THR A 430 1989 774 2077 -63 -79 28 A O ATOM 3461 CB THR A 430 50.300 4.803 50.463 1.00 12.09 A C ANISOU 3461 CB THR A 430 1504 1223 1864 64 -87 -101 A C ATOM 3462 CG2 THR A 430 50.775 4.269 49.132 1.00 11.59 A C ANISOU 3462 CG2 THR A 430 1561 981 1858 -124 20 -58 A C ATOM 3463 OG1 THR A 430 48.978 4.334 50.722 1.00 11.46 A O ANISOU 3463 OG1 THR A 430 1488 1054 1811 -103 -59 -234 A O ATOM 3464 N GLY A 431 50.151 4.869 53.797 1.00 10.83 A N ANISOU 3464 N GLY A 431 1326 1036 1750 -4 -50 -134 A N ATOM 3465 CA GLY A 431 49.634 5.784 54.810 1.00 10.79 A C ANISOU 3465 CA GLY A 431 1552 907 1640 -229 -109 -202 A C ATOM 3466 C GLY A 431 49.939 5.353 56.221 1.00 12.29 A C ANISOU 3466 C GLY A 431 2036 942 1689 118 -181 -220 A C ATOM 3467 O GLY A 431 49.816 4.156 56.549 1.00 12.74 A O ANISOU 3467 O GLY A 431 2189 867 1784 54 -209 -141 A O ATOM 3468 N TYR A 432 50.321 6.315 57.064 1.00 12.37 A N ANISOU 3468 N TYR A 432 1828 1210 1660 -86 -290 -282 A N ATOM 3469 CA TYR A 432 50.816 6.070 58.406 1.00 13.19 A C ANISOU 3469 CA TYR A 432 1973 1210 1827 -31 -166 -188 A C ATOM 3470 C TYR A 432 50.210 7.109 59.347 1.00 11.32 A C ANISOU 3470 C TYR A 432 1652 994 1652 -123 -197 -41 A C ATOM 3471 O TYR A 432 50.076 8.280 58.964 1.00 13.50 A O ANISOU 3471 O TYR A 432 2108 926 2092 -235 -267 -33 A O ATOM 3472 CB TYR A 432 52.337 6.155 58.462 1.00 13.24 A C ANISOU 3472 CB TYR A 432 1955 1271 1804 80 -191 -197 A C ATOM 3473 CG TYR A 432 53.082 5.293 57.474 1.00 14.08 A C ANISOU 3473 CG TYR A 432 1507 1738 2104 -115 53 -339 A C ATOM 3474 CD1 TYR A 432 53.224 5.682 56.149 1.00 14.28 A C ANISOU 3474 CD1 TYR A 432 1761 1627 2036 -328 -195 -470 A C ATOM 3475 CD2 TYR A 432 53.598 4.065 57.848 1.00 15.76 A C ANISOU 3475 CD2 TYR A 432 1948 1763 2275 -90 21 -330 A C ATOM 3476 CE1 TYR A 432 53.909 4.915 55.229 1.00 15.36 A C ANISOU 3476 CE1 TYR A 432 1824 1825 2187 -194 -23 -281 A C ATOM 3477 CE2 TYR A 432 54.274 3.266 56.927 1.00 16.66 A C ANISOU 3477 CE2 TYR A 432 2186 1815 2327 -26 -298 -675 A C ATOM 3478 CZ TYR A 432 54.403 3.683 55.617 1.00 15.76 A C ANISOU 3478 CZ TYR A 432 2042 1610 2333 -81 -24 -470 A C ATOM 3479 OH TYR A 432 55.076 2.929 54.708 1.00 20.26 A O ANISOU 3479 OH TYR A 432 2008 2605 3084 -383 167 -1220 A O ATOM 3480 N PHE A 433 49.991 6.716 60.602 1.00 12.93 A N ANISOU 3480 N PHE A 433 2174 1128 1608 79 -82 -95 A N ATOM 3481 CA PHE A 433 49.440 7.618 61.590 1.00 13.11 A C ANISOU 3481 CA PHE A 433 2104 1100 1777 -167 -47 -176 A C ATOM 3482 C PHE A 433 49.864 7.179 62.991 1.00 14.94 A C ANISOU 3482 C PHE A 433 2485 1461 1730 -252 -309 -240 A C ATOM 3483 O PHE A 433 49.698 5.994 63.349 1.00 14.95 A O ANISOU 3483 O PHE A 433 2351 1489 1839 7 -297 -70 A O ATOM 3484 CB PHE A 433 47.907 7.655 61.493 1.00 14.56 A C ANISOU 3484 CB PHE A 433 2137 1420 1973 -109 -134 -88 A C ATOM 3485 CG PHE A 433 47.258 8.425 62.615 1.00 13.52 A C ANISOU 3485 CG PHE A 433 1977 1299 1860 -86 -100 -94 A C ATOM 3486 CD1 PHE A 433 47.071 9.808 62.547 1.00 14.21 A C ANISOU 3486 CD1 PHE A 433 2028 1377 1991 85 -223 69 A C ATOM 3487 CD2 PHE A 433 46.936 7.780 63.794 1.00 14.89 A C ANISOU 3487 CD2 PHE A 433 2332 1563 1761 -71 246 -275 A C ATOM 3488 CE1 PHE A 433 46.506 10.499 63.617 1.00 15.05 A C ANISOU 3488 CE1 PHE A 433 2133 1492 2092 -8 -368 -165 A C ATOM 3489 CE2 PHE A 433 46.380 8.487 64.857 1.00 14.26 A C ANISOU 3489 CE2 PHE A 433 2267 1605 1546 -264 29 -360 A C ATOM 3490 CZ PHE A 433 46.157 9.841 64.768 1.00 14.41 A C ANISOU 3490 CZ PHE A 433 2141 1563 1769 -210 -302 -613 A C ATOM 3491 N GLU A 434 50.295 8.139 63.810 1.00 15.03 A N ANISOU 3491 N GLU A 434 2462 1617 1632 -167 -358 -270 A N ATOM 3492 CA GLU A 434 50.439 7.904 65.242 1.00 17.01 A C ANISOU 3492 CA GLU A 434 2770 1883 1807 138 -571 -297 A C ATOM 3493 C GLU A 434 50.202 9.235 65.956 1.00 15.48 A C ANISOU 3493 C GLU A 434 2218 1630 2030 -219 -108 -240 A C ATOM 3494 O GLU A 434 50.314 10.305 65.346 1.00 16.55 A O ANISOU 3494 O GLU A 434 2793 1557 1938 -194 -369 -306 A O ATOM 3495 CB GLU A 434 51.809 7.332 65.591 1.00 20.71 A C ANISOU 3495 CB GLU A 434 2796 2703 2371 523 -308 -586 A C ATOM 3496 CG GLU A 434 52.969 8.177 65.181 1.00 23.09 A C ANISOU 3496 CG GLU A 434 3074 3342 2357 388 -414 -380 A C ATOM 3497 CD GLU A 434 54.277 7.496 65.550 1.00 33.85 A C ANISOU 3497 CD GLU A 434 3387 5914 3557 1275 -446 -12 A C ATOM 3498 OE1 GLU A 434 54.518 7.286 66.743 1.00 46.41 A O ANISOU 3498 OE1 GLU A 434 4899 8686 4048 1673 -1302 253 A O ATOM 3499 OE2 GLU A 434 55.005 7.119 64.652 1.00 43.60 A O ANISOU 3499 OE2 GLU A 434 3849 9230 3485 2499 -398 709 A O ATOM 3500 N CYS A 435 49.914 9.149 67.256 1.00 16.31 A N ANISOU 3500 N CYS A 435 3075 1118 2001 -326 -272 -262 A N ATOM 3501 CA CYS A 435 49.703 10.348 67.999 1.00 16.30 A C ANISOU 3501 CA CYS A 435 2947 1482 1763 -744 -263 -577 A C ATOM 3502 C CYS A 435 50.120 10.136 69.444 1.00 18.82 A C ANISOU 3502 C CYS A 435 3440 1857 1853 -2 -557 -536 A C ATOM 3503 O CYS A 435 50.553 9.077 69.810 1.00 20.49 A O ANISOU 3503 O CYS A 435 3441 2357 1987 338 -712 -394 A O ATOM 3504 CB CYS A 435 48.269 10.840 67.859 1.00 18.66 A C ANISOU 3504 CB CYS A 435 3051 2004 2032 -481 -301 -613 A C ATOM 3505 SG CYS A 435 47.046 9.813 68.714 1.00 18.77 A S ANISOU 3505 SG CYS A 435 2982 2043 2105 -357 -280 -354 A S ATOM 3506 N SER A 436 49.981 11.187 70.261 1.00 18.47 A N ANISOU 3506 N SER A 436 3330 1664 2020 -80 -583 -483 A N ATOM 3507 CA SER A 436 50.411 11.156 71.647 1.00 18.21 A C ANISOU 3507 CA SER A 436 2984 1882 2053 -484 -618 -374 A C ATOM 3508 C SER A 436 49.552 10.247 72.532 1.00 18.62 A C ANISOU 3508 C SER A 436 2954 1926 2194 -318 -586 -114 A C ATOM 3509 O SER A 436 49.997 9.888 73.618 1.00 21.57 A O ANISOU 3509 O SER A 436 3398 2238 2558 -343 -1001 44 A O ATOM 3510 CB SER A 436 50.457 12.581 72.215 1.00 18.39 A C ANISOU 3510 CB SER A 436 3109 1966 1910 -569 -606 -540 A C ATOM 3511 OG SER A 436 49.154 13.169 72.275 1.00 20.43 A O ANISOU 3511 OG SER A 436 3470 2089 2203 -289 -544 -614 A O ATOM 3512 N ASN A 437 48.318 9.941 72.114 1.00 17.55 A N ANISOU 3512 N ASN A 437 2976 1617 2076 -71 -511 18 A N ATOM 3513 CA ASN A 437 47.424 9.074 72.853 1.00 16.64 A C ANISOU 3513 CA ASN A 437 2711 1975 1634 -328 -363 -472 A C ATOM 3514 C ASN A 437 47.691 7.638 72.422 1.00 17.30 A C ANISOU 3514 C ASN A 437 2843 1992 1736 -195 -312 -257 A C ATOM 3515 O ASN A 437 47.396 7.246 71.287 1.00 17.60 A O ANISOU 3515 O ASN A 437 3129 1668 1889 -183 -544 -373 A O ATOM 3516 CB ASN A 437 45.966 9.444 72.603 1.00 18.39 A C ANISOU 3516 CB ASN A 437 2883 1720 2382 31 -197 -824 A C ATOM 3517 CG ASN A 437 44.987 8.666 73.445 1.00 18.48 A C ANISOU 3517 CG ASN A 437 2792 2037 2192 101 -388 -316 A C ATOM 3518 ND2 ASN A 437 44.002 9.359 73.992 1.00 23.38 A N ANISOU 3518 ND2 ASN A 437 3714 3021 2145 525 -87 -601 A N ATOM 3519 OD1 ASN A 437 45.064 7.434 73.509 1.00 20.43 A O ANISOU 3519 OD1 ASN A 437 3260 1885 2618 -87 38 -562 A O ATOM 3520 N PRO A 438 48.266 6.809 73.308 1.00 18.73 A N ANISOU 3520 N PRO A 438 3154 1860 2100 93 -754 -400 A N ATOM 3521 CA PRO A 438 48.648 5.454 72.925 1.00 17.09 A C ANISOU 3521 CA PRO A 438 2998 1638 1856 -128 -454 -264 A C ATOM 3522 C PRO A 438 47.468 4.562 72.531 1.00 16.62 A C ANISOU 3522 C PRO A 438 2614 1843 1857 -14 -322 64 A C ATOM 3523 O PRO A 438 47.659 3.647 71.726 1.00 18.36 A O ANISOU 3523 O PRO A 438 2586 1978 2410 -16 -452 -516 A O ATOM 3524 CB PRO A 438 49.417 4.875 74.116 1.00 20.43 A C ANISOU 3524 CB PRO A 438 3139 2334 2287 0 -769 -180 A C ATOM 3525 CG PRO A 438 49.325 5.889 75.223 1.00 26.30 A C ANISOU 3525 CG PRO A 438 4721 2908 2365 549 -988 -347 A C ATOM 3526 CD PRO A 438 48.609 7.110 74.714 1.00 21.26 A C ANISOU 3526 CD PRO A 438 3857 2323 1897 -66 -565 -61 A C ATOM 3527 N LEU A 439 46.284 4.806 73.104 1.00 15.77 A N ANISOU 3527 N LEU A 439 2701 1654 1633 8 -431 -245 A N ATOM 3528 CA LEU A 439 45.113 4.014 72.715 1.00 15.74 A C ANISOU 3528 CA LEU A 439 2734 1537 1706 -194 -280 -269 A C ATOM 3529 C LEU A 439 44.697 4.359 71.276 1.00 15.14 A C ANISOU 3529 C LEU A 439 2629 1430 1694 -211 -297 -141 A C ATOM 3530 O LEU A 439 44.273 3.477 70.545 1.00 15.73 A O ANISOU 3530 O LEU A 439 2771 1623 1579 -78 -320 -364 A O ATOM 3531 CB LEU A 439 43.958 4.214 73.692 1.00 17.84 A C ANISOU 3531 CB LEU A 439 2993 1666 2120 219 -153 -287 A C ATOM 3532 CG LEU A 439 44.254 3.846 75.146 1.00 19.81 A C ANISOU 3532 CG LEU A 439 3405 2019 2101 24 -66 -171 A C ATOM 3533 CD1 LEU A 439 43.032 4.094 76.002 1.00 21.77 A C ANISOU 3533 CD1 LEU A 439 3589 2792 1888 15 -30 -179 A C ATOM 3534 CD2 LEU A 439 44.719 2.420 75.279 1.00 22.43 A C ANISOU 3534 CD2 LEU A 439 3941 2354 2226 357 -61 -4 A C ATOM 3535 N ILE A 440 44.691 5.644 70.901 1.00 15.50 A N ANISOU 3535 N ILE A 440 2845 1479 1564 5 -276 -133 A N ATOM 3536 CA ILE A 440 44.284 6.045 69.541 1.00 14.39 A C ANISOU 3536 CA ILE A 440 2562 1412 1492 -111 -122 -270 A C ATOM 3537 C ILE A 440 45.369 5.582 68.556 1.00 14.40 A C ANISOU 3537 C ILE A 440 2292 1438 1740 -12 -127 -109 A C ATOM 3538 O ILE A 440 45.061 5.120 67.434 1.00 15.75 A O ANISOU 3538 O ILE A 440 2683 1395 1906 127 -579 -194 A O ATOM 3539 CB ILE A 440 44.014 7.559 69.480 1.00 14.49 A C ANISOU 3539 CB ILE A 440 2314 1416 1773 -117 -164 -316 A C ATOM 3540 CG1 ILE A 440 42.825 7.916 70.361 1.00 15.92 A C ANISOU 3540 CG1 ILE A 440 2461 1845 1740 99 -206 -206 A C ATOM 3541 CG2 ILE A 440 43.779 8.036 68.056 1.00 15.57 A C ANISOU 3541 CG2 ILE A 440 2630 1477 1807 -148 -131 -305 A C ATOM 3542 CD1 ILE A 440 42.578 9.396 70.458 1.00 17.64 A C ANISOU 3542 CD1 ILE A 440 2762 1772 2169 -91 -61 -232 A C ATOM 3543 N SER A 441 46.643 5.658 68.954 1.00 15.77 A N ANISOU 3543 N SER A 441 2406 1376 2210 40 -348 -279 A N ATOM 3544 CA SER A 441 47.699 5.089 68.084 1.00 15.26 A C ANISOU 3544 CA SER A 441 2238 1488 2071 7 -321 -81 A C ATOM 3545 C SER A 441 47.470 3.579 67.872 1.00 15.35 A C ANISOU 3545 C SER A 441 2232 1500 2098 174 -120 -15 A C ATOM 3546 O SER A 441 47.620 3.090 66.740 1.00 15.98 A O ANISOU 3546 O SER A 441 2368 1654 2050 -104 -169 -156 A O ATOM 3547 CB SER A 441 49.095 5.313 68.618 1.00 15.94 A C ANISOU 3547 CB SER A 441 2305 1440 2309 -10 -412 -275 A C ATOM 3548 OG SER A 441 49.374 6.693 68.711 1.00 17.29 A O ANISOU 3548 OG SER A 441 2810 1497 2260 -240 -700 111 A O ATOM 3549 N LYS A 442 47.104 2.859 68.943 1.00 14.29 A N ANISOU 3549 N LYS A 442 2576 1353 1497 -89 -497 -379 A N ATOM 3550 CA LYS A 442 46.843 1.433 68.802 1.00 14.43 A C ANISOU 3550 CA LYS A 442 2428 1356 1696 -31 -323 -509 A C ATOM 3551 C LYS A 442 45.606 1.189 67.932 1.00 14.82 A C ANISOU 3551 C LYS A 442 2310 1714 1607 223 -307 -301 A C ATOM 3552 O LYS A 442 45.581 0.221 67.155 1.00 15.19 A O ANISOU 3552 O LYS A 442 2785 1143 1844 57 -476 -172 A O ATOM 3553 CB LYS A 442 46.664 0.782 70.174 1.00 15.42 A C ANISOU 3553 CB LYS A 442 2578 1475 1806 -46 -301 -275 A C ATOM 3554 CG LYS A 442 46.382 -0.722 70.138 1.00 15.17 A C ANISOU 3554 CG LYS A 442 2475 1502 1785 -167 -397 -163 A C ATOM 3555 CD LYS A 442 47.484 -1.532 69.488 1.00 16.60 A C ANISOU 3555 CD LYS A 442 2469 1792 2045 13 -511 112 A C ATOM 3556 CE LYS A 442 47.448 -3.001 69.846 1.00 17.11 A C ANISOU 3556 CE LYS A 442 2672 1921 1907 -52 -559 287 A C ATOM 3557 NZ LYS A 442 48.557 -3.746 69.186 1.00 18.87 A N ANISOU 3557 NZ LYS A 442 2831 2084 2254 127 -708 21 A N ATOM 3558 N LEU A 443 44.566 2.009 68.087 1.00 13.84 A N ANISOU 3558 N LEU A 443 2311 1356 1591 90 -227 -305 A N ATOM 3559 CA LEU A 443 43.383 1.912 67.207 1.00 13.18 A C ANISOU 3559 CA LEU A 443 2152 1181 1674 21 -93 -189 A C ATOM 3560 C LEU A 443 43.805 1.925 65.731 1.00 12.28 A C ANISOU 3560 C LEU A 443 2063 1080 1521 -102 -260 -86 A C ATOM 3561 O LEU A 443 43.343 1.091 64.948 1.00 13.87 A O ANISOU 3561 O LEU A 443 2316 1181 1770 -202 -60 -429 A O ATOM 3562 CB LEU A 443 42.398 3.036 67.495 1.00 13.95 A C ANISOU 3562 CB LEU A 443 2098 1471 1731 92 66 -199 A C ATOM 3563 CG LEU A 443 41.161 3.068 66.600 1.00 13.81 A C ANISOU 3563 CG LEU A 443 2555 1230 1459 183 -303 -311 A C ATOM 3564 CD1 LEU A 443 40.351 1.766 66.719 1.00 15.77 A C ANISOU 3564 CD1 LEU A 443 2700 1758 1531 -16 -324 -219 A C ATOM 3565 CD2 LEU A 443 40.327 4.312 66.920 1.00 14.22 A C ANISOU 3565 CD2 LEU A 443 2205 1494 1704 84 -33 -543 A C ATOM 3566 N HIS A 444 44.680 2.848 65.341 1.00 13.48 A N ANISOU 3566 N HIS A 444 2344 1194 1582 -211 -261 19 A N ATOM 3567 CA HIS A 444 45.123 2.911 63.960 1.00 12.26 A C ANISOU 3567 CA HIS A 444 1807 1106 1742 -15 -194 21 A C ATOM 3568 C HIS A 444 45.863 1.614 63.565 1.00 12.37 A C ANISOU 3568 C HIS A 444 2027 1294 1376 37 -274 -203 A C ATOM 3569 O HIS A 444 45.661 1.100 62.482 1.00 12.95 A O ANISOU 3569 O HIS A 444 2119 1172 1628 -41 -395 -341 A O ATOM 3570 CB HIS A 444 45.931 4.183 63.659 1.00 13.08 A C ANISOU 3570 CB HIS A 444 2276 1119 1575 -234 -195 -253 A C ATOM 3571 CG HIS A 444 46.149 4.308 62.192 1.00 12.80 A C ANISOU 3571 CG HIS A 444 2060 1172 1629 -115 -72 -428 A C ATOM 3572 CD2 HIS A 444 45.394 4.907 61.247 1.00 13.95 A C ANISOU 3572 CD2 HIS A 444 2145 1303 1850 111 3 -296 A C ATOM 3573 ND1 HIS A 444 47.245 3.751 61.538 1.00 13.06 A N ANISOU 3573 ND1 HIS A 444 1916 1213 1832 -212 -43 -267 A N ATOM 3574 CE1 HIS A 444 47.131 4.011 60.240 1.00 13.92 A C ANISOU 3574 CE1 HIS A 444 2050 1479 1758 -13 -64 -371 A C ATOM 3575 NE2 HIS A 444 46.003 4.740 60.048 1.00 12.89 A N ANISOU 3575 NE2 HIS A 444 2093 1107 1697 -112 -62 -191 A N ATOM 3576 N GLU A 445 46.749 1.116 64.436 1.00 13.27 A N ANISOU 3576 N GLU A 445 2205 1330 1505 155 -360 -281 A N ATOM 3577 CA AGLU A 445 47.438 -0.143 64.168 0.50 12.66 A C ANISOU 3577 CA AGLU A 445 1993 1206 1610 99 -313 -70 A C ATOM 3578 CA BGLU A 445 47.445 -0.171 64.195 0.50 13.03 A C ANISOU 3578 CA BGLU A 445 2040 1219 1689 65 -260 -125 A C ATOM 3579 C GLU A 445 46.408 -1.271 63.949 1.00 12.34 A C ANISOU 3579 C GLU A 445 1878 1488 1322 37 -275 -151 A C ATOM 3580 O GLU A 445 46.567 -2.124 63.040 1.00 13.72 A O ANISOU 3580 O GLU A 445 2119 1129 1963 136 -82 -343 A O ATOM 3581 CB AGLU A 445 48.446 -0.387 65.290 0.50 13.03 A C ANISOU 3581 CB AGLU A 445 2214 1236 1498 130 -357 -112 A C ATOM 3582 CB BGLU A 445 48.319 -0.618 65.368 0.50 15.43 A C ANISOU 3582 CB BGLU A 445 2392 1922 1547 23 -427 -247 A C ATOM 3583 CG AGLU A 445 49.279 -1.620 65.065 0.50 15.24 A C ANISOU 3583 CG AGLU A 445 2532 1369 1887 357 -470 -349 A C ATOM 3584 CG BGLU A 445 49.538 0.234 65.646 0.50 17.42 A C ANISOU 3584 CG BGLU A 445 2498 1960 2161 -15 -235 -575 A C ATOM 3585 CD AGLU A 445 50.514 -1.784 65.951 0.50 19.88 A C ANISOU 3585 CD AGLU A 445 2954 2345 2253 471 -686 484 A C ATOM 3586 CD BGLU A 445 50.226 -0.145 66.957 0.50 21.68 A C ANISOU 3586 CD BGLU A 445 3264 2175 2798 190 -884 -460 A C ATOM 3587 OE1AGLU A 445 50.793 -0.908 66.778 0.50 26.80 A O ANISOU 3587 OE1AGLU A 445 3342 3451 3389 -37 -1139 77 A O ATOM 3588 OE1BGLU A 445 50.230 -1.358 67.283 0.50 23.88 A O ANISOU 3588 OE1BGLU A 445 3002 3075 2996 -291 -768 1125 A O ATOM 3589 OE2AGLU A 445 51.191 -2.805 65.791 0.50 29.78 A O ANISOU 3589 OE2AGLU A 445 3364 4164 3785 1873 -216 743 A O ATOM 3590 OE2BGLU A 445 50.752 0.760 67.658 0.50 29.87 A O ANISOU 3590 OE2BGLU A 445 4495 3647 3207 -579 -2155 -498 A O ATOM 3591 N ASN A 446 45.349 -1.266 64.754 1.00 12.22 A N ANISOU 3591 N ASN A 446 1941 1171 1530 36 -228 -256 A N ATOM 3592 CA ASN A 446 44.316 -2.298 64.658 1.00 12.66 A C ANISOU 3592 CA ASN A 446 2007 1237 1565 -32 -233 -54 A C ATOM 3593 C ASN A 446 43.549 -2.195 63.336 1.00 12.67 A C ANISOU 3593 C ASN A 446 1929 1255 1627 34 -301 -167 A C ATOM 3594 O ASN A 446 43.212 -3.238 62.739 1.00 13.15 A O ANISOU 3594 O ASN A 446 2021 1222 1753 -23 -246 -268 A O ATOM 3595 CB ASN A 446 43.319 -2.236 65.815 1.00 12.92 A C ANISOU 3595 CB ASN A 446 1991 1283 1631 -86 -107 63 A C ATOM 3596 CG ASN A 446 43.935 -2.619 67.146 1.00 12.80 A C ANISOU 3596 CG ASN A 446 2061 1143 1656 -112 -221 -144 A C ATOM 3597 ND2 ASN A 446 43.114 -2.537 68.189 1.00 13.97 A N ANISOU 3597 ND2 ASN A 446 2479 1257 1569 -83 -222 -106 A N ATOM 3598 OD1 ASN A 446 45.138 -2.942 67.241 1.00 13.44 A O ANISOU 3598 OD1 ASN A 446 2213 1281 1611 6 -166 -177 A O ATOM 3599 N ILE A 447 43.309 -0.967 62.865 1.00 12.13 A N ANISOU 3599 N ILE A 447 1822 1228 1557 73 -200 -161 A N ATOM 3600 CA ILE A 447 42.672 -0.747 61.573 1.00 11.38 A C ANISOU 3600 CA ILE A 447 1666 1111 1544 -101 -141 -255 A C ATOM 3601 C ILE A 447 43.557 -1.263 60.441 1.00 11.41 A C ANISOU 3601 C ILE A 447 1431 1201 1701 109 -80 -92 A C ATOM 3602 O ILE A 447 43.125 -1.990 59.509 1.00 12.21 A O ANISOU 3602 O ILE A 447 1819 1077 1743 127 -64 -239 A O ATOM 3603 CB ILE A 447 42.344 0.744 61.371 1.00 12.65 A C ANISOU 3603 CB ILE A 447 1719 1041 2045 -72 -104 -257 A C ATOM 3604 CG1 ILE A 447 41.307 1.183 62.409 1.00 11.95 A C ANISOU 3604 CG1 ILE A 447 1769 1117 1651 -41 -201 38 A C ATOM 3605 CG2 ILE A 447 41.882 1.023 59.952 1.00 13.13 A C ANISOU 3605 CG2 ILE A 447 1658 1255 2075 124 157 -8 A C ATOM 3606 CD1 ILE A 447 41.091 2.698 62.475 1.00 12.42 A C ANISOU 3606 CD1 ILE A 447 1723 1198 1797 107 -58 -455 A C ATOM 3607 N LEU A 448 44.828 -0.953 60.551 1.00 12.19 A N ANISOU 3607 N LEU A 448 1581 1204 1846 21 -168 -82 A N ATOM 3608 CA LEU A 448 45.836 -1.447 59.594 1.00 11.47 A C ANISOU 3608 CA LEU A 448 1501 1168 1687 -38 -103 -122 A C ATOM 3609 C LEU A 448 45.799 -2.990 59.526 1.00 11.95 A C ANISOU 3609 C LEU A 448 1629 1225 1686 -70 -265 59 A C ATOM 3610 O LEU A 448 45.801 -3.569 58.406 1.00 12.02 A O ANISOU 3610 O LEU A 448 1784 1001 1782 55 -129 -41 A O ATOM 3611 CB LEU A 448 47.207 -0.945 60.055 1.00 11.56 A C ANISOU 3611 CB LEU A 448 1649 1035 1706 -108 -168 -15 A C ATOM 3612 CG LEU A 448 48.440 -1.523 59.375 1.00 12.43 A C ANISOU 3612 CG LEU A 448 1744 1138 1839 114 -209 -88 A C ATOM 3613 CD1 LEU A 448 48.513 -1.168 57.915 1.00 12.39 A C ANISOU 3613 CD1 LEU A 448 1679 1407 1621 113 -185 -418 A C ATOM 3614 CD2 LEU A 448 49.702 -1.116 60.122 1.00 13.29 A C ANISOU 3614 CD2 LEU A 448 1753 1484 1811 127 -205 -123 A C ATOM 3615 N TRP A 449 45.792 -3.633 60.690 1.00 11.00 A N ANISOU 3615 N TRP A 449 1948 862 1366 -120 -329 -370 A N ATOM 3616 CA TRP A 449 45.749 -5.075 60.703 1.00 11.00 A C ANISOU 3616 CA TRP A 449 1735 839 1603 53 -215 -243 A C ATOM 3617 C TRP A 449 44.420 -5.637 60.174 1.00 11.55 A C ANISOU 3617 C TRP A 449 1669 1197 1520 -31 -104 -182 A C ATOM 3618 O TRP A 449 44.445 -6.737 59.563 1.00 12.11 A O ANISOU 3618 O TRP A 449 1867 1022 1710 23 -199 -133 A O ATOM 3619 CB TRP A 449 46.075 -5.615 62.103 1.00 12.41 A C ANISOU 3619 CB TRP A 449 1996 1223 1493 254 -80 -285 A C ATOM 3620 CG TRP A 449 47.544 -5.640 62.371 1.00 14.17 A C ANISOU 3620 CG TRP A 449 2044 1600 1737 233 -544 -144 A C ATOM 3621 CD1 TRP A 449 48.265 -4.762 63.130 1.00 15.08 A C ANISOU 3621 CD1 TRP A 449 2135 1147 2445 49 -195 -333 A C ATOM 3622 CD2 TRP A 449 48.492 -6.647 61.950 1.00 13.42 A C ANISOU 3622 CD2 TRP A 449 1904 1330 1865 -39 -94 -187 A C ATOM 3623 CE2 TRP A 449 49.739 -6.322 62.521 1.00 14.23 A C ANISOU 3623 CE2 TRP A 449 1995 1511 1901 30 -151 -277 A C ATOM 3624 CE3 TRP A 449 48.395 -7.849 61.231 1.00 14.20 A C ANISOU 3624 CE3 TRP A 449 1796 1677 1922 -148 -160 -418 A C ATOM 3625 NE1 TRP A 449 49.579 -5.123 63.160 1.00 14.90 A N ANISOU 3625 NE1 TRP A 449 2061 1332 2267 -70 -552 -328 A N ATOM 3626 CZ2 TRP A 449 50.897 -7.069 62.297 1.00 15.38 A C ANISOU 3626 CZ2 TRP A 449 1781 1747 2316 -40 -33 8 A C ATOM 3627 CZ3 TRP A 449 49.519 -8.618 61.049 1.00 16.32 A C ANISOU 3627 CZ3 TRP A 449 2131 1566 2503 242 -405 -61 A C ATOM 3628 CH2 TRP A 449 50.757 -8.229 61.563 1.00 15.91 A C ANISOU 3628 CH2 TRP A 449 1769 1760 2514 294 -95 -79 A C ATOM 3629 N SER A 450 43.282 -4.977 60.436 1.00 10.96 A N ANISOU 3629 N SER A 450 1592 1242 1329 -39 -143 -103 A N ATOM 3630 CA SER A 450 42.029 -5.423 59.853 1.00 10.56 A C ANISOU 3630 CA SER A 450 1516 1028 1465 1 -90 -13 A C ATOM 3631 C SER A 450 42.032 -5.276 58.320 1.00 11.14 A C ANISOU 3631 C SER A 450 1824 1068 1337 -91 -36 -183 A C ATOM 3632 O SER A 450 41.429 -6.094 57.584 1.00 12.32 A O ANISOU 3632 O SER A 450 1754 1272 1655 -252 -12 -328 A O ATOM 3633 CB SER A 450 40.817 -4.810 60.494 1.00 12.80 A C ANISOU 3633 CB SER A 450 1535 1356 1973 -52 76 -178 A C ATOM 3634 OG SER A 450 40.572 -5.389 61.758 1.00 14.62 A O ANISOU 3634 OG SER A 450 1985 1470 2099 152 163 -76 A O ATOM 3635 N MET A 451 42.665 -4.218 57.810 1.00 11.09 A N ANISOU 3635 N MET A 451 1537 1191 1486 -14 -199 -94 A N ATOM 3636 CA MET A 451 42.808 -4.067 56.388 1.00 10.23 A C ANISOU 3636 CA MET A 451 1391 909 1585 -2 -161 -103 A C ATOM 3637 C MET A 451 43.671 -5.213 55.814 1.00 11.05 A C ANISOU 3637 C MET A 451 1757 977 1462 177 -157 72 A C ATOM 3638 O MET A 451 43.301 -5.819 54.781 1.00 11.63 A O ANISOU 3638 O MET A 451 1912 826 1678 -16 -329 -71 A O ATOM 3639 CB MET A 451 43.357 -2.684 56.007 1.00 11.79 A C ANISOU 3639 CB MET A 451 1658 764 2056 62 -200 -157 A C ATOM 3640 CG MET A 451 43.630 -2.569 54.493 1.00 11.25 A C ANISOU 3640 CG MET A 451 1730 511 2032 22 -179 -284 A C ATOM 3641 SD MET A 451 43.835 -0.907 54.005 1.00 12.01 A S ANISOU 3641 SD MET A 451 1868 728 1966 48 -55 -186 A S ATOM 3642 CE MET A 451 43.928 -1.207 52.236 1.00 12.19 A C ANISOU 3642 CE MET A 451 1677 859 2093 -36 -8 -168 A C ATOM 3643 N ARG A 452 44.824 -5.429 56.434 1.00 11.45 A N ANISOU 3643 N ARG A 452 1597 1079 1674 231 -186 -255 A N ATOM 3644 CA ARG A 452 45.687 -6.524 55.981 1.00 11.33 A C ANISOU 3644 CA ARG A 452 1658 934 1712 255 -179 -152 A C ATOM 3645 C ARG A 452 44.941 -7.868 55.965 1.00 11.85 A C ANISOU 3645 C ARG A 452 1750 1306 1444 -54 1 -171 A C ATOM 3646 O ARG A 452 45.099 -8.662 55.025 1.00 12.87 A O ANISOU 3646 O ARG A 452 1857 1256 1777 48 163 -390 A O ATOM 3647 CB ARG A 452 46.903 -6.645 56.895 1.00 12.27 A C ANISOU 3647 CB ARG A 452 1554 1323 1782 115 -124 -229 A C ATOM 3648 CG ARG A 452 47.890 -5.507 56.754 1.00 12.30 A C ANISOU 3648 CG ARG A 452 1555 1218 1900 111 -136 -346 A C ATOM 3649 CD ARG A 452 48.908 -5.519 57.872 1.00 13.67 A C ANISOU 3649 CD ARG A 452 1684 1635 1875 -62 -111 48 A C ATOM 3650 NE ARG A 452 49.929 -4.521 57.678 1.00 13.67 A N ANISOU 3650 NE ARG A 452 1912 1247 2033 -81 -236 -180 A N ATOM 3651 CZ ARG A 452 50.874 -4.216 58.582 1.00 14.97 A C ANISOU 3651 CZ ARG A 452 2024 1533 2131 -39 -376 -108 A C ATOM 3652 NH1 ARG A 452 50.794 -4.693 59.826 1.00 17.31 A N ANISOU 3652 NH1 ARG A 452 2163 2259 2153 -207 -478 109 A N ATOM 3653 NH2 ARG A 452 51.853 -3.391 58.232 1.00 15.62 A N ANISOU 3653 NH2 ARG A 452 2102 1475 2355 -108 5 -106 A N ATOM 3654 N GLY A 453 44.087 -8.114 56.958 1.00 10.32 A N ANISOU 3654 N GLY A 453 1630 738 1552 68 14 -100 A N ATOM 3655 CA GLY A 453 43.472 -9.385 57.031 1.00 11.28 A C ANISOU 3655 CA GLY A 453 1787 699 1800 45 -81 41 A C ATOM 3656 C GLY A 453 42.419 -9.622 55.945 1.00 11.42 A C ANISOU 3656 C GLY A 453 1651 1048 1638 37 14 106 A C ATOM 3657 O GLY A 453 42.105 -10.776 55.603 1.00 12.71 A O ANISOU 3657 O GLY A 453 1749 1276 1802 -167 -181 -90 A O ATOM 3658 N ASN A 454 41.835 -8.528 55.455 1.00 10.45 A N ANISOU 3658 N ASN A 454 1491 925 1554 -9 -87 29 A N ATOM 3659 CA ASN A 454 40.668 -8.547 54.614 1.00 10.63 A C ANISOU 3659 CA ASN A 454 1468 1010 1559 -14 -29 -54 A C ATOM 3660 C ASN A 454 40.901 -7.996 53.197 1.00 10.68 A C ANISOU 3660 C ASN A 454 1590 810 1656 -22 62 -82 A C ATOM 3661 O ASN A 454 39.935 -7.918 52.413 1.00 12.60 A O ANISOU 3661 O ASN A 454 1558 1807 1421 -172 86 128 A O ATOM 3662 CB ASN A 454 39.534 -7.812 55.291 1.00 10.50 A C ANISOU 3662 CB ASN A 454 1651 897 1441 -77 -46 -280 A C ATOM 3663 CG ASN A 454 38.980 -8.585 56.462 1.00 12.16 A C ANISOU 3663 CG ASN A 454 1706 1269 1645 -249 96 -160 A C ATOM 3664 ND2 ASN A 454 39.194 -8.099 57.687 1.00 12.28 A N ANISOU 3664 ND2 ASN A 454 1823 1226 1617 -20 -18 -154 A N ATOM 3665 OD1 ASN A 454 38.362 -9.648 56.253 1.00 12.15 A O ANISOU 3665 OD1 ASN A 454 1875 1138 1601 -207 14 -178 A O ATOM 3666 N PHE A 455 42.146 -7.710 52.821 1.00 9.88 A N ANISOU 3666 N PHE A 455 1307 987 1459 141 -161 16 A N ATOM 3667 CA PHE A 455 42.485 -7.436 51.420 1.00 9.83 A C ANISOU 3667 CA PHE A 455 1202 966 1566 24 -56 44 A C ATOM 3668 C PHE A 455 43.241 -8.667 50.930 1.00 10.34 A C ANISOU 3668 C PHE A 455 1475 991 1462 -21 47 34 A C ATOM 3669 O PHE A 455 44.454 -8.720 50.962 1.00 11.00 A O ANISOU 3669 O PHE A 455 1472 944 1763 -6 -31 -250 A O ATOM 3670 CB PHE A 455 43.237 -6.108 51.294 1.00 10.12 A C ANISOU 3670 CB PHE A 455 1405 884 1556 -14 -11 -54 A C ATOM 3671 CG PHE A 455 42.338 -4.897 51.175 1.00 9.81 A C ANISOU 3671 CG PHE A 455 1444 744 1540 -97 -174 -220 A C ATOM 3672 CD1 PHE A 455 41.457 -4.533 52.189 1.00 11.33 A C ANISOU 3672 CD1 PHE A 455 1933 756 1614 25 -17 -137 A C ATOM 3673 CD2 PHE A 455 42.288 -4.207 49.976 1.00 11.31 A C ANISOU 3673 CD2 PHE A 455 1712 918 1664 64 -99 -117 A C ATOM 3674 CE1 PHE A 455 40.627 -3.422 52.041 1.00 11.69 A C ANISOU 3674 CE1 PHE A 455 1698 972 1771 65 -27 -185 A C ATOM 3675 CE2 PHE A 455 41.442 -3.111 49.841 1.00 11.68 A C ANISOU 3675 CE2 PHE A 455 1771 839 1827 -14 -284 -146 A C ATOM 3676 CZ PHE A 455 40.587 -2.775 50.843 1.00 12.35 A C ANISOU 3676 CZ PHE A 455 1736 1080 1876 154 -240 -146 A C ATOM 3677 N PHE A 456 42.455 -9.713 50.663 1.00 10.34 A N ANISOU 3677 N PHE A 456 1245 962 1719 46 -83 -50 A N ATOM 3678 CA PHE A 456 43.007 -11.067 50.389 1.00 10.41 A C ANISOU 3678 CA PHE A 456 1609 828 1518 263 -358 60 A C ATOM 3679 C PHE A 456 42.414 -11.530 49.063 1.00 10.36 A C ANISOU 3679 C PHE A 456 1432 1002 1503 31 -190 128 A C ATOM 3680 O PHE A 456 41.413 -12.270 49.096 1.00 13.22 A O ANISOU 3680 O PHE A 456 1744 1139 2140 -203 -148 -37 A O ATOM 3681 CB PHE A 456 42.622 -12.015 51.522 1.00 11.73 A C ANISOU 3681 CB PHE A 456 1581 1260 1616 110 -24 -2 A C ATOM 3682 CG PHE A 456 43.449 -13.274 51.647 1.00 10.77 A C ANISOU 3682 CG PHE A 456 1768 731 1593 114 148 89 A C ATOM 3683 CD1 PHE A 456 43.262 -14.359 50.781 1.00 11.70 A C ANISOU 3683 CD1 PHE A 456 1889 967 1586 10 -329 -74 A C ATOM 3684 CD2 PHE A 456 44.443 -13.381 52.609 1.00 12.06 A C ANISOU 3684 CD2 PHE A 456 1969 1054 1557 -218 -57 -150 A C ATOM 3685 CE1 PHE A 456 44.023 -15.499 50.898 1.00 12.37 A C ANISOU 3685 CE1 PHE A 456 2054 702 1942 79 -103 216 A C ATOM 3686 CE2 PHE A 456 45.194 -14.541 52.720 1.00 12.50 A C ANISOU 3686 CE2 PHE A 456 2080 1078 1592 162 -26 144 A C ATOM 3687 CZ PHE A 456 44.995 -15.588 51.870 1.00 11.59 A C ANISOU 3687 CZ PHE A 456 1902 1069 1430 -197 89 111 A C ATOM 3688 N SER A 457 42.957 -11.020 47.946 1.00 10.18 A N ANISOU 3688 N SER A 457 1289 873 1703 76 95 -117 A N ATOM 3689 CA SER A 457 42.489 -11.196 46.518 1.00 10.92 A C ANISOU 3689 CA SER A 457 1612 742 1796 339 90 -139 A C ATOM 3690 C SER A 457 41.280 -10.267 46.246 1.00 10.45 A C ANISOU 3690 C SER A 457 1364 968 1635 162 -58 -222 A C ATOM 3691 O SER A 457 41.286 -9.565 45.253 1.00 11.86 A O ANISOU 3691 O SER A 457 1737 1151 1616 239 185 -146 A O ATOM 3692 CB SER A 457 42.247 -12.685 46.107 1.00 13.77 A C ANISOU 3692 CB SER A 457 2390 579 2260 923 67 -215 A C ATOM 3693 OG SER A 457 42.010 -12.750 44.747 1.00 17.51 A O ANISOU 3693 OG SER A 457 2509 1601 2543 173 -182 -484 A O ATOM 3694 N ILE A 458 40.263 -10.348 47.118 1.00 10.65 A N ANISOU 3694 N ILE A 458 1511 1165 1369 99 -38 -229 A N ATOM 3695 CA ILE A 458 39.040 -9.530 47.096 1.00 10.94 A C ANISOU 3695 CA ILE A 458 1481 1278 1396 158 -38 -116 A C ATOM 3696 C ILE A 458 38.918 -8.858 48.474 1.00 10.12 A C ANISOU 3696 C ILE A 458 1658 840 1348 -10 136 201 A C ATOM 3697 O ILE A 458 39.541 -9.305 49.441 1.00 9.81 A O ANISOU 3697 O ILE A 458 1438 887 1402 -22 91 -36 A O ATOM 3698 CB ILE A 458 37.805 -10.391 46.775 1.00 12.72 A C ANISOU 3698 CB ILE A 458 1603 1386 1842 6 -228 -45 A C ATOM 3699 CG1 ILE A 458 37.558 -11.431 47.871 1.00 13.60 A C ANISOU 3699 CG1 ILE A 458 1902 1728 1537 -387 -254 -311 A C ATOM 3700 CG2 ILE A 458 37.916 -11.023 45.405 1.00 13.18 A C ANISOU 3700 CG2 ILE A 458 1851 1379 1776 113 -96 -146 A C ATOM 3701 CD1 ILE A 458 36.133 -11.948 47.912 1.00 13.57 A C ANISOU 3701 CD1 ILE A 458 1753 1113 2289 -123 210 -191 A C ATOM 3702 N PRO A 459 38.143 -7.763 48.607 1.00 11.05 A N ANISOU 3702 N PRO A 459 1553 1034 1610 24 -23 -59 A N ATOM 3703 CA PRO A 459 37.919 -7.137 49.896 1.00 11.24 A C ANISOU 3703 CA PRO A 459 1697 887 1686 -214 29 17 A C ATOM 3704 C PRO A 459 36.847 -7.911 50.657 1.00 10.77 A C ANISOU 3704 C PRO A 459 1612 1001 1477 -154 184 -298 A C ATOM 3705 O PRO A 459 35.659 -7.822 50.340 1.00 11.57 A O ANISOU 3705 O PRO A 459 1664 987 1743 -202 81 -20 A O ATOM 3706 CB PRO A 459 37.481 -5.716 49.525 1.00 10.94 A C ANISOU 3706 CB PRO A 459 1654 905 1594 -155 10 -2 A C ATOM 3707 CG PRO A 459 36.811 -5.889 48.162 1.00 11.28 A C ANISOU 3707 CG PRO A 459 1632 1039 1612 139 43 -131 A C ATOM 3708 CD PRO A 459 37.433 -7.106 47.520 1.00 11.39 A C ANISOU 3708 CD PRO A 459 1815 1088 1424 77 -68 -290 A C ATOM 3709 N THR A 460 37.307 -8.650 51.642 1.00 11.23 A N ANISOU 3709 N THR A 460 1346 1332 1586 -2 115 -159 A N ATOM 3710 CA THR A 460 36.439 -9.565 52.379 1.00 10.67 A C ANISOU 3710 CA THR A 460 1439 1163 1452 -53 16 -83 A C ATOM 3711 C THR A 460 35.815 -8.894 53.607 1.00 11.55 A C ANISOU 3711 C THR A 460 1522 1035 1830 -145 199 -318 A C ATOM 3712 O THR A 460 36.383 -7.963 54.172 1.00 11.28 A O ANISOU 3712 O THR A 460 1566 903 1817 -123 168 -282 A O ATOM 3713 CB THR A 460 37.149 -10.840 52.855 1.00 11.28 A C ANISOU 3713 CB THR A 460 1410 1172 1701 -18 64 -33 A C ATOM 3714 CG2 THR A 460 37.650 -11.707 51.725 1.00 12.02 A C ANISOU 3714 CG2 THR A 460 1674 1369 1524 -17 -123 -173 A C ATOM 3715 OG1 THR A 460 38.270 -10.531 53.674 1.00 10.98 A O ANISOU 3715 OG1 THR A 460 1543 903 1722 -105 -16 -151 A O ATOM 3716 N ASP A 461 34.619 -9.359 53.991 1.00 10.81 A N ANISOU 3716 N ASP A 461 1527 1028 1550 -28 152 -355 A N ATOM 3717 CA ASP A 461 34.033 -8.961 55.227 1.00 10.55 A C ANISOU 3717 CA ASP A 461 1705 956 1348 -78 175 -38 A C ATOM 3718 C ASP A 461 34.862 -9.416 56.431 1.00 10.44 A C ANISOU 3718 C ASP A 461 1575 830 1559 33 45 -48 A C ATOM 3719 O ASP A 461 35.051 -8.689 57.399 1.00 11.74 A O ANISOU 3719 O ASP A 461 1873 1138 1446 -7 -97 12 A O ATOM 3720 CB ASP A 461 32.603 -9.463 55.399 1.00 11.12 A C ANISOU 3720 CB ASP A 461 1570 937 1715 79 149 -18 A C ATOM 3721 CG ASP A 461 32.414 -10.983 55.388 1.00 11.49 A C ANISOU 3721 CG ASP A 461 1779 969 1617 136 164 -52 A C ATOM 3722 OD1 ASP A 461 33.093 -11.685 54.600 1.00 11.71 A O ANISOU 3722 OD1 ASP A 461 1671 905 1872 -59 146 -323 A O ATOM 3723 OD2 ASP A 461 31.554 -11.429 56.193 1.00 14.24 A O ANISOU 3723 OD2 ASP A 461 2107 1113 2188 -27 495 -59 A O ATOM 3724 N CYS A 462 35.302 -10.686 56.386 1.00 10.22 A N ANISOU 3724 N CYS A 462 1706 719 1457 -55 113 64 A N ATOM 3725 CA CYS A 462 36.088 -11.245 57.471 1.00 12.02 A C ANISOU 3725 CA CYS A 462 1928 1095 1544 125 9 -19 A C ATOM 3726 C CYS A 462 36.951 -12.390 56.940 1.00 11.19 A C ANISOU 3726 C CYS A 462 1528 1045 1676 -58 -7 -24 A C ATOM 3727 O CYS A 462 36.745 -12.825 55.825 1.00 12.10 A O ANISOU 3727 O CYS A 462 1761 1008 1826 100 -230 -21 A O ATOM 3728 CB CYS A 462 35.215 -11.740 58.626 1.00 13.24 A C ANISOU 3728 CB CYS A 462 2154 987 1889 51 241 105 A C ATOM 3729 SG CYS A 462 33.998 -13.001 58.168 1.00 14.98 A S ANISOU 3729 SG CYS A 462 2100 1265 2324 -74 133 312 A S ATOM 3730 N PRO A 463 37.996 -12.782 57.679 1.00 11.09 A N ANISOU 3730 N PRO A 463 1492 956 1765 0 -94 -124 A N ATOM 3731 CA PRO A 463 38.943 -13.786 57.214 1.00 11.20 A C ANISOU 3731 CA PRO A 463 1545 1197 1513 103 51 -94 A C ATOM 3732 C PRO A 463 38.925 -15.120 57.950 1.00 11.02 A C ANISOU 3732 C PRO A 463 1605 1287 1292 272 -212 -37 A C ATOM 3733 O PRO A 463 39.743 -15.942 57.608 1.00 12.64 A O ANISOU 3733 O PRO A 463 1893 1242 1665 202 79 -61 A O ATOM 3734 CB PRO A 463 40.266 -13.073 57.592 1.00 12.62 A C ANISOU 3734 CB PRO A 463 1919 1094 1783 117 -252 -127 A C ATOM 3735 CG PRO A 463 39.962 -12.432 58.930 1.00 12.89 A C ANISOU 3735 CG PRO A 463 1975 1047 1875 -80 -106 -92 A C ATOM 3736 CD PRO A 463 38.487 -12.079 58.873 1.00 12.54 A C ANISOU 3736 CD PRO A 463 2127 1016 1618 66 -134 78 A C ATOM 3737 N GLN A 464 38.008 -15.316 58.885 1.00 11.37 A N ANISOU 3737 N GLN A 464 1754 1015 1550 267 -1 -90 A N ATOM 3738 CA GLN A 464 38.142 -16.462 59.825 1.00 11.57 A C ANISOU 3738 CA GLN A 464 1597 1214 1584 225 113 126 A C ATOM 3739 C GLN A 464 37.008 -17.476 59.716 1.00 11.36 A C ANISOU 3739 C GLN A 464 1893 1004 1417 108 263 -32 A C ATOM 3740 O GLN A 464 37.314 -18.677 59.722 1.00 12.70 A O ANISOU 3740 O GLN A 464 2176 977 1670 266 188 -102 A O ATOM 3741 CB GLN A 464 38.335 -15.926 61.249 1.00 12.83 A C ANISOU 3741 CB GLN A 464 1836 1181 1856 52 -151 -134 A C ATOM 3742 CG GLN A 464 37.088 -15.454 61.988 1.00 13.23 A C ANISOU 3742 CG GLN A 464 2155 1112 1759 -55 22 -22 A C ATOM 3743 CD GLN A 464 36.415 -14.244 61.389 1.00 12.99 A C ANISOU 3743 CD GLN A 464 2167 878 1888 -17 185 -152 A C ATOM 3744 NE2 GLN A 464 36.622 -13.071 61.979 1.00 13.29 A N ANISOU 3744 NE2 GLN A 464 2117 1277 1652 67 0 -370 A N ATOM 3745 OE1 GLN A 464 35.694 -14.350 60.402 1.00 14.59 A O ANISOU 3745 OE1 GLN A 464 2212 1146 2182 60 165 -232 A O ATOM 3746 N ARG A 465 35.761 -17.055 59.656 1.00 11.85 A N ANISOU 3746 N ARG A 465 1865 1244 1393 -54 191 8 A N ATOM 3747 CA ARG A 465 34.627 -17.947 59.685 1.00 11.84 A C ANISOU 3747 CA ARG A 465 1704 1294 1497 26 201 276 A C ATOM 3748 C ARG A 465 34.300 -18.431 58.265 1.00 11.72 A C ANISOU 3748 C ARG A 465 1732 1021 1700 -57 229 -14 A C ATOM 3749 O ARG A 465 35.063 -18.255 57.326 1.00 11.31 A O ANISOU 3749 O ARG A 465 1832 882 1580 -29 204 -33 A O ATOM 3750 CB ARG A 465 33.431 -17.299 60.396 1.00 12.28 A C ANISOU 3750 CB ARG A 465 1982 1177 1507 -38 425 146 A C ATOM 3751 CG ARG A 465 32.775 -16.142 59.649 1.00 12.23 A C ANISOU 3751 CG ARG A 465 2023 972 1651 17 211 -60 A C ATOM 3752 CD ARG A 465 31.739 -15.465 60.519 1.00 13.14 A C ANISOU 3752 CD ARG A 465 1842 1386 1763 -39 216 7 A C ATOM 3753 NE ARG A 465 31.090 -14.359 59.847 1.00 12.66 A N ANISOU 3753 NE ARG A 465 2284 1243 1283 154 291 -256 A N ATOM 3754 CZ ARG A 465 30.695 -13.228 60.431 1.00 11.80 A C ANISOU 3754 CZ ARG A 465 1913 929 1638 -5 375 -65 A C ATOM 3755 NH1 ARG A 465 30.732 -13.142 61.750 1.00 13.48 A N ANISOU 3755 NH1 ARG A 465 2094 1301 1726 157 512 -159 A N ATOM 3756 NH2 ARG A 465 30.283 -12.213 59.668 1.00 13.27 A N ANISOU 3756 NH2 ARG A 465 1852 1242 1948 23 223 98 A N ATOM 3757 N ASP A 466 33.152 -19.105 58.162 1.00 11.52 A N ANISOU 3757 N ASP A 466 1790 890 1695 -35 160 36 A N ATOM 3758 CA ASP A 466 32.643 -19.672 56.914 1.00 11.59 A C ANISOU 3758 CA ASP A 466 1585 1036 1782 -109 189 -114 A C ATOM 3759 C ASP A 466 31.964 -18.604 56.068 1.00 11.87 A C ANISOU 3759 C ASP A 466 1747 1053 1707 -208 -76 -187 A C ATOM 3760 O ASP A 466 30.828 -18.703 55.754 1.00 11.70 A O ANISOU 3760 O ASP A 466 1823 852 1770 -100 165 -61 A O ATOM 3761 CB ASP A 466 31.711 -20.846 57.203 1.00 12.76 A C ANISOU 3761 CB ASP A 466 2141 849 1859 -138 269 234 A C ATOM 3762 CG ASP A 466 30.534 -20.526 58.107 1.00 14.59 A C ANISOU 3762 CG ASP A 466 1958 1677 1906 -393 227 -337 A C ATOM 3763 OD1 ASP A 466 30.512 -19.404 58.682 1.00 13.34 A O ANISOU 3763 OD1 ASP A 466 1910 1391 1767 -90 441 -59 A O ATOM 3764 OD2 ASP A 466 29.659 -21.363 58.233 1.00 13.34 A O ANISOU 3764 OD2 ASP A 466 1801 1416 1851 -131 555 -71 A O ATOM 3765 N GLU A 467 32.722 -17.569 55.756 1.00 10.54 A N ANISOU 3765 N GLU A 467 1412 1069 1524 -71 96 -73 A N ATOM 3766 CA GLU A 467 32.201 -16.432 54.968 1.00 11.29 A C ANISOU 3766 CA GLU A 467 1569 1209 1511 97 87 -27 A C ATOM 3767 C GLU A 467 33.349 -15.947 54.085 1.00 10.57 A C ANISOU 3767 C GLU A 467 1703 803 1507 -197 1 -23 A C ATOM 3768 O GLU A 467 33.640 -16.560 53.106 1.00 11.15 A O ANISOU 3768 O GLU A 467 1767 891 1575 72 225 81 A O ATOM 3769 CB GLU A 467 31.548 -15.412 55.916 1.00 10.91 A C ANISOU 3769 CB GLU A 467 1696 1144 1306 -143 175 -29 A C ATOM 3770 CG GLU A 467 30.672 -14.386 55.217 1.00 12.58 A C ANISOU 3770 CG GLU A 467 1737 1259 1780 -20 156 46 A C ATOM 3771 CD GLU A 467 29.604 -13.768 56.092 1.00 13.27 A C ANISOU 3771 CD GLU A 467 1780 1380 1881 -29 317 249 A C ATOM 3772 OE1 GLU A 467 29.603 -14.037 57.298 1.00 13.10 A O ANISOU 3772 OE1 GLU A 467 2110 1078 1788 105 317 153 A O ATOM 3773 OE2 GLU A 467 28.771 -13.031 55.562 1.00 12.83 A O ANISOU 3773 OE2 GLU A 467 1969 1013 1890 90 289 -29 A O ATOM 3774 N ARG A 468 33.955 -14.793 54.409 1.00 9.51 A N ANISOU 3774 N ARG A 468 1533 623 1458 126 102 -149 A N ATOM 3775 CA ARG A 468 35.127 -14.281 53.657 1.00 11.07 A C ANISOU 3775 CA ARG A 468 1509 1112 1585 88 89 46 A C ATOM 3776 C ARG A 468 34.676 -13.956 52.236 1.00 9.61 A C ANISOU 3776 C ARG A 468 1337 807 1507 53 145 -56 A C ATOM 3777 O ARG A 468 35.330 -14.315 51.273 1.00 10.61 A O ANISOU 3777 O ARG A 468 1631 825 1572 -3 228 -147 A O ATOM 3778 CB ARG A 468 36.342 -15.221 53.736 1.00 11.54 A C ANISOU 3778 CB ARG A 468 1651 958 1776 137 55 22 A C ATOM 3779 CG ARG A 468 36.509 -16.012 55.028 1.00 11.75 A C ANISOU 3779 CG ARG A 468 1673 1037 1752 -72 -56 2 A C ATOM 3780 CD ARG A 468 37.726 -16.886 54.995 1.00 12.03 A C ANISOU 3780 CD ARG A 468 1646 1002 1920 -64 165 147 A C ATOM 3781 NE ARG A 468 37.698 -17.845 56.066 1.00 11.28 A N ANISOU 3781 NE ARG A 468 1770 796 1719 69 331 -3 A N ATOM 3782 CZ ARG A 468 38.686 -18.700 56.294 1.00 11.65 A C ANISOU 3782 CZ ARG A 468 1814 1157 1452 90 -28 -70 A C ATOM 3783 NH1 ARG A 468 39.777 -18.653 55.564 1.00 10.94 A N ANISOU 3783 NH1 ARG A 468 1804 644 1709 -29 -29 -20 A N ATOM 3784 NH2 ARG A 468 38.595 -19.609 57.260 1.00 12.11 A N ANISOU 3784 NH2 ARG A 468 2052 1136 1410 -64 91 16 A N ATOM 3785 N LEU A 469 33.561 -13.209 52.127 1.00 10.23 A N ANISOU 3785 N LEU A 469 1503 814 1569 258 5 -225 A N ATOM 3786 CA LEU A 469 32.975 -12.887 50.838 1.00 9.84 A C ANISOU 3786 CA LEU A 469 1604 674 1458 -131 -37 -104 A C ATOM 3787 C LEU A 469 33.179 -11.395 50.550 1.00 8.86 A C ANISOU 3787 C LEU A 469 1211 702 1451 122 -7 3 A C ATOM 3788 O LEU A 469 33.409 -10.571 51.489 1.00 10.91 A O ANISOU 3788 O LEU A 469 1698 881 1564 -105 5 -102 A O ATOM 3789 CB LEU A 469 31.470 -13.184 50.868 1.00 9.83 A C ANISOU 3789 CB LEU A 469 1575 760 1397 39 -52 68 A C ATOM 3790 CG LEU A 469 31.100 -14.597 51.319 1.00 10.44 A C ANISOU 3790 CG LEU A 469 1665 738 1561 -5 -84 100 A C ATOM 3791 CD1 LEU A 469 29.597 -14.754 51.413 1.00 11.87 A C ANISOU 3791 CD1 LEU A 469 1766 911 1833 -254 272 -33 A C ATOM 3792 CD2 LEU A 469 31.710 -15.675 50.399 1.00 10.89 A C ANISOU 3792 CD2 LEU A 469 1613 759 1763 -174 113 -4 A C ATOM 3793 N GLY A 470 33.062 -11.064 49.267 1.00 8.89 A N ANISOU 3793 N GLY A 470 1344 612 1422 27 -29 -63 A N ATOM 3794 CA GLY A 470 33.279 -9.662 48.855 1.00 10.17 A C ANISOU 3794 CA GLY A 470 1663 620 1577 39 8 -23 A C ATOM 3795 C GLY A 470 32.078 -8.763 49.104 1.00 10.27 A C ANISOU 3795 C GLY A 470 1418 924 1558 -87 40 -93 A C ATOM 3796 O GLY A 470 31.418 -8.322 48.162 1.00 10.04 A O ANISOU 3796 O GLY A 470 1412 913 1488 -51 84 -74 A O ATOM 3797 N TRP A 471 31.748 -8.600 50.388 1.00 10.85 A N ANISOU 3797 N TRP A 471 1582 941 1597 205 116 -15 A N ATOM 3798 CA TRP A 471 30.559 -7.828 50.771 1.00 10.11 A C ANISOU 3798 CA TRP A 471 1557 823 1459 168 149 -71 A C ATOM 3799 C TRP A 471 30.664 -6.351 50.330 1.00 9.54 A C ANISOU 3799 C TRP A 471 1388 877 1358 83 -18 -20 A C ATOM 3800 O TRP A 471 31.606 -5.619 50.656 1.00 10.83 A O ANISOU 3800 O TRP A 471 1400 1065 1649 55 -49 -171 A O ATOM 3801 CB TRP A 471 30.315 -7.955 52.263 1.00 10.41 A C ANISOU 3801 CB TRP A 471 1633 896 1425 88 125 -153 A C ATOM 3802 CG TRP A 471 29.588 -9.217 52.639 1.00 10.58 A C ANISOU 3802 CG TRP A 471 1601 762 1656 117 21 -221 A C ATOM 3803 CD1 TRP A 471 30.122 -10.373 53.127 1.00 11.06 A C ANISOU 3803 CD1 TRP A 471 1560 1135 1507 189 69 -15 A C ATOM 3804 CD2 TRP A 471 28.171 -9.411 52.596 1.00 10.85 A C ANISOU 3804 CD2 TRP A 471 1657 995 1470 27 233 -60 A C ATOM 3805 CE2 TRP A 471 27.913 -10.718 53.055 1.00 12.79 A C ANISOU 3805 CE2 TRP A 471 1860 1127 1873 -88 124 65 A C ATOM 3806 CE3 TRP A 471 27.112 -8.607 52.205 1.00 12.78 A C ANISOU 3806 CE3 TRP A 471 1730 1285 1838 234 268 -98 A C ATOM 3807 NE1 TRP A 471 29.122 -11.267 53.389 1.00 12.51 A N ANISOU 3807 NE1 TRP A 471 1811 1224 1716 -30 138 -20 A N ATOM 3808 CZ2 TRP A 471 26.620 -11.215 53.146 1.00 13.63 A C ANISOU 3808 CZ2 TRP A 471 1881 1370 1926 20 102 149 A C ATOM 3809 CZ3 TRP A 471 25.831 -9.090 52.287 1.00 13.32 A C ANISOU 3809 CZ3 TRP A 471 1741 1486 1834 154 133 140 A C ATOM 3810 CH2 TRP A 471 25.594 -10.402 52.741 1.00 14.27 A C ANISOU 3810 CH2 TRP A 471 1676 1689 2054 81 192 230 A C ATOM 3811 N THR A 472 29.674 -5.953 49.545 1.00 9.63 A N ANISOU 3811 N THR A 472 1286 847 1525 10 -84 -4 A N ATOM 3812 CA THR A 472 29.686 -4.652 48.864 1.00 9.27 A C ANISOU 3812 CA THR A 472 1186 842 1494 32 145 36 A C ATOM 3813 C THR A 472 29.578 -3.465 49.829 1.00 10.05 A C ANISOU 3813 C THR A 472 1295 973 1551 -52 112 -13 A C ATOM 3814 O THR A 472 30.265 -2.472 49.679 1.00 11.30 A O ANISOU 3814 O THR A 472 1690 847 1753 -144 138 -70 A O ATOM 3815 CB THR A 472 28.605 -4.675 47.779 1.00 9.70 A C ANISOU 3815 CB THR A 472 1445 795 1445 119 60 29 A C ATOM 3816 CG2 THR A 472 29.006 -5.588 46.649 1.00 10.33 A C ANISOU 3816 CG2 THR A 472 1436 812 1677 14 -45 -145 A C ATOM 3817 OG1 THR A 472 27.338 -5.070 48.324 1.00 10.47 A O ANISOU 3817 OG1 THR A 472 1308 964 1705 119 55 -71 A O ATOM 3818 N GLY A 473 28.676 -3.546 50.809 1.00 9.79 A N ANISOU 3818 N GLY A 473 1458 524 1735 -78 320 -127 A N ATOM 3819 CA GLY A 473 28.483 -2.416 51.683 1.00 10.32 A C ANISOU 3819 CA GLY A 473 1426 867 1627 246 17 -296 A C ATOM 3820 C GLY A 473 29.729 -2.131 52.508 1.00 9.92 A C ANISOU 3820 C GLY A 473 1473 922 1374 49 30 -176 A C ATOM 3821 O GLY A 473 30.095 -0.964 52.751 1.00 11.07 A O ANISOU 3821 O GLY A 473 1528 985 1690 -220 -38 -176 A O ATOM 3822 N ASP A 474 30.429 -3.169 52.976 1.00 10.96 A N ANISOU 3822 N ASP A 474 1426 960 1778 112 58 -119 A N ATOM 3823 CA ASP A 474 31.561 -2.998 53.853 1.00 10.73 A C ANISOU 3823 CA ASP A 474 1605 947 1524 39 89 -129 A C ATOM 3824 C ASP A 474 32.670 -2.202 53.131 1.00 10.51 A C ANISOU 3824 C ASP A 474 1472 1147 1373 -87 -125 -165 A C ATOM 3825 O ASP A 474 33.270 -1.303 53.722 1.00 10.87 A O ANISOU 3825 O ASP A 474 1614 940 1575 -77 -17 -226 A O ATOM 3826 CB ASP A 474 32.111 -4.345 54.342 1.00 11.11 A C ANISOU 3826 CB ASP A 474 1567 810 1844 -59 83 -125 A C ATOM 3827 CG ASP A 474 31.120 -5.251 55.047 1.00 12.67 A C ANISOU 3827 CG ASP A 474 1726 1363 1724 -107 162 -45 A C ATOM 3828 OD1 ASP A 474 29.999 -5.418 54.503 1.00 13.02 A O ANISOU 3828 OD1 ASP A 474 1829 973 2144 -36 32 -47 A O ATOM 3829 OD2 ASP A 474 31.469 -5.747 56.146 1.00 13.13 A O ANISOU 3829 OD2 ASP A 474 1931 1311 1745 -175 101 -14 A O ATOM 3830 N ILE A 475 32.956 -2.555 51.872 1.00 10.35 A N ANISOU 3830 N ILE A 475 1485 940 1506 -94 240 -200 A N ATOM 3831 CA ILE A 475 33.999 -1.856 51.146 1.00 10.02 A C ANISOU 3831 CA ILE A 475 1221 1216 1368 118 138 -156 A C ATOM 3832 C ILE A 475 33.545 -0.445 50.766 1.00 10.55 A C ANISOU 3832 C ILE A 475 1343 1169 1494 -123 37 -178 A C ATOM 3833 O ILE A 475 34.363 0.455 50.713 1.00 10.27 A O ANISOU 3833 O ILE A 475 1412 866 1622 -13 -49 -119 A O ATOM 3834 CB ILE A 475 34.581 -2.690 49.986 1.00 10.43 A C ANISOU 3834 CB ILE A 475 1593 996 1372 127 303 -52 A C ATOM 3835 CG1 ILE A 475 35.778 -1.999 49.347 1.00 10.16 A C ANISOU 3835 CG1 ILE A 475 1449 1131 1281 108 261 -119 A C ATOM 3836 CG2 ILE A 475 33.538 -3.045 48.963 1.00 10.57 A C ANISOU 3836 CG2 ILE A 475 1626 933 1454 0 280 -167 A C ATOM 3837 CD1 ILE A 475 36.937 -1.725 50.310 1.00 11.88 A C ANISOU 3837 CD1 ILE A 475 1459 1378 1674 35 156 39 A C ATOM 3838 N HIS A 476 32.254 -0.259 50.535 1.00 9.42 A N ANISOU 3838 N HIS A 476 1306 581 1691 -22 28 -42 A N ATOM 3839 CA HIS A 476 31.741 1.091 50.316 1.00 9.33 A C ANISOU 3839 CA HIS A 476 1288 797 1460 239 125 -52 A C ATOM 3840 C HIS A 476 32.104 1.966 51.527 1.00 10.64 A C ANISOU 3840 C HIS A 476 1508 1049 1485 -159 -77 -2 A C ATOM 3841 O HIS A 476 32.641 3.079 51.383 1.00 10.63 A O ANISOU 3841 O HIS A 476 1628 787 1625 -33 -21 -29 A O ATOM 3842 CB HIS A 476 30.241 1.053 50.008 1.00 9.09 A C ANISOU 3842 CB HIS A 476 1290 625 1538 131 123 -69 A C ATOM 3843 CG HIS A 476 29.630 2.367 49.629 1.00 9.79 A C ANISOU 3843 CG HIS A 476 1432 578 1709 119 27 -90 A C ATOM 3844 CD2 HIS A 476 30.135 3.611 49.492 1.00 12.44 A C ANISOU 3844 CD2 HIS A 476 1513 967 2243 -245 -1 134 A C ATOM 3845 ND1 HIS A 476 28.256 2.476 49.448 1.00 10.08 A N ANISOU 3845 ND1 HIS A 476 1460 790 1579 425 31 26 A N ATOM 3846 CE1 HIS A 476 27.955 3.752 49.168 1.00 11.62 A C ANISOU 3846 CE1 HIS A 476 1328 897 2188 515 137 135 A C ATOM 3847 NE2 HIS A 476 29.091 4.451 49.177 1.00 14.73 A N ANISOU 3847 NE2 HIS A 476 1639 1532 2426 33 23 33 A N ATOM 3848 N ALA A 477 31.810 1.493 52.725 1.00 9.39 A N ANISOU 3848 N ALA A 477 1396 712 1457 7 -9 -119 A N ATOM 3849 CA ALA A 477 32.081 2.248 53.948 1.00 10.30 A C ANISOU 3849 CA ALA A 477 1511 1085 1317 147 13 -198 A C ATOM 3850 C ALA A 477 33.577 2.469 54.193 1.00 10.07 A C ANISOU 3850 C ALA A 477 1530 851 1443 107 15 -88 A C ATOM 3851 O ALA A 477 33.979 3.551 54.642 1.00 11.81 A O ANISOU 3851 O ALA A 477 1580 931 1974 -43 -103 -179 A O ATOM 3852 CB ALA A 477 31.474 1.535 55.152 1.00 11.60 A C ANISOU 3852 CB ALA A 477 1721 1136 1548 156 196 -137 A C ATOM 3853 N PHE A 478 34.403 1.479 53.873 1.00 9.68 A N ANISOU 3853 N PHE A 478 1406 913 1356 53 70 -248 A N ATOM 3854 CA PHE A 478 35.819 1.479 54.307 1.00 9.00 A C ANISOU 3854 CA PHE A 478 1538 539 1342 43 16 -272 A C ATOM 3855 C PHE A 478 36.780 2.101 53.269 1.00 9.03 A C ANISOU 3855 C PHE A 478 1418 589 1421 143 -53 -123 A C ATOM 3856 O PHE A 478 37.906 2.412 53.647 1.00 9.38 A O ANISOU 3856 O PHE A 478 1361 719 1481 14 -66 -88 A O ATOM 3857 CB PHE A 478 36.258 0.046 54.650 1.00 8.82 A C ANISOU 3857 CB PHE A 478 1423 558 1371 -6 0 -148 A C ATOM 3858 CG PHE A 478 37.626 -0.032 55.282 1.00 9.57 A C ANISOU 3858 CG PHE A 478 1504 674 1457 113 -160 -95 A C ATOM 3859 CD1 PHE A 478 37.852 0.519 56.541 1.00 10.48 A C ANISOU 3859 CD1 PHE A 478 1362 1057 1561 146 -102 -266 A C ATOM 3860 CD2 PHE A 478 38.673 -0.680 54.635 1.00 9.93 A C ANISOU 3860 CD2 PHE A 478 1428 876 1466 -78 -45 -89 A C ATOM 3861 CE1 PHE A 478 39.112 0.490 57.107 1.00 10.16 A C ANISOU 3861 CE1 PHE A 478 1590 917 1351 -12 -331 -182 A C ATOM 3862 CE2 PHE A 478 39.938 -0.713 55.207 1.00 9.98 A C ANISOU 3862 CE2 PHE A 478 1489 856 1447 -86 -58 95 A C ATOM 3863 CZ PHE A 478 40.145 -0.135 56.447 1.00 11.24 A C ANISOU 3863 CZ PHE A 478 1462 1259 1549 -10 -231 -74 A C ATOM 3864 N SER A 479 36.408 2.227 51.985 1.00 8.92 A N ANISOU 3864 N SER A 479 1186 790 1411 139 -76 -109 A N ATOM 3865 CA SER A 479 37.464 2.481 50.969 1.00 10.52 A C ANISOU 3865 CA SER A 479 1656 757 1583 -44 61 189 A C ATOM 3866 C SER A 479 38.143 3.873 51.160 1.00 9.05 A C ANISOU 3866 C SER A 479 1364 831 1242 7 -66 13 A C ATOM 3867 O SER A 479 39.326 3.981 50.824 1.00 10.85 A O ANISOU 3867 O SER A 479 1473 1047 1599 -126 33 -114 A O ATOM 3868 CB SER A 479 36.968 2.269 49.540 1.00 11.07 A C ANISOU 3868 CB SER A 479 1957 716 1532 0 306 48 A C ATOM 3869 OG SER A 479 36.390 3.427 49.006 1.00 11.03 A O ANISOU 3869 OG SER A 479 1503 903 1784 -33 4 4 A O ATOM 3870 N ARG A 480 37.458 4.890 51.747 1.00 9.70 A N ANISOU 3870 N ARG A 480 1250 1061 1373 -89 12 -52 A N ATOM 3871 CA ARG A 480 38.109 6.151 51.985 1.00 10.72 A C ANISOU 3871 CA ARG A 480 1363 1126 1582 -198 32 -67 A C ATOM 3872 C ARG A 480 39.324 5.972 52.909 1.00 9.96 A C ANISOU 3872 C ARG A 480 1394 1186 1201 -52 116 -210 A C ATOM 3873 O ARG A 480 40.384 6.596 52.719 1.00 11.29 A O ANISOU 3873 O ARG A 480 1420 1078 1790 -57 104 -83 A O ATOM 3874 CB ARG A 480 37.090 7.130 52.578 1.00 11.35 A C ANISOU 3874 CB ARG A 480 1260 1237 1815 -225 104 -114 A C ATOM 3875 CG ARG A 480 37.570 8.551 52.811 1.00 11.41 A C ANISOU 3875 CG ARG A 480 1581 1115 1640 -168 4 80 A C ATOM 3876 CD ARG A 480 36.361 9.365 53.209 1.00 12.98 A C ANISOU 3876 CD ARG A 480 1788 1029 2114 -68 -41 -174 A C ATOM 3877 NE ARG A 480 36.676 10.739 53.568 1.00 12.56 A N ANISOU 3877 NE ARG A 480 1577 1154 2039 -130 -165 -191 A N ATOM 3878 CZ ARG A 480 35.715 11.659 53.794 1.00 13.30 A C ANISOU 3878 CZ ARG A 480 1978 1057 2016 102 -253 -235 A C ATOM 3879 NH1 ARG A 480 34.423 11.379 53.595 1.00 15.09 A N ANISOU 3879 NH1 ARG A 480 1926 1588 2219 79 144 -455 A N ATOM 3880 NH2 ARG A 480 36.062 12.874 54.177 1.00 15.69 A N ANISOU 3880 NH2 ARG A 480 2608 931 2423 50 -219 -311 A N ATOM 3881 N THR A 481 39.168 5.134 53.927 1.00 10.20 A N ANISOU 3881 N THR A 481 1466 1047 1362 -203 -100 -122 A N ATOM 3882 CA THR A 481 40.233 4.758 54.826 1.00 10.28 A C ANISOU 3882 CA THR A 481 1494 1043 1367 83 -61 -371 A C ATOM 3883 C THR A 481 41.291 3.891 54.088 1.00 10.42 A C ANISOU 3883 C THR A 481 1400 1123 1436 14 136 -173 A C ATOM 3884 O THR A 481 42.509 4.127 54.147 1.00 11.21 A O ANISOU 3884 O THR A 481 1495 974 1788 56 -54 -119 A O ATOM 3885 CB THR A 481 39.673 4.035 56.064 1.00 11.35 A C ANISOU 3885 CB THR A 481 1704 1073 1532 128 -41 -250 A C ATOM 3886 CG2 THR A 481 40.795 3.645 57.012 1.00 11.98 A C ANISOU 3886 CG2 THR A 481 1625 1250 1674 153 20 -122 A C ATOM 3887 OG1 THR A 481 38.725 4.878 56.730 1.00 10.98 A O ANISOU 3887 OG1 THR A 481 1751 959 1461 12 33 -189 A O ATOM 3888 N ALA A 482 40.807 2.841 53.418 1.00 9.66 A N ANISOU 3888 N ALA A 482 1095 1027 1549 5 20 -105 A N ATOM 3889 CA ALA A 482 41.686 1.846 52.828 1.00 10.38 A C ANISOU 3889 CA ALA A 482 1320 932 1689 86 -53 -146 A C ATOM 3890 C ALA A 482 42.671 2.474 51.841 1.00 9.91 A C ANISOU 3890 C ALA A 482 1502 795 1469 109 -50 -142 A C ATOM 3891 O ALA A 482 43.849 2.153 51.831 1.00 10.68 A O ANISOU 3891 O ALA A 482 1547 682 1827 54 -45 -118 A O ATOM 3892 CB ALA A 482 40.855 0.834 52.075 1.00 10.47 A C ANISOU 3892 CB ALA A 482 1505 769 1702 149 -96 -199 A C ATOM 3893 N ASN A 483 42.166 3.400 50.985 1.00 9.24 A N ANISOU 3893 N ASN A 483 1323 826 1362 36 -107 -152 A N ATOM 3894 CA ASN A 483 42.922 3.941 49.909 1.00 9.66 A C ANISOU 3894 CA ASN A 483 1525 876 1268 -30 -62 -214 A C ATOM 3895 C ASN A 483 44.022 4.921 50.380 1.00 11.12 A C ANISOU 3895 C ASN A 483 1648 1009 1568 -213 55 -178 A C ATOM 3896 O ASN A 483 44.907 5.287 49.584 1.00 11.69 A O ANISOU 3896 O ASN A 483 1519 1096 1824 -179 11 -158 A O ATOM 3897 CB ASN A 483 42.028 4.731 48.947 1.00 10.05 A C ANISOU 3897 CB ASN A 483 1292 918 1608 -42 -38 -41 A C ATOM 3898 CG ASN A 483 40.949 3.940 48.252 1.00 9.30 A C ANISOU 3898 CG ASN A 483 1252 880 1401 52 -57 -58 A C ATOM 3899 ND2 ASN A 483 40.135 4.593 47.422 1.00 10.12 A N ANISOU 3899 ND2 ASN A 483 1293 867 1683 52 -295 -153 A N ATOM 3900 OD1 ASN A 483 40.917 2.687 48.362 1.00 10.08 A O ANISOU 3900 OD1 ASN A 483 1451 815 1563 -9 114 -241 A O ATOM 3901 N PHE A 484 43.962 5.317 51.651 1.00 9.94 A N ANISOU 3901 N PHE A 484 1507 770 1497 -159 -60 39 A N ATOM 3902 CA PHE A 484 45.025 6.082 52.253 1.00 10.41 A C ANISOU 3902 CA PHE A 484 1412 955 1586 -89 -87 -169 A C ATOM 3903 C PHE A 484 46.119 5.147 52.792 1.00 10.00 A C ANISOU 3903 C PHE A 484 1348 922 1527 -64 45 -77 A C ATOM 3904 O PHE A 484 47.337 5.422 52.688 1.00 10.89 A O ANISOU 3904 O PHE A 484 1425 802 1908 -110 -49 -160 A O ATOM 3905 CB PHE A 484 44.448 6.925 53.394 1.00 10.85 A C ANISOU 3905 CB PHE A 484 1410 826 1886 16 -64 -195 A C ATOM 3906 CG PHE A 484 45.413 7.869 54.060 1.00 11.35 A C ANISOU 3906 CG PHE A 484 1641 1020 1650 -62 23 -373 A C ATOM 3907 CD1 PHE A 484 46.222 7.458 55.103 1.00 13.20 A C ANISOU 3907 CD1 PHE A 484 1639 1599 1775 -68 -130 -365 A C ATOM 3908 CD2 PHE A 484 45.474 9.208 53.683 1.00 12.95 A C ANISOU 3908 CD2 PHE A 484 1563 1165 2192 -166 -279 21 A C ATOM 3909 CE1 PHE A 484 47.081 8.346 55.751 1.00 13.90 A C ANISOU 3909 CE1 PHE A 484 1515 1647 2120 -50 -325 -296 A C ATOM 3910 CE2 PHE A 484 46.291 10.110 54.365 1.00 15.52 A C ANISOU 3910 CE2 PHE A 484 2353 1661 1882 -386 -212 -415 A C ATOM 3911 CZ PHE A 484 47.104 9.674 55.388 1.00 13.23 A C ANISOU 3911 CZ PHE A 484 1582 1465 1978 -134 -12 -612 A C ATOM 3912 N ILE A 485 45.708 4.024 53.400 1.00 10.24 A N ANISOU 3912 N ILE A 485 1458 922 1507 -99 -109 34 A N ATOM 3913 CA ILE A 485 46.699 3.156 54.076 1.00 10.05 A C ANISOU 3913 CA ILE A 485 1258 1082 1476 15 -129 -253 A C ATOM 3914 C ILE A 485 47.579 2.400 53.070 1.00 9.91 A C ANISOU 3914 C ILE A 485 1489 824 1453 141 -155 -42 A C ATOM 3915 O ILE A 485 48.780 2.284 53.287 1.00 10.35 A O ANISOU 3915 O ILE A 485 1416 878 1638 26 -95 -154 A O ATOM 3916 CB ILE A 485 46.006 2.213 55.071 1.00 11.03 A C ANISOU 3916 CB ILE A 485 1367 1203 1619 -39 -38 -193 A C ATOM 3917 CG1 ILE A 485 45.199 3.004 56.112 1.00 12.63 A C ANISOU 3917 CG1 ILE A 485 1567 1348 1883 41 179 -147 A C ATOM 3918 CG2 ILE A 485 47.007 1.269 55.720 1.00 11.31 A C ANISOU 3918 CG2 ILE A 485 1422 1205 1669 11 58 -92 A C ATOM 3919 CD1 ILE A 485 44.472 2.143 57.081 1.00 12.92 A C ANISOU 3919 CD1 ILE A 485 1511 1763 1633 -114 8 -89 A C ATOM 3920 N TYR A 486 46.947 1.902 51.989 1.00 10.36 A N ANISOU 3920 N TYR A 486 1444 1056 1435 40 -137 -146 A N ATOM 3921 CA TYR A 486 47.668 1.179 50.950 1.00 10.15 A C ANISOU 3921 CA TYR A 486 1540 822 1495 -95 -110 -271 A C ATOM 3922 C TYR A 486 47.209 1.673 49.582 1.00 10.90 A C ANISOU 3922 C TYR A 486 1563 995 1582 -22 43 -89 A C ATOM 3923 O TYR A 486 46.106 2.186 49.441 1.00 10.82 A O ANISOU 3923 O TYR A 486 1590 959 1561 47 -82 -79 A O ATOM 3924 CB TYR A 486 47.367 -0.325 51.009 1.00 10.41 A C ANISOU 3924 CB TYR A 486 1586 847 1523 -33 -77 -275 A C ATOM 3925 CG TYR A 486 48.079 -1.142 52.073 1.00 10.57 A C ANISOU 3925 CG TYR A 486 1730 796 1488 -11 -129 -305 A C ATOM 3926 CD1 TYR A 486 49.348 -1.660 51.835 1.00 10.98 A C ANISOU 3926 CD1 TYR A 486 1812 926 1432 23 -65 -63 A C ATOM 3927 CD2 TYR A 486 47.511 -1.390 53.314 1.00 11.21 A C ANISOU 3927 CD2 TYR A 486 1723 995 1538 120 -164 -161 A C ATOM 3928 CE1 TYR A 486 50.010 -2.420 52.793 1.00 11.07 A C ANISOU 3928 CE1 TYR A 486 1799 754 1652 139 -165 -207 A C ATOM 3929 CE2 TYR A 486 48.164 -2.142 54.274 1.00 11.32 A C ANISOU 3929 CE2 TYR A 486 1838 1026 1436 113 -32 -60 A C ATOM 3930 CZ TYR A 486 49.427 -2.651 54.020 1.00 11.59 A C ANISOU 3930 CZ TYR A 486 1744 901 1760 -90 -150 -157 A C ATOM 3931 OH TYR A 486 50.096 -3.403 54.965 1.00 14.36 A O ANISOU 3931 OH TYR A 486 2194 1215 2046 103 -300 87 A O ATOM 3932 N ASP A 487 48.064 1.480 48.571 1.00 10.17 A N ANISOU 3932 N ASP A 487 1375 865 1624 -20 40 -97 A N ATOM 3933 CA ASP A 487 47.719 1.728 47.186 1.00 10.97 A C ANISOU 3933 CA ASP A 487 1645 882 1639 -35 -15 -51 A C ATOM 3934 C ASP A 487 46.840 0.569 46.688 1.00 10.18 A C ANISOU 3934 C ASP A 487 1351 964 1550 128 -42 -106 A C ATOM 3935 O ASP A 487 47.322 -0.513 46.320 1.00 10.66 A O ANISOU 3935 O ASP A 487 1347 924 1779 123 -1 -162 A O ATOM 3936 CB ASP A 487 48.963 1.930 46.336 1.00 12.41 A C ANISOU 3936 CB ASP A 487 1832 1271 1611 -109 39 -147 A C ATOM 3937 CG ASP A 487 48.655 2.290 44.890 1.00 13.93 A C ANISOU 3937 CG ASP A 487 1606 1815 1872 53 -89 148 A C ATOM 3938 OD1 ASP A 487 47.530 2.000 44.408 1.00 13.56 A O ANISOU 3938 OD1 ASP A 487 1653 1471 2028 -38 -94 6 A O ATOM 3939 OD2 ASP A 487 49.530 2.991 44.293 1.00 18.54 A O ANISOU 3939 OD2 ASP A 487 2061 2372 2612 -409 -6 337 A O ATOM 3940 N THR A 488 45.523 0.800 46.782 1.00 9.64 A N ANISOU 3940 N THR A 488 1220 700 1741 -121 110 -158 A N ATOM 3941 CA THR A 488 44.507 -0.182 46.447 1.00 9.13 A C ANISOU 3941 CA THR A 488 1431 402 1636 -45 -26 71 A C ATOM 3942 C THR A 488 44.023 -0.102 45.005 1.00 9.94 A C ANISOU 3942 C THR A 488 1368 929 1480 -49 31 -160 A C ATOM 3943 O THR A 488 43.088 -0.827 44.648 1.00 9.82 A O ANISOU 3943 O THR A 488 1614 755 1360 -86 -78 -224 A O ATOM 3944 CB THR A 488 43.278 0.087 47.307 1.00 9.42 A C ANISOU 3944 CB THR A 488 1471 463 1645 -65 31 -119 A C ATOM 3945 CG2 THR A 488 43.561 -0.098 48.789 1.00 10.87 A C ANISOU 3945 CG2 THR A 488 1593 818 1716 111 88 -122 A C ATOM 3946 OG1 THR A 488 42.953 1.450 47.067 1.00 9.63 A O ANISOU 3946 OG1 THR A 488 1432 499 1725 -40 56 -78 A O ATOM 3947 N ALA A 489 44.636 0.767 44.179 1.00 9.62 A N ANISOU 3947 N ALA A 489 1404 747 1503 -177 -106 -188 A N ATOM 3948 CA ALA A 489 44.030 1.085 42.897 1.00 9.93 A C ANISOU 3948 CA ALA A 489 1466 692 1615 -81 -138 -178 A C ATOM 3949 C ALA A 489 43.863 -0.166 42.001 1.00 9.36 A C ANISOU 3949 C ALA A 489 1386 824 1343 -93 128 -154 A C ATOM 3950 O ALA A 489 42.758 -0.378 41.461 1.00 10.09 A O ANISOU 3950 O ALA A 489 1415 557 1860 36 -117 -6 A O ATOM 3951 CB ALA A 489 44.816 2.184 42.216 1.00 10.49 A C ANISOU 3951 CB ALA A 489 1587 584 1812 121 -73 -19 A C ATOM 3952 N GLY A 490 44.952 -0.901 41.785 1.00 9.52 A N ANISOU 3952 N GLY A 490 1270 881 1465 -35 -57 -131 A N ATOM 3953 CA GLY A 490 44.852 -2.092 40.919 1.00 10.02 A C ANISOU 3953 CA GLY A 490 1631 552 1623 -78 5 -14 A C ATOM 3954 C GLY A 490 43.971 -3.200 41.482 1.00 8.86 A C ANISOU 3954 C GLY A 490 1429 682 1256 94 60 7 A C ATOM 3955 O GLY A 490 43.171 -3.823 40.739 1.00 10.24 A O ANISOU 3955 O GLY A 490 1490 921 1478 -18 -36 -122 A O ATOM 3956 N PHE A 491 44.071 -3.384 42.789 1.00 8.64 A N ANISOU 3956 N PHE A 491 1370 616 1297 -17 -71 -3 A N ATOM 3957 CA PHE A 491 43.237 -4.358 43.496 1.00 9.13 A C ANISOU 3957 CA PHE A 491 1425 509 1533 -89 -83 72 A C ATOM 3958 C PHE A 491 41.761 -4.059 43.262 1.00 9.64 A C ANISOU 3958 C PHE A 491 1395 887 1380 16 54 -59 A C ATOM 3959 O PHE A 491 40.968 -4.931 42.949 1.00 9.98 A O ANISOU 3959 O PHE A 491 1335 894 1560 12 -81 -32 A O ATOM 3960 CB PHE A 491 43.626 -4.325 44.965 1.00 9.73 A C ANISOU 3960 CB PHE A 491 1325 808 1562 71 -9 45 A C ATOM 3961 CG PHE A 491 42.852 -5.197 45.903 1.00 9.73 A C ANISOU 3961 CG PHE A 491 1525 612 1560 80 94 31 A C ATOM 3962 CD1 PHE A 491 41.606 -4.831 46.348 1.00 10.51 A C ANISOU 3962 CD1 PHE A 491 1338 884 1770 -64 19 1 A C ATOM 3963 CD2 PHE A 491 43.355 -6.416 46.332 1.00 10.22 A C ANISOU 3963 CD2 PHE A 491 1268 662 1952 21 91 166 A C ATOM 3964 CE1 PHE A 491 40.889 -5.596 47.257 1.00 10.36 A C ANISOU 3964 CE1 PHE A 491 1368 1013 1555 22 75 -47 A C ATOM 3965 CE2 PHE A 491 42.646 -7.161 47.258 1.00 10.87 A C ANISOU 3965 CE2 PHE A 491 1523 827 1779 -118 86 106 A C ATOM 3966 CZ PHE A 491 41.403 -6.785 47.697 1.00 11.00 A C ANISOU 3966 CZ PHE A 491 1400 831 1947 -201 79 93 A C ATOM 3967 N LEU A 492 41.364 -2.803 43.467 1.00 9.67 A N ANISOU 3967 N LEU A 492 1333 797 1542 35 -24 -13 A N ATOM 3968 CA LEU A 492 39.944 -2.437 43.330 1.00 8.74 A C ANISOU 3968 CA LEU A 492 1338 575 1406 -90 6 -9 A C ATOM 3969 C LEU A 492 39.546 -2.310 41.864 1.00 9.10 A C ANISOU 3969 C LEU A 492 1275 741 1441 153 79 -113 A C ATOM 3970 O LEU A 492 38.383 -2.573 41.543 1.00 10.51 A O ANISOU 3970 O LEU A 492 1418 743 1830 -179 107 -54 A O ATOM 3971 CB LEU A 492 39.642 -1.171 44.122 1.00 9.00 A C ANISOU 3971 CB LEU A 492 1183 680 1556 74 -82 -73 A C ATOM 3972 CG LEU A 492 39.688 -1.346 45.635 1.00 10.19 A C ANISOU 3972 CG LEU A 492 1437 923 1509 -24 121 -256 A C ATOM 3973 CD1 LEU A 492 39.582 0.001 46.308 1.00 12.01 A C ANISOU 3973 CD1 LEU A 492 1853 806 1904 90 59 -257 A C ATOM 3974 CD2 LEU A 492 38.606 -2.308 46.139 1.00 10.58 A C ANISOU 3974 CD2 LEU A 492 1539 1274 1206 -117 62 -67 A C ATOM 3975 N ARG A 493 40.508 -2.003 40.974 1.00 9.05 A N ANISOU 3975 N ARG A 493 1252 691 1494 -41 53 -80 A N ATOM 3976 CA ARG A 493 40.171 -2.007 39.573 1.00 9.20 A C ANISOU 3976 CA ARG A 493 1437 726 1331 5 201 -124 A C ATOM 3977 C ARG A 493 39.610 -3.381 39.143 1.00 8.82 A C ANISOU 3977 C ARG A 493 1359 867 1123 1 167 -147 A C ATOM 3978 O ARG A 493 38.602 -3.479 38.412 1.00 10.34 A O ANISOU 3978 O ARG A 493 1581 694 1653 -89 -64 67 A O ATOM 3979 CB ARG A 493 41.375 -1.639 38.710 1.00 9.63 A C ANISOU 3979 CB ARG A 493 1590 621 1448 -202 179 -91 A C ATOM 3980 CG ARG A 493 41.046 -1.402 37.246 1.00 10.29 A C ANISOU 3980 CG ARG A 493 1646 770 1493 -358 15 -127 A C ATOM 3981 CD ARG A 493 42.254 -1.098 36.380 1.00 10.60 A C ANISOU 3981 CD ARG A 493 1693 847 1486 -264 118 48 A C ATOM 3982 NE ARG A 493 41.795 -0.554 35.104 1.00 11.15 A N ANISOU 3982 NE ARG A 493 1322 1199 1716 -128 89 205 A N ATOM 3983 CZ ARG A 493 42.609 0.072 34.249 1.00 11.26 A C ANISOU 3983 CZ ARG A 493 1384 1178 1716 -140 163 120 A C ATOM 3984 NH1 ARG A 493 43.935 0.000 34.432 1.00 11.14 A N ANISOU 3984 NH1 ARG A 493 1382 1010 1838 9 87 38 A N ATOM 3985 NH2 ARG A 493 42.095 0.808 33.249 1.00 12.39 A N ANISOU 3985 NH2 ARG A 493 1742 1134 1829 42 -32 37 A N ATOM 3986 N ALA A 494 40.341 -4.428 39.547 1.00 9.18 A N ANISOU 3986 N ALA A 494 1339 782 1364 -165 42 80 A N ATOM 3987 CA ALA A 494 39.968 -5.804 39.212 1.00 10.35 A C ANISOU 3987 CA ALA A 494 1429 922 1581 -257 -12 -92 A C ATOM 3988 C ALA A 494 38.605 -6.162 39.829 1.00 8.85 A C ANISOU 3988 C ALA A 494 1356 713 1293 40 -101 122 A C ATOM 3989 O ALA A 494 37.706 -6.725 39.145 1.00 9.88 A O ANISOU 3989 O ALA A 494 1502 870 1379 23 -122 -146 A O ATOM 3990 CB ALA A 494 41.080 -6.741 39.643 1.00 11.09 A C ANISOU 3990 CB ALA A 494 1289 932 1993 -273 140 79 A C ATOM 3991 N TRP A 495 38.452 -5.849 41.112 1.00 9.34 A N ANISOU 3991 N TRP A 495 1422 710 1416 -51 65 -64 A N ATOM 3992 CA TRP A 495 37.210 -6.168 41.809 1.00 9.43 A C ANISOU 3992 CA TRP A 495 1389 859 1332 -61 32 -8 A C ATOM 3993 C TRP A 495 36.006 -5.527 41.119 1.00 9.77 A C ANISOU 3993 C TRP A 495 1459 689 1562 -19 -32 -42 A C ATOM 3994 O TRP A 495 34.929 -6.118 40.960 1.00 10.46 A O ANISOU 3994 O TRP A 495 1564 816 1592 -88 -75 28 A O ATOM 3995 CB TRP A 495 37.320 -5.825 43.286 1.00 10.51 A C ANISOU 3995 CB TRP A 495 1512 1142 1337 -11 -47 -7 A C ATOM 3996 CG TRP A 495 36.141 -6.235 44.091 1.00 9.47 A C ANISOU 3996 CG TRP A 495 1390 722 1485 -190 -134 69 A C ATOM 3997 CD1 TRP A 495 35.815 -7.507 44.466 1.00 9.39 A C ANISOU 3997 CD1 TRP A 495 1407 667 1491 -69 -13 22 A C ATOM 3998 CD2 TRP A 495 35.103 -5.406 44.615 1.00 10.28 A C ANISOU 3998 CD2 TRP A 495 1295 1048 1563 -196 114 -8 A C ATOM 3999 CE2 TRP A 495 34.169 -6.224 45.288 1.00 10.34 A C ANISOU 3999 CE2 TRP A 495 1560 1056 1311 -147 230 -52 A C ATOM 4000 CE3 TRP A 495 34.844 -4.027 44.552 1.00 10.68 A C ANISOU 4000 CE3 TRP A 495 1691 943 1423 -412 239 53 A C ATOM 4001 NE1 TRP A 495 34.655 -7.497 45.204 1.00 10.80 A N ANISOU 4001 NE1 TRP A 495 1517 905 1680 -307 180 -136 A N ATOM 4002 CZ2 TRP A 495 33.020 -5.735 45.912 1.00 10.07 A C ANISOU 4002 CZ2 TRP A 495 1224 1038 1562 -342 167 108 A C ATOM 4003 CZ3 TRP A 495 33.704 -3.544 45.148 1.00 12.28 A C ANISOU 4003 CZ3 TRP A 495 1548 1376 1740 -294 231 -66 A C ATOM 4004 CH2 TRP A 495 32.796 -4.379 45.806 1.00 11.55 A C ANISOU 4004 CH2 TRP A 495 1703 993 1691 -221 295 -119 A C ATOM 4005 N LEU A 496 36.168 -4.237 40.747 1.00 9.34 A N ANISOU 4005 N LEU A 496 1387 673 1487 -109 -79 -46 A N ATOM 4006 CA LEU A 496 35.086 -3.506 40.140 1.00 9.22 A C ANISOU 4006 CA LEU A 496 1354 790 1357 4 49 -1 A C ATOM 4007 C LEU A 496 34.739 -3.984 38.722 1.00 8.30 A C ANISOU 4007 C LEU A 496 1227 547 1376 -41 34 123 A C ATOM 4008 O LEU A 496 33.570 -3.852 38.316 1.00 9.23 A O ANISOU 4008 O LEU A 496 1239 720 1548 -19 -108 33 A O ATOM 4009 CB LEU A 496 35.362 -2.001 40.177 1.00 9.68 A C ANISOU 4009 CB LEU A 496 1321 784 1570 14 178 17 A C ATOM 4010 CG LEU A 496 35.215 -1.366 41.574 1.00 10.58 A C ANISOU 4010 CG LEU A 496 1729 666 1621 -132 134 -28 A C ATOM 4011 CD1 LEU A 496 35.889 -0.012 41.615 1.00 11.96 A C ANISOU 4011 CD1 LEU A 496 2024 576 1943 -119 43 -9 A C ATOM 4012 CD2 LEU A 496 33.745 -1.255 41.952 1.00 12.71 A C ANISOU 4012 CD2 LEU A 496 1907 1118 1804 -149 335 -174 A C ATOM 4013 N LYS A 497 35.721 -4.573 38.003 1.00 9.74 A N ANISOU 4013 N LYS A 497 1420 783 1495 -47 130 -84 A N ATOM 4014 CA LYS A 497 35.382 -5.239 36.743 1.00 10.06 A C ANISOU 4014 CA LYS A 497 1510 866 1444 -20 23 -69 A C ATOM 4015 C LYS A 497 34.389 -6.397 36.976 1.00 10.32 A C ANISOU 4015 C LYS A 497 1481 1093 1347 -102 15 -111 A C ATOM 4016 O LYS A 497 33.414 -6.569 36.250 1.00 11.18 A O ANISOU 4016 O LYS A 497 1612 820 1815 -175 -158 -96 A O ATOM 4017 CB LYS A 497 36.659 -5.782 36.072 1.00 9.83 A C ANISOU 4017 CB LYS A 497 1273 910 1551 -187 -111 -100 A C ATOM 4018 CG LYS A 497 37.531 -4.679 35.503 1.00 10.19 A C ANISOU 4018 CG LYS A 497 1461 950 1460 -114 46 -10 A C ATOM 4019 CD LYS A 497 38.815 -5.231 34.907 1.00 10.50 A C ANISOU 4019 CD LYS A 497 1420 1030 1536 -72 -6 -151 A C ATOM 4020 CE LYS A 497 39.615 -4.139 34.249 1.00 12.05 A C ANISOU 4020 CE LYS A 497 1685 1122 1769 -24 158 -58 A C ATOM 4021 NZ LYS A 497 40.922 -4.656 33.777 1.00 13.69 A N ANISOU 4021 NZ LYS A 497 1660 1579 1962 9 205 -120 A N ATOM 4022 N ASP A 498 34.669 -7.161 38.025 1.00 9.64 A N ANISOU 4022 N ASP A 498 1185 953 1524 -58 -136 2 A N ATOM 4023 CA ASP A 498 33.795 -8.303 38.375 1.00 10.31 A C ANISOU 4023 CA ASP A 498 1235 1092 1588 -153 -87 -103 A C ATOM 4024 C ASP A 498 32.441 -7.791 38.842 1.00 10.33 A C ANISOU 4024 C ASP A 498 1457 946 1522 80 -62 -146 A C ATOM 4025 O ASP A 498 31.385 -8.345 38.482 1.00 11.50 A O ANISOU 4025 O ASP A 498 1632 851 1883 -132 -128 -50 A O ATOM 4026 CB ASP A 498 34.463 -9.230 39.383 1.00 10.83 A C ANISOU 4026 CB ASP A 498 1658 999 1455 -65 53 -133 A C ATOM 4027 CG ASP A 498 35.621 -10.018 38.779 1.00 11.81 A C ANISOU 4027 CG ASP A 498 1666 1057 1762 66 11 42 A C ATOM 4028 OD1 ASP A 498 35.792 -9.980 37.522 1.00 11.57 A O ANISOU 4028 OD1 ASP A 498 1663 950 1780 -7 118 -137 A O ATOM 4029 OD2 ASP A 498 36.337 -10.678 39.595 1.00 11.40 A O ANISOU 4029 OD2 ASP A 498 1657 834 1839 24 -23 13 A O ATOM 4030 N ALA A 499 32.445 -6.678 39.612 1.00 9.75 A N ANISOU 4030 N ALA A 499 1394 732 1578 -210 -65 -56 A N ATOM 4031 CA ALA A 499 31.179 -6.139 40.091 1.00 10.12 A C ANISOU 4031 CA ALA A 499 1336 809 1698 -206 -105 31 A C ATOM 4032 C ALA A 499 30.286 -5.825 38.869 1.00 10.24 A C ANISOU 4032 C ALA A 499 1446 972 1472 18 14 -80 A C ATOM 4033 O ALA A 499 29.083 -6.098 38.863 1.00 10.66 A O ANISOU 4033 O ALA A 499 1503 882 1664 -64 -4 108 A O ATOM 4034 CB ALA A 499 31.412 -4.911 40.944 1.00 10.93 A C ANISOU 4034 CB ALA A 499 1506 951 1693 -67 -142 -77 A C ATOM 4035 N ARG A 500 30.876 -5.178 37.840 1.00 9.86 A N ANISOU 4035 N ARG A 500 1423 657 1663 7 -51 49 A N ATOM 4036 CA ARG A 500 30.167 -4.796 36.642 1.00 10.29 A C ANISOU 4036 CA ARG A 500 1526 910 1471 0 3 -66 A C ATOM 4037 C ARG A 500 29.628 -6.053 35.923 1.00 10.27 A C ANISOU 4037 C ARG A 500 1554 812 1535 -40 -45 137 A C ATOM 4038 O ARG A 500 28.470 -6.077 35.511 1.00 12.00 A O ANISOU 4038 O ARG A 500 1640 861 2057 -139 -198 15 A O ATOM 4039 CB ARG A 500 31.074 -3.946 35.744 1.00 11.41 A C ANISOU 4039 CB ARG A 500 1606 829 1900 26 47 69 A C ATOM 4040 CG ARG A 500 30.467 -3.563 34.410 1.00 11.44 A C ANISOU 4040 CG ARG A 500 1536 925 1886 -168 13 31 A C ATOM 4041 CD ARG A 500 29.136 -2.850 34.577 1.00 11.13 A C ANISOU 4041 CD ARG A 500 1527 1044 1656 -52 -151 10 A C ATOM 4042 NE ARG A 500 28.740 -2.211 33.342 1.00 13.06 A N ANISOU 4042 NE ARG A 500 1614 1435 1910 10 -57 394 A N ATOM 4043 CZ ARG A 500 27.503 -1.758 33.069 1.00 11.95 A C ANISOU 4043 CZ ARG A 500 1536 1269 1733 -153 -113 47 A C ATOM 4044 NH1 ARG A 500 26.546 -1.900 33.987 1.00 12.02 A N ANISOU 4044 NH1 ARG A 500 1559 1119 1887 -48 13 -24 A N ATOM 4045 NH2 ARG A 500 27.289 -1.154 31.902 1.00 14.33 A N ANISOU 4045 NH2 ARG A 500 1942 1589 1912 -104 -293 297 A N ATOM 4046 N SER A 501 30.487 -7.059 35.706 1.00 10.16 A N ANISOU 4046 N SER A 501 1248 967 1642 -52 -37 -9 A N ATOM 4047 CA SER A 501 30.050 -8.280 35.037 1.00 10.91 A C ANISOU 4047 CA SER A 501 1311 1011 1821 -108 -22 -75 A C ATOM 4048 C SER A 501 28.871 -8.941 35.776 1.00 10.14 A C ANISOU 4048 C SER A 501 1479 842 1531 98 78 -63 A C ATOM 4049 O SER A 501 27.869 -9.361 35.112 1.00 12.26 A O ANISOU 4049 O SER A 501 1705 1021 1929 -219 -169 156 A O ATOM 4050 CB SER A 501 31.204 -9.270 34.939 1.00 12.48 A C ANISOU 4050 CB SER A 501 1506 1135 2100 55 -38 -187 A C ATOM 4051 OG SER A 501 32.251 -8.795 34.097 1.00 13.29 A O ANISOU 4051 OG SER A 501 1856 1190 2001 -12 168 -178 A O ATOM 4052 N GLU A 502 28.969 -8.991 37.108 1.00 10.20 A N ANISOU 4052 N GLU A 502 1478 909 1487 -35 43 -51 A N ATOM 4053 CA GLU A 502 27.950 -9.603 37.909 1.00 10.43 A C ANISOU 4053 CA GLU A 502 1413 986 1563 -113 17 -110 A C ATOM 4054 C GLU A 502 26.635 -8.830 37.775 1.00 10.31 A C ANISOU 4054 C GLU A 502 1445 877 1595 -77 15 128 A C ATOM 4055 O GLU A 502 25.538 -9.401 37.643 1.00 12.16 A O ANISOU 4055 O GLU A 502 1554 965 2101 -142 -4 102 A O ATOM 4056 CB GLU A 502 28.402 -9.736 39.360 1.00 10.80 A C ANISOU 4056 CB GLU A 502 1531 1035 1537 0 116 170 A C ATOM 4057 CG GLU A 502 29.581 -10.680 39.572 1.00 11.06 A C ANISOU 4057 CG GLU A 502 1690 818 1692 -5 65 -67 A C ATOM 4058 CD GLU A 502 29.346 -12.168 39.638 1.00 11.99 A C ANISOU 4058 CD GLU A 502 1843 849 1862 -22 -193 -179 A C ATOM 4059 OE1 GLU A 502 28.294 -12.604 39.159 1.00 13.86 A O ANISOU 4059 OE1 GLU A 502 1672 1280 2315 -85 -277 79 A O ATOM 4060 OE2 GLU A 502 30.249 -12.805 40.226 1.00 12.16 A O ANISOU 4060 OE2 GLU A 502 1627 1085 1907 -74 -94 -100 A O ATOM 4061 N GLN A 503 26.721 -7.480 37.866 1.00 10.31 A N ANISOU 4061 N GLN A 503 1349 875 1693 -173 -69 -4 A N ATOM 4062 CA GLN A 503 25.569 -6.603 37.721 1.00 11.20 A C ANISOU 4062 CA GLN A 503 1198 1318 1736 -288 -180 85 A C ATOM 4063 C GLN A 503 24.862 -6.823 36.383 1.00 10.98 A C ANISOU 4063 C GLN A 503 1546 1013 1614 82 -124 141 A C ATOM 4064 O GLN A 503 23.600 -6.780 36.328 1.00 12.15 A O ANISOU 4064 O GLN A 503 1452 1134 2028 -112 70 -164 A O ATOM 4065 CB GLN A 503 26.074 -5.170 37.867 1.00 11.44 A C ANISOU 4065 CB GLN A 503 1347 1192 1804 -263 39 73 A C ATOM 4066 CG GLN A 503 24.973 -4.132 37.644 1.00 12.85 A C ANISOU 4066 CG GLN A 503 1569 1309 2002 -138 -7 239 A C ATOM 4067 CD GLN A 503 25.540 -2.755 37.402 1.00 12.31 A C ANISOU 4067 CD GLN A 503 1401 1094 2181 55 80 -4 A C ATOM 4068 NE2 GLN A 503 24.796 -1.752 37.854 1.00 11.18 A N ANISOU 4068 NE2 GLN A 503 1412 932 1903 98 -140 77 A N ATOM 4069 OE1 GLN A 503 26.624 -2.613 36.819 1.00 12.84 A O ANISOU 4069 OE1 GLN A 503 1644 1107 2127 -104 209 -62 A O ATOM 4070 N LEU A 504 25.631 -6.986 35.303 1.00 11.73 A N ANISOU 4070 N LEU A 504 1546 1113 1794 -95 -55 148 A N ATOM 4071 CA LEU A 504 25.006 -7.109 33.983 1.00 12.36 A C ANISOU 4071 CA LEU A 504 1810 996 1889 -6 -226 36 A C ATOM 4072 C LEU A 504 24.189 -8.409 33.871 1.00 14.45 A C ANISOU 4072 C LEU A 504 1959 1635 1895 -437 -280 -12 A C ATOM 4073 O LEU A 504 23.336 -8.480 32.976 1.00 18.66 A O ANISOU 4073 O LEU A 504 2277 2194 2617 -794 -815 211 A O ATOM 4074 CB LEU A 504 26.061 -7.017 32.887 1.00 13.09 A C ANISOU 4074 CB LEU A 504 1964 1265 1744 63 -201 -98 A C ATOM 4075 CG LEU A 504 26.560 -5.588 32.656 1.00 14.56 A C ANISOU 4075 CG LEU A 504 1982 1519 2032 -222 -15 235 A C ATOM 4076 CD1 LEU A 504 27.855 -5.605 31.842 1.00 17.37 A C ANISOU 4076 CD1 LEU A 504 2114 2230 2253 -380 49 3 A C ATOM 4077 CD2 LEU A 504 25.477 -4.715 32.003 1.00 16.06 A C ANISOU 4077 CD2 LEU A 504 2155 1624 2322 -248 -91 206 A C ATOM 4078 N ASN A 505 24.448 -9.397 34.723 1.00 13.41 A N ANISOU 4078 N ASN A 505 1778 1623 1693 -315 -236 -9 A N ATOM 4079 CA ASN A 505 23.603 -10.595 34.762 1.00 14.62 A C ANISOU 4079 CA ASN A 505 2031 1439 2085 -277 -196 -65 A C ATOM 4080 C ASN A 505 22.643 -10.615 35.943 1.00 14.62 A C ANISOU 4080 C ASN A 505 2162 1314 2077 -85 -99 -66 A C ATOM 4081 O ASN A 505 22.094 -11.664 36.290 1.00 18.23 A O ANISOU 4081 O ASN A 505 2843 1474 2609 -395 87 1 A O ATOM 4082 CB ASN A 505 24.452 -11.852 34.789 1.00 15.90 A C ANISOU 4082 CB ASN A 505 2214 1509 2316 -155 107 -250 A C ATOM 4083 CG ASN A 505 23.651 -13.086 34.427 1.00 18.49 A C ANISOU 4083 CG ASN A 505 2546 1969 2509 -634 -548 240 A C ATOM 4084 ND2 ASN A 505 23.934 -14.168 35.126 1.00 17.62 A N ANISOU 4084 ND2 ASN A 505 2460 1595 2639 -229 -117 23 A N ATOM 4085 OD1 ASN A 505 22.779 -13.039 33.537 1.00 18.48 A O ANISOU 4085 OD1 ASN A 505 2643 1700 2679 -274 -562 -308 A O ATOM 4086 N HIS A 506 22.349 -9.456 36.515 1.00 13.77 A N ANISOU 4086 N HIS A 506 2034 1271 1925 -356 63 -95 A N ATOM 4087 CA HIS A 506 21.488 -9.306 37.688 1.00 13.64 A C ANISOU 4087 CA HIS A 506 1952 1311 1918 -435 45 -100 A C ATOM 4088 C HIS A 506 20.517 -8.129 37.508 1.00 14.79 A C ANISOU 4088 C HIS A 506 2069 1488 2061 -454 -30 138 A C ATOM 4089 O HIS A 506 20.176 -7.439 38.477 1.00 14.93 A O ANISOU 4089 O HIS A 506 1833 1483 2357 -248 -4 72 A O ATOM 4090 CB HIS A 506 22.401 -9.145 38.916 1.00 14.44 A C ANISOU 4090 CB HIS A 506 2128 1255 2103 -103 -177 144 A C ATOM 4091 CG HIS A 506 21.819 -9.488 40.228 1.00 17.95 A C ANISOU 4091 CG HIS A 506 2812 1666 2340 -497 221 83 A C ATOM 4092 CD2 HIS A 506 21.781 -10.668 40.869 1.00 22.63 A C ANISOU 4092 CD2 HIS A 506 3929 1603 3066 -446 299 332 A C ATOM 4093 ND1 HIS A 506 21.362 -8.559 41.137 1.00 24.45 A N ANISOU 4093 ND1 HIS A 506 3592 2480 3218 -9 886 -124 A N ATOM 4094 CE1 HIS A 506 20.937 -9.184 42.225 1.00 23.53 A C ANISOU 4094 CE1 HIS A 506 4280 2262 2396 -219 114 -192 A C ATOM 4095 NE2 HIS A 506 21.201 -10.459 42.094 1.00 26.10 A N ANISOU 4095 NE2 HIS A 506 3992 2676 3247 -189 535 -127 A N ATOM 4096 N SER A 507 20.085 -7.918 36.261 1.00 15.35 A N ANISOU 4096 N SER A 507 1994 1437 2399 -399 -298 72 A N ATOM 4097 CA SER A 507 19.064 -6.900 35.924 1.00 18.33 A C ANISOU 4097 CA SER A 507 2107 1806 3051 -94 -448 129 A C ATOM 4098 C SER A 507 19.457 -5.512 36.455 1.00 16.24 A C ANISOU 4098 C SER A 507 1902 1874 2392 -398 -167 298 A C ATOM 4099 O SER A 507 18.613 -4.755 36.990 1.00 18.61 A O ANISOU 4099 O SER A 507 1806 2220 3041 -324 -291 193 A O ATOM 4100 CB SER A 507 17.714 -7.342 36.437 1.00 23.36 A C ANISOU 4100 CB SER A 507 2255 2136 4484 -288 -179 -79 A C ATOM 4101 OG SER A 507 17.342 -8.588 35.833 1.00 30.40 A O ANISOU 4101 OG SER A 507 2769 2761 6020 -980 -421 -466 A O ATOM 4102 N TYR A 508 20.766 -5.220 36.355 1.00 13.59 A N ANISOU 4102 N TYR A 508 1756 1304 2102 -54 7 60 A N ATOM 4103 CA TYR A 508 21.377 -3.901 36.623 1.00 13.02 A C ANISOU 4103 CA TYR A 508 1870 1141 1935 27 66 -70 A C ATOM 4104 C TYR A 508 21.484 -3.614 38.114 1.00 12.04 A C ANISOU 4104 C TYR A 508 1428 1361 1783 8 23 80 A C ATOM 4105 O TYR A 508 21.977 -2.560 38.513 1.00 12.95 A O ANISOU 4105 O TYR A 508 1617 1330 1972 104 -25 -296 A O ATOM 4106 CB TYR A 508 20.691 -2.771 35.875 1.00 14.31 A C ANISOU 4106 CB TYR A 508 1793 1617 2025 178 -122 39 A C ATOM 4107 CG TYR A 508 20.653 -3.007 34.395 1.00 16.99 A C ANISOU 4107 CG TYR A 508 2716 1676 2062 -25 -241 60 A C ATOM 4108 CD1 TYR A 508 21.817 -2.939 33.629 1.00 16.99 A C ANISOU 4108 CD1 TYR A 508 2659 1567 2227 27 -210 -79 A C ATOM 4109 CD2 TYR A 508 19.468 -3.334 33.755 1.00 18.63 A C ANISOU 4109 CD2 TYR A 508 2610 1871 2597 254 -342 -33 A C ATOM 4110 CE1 TYR A 508 21.795 -3.157 32.264 1.00 19.04 A C ANISOU 4110 CE1 TYR A 508 2725 2307 2202 -29 380 -65 A C ATOM 4111 CE2 TYR A 508 19.440 -3.546 32.383 1.00 20.43 A C ANISOU 4111 CE2 TYR A 508 2887 2287 2588 173 -616 -246 A C ATOM 4112 CZ TYR A 508 20.602 -3.462 31.641 1.00 21.07 A C ANISOU 4112 CZ TYR A 508 3380 2238 2386 -78 -227 -332 A C ATOM 4113 OH TYR A 508 20.557 -3.664 30.285 1.00 25.55 A O ANISOU 4113 OH TYR A 508 3585 3553 2569 177 -423 -658 A O ATOM 4114 N SER A 509 21.076 -4.559 38.956 1.00 13.90 A N ANISOU 4114 N SER A 509 1946 1209 2125 -128 -37 160 A N ATOM 4115 CA SER A 509 21.286 -4.529 40.378 1.00 13.95 A C ANISOU 4115 CA SER A 509 1864 1324 2112 31 -176 72 A C ATOM 4116 C SER A 509 22.628 -5.199 40.705 1.00 13.88 A C ANISOU 4116 C SER A 509 1563 1498 2212 -107 18 -252 A C ATOM 4117 O SER A 509 23.105 -6.070 40.016 1.00 17.24 A O ANISOU 4117 O SER A 509 1872 2140 2538 184 -220 -818 A O ATOM 4118 CB SER A 509 20.126 -5.249 41.071 1.00 16.91 A C ANISOU 4118 CB SER A 509 1561 2758 2103 459 333 305 A C ATOM 4119 OG SER A 509 20.239 -5.095 42.462 1.00 20.68 A O ANISOU 4119 OG SER A 509 2677 2576 2603 -164 382 -170 A O ATOM 4120 N LEU A 510 23.244 -4.807 41.805 1.00 14.66 A N ANISOU 4120 N LEU A 510 2353 1236 1979 325 -172 -51 A N ATOM 4121 CA LEU A 510 24.497 -5.385 42.253 1.00 13.16 A C ANISOU 4121 CA LEU A 510 1648 1650 1700 -85 69 -10 A C ATOM 4122 C LEU A 510 24.209 -6.507 43.246 1.00 13.71 A C ANISOU 4122 C LEU A 510 2004 1322 1883 63 -3 -36 A C ATOM 4123 O LEU A 510 23.513 -6.313 44.236 1.00 13.90 A O ANISOU 4123 O LEU A 510 1943 1400 1937 342 83 146 A O ATOM 4124 CB LEU A 510 25.356 -4.293 42.891 1.00 14.31 A C ANISOU 4124 CB LEU A 510 1859 1695 1883 -147 -49 -5 A C ATOM 4125 CG LEU A 510 26.783 -4.679 43.210 1.00 13.85 A C ANISOU 4125 CG LEU A 510 1888 1381 1992 -96 144 35 A C ATOM 4126 CD1 LEU A 510 27.584 -4.936 41.932 1.00 15.06 A C ANISOU 4126 CD1 LEU A 510 2219 1545 1958 -260 258 247 A C ATOM 4127 CD2 LEU A 510 27.425 -3.598 44.073 1.00 14.01 A C ANISOU 4127 CD2 LEU A 510 2040 1155 2125 47 46 5 A C ATOM 4128 N PRO A 511 24.724 -7.731 43.013 1.00 12.26 A N ANISOU 4128 N PRO A 511 1885 1342 1429 155 -93 14 A N ATOM 4129 CA PRO A 511 24.641 -8.773 44.036 1.00 11.74 A C ANISOU 4129 CA PRO A 511 1682 1122 1656 102 -66 -6 A C ATOM 4130 C PRO A 511 25.273 -8.297 45.340 1.00 11.62 A C ANISOU 4130 C PRO A 511 1623 1213 1578 115 -2 50 A C ATOM 4131 O PRO A 511 26.126 -7.428 45.342 1.00 11.66 A O ANISOU 4131 O PRO A 511 1584 1205 1638 14 213 -58 A O ATOM 4132 CB PRO A 511 25.388 -9.950 43.442 1.00 11.83 A C ANISOU 4132 CB PRO A 511 1607 1176 1708 -101 34 -276 A C ATOM 4133 CG PRO A 511 25.284 -9.724 41.969 1.00 12.37 A C ANISOU 4133 CG PRO A 511 1665 1310 1724 -187 97 -85 A C ATOM 4134 CD PRO A 511 25.382 -8.217 41.791 1.00 12.82 A C ANISOU 4134 CD PRO A 511 1970 1305 1594 -34 93 15 A C ATOM 4135 N TYR A 512 24.847 -8.867 46.450 1.00 10.72 A N ANISOU 4135 N TYR A 512 1486 1015 1572 66 170 -45 A N ATOM 4136 CA TYR A 512 25.358 -8.468 47.756 1.00 10.15 A C ANISOU 4136 CA TYR A 512 1423 879 1554 166 183 -70 A C ATOM 4137 C TYR A 512 26.857 -8.680 47.909 1.00 10.33 A C ANISOU 4137 C TYR A 512 1313 1119 1491 -133 37 -181 A C ATOM 4138 O TYR A 512 27.534 -7.909 48.572 1.00 10.91 A O ANISOU 4138 O TYR A 512 1429 865 1849 -201 -74 -14 A O ATOM 4139 CB TYR A 512 24.586 -9.138 48.895 1.00 10.73 A C ANISOU 4139 CB TYR A 512 1538 1073 1465 -25 0 71 A C ATOM 4140 CG TYR A 512 23.107 -8.833 48.894 1.00 11.12 A C ANISOU 4140 CG TYR A 512 1485 1192 1547 -193 153 6 A C ATOM 4141 CD1 TYR A 512 22.569 -7.692 48.306 1.00 11.68 A C ANISOU 4141 CD1 TYR A 512 1334 1275 1827 -184 282 59 A C ATOM 4142 CD2 TYR A 512 22.253 -9.670 49.597 1.00 13.34 A C ANISOU 4142 CD2 TYR A 512 1512 1561 1993 -281 171 298 A C ATOM 4143 CE1 TYR A 512 21.198 -7.495 48.292 1.00 13.33 A C ANISOU 4143 CE1 TYR A 512 1338 1149 2577 -129 362 66 A C ATOM 4144 CE2 TYR A 512 20.892 -9.461 49.616 1.00 15.57 A C ANISOU 4144 CE2 TYR A 512 1512 1959 2442 -263 329 666 A C ATOM 4145 CZ TYR A 512 20.357 -8.369 48.966 1.00 13.45 A C ANISOU 4145 CZ TYR A 512 1498 1491 2120 -184 278 181 A C ATOM 4146 OH TYR A 512 19.004 -8.166 48.961 1.00 15.04 A O ANISOU 4146 OH TYR A 512 1492 1853 2367 -24 468 136 A O ATOM 4147 N VAL A 513 27.347 -9.802 47.369 1.00 10.33 A N ANISOU 4147 N VAL A 513 1380 991 1551 -82 66 -100 A N ATOM 4148 CA VAL A 513 28.770 -10.103 47.411 1.00 10.48 A C ANISOU 4148 CA VAL A 513 1442 992 1547 -55 46 96 A C ATOM 4149 C VAL A 513 29.316 -10.314 46.006 1.00 9.63 A C ANISOU 4149 C VAL A 513 1175 898 1584 -88 65 106 A C ATOM 4150 O VAL A 513 28.597 -10.759 45.118 1.00 10.63 A O ANISOU 4150 O VAL A 513 1424 1008 1604 -7 -64 -99 A O ATOM 4151 CB VAL A 513 29.114 -11.322 48.287 1.00 10.41 A C ANISOU 4151 CB VAL A 513 1435 772 1748 2 75 18 A C ATOM 4152 CG1 VAL A 513 28.492 -11.172 49.665 1.00 11.32 A C ANISOU 4152 CG1 VAL A 513 1738 1028 1535 -17 -5 104 A C ATOM 4153 CG2 VAL A 513 28.705 -12.669 47.689 1.00 11.89 A C ANISOU 4153 CG2 VAL A 513 1881 810 1823 -235 236 56 A C ATOM 4154 N ILE A 514 30.586 -9.930 45.840 1.00 9.39 A N ANISOU 4154 N ILE A 514 1088 903 1575 -28 -22 -146 A N ATOM 4155 CA ILE A 514 31.296 -10.025 44.575 1.00 9.09 A C ANISOU 4155 CA ILE A 514 1350 525 1577 -224 0 -98 A C ATOM 4156 C ILE A 514 32.658 -10.627 44.849 1.00 9.19 A C ANISOU 4156 C ILE A 514 1280 889 1321 -94 48 18 A C ATOM 4157 O ILE A 514 33.457 -10.085 45.639 1.00 10.20 A O ANISOU 4157 O ILE A 514 1362 833 1678 -94 -124 44 A O ATOM 4158 CB ILE A 514 31.518 -8.649 43.949 1.00 9.24 A C ANISOU 4158 CB ILE A 514 1338 679 1494 -315 7 22 A C ATOM 4159 CG1 ILE A 514 30.216 -7.865 43.751 1.00 13.38 A C ANISOU 4159 CG1 ILE A 514 1557 1346 2181 6 -4 -77 A C ATOM 4160 CG2 ILE A 514 32.321 -8.740 42.669 1.00 10.62 A C ANISOU 4160 CG2 ILE A 514 1588 919 1528 -129 -8 187 A C ATOM 4161 CD1 ILE A 514 29.234 -8.415 42.710 1.00 11.80 A C ANISOU 4161 CD1 ILE A 514 1476 1069 1936 -28 121 -16 A C ATOM 4162 N PRO A 515 33.032 -11.758 44.203 1.00 10.19 A N ANISOU 4162 N PRO A 515 1327 867 1675 -47 -32 -74 A N ATOM 4163 CA PRO A 515 32.207 -12.539 43.258 1.00 9.46 A C ANISOU 4163 CA PRO A 515 1243 820 1529 40 117 -81 A C ATOM 4164 C PRO A 515 30.905 -13.079 43.866 1.00 8.91 A C ANISOU 4164 C PRO A 515 1358 583 1445 1 109 -247 A C ATOM 4165 O PRO A 515 30.827 -13.326 45.093 1.00 10.29 A O ANISOU 4165 O PRO A 515 1768 740 1400 0 69 -195 A O ATOM 4166 CB PRO A 515 33.124 -13.723 42.927 1.00 10.01 A C ANISOU 4166 CB PRO A 515 1428 824 1551 98 178 -99 A C ATOM 4167 CG PRO A 515 34.545 -13.147 43.082 1.00 11.07 A C ANISOU 4167 CG PRO A 515 1479 958 1767 65 132 -176 A C ATOM 4168 CD PRO A 515 34.407 -12.265 44.313 1.00 10.38 A C ANISOU 4168 CD PRO A 515 1210 1090 1643 -124 52 -137 A C ATOM 4169 N ASN A 516 29.894 -13.166 43.012 1.00 10.46 A N ANISOU 4169 N ASN A 516 1562 989 1423 -2 -10 -88 A N ATOM 4170 CA ASN A 516 28.562 -13.509 43.461 1.00 11.64 A C ANISOU 4170 CA ASN A 516 1448 996 1976 124 148 -164 A C ATOM 4171 C ASN A 516 28.387 -15.046 43.497 1.00 12.72 A C ANISOU 4171 C ASN A 516 1701 1063 2066 -49 234 -110 A C ATOM 4172 O ASN A 516 28.260 -15.653 42.443 1.00 14.89 A O ANISOU 4172 O ASN A 516 2280 1215 2160 -502 469 -233 A O ATOM 4173 CB ASN A 516 27.523 -12.866 42.559 1.00 11.72 A C ANISOU 4173 CB ASN A 516 1396 1159 1896 -55 -32 -204 A C ATOM 4174 CG ASN A 516 26.114 -13.295 42.891 1.00 12.84 A C ANISOU 4174 CG ASN A 516 1617 1243 2018 -50 132 -250 A C ATOM 4175 ND2 ASN A 516 25.225 -13.213 41.884 1.00 15.00 A N ANISOU 4175 ND2 ASN A 516 2101 1243 2353 -64 -325 -147 A N ATOM 4176 OD1 ASN A 516 25.849 -13.596 44.059 1.00 13.41 A O ANISOU 4176 OD1 ASN A 516 1771 1051 2271 -212 390 -34 A O ATOM 4177 N ILE A 517 28.243 -15.598 44.705 1.00 11.94 A N ANISOU 4177 N ILE A 517 1805 816 1914 -242 15 -390 A N ATOM 4178 CA ILE A 517 28.018 -17.030 44.891 1.00 12.67 A C ANISOU 4178 CA ILE A 517 1960 878 1974 -333 -94 -327 A C ATOM 4179 C ILE A 517 26.541 -17.325 45.119 1.00 15.13 A C ANISOU 4179 C ILE A 517 1899 1672 2176 -335 23 115 A C ATOM 4180 O ILE A 517 26.204 -18.472 45.337 1.00 18.83 A O ANISOU 4180 O ILE A 517 2622 1780 2750 -875 27 205 A O ATOM 4181 CB ILE A 517 28.861 -17.582 46.057 1.00 14.82 A C ANISOU 4181 CB ILE A 517 2181 942 2507 -193 5 217 A C ATOM 4182 CG1 ILE A 517 28.574 -16.866 47.387 1.00 16.07 A C ANISOU 4182 CG1 ILE A 517 2034 1767 2302 -99 -58 -39 A C ATOM 4183 CG2 ILE A 517 30.309 -17.526 45.666 1.00 18.14 A C ANISOU 4183 CG2 ILE A 517 2085 1239 3568 -98 167 642 A C ATOM 4184 CD1 ILE A 517 28.956 -17.607 48.641 1.00 18.27 A C ANISOU 4184 CD1 ILE A 517 2431 1712 2798 -45 -431 -81 A C ATOM 4185 N HIS A 518 25.674 -16.309 45.153 1.00 15.55 A N ANISOU 4185 N HIS A 518 1985 1619 2301 -450 -178 -88 A N ATOM 4186 CA HIS A 518 24.288 -16.425 45.617 1.00 16.81 A C ANISOU 4186 CA HIS A 518 2088 1597 2699 -507 71 113 A C ATOM 4187 C HIS A 518 23.241 -16.431 44.493 1.00 20.21 A C ANISOU 4187 C HIS A 518 2633 2298 2745 -879 -213 -32 A C ATOM 4188 O HIS A 518 22.024 -16.530 44.799 1.00 32.15 A O ANISOU 4188 O HIS A 518 2835 5272 4108 -1324 -163 -148 A O ATOM 4189 CB HIS A 518 23.944 -15.310 46.618 1.00 17.89 A C ANISOU 4189 CB HIS A 518 2124 2208 2465 -213 -224 -249 A C ATOM 4190 CG HIS A 518 24.750 -15.382 47.871 1.00 16.77 A C ANISOU 4190 CG HIS A 518 2031 1974 2366 -39 -106 39 A C ATOM 4191 CD2 HIS A 518 25.109 -16.436 48.647 1.00 19.99 A C ANISOU 4191 CD2 HIS A 518 2604 2043 2947 -19 -200 264 A C ATOM 4192 ND1 HIS A 518 25.268 -14.273 48.498 1.00 19.71 A N ANISOU 4192 ND1 HIS A 518 2494 2213 2782 -447 -550 121 A N ATOM 4193 CE1 HIS A 518 25.938 -14.653 49.594 1.00 18.63 A C ANISOU 4193 CE1 HIS A 518 2452 1883 2744 -238 -296 274 A C ATOM 4194 NE2 HIS A 518 25.865 -15.971 49.693 1.00 17.53 A N ANISOU 4194 NE2 HIS A 518 2619 1781 2260 102 224 25 A N ATOM 4195 N GLY A 519 23.637 -16.349 43.229 1.00 19.22 A N ANISOU 4195 N GLY A 519 2325 2129 2848 -103 -186 -12 A N ATOM 4196 CA GLY A 519 22.633 -16.414 42.132 1.00 25.48 A C ANISOU 4196 CA GLY A 519 3567 2623 3489 81 -746 -181 A C ATOM 4197 C GLY A 519 21.908 -15.084 41.945 1.00 21.80 A C ANISOU 4197 C GLY A 519 3198 1997 3086 -361 -121 -187 A C ATOM 4198 O GLY A 519 22.478 -14.048 42.280 1.00 20.84 A O ANISOU 4198 O GLY A 519 1980 2445 3492 -358 -102 -299 A O ATOM 4199 N ASN A 520 20.658 -15.117 41.441 1.00 21.88 A N ANISOU 4199 N ASN A 520 3259 1947 3105 -141 -41 -334 A N ATOM 4200 CA ASN A 520 20.001 -13.912 40.985 1.00 23.00 A C ANISOU 4200 CA ASN A 520 2867 2438 3433 181 -45 -484 A C ATOM 4201 C ASN A 520 18.819 -13.474 41.873 1.00 23.31 A C ANISOU 4201 C ASN A 520 2402 3387 3065 -47 -298 -373 A C ATOM 4202 O ASN A 520 18.093 -12.550 41.509 1.00 31.52 A O ANISOU 4202 O ASN A 520 3424 4019 4534 839 -357 99 A O ATOM 4203 CB ASN A 520 19.589 -14.042 39.521 1.00 28.13 A C ANISOU 4203 CB ASN A 520 3418 3416 3853 214 -682 -1149 A C ATOM 4204 CG ASN A 520 18.373 -14.916 39.324 1.00 31.61 A C ANISOU 4204 CG ASN A 520 3847 4725 3436 -471 -838 -982 A C ATOM 4205 ND2 ASN A 520 17.795 -14.875 38.125 1.00 40.02 A N ANISOU 4205 ND2 ASN A 520 4046 7040 4119 527 -1706 -1213 A N ATOM 4206 OD1 ASN A 520 17.973 -15.640 40.236 1.00 39.34 A O ANISOU 4206 OD1 ASN A 520 5181 5604 4160 -200 218 -462 A O ATOM 4207 N GLY A 521 18.685 -14.037 43.064 1.00 25.87 A N ANISOU 4207 N GLY A 521 3551 2660 3618 -321 342 -250 A N ATOM 4208 CA GLY A 521 17.472 -13.850 43.891 1.00 27.21 A C ANISOU 4208 CA GLY A 521 3342 3439 3556 -428 331 -894 A C ATOM 4209 C GLY A 521 17.517 -12.632 44.810 1.00 25.30 A C ANISOU 4209 C GLY A 521 2968 2772 3869 -415 74 -615 A C ATOM 4210 O GLY A 521 16.478 -12.209 45.332 1.00 27.73 A O ANISOU 4210 O GLY A 521 3315 2947 4273 -681 456 -915 A O ATOM 4211 N GLU A 522 18.699 -12.062 45.037 1.00 22.98 A N ANISOU 4211 N GLU A 522 2959 1781 3989 -37 370 -158 A N ATOM 4212 CA GLU A 522 18.840 -10.950 45.960 1.00 19.07 A C ANISOU 4212 CA GLU A 522 2198 1749 3298 498 317 -51 A C ATOM 4213 C GLU A 522 18.201 -9.692 45.360 1.00 23.89 A C ANISOU 4213 C GLU A 522 3619 2602 2854 1365 816 474 A C ATOM 4214 O GLU A 522 18.469 -9.367 44.222 1.00 28.81 A O ANISOU 4214 O GLU A 522 4546 3410 2990 1540 1101 522 A O ATOM 4215 CB GLU A 522 20.313 -10.716 46.275 1.00 18.31 A C ANISOU 4215 CB GLU A 522 2242 1606 3108 -147 299 -111 A C ATOM 4216 CG GLU A 522 20.933 -11.898 46.995 1.00 20.19 A C ANISOU 4216 CG GLU A 522 2014 1764 3894 228 586 -149 A C ATOM 4217 CD GLU A 522 22.458 -11.867 47.075 1.00 16.53 A C ANISOU 4217 CD GLU A 522 2048 1730 2501 246 212 -547 A C ATOM 4218 OE1 GLU A 522 23.025 -12.323 48.129 1.00 21.59 A O ANISOU 4218 OE1 GLU A 522 2581 2181 3441 -69 -247 -56 A O ATOM 4219 OE2 GLU A 522 23.060 -11.330 46.153 1.00 19.43 A O ANISOU 4219 OE2 GLU A 522 2450 2074 2858 -419 317 -216 A O ATOM 4220 N THR A 523 17.387 -8.998 46.149 1.00 14.88 A N ANISOU 4220 N THR A 523 1951 1475 2225 -40 230 -8 A N ATOM 4221 CA THR A 523 16.757 -7.769 45.688 1.00 14.94 A C ANISOU 4221 CA THR A 523 1840 1401 2433 -151 131 54 A C ATOM 4222 C THR A 523 17.665 -6.567 45.929 1.00 13.33 A C ANISOU 4222 C THR A 523 1690 1436 1939 -99 57 -95 A C ATOM 4223 O THR A 523 18.542 -6.604 46.789 1.00 15.02 A O ANISOU 4223 O THR A 523 1820 1382 2504 -86 -162 23 A O ATOM 4224 CB THR A 523 15.369 -7.611 46.327 1.00 15.20 A C ANISOU 4224 CB THR A 523 2017 1053 2705 -289 180 -68 A C ATOM 4225 CG2 THR A 523 14.442 -8.715 45.858 1.00 16.74 A C ANISOU 4225 CG2 THR A 523 2331 1301 2727 -355 214 -660 A C ATOM 4226 OG1 THR A 523 15.464 -7.616 47.746 1.00 16.32 A O ANISOU 4226 OG1 THR A 523 1935 1796 2467 -157 442 48 A O ATOM 4227 N PRO A 524 17.509 -5.473 45.148 1.00 14.41 A N ANISOU 4227 N PRO A 524 1734 1308 2433 -156 -68 -133 A N ATOM 4228 CA PRO A 524 18.439 -4.336 45.243 1.00 13.41 A C ANISOU 4228 CA PRO A 524 1563 1557 1974 -252 75 -199 A C ATOM 4229 C PRO A 524 18.391 -3.648 46.617 1.00 10.75 A C ANISOU 4229 C PRO A 524 1457 908 1720 -66 -24 188 A C ATOM 4230 O PRO A 524 17.311 -3.410 47.164 1.00 12.43 A O ANISOU 4230 O PRO A 524 1467 1101 2153 -174 123 57 A O ATOM 4231 CB PRO A 524 17.915 -3.381 44.166 1.00 14.82 A C ANISOU 4231 CB PRO A 524 2145 1613 1870 7 244 -148 A C ATOM 4232 CG PRO A 524 17.117 -4.264 43.215 1.00 17.32 A C ANISOU 4232 CG PRO A 524 2109 2182 2287 -207 -209 129 A C ATOM 4233 CD PRO A 524 16.501 -5.310 44.093 1.00 16.12 A C ANISOU 4233 CD PRO A 524 2085 1606 2431 145 -73 94 A C ATOM 4234 N THR A 525 19.573 -3.287 47.150 1.00 10.88 A N ANISOU 4234 N THR A 525 1386 1006 1741 42 49 1 A N ATOM 4235 CA THR A 525 19.656 -2.626 48.468 1.00 12.09 A C ANISOU 4235 CA THR A 525 1406 1495 1694 49 159 29 A C ATOM 4236 C THR A 525 20.514 -1.355 48.373 1.00 12.58 A C ANISOU 4236 C THR A 525 1707 1300 1770 112 286 -84 A C ATOM 4237 O THR A 525 21.486 -1.273 47.622 1.00 11.45 A O ANISOU 4237 O THR A 525 1427 1104 1819 51 136 -117 A O ATOM 4238 CB THR A 525 20.234 -3.554 49.542 1.00 11.89 A C ANISOU 4238 CB THR A 525 1421 1374 1721 -100 232 63 A C ATOM 4239 CG2 THR A 525 19.318 -4.733 49.756 1.00 12.18 A C ANISOU 4239 CG2 THR A 525 1251 1200 2176 37 366 -49 A C ATOM 4240 OG1 THR A 525 21.563 -3.995 49.213 1.00 12.43 A O ANISOU 4240 OG1 THR A 525 1404 1102 2215 -32 186 133 A O ATOM 4241 N SER A 526 20.173 -0.407 49.244 1.00 10.93 A N ANISOU 4241 N SER A 526 1260 1097 1794 -18 461 -3 A N ATOM 4242 CA SER A 526 20.978 0.802 49.437 1.00 11.00 A C ANISOU 4242 CA SER A 526 1351 1205 1621 -55 222 15 A C ATOM 4243 C SER A 526 22.264 0.429 50.173 1.00 10.65 A C ANISOU 4243 C SER A 526 1467 969 1608 -90 87 14 A C ATOM 4244 O SER A 526 22.306 -0.609 50.847 1.00 11.06 A O ANISOU 4244 O SER A 526 1476 977 1748 43 250 112 A O ATOM 4245 CB SER A 526 20.219 1.821 50.236 1.00 12.25 A C ANISOU 4245 CB SER A 526 1341 1391 1919 162 155 -93 A C ATOM 4246 OG SER A 526 20.080 1.403 51.575 1.00 12.99 A O ANISOU 4246 OG SER A 526 1745 1129 2062 210 157 -1 A O ATOM 4247 N ILE A 527 23.312 1.227 49.972 1.00 10.92 A N ANISOU 4247 N ILE A 527 1556 734 1856 37 195 60 A N ATOM 4248 CA ILE A 527 24.644 1.152 50.622 1.00 10.94 A C ANISOU 4248 CA ILE A 527 1573 850 1733 95 170 -143 A C ATOM 4249 C ILE A 527 25.469 0.012 50.004 1.00 10.56 A C ANISOU 4249 C ILE A 527 1597 866 1547 126 106 -76 A C ATOM 4250 O ILE A 527 26.544 0.255 49.519 1.00 12.13 A O ANISOU 4250 O ILE A 527 1718 894 1994 -126 102 0 A O ATOM 4251 CB ILE A 527 24.586 1.076 52.160 1.00 11.23 A C ANISOU 4251 CB ILE A 527 1798 734 1733 3 44 -211 A C ATOM 4252 CG1 ILE A 527 23.662 2.160 52.744 1.00 11.97 A C ANISOU 4252 CG1 ILE A 527 1618 1031 1898 16 13 -398 A C ATOM 4253 CG2 ILE A 527 25.999 1.166 52.729 1.00 13.22 A C ANISOU 4253 CG2 ILE A 527 1893 1254 1874 92 -43 -277 A C ATOM 4254 CD1 ILE A 527 23.401 1.988 54.205 1.00 14.84 A C ANISOU 4254 CD1 ILE A 527 2135 1430 2074 425 49 -218 A C ATOM 4255 N TRP A 528 24.951 -1.213 50.123 1.00 10.51 A N ANISOU 4255 N TRP A 528 1411 1003 1576 69 286 -57 A N ATOM 4256 CA TRP A 528 25.502 -2.417 49.485 1.00 10.71 A C ANISOU 4256 CA TRP A 528 1392 959 1716 24 133 -205 A C ATOM 4257 C TRP A 528 25.422 -2.233 47.967 1.00 10.17 A C ANISOU 4257 C TRP A 528 1375 721 1766 -9 102 -189 A C ATOM 4258 O TRP A 528 26.471 -2.138 47.338 1.00 10.24 A O ANISOU 4258 O TRP A 528 1228 703 1959 48 85 -18 A O ATOM 4259 CB TRP A 528 24.730 -3.638 50.010 1.00 10.96 A C ANISOU 4259 CB TRP A 528 1553 1070 1540 -186 154 -256 A C ATOM 4260 CG TRP A 528 25.254 -4.117 51.332 1.00 11.09 A C ANISOU 4260 CG TRP A 528 1750 718 1745 0 107 -35 A C ATOM 4261 CD1 TRP A 528 26.002 -5.238 51.548 1.00 12.68 A C ANISOU 4261 CD1 TRP A 528 1872 989 1956 228 158 70 A C ATOM 4262 CD2 TRP A 528 25.102 -3.511 52.634 1.00 11.96 A C ANISOU 4262 CD2 TRP A 528 1862 970 1711 -217 154 -90 A C ATOM 4263 CE2 TRP A 528 25.817 -4.289 53.557 1.00 12.69 A C ANISOU 4263 CE2 TRP A 528 2034 977 1811 3 105 -206 A C ATOM 4264 CE3 TRP A 528 24.450 -2.367 53.117 1.00 13.13 A C ANISOU 4264 CE3 TRP A 528 2157 1015 1816 -171 334 -134 A C ATOM 4265 NE1 TRP A 528 26.336 -5.347 52.865 1.00 13.74 A N ANISOU 4265 NE1 TRP A 528 2416 755 2047 254 108 24 A N ATOM 4266 CZ2 TRP A 528 25.889 -3.991 54.917 1.00 13.89 A C ANISOU 4266 CZ2 TRP A 528 2111 1351 1814 228 -114 -105 A C ATOM 4267 CZ3 TRP A 528 24.536 -2.061 54.462 1.00 14.35 A C ANISOU 4267 CZ3 TRP A 528 2139 1494 1818 318 262 -22 A C ATOM 4268 CH2 TRP A 528 25.238 -2.862 55.358 1.00 13.79 A C ANISOU 4268 CH2 TRP A 528 2362 1538 1339 184 -119 -377 A C ATOM 4269 N GLY A 529 24.236 -2.030 47.397 1.00 10.27 A N ANISOU 4269 N GLY A 529 1375 831 1696 -131 40 -52 A N ATOM 4270 CA GLY A 529 24.172 -1.846 45.978 1.00 11.17 A C ANISOU 4270 CA GLY A 529 1568 887 1788 12 -97 132 A C ATOM 4271 C GLY A 529 24.868 -0.564 45.524 1.00 9.73 A C ANISOU 4271 C GLY A 529 1350 849 1495 32 -79 -31 A C ATOM 4272 O GLY A 529 25.429 -0.496 44.427 1.00 10.77 A O ANISOU 4272 O GLY A 529 1572 907 1610 48 5 -32 A O ATOM 4273 N ASP A 530 24.791 0.462 46.384 1.00 10.02 A N ANISOU 4273 N ASP A 530 1206 989 1610 -79 258 -95 A N ATOM 4274 CA ASP A 530 25.408 1.752 46.098 1.00 9.71 A C ANISOU 4274 CA ASP A 530 1346 907 1435 -52 155 51 A C ATOM 4275 C ASP A 530 26.932 1.657 45.987 1.00 9.99 A C ANISOU 4275 C ASP A 530 1343 882 1570 73 264 -149 A C ATOM 4276 O ASP A 530 27.547 2.622 45.532 1.00 10.37 A O ANISOU 4276 O ASP A 530 1493 897 1549 -135 170 -24 A O ATOM 4277 CB ASP A 530 25.007 2.815 47.108 1.00 10.24 A C ANISOU 4277 CB ASP A 530 1494 924 1471 120 332 130 A C ATOM 4278 CG ASP A 530 23.537 3.213 46.975 1.00 10.78 A C ANISOU 4278 CG ASP A 530 1501 862 1730 -57 82 -165 A C ATOM 4279 OD1 ASP A 530 23.151 3.639 45.840 1.00 11.78 A O ANISOU 4279 OD1 ASP A 530 1624 1143 1707 78 193 -41 A O ATOM 4280 OD2 ASP A 530 22.842 3.123 48.014 1.00 11.65 A O ANISOU 4280 OD2 ASP A 530 1538 1020 1866 173 246 78 A O ATOM 4281 N ALA A 531 27.559 0.534 46.390 1.00 9.81 A N ANISOU 4281 N ALA A 531 1215 827 1681 -72 55 -136 A N ATOM 4282 CA ALA A 531 28.994 0.394 46.204 1.00 8.76 A C ANISOU 4282 CA ALA A 531 1312 696 1319 -99 232 -213 A C ATOM 4283 C ALA A 531 29.445 0.602 44.757 1.00 9.10 A C ANISOU 4283 C ALA A 531 1368 872 1215 195 43 -39 A C ATOM 4284 O ALA A 531 30.604 1.037 44.530 1.00 10.17 A O ANISOU 4284 O ALA A 531 1456 827 1580 127 138 -27 A O ATOM 4285 CB ALA A 531 29.469 -0.949 46.686 1.00 10.60 A C ANISOU 4285 CB ALA A 531 1524 822 1680 56 85 -190 A C ATOM 4286 N ILE A 532 28.567 0.252 43.802 1.00 9.48 A N ANISOU 4286 N ILE A 532 1339 791 1471 -35 9 -52 A N ATOM 4287 CA ILE A 532 28.934 0.348 42.382 1.00 9.65 A C ANISOU 4287 CA ILE A 532 1267 953 1447 11 162 -95 A C ATOM 4288 C ILE A 532 29.095 1.819 41.926 1.00 9.93 A C ANISOU 4288 C ILE A 532 1422 1008 1341 78 25 -75 A C ATOM 4289 O ILE A 532 29.650 2.059 40.842 1.00 10.07 A O ANISOU 4289 O ILE A 532 1526 754 1544 1 44 33 A O ATOM 4290 CB ILE A 532 27.927 -0.441 41.514 1.00 11.09 A C ANISOU 4290 CB ILE A 532 1643 816 1752 -158 -11 174 A C ATOM 4291 CG1 ILE A 532 28.450 -0.790 40.123 1.00 14.24 A C ANISOU 4291 CG1 ILE A 532 2037 1234 2139 -192 178 -229 A C ATOM 4292 CG2 ILE A 532 26.568 0.250 41.467 1.00 12.42 A C ANISOU 4292 CG2 ILE A 532 1594 1188 1935 -103 -204 148 A C ATOM 4293 CD1 ILE A 532 29.593 -1.716 40.141 1.00 14.49 A C ANISOU 4293 CD1 ILE A 532 1951 1658 1894 -68 391 203 A C ATOM 4294 N VAL A 533 28.589 2.751 42.746 1.00 9.42 A N ANISOU 4294 N VAL A 533 1301 804 1473 -62 88 -56 A N ATOM 4295 CA VAL A 533 28.798 4.207 42.555 1.00 9.33 A C ANISOU 4295 CA VAL A 533 1209 807 1529 -7 -4 81 A C ATOM 4296 C VAL A 533 29.917 4.683 43.481 1.00 10.21 A C ANISOU 4296 C VAL A 533 1348 894 1637 89 22 -88 A C ATOM 4297 O VAL A 533 30.817 5.406 43.072 1.00 10.87 A O ANISOU 4297 O VAL A 533 1450 941 1738 -37 220 -50 A O ATOM 4298 CB VAL A 533 27.501 5.008 42.817 1.00 10.04 A C ANISOU 4298 CB VAL A 533 1341 917 1556 101 92 81 A C ATOM 4299 CG1 VAL A 533 27.714 6.502 42.528 1.00 10.49 A C ANISOU 4299 CG1 VAL A 533 1566 854 1564 218 -8 -84 A C ATOM 4300 CG2 VAL A 533 26.334 4.503 41.986 1.00 11.95 A C ANISOU 4300 CG2 VAL A 533 1631 1158 1751 264 -128 93 A C ATOM 4301 N GLY A 534 29.758 4.371 44.758 1.00 9.94 A N ANISOU 4301 N GLY A 534 1351 825 1600 79 133 -53 A N ATOM 4302 CA GLY A 534 30.604 4.948 45.816 1.00 10.79 A C ANISOU 4302 CA GLY A 534 1411 1109 1577 12 100 -51 A C ATOM 4303 C GLY A 534 32.066 4.531 45.733 1.00 10.80 A C ANISOU 4303 C GLY A 534 1440 1042 1620 99 54 -126 A C ATOM 4304 O GLY A 534 32.995 5.290 46.039 1.00 12.22 A O ANISOU 4304 O GLY A 534 1579 1063 1999 -6 215 -93 A O ATOM 4305 N VAL A 535 32.309 3.234 45.452 1.00 9.85 A N ANISOU 4305 N VAL A 535 1352 922 1469 11 168 -21 A N ATOM 4306 CA VAL A 535 33.697 2.762 45.414 1.00 9.60 A C ANISOU 4306 CA VAL A 535 1439 760 1448 -73 8 -256 A C ATOM 4307 C VAL A 535 34.410 3.425 44.223 1.00 9.97 A C ANISOU 4307 C VAL A 535 1442 848 1497 18 71 -182 A C ATOM 4308 O VAL A 535 35.497 3.968 44.408 1.00 10.35 A O ANISOU 4308 O VAL A 535 1569 755 1609 -72 -167 34 A O ATOM 4309 CB VAL A 535 33.843 1.236 45.494 1.00 9.83 A C ANISOU 4309 CB VAL A 535 1490 722 1521 -142 -117 -34 A C ATOM 4310 CG1 VAL A 535 35.298 0.817 45.444 1.00 11.65 A C ANISOU 4310 CG1 VAL A 535 1659 828 1938 46 175 -117 A C ATOM 4311 CG2 VAL A 535 33.237 0.758 46.803 1.00 9.45 A C ANISOU 4311 CG2 VAL A 535 1324 839 1428 102 23 -243 A C ATOM 4312 N PRO A 536 33.850 3.442 42.995 1.00 9.51 A N ANISOU 4312 N PRO A 536 1458 711 1442 13 38 -84 A N ATOM 4313 CA PRO A 536 34.415 4.250 41.899 1.00 9.64 A C ANISOU 4313 CA PRO A 536 1310 739 1612 160 4 162 A C ATOM 4314 C PRO A 536 34.624 5.735 42.242 1.00 10.60 A C ANISOU 4314 C PRO A 536 1239 877 1910 128 30 -82 A C ATOM 4315 O PRO A 536 35.697 6.289 41.910 1.00 10.82 A O ANISOU 4315 O PRO A 536 1342 829 1938 80 10 98 A O ATOM 4316 CB PRO A 536 33.424 4.048 40.749 1.00 10.05 A C ANISOU 4316 CB PRO A 536 1516 678 1624 75 18 77 A C ATOM 4317 CG PRO A 536 32.904 2.647 41.007 1.00 9.36 A C ANISOU 4317 CG PRO A 536 1308 695 1553 -79 -154 -170 A C ATOM 4318 CD PRO A 536 32.721 2.622 42.510 1.00 9.46 A C ANISOU 4318 CD PRO A 536 1263 816 1515 94 -72 -115 A C ATOM 4319 N TRP A 537 33.630 6.351 42.889 1.00 9.42 A N ANISOU 4319 N TRP A 537 1210 520 1846 -35 62 30 A N ATOM 4320 CA TRP A 537 33.779 7.782 43.189 1.00 10.14 A C ANISOU 4320 CA TRP A 537 1413 522 1918 -102 -117 28 A C ATOM 4321 C TRP A 537 35.016 7.992 44.081 1.00 10.52 A C ANISOU 4321 C TRP A 537 1261 1168 1566 -33 70 -72 A C ATOM 4322 O TRP A 537 35.845 8.877 43.842 1.00 11.48 A O ANISOU 4322 O TRP A 537 1729 787 1847 -149 -109 -192 A O ATOM 4323 CB TRP A 537 32.520 8.296 43.886 1.00 12.40 A C ANISOU 4323 CB TRP A 537 1412 999 2298 -15 -101 9 A C ATOM 4324 CG TRP A 537 32.569 9.741 44.310 1.00 13.83 A C ANISOU 4324 CG TRP A 537 1604 1150 2499 -388 -314 -102 A C ATOM 4325 CD1 TRP A 537 32.247 10.828 43.575 1.00 17.02 A C ANISOU 4325 CD1 TRP A 537 2153 1561 2751 48 -566 -115 A C ATOM 4326 CD2 TRP A 537 32.954 10.218 45.597 1.00 14.21 A C ANISOU 4326 CD2 TRP A 537 2045 1118 2235 -5 173 -41 A C ATOM 4327 CE2 TRP A 537 32.874 11.630 45.556 1.00 16.17 A C ANISOU 4327 CE2 TRP A 537 2120 1179 2843 165 147 -348 A C ATOM 4328 CE3 TRP A 537 33.449 9.593 46.736 1.00 17.31 A C ANISOU 4328 CE3 TRP A 537 2152 1978 2446 149 -181 -30 A C ATOM 4329 NE1 TRP A 537 32.390 11.963 44.320 1.00 18.24 A N ANISOU 4329 NE1 TRP A 537 2254 1619 3054 72 20 -325 A N ATOM 4330 CZ2 TRP A 537 33.235 12.407 46.655 1.00 21.65 A C ANISOU 4330 CZ2 TRP A 537 3055 2402 2768 -15 -50 -460 A C ATOM 4331 CZ3 TRP A 537 33.813 10.355 47.822 1.00 19.79 A C ANISOU 4331 CZ3 TRP A 537 2609 1997 2913 -216 61 -402 A C ATOM 4332 CH2 TRP A 537 33.699 11.745 47.777 1.00 21.68 A C ANISOU 4332 CH2 TRP A 537 2948 2109 3178 -57 106 -121 A C ATOM 4333 N GLN A 538 35.132 7.189 45.139 1.00 10.16 A N ANISOU 4333 N GLN A 538 1303 940 1615 -61 53 -101 A N ATOM 4334 CA GLN A 538 36.259 7.276 46.061 1.00 9.91 A C ANISOU 4334 CA GLN A 538 1380 819 1565 26 43 -222 A C ATOM 4335 C GLN A 538 37.590 6.932 45.367 1.00 10.24 A C ANISOU 4335 C GLN A 538 1390 962 1539 5 77 -217 A C ATOM 4336 O GLN A 538 38.669 7.453 45.734 1.00 11.53 A O ANISOU 4336 O GLN A 538 1552 949 1880 -33 -135 -209 A O ATOM 4337 CB GLN A 538 36.031 6.499 47.343 1.00 11.22 A C ANISOU 4337 CB GLN A 538 1608 868 1785 -15 34 -126 A C ATOM 4338 CG GLN A 538 37.164 6.612 48.348 1.00 10.36 A C ANISOU 4338 CG GLN A 538 1704 566 1665 -145 52 73 A C ATOM 4339 CD GLN A 538 37.372 8.032 48.843 1.00 10.81 A C ANISOU 4339 CD GLN A 538 1629 599 1878 65 -22 -53 A C ATOM 4340 NE2 GLN A 538 38.579 8.556 48.632 1.00 12.71 A N ANISOU 4340 NE2 GLN A 538 1810 1062 1956 -187 79 -41 A N ATOM 4341 OE1 GLN A 538 36.482 8.587 49.459 1.00 12.50 A O ANISOU 4341 OE1 GLN A 538 1758 1193 1796 80 128 -255 A O ATOM 4342 N LEU A 539 37.554 5.920 44.485 1.00 10.35 A N ANISOU 4342 N LEU A 539 1547 801 1582 -72 72 -174 A N ATOM 4343 CA LEU A 539 38.756 5.524 43.817 1.00 10.56 A C ANISOU 4343 CA LEU A 539 1351 1014 1647 -172 -120 -98 A C ATOM 4344 C LEU A 539 39.316 6.712 43.019 1.00 9.96 A C ANISOU 4344 C LEU A 539 1324 701 1758 -12 -10 -207 A C ATOM 4345 O LEU A 539 40.534 6.877 42.933 1.00 10.40 A O ANISOU 4345 O LEU A 539 1316 787 1846 -89 64 -170 A O ATOM 4346 CB LEU A 539 38.462 4.295 42.946 1.00 11.99 A C ANISOU 4346 CB LEU A 539 1719 860 1977 -134 -304 -108 A C ATOM 4347 CG LEU A 539 39.644 3.435 42.587 1.00 15.26 A C ANISOU 4347 CG LEU A 539 2134 1492 2170 29 -170 -573 A C ATOM 4348 CD1 LEU A 539 40.313 2.826 43.823 1.00 13.98 A C ANISOU 4348 CD1 LEU A 539 1924 1011 2377 11 -87 -256 A C ATOM 4349 CD2 LEU A 539 39.183 2.360 41.625 1.00 15.33 A C ANISOU 4349 CD2 LEU A 539 2239 1033 2553 -52 -180 -474 A C ATOM 4350 N TYR A 540 38.407 7.448 42.355 1.00 10.58 A N ANISOU 4350 N TYR A 540 1231 832 1956 -110 3 52 A N ATOM 4351 CA TYR A 540 38.827 8.623 41.587 1.00 10.23 A C ANISOU 4351 CA TYR A 540 1397 781 1708 -192 5 -63 A C ATOM 4352 C TYR A 540 39.344 9.765 42.506 1.00 10.25 A C ANISOU 4352 C TYR A 540 1364 780 1750 140 -104 -153 A C ATOM 4353 O TYR A 540 40.414 10.309 42.228 1.00 11.82 A O ANISOU 4353 O TYR A 540 1628 851 2012 44 197 -167 A O ATOM 4354 CB TYR A 540 37.664 9.088 40.723 1.00 10.38 A C ANISOU 4354 CB TYR A 540 1394 895 1653 -44 70 -156 A C ATOM 4355 CG TYR A 540 38.016 10.265 39.857 1.00 11.06 A C ANISOU 4355 CG TYR A 540 1589 911 1699 -56 -109 4 A C ATOM 4356 CD1 TYR A 540 38.963 10.123 38.868 1.00 11.63 A C ANISOU 4356 CD1 TYR A 540 1514 1151 1752 -224 -96 33 A C ATOM 4357 CD2 TYR A 540 37.445 11.510 40.009 1.00 13.29 A C ANISOU 4357 CD2 TYR A 540 2014 1060 1974 123 -84 34 A C ATOM 4358 CE1 TYR A 540 39.351 11.167 38.041 1.00 13.93 A C ANISOU 4358 CE1 TYR A 540 1806 1472 2011 -252 -158 330 A C ATOM 4359 CE2 TYR A 540 37.764 12.554 39.152 1.00 14.69 A C ANISOU 4359 CE2 TYR A 540 2155 1245 2182 -131 -453 275 A C ATOM 4360 CZ TYR A 540 38.733 12.393 38.169 1.00 14.61 A C ANISOU 4360 CZ TYR A 540 1965 1212 2374 -434 -317 368 A C ATOM 4361 OH TYR A 540 39.115 13.419 37.355 1.00 20.57 A O ANISOU 4361 OH TYR A 540 3159 1563 3093 -769 -663 903 A O ATOM 4362 N GLU A 541 38.664 9.980 43.633 1.00 10.48 A N ANISOU 4362 N GLU A 541 1523 798 1660 -119 -113 -180 A N ATOM 4363 CA GLU A 541 39.140 10.961 44.601 1.00 10.44 A C ANISOU 4363 CA GLU A 541 1418 691 1855 -9 -193 -235 A C ATOM 4364 C GLU A 541 40.580 10.622 45.023 1.00 11.22 A C ANISOU 4364 C GLU A 541 1378 852 2031 -129 -237 -20 A C ATOM 4365 O GLU A 541 41.461 11.499 45.128 1.00 12.10 A O ANISOU 4365 O GLU A 541 1479 952 2164 -249 -101 -78 A O ATOM 4366 CB GLU A 541 38.256 11.005 45.828 1.00 12.41 A C ANISOU 4366 CB GLU A 541 1941 881 1892 6 -36 -314 A C ATOM 4367 CG GLU A 541 36.894 11.622 45.555 1.00 15.79 A C ANISOU 4367 CG GLU A 541 2149 1278 2572 115 34 -104 A C ATOM 4368 CD GLU A 541 36.886 13.072 45.127 1.00 17.11 A C ANISOU 4368 CD GLU A 541 2370 1252 2877 47 187 -99 A C ATOM 4369 OE1 GLU A 541 37.339 13.908 45.941 1.00 25.57 A O ANISOU 4369 OE1 GLU A 541 4318 2045 3351 -91 -502 -618 A O ATOM 4370 OE2 GLU A 541 36.465 13.319 43.965 1.00 22.63 A O ANISOU 4370 OE2 GLU A 541 2603 2562 3431 74 -302 312 A O ATOM 4371 N SER A 542 40.839 9.321 45.223 1.00 10.45 A N ANISOU 4371 N SER A 542 1430 765 1773 -52 -163 -229 A N ATOM 4372 CA SER A 542 42.146 8.907 45.770 1.00 9.89 A C ANISOU 4372 CA SER A 542 1444 526 1787 -73 -47 -177 A C ATOM 4373 C SER A 542 43.254 8.900 44.701 1.00 10.38 A C ANISOU 4373 C SER A 542 1428 753 1761 141 -63 -157 A C ATOM 4374 O SER A 542 44.414 9.288 44.999 1.00 13.56 A O ANISOU 4374 O SER A 542 1567 1442 2141 -135 -67 -592 A O ATOM 4375 CB SER A 542 42.008 7.506 46.341 1.00 10.82 A C ANISOU 4375 CB SER A 542 1768 408 1934 33 91 -207 A C ATOM 4376 OG SER A 542 41.177 7.515 47.482 1.00 11.50 A O ANISOU 4376 OG SER A 542 1888 658 1823 -79 53 -56 A O ATOM 4377 N PHE A 543 42.933 8.418 43.484 1.00 10.87 A N ANISOU 4377 N PHE A 543 1393 1166 1570 -32 -77 -120 A N ATOM 4378 CA PHE A 543 44.019 8.127 42.495 1.00 10.67 A C ANISOU 4378 CA PHE A 543 1557 811 1683 -158 32 -165 A C ATOM 4379 C PHE A 543 43.923 8.938 41.193 1.00 11.02 A C ANISOU 4379 C PHE A 543 1397 1095 1692 -210 116 -87 A C ATOM 4380 O PHE A 543 44.860 8.970 40.411 1.00 12.80 A O ANISOU 4380 O PHE A 543 1749 1053 2060 -180 372 59 A O ATOM 4381 CB PHE A 543 44.125 6.629 42.237 1.00 11.37 A C ANISOU 4381 CB PHE A 543 1731 829 1760 15 213 -117 A C ATOM 4382 CG PHE A 543 44.366 5.818 43.479 1.00 11.13 A C ANISOU 4382 CG PHE A 543 1310 1237 1679 20 36 -74 A C ATOM 4383 CD1 PHE A 543 45.570 5.861 44.154 1.00 14.92 A C ANISOU 4383 CD1 PHE A 543 1698 1683 2286 -345 -356 -20 A C ATOM 4384 CD2 PHE A 543 43.352 5.051 43.994 1.00 11.04 A C ANISOU 4384 CD2 PHE A 543 1201 1149 1842 65 65 -43 A C ATOM 4385 CE1 PHE A 543 45.761 5.136 45.318 1.00 15.08 A C ANISOU 4385 CE1 PHE A 543 1660 1615 2455 -214 -94 217 A C ATOM 4386 CE2 PHE A 543 43.532 4.330 45.174 1.00 11.08 A C ANISOU 4386 CE2 PHE A 543 1418 911 1878 -22 16 -146 A C ATOM 4387 CZ PHE A 543 44.728 4.370 45.835 1.00 10.88 A C ANISOU 4387 CZ PHE A 543 1591 1132 1410 99 -71 193 A C ATOM 4388 N GLY A 544 42.789 9.610 40.979 1.00 11.15 A N ANISOU 4388 N GLY A 544 1570 901 1763 -159 -18 23 A N ATOM 4389 CA GLY A 544 42.632 10.523 39.865 1.00 11.94 A C ANISOU 4389 CA GLY A 544 1570 1147 1817 -123 -81 130 A C ATOM 4390 C GLY A 544 42.624 9.936 38.467 1.00 11.52 A C ANISOU 4390 C GLY A 544 1436 1000 1939 -50 228 -60 A C ATOM 4391 O GLY A 544 42.910 10.624 37.487 1.00 14.14 A O ANISOU 4391 O GLY A 544 2051 1383 1935 -90 79 64 A O ATOM 4392 N ASP A 545 42.330 8.631 38.332 1.00 10.37 A N ANISOU 4392 N ASP A 545 1370 964 1606 -165 2 -11 A N ATOM 4393 CA ASP A 545 42.446 7.963 37.060 1.00 10.37 A C ANISOU 4393 CA ASP A 545 1198 1137 1603 -51 107 141 A C ATOM 4394 C ASP A 545 41.152 8.116 36.232 1.00 9.77 A C ANISOU 4394 C ASP A 545 1161 892 1657 -99 87 222 A C ATOM 4395 O ASP A 545 40.153 7.452 36.539 1.00 10.37 A O ANISOU 4395 O ASP A 545 1377 790 1773 -228 282 139 A O ATOM 4396 CB ASP A 545 42.792 6.500 37.308 1.00 10.69 A C ANISOU 4396 CB ASP A 545 1429 1088 1544 -93 85 226 A C ATOM 4397 CG ASP A 545 43.047 5.753 36.023 1.00 11.43 A C ANISOU 4397 CG ASP A 545 1783 903 1656 -196 202 193 A C ATOM 4398 OD1 ASP A 545 42.579 6.174 34.969 1.00 11.21 A O ANISOU 4398 OD1 ASP A 545 1559 1015 1685 82 121 85 A O ATOM 4399 OD2 ASP A 545 43.633 4.649 36.120 1.00 11.81 A O ANISOU 4399 OD2 ASP A 545 1423 946 2116 -120 140 59 A O ATOM 4400 N LYS A 546 41.166 8.981 35.206 1.00 10.17 A N ANISOU 4400 N LYS A 546 1467 669 1726 -176 96 148 A N ATOM 4401 CA LYS A 546 39.969 9.251 34.411 1.00 12.65 A C ANISOU 4401 CA LYS A 546 1645 1161 1997 -185 -59 345 A C ATOM 4402 C LYS A 546 39.562 8.026 33.573 1.00 12.53 A C ANISOU 4402 C LYS A 546 1614 1321 1823 -152 99 274 A C ATOM 4403 O LYS A 546 38.398 7.864 33.261 1.00 12.24 A O ANISOU 4403 O LYS A 546 1618 882 2147 5 68 162 A O ATOM 4404 CB LYS A 546 40.168 10.515 33.548 1.00 18.06 A C ANISOU 4404 CB LYS A 546 2655 948 3258 -725 475 519 A C ATOM 4405 CG LYS A 546 40.155 11.804 34.359 1.00 27.06 A C ANISOU 4405 CG LYS A 546 4516 1952 3810 -309 141 190 A C ATOM 4406 CD LYS A 546 39.678 13.072 33.640 1.00 36.28 A C ANISOU 4406 CD LYS A 546 6077 2025 5679 -1189 224 1555 A C ATOM 4407 CE LYS A 546 40.168 14.299 34.374 1.00 44.70 A C ANISOU 4407 CE LYS A 546 6975 2923 7084 -592 -1141 808 A C ATOM 4408 NZ LYS A 546 41.648 14.345 34.409 1.00 47.62 A N ANISOU 4408 NZ LYS A 546 7206 2800 8087 123 110 1849 A N ATOM 4409 N VAL A 547 40.541 7.226 33.133 1.00 11.94 A N ANISOU 4409 N VAL A 547 1517 1288 1729 -203 -27 89 A N ATOM 4410 CA VAL A 547 40.254 6.025 32.335 1.00 12.36 A C ANISOU 4410 CA VAL A 547 1782 1405 1509 -101 -20 52 A C ATOM 4411 C VAL A 547 39.468 5.005 33.170 1.00 11.27 A C ANISOU 4411 C VAL A 547 1460 1263 1560 -3 92 -183 A C ATOM 4412 O VAL A 547 38.469 4.443 32.701 1.00 12.16 A O ANISOU 4412 O VAL A 547 1735 1168 1715 -78 -151 -143 A O ATOM 4413 CB VAL A 547 41.532 5.424 31.719 1.00 14.18 A C ANISOU 4413 CB VAL A 547 1831 1642 1911 -71 110 -231 A C ATOM 4414 CG1 VAL A 547 41.247 4.077 31.048 1.00 15.68 A C ANISOU 4414 CG1 VAL A 547 1774 1936 2246 71 -155 -527 A C ATOM 4415 CG2 VAL A 547 42.141 6.406 30.747 1.00 16.14 A C ANISOU 4415 CG2 VAL A 547 1946 2041 2146 -83 121 -33 A C ATOM 4416 N MET A 548 39.935 4.786 34.398 1.00 10.73 A N ANISOU 4416 N MET A 548 1315 1042 1719 -152 -95 -15 A N ATOM 4417 CA AMET A 548 39.257 3.877 35.267 0.60 11.65 A C ANISOU 4417 CA AMET A 548 1670 994 1761 -85 34 47 A C ATOM 4418 CA BMET A 548 39.246 3.870 35.337 0.40 11.01 A C ANISOU 4418 CA BMET A 548 1587 930 1664 -51 -40 21 A C ATOM 4419 C MET A 548 37.858 4.407 35.654 1.00 10.62 A C ANISOU 4419 C MET A 548 1553 933 1546 -92 -120 -88 A C ATOM 4420 O MET A 548 36.886 3.652 35.755 1.00 11.74 A O ANISOU 4420 O MET A 548 1402 1089 1969 -18 128 69 A O ATOM 4421 CB AMET A 548 40.152 3.576 36.467 0.60 13.62 A C ANISOU 4421 CB AMET A 548 2099 962 2111 -355 -359 25 A C ATOM 4422 CB BMET A 548 39.967 3.631 36.668 0.40 11.05 A C ANISOU 4422 CB BMET A 548 1618 869 1710 40 -56 -5 A C ATOM 4423 CG AMET A 548 39.584 2.588 37.385 0.60 14.02 A C ANISOU 4423 CG AMET A 548 1985 1291 2048 -243 -117 123 A C ATOM 4424 CG BMET A 548 41.074 2.620 36.562 0.40 11.23 A C ANISOU 4424 CG BMET A 548 1577 1052 1637 140 65 54 A C ATOM 4425 SD AMET A 548 40.832 1.846 38.481 0.60 12.70 A S ANISOU 4425 SD AMET A 548 1789 866 2168 68 165 46 A S ATOM 4426 SD BMET A 548 41.549 1.886 38.157 0.40 9.00 A S ANISOU 4426 SD BMET A 548 1169 556 1695 12 214 139 A S ATOM 4427 CE AMET A 548 41.465 3.282 39.339 0.60 12.30 A C ANISOU 4427 CE AMET A 548 1569 620 2484 34 108 118 A C ATOM 4428 CE BMET A 548 42.081 3.338 39.056 0.40 9.08 A C ANISOU 4428 CE BMET A 548 1394 352 1701 102 190 208 A C ATOM 4429 N LEU A 549 37.750 5.730 35.837 1.00 11.09 A N ANISOU 4429 N LEU A 549 1450 837 1926 -59 27 20 A N ATOM 4430 CA LEU A 549 36.416 6.299 36.141 1.00 10.88 A C ANISOU 4430 CA LEU A 549 1455 824 1853 -88 29 177 A C ATOM 4431 C LEU A 549 35.450 6.049 34.977 1.00 10.50 A C ANISOU 4431 C LEU A 549 1380 897 1713 194 144 -59 A C ATOM 4432 O LEU A 549 34.304 5.634 35.169 1.00 11.87 A O ANISOU 4432 O LEU A 549 1640 1025 1845 -182 170 201 A O ATOM 4433 CB LEU A 549 36.542 7.789 36.446 1.00 11.55 A C ANISOU 4433 CB LEU A 549 1683 785 1920 11 86 188 A C ATOM 4434 CG LEU A 549 35.250 8.460 36.902 1.00 11.75 A C ANISOU 4434 CG LEU A 549 1577 982 1903 91 -154 -4 A C ATOM 4435 CD1 LEU A 549 34.748 7.881 38.194 1.00 13.19 A C ANISOU 4435 CD1 LEU A 549 1426 1585 1999 319 133 -184 A C ATOM 4436 CD2 LEU A 549 35.459 9.968 37.058 1.00 12.52 A C ANISOU 4436 CD2 LEU A 549 1667 999 2089 117 -71 -41 A C ATOM 4437 N GLU A 550 35.937 6.241 33.743 1.00 11.50 A N ANISOU 4437 N GLU A 550 1550 1184 1635 -79 18 -13 A N ATOM 4438 CA GLU A 550 35.110 5.959 32.569 1.00 10.57 A C ANISOU 4438 CA GLU A 550 1576 1052 1386 73 96 53 A C ATOM 4439 C GLU A 550 34.725 4.466 32.501 1.00 11.35 A C ANISOU 4439 C GLU A 550 1553 1132 1624 14 25 71 A C ATOM 4440 O GLU A 550 33.558 4.183 32.212 1.00 12.62 A O ANISOU 4440 O GLU A 550 1648 1210 1937 -103 -150 -18 A O ATOM 4441 CB GLU A 550 35.824 6.360 31.283 1.00 11.90 A C ANISOU 4441 CB GLU A 550 1667 1147 1708 -1 204 196 A C ATOM 4442 CG GLU A 550 34.996 6.188 30.036 1.00 15.01 A C ANISOU 4442 CG GLU A 550 1788 1971 1944 -166 221 336 A C ATOM 4443 CD GLU A 550 33.866 7.180 29.878 1.00 19.06 A C ANISOU 4443 CD GLU A 550 2431 1903 2905 113 -138 224 A C ATOM 4444 OE1 GLU A 550 34.111 8.383 30.111 1.00 23.79 A O ANISOU 4444 OE1 GLU A 550 3278 2093 3668 -19 -334 84 A O ATOM 4445 OE2 GLU A 550 32.747 6.741 29.497 1.00 27.01 A O ANISOU 4445 OE2 GLU A 550 2365 3988 3907 6 -667 -21 A O ATOM 4446 N GLU A 551 35.656 3.536 32.781 1.00 11.11 A N ANISOU 4446 N GLU A 551 1398 1294 1530 -64 38 80 A N ATOM 4447 CA GLU A 551 35.261 2.105 32.697 1.00 11.44 A C ANISOU 4447 CA GLU A 551 1492 1338 1515 -128 246 -151 A C ATOM 4448 C GLU A 551 34.237 1.748 33.772 1.00 11.38 A C ANISOU 4448 C GLU A 551 1491 1312 1520 -184 163 -71 A C ATOM 4449 O GLU A 551 33.431 0.815 33.560 1.00 12.53 A O ANISOU 4449 O GLU A 551 1560 1274 1925 -255 58 -50 A O ATOM 4450 CB GLU A 551 36.508 1.234 32.673 1.00 14.69 A C ANISOU 4450 CB GLU A 551 1662 1909 2007 154 274 241 A C ATOM 4451 CG GLU A 551 37.099 0.851 33.984 1.00 16.75 A C ANISOU 4451 CG GLU A 551 1541 2650 2172 55 175 304 A C ATOM 4452 CD GLU A 551 38.522 0.306 33.909 1.00 18.71 A C ANISOU 4452 CD GLU A 551 1626 2809 2672 162 213 579 A C ATOM 4453 OE1 GLU A 551 39.241 0.674 32.924 1.00 19.42 A O ANISOU 4453 OE1 GLU A 551 1788 3197 2393 -45 127 327 A O ATOM 4454 OE2 GLU A 551 38.919 -0.423 34.854 1.00 14.46 A O ANISOU 4454 OE2 GLU A 551 1638 1896 1958 87 86 100 A O ATOM 4455 N GLN A 552 34.258 2.460 34.899 1.00 9.39 A N ANISOU 4455 N GLN A 552 1270 776 1520 -147 163 -11 A N ATOM 4456 CA GLN A 552 33.360 2.208 36.030 1.00 10.26 A C ANISOU 4456 CA GLN A 552 1272 956 1666 -235 111 184 A C ATOM 4457 C GLN A 552 32.023 2.966 35.906 1.00 10.44 A C ANISOU 4457 C GLN A 552 1553 926 1486 15 131 79 A C ATOM 4458 O GLN A 552 31.104 2.760 36.711 1.00 11.69 A O ANISOU 4458 O GLN A 552 1583 1049 1807 38 217 33 A O ATOM 4459 CB GLN A 552 34.093 2.487 37.337 1.00 10.24 A C ANISOU 4459 CB GLN A 552 1346 984 1558 121 31 246 A C ATOM 4460 CG GLN A 552 35.200 1.471 37.569 1.00 9.78 A C ANISOU 4460 CG GLN A 552 1304 874 1535 85 -38 -15 A C ATOM 4461 CD GLN A 552 36.254 1.874 38.570 1.00 11.27 A C ANISOU 4461 CD GLN A 552 1428 1267 1586 26 -94 -128 A C ATOM 4462 NE2 GLN A 552 37.339 1.109 38.633 1.00 11.23 A N ANISOU 4462 NE2 GLN A 552 1361 1139 1764 13 -113 -292 A N ATOM 4463 OE1 GLN A 552 36.097 2.852 39.306 1.00 12.12 A O ANISOU 4463 OE1 GLN A 552 1490 1086 2029 31 -186 -280 A O ATOM 4464 N TYR A 553 31.929 3.863 34.922 1.00 11.32 A N ANISOU 4464 N TYR A 553 1276 1132 1893 -49 105 393 A N ATOM 4465 CA TYR A 553 30.768 4.690 34.782 1.00 10.80 A C ANISOU 4465 CA TYR A 553 1188 1021 1894 -123 219 112 A C ATOM 4466 C TYR A 553 29.495 3.915 34.481 1.00 9.70 A C ANISOU 4466 C TYR A 553 1274 848 1562 -40 47 226 A C ATOM 4467 O TYR A 553 28.444 4.187 35.111 1.00 12.13 A O ANISOU 4467 O TYR A 553 1479 959 2168 -111 307 164 A O ATOM 4468 CB TYR A 553 30.975 5.761 33.709 1.00 11.67 A C ANISOU 4468 CB TYR A 553 1620 970 1843 -85 -46 183 A C ATOM 4469 CG TYR A 553 29.846 6.750 33.625 1.00 11.95 A C ANISOU 4469 CG TYR A 553 1518 1078 1943 -169 75 371 A C ATOM 4470 CD1 TYR A 553 29.670 7.706 34.608 1.00 13.03 A C ANISOU 4470 CD1 TYR A 553 1705 1028 2216 135 -228 269 A C ATOM 4471 CD2 TYR A 553 28.927 6.716 32.593 1.00 13.23 A C ANISOU 4471 CD2 TYR A 553 1942 1004 2081 -40 -119 400 A C ATOM 4472 CE1 TYR A 553 28.676 8.663 34.521 1.00 13.22 A C ANISOU 4472 CE1 TYR A 553 1646 1001 2373 98 -60 284 A C ATOM 4473 CE2 TYR A 553 27.902 7.656 32.502 1.00 15.06 A C ANISOU 4473 CE2 TYR A 553 1919 1375 2426 140 -95 261 A C ATOM 4474 CZ TYR A 553 27.759 8.613 33.485 1.00 13.89 A C ANISOU 4474 CZ TYR A 553 1801 1189 2287 31 -97 396 A C ATOM 4475 OH TYR A 553 26.771 9.565 33.400 1.00 13.99 A O ANISOU 4475 OH TYR A 553 1760 1206 2347 105 -93 319 A O ATOM 4476 N GLY A 554 29.598 2.933 33.575 1.00 12.04 A N ANISOU 4476 N GLY A 554 1559 1130 1882 -140 275 -85 A N ATOM 4477 CA GLY A 554 28.373 2.235 33.173 1.00 11.84 A C ANISOU 4477 CA GLY A 554 1521 1418 1556 -59 126 148 A C ATOM 4478 C GLY A 554 27.709 1.502 34.332 1.00 11.15 A C ANISOU 4478 C GLY A 554 1476 1349 1411 -39 104 -35 A C ATOM 4479 O GLY A 554 26.483 1.531 34.494 1.00 12.29 A O ANISOU 4479 O GLY A 554 1483 956 2229 -39 66 -18 A O ATOM 4480 N GLY A 555 28.520 0.931 35.219 1.00 10.33 A N ANISOU 4480 N GLY A 555 1259 1084 1580 -63 44 -126 A N ATOM 4481 CA GLY A 555 27.962 0.283 36.402 1.00 10.98 A C ANISOU 4481 CA GLY A 555 1490 1117 1564 -19 -11 -6 A C ATOM 4482 C GLY A 555 27.193 1.250 37.285 1.00 10.54 A C ANISOU 4482 C GLY A 555 1487 1000 1518 31 -72 108 A C ATOM 4483 O GLY A 555 26.087 0.971 37.780 1.00 11.35 A O ANISOU 4483 O GLY A 555 1659 741 1912 -90 193 28 A O ATOM 4484 N ALA A 556 27.818 2.410 37.541 1.00 10.69 A N ANISOU 4484 N ALA A 556 1428 956 1678 -119 120 266 A N ATOM 4485 CA ALA A 556 27.205 3.439 38.377 1.00 10.59 A C ANISOU 4485 CA ALA A 556 1320 1095 1606 -184 97 139 A C ATOM 4486 C ALA A 556 25.895 3.966 37.767 1.00 10.07 A C ANISOU 4486 C ALA A 556 1504 826 1494 -157 -19 -47 A C ATOM 4487 O ALA A 556 24.884 4.049 38.449 1.00 11.60 A O ANISOU 4487 O ALA A 556 1493 1044 1869 -122 128 98 A O ATOM 4488 CB ALA A 556 28.222 4.557 38.605 1.00 11.68 A C ANISOU 4488 CB ALA A 556 1557 983 1895 -186 62 -109 A C ATOM 4489 N LYS A 557 25.938 4.285 36.484 1.00 10.43 A N ANISOU 4489 N LYS A 557 1372 1071 1519 -65 10 155 A N ATOM 4490 CA LYS A 557 24.782 4.827 35.815 1.00 11.29 A C ANISOU 4490 CA LYS A 557 1396 1371 1520 13 -6 101 A C ATOM 4491 C LYS A 557 23.641 3.801 35.718 1.00 11.36 A C ANISOU 4491 C LYS A 557 1440 1295 1578 31 -109 126 A C ATOM 4492 O LYS A 557 22.479 4.111 35.987 1.00 12.74 A O ANISOU 4492 O LYS A 557 1720 895 2223 67 234 125 A O ATOM 4493 CB LYS A 557 25.163 5.353 34.433 1.00 12.97 A C ANISOU 4493 CB LYS A 557 1878 1486 1562 -186 -114 164 A C ATOM 4494 CG LYS A 557 23.984 5.837 33.598 1.00 15.07 A C ANISOU 4494 CG LYS A 557 1990 1816 1918 -39 -247 340 A C ATOM 4495 CD LYS A 557 24.415 6.676 32.417 1.00 15.53 A C ANISOU 4495 CD LYS A 557 2004 1973 1923 53 -10 320 A C ATOM 4496 CE LYS A 557 23.328 6.946 31.389 1.00 18.05 A C ANISOU 4496 CE LYS A 557 2220 2629 2008 263 0 658 A C ATOM 4497 NZ LYS A 557 22.054 7.511 31.891 1.00 17.07 A N ANISOU 4497 NZ LYS A 557 2301 1906 2276 265 -181 390 A N ATOM 4498 N ASP A 558 23.961 2.547 35.399 1.00 11.36 A N ANISOU 4498 N ASP A 558 1334 1300 1682 147 121 201 A N ATOM 4499 CA ASP A 558 22.914 1.540 35.260 1.00 12.17 A C ANISOU 4499 CA ASP A 558 1439 1347 1836 165 -112 189 A C ATOM 4500 C ASP A 558 22.276 1.243 36.622 1.00 11.03 A C ANISOU 4500 C ASP A 558 1550 879 1761 -24 -160 17 A C ATOM 4501 O ASP A 558 21.076 0.968 36.682 1.00 12.12 A O ANISOU 4501 O ASP A 558 1445 1206 1952 -61 -166 69 A O ATOM 4502 CB ASP A 558 23.451 0.243 34.666 1.00 12.12 A C ANISOU 4502 CB ASP A 558 1433 1344 1826 17 -228 12 A C ATOM 4503 CG ASP A 558 23.684 0.271 33.167 1.00 13.74 A C ANISOU 4503 CG ASP A 558 1575 1789 1855 136 -2 -36 A C ATOM 4504 OD1 ASP A 558 23.190 1.210 32.493 1.00 18.00 A O ANISOU 4504 OD1 ASP A 558 2492 2204 2144 742 -93 123 A O ATOM 4505 OD2 ASP A 558 24.360 -0.669 32.653 1.00 14.89 A O ANISOU 4505 OD2 ASP A 558 1782 1882 1994 331 -137 -231 A O ATOM 4506 N TRP A 559 23.053 1.309 37.709 1.00 11.33 A N ANISOU 4506 N TRP A 559 1596 1046 1662 -115 -64 -23 A N ATOM 4507 CA TRP A 559 22.505 1.116 39.029 1.00 10.74 A C ANISOU 4507 CA TRP A 559 1534 926 1620 -190 -2 6 A C ATOM 4508 C TRP A 559 21.415 2.159 39.334 1.00 11.56 A C ANISOU 4508 C TRP A 559 1585 1319 1487 -103 8 51 A C ATOM 4509 O TRP A 559 20.306 1.825 39.785 1.00 12.18 A O ANISOU 4509 O TRP A 559 1659 856 2112 -149 18 204 A O ATOM 4510 CB TRP A 559 23.608 1.152 40.070 1.00 11.11 A C ANISOU 4510 CB TRP A 559 1640 1031 1549 -3 8 35 A C ATOM 4511 CG TRP A 559 23.143 1.243 41.481 1.00 10.05 A C ANISOU 4511 CG TRP A 559 1235 1037 1544 134 18 -104 A C ATOM 4512 CD1 TRP A 559 23.321 2.292 42.319 1.00 11.43 A C ANISOU 4512 CD1 TRP A 559 1422 1128 1790 -20 260 -259 A C ATOM 4513 CD2 TRP A 559 22.412 0.269 42.243 1.00 11.37 A C ANISOU 4513 CD2 TRP A 559 1414 1199 1706 19 -32 80 A C ATOM 4514 CE2 TRP A 559 22.213 0.799 43.535 1.00 10.92 A C ANISOU 4514 CE2 TRP A 559 1438 964 1746 -62 47 19 A C ATOM 4515 CE3 TRP A 559 21.920 -1.024 41.987 1.00 12.12 A C ANISOU 4515 CE3 TRP A 559 1418 1313 1872 -133 -13 37 A C ATOM 4516 NE1 TRP A 559 22.772 2.057 43.546 1.00 10.66 A N ANISOU 4516 NE1 TRP A 559 1586 832 1631 0 19 -71 A N ATOM 4517 CZ2 TRP A 559 21.527 0.136 44.546 1.00 11.65 A C ANISOU 4517 CZ2 TRP A 559 1402 1166 1859 124 272 12 A C ATOM 4518 CZ3 TRP A 559 21.233 -1.670 42.988 1.00 13.08 A C ANISOU 4518 CZ3 TRP A 559 1773 1220 1977 -72 40 111 A C ATOM 4519 CH2 TRP A 559 21.080 -1.133 44.265 1.00 12.86 A C ANISOU 4519 CH2 TRP A 559 1505 1408 1972 -175 228 129 A C ATOM 4520 N VAL A 560 21.758 3.442 39.134 1.00 12.17 A N ANISOU 4520 N VAL A 560 1522 1289 1812 -80 91 66 A N ATOM 4521 CA VAL A 560 20.800 4.492 39.434 1.00 11.40 A C ANISOU 4521 CA VAL A 560 1494 1091 1746 -191 116 195 A C ATOM 4522 C VAL A 560 19.606 4.379 38.472 1.00 11.28 A C ANISOU 4522 C VAL A 560 1557 780 1945 -42 -5 -30 A C ATOM 4523 O VAL A 560 18.449 4.521 38.889 1.00 13.39 A O ANISOU 4523 O VAL A 560 1621 1191 2274 -13 200 2 A O ATOM 4524 CB VAL A 560 21.467 5.859 39.383 1.00 11.99 A C ANISOU 4524 CB VAL A 560 1710 931 1914 -145 94 83 A C ATOM 4525 CG1 VAL A 560 20.490 7.003 39.522 1.00 12.97 A C ANISOU 4525 CG1 VAL A 560 1527 1176 2225 -100 136 -81 A C ATOM 4526 CG2 VAL A 560 22.513 5.934 40.476 1.00 12.48 A C ANISOU 4526 CG2 VAL A 560 1775 1065 1900 -44 113 17 A C ATOM 4527 N ASP A 561 19.879 4.159 37.184 1.00 12.29 A N ANISOU 4527 N ASP A 561 1596 1178 1896 -220 0 146 A N ATOM 4528 CA ASP A 561 18.835 4.216 36.194 1.00 12.73 A C ANISOU 4528 CA ASP A 561 1507 1304 2026 -95 -64 53 A C ATOM 4529 C ASP A 561 17.867 3.017 36.287 1.00 13.41 A C ANISOU 4529 C ASP A 561 1572 1275 2246 -49 -170 -7 A C ATOM 4530 O ASP A 561 16.662 3.178 35.993 1.00 14.04 A O ANISOU 4530 O ASP A 561 1472 1497 2362 31 -242 173 A O ATOM 4531 CB ASP A 561 19.411 4.257 34.794 1.00 13.06 A C ANISOU 4531 CB ASP A 561 1685 1368 1909 102 -219 361 A C ATOM 4532 CG ASP A 561 20.118 5.557 34.442 1.00 13.26 A C ANISOU 4532 CG ASP A 561 1533 1431 2075 -7 49 105 A C ATOM 4533 OD1 ASP A 561 19.954 6.575 35.216 1.00 14.04 A O ANISOU 4533 OD1 ASP A 561 1738 1570 2024 178 -14 80 A O ATOM 4534 OD2 ASP A 561 20.774 5.550 33.365 1.00 15.31 A O ANISOU 4534 OD2 ASP A 561 2209 1631 1976 -6 40 167 A O ATOM 4535 N LYS A 562 18.404 1.817 36.543 1.00 13.65 A N ANISOU 4535 N LYS A 562 1339 1358 2487 15 -134 0 A N ATOM 4536 CA LYS A 562 17.648 0.581 36.321 1.00 14.89 A C ANISOU 4536 CA LYS A 562 1702 1540 2414 -256 -452 135 A C ATOM 4537 C LYS A 562 17.719 -0.415 37.492 1.00 15.10 A C ANISOU 4537 C LYS A 562 1538 1903 2295 -201 -307 263 A C ATOM 4538 O LYS A 562 16.947 -1.390 37.532 1.00 19.53 A O ANISOU 4538 O LYS A 562 1980 2479 2961 -783 -333 507 A O ATOM 4539 CB LYS A 562 18.164 -0.092 35.045 1.00 16.85 A C ANISOU 4539 CB LYS A 562 2021 1753 2627 -329 -355 61 A C ATOM 4540 CG LYS A 562 17.973 0.724 33.778 1.00 18.09 A C ANISOU 4540 CG LYS A 562 2402 2026 2444 0 -160 111 A C ATOM 4541 CD LYS A 562 18.455 0.037 32.512 1.00 22.92 A C ANISOU 4541 CD LYS A 562 3341 2864 2503 -174 -246 -300 A C ATOM 4542 CE LYS A 562 18.416 0.915 31.288 1.00 28.67 A C ANISOU 4542 CE LYS A 562 4220 3987 2684 314 -249 16 A C ATOM 4543 NZ LYS A 562 18.947 0.178 30.109 1.00 34.87 A N ANISOU 4543 NZ LYS A 562 4725 5145 3377 118 849 -272 A N ATOM 4544 N GLY A 563 18.719 -0.261 38.367 1.00 12.13 A N ANISOU 4544 N GLY A 563 1491 1052 2065 -273 -143 55 A N ATOM 4545 CA GLY A 563 18.912 -1.172 39.488 1.00 13.94 A C ANISOU 4545 CA GLY A 563 1650 1368 2277 -140 -70 300 A C ATOM 4546 C GLY A 563 18.042 -0.853 40.700 1.00 13.45 A C ANISOU 4546 C GLY A 563 1651 1345 2114 -318 -91 174 A C ATOM 4547 O GLY A 563 17.344 -1.703 41.220 1.00 15.67 A O ANISOU 4547 O GLY A 563 1863 1678 2413 -356 81 384 A O ATOM 4548 N ILE A 564 18.087 0.405 41.150 1.00 13.40 A N ANISOU 4548 N ILE A 564 1503 1426 2161 -62 298 63 A N ATOM 4549 CA ILE A 564 17.279 0.835 42.276 1.00 13.17 A C ANISOU 4549 CA ILE A 564 1707 1474 1821 -4 65 204 A C ATOM 4550 C ILE A 564 15.793 0.653 41.938 1.00 14.20 A C ANISOU 4550 C ILE A 564 1796 1608 1990 -329 21 15 A C ATOM 4551 O ILE A 564 15.369 0.942 40.821 1.00 15.10 A O ANISOU 4551 O ILE A 564 2013 1683 2041 -112 35 233 A O ATOM 4552 CB ILE A 564 17.609 2.296 42.624 1.00 13.92 A C ANISOU 4552 CB ILE A 564 1792 1383 2114 16 16 206 A C ATOM 4553 CG1 ILE A 564 19.067 2.406 43.120 1.00 14.76 A C ANISOU 4553 CG1 ILE A 564 1435 1641 2531 47 344 313 A C ATOM 4554 CG2 ILE A 564 16.634 2.850 43.647 1.00 14.99 A C ANISOU 4554 CG2 ILE A 564 1838 1611 2244 69 125 269 A C ATOM 4555 CD1 ILE A 564 19.524 3.804 43.418 1.00 16.25 A C ANISOU 4555 CD1 ILE A 564 1551 2121 2500 1 44 -311 A C ATOM 4556 N VAL A 565 15.028 0.127 42.914 1.00 14.71 A N ANISOU 4556 N VAL A 565 1636 1648 2305 21 228 231 A N ATOM 4557 CA VAL A 565 13.599 -0.108 42.781 1.00 15.62 A C ANISOU 4557 CA VAL A 565 1704 1544 2687 -275 169 -22 A C ATOM 4558 C VAL A 565 12.884 1.056 43.482 1.00 15.77 A C ANISOU 4558 C VAL A 565 1883 1764 2342 -71 22 -39 A C ATOM 4559 O VAL A 565 13.055 1.263 44.657 1.00 15.83 A O ANISOU 4559 O VAL A 565 1798 1910 2303 -84 85 46 A O ATOM 4560 CB VAL A 565 13.192 -1.469 43.403 1.00 20.24 A C ANISOU 4560 CB VAL A 565 2270 1367 4053 -786 312 -252 A C ATOM 4561 CG1 VAL A 565 11.698 -1.729 43.334 1.00 22.73 A C ANISOU 4561 CG1 VAL A 565 2401 2090 4146 -585 109 -296 A C ATOM 4562 CG2 VAL A 565 13.923 -2.584 42.737 1.00 26.19 A C ANISOU 4562 CG2 VAL A 565 2229 2161 5561 -487 746 -326 A C ATOM 4563 N ARG A 566 12.034 1.770 42.745 1.00 14.88 A N ANISOU 4563 N ARG A 566 1628 1411 2612 -164 -66 -260 A N ATOM 4564 CA ARG A 566 11.528 3.047 43.197 1.00 13.96 A C ANISOU 4564 CA ARG A 566 1365 1505 2431 -127 150 -165 A C ATOM 4565 C ARG A 566 10.004 3.022 43.421 1.00 15.53 A C ANISOU 4565 C ARG A 566 1301 1846 2750 4 44 44 A C ATOM 4566 O ARG A 566 9.266 2.252 42.795 1.00 16.66 A O ANISOU 4566 O ARG A 566 1301 2051 2977 -135 26 -61 A O ATOM 4567 CB ARG A 566 11.826 4.158 42.213 1.00 15.18 A C ANISOU 4567 CB ARG A 566 1337 1896 2531 -140 355 35 A C ATOM 4568 CG ARG A 566 13.326 4.387 42.053 1.00 14.92 A C ANISOU 4568 CG ARG A 566 1302 1620 2745 148 320 174 A C ATOM 4569 CD ARG A 566 13.660 5.401 41.025 1.00 15.73 A C ANISOU 4569 CD ARG A 566 1461 1952 2561 32 479 255 A C ATOM 4570 NE ARG A 566 15.076 5.449 40.750 1.00 13.50 A N ANISOU 4570 NE ARG A 566 1422 1434 2272 147 416 11 A N ATOM 4571 CZ ARG A 566 15.887 6.475 41.008 1.00 14.06 A C ANISOU 4571 CZ ARG A 566 1430 1612 2297 173 159 -216 A C ATOM 4572 NH1 ARG A 566 15.464 7.524 41.706 1.00 13.45 A N ANISOU 4572 NH1 ARG A 566 1397 1577 2136 399 310 45 A N ATOM 4573 NH2 ARG A 566 17.125 6.438 40.554 1.00 13.62 A N ANISOU 4573 NH2 ARG A 566 1457 1526 2193 112 315 -2 A N ATOM 4574 N ASN A 567 9.572 3.901 44.325 1.00 15.12 A N ANISOU 4574 N ASN A 567 1240 1843 2661 -139 80 -45 A N ATOM 4575 CA ASN A 567 8.161 4.224 44.521 1.00 16.41 A C ANISOU 4575 CA ASN A 567 1329 1954 2951 0 280 135 A C ATOM 4576 C ASN A 567 7.721 5.253 43.459 1.00 18.22 A C ANISOU 4576 C ASN A 567 1636 2186 3100 337 158 78 A C ATOM 4577 O ASN A 567 8.499 5.634 42.554 1.00 17.55 A O ANISOU 4577 O ASN A 567 1522 2265 2880 116 -7 -35 A O ATOM 4578 CB ASN A 567 7.876 4.622 45.971 1.00 18.77 A C ANISOU 4578 CB ASN A 567 1652 2353 3125 196 170 -38 A C ATOM 4579 CG ASN A 567 8.300 6.027 46.349 1.00 17.25 A C ANISOU 4579 CG ASN A 567 1293 2425 2835 -68 195 112 A C ATOM 4580 ND2 ASN A 567 8.001 6.419 47.599 1.00 20.89 A N ANISOU 4580 ND2 ASN A 567 2343 2757 2837 -141 488 123 A N ATOM 4581 OD1 ASN A 567 8.906 6.724 45.532 1.00 17.67 A O ANISOU 4581 OD1 ASN A 567 1779 2199 2734 146 272 161 A O ATOM 4582 N ASP A 568 6.455 5.683 43.563 1.00 20.40 A N ANISOU 4582 N ASP A 568 1361 2500 3888 49 -8 252 A N ATOM 4583 CA ASP A 568 5.858 6.529 42.542 1.00 22.28 A C ANISOU 4583 CA ASP A 568 1925 2610 3929 219 -277 38 A C ATOM 4584 C ASP A 568 6.529 7.904 42.444 1.00 21.26 A C ANISOU 4584 C ASP A 568 2183 2607 3285 331 -108 147 A C ATOM 4585 O ASP A 568 6.378 8.537 41.432 1.00 27.61 A O ANISOU 4585 O ASP A 568 3914 2857 3719 -355 -836 548 A O ATOM 4586 CB ASP A 568 4.362 6.724 42.813 1.00 26.75 A C ANISOU 4586 CB ASP A 568 1682 3552 4926 45 -676 -88 A C ATOM 4587 CG ASP A 568 4.001 7.288 44.200 1.00 40.51 A C ANISOU 4587 CG ASP A 568 2478 6447 6466 29 1146 -598 A C ATOM 4588 OD1 ASP A 568 4.922 7.506 45.066 1.00 43.57 A O ANISOU 4588 OD1 ASP A 568 3091 5705 7756 -1147 522 -46 A O ATOM 4589 OD2 ASP A 568 2.787 7.518 44.434 1.00 60.80 A O ANISOU 4589 OD2 ASP A 568 2513 10669 9917 1350 599 1139 A O ATOM 4590 N VAL A 569 7.188 8.395 43.493 1.00 18.11 A N ANISOU 4590 N VAL A 569 1704 2093 3083 408 21 306 A N ATOM 4591 CA VAL A 569 7.836 9.728 43.428 1.00 19.35 A C ANISOU 4591 CA VAL A 569 1688 2254 3410 381 -17 83 A C ATOM 4592 C VAL A 569 9.358 9.593 43.258 1.00 17.37 A C ANISOU 4592 C VAL A 569 1578 2145 2876 109 -59 -173 A C ATOM 4593 O VAL A 569 10.060 10.560 43.310 1.00 20.75 A O ANISOU 4593 O VAL A 569 1611 2153 4119 202 174 107 A O ATOM 4594 CB VAL A 569 7.505 10.586 44.660 1.00 19.55 A C ANISOU 4594 CB VAL A 569 1661 2543 3222 407 94 -152 A C ATOM 4595 CG1 VAL A 569 6.012 10.873 44.759 1.00 23.03 A C ANISOU 4595 CG1 VAL A 569 1713 2917 4120 441 38 -239 A C ATOM 4596 CG2 VAL A 569 8.027 9.987 45.961 1.00 21.07 A C ANISOU 4596 CG2 VAL A 569 2348 2690 2964 383 207 -427 A C ATOM 4597 N GLY A 570 9.868 8.383 43.069 1.00 15.11 A N ANISOU 4597 N GLY A 570 1430 1944 2365 19 183 223 A N ATOM 4598 CA GLY A 570 11.272 8.190 42.725 1.00 15.51 A C ANISOU 4598 CA GLY A 570 1489 2144 2260 -160 234 94 A C ATOM 4599 C GLY A 570 12.196 7.818 43.882 1.00 13.30 A C ANISOU 4599 C GLY A 570 1672 1263 2116 104 357 -45 A C ATOM 4600 O GLY A 570 13.417 7.668 43.640 1.00 14.89 A O ANISOU 4600 O GLY A 570 1562 1747 2348 79 383 24 A O ATOM 4601 N LEU A 571 11.673 7.749 45.116 1.00 13.25 A N ANISOU 4601 N LEU A 571 1469 1699 1866 264 261 -131 A N ATOM 4602 CA LEU A 571 12.451 7.274 46.243 1.00 13.63 A C ANISOU 4602 CA LEU A 571 1387 1641 2148 47 187 -14 A C ATOM 4603 C LEU A 571 12.396 5.736 46.231 1.00 14.34 A C ANISOU 4603 C LEU A 571 1411 1743 2291 104 125 28 A C ATOM 4604 O LEU A 571 11.867 5.156 45.285 1.00 14.58 A O ANISOU 4604 O LEU A 571 1404 1844 2291 -97 34 37 A O ATOM 4605 CB LEU A 571 11.957 7.898 47.554 1.00 14.01 A C ANISOU 4605 CB LEU A 571 1820 1385 2116 -58 159 46 A C ATOM 4606 CG LEU A 571 12.129 9.421 47.659 1.00 14.19 A C ANISOU 4606 CG LEU A 571 2068 1329 1992 163 261 76 A C ATOM 4607 CD1 LEU A 571 11.492 9.935 48.950 1.00 15.83 A C ANISOU 4607 CD1 LEU A 571 2322 1479 2210 462 390 -105 A C ATOM 4608 CD2 LEU A 571 13.605 9.819 47.574 1.00 16.56 A C ANISOU 4608 CD2 LEU A 571 2107 1579 2604 -45 87 79 A C ATOM 4609 N TRP A 572 12.980 5.111 47.239 1.00 12.40 A N ANISOU 4609 N TRP A 572 1545 1114 2051 -155 172 -234 A N ATOM 4610 CA TRP A 572 12.965 3.674 47.303 1.00 12.82 A C ANISOU 4610 CA TRP A 572 1594 1062 2215 -22 239 -294 A C ATOM 4611 C TRP A 572 11.542 3.140 47.498 1.00 14.97 A C ANISOU 4611 C TRP A 572 1649 1643 2394 -115 144 161 A C ATOM 4612 O TRP A 572 10.766 3.640 48.283 1.00 16.84 A O ANISOU 4612 O TRP A 572 1708 1683 3008 -63 402 255 A O ATOM 4613 CB TRP A 572 13.860 3.165 48.421 1.00 12.66 A C ANISOU 4613 CB TRP A 572 1627 1245 1936 -140 310 -89 A C ATOM 4614 CG TRP A 572 15.304 2.969 48.070 1.00 12.92 A C ANISOU 4614 CG TRP A 572 1563 1301 2042 -72 305 37 A C ATOM 4615 CD1 TRP A 572 16.335 3.828 48.276 1.00 12.66 A C ANISOU 4615 CD1 TRP A 572 1480 1210 2119 60 119 121 A C ATOM 4616 CD2 TRP A 572 15.886 1.824 47.438 1.00 12.11 A C ANISOU 4616 CD2 TRP A 572 1347 1211 2043 54 29 58 A C ATOM 4617 CE2 TRP A 572 17.275 2.067 47.322 1.00 12.11 A C ANISOU 4617 CE2 TRP A 572 1425 1152 2022 111 113 115 A C ATOM 4618 CE3 TRP A 572 15.384 0.588 47.016 1.00 13.64 A C ANISOU 4618 CE3 TRP A 572 1532 1216 2432 -13 119 32 A C ATOM 4619 NE1 TRP A 572 17.507 3.322 47.825 1.00 12.77 A N ANISOU 4619 NE1 TRP A 572 1455 1322 2073 5 59 19 A N ATOM 4620 CZ2 TRP A 572 18.152 1.129 46.781 1.00 12.53 A C ANISOU 4620 CZ2 TRP A 572 1118 1394 2246 175 215 251 A C ATOM 4621 CZ3 TRP A 572 16.245 -0.325 46.454 1.00 13.20 A C ANISOU 4621 CZ3 TRP A 572 1490 1306 2216 -12 139 41 A C ATOM 4622 CH2 TRP A 572 17.614 -0.064 46.354 1.00 13.39 A C ANISOU 4622 CH2 TRP A 572 1495 1456 2137 70 197 283 A C ATOM 4623 N ASP A 573 11.283 2.014 46.837 1.00 15.49 A N ANISOU 4623 N ASP A 573 1591 1670 2622 -84 -25 49 A N ATOM 4624 CA ASP A 573 10.077 1.226 47.076 1.00 16.39 A C ANISOU 4624 CA ASP A 573 1639 2000 2586 -146 -160 444 A C ATOM 4625 C ASP A 573 10.108 0.725 48.529 1.00 16.02 A C ANISOU 4625 C ASP A 573 1799 1604 2684 -439 118 411 A C ATOM 4626 O ASP A 573 11.107 0.144 48.982 1.00 16.68 A O ANISOU 4626 O ASP A 573 1879 1687 2769 -110 166 353 A O ATOM 4627 CB ASP A 573 10.022 0.085 46.060 1.00 18.95 A C ANISOU 4627 CB ASP A 573 2517 1929 2753 -657 -141 443 A C ATOM 4628 CG ASP A 573 8.894 -0.912 46.223 1.00 23.71 A C ANISOU 4628 CG ASP A 573 2801 2755 3452 -1234 -237 240 A C ATOM 4629 OD1 ASP A 573 8.542 -1.247 47.360 1.00 25.27 A O ANISOU 4629 OD1 ASP A 573 3278 3062 3260 -1130 -113 -80 A O ATOM 4630 OD2 ASP A 573 8.438 -1.362 45.187 1.00 31.04 A O ANISOU 4630 OD2 ASP A 573 4475 3257 4059 -1836 -1039 404 A O ATOM 4631 N ARG A 574 9.040 1.021 49.275 1.00 18.67 A N ANISOU 4631 N ARG A 574 2010 1882 3202 -171 373 331 A N ATOM 4632 CA ARG A 574 9.019 0.772 50.721 1.00 18.97 A C ANISOU 4632 CA ARG A 574 1906 2224 3076 -155 339 394 A C ATOM 4633 C ARG A 574 8.652 -0.687 51.054 1.00 20.97 A C ANISOU 4633 C ARG A 574 2089 2268 3608 -115 495 177 A C ATOM 4634 O ARG A 574 8.415 -0.980 52.230 1.00 23.77 A O ANISOU 4634 O ARG A 574 2559 2719 3751 -519 579 863 A O ATOM 4635 CB ARG A 574 8.123 1.786 51.441 1.00 23.06 A C ANISOU 4635 CB ARG A 574 2368 2765 3628 -378 1250 364 A C ATOM 4636 CG ARG A 574 8.745 3.174 51.593 1.00 24.70 A C ANISOU 4636 CG ARG A 574 3211 2334 3838 -138 1077 498 A C ATOM 4637 CD ARG A 574 8.517 4.078 50.428 1.00 26.35 A C ANISOU 4637 CD ARG A 574 2950 3011 4049 281 1230 325 A C ATOM 4638 NE ARG A 574 8.781 5.442 50.878 1.00 26.16 A N ANISOU 4638 NE ARG A 574 2238 3259 4442 -162 1081 -563 A N ATOM 4639 CZ ARG A 574 9.962 6.064 50.836 1.00 22.98 A C ANISOU 4639 CZ ARG A 574 2715 2509 3504 -333 866 53 A C ATOM 4640 NH1 ARG A 574 11.026 5.447 50.347 1.00 18.16 A N ANISOU 4640 NH1 ARG A 574 2246 2086 2567 -459 318 222 A N ATOM 4641 NH2 ARG A 574 10.057 7.320 51.287 1.00 23.57 A N ANISOU 4641 NH2 ARG A 574 2964 2480 3510 -528 682 -455 A N ATOM 4642 N SER A 575 8.595 -1.579 50.053 1.00 18.19 A N ANISOU 4642 N SER A 575 1759 2050 3100 -136 468 568 A N ATOM 4643 CA SER A 575 8.402 -3.003 50.321 1.00 19.90 A C ANISOU 4643 CA SER A 575 2254 1857 3448 -190 578 262 A C ATOM 4644 C SER A 575 9.709 -3.784 50.152 1.00 19.90 A C ANISOU 4644 C SER A 575 2128 1402 4032 -433 340 241 A C ATOM 4645 O SER A 575 9.704 -5.019 50.248 1.00 23.05 A O ANISOU 4645 O SER A 575 2701 1438 4618 -318 486 369 A O ATOM 4646 CB SER A 575 7.328 -3.537 49.439 1.00 23.79 A C ANISOU 4646 CB SER A 575 2995 2050 3990 -762 38 781 A C ATOM 4647 OG SER A 575 7.738 -3.638 48.071 1.00 26.75 A O ANISOU 4647 OG SER A 575 3085 3355 3721 -806 -360 -105 A O ATOM 4648 N THR A 576 10.823 -3.099 49.900 1.00 16.86 A N ANISOU 4648 N THR A 576 1830 1644 2930 -248 157 278 A N ATOM 4649 CA THR A 576 12.076 -3.782 49.650 1.00 15.75 A C ANISOU 4649 CA THR A 576 1914 1749 2320 -227 221 25 A C ATOM 4650 C THR A 576 12.828 -4.142 50.939 1.00 15.60 A C ANISOU 4650 C THR A 576 1999 1424 2501 -253 239 241 A C ATOM 4651 O THR A 576 12.873 -3.418 51.895 1.00 16.74 A O ANISOU 4651 O THR A 576 2135 1519 2706 -148 223 -34 A O ATOM 4652 CB THR A 576 13.010 -2.924 48.799 1.00 15.43 A C ANISOU 4652 CB THR A 576 1886 1783 2192 -146 288 0 A C ATOM 4653 CG2 THR A 576 12.533 -2.819 47.367 1.00 18.61 A C ANISOU 4653 CG2 THR A 576 2914 1979 2175 -179 85 -146 A C ATOM 4654 OG1 THR A 576 13.166 -1.606 49.334 1.00 15.64 A O ANISOU 4654 OG1 THR A 576 1731 1653 2558 -125 237 0 A O ATOM 4655 N PHE A 577 13.438 -5.335 50.932 1.00 15.05 A N ANISOU 4655 N PHE A 577 2016 1215 2487 -280 283 232 A N ATOM 4656 CA PHE A 577 14.437 -5.682 51.907 1.00 15.04 A C ANISOU 4656 CA PHE A 577 2464 700 2550 -357 126 68 A C ATOM 4657 C PHE A 577 15.546 -4.622 51.899 1.00 13.31 A C ANISOU 4657 C PHE A 577 1790 1069 2196 -46 203 -10 A C ATOM 4658 O PHE A 577 16.032 -4.233 50.802 1.00 13.11 A O ANISOU 4658 O PHE A 577 1816 1047 2115 -21 312 37 A O ATOM 4659 CB PHE A 577 14.996 -7.077 51.601 1.00 14.15 A C ANISOU 4659 CB PHE A 577 2022 777 2577 -357 284 150 A C ATOM 4660 CG PHE A 577 16.162 -7.400 52.494 1.00 14.67 A C ANISOU 4660 CG PHE A 577 2169 998 2404 -197 130 -74 A C ATOM 4661 CD1 PHE A 577 15.962 -7.748 53.818 1.00 17.40 A C ANISOU 4661 CD1 PHE A 577 2320 1801 2490 7 285 283 A C ATOM 4662 CD2 PHE A 577 17.455 -7.200 52.063 1.00 14.78 A C ANISOU 4662 CD2 PHE A 577 2240 1318 2057 -183 250 355 A C ATOM 4663 CE1 PHE A 577 17.033 -7.964 54.668 1.00 18.37 A C ANISOU 4663 CE1 PHE A 577 2382 2067 2529 81 258 472 A C ATOM 4664 CE2 PHE A 577 18.527 -7.405 52.915 1.00 16.28 A C ANISOU 4664 CE2 PHE A 577 2065 1758 2362 114 240 450 A C ATOM 4665 CZ PHE A 577 18.322 -7.770 54.220 1.00 17.56 A C ANISOU 4665 CZ PHE A 577 2202 2073 2394 150 26 505 A C ATOM 4666 N GLN A 578 16.031 -4.283 53.095 1.00 13.07 A N ANISOU 4666 N GLN A 578 1753 1281 1931 -120 305 186 A N ATOM 4667 CA GLN A 578 17.162 -3.389 53.219 1.00 12.61 A C ANISOU 4667 CA GLN A 578 1752 1132 1906 -126 299 -216 A C ATOM 4668 C GLN A 578 18.057 -3.802 54.406 1.00 13.16 A C ANISOU 4668 C GLN A 578 1653 1321 2027 -113 169 -177 A C ATOM 4669 O GLN A 578 17.548 -4.182 55.478 1.00 17.65 A O ANISOU 4669 O GLN A 578 2360 1996 2351 -28 407 187 A O ATOM 4670 CB GLN A 578 16.741 -1.931 53.394 1.00 12.99 A C ANISOU 4670 CB GLN A 578 1951 1120 1863 -94 451 -149 A C ATOM 4671 CG GLN A 578 15.970 -1.351 52.224 1.00 13.17 A C ANISOU 4671 CG GLN A 578 1754 1259 1990 -213 325 -132 A C ATOM 4672 CD GLN A 578 16.786 -1.186 50.959 1.00 11.44 A C ANISOU 4672 CD GLN A 578 1657 708 1980 -286 236 -231 A C ATOM 4673 NE2 GLN A 578 16.071 -1.028 49.839 1.00 13.32 A N ANISOU 4673 NE2 GLN A 578 1751 1236 2073 43 218 78 A N ATOM 4674 OE1 GLN A 578 18.027 -1.138 50.999 1.00 12.82 A O ANISOU 4674 OE1 GLN A 578 1551 1228 2091 -216 194 103 A O ATOM 4675 N TRP A 579 19.385 -3.783 54.190 1.00 12.99 A N ANISOU 4675 N TRP A 579 1764 1363 1807 23 384 -33 A N ATOM 4676 CA TRP A 579 20.375 -3.879 55.261 1.00 13.00 A C ANISOU 4676 CA TRP A 579 1684 1189 2064 -28 199 104 A C ATOM 4677 C TRP A 579 20.410 -2.595 56.103 1.00 14.08 A C ANISOU 4677 C TRP A 579 2097 1230 2024 102 109 139 A C ATOM 4678 O TRP A 579 20.396 -2.628 57.364 1.00 14.97 A O ANISOU 4678 O TRP A 579 2488 1243 1955 -20 430 -132 A O ATOM 4679 CB TRP A 579 21.782 -4.139 54.687 1.00 14.08 A C ANISOU 4679 CB TRP A 579 1706 1338 2302 63 226 95 A C ATOM 4680 CG TRP A 579 21.908 -5.356 53.816 1.00 14.23 A C ANISOU 4680 CG TRP A 579 1934 1390 2082 -150 237 79 A C ATOM 4681 CD1 TRP A 579 22.038 -5.404 52.452 1.00 14.02 A C ANISOU 4681 CD1 TRP A 579 1613 1478 2236 -36 304 -78 A C ATOM 4682 CD2 TRP A 579 21.883 -6.721 54.263 1.00 13.91 A C ANISOU 4682 CD2 TRP A 579 1808 1384 2089 -114 258 -30 A C ATOM 4683 CE2 TRP A 579 22.019 -7.519 53.117 1.00 14.31 A C ANISOU 4683 CE2 TRP A 579 1780 1416 2241 99 82 -78 A C ATOM 4684 CE3 TRP A 579 21.787 -7.329 55.512 1.00 16.82 A C ANISOU 4684 CE3 TRP A 579 2665 1240 2483 33 45 339 A C ATOM 4685 NE1 TRP A 579 22.068 -6.709 52.033 1.00 14.53 A N ANISOU 4685 NE1 TRP A 579 1720 1729 2069 -80 548 -180 A N ATOM 4686 CZ2 TRP A 579 22.056 -8.910 53.192 1.00 16.15 A C ANISOU 4686 CZ2 TRP A 579 2317 1333 2485 247 432 -314 A C ATOM 4687 CZ3 TRP A 579 21.814 -8.703 55.585 1.00 17.93 A C ANISOU 4687 CZ3 TRP A 579 3039 1301 2472 371 194 231 A C ATOM 4688 CH2 TRP A 579 21.959 -9.475 54.439 1.00 19.03 A C ANISOU 4688 CH2 TRP A 579 3047 1492 2690 335 333 -24 A C ATOM 4689 N ALA A 580 20.450 -1.460 55.392 1.00 13.47 A N ANISOU 4689 N ALA A 580 2135 1178 1805 116 205 68 A N ATOM 4690 CA ALA A 580 20.428 -0.086 55.977 1.00 14.69 A C ANISOU 4690 CA ALA A 580 2116 1295 2168 281 248 -150 A C ATOM 4691 C ALA A 580 21.446 0.004 57.121 1.00 12.63 A C ANISOU 4691 C ALA A 580 1935 948 1914 75 398 -97 A C ATOM 4692 O ALA A 580 22.617 -0.328 56.918 1.00 13.20 A O ANISOU 4692 O ALA A 580 1752 1333 1928 132 116 93 A O ATOM 4693 CB ALA A 580 19.020 0.315 56.349 1.00 14.85 A C ANISOU 4693 CB ALA A 580 2020 1277 2345 221 257 91 A C ATOM 4694 N ASP A 581 21.062 0.570 58.286 1.00 12.91 A N ANISOU 4694 N ASP A 581 1837 1192 1876 191 380 -117 A N ATOM 4695 CA ASP A 581 22.048 0.823 59.343 1.00 12.73 A C ANISOU 4695 CA ASP A 581 2076 1098 1661 -23 341 34 A C ATOM 4696 C ASP A 581 22.318 -0.435 60.165 1.00 13.94 A C ANISOU 4696 C ASP A 581 2087 1303 1903 156 441 168 A C ATOM 4697 O ASP A 581 22.098 -0.476 61.381 1.00 15.68 A O ANISOU 4697 O ASP A 581 2803 1297 1854 99 250 111 A O ATOM 4698 CB ASP A 581 21.666 2.021 60.220 1.00 13.31 A C ANISOU 4698 CB ASP A 581 2022 1158 1877 107 285 -12 A C ATOM 4699 CG ASP A 581 22.864 2.617 60.962 1.00 13.28 A C ANISOU 4699 CG ASP A 581 2038 1196 1810 65 250 17 A C ATOM 4700 OD1 ASP A 581 24.025 2.511 60.458 1.00 13.70 A O ANISOU 4700 OD1 ASP A 581 1939 1295 1972 -35 157 -161 A O ATOM 4701 OD2 ASP A 581 22.637 3.192 62.065 1.00 14.82 A O ANISOU 4701 OD2 ASP A 581 2644 1141 1843 73 351 -1 A O ATOM 4702 N TRP A 582 22.931 -1.406 59.487 1.00 13.28 A N ANISOU 4702 N TRP A 582 2187 1317 1540 158 237 91 A N ATOM 4703 CA TRP A 582 23.279 -2.713 60.014 1.00 12.55 A C ANISOU 4703 CA TRP A 582 1916 1177 1673 -82 197 114 A C ATOM 4704 C TRP A 582 24.171 -2.575 61.252 1.00 13.81 A C ANISOU 4704 C TRP A 582 1874 1384 1987 134 65 107 A C ATOM 4705 O TRP A 582 25.119 -1.824 61.235 1.00 13.85 A O ANISOU 4705 O TRP A 582 2159 1129 1973 11 8 -77 A O ATOM 4706 CB TRP A 582 23.987 -3.450 58.870 1.00 12.69 A C ANISOU 4706 CB TRP A 582 1831 1299 1690 -36 118 19 A C ATOM 4707 CG TRP A 582 24.354 -4.882 59.111 1.00 13.70 A C ANISOU 4707 CG TRP A 582 1880 1351 1973 48 102 -145 A C ATOM 4708 CD1 TRP A 582 25.622 -5.366 59.331 1.00 12.54 A C ANISOU 4708 CD1 TRP A 582 2107 905 1752 280 9 -26 A C ATOM 4709 CD2 TRP A 582 23.468 -6.009 59.136 1.00 14.18 A C ANISOU 4709 CD2 TRP A 582 1846 1620 1922 -81 170 -50 A C ATOM 4710 CE2 TRP A 582 24.273 -7.143 59.360 1.00 15.48 A C ANISOU 4710 CE2 TRP A 582 2188 1572 2121 34 93 -180 A C ATOM 4711 CE3 TRP A 582 22.085 -6.172 58.950 1.00 14.71 A C ANISOU 4711 CE3 TRP A 582 1962 1501 2126 -80 -164 -329 A C ATOM 4712 NE1 TRP A 582 25.568 -6.728 59.482 1.00 13.59 A N ANISOU 4712 NE1 TRP A 582 2092 919 2152 455 -40 -61 A N ATOM 4713 CZ2 TRP A 582 23.737 -8.434 59.399 1.00 15.79 A C ANISOU 4713 CZ2 TRP A 582 2420 1513 2065 146 208 -127 A C ATOM 4714 CZ3 TRP A 582 21.556 -7.449 59.040 1.00 16.56 A C ANISOU 4714 CZ3 TRP A 582 2237 1796 2256 -214 117 -107 A C ATOM 4715 CH2 TRP A 582 22.378 -8.555 59.241 1.00 18.19 A C ANISOU 4715 CH2 TRP A 582 2539 1894 2478 -30 405 -177 A C ATOM 4716 N LEU A 583 23.871 -3.345 62.313 1.00 14.41 A N ANISOU 4716 N LEU A 583 2578 1148 1748 134 65 -190 A N ATOM 4717 CA LEU A 583 24.720 -3.465 63.495 1.00 14.42 A C ANISOU 4717 CA LEU A 583 2156 1443 1878 -132 31 46 A C ATOM 4718 C LEU A 583 24.770 -2.146 64.278 1.00 14.59 A C ANISOU 4718 C LEU A 583 2159 1360 2022 -74 100 147 A C ATOM 4719 O LEU A 583 25.702 -1.909 65.013 1.00 15.08 A O ANISOU 4719 O LEU A 583 2432 1346 1950 -51 178 -238 A O ATOM 4720 CB LEU A 583 26.113 -4.005 63.110 1.00 14.28 A C ANISOU 4720 CB LEU A 583 2304 1250 1869 -55 -114 -111 A C ATOM 4721 CG LEU A 583 26.177 -5.519 62.935 1.00 14.79 A C ANISOU 4721 CG LEU A 583 2392 1295 1929 -44 58 -173 A C ATOM 4722 CD1 LEU A 583 27.538 -5.953 62.405 1.00 15.03 A C ANISOU 4722 CD1 LEU A 583 2396 1395 1920 -193 118 82 A C ATOM 4723 CD2 LEU A 583 25.829 -6.230 64.230 1.00 16.50 A C ANISOU 4723 CD2 LEU A 583 2633 1805 1828 302 153 -63 A C ATOM 4724 N ASP A 584 23.680 -1.371 64.199 1.00 15.30 A N ANISOU 4724 N ASP A 584 2543 1468 1800 292 11 -214 A N ATOM 4725 CA ASP A 584 23.370 -0.342 65.204 1.00 14.97 A C ANISOU 4725 CA ASP A 584 2669 1280 1737 -63 8 -213 A C ATOM 4726 C ASP A 584 23.612 -1.006 66.553 1.00 17.09 A C ANISOU 4726 C ASP A 584 2648 1703 2139 -78 -40 272 A C ATOM 4727 O ASP A 584 23.146 -2.126 66.747 1.00 15.85 A O ANISOU 4727 O ASP A 584 2529 1629 1861 -122 402 -238 A O ATOM 4728 CB ASP A 584 21.915 0.122 65.008 1.00 16.26 A C ANISOU 4728 CB ASP A 584 2541 1538 2096 -84 239 -347 A C ATOM 4729 CG ASP A 584 21.326 1.095 66.010 1.00 16.12 A C ANISOU 4729 CG ASP A 584 2317 1711 2094 220 182 -169 A C ATOM 4730 OD1 ASP A 584 21.802 1.118 67.176 1.00 16.62 A O ANISOU 4730 OD1 ASP A 584 2804 1385 2124 157 194 -85 A O ATOM 4731 OD2 ASP A 584 20.382 1.799 65.604 1.00 16.20 A O ANISOU 4731 OD2 ASP A 584 2316 1738 2101 123 154 -4 A O ATOM 4732 N PRO A 585 24.343 -0.406 67.508 1.00 15.07 A N ANISOU 4732 N PRO A 585 2548 1412 1766 4 447 -13 A N ATOM 4733 CA PRO A 585 24.611 -1.076 68.785 1.00 15.83 A C ANISOU 4733 CA PRO A 585 2537 1948 1527 152 152 -305 A C ATOM 4734 C PRO A 585 23.359 -1.426 69.611 1.00 16.43 A C ANISOU 4734 C PRO A 585 2647 2062 1532 -52 115 -108 A C ATOM 4735 O PRO A 585 23.429 -2.288 70.505 1.00 18.23 A O ANISOU 4735 O PRO A 585 2976 1908 2039 7 427 206 A O ATOM 4736 CB PRO A 585 25.488 -0.079 69.542 1.00 16.27 A C ANISOU 4736 CB PRO A 585 2320 1991 1868 124 -54 -105 A C ATOM 4737 CG PRO A 585 25.198 1.238 68.908 1.00 16.62 A C ANISOU 4737 CG PRO A 585 2243 1912 2157 181 170 -57 A C ATOM 4738 CD PRO A 585 24.930 0.939 67.446 1.00 15.12 A C ANISOU 4738 CD PRO A 585 2463 1234 2047 140 610 -148 A C ATOM 4739 N LYS A 586 22.219 -0.801 69.326 1.00 16.83 A N ANISOU 4739 N LYS A 586 2898 1710 1784 0 109 -72 A N ATOM 4740 CA LYS A 586 20.967 -1.085 69.999 1.00 19.13 A C ANISOU 4740 CA LYS A 586 2773 2163 2332 148 407 -537 A C ATOM 4741 C LYS A 586 20.176 -2.218 69.315 1.00 18.43 A C ANISOU 4741 C LYS A 586 2410 2315 2275 53 375 -295 A C ATOM 4742 O LYS A 586 19.182 -2.673 69.886 1.00 20.76 A O ANISOU 4742 O LYS A 586 2356 2773 2756 -22 738 -747 A O ATOM 4743 CB LYS A 586 20.094 0.171 70.061 1.00 19.85 A C ANISOU 4743 CB LYS A 586 2727 2427 2388 273 354 -103 A C ATOM 4744 CG LYS A 586 20.659 1.352 70.825 1.00 28.24 A C ANISOU 4744 CG LYS A 586 3964 3272 3494 -579 555 -469 A C ATOM 4745 CD LYS A 586 20.665 1.223 72.284 1.00 36.42 A C ANISOU 4745 CD LYS A 586 5770 4374 3692 -776 343 -722 A C ATOM 4746 CE LYS A 586 20.871 2.578 72.941 1.00 37.82 A C ANISOU 4746 CE LYS A 586 5850 5207 3310 -1174 1158 -1430 A C ATOM 4747 NZ LYS A 586 21.487 2.426 74.276 1.00 49.71 A N ANISOU 4747 NZ LYS A 586 6514 7470 4902 -321 -367 -980 A N ATOM 4748 N ALA A 587 20.599 -2.672 68.126 1.00 17.33 A N ANISOU 4748 N ALA A 587 2539 1943 2101 -66 275 -179 A N ATOM 4749 CA ALA A 587 19.905 -3.800 67.493 1.00 18.28 A C ANISOU 4749 CA ALA A 587 2666 1731 2548 -54 345 -89 A C ATOM 4750 C ALA A 587 20.109 -5.059 68.343 1.00 17.91 A C ANISOU 4750 C ALA A 587 2661 2057 2086 -54 299 -19 A C ATOM 4751 O ALA A 587 21.188 -5.264 68.920 1.00 18.73 A O ANISOU 4751 O ALA A 587 2800 2012 2302 -266 224 53 A O ATOM 4752 CB ALA A 587 20.395 -4.013 66.088 1.00 19.85 A C ANISOU 4752 CB ALA A 587 2696 2312 2532 -43 205 -191 A C ATOM 4753 N PRO A 588 19.095 -5.946 68.432 1.00 18.24 A N ANISOU 4753 N PRO A 588 2624 1967 2336 -70 308 -131 A N ATOM 4754 CA PRO A 588 19.261 -7.217 69.136 1.00 19.44 A C ANISOU 4754 CA PRO A 588 2930 2093 2361 155 416 -34 A C ATOM 4755 C PRO A 588 20.374 -8.048 68.484 1.00 19.94 A C ANISOU 4755 C PRO A 588 2775 2399 2402 318 234 179 A C ATOM 4756 O PRO A 588 20.525 -7.982 67.257 1.00 18.03 A O ANISOU 4756 O PRO A 588 3008 1541 2300 -119 179 76 A O ATOM 4757 CB PRO A 588 17.905 -7.923 68.973 1.00 20.95 A C ANISOU 4757 CB PRO A 588 2942 2359 2659 12 354 -371 A C ATOM 4758 CG PRO A 588 16.935 -6.846 68.600 1.00 24.10 A C ANISOU 4758 CG PRO A 588 2977 2448 3730 -559 -211 98 A C ATOM 4759 CD PRO A 588 17.758 -5.838 67.816 1.00 20.35 A C ANISOU 4759 CD PRO A 588 2864 2111 2754 -160 70 -150 A C ATOM 4760 N ALA A 589 21.129 -8.821 69.286 1.00 17.62 A N ANISOU 4760 N ALA A 589 2541 2286 1864 270 359 169 A N ATOM 4761 CA ALA A 589 22.253 -9.644 68.722 1.00 18.58 A C ANISOU 4761 CA ALA A 589 2397 2038 2621 36 291 -152 A C ATOM 4762 C ALA A 589 21.784 -10.581 67.591 1.00 19.47 A C ANISOU 4762 C ALA A 589 2561 2239 2595 -33 328 -42 A C ATOM 4763 O ALA A 589 22.526 -10.755 66.593 1.00 19.15 A O ANISOU 4763 O ALA A 589 2642 1991 2644 -111 383 -264 A O ATOM 4764 CB ALA A 589 22.938 -10.412 69.819 1.00 21.74 A C ANISOU 4764 CB ALA A 589 3629 2137 2493 23 178 -16 A C ATOM 4765 N ASP A 590 20.554 -11.123 67.684 1.00 18.38 A N ANISOU 4765 N ASP A 590 2265 2310 2407 24 395 55 A N ATOM 4766 CA ASP A 590 20.050 -12.059 66.688 1.00 19.50 A C ANISOU 4766 CA ASP A 590 2379 2278 2749 38 290 -19 A C ATOM 4767 C ASP A 590 19.479 -11.385 65.436 1.00 20.18 A C ANISOU 4767 C ASP A 590 2836 2010 2820 338 -38 -124 A C ATOM 4768 O ASP A 590 19.252 -12.078 64.430 1.00 21.53 A O ANISOU 4768 O ASP A 590 3082 2155 2941 -154 -133 -52 A O ATOM 4769 CB ASP A 590 18.911 -12.917 67.230 1.00 23.99 A C ANISOU 4769 CB ASP A 590 3077 2204 3831 -793 -157 369 A C ATOM 4770 CG ASP A 590 19.345 -13.842 68.314 1.00 30.97 A C ANISOU 4770 CG ASP A 590 4033 4041 3692 -672 245 779 A C ATOM 4771 OD1 ASP A 590 20.587 -14.153 68.356 1.00 36.16 A O ANISOU 4771 OD1 ASP A 590 4374 4331 5033 -394 1427 110 A O ATOM 4772 OD2 ASP A 590 18.439 -14.227 69.109 1.00 36.07 A O ANISOU 4772 OD2 ASP A 590 5320 3644 4740 -1447 1521 20 A O ATOM 4773 N ASP A 591 19.298 -10.051 65.451 1.00 17.91 A N ANISOU 4773 N ASP A 591 2324 1892 2589 59 167 -26 A N ATOM 4774 CA ASP A 591 18.614 -9.347 64.342 1.00 18.39 A C ANISOU 4774 CA ASP A 591 2718 1752 2516 -269 6 -183 A C ATOM 4775 C ASP A 591 19.355 -8.043 64.095 1.00 16.05 A C ANISOU 4775 C ASP A 591 2084 1585 2426 122 118 -28 A C ATOM 4776 O ASP A 591 18.871 -6.948 64.429 1.00 17.51 A O ANISOU 4776 O ASP A 591 2602 1671 2380 123 284 -244 A O ATOM 4777 CB ASP A 591 17.146 -9.107 64.714 1.00 20.18 A C ANISOU 4777 CB ASP A 591 2482 1658 3528 -622 125 314 A C ATOM 4778 CG ASP A 591 16.201 -8.729 63.572 1.00 23.72 A C ANISOU 4778 CG ASP A 591 3158 2250 3604 -886 -231 -149 A C ATOM 4779 OD1 ASP A 591 16.640 -8.709 62.373 1.00 29.85 A O ANISOU 4779 OD1 ASP A 591 5055 3150 3134 99 -153 58 A O ATOM 4780 OD2 ASP A 591 15.025 -8.421 63.898 1.00 27.00 A O ANISOU 4780 OD2 ASP A 591 3304 2923 4030 -159 -337 463 A O ATOM 4781 N PRO A 592 20.573 -8.116 63.520 1.00 16.31 A N ANISOU 4781 N PRO A 592 2199 1654 2343 320 142 -406 A N ATOM 4782 CA PRO A 592 21.399 -6.930 63.336 1.00 17.86 A C ANISOU 4782 CA PRO A 592 2630 2113 2039 -85 137 -299 A C ATOM 4783 C PRO A 592 20.787 -5.835 62.464 1.00 15.58 A C ANISOU 4783 C PRO A 592 2021 1996 1899 74 331 -544 A C ATOM 4784 O PRO A 592 21.276 -4.702 62.556 1.00 18.04 A O ANISOU 4784 O PRO A 592 2518 2009 2326 -181 391 -274 A O ATOM 4785 CB PRO A 592 22.701 -7.452 62.725 1.00 18.39 A C ANISOU 4785 CB PRO A 592 2487 1933 2565 269 -90 -47 A C ATOM 4786 CG PRO A 592 22.714 -8.918 63.105 1.00 19.56 A C ANISOU 4786 CG PRO A 592 2692 2132 2604 365 121 191 A C ATOM 4787 CD PRO A 592 21.267 -9.349 63.103 1.00 17.32 A C ANISOU 4787 CD PRO A 592 2463 1647 2468 592 -118 -199 A C ATOM 4788 N GLY A 593 19.759 -6.146 61.669 1.00 15.93 A N ANISOU 4788 N GLY A 593 2439 1746 1867 253 100 -289 A N ATOM 4789 CA GLY A 593 19.091 -5.134 60.852 1.00 16.46 A C ANISOU 4789 CA GLY A 593 1924 2069 2259 364 167 -55 A C ATOM 4790 C GLY A 593 17.992 -4.370 61.577 1.00 16.14 A C ANISOU 4790 C GLY A 593 2124 1844 2161 326 335 52 A C ATOM 4791 O GLY A 593 17.440 -3.390 61.038 1.00 17.60 A O ANISOU 4791 O GLY A 593 2597 1466 2623 7 222 182 A O ATOM 4792 N ASP A 594 17.693 -4.725 62.821 1.00 16.67 A N ANISOU 4792 N ASP A 594 2317 1482 2533 -96 439 129 A N ATOM 4793 CA ASP A 594 16.565 -4.094 63.566 1.00 16.56 A C ANISOU 4793 CA ASP A 594 2099 1895 2296 -140 452 66 A C ATOM 4794 C ASP A 594 17.085 -2.824 64.248 1.00 17.11 A C ANISOU 4794 C ASP A 594 2376 1836 2287 256 330 86 A C ATOM 4795 O ASP A 594 17.293 -2.785 65.425 1.00 18.31 A O ANISOU 4795 O ASP A 594 2853 2041 2063 -313 641 -194 A O ATOM 4796 CB ASP A 594 15.935 -5.112 64.502 1.00 19.26 A C ANISOU 4796 CB ASP A 594 2360 2308 2649 -138 694 349 A C ATOM 4797 CG ASP A 594 14.745 -4.591 65.301 1.00 23.02 A C ANISOU 4797 CG ASP A 594 2316 2798 3633 49 1127 456 A C ATOM 4798 OD1 ASP A 594 14.106 -3.618 64.894 1.00 27.31 A O ANISOU 4798 OD1 ASP A 594 2908 3273 4195 411 972 834 A O ATOM 4799 OD2 ASP A 594 14.444 -5.185 66.350 1.00 29.34 A O ANISOU 4799 OD2 ASP A 594 3952 3540 3656 -352 1218 688 A O ATOM 4800 N ALA A 595 17.298 -1.790 63.429 1.00 17.80 A N ANISOU 4800 N ALA A 595 2750 1696 2315 -248 93 81 A N ATOM 4801 CA ALA A 595 17.969 -0.560 63.837 1.00 16.95 A C ANISOU 4801 CA ALA A 595 2574 1605 2259 -72 263 -212 A C ATOM 4802 C ALA A 595 16.967 0.431 64.413 1.00 16.67 A C ANISOU 4802 C ALA A 595 2411 1431 2489 -242 605 198 A C ATOM 4803 O ALA A 595 15.741 0.347 64.209 1.00 18.20 A O ANISOU 4803 O ALA A 595 2583 1718 2614 -382 447 -121 A O ATOM 4804 CB ALA A 595 18.703 0.059 62.678 1.00 20.03 A C ANISOU 4804 CB ALA A 595 2815 1941 2851 -112 660 -106 A C ATOM 4805 N THR A 596 17.548 1.454 65.048 1.00 17.08 A N ANISOU 4805 N THR A 596 2163 1763 2561 -105 482 -121 A N ATOM 4806 CA THR A 596 16.763 2.562 65.614 1.00 17.21 A C ANISOU 4806 CA THR A 596 2396 1888 2252 250 627 91 A C ATOM 4807 C THR A 596 16.407 3.626 64.565 1.00 17.78 A C ANISOU 4807 C THR A 596 2584 1906 2263 129 595 -18 A C ATOM 4808 O THR A 596 15.654 4.568 64.866 1.00 18.59 A O ANISOU 4808 O THR A 596 2705 1942 2415 265 983 85 A O ATOM 4809 CB THR A 596 17.468 3.217 66.812 1.00 19.34 A C ANISOU 4809 CB THR A 596 2730 2419 2198 141 366 42 A C ATOM 4810 CG2 THR A 596 17.718 2.251 67.955 1.00 20.46 A C ANISOU 4810 CG2 THR A 596 3102 2209 2461 146 671 246 A C ATOM 4811 OG1 THR A 596 18.697 3.784 66.355 1.00 18.42 A O ANISOU 4811 OG1 THR A 596 2869 1731 2397 102 333 -313 A O ATOM 4812 N THR A 597 16.978 3.524 63.376 1.00 16.31 A N ANISOU 4812 N THR A 597 2336 1577 2283 250 537 -188 A N ATOM 4813 CA THR A 597 16.694 4.435 62.273 1.00 16.16 A C ANISOU 4813 CA THR A 597 2369 1585 2183 151 474 -178 A C ATOM 4814 C THR A 597 15.942 3.682 61.174 1.00 14.55 A C ANISOU 4814 C THR A 597 2115 1393 2020 111 518 -32 A C ATOM 4815 O THR A 597 16.353 2.584 60.795 1.00 15.36 A O ANISOU 4815 O THR A 597 2490 1165 2178 153 347 -28 A O ATOM 4816 CB THR A 597 17.989 5.019 61.679 1.00 17.49 A C ANISOU 4816 CB THR A 597 2246 2085 2313 -65 115 187 A C ATOM 4817 CG2 THR A 597 17.717 6.144 60.702 1.00 15.97 A C ANISOU 4817 CG2 THR A 597 2059 1641 2366 141 229 -58 A C ATOM 4818 OG1 THR A 597 18.804 5.515 62.747 1.00 15.36 A O ANISOU 4818 OG1 THR A 597 2172 1526 2137 -25 348 31 A O ATOM 4819 N ASN A 598 14.861 4.258 60.672 1.00 15.51 A N ANISOU 4819 N ASN A 598 2049 1841 2001 20 461 3 A N ATOM 4820 CA ASN A 598 14.032 3.663 59.625 1.00 14.74 A C ANISOU 4820 CA ASN A 598 1937 1712 1948 0 471 140 A C ATOM 4821 C ASN A 598 14.896 3.291 58.405 1.00 13.54 A C ANISOU 4821 C ASN A 598 1858 1608 1677 29 147 -162 A C ATOM 4822 O ASN A 598 15.710 4.092 57.912 1.00 14.05 A O ANISOU 4822 O ASN A 598 2032 1278 2028 66 365 -185 A O ATOM 4823 CB ASN A 598 12.883 4.591 59.251 1.00 15.54 A C ANISOU 4823 CB ASN A 598 1662 1946 2296 85 567 127 A C ATOM 4824 CG ASN A 598 11.983 4.031 58.187 1.00 16.59 A C ANISOU 4824 CG ASN A 598 1890 1798 2615 117 354 251 A C ATOM 4825 ND2 ASN A 598 10.869 3.471 58.629 1.00 20.70 A N ANISOU 4825 ND2 ASN A 598 2322 2873 2669 -627 629 123 A N ATOM 4826 OD1 ASN A 598 12.315 4.057 56.998 1.00 18.65 A O ANISOU 4826 OD1 ASN A 598 2240 2250 2594 271 347 -253 A O ATOM 4827 N LYS A 599 14.695 2.064 57.901 1.00 14.20 A N ANISOU 4827 N LYS A 599 1957 1477 1959 -72 446 -105 A N ATOM 4828 CA LYS A 599 15.507 1.526 56.814 1.00 13.21 A C ANISOU 4828 CA LYS A 599 1744 1161 2115 -71 454 -108 A C ATOM 4829 C LYS A 599 15.349 2.331 55.525 1.00 12.69 A C ANISOU 4829 C LYS A 599 1649 1072 2098 25 407 -116 A C ATOM 4830 O LYS A 599 16.294 2.380 54.725 1.00 13.10 A O ANISOU 4830 O LYS A 599 1682 1161 2132 66 482 112 A O ATOM 4831 CB LYS A 599 15.162 0.046 56.549 1.00 15.61 A C ANISOU 4831 CB LYS A 599 2511 1018 2401 103 505 -208 A C ATOM 4832 CG LYS A 599 15.563 -0.887 57.658 1.00 20.36 A C ANISOU 4832 CG LYS A 599 2643 2277 2813 27 43 -65 A C ATOM 4833 CD LYS A 599 15.123 -2.310 57.396 1.00 23.90 A C ANISOU 4833 CD LYS A 599 3282 2437 3363 -490 242 73 A C ATOM 4834 CE LYS A 599 15.748 -3.255 58.387 1.00 29.01 A C ANISOU 4834 CE LYS A 599 4367 3055 3599 -199 -456 144 A C ATOM 4835 NZ LYS A 599 15.813 -4.628 57.865 1.00 31.49 A N ANISOU 4835 NZ LYS A 599 4448 3414 4101 -23 -193 -35 A N ATOM 4836 N TYR A 600 14.168 2.915 55.308 1.00 13.46 A N ANISOU 4836 N TYR A 600 1522 1489 2102 45 495 199 A N ATOM 4837 CA TYR A 600 13.876 3.682 54.086 1.00 12.99 A C ANISOU 4837 CA TYR A 600 1721 1213 2001 240 140 -123 A C ATOM 4838 C TYR A 600 14.383 5.123 54.208 1.00 13.76 A C ANISOU 4838 C TYR A 600 1777 1437 2011 -52 203 -127 A C ATOM 4839 O TYR A 600 14.772 5.695 53.174 1.00 13.88 A O ANISOU 4839 O TYR A 600 1716 1535 2020 175 367 -120 A O ATOM 4840 CB TYR A 600 12.385 3.556 53.705 1.00 13.80 A C ANISOU 4840 CB TYR A 600 1519 1333 2390 162 321 33 A C ATOM 4841 CG TYR A 600 12.015 2.109 53.532 1.00 14.01 A C ANISOU 4841 CG TYR A 600 1634 1308 2379 92 290 154 A C ATOM 4842 CD1 TYR A 600 12.536 1.346 52.499 1.00 15.30 A C ANISOU 4842 CD1 TYR A 600 1715 1581 2515 149 166 23 A C ATOM 4843 CD2 TYR A 600 11.243 1.475 54.477 1.00 16.48 A C ANISOU 4843 CD2 TYR A 600 2168 1641 2451 32 645 -22 A C ATOM 4844 CE1 TYR A 600 12.284 -0.014 52.396 1.00 15.55 A C ANISOU 4844 CE1 TYR A 600 1845 1552 2511 134 357 5 A C ATOM 4845 CE2 TYR A 600 10.962 0.122 54.374 1.00 18.20 A C ANISOU 4845 CE2 TYR A 600 2417 1660 2838 -84 877 -5 A C ATOM 4846 CZ TYR A 600 11.503 -0.623 53.348 1.00 17.54 A C ANISOU 4846 CZ TYR A 600 2253 1541 2868 -235 575 -251 A C ATOM 4847 OH TYR A 600 11.261 -1.966 53.292 1.00 19.44 A O ANISOU 4847 OH TYR A 600 2423 1510 3452 -430 802 -323 A O ATOM 4848 N LEU A 601 14.399 5.688 55.419 1.00 13.22 A N ANISOU 4848 N LEU A 601 1622 1249 2151 -67 557 -19 A N ATOM 4849 CA LEU A 601 15.048 7.003 55.606 1.00 13.54 A C ANISOU 4849 CA LEU A 601 1952 966 2224 88 382 33 A C ATOM 4850 C LEU A 601 16.526 6.846 55.224 1.00 13.41 A C ANISOU 4850 C LEU A 601 1815 1156 2123 230 209 90 A C ATOM 4851 O LEU A 601 17.086 7.620 54.427 1.00 13.53 A O ANISOU 4851 O LEU A 601 1854 1183 2104 87 333 -97 A O ATOM 4852 CB LEU A 601 14.893 7.424 57.060 1.00 13.10 A C ANISOU 4852 CB LEU A 601 1817 1027 2131 198 441 -20 A C ATOM 4853 CG LEU A 601 15.418 8.807 57.473 1.00 15.05 A C ANISOU 4853 CG LEU A 601 2322 1338 2056 79 262 -112 A C ATOM 4854 CD1 LEU A 601 14.784 9.157 58.824 1.00 18.17 A C ANISOU 4854 CD1 LEU A 601 2645 1633 2626 205 935 -99 A C ATOM 4855 CD2 LEU A 601 16.939 8.812 57.605 1.00 15.12 A C ANISOU 4855 CD2 LEU A 601 2339 1357 2047 158 533 -29 A C ATOM 4856 N VAL A 602 17.145 5.767 55.742 1.00 12.28 A N ANISOU 4856 N VAL A 602 1947 908 1810 222 406 -37 A N ATOM 4857 CA VAL A 602 18.550 5.480 55.439 1.00 12.66 A C ANISOU 4857 CA VAL A 602 1754 1063 1990 30 171 19 A C ATOM 4858 C VAL A 602 18.742 5.271 53.932 1.00 12.56 A C ANISOU 4858 C VAL A 602 1603 1261 1909 -55 -28 54 A C ATOM 4859 O VAL A 602 19.653 5.839 53.305 1.00 12.43 A O ANISOU 4859 O VAL A 602 1672 969 2081 158 446 -117 A O ATOM 4860 CB VAL A 602 19.083 4.274 56.241 1.00 12.51 A C ANISOU 4860 CB VAL A 602 1778 1014 1960 -21 299 126 A C ATOM 4861 CG1 VAL A 602 20.457 3.819 55.790 1.00 14.11 A C ANISOU 4861 CG1 VAL A 602 1931 1205 2224 217 305 -216 A C ATOM 4862 CG2 VAL A 602 19.136 4.584 57.727 1.00 13.94 A C ANISOU 4862 CG2 VAL A 602 1940 1337 2017 60 -31 103 A C ATOM 4863 N SER A 603 17.893 4.418 53.352 1.00 11.54 A N ANISOU 4863 N SER A 603 1509 933 1942 -31 296 -125 A N ATOM 4864 CA SER A 603 18.016 4.074 51.944 1.00 11.27 A C ANISOU 4864 CA SER A 603 1351 1142 1789 194 -3 -11 A C ATOM 4865 C SER A 603 17.855 5.292 51.025 1.00 11.91 A C ANISOU 4865 C SER A 603 1660 1185 1679 247 133 -107 A C ATOM 4866 O SER A 603 18.569 5.455 50.035 1.00 12.34 A O ANISOU 4866 O SER A 603 1819 847 2023 83 320 -71 A O ATOM 4867 CB SER A 603 17.026 2.968 51.606 1.00 12.46 A C ANISOU 4867 CB SER A 603 1800 1019 1913 -21 352 -15 A C ATOM 4868 OG SER A 603 17.335 1.741 52.269 1.00 12.97 A O ANISOU 4868 OG SER A 603 1637 1010 2278 138 322 35 A O ATOM 4869 N ASP A 604 16.840 6.103 51.328 1.00 11.70 A N ANISOU 4869 N ASP A 604 1491 1156 1798 135 390 38 A N ATOM 4870 CA ASP A 604 16.587 7.283 50.516 1.00 13.37 A C ANISOU 4870 CA ASP A 604 1755 1282 2040 240 177 112 A C ATOM 4871 C ASP A 604 17.731 8.282 50.626 1.00 12.13 A C ANISOU 4871 C ASP A 604 1556 1209 1841 493 192 -215 A C ATOM 4872 O ASP A 604 18.088 8.916 49.589 1.00 13.04 A O ANISOU 4872 O ASP A 604 1626 1312 2014 145 115 -98 A O ATOM 4873 CB ASP A 604 15.284 7.946 50.950 1.00 12.67 A C ANISOU 4873 CB ASP A 604 1582 1449 1781 86 201 -32 A C ATOM 4874 CG ASP A 604 14.026 7.195 50.539 1.00 12.45 A C ANISOU 4874 CG ASP A 604 1720 1232 1778 -67 264 -5 A C ATOM 4875 OD1 ASP A 604 14.123 6.266 49.677 1.00 13.67 A O ANISOU 4875 OD1 ASP A 604 1651 1324 2219 52 118 -342 A O ATOM 4876 OD2 ASP A 604 12.931 7.546 51.075 1.00 14.13 A O ANISOU 4876 OD2 ASP A 604 1844 1311 2214 72 389 -110 A O ATOM 4877 N ALA A 605 18.323 8.386 51.820 1.00 11.33 A N ANISOU 4877 N ALA A 605 1448 1067 1789 177 253 -36 A N ATOM 4878 CA ALA A 605 19.494 9.279 51.974 1.00 11.63 A C ANISOU 4878 CA ALA A 605 1496 1280 1640 14 269 -71 A C ATOM 4879 C ALA A 605 20.618 8.816 51.040 1.00 10.69 A C ANISOU 4879 C ALA A 605 1393 919 1747 85 213 32 A C ATOM 4880 O ALA A 605 21.215 9.637 50.325 1.00 11.41 A O ANISOU 4880 O ALA A 605 1575 970 1787 -88 349 -82 A O ATOM 4881 CB ALA A 605 19.941 9.341 53.399 1.00 12.30 A C ANISOU 4881 CB ALA A 605 1811 1138 1721 201 223 -358 A C ATOM 4882 N TYR A 606 20.881 7.490 51.039 1.00 11.61 A N ANISOU 4882 N TYR A 606 1661 930 1819 202 104 -27 A N ATOM 4883 CA TYR A 606 21.916 6.960 50.180 1.00 10.83 A C ANISOU 4883 CA TYR A 606 1558 807 1747 35 81 118 A C ATOM 4884 C TYR A 606 21.570 7.021 48.670 1.00 10.41 A C ANISOU 4884 C TYR A 606 1520 657 1777 56 88 25 A C ATOM 4885 O TYR A 606 22.479 7.154 47.829 1.00 11.26 A O ANISOU 4885 O TYR A 606 1363 1079 1834 167 182 36 A O ATOM 4886 CB TYR A 606 22.321 5.548 50.607 1.00 11.26 A C ANISOU 4886 CB TYR A 606 1595 744 1936 130 108 -27 A C ATOM 4887 CG TYR A 606 23.397 5.535 51.652 1.00 10.74 A C ANISOU 4887 CG TYR A 606 1629 746 1704 160 119 105 A C ATOM 4888 CD1 TYR A 606 23.094 5.644 53.005 1.00 10.29 A C ANISOU 4888 CD1 TYR A 606 1457 706 1744 122 203 -67 A C ATOM 4889 CD2 TYR A 606 24.730 5.454 51.291 1.00 11.99 A C ANISOU 4889 CD2 TYR A 606 1650 1158 1746 91 189 -124 A C ATOM 4890 CE1 TYR A 606 24.079 5.613 53.978 1.00 10.80 A C ANISOU 4890 CE1 TYR A 606 1800 677 1626 133 110 17 A C ATOM 4891 CE2 TYR A 606 25.728 5.442 52.259 1.00 11.95 A C ANISOU 4891 CE2 TYR A 606 1787 1173 1579 99 155 1 A C ATOM 4892 CZ TYR A 606 25.409 5.523 53.606 1.00 10.86 A C ANISOU 4892 CZ TYR A 606 1753 798 1573 54 152 -93 A C ATOM 4893 OH TYR A 606 26.417 5.518 54.551 1.00 12.95 A O ANISOU 4893 OH TYR A 606 1802 1360 1758 145 68 14 A O ATOM 4894 N LEU A 607 20.269 6.968 48.330 1.00 10.67 A N ANISOU 4894 N LEU A 607 1332 1080 1639 -25 323 -197 A N ATOM 4895 CA ALEU A 607 19.840 7.187 46.942 0.50 11.11 A C ANISOU 4895 CA ALEU A 607 1444 906 1870 74 69 -93 A C ATOM 4896 CA BLEU A 607 19.818 7.191 46.951 0.50 11.35 A C ANISOU 4896 CA BLEU A 607 1542 867 1901 104 25 -95 A C ATOM 4897 C LEU A 607 20.210 8.614 46.508 1.00 11.09 A C ANISOU 4897 C LEU A 607 1452 994 1767 96 20 65 A C ATOM 4898 O LEU A 607 20.728 8.799 45.410 1.00 12.62 A O ANISOU 4898 O LEU A 607 1699 1151 1943 28 267 102 A O ATOM 4899 CB ALEU A 607 18.335 6.915 46.810 0.50 11.76 A C ANISOU 4899 CB ALEU A 607 1491 1094 1884 -130 62 -117 A C ATOM 4900 CB BLEU A 607 18.303 6.936 46.911 0.50 12.09 A C ANISOU 4900 CB BLEU A 607 1614 1013 1965 -121 -84 -96 A C ATOM 4901 CG ALEU A 607 17.651 7.518 45.582 0.50 13.48 A C ANISOU 4901 CG ALEU A 607 1503 1664 1952 -155 31 29 A C ATOM 4902 CG BLEU A 607 17.587 7.017 45.563 0.50 14.30 A C ANISOU 4902 CG BLEU A 607 1950 1323 2158 -37 -355 -238 A C ATOM 4903 CD1ALEU A 607 18.219 6.956 44.300 0.50 12.24 A C ANISOU 4903 CD1ALEU A 607 1352 1510 1789 -378 30 117 A C ATOM 4904 CD1BLEU A 607 16.259 6.269 45.628 0.50 15.63 A C ANISOU 4904 CD1BLEU A 607 1639 2399 1900 27 -294 1 A C ATOM 4905 CD2ALEU A 607 16.145 7.335 45.644 0.50 13.44 A C ANISOU 4905 CD2ALEU A 607 1488 1675 1943 -137 159 -135 A C ATOM 4906 CD2BLEU A 607 17.340 8.464 45.179 0.50 17.16 A C ANISOU 4906 CD2BLEU A 607 2650 1545 2323 118 -211 95 A C ATOM 4907 N LEU A 608 19.915 9.596 47.355 1.00 11.76 A N ANISOU 4907 N LEU A 608 1411 1298 1756 -35 160 24 A N ATOM 4908 CA LEU A 608 20.286 10.971 47.044 1.00 12.48 A C ANISOU 4908 CA LEU A 608 1493 1295 1954 46 98 321 A C ATOM 4909 C LEU A 608 21.815 11.082 46.895 1.00 11.98 A C ANISOU 4909 C LEU A 608 1485 1381 1685 224 221 67 A C ATOM 4910 O LEU A 608 22.305 11.712 45.977 1.00 11.69 A O ANISOU 4910 O LEU A 608 1708 922 1812 94 162 102 A O ATOM 4911 CB LEU A 608 19.766 11.899 48.139 1.00 13.15 A C ANISOU 4911 CB LEU A 608 1757 1202 2038 112 220 282 A C ATOM 4912 CG LEU A 608 18.383 12.508 47.938 1.00 16.81 A C ANISOU 4912 CG LEU A 608 1939 2082 2363 305 -46 243 A C ATOM 4913 CD1 LEU A 608 18.371 13.421 46.750 1.00 18.77 A C ANISOU 4913 CD1 LEU A 608 2292 2366 2472 639 274 463 A C ATOM 4914 CD2 LEU A 608 17.294 11.522 47.775 1.00 18.13 A C ANISOU 4914 CD2 LEU A 608 2131 1836 2921 448 79 409 A C ATOM 4915 N HIS A 609 22.546 10.454 47.828 1.00 11.25 A N ANISOU 4915 N HIS A 609 1478 967 1827 -22 106 60 A N ATOM 4916 CA HIS A 609 24.016 10.497 47.789 1.00 11.00 A C ANISOU 4916 CA HIS A 609 1482 913 1784 -76 80 -37 A C ATOM 4917 C HIS A 609 24.536 9.885 46.468 1.00 11.61 A C ANISOU 4917 C HIS A 609 1427 1249 1734 -71 119 -59 A C ATOM 4918 O HIS A 609 25.470 10.416 45.822 1.00 11.79 A O ANISOU 4918 O HIS A 609 1582 865 2031 105 360 44 A O ATOM 4919 CB HIS A 609 24.608 9.837 49.032 1.00 12.38 A C ANISOU 4919 CB HIS A 609 1679 1138 1885 -91 -94 -128 A C ATOM 4920 CG HIS A 609 26.079 9.817 49.046 1.00 12.92 A C ANISOU 4920 CG HIS A 609 1695 1438 1775 -128 26 -106 A C ATOM 4921 CD2 HIS A 609 26.921 8.788 49.223 1.00 13.95 A C ANISOU 4921 CD2 HIS A 609 1743 1591 1964 170 142 -230 A C ATOM 4922 ND1 HIS A 609 26.834 10.964 48.949 1.00 14.26 A N ANISOU 4922 ND1 HIS A 609 1355 1617 2444 -233 398 21 A N ATOM 4923 CE1 HIS A 609 28.117 10.624 49.035 1.00 13.39 A C ANISOU 4923 CE1 HIS A 609 1488 1052 2547 -121 58 24 A C ATOM 4924 NE2 HIS A 609 28.182 9.272 49.232 1.00 14.45 A N ANISOU 4924 NE2 HIS A 609 1701 1140 2649 137 157 68 A N ATOM 4925 N SER A 610 24.008 8.712 46.072 1.00 11.23 A N ANISOU 4925 N SER A 610 1364 1132 1770 -28 207 58 A N ATOM 4926 CA SER A 610 24.442 8.133 44.803 1.00 11.25 A C ANISOU 4926 CA SER A 610 1632 1176 1465 -220 161 218 A C ATOM 4927 C SER A 610 24.116 9.029 43.600 1.00 10.89 A C ANISOU 4927 C SER A 610 1549 960 1629 225 109 -20 A C ATOM 4928 O SER A 610 24.873 9.065 42.621 1.00 11.57 A O ANISOU 4928 O SER A 610 1679 862 1854 170 304 -45 A O ATOM 4929 CB SER A 610 23.836 6.766 44.639 1.00 11.63 A C ANISOU 4929 CB SER A 610 1801 1002 1615 -98 115 193 A C ATOM 4930 OG SER A 610 24.643 5.780 45.277 1.00 12.74 A O ANISOU 4930 OG SER A 610 1627 1083 2128 55 -19 -9 A O ATOM 4931 N THR A 611 22.938 9.679 43.651 1.00 11.67 A N ANISOU 4931 N THR A 611 1416 1228 1786 224 137 157 A N ATOM 4932 CA THR A 611 22.554 10.553 42.555 1.00 11.67 A C ANISOU 4932 CA THR A 611 1404 1218 1811 217 -45 94 A C ATOM 4933 C THR A 611 23.521 11.742 42.448 1.00 11.31 A C ANISOU 4933 C THR A 611 1421 1161 1716 291 7 76 A C ATOM 4934 O THR A 611 23.904 12.134 41.321 1.00 12.30 A O ANISOU 4934 O THR A 611 1878 969 1825 181 249 101 A O ATOM 4935 CB THR A 611 21.080 11.004 42.704 1.00 11.26 A C ANISOU 4935 CB THR A 611 1265 1104 1906 49 32 192 A C ATOM 4936 CG2 THR A 611 20.605 11.829 41.525 1.00 13.69 A C ANISOU 4936 CG2 THR A 611 2141 1136 1925 240 27 170 A C ATOM 4937 OG1 THR A 611 20.271 9.826 42.870 1.00 12.64 A O ANISOU 4937 OG1 THR A 611 1501 1309 1991 -122 225 128 A O ATOM 4938 N ASP A 612 23.921 12.258 43.622 1.00 11.67 A N ANISOU 4938 N ASP A 612 1670 962 1801 101 69 102 A N ATOM 4939 CA ASP A 612 24.859 13.374 43.708 1.00 12.25 A C ANISOU 4939 CA ASP A 612 1606 950 2097 58 268 188 A C ATOM 4940 C ASP A 612 26.241 12.944 43.168 1.00 12.14 A C ANISOU 4940 C ASP A 612 1702 1003 1905 118 295 35 A C ATOM 4941 O ASP A 612 26.859 13.599 42.300 1.00 13.14 A O ANISOU 4941 O ASP A 612 1795 934 2263 -27 356 -15 A O ATOM 4942 CB ASP A 612 24.969 13.795 45.159 1.00 13.79 A C ANISOU 4942 CB ASP A 612 1974 909 2353 104 415 -144 A C ATOM 4943 CG ASP A 612 25.732 15.073 45.424 1.00 17.67 A C ANISOU 4943 CG ASP A 612 2832 1207 2676 -356 320 -221 A C ATOM 4944 OD1 ASP A 612 25.633 15.990 44.606 1.00 22.67 A O ANISOU 4944 OD1 ASP A 612 4062 1614 2936 -425 442 5 A O ATOM 4945 OD2 ASP A 612 26.358 15.142 46.498 1.00 21.31 A O ANISOU 4945 OD2 ASP A 612 3343 1412 3341 -555 -59 -40 A O ATOM 4946 N MET A 613 26.698 11.758 43.618 1.00 11.95 A N ANISOU 4946 N MET A 613 1623 883 2032 49 273 -32 A N ATOM 4947 CA MET A 613 27.984 11.241 43.155 1.00 12.15 A C ANISOU 4947 CA MET A 613 1609 924 2081 -150 254 -74 A C ATOM 4948 C MET A 613 27.942 11.023 41.643 1.00 11.69 A C ANISOU 4948 C MET A 613 1460 977 2005 114 86 50 A C ATOM 4949 O MET A 613 28.935 11.330 40.930 1.00 13.09 A O ANISOU 4949 O MET A 613 1840 844 2289 35 326 -18 A O ATOM 4950 CB MET A 613 28.384 9.936 43.843 1.00 11.32 A C ANISOU 4950 CB MET A 613 1501 754 2043 -72 306 -148 A C ATOM 4951 CG MET A 613 28.866 10.109 45.286 1.00 12.24 A C ANISOU 4951 CG MET A 613 1917 626 2106 90 337 -62 A C ATOM 4952 SD MET A 613 29.486 8.577 45.996 1.00 13.09 A S ANISOU 4952 SD MET A 613 1691 1049 2232 106 235 112 A S ATOM 4953 CE MET A 613 28.018 7.566 46.180 1.00 13.46 A C ANISOU 4953 CE MET A 613 1691 1036 2387 32 165 137 A C ATOM 4954 N LEU A 614 26.826 10.493 41.137 1.00 11.33 A N ANISOU 4954 N LEU A 614 1425 1056 1824 -50 198 46 A N ATOM 4955 CA LEU A 614 26.728 10.215 39.699 1.00 12.47 A C ANISOU 4955 CA LEU A 614 1695 1202 1841 -123 174 128 A C ATOM 4956 C LEU A 614 26.713 11.532 38.876 1.00 12.86 A C ANISOU 4956 C LEU A 614 1823 1228 1832 23 12 132 A C ATOM 4957 O LEU A 614 27.319 11.588 37.818 1.00 12.63 A O ANISOU 4957 O LEU A 614 1833 907 2058 -148 115 180 A O ATOM 4958 CB LEU A 614 25.516 9.313 39.418 1.00 13.48 A C ANISOU 4958 CB LEU A 614 1689 1250 2181 -84 128 -13 A C ATOM 4959 CG LEU A 614 25.354 8.883 37.949 1.00 13.62 A C ANISOU 4959 CG LEU A 614 1632 1442 2100 30 123 71 A C ATOM 4960 CD1 LEU A 614 26.574 8.098 37.446 1.00 13.82 A C ANISOU 4960 CD1 LEU A 614 1877 1659 1713 -130 449 -273 A C ATOM 4961 CD2 LEU A 614 24.079 8.067 37.821 1.00 13.98 A C ANISOU 4961 CD2 LEU A 614 2095 1246 1969 -216 93 54 A C ATOM 4962 N ALA A 615 26.031 12.571 39.370 1.00 12.45 A N ANISOU 4962 N ALA A 615 1546 1329 1853 -162 316 117 A N ATOM 4963 CA ALA A 615 26.088 13.902 38.751 1.00 13.40 A C ANISOU 4963 CA ALA A 615 1869 1345 1875 -136 198 138 A C ATOM 4964 C ALA A 615 27.548 14.357 38.664 1.00 11.41 A C ANISOU 4964 C ALA A 615 1693 1112 1531 158 208 -182 A C ATOM 4965 O ALA A 615 27.983 14.820 37.616 1.00 12.74 A O ANISOU 4965 O ALA A 615 1793 1200 1845 -150 193 197 A O ATOM 4966 CB ALA A 615 25.256 14.904 39.515 1.00 13.50 A C ANISOU 4966 CB ALA A 615 1916 1391 1821 62 73 152 A C ATOM 4967 N ASN A 616 28.280 14.230 39.780 1.00 12.15 A N ANISOU 4967 N ASN A 616 1800 1000 1814 -185 -21 1 A N ATOM 4968 CA ASN A 616 29.636 14.729 39.882 1.00 13.80 A C ANISOU 4968 CA ASN A 616 1552 1479 2210 -59 228 -3 A C ATOM 4969 C ASN A 616 30.578 13.931 38.984 1.00 12.68 A C ANISOU 4969 C ASN A 616 1723 1183 1909 -153 109 -35 A C ATOM 4970 O ASN A 616 31.432 14.507 38.300 1.00 13.95 A O ANISOU 4970 O ASN A 616 1841 1435 2025 -172 231 91 A O ATOM 4971 CB ASN A 616 30.090 14.808 41.333 1.00 13.90 A C ANISOU 4971 CB ASN A 616 1771 1276 2231 -172 112 -15 A C ATOM 4972 CG ASN A 616 29.376 15.918 42.075 1.00 16.84 A C ANISOU 4972 CG ASN A 616 2440 1490 2465 69 48 -180 A C ATOM 4973 ND2 ASN A 616 29.831 16.174 43.285 1.00 18.42 A N ANISOU 4973 ND2 ASN A 616 2533 1892 2572 -194 151 -581 A N ATOM 4974 OD1 ASN A 616 28.406 16.526 41.566 1.00 18.21 A O ANISOU 4974 OD1 ASN A 616 2485 1703 2727 94 171 -275 A O ATOM 4975 N ILE A 617 30.401 12.599 38.965 1.00 12.65 A N ANISOU 4975 N ILE A 617 1763 1127 1915 16 199 217 A N ATOM 4976 CA ILE A 617 31.218 11.763 38.072 1.00 12.74 A C ANISOU 4976 CA ILE A 617 1680 1236 1923 18 41 74 A C ATOM 4977 C ILE A 617 30.939 12.135 36.615 1.00 11.45 A C ANISOU 4977 C ILE A 617 1560 782 2009 -132 65 -49 A C ATOM 4978 O ILE A 617 31.857 12.224 35.788 1.00 12.86 A O ANISOU 4978 O ILE A 617 1693 1141 2050 63 143 195 A O ATOM 4979 CB ILE A 617 30.926 10.264 38.334 1.00 14.27 A C ANISOU 4979 CB ILE A 617 1960 1239 2223 271 148 320 A C ATOM 4980 CG1 ILE A 617 31.446 9.830 39.699 1.00 15.41 A C ANISOU 4980 CG1 ILE A 617 2497 1122 2235 426 130 195 A C ATOM 4981 CG2 ILE A 617 31.463 9.433 37.200 1.00 17.10 A C ANISOU 4981 CG2 ILE A 617 2637 1566 2294 324 168 329 A C ATOM 4982 CD1 ILE A 617 30.813 8.497 40.107 1.00 18.34 A C ANISOU 4982 CD1 ILE A 617 2980 1394 2591 159 -243 479 A C ATOM 4983 N SER A 618 29.645 12.364 36.311 1.00 11.84 A N ANISOU 4983 N SER A 618 1495 1142 1861 -45 -31 -74 A N ATOM 4984 CA SER A 618 29.257 12.764 34.954 1.00 12.52 A C ANISOU 4984 CA SER A 618 1736 1072 1947 -126 -33 -40 A C ATOM 4985 C SER A 618 30.002 14.058 34.566 1.00 13.35 A C ANISOU 4985 C SER A 618 1675 1315 2080 -146 82 210 A C ATOM 4986 O SER A 618 30.535 14.144 33.480 1.00 14.09 A O ANISOU 4986 O SER A 618 2038 1122 2193 -51 262 430 A O ATOM 4987 CB SER A 618 27.728 12.918 34.842 1.00 11.58 A C ANISOU 4987 CB SER A 618 1666 980 1752 -116 4 38 A C ATOM 4988 OG SER A 618 27.092 11.674 35.107 1.00 12.67 A O ANISOU 4988 OG SER A 618 1938 831 2044 17 47 108 A O ATOM 4989 N THR A 619 30.035 15.033 35.476 1.00 13.21 A N ANISOU 4989 N THR A 619 1700 1469 1849 -156 343 322 A N ATOM 4990 CA THR A 619 30.745 16.280 35.215 1.00 14.07 A C ANISOU 4990 CA THR A 619 1624 1424 2297 -191 104 344 A C ATOM 4991 C THR A 619 32.243 16.038 34.984 1.00 14.10 A C ANISOU 4991 C THR A 619 1740 1449 2164 -26 102 200 A C ATOM 4992 O THR A 619 32.831 16.558 34.040 1.00 14.39 A O ANISOU 4992 O THR A 619 2114 1095 2257 -176 138 224 A O ATOM 4993 CB THR A 619 30.488 17.234 36.372 1.00 15.95 A C ANISOU 4993 CB THR A 619 2060 1553 2447 2 -11 239 A C ATOM 4994 CG2 THR A 619 31.249 18.525 36.201 1.00 17.25 A C ANISOU 4994 CG2 THR A 619 2312 1550 2693 -76 -38 352 A C ATOM 4995 OG1 THR A 619 29.093 17.506 36.427 1.00 16.78 A O ANISOU 4995 OG1 THR A 619 1855 1490 3028 -137 132 -118 A O ATOM 4996 N SER A 620 32.854 15.193 35.812 1.00 13.68 A N ANISOU 4996 N SER A 620 1689 1019 2487 -22 219 246 A N ATOM 4997 CA SER A 620 34.284 14.871 35.692 1.00 13.07 A C ANISOU 4997 CA SER A 620 1623 929 2411 -198 106 32 A C ATOM 4998 C SER A 620 34.583 14.298 34.302 1.00 14.08 A C ANISOU 4998 C SER A 620 1839 1270 2240 -109 171 192 A C ATOM 4999 O SER A 620 35.681 14.515 33.746 1.00 17.67 A O ANISOU 4999 O SER A 620 2049 1653 3010 -339 507 -114 A O ATOM 5000 CB SER A 620 34.747 13.921 36.786 1.00 16.22 A C ANISOU 5000 CB SER A 620 2134 1682 2345 73 212 263 A C ATOM 5001 OG SER A 620 34.643 14.511 38.075 1.00 18.00 A O ANISOU 5001 OG SER A 620 2260 2017 2560 119 -100 -187 A O ATOM 5002 N LEU A 621 33.634 13.499 33.788 1.00 13.55 A N ANISOU 5002 N LEU A 621 1756 1267 2122 -256 415 167 A N ATOM 5003 CA LEU A 621 33.792 12.812 32.499 1.00 13.09 A C ANISOU 5003 CA LEU A 621 1683 1140 2149 -279 271 85 A C ATOM 5004 C LEU A 621 33.225 13.581 31.309 1.00 13.61 A C ANISOU 5004 C LEU A 621 1810 1309 2051 -87 220 -35 A C ATOM 5005 O LEU A 621 33.231 13.095 30.217 1.00 14.11 A O ANISOU 5005 O LEU A 621 2232 1127 1998 -312 352 322 A O ATOM 5006 CB LEU A 621 33.094 11.452 32.577 1.00 13.47 A C ANISOU 5006 CB LEU A 621 2076 817 2224 -146 132 -3 A C ATOM 5007 CG LEU A 621 33.723 10.432 33.519 1.00 14.65 A C ANISOU 5007 CG LEU A 621 2430 1063 2071 -195 201 122 A C ATOM 5008 CD1 LEU A 621 32.894 9.153 33.553 1.00 16.85 A C ANISOU 5008 CD1 LEU A 621 2968 1099 2333 -436 67 -56 A C ATOM 5009 CD2 LEU A 621 35.183 10.126 33.184 1.00 16.99 A C ANISOU 5009 CD2 LEU A 621 2700 1457 2298 -135 401 296 A C ATOM 5010 N SER A 622 32.834 14.841 31.516 1.00 13.83 A N ANISOU 5010 N SER A 622 1845 1171 2237 -110 322 224 A N ATOM 5011 CA ASER A 622 32.315 15.689 30.415 0.50 15.34 A C ANISOU 5011 CA ASER A 622 2189 1400 2239 -91 367 299 A C ATOM 5012 CA BSER A 622 32.348 15.671 30.421 0.50 16.36 A C ANISOU 5012 CA BSER A 622 2212 1658 2344 -25 287 396 A C ATOM 5013 C SER A 622 31.096 15.055 29.750 1.00 14.53 A C ANISOU 5013 C SER A 622 2119 1258 2141 259 366 89 A C ATOM 5014 O SER A 622 30.889 15.155 28.545 1.00 16.77 A O ANISOU 5014 O SER A 622 2551 1588 2232 -13 321 329 A O ATOM 5015 CB ASER A 622 33.372 16.005 29.381 0.50 14.30 A C ANISOU 5015 CB ASER A 622 2027 869 2535 -360 390 -19 A C ATOM 5016 CB BSER A 622 33.511 15.897 29.467 0.50 18.97 A C ANISOU 5016 CB BSER A 622 2217 2164 2826 109 483 454 A C ATOM 5017 OG ASER A 622 33.957 17.210 29.714 0.50 12.94 A O ANISOU 5017 OG ASER A 622 1680 837 2398 -298 502 -68 A O ATOM 5018 OG BSER A 622 33.291 17.012 28.657 0.50 22.83 A O ANISOU 5018 OG BSER A 622 2629 2171 3871 697 800 840 A O ATOM 5019 N LYS A 623 30.229 14.455 30.564 1.00 14.54 A N ANISOU 5019 N LYS A 623 1810 1651 2062 169 173 373 A N ATOM 5020 CA LYS A 623 28.958 13.939 30.110 1.00 14.39 A C ANISOU 5020 CA LYS A 623 1741 1974 1749 46 44 321 A C ATOM 5021 C LYS A 623 27.867 14.924 30.571 1.00 14.02 A C ANISOU 5021 C LYS A 623 1577 1735 2013 -67 -26 676 A C ATOM 5022 O LYS A 623 27.264 14.791 31.630 1.00 15.79 A O ANISOU 5022 O LYS A 623 2027 1651 2320 52 332 354 A O ATOM 5023 CB LYS A 623 28.745 12.531 30.661 1.00 15.20 A C ANISOU 5023 CB LYS A 623 1894 2046 1833 -235 73 49 A C ATOM 5024 CG LYS A 623 29.749 11.505 30.179 1.00 17.14 A C ANISOU 5024 CG LYS A 623 1850 2023 2639 -283 212 123 A C ATOM 5025 CD LYS A 623 29.478 10.145 30.727 1.00 18.14 A C ANISOU 5025 CD LYS A 623 2334 1983 2575 23 145 304 A C ATOM 5026 CE LYS A 623 30.596 9.140 30.533 1.00 17.12 A C ANISOU 5026 CE LYS A 623 2200 1736 2565 -133 18 564 A C ATOM 5027 NZ LYS A 623 30.789 8.805 29.126 1.00 24.79 A N ANISOU 5027 NZ LYS A 623 3878 2576 2962 276 288 323 A N ATOM 5028 N GLY A 624 27.642 15.973 29.760 1.00 13.75 A N ANISOU 5028 N GLY A 624 1779 1327 2116 28 63 485 A N ATOM 5029 CA GLY A 624 26.822 17.102 30.157 1.00 13.95 A C ANISOU 5029 CA GLY A 624 1937 1215 2146 -73 73 208 A C ATOM 5030 C GLY A 624 25.353 16.761 30.327 1.00 12.93 A C ANISOU 5030 C GLY A 624 1939 1063 1910 -5 245 344 A C ATOM 5031 O GLY A 624 24.715 17.226 31.272 1.00 13.62 A O ANISOU 5031 O GLY A 624 1823 1384 1968 -131 180 104 A O ATOM 5032 N GLU A 625 24.801 16.005 29.366 1.00 13.75 A N ANISOU 5032 N GLU A 625 1850 1319 2053 -205 466 166 A N ATOM 5033 CA GLU A 625 23.406 15.651 29.457 1.00 15.00 A C ANISOU 5033 CA GLU A 625 1797 1615 2285 -141 366 169 A C ATOM 5034 C GLU A 625 23.128 14.904 30.765 1.00 13.33 A C ANISOU 5034 C GLU A 625 1840 1261 1962 131 166 22 A C ATOM 5035 O GLU A 625 22.159 15.161 31.501 1.00 14.13 A O ANISOU 5035 O GLU A 625 1873 1186 2309 -151 422 168 A O ATOM 5036 CB GLU A 625 22.956 14.803 28.276 1.00 17.87 A C ANISOU 5036 CB GLU A 625 2312 2260 2215 -318 279 113 A C ATOM 5037 CG GLU A 625 22.856 15.603 26.996 1.00 20.96 A C ANISOU 5037 CG GLU A 625 2456 3119 2389 -310 67 310 A C ATOM 5038 CD GLU A 625 22.571 14.732 25.771 1.00 25.70 A C ANISOU 5038 CD GLU A 625 3377 3168 3219 -839 -414 -141 A C ATOM 5039 OE1 GLU A 625 22.058 15.288 24.801 1.00 36.12 A O ANISOU 5039 OE1 GLU A 625 4067 5636 4018 -2107 -1783 639 A O ATOM 5040 OE2 GLU A 625 22.875 13.503 25.786 1.00 34.70 A O ANISOU 5040 OE2 GLU A 625 6312 3748 3121 -295 -784 -78 A O ATOM 5041 N GLU A 626 23.980 13.936 31.038 1.00 13.51 A N ANISOU 5041 N GLU A 626 1616 1428 2089 138 415 190 A N ATOM 5042 CA GLU A 626 23.879 13.137 32.256 1.00 13.63 A C ANISOU 5042 CA GLU A 626 1586 1625 1965 3 199 209 A C ATOM 5043 C GLU A 626 24.062 13.991 33.509 1.00 12.67 A C ANISOU 5043 C GLU A 626 1659 1103 2049 118 209 275 A C ATOM 5044 O GLU A 626 23.268 13.886 34.448 1.00 14.56 A O ANISOU 5044 O GLU A 626 1983 1226 2323 286 415 554 A O ATOM 5045 CB GLU A 626 24.917 12.029 32.241 1.00 15.24 A C ANISOU 5045 CB GLU A 626 1968 1527 2293 168 320 24 A C ATOM 5046 CG GLU A 626 24.658 10.965 31.163 1.00 17.24 A C ANISOU 5046 CG GLU A 626 1882 1861 2807 127 -404 -80 A C ATOM 5047 CD GLU A 626 25.152 11.217 29.744 1.00 21.42 A C ANISOU 5047 CD GLU A 626 2973 2306 2860 687 -139 -407 A C ATOM 5048 OE1 GLU A 626 25.562 12.343 29.383 1.00 20.39 A O ANISOU 5048 OE1 GLU A 626 2500 2622 2624 320 -280 -532 A O ATOM 5049 OE2 GLU A 626 25.089 10.239 28.961 1.00 31.44 A O ANISOU 5049 OE2 GLU A 626 4603 3248 4092 732 -1002 -1494 A O ATOM 5050 N ALA A 627 25.067 14.881 33.498 1.00 12.70 A N ANISOU 5050 N ALA A 627 1485 1426 1911 -42 325 483 A N ATOM 5051 CA ALA A 627 25.342 15.678 34.684 1.00 14.18 A C ANISOU 5051 CA ALA A 627 1571 1871 1943 189 192 385 A C ATOM 5052 C ALA A 627 24.116 16.533 35.015 1.00 14.29 A C ANISOU 5052 C ALA A 627 1823 1680 1926 327 157 322 A C ATOM 5053 O ALA A 627 23.682 16.584 36.173 1.00 14.01 A O ANISOU 5053 O ALA A 627 1991 1415 1916 241 106 131 A O ATOM 5054 CB ALA A 627 26.575 16.554 34.503 1.00 13.88 A C ANISOU 5054 CB ALA A 627 1648 1729 1897 168 67 189 A C ATOM 5055 N SER A 628 23.555 17.206 34.010 1.00 12.58 A N ANISOU 5055 N SER A 628 1691 1133 1955 50 188 255 A N ATOM 5056 CA ASER A 628 22.370 18.029 34.269 0.50 13.51 A C ANISOU 5056 CA ASER A 628 1702 1342 2088 135 225 256 A C ATOM 5057 CA BSER A 628 22.362 18.021 34.214 0.50 14.41 A C ANISOU 5057 CA BSER A 628 1730 1428 2315 144 290 233 A C ATOM 5058 C SER A 628 21.182 17.175 34.716 1.00 12.88 A C ANISOU 5058 C SER A 628 1546 1240 2108 168 93 118 A C ATOM 5059 O SER A 628 20.446 17.584 35.624 1.00 14.94 A O ANISOU 5059 O SER A 628 1969 1439 2269 111 356 69 A O ATOM 5060 CB ASER A 628 22.001 18.860 33.077 0.50 14.13 A C ANISOU 5060 CB ASER A 628 1844 1186 2336 -15 91 389 A C ATOM 5061 CB BSER A 628 22.013 18.734 32.934 0.50 17.49 A C ANISOU 5061 CB BSER A 628 2490 1482 2673 1 -63 461 A C ATOM 5062 OG ASER A 628 22.898 19.944 32.951 0.50 13.93 A O ANISOU 5062 OG ASER A 628 1685 1401 2204 -66 26 659 A O ATOM 5063 OG BSER A 628 20.913 19.599 33.132 0.50 21.79 A O ANISOU 5063 OG BSER A 628 2518 2163 3596 320 -55 978 A O ATOM 5064 N ASN A 629 21.000 15.998 34.092 1.00 12.52 A N ANISOU 5064 N ASN A 629 1574 1309 1870 150 254 193 A N ATOM 5065 CA ASN A 629 19.908 15.118 34.415 1.00 13.40 A C ANISOU 5065 CA ASN A 629 1651 1452 1988 123 2 279 A C ATOM 5066 C ASN A 629 19.997 14.736 35.888 1.00 12.76 A C ANISOU 5066 C ASN A 629 1577 1494 1776 -136 109 113 A C ATOM 5067 O ASN A 629 19.004 14.816 36.624 1.00 13.68 A O ANISOU 5067 O ASN A 629 1784 1264 2148 68 330 255 A O ATOM 5068 CB ASN A 629 20.010 13.853 33.595 1.00 14.03 A C ANISOU 5068 CB ASN A 629 1853 1503 1971 70 125 212 A C ATOM 5069 CG ASN A 629 18.841 12.915 33.757 1.00 15.17 A C ANISOU 5069 CG ASN A 629 1803 1590 2368 84 -29 169 A C ATOM 5070 ND2 ASN A 629 19.142 11.642 33.938 1.00 15.96 A N ANISOU 5070 ND2 ASN A 629 1815 1467 2780 -8 -298 419 A N ATOM 5071 OD1 ASN A 629 17.681 13.317 33.730 1.00 16.79 A O ANISOU 5071 OD1 ASN A 629 1847 1638 2894 -53 -36 578 A O ATOM 5072 N TYR A 630 21.179 14.288 36.335 1.00 12.66 A N ANISOU 5072 N TYR A 630 1675 1018 2116 -104 306 303 A N ATOM 5073 CA TYR A 630 21.283 13.821 37.732 1.00 13.54 A C ANISOU 5073 CA TYR A 630 1539 1555 2049 103 162 349 A C ATOM 5074 C TYR A 630 21.222 14.965 38.730 1.00 12.86 A C ANISOU 5074 C TYR A 630 1589 1339 1957 -6 162 494 A C ATOM 5075 O TYR A 630 20.704 14.787 39.830 1.00 14.31 A O ANISOU 5075 O TYR A 630 2053 1204 2179 249 270 414 A O ATOM 5076 CB TYR A 630 22.506 12.918 37.903 1.00 13.52 A C ANISOU 5076 CB TYR A 630 1423 1504 2208 106 159 144 A C ATOM 5077 CG TYR A 630 22.391 11.653 37.076 1.00 13.15 A C ANISOU 5077 CG TYR A 630 1622 1364 2007 -77 41 223 A C ATOM 5078 CD1 TYR A 630 21.303 10.802 37.228 1.00 12.83 A C ANISOU 5078 CD1 TYR A 630 1326 1425 2123 100 389 -152 A C ATOM 5079 CD2 TYR A 630 23.308 11.350 36.085 1.00 13.07 A C ANISOU 5079 CD2 TYR A 630 1675 966 2324 83 145 322 A C ATOM 5080 CE1 TYR A 630 21.121 9.693 36.405 1.00 13.39 A C ANISOU 5080 CE1 TYR A 630 1811 1111 2163 38 201 87 A C ATOM 5081 CE2 TYR A 630 23.170 10.230 35.273 1.00 14.65 A C ANISOU 5081 CE2 TYR A 630 1950 1169 2446 -167 355 167 A C ATOM 5082 CZ TYR A 630 22.043 9.429 35.410 1.00 13.24 A C ANISOU 5082 CZ TYR A 630 1605 1197 2226 40 132 -52 A C ATOM 5083 OH TYR A 630 21.889 8.330 34.615 1.00 14.84 A O ANISOU 5083 OH TYR A 630 2288 1227 2123 -97 262 4 A O ATOM 5084 N THR A 631 21.687 16.165 38.316 1.00 13.07 A N ANISOU 5084 N THR A 631 1832 1219 1912 68 261 345 A N ATOM 5085 CA THR A 631 21.532 17.351 39.145 1.00 13.84 A C ANISOU 5085 CA THR A 631 1792 1510 1954 -10 464 114 A C ATOM 5086 C THR A 631 20.033 17.635 39.359 1.00 12.26 A C ANISOU 5086 C THR A 631 1795 853 2007 -6 102 271 A C ATOM 5087 O THR A 631 19.595 17.948 40.517 1.00 15.22 A O ANISOU 5087 O THR A 631 2201 1277 2304 161 595 207 A O ATOM 5088 CB THR A 631 22.298 18.528 38.532 1.00 15.27 A C ANISOU 5088 CB THR A 631 1982 1265 2555 -93 421 -33 A C ATOM 5089 CG2 THR A 631 22.101 19.825 39.287 1.00 18.83 A C ANISOU 5089 CG2 THR A 631 3035 1356 2764 -187 206 -260 A C ATOM 5090 OG1 THR A 631 23.694 18.229 38.520 1.00 16.16 A O ANISOU 5090 OG1 THR A 631 1942 1399 2800 -46 224 330 A O ATOM 5091 N GLU A 632 19.258 17.544 38.278 1.00 13.87 A N ANISOU 5091 N GLU A 632 1969 1332 1967 144 107 233 A N ATOM 5092 CA AGLU A 632 17.783 17.775 38.271 0.50 15.32 A C ANISOU 5092 CA AGLU A 632 1926 1459 2434 164 115 115 A C ATOM 5093 CA BGLU A 632 17.823 17.848 38.390 0.50 16.12 A C ANISOU 5093 CA BGLU A 632 1954 1592 2577 216 183 190 A C ATOM 5094 C GLU A 632 17.094 16.746 39.182 1.00 14.83 A C ANISOU 5094 C GLU A 632 1978 1521 2133 328 173 85 A C ATOM 5095 O GLU A 632 16.234 17.058 40.007 1.00 15.57 A O ANISOU 5095 O GLU A 632 1781 1731 2404 395 279 368 A O ATOM 5096 CB AGLU A 632 17.228 17.706 36.839 0.50 16.83 A C ANISOU 5096 CB AGLU A 632 2170 1675 2546 320 42 149 A C ATOM 5097 CB BGLU A 632 17.247 18.146 37.008 0.50 18.80 A C ANISOU 5097 CB BGLU A 632 2293 2037 2811 504 107 392 A C ATOM 5098 CG AGLU A 632 17.577 18.929 35.980 0.50 20.52 A C ANISOU 5098 CG AGLU A 632 2592 2281 2923 192 152 531 A C ATOM 5099 CG BGLU A 632 17.828 19.427 36.383 0.50 21.98 A C ANISOU 5099 CG BGLU A 632 2397 2365 3587 531 617 611 A C ATOM 5100 CD AGLU A 632 17.263 18.899 34.486 0.50 28.97 A C ANISOU 5100 CD AGLU A 632 4454 3507 3046 9 -130 167 A C ATOM 5101 CD BGLU A 632 17.666 20.715 37.182 0.50 26.86 A C ANISOU 5101 CD BGLU A 632 3255 2407 4542 845 1205 527 A C ATOM 5102 OE1AGLU A 632 16.552 17.956 34.013 0.50 28.65 A O ANISOU 5102 OE1AGLU A 632 4289 3095 3502 -144 -4 682 A O ATOM 5103 OE1BGLU A 632 16.683 20.820 37.930 0.50 32.17 A O ANISOU 5103 OE1BGLU A 632 4225 2893 5104 1814 2031 1273 A O ATOM 5104 OE2AGLU A 632 17.738 19.836 33.776 0.50 34.04 A O ANISOU 5104 OE2AGLU A 632 4700 3375 4856 166 -64 585 A O ATOM 5105 OE2BGLU A 632 18.531 21.608 37.065 0.50 35.36 A O ANISOU 5105 OE2BGLU A 632 4082 3389 5962 39 959 -286 A O ATOM 5106 N TRP A 633 17.413 15.467 38.958 1.00 13.35 A N ANISOU 5106 N TRP A 633 1660 1583 1828 418 175 66 A N ATOM 5107 CA TRP A 633 16.834 14.373 39.774 1.00 14.74 A C ANISOU 5107 CA TRP A 633 1551 1867 2180 236 337 42 A C ATOM 5108 C TRP A 633 17.198 14.572 41.244 1.00 13.19 A C ANISOU 5108 C TRP A 633 1593 1382 2034 32 293 231 A C ATOM 5109 O TRP A 633 16.359 14.385 42.126 1.00 13.88 A O ANISOU 5109 O TRP A 633 1759 1407 2106 217 467 48 A O ATOM 5110 CB TRP A 633 17.317 12.996 39.294 1.00 14.00 A C ANISOU 5110 CB TRP A 633 1737 1658 1924 196 342 147 A C ATOM 5111 CG TRP A 633 16.527 12.439 38.157 1.00 14.44 A C ANISOU 5111 CG TRP A 633 1516 1691 2276 132 174 131 A C ATOM 5112 CD1 TRP A 633 16.577 12.765 36.837 1.00 16.80 A C ANISOU 5112 CD1 TRP A 633 2099 1982 2299 -193 215 175 A C ATOM 5113 CD2 TRP A 633 15.479 11.471 38.269 1.00 15.89 A C ANISOU 5113 CD2 TRP A 633 1799 1916 2320 -181 107 135 A C ATOM 5114 CE2 TRP A 633 14.948 11.269 36.979 1.00 16.51 A C ANISOU 5114 CE2 TRP A 633 1835 1958 2480 91 34 -61 A C ATOM 5115 CE3 TRP A 633 14.969 10.735 39.339 1.00 17.59 A C ANISOU 5115 CE3 TRP A 633 2198 2069 2415 -57 35 484 A C ATOM 5116 NE1 TRP A 633 15.637 12.067 36.127 1.00 16.61 A N ANISOU 5116 NE1 TRP A 633 1832 2354 2125 117 146 -5 A N ATOM 5117 CZ2 TRP A 633 13.920 10.354 36.726 1.00 18.07 A C ANISOU 5117 CZ2 TRP A 633 1754 2389 2721 -36 -215 159 A C ATOM 5118 CZ3 TRP A 633 13.952 9.844 39.089 1.00 19.22 A C ANISOU 5118 CZ3 TRP A 633 2485 2049 2768 -52 -97 260 A C ATOM 5119 CH2 TRP A 633 13.437 9.664 37.807 1.00 18.70 A C ANISOU 5119 CH2 TRP A 633 1945 2215 2945 -146 -235 246 A C ATOM 5120 N HIS A 634 18.448 14.963 41.520 1.00 13.77 A N ANISOU 5120 N HIS A 634 1756 1542 1932 -30 52 358 A N ATOM 5121 CA HIS A 634 18.855 15.176 42.902 1.00 13.28 A C ANISOU 5121 CA HIS A 634 1727 1334 1985 -70 -33 221 A C ATOM 5122 C HIS A 634 17.991 16.270 43.557 1.00 15.99 A C ANISOU 5122 C HIS A 634 2316 1569 2189 90 225 133 A C ATOM 5123 O HIS A 634 17.564 16.131 44.699 1.00 15.23 A O ANISOU 5123 O HIS A 634 2019 1492 2275 251 407 20 A O ATOM 5124 CB HIS A 634 20.341 15.481 42.967 1.00 14.76 A C ANISOU 5124 CB HIS A 634 1829 1498 2281 -74 84 457 A C ATOM 5125 CG HIS A 634 20.861 15.607 44.340 1.00 14.21 A C ANISOU 5125 CG HIS A 634 1810 1321 2267 137 15 84 A C ATOM 5126 CD2 HIS A 634 21.433 14.693 45.147 1.00 14.66 A C ANISOU 5126 CD2 HIS A 634 1937 1294 2339 47 -26 201 A C ATOM 5127 ND1 HIS A 634 20.889 16.785 45.033 1.00 20.01 A N ANISOU 5127 ND1 HIS A 634 2931 1737 2935 333 -711 -459 A N ATOM 5128 CE1 HIS A 634 21.436 16.568 46.217 1.00 20.40 A C ANISOU 5128 CE1 HIS A 634 2982 1851 2918 671 -692 -462 A C ATOM 5129 NE2 HIS A 634 21.772 15.283 46.320 1.00 14.87 A N ANISOU 5129 NE2 HIS A 634 1715 1689 2243 298 174 -91 A N ATOM 5130 N ALA A 635 17.739 17.373 42.830 1.00 15.07 A N ANISOU 5130 N ALA A 635 1905 1777 2040 108 250 175 A N ATOM 5131 CA ALA A 635 16.956 18.441 43.413 1.00 16.61 A C ANISOU 5131 CA ALA A 635 2343 1410 2557 91 206 160 A C ATOM 5132 C ALA A 635 15.516 17.980 43.657 1.00 16.30 A C ANISOU 5132 C ALA A 635 2234 1645 2312 273 240 192 A C ATOM 5133 O ALA A 635 14.961 18.247 44.720 1.00 18.71 A O ANISOU 5133 O ALA A 635 2834 1581 2694 392 677 254 A O ATOM 5134 CB ALA A 635 17.001 19.655 42.506 1.00 18.44 A C ANISOU 5134 CB ALA A 635 2691 1527 2786 102 401 336 A C ATOM 5135 N LYS A 636 14.916 17.265 42.690 1.00 15.58 A N ANISOU 5135 N LYS A 636 1817 1663 2440 433 353 130 A N ATOM 5136 CA LYS A 636 13.527 16.823 42.840 1.00 17.14 A C ANISOU 5136 CA LYS A 636 1774 1868 2869 401 589 152 A C ATOM 5137 C LYS A 636 13.406 15.806 43.980 1.00 16.25 A C ANISOU 5137 C LYS A 636 1676 1726 2769 388 293 5 A C ATOM 5138 O LYS A 636 12.473 15.867 44.808 1.00 17.56 A O ANISOU 5138 O LYS A 636 2120 1844 2708 460 435 180 A O ATOM 5139 CB LYS A 636 12.974 16.295 41.513 1.00 19.32 A C ANISOU 5139 CB LYS A 636 2047 2138 3152 -9 300 319 A C ATOM 5140 CG LYS A 636 12.787 17.342 40.412 1.00 27.91 A C ANISOU 5140 CG LYS A 636 2875 3390 4336 258 290 1305 A C ATOM 5141 CD LYS A 636 11.914 18.521 40.765 1.00 42.54 A C ANISOU 5141 CD LYS A 636 5163 5157 5841 1088 715 -223 A C ATOM 5142 N LEU A 637 14.369 14.889 44.073 1.00 14.99 A N ANISOU 5142 N LEU A 637 1770 1492 2431 344 699 52 A N ATOM 5143 CA LEU A 637 14.310 13.875 45.105 1.00 15.01 A C ANISOU 5143 CA LEU A 637 1704 1646 2353 241 437 186 A C ATOM 5144 C LEU A 637 14.703 14.401 46.485 1.00 14.59 A C ANISOU 5144 C LEU A 637 1669 1534 2341 254 506 82 A C ATOM 5145 O LEU A 637 14.292 13.845 47.492 1.00 16.00 A O ANISOU 5145 O LEU A 637 2274 1568 2234 403 512 122 A O ATOM 5146 CB LEU A 637 15.167 12.668 44.735 1.00 15.56 A C ANISOU 5146 CB LEU A 637 1944 1658 2306 300 440 123 A C ATOM 5147 CG LEU A 637 14.724 11.902 43.498 1.00 17.53 A C ANISOU 5147 CG LEU A 637 2435 2079 2144 455 39 240 A C ATOM 5148 CD1 LEU A 637 15.675 10.744 43.248 1.00 20.45 A C ANISOU 5148 CD1 LEU A 637 3185 1754 2831 603 144 211 A C ATOM 5149 CD2 LEU A 637 13.319 11.376 43.676 1.00 21.48 A C ANISOU 5149 CD2 LEU A 637 2961 2990 2209 -363 -134 78 A C ATOM 5150 N THR A 638 15.462 15.506 46.540 1.00 14.56 A N ANISOU 5150 N THR A 638 1982 1254 2294 327 479 183 A N ATOM 5151 CA THR A 638 15.737 16.133 47.798 1.00 15.66 A C ANISOU 5151 CA THR A 638 1968 1649 2330 350 378 -117 A C ATOM 5152 C THR A 638 14.407 16.638 48.415 1.00 16.18 A C ANISOU 5152 C THR A 638 1828 1906 2411 321 288 75 A C ATOM 5153 O THR A 638 14.148 16.462 49.613 1.00 16.19 A O ANISOU 5153 O THR A 638 2145 1432 2572 383 599 -154 A O ATOM 5154 CB THR A 638 16.753 17.263 47.650 1.00 18.29 A C ANISOU 5154 CB THR A 638 2143 2192 2614 224 615 -114 A C ATOM 5155 CG2 THR A 638 16.847 18.053 48.928 1.00 20.29 A C ANISOU 5155 CG2 THR A 638 2556 2428 2724 -84 965 -428 A C ATOM 5156 OG1 THR A 638 18.051 16.763 47.326 1.00 19.31 A O ANISOU 5156 OG1 THR A 638 1898 2685 2754 449 226 -36 A O ATOM 5157 N LYS A 639 13.559 17.249 47.577 1.00 15.45 A N ANISOU 5157 N LYS A 639 1728 1648 2491 414 336 196 A N ATOM 5158 CA ALYS A 639 12.205 17.680 47.998 0.50 16.35 A C ANISOU 5158 CA ALYS A 639 1771 1825 2613 415 458 284 A C ATOM 5159 CA BLYS A 639 12.220 17.670 47.999 0.50 16.66 A C ANISOU 5159 CA BLYS A 639 1803 1833 2693 349 530 172 A C ATOM 5160 C LYS A 639 11.393 16.474 48.501 1.00 15.26 A C ANISOU 5160 C LYS A 639 1636 1743 2418 369 297 130 A C ATOM 5161 O LYS A 639 10.768 16.540 49.575 1.00 16.26 A O ANISOU 5161 O LYS A 639 2054 1412 2710 409 661 19 A O ATOM 5162 CB ALYS A 639 11.466 18.435 46.883 0.50 18.53 A C ANISOU 5162 CB ALYS A 639 2062 1867 3109 938 475 440 A C ATOM 5163 CB BLYS A 639 11.537 18.449 46.874 0.50 19.98 A C ANISOU 5163 CB BLYS A 639 2302 2112 3178 815 384 289 A C ATOM 5164 CG ALYS A 639 10.027 18.843 47.195 0.50 21.43 A C ANISOU 5164 CG ALYS A 639 2042 2714 3384 860 753 617 A C ATOM 5165 CG BLYS A 639 12.160 19.815 46.657 0.50 25.04 A C ANISOU 5165 CG BLYS A 639 2768 2648 4097 232 870 239 A C ATOM 5166 CD ALYS A 639 9.290 19.497 46.020 0.50 24.67 A C ANISOU 5166 CD ALYS A 639 3055 2440 3878 1573 729 897 A C ATOM 5167 CD BLYS A 639 12.479 20.449 47.986 0.50 34.03 A C ANISOU 5167 CD BLYS A 639 4543 3915 4472 47 344 162 A C ATOM 5168 CE ALYS A 639 7.849 19.826 46.352 0.50 31.55 A C ANISOU 5168 CE ALYS A 639 2975 3699 5312 1509 769 1310 A C ATOM 5169 CE BLYS A 639 13.691 21.347 47.970 0.50 39.45 A C ANISOU 5169 CE BLYS A 639 5332 3606 6050 -486 382 -107 A C ATOM 5170 NZ ALYS A 639 7.394 21.058 45.662 0.50 36.71 A N ANISOU 5170 NZ ALYS A 639 4572 4297 5077 1966 1130 1753 A N ATOM 5171 NZ BLYS A 639 13.459 22.561 48.790 0.50 49.21 A N ANISOU 5171 NZ BLYS A 639 6957 3672 8069 -824 774 -655 A N ATOM 5172 N GLU A 640 11.460 15.349 47.763 1.00 15.27 A N ANISOU 5172 N GLU A 640 1577 1817 2407 466 564 95 A N ATOM 5173 CA GLU A 640 10.713 14.137 48.183 1.00 15.97 A C ANISOU 5173 CA GLU A 640 1635 1855 2576 235 355 13 A C ATOM 5174 C GLU A 640 11.281 13.566 49.499 1.00 14.71 A C ANISOU 5174 C GLU A 640 1902 1244 2443 117 376 -113 A C ATOM 5175 O GLU A 640 10.517 13.134 50.366 1.00 16.64 A O ANISOU 5175 O GLU A 640 1956 1399 2967 387 689 123 A O ATOM 5176 CB GLU A 640 10.702 13.083 47.081 1.00 16.92 A C ANISOU 5176 CB GLU A 640 1941 2038 2448 511 315 35 A C ATOM 5177 CG GLU A 640 10.027 13.503 45.815 1.00 17.47 A C ANISOU 5177 CG GLU A 640 2170 1789 2678 324 -47 -4 A C ATOM 5178 CD GLU A 640 8.569 13.918 45.975 1.00 20.24 A C ANISOU 5178 CD GLU A 640 2101 2578 3008 263 211 -130 A C ATOM 5179 OE1 GLU A 640 7.897 13.433 46.938 1.00 20.15 A O ANISOU 5179 OE1 GLU A 640 2195 2224 3235 316 282 -121 A O ATOM 5180 OE2 GLU A 640 8.080 14.695 45.111 1.00 26.18 A O ANISOU 5180 OE2 GLU A 640 2690 3176 4080 453 141 473 A O ATOM 5181 N PHE A 641 12.604 13.593 49.674 1.00 14.90 A N ANISOU 5181 N PHE A 641 1879 1471 2309 261 433 45 A N ATOM 5182 CA PHE A 641 13.249 13.181 50.921 1.00 14.02 A C ANISOU 5182 CA PHE A 641 1830 1279 2217 -61 374 -38 A C ATOM 5183 C PHE A 641 12.709 13.982 52.102 1.00 13.92 A C ANISOU 5183 C PHE A 641 1697 1478 2112 130 103 -44 A C ATOM 5184 O PHE A 641 12.355 13.431 53.165 1.00 14.91 A O ANISOU 5184 O PHE A 641 2001 1424 2240 307 457 -27 A O ATOM 5185 CB PHE A 641 14.775 13.228 50.840 1.00 13.82 A C ANISOU 5185 CB PHE A 641 1767 1248 2234 29 317 -146 A C ATOM 5186 CG PHE A 641 15.441 12.765 52.105 1.00 14.10 A C ANISOU 5186 CG PHE A 641 1732 1409 2215 150 345 -193 A C ATOM 5187 CD1 PHE A 641 15.650 13.639 53.157 1.00 13.84 A C ANISOU 5187 CD1 PHE A 641 1866 1277 2115 250 386 -145 A C ATOM 5188 CD2 PHE A 641 15.856 11.446 52.261 1.00 13.50 A C ANISOU 5188 CD2 PHE A 641 1560 1408 2159 86 423 -20 A C ATOM 5189 CE1 PHE A 641 16.227 13.214 54.333 1.00 14.51 A C ANISOU 5189 CE1 PHE A 641 1510 1499 2503 127 387 146 A C ATOM 5190 CE2 PHE A 641 16.418 11.031 53.449 1.00 14.03 A C ANISOU 5190 CE2 PHE A 641 1527 1588 2212 72 239 -142 A C ATOM 5191 CZ PHE A 641 16.578 11.892 54.486 1.00 14.08 A C ANISOU 5191 CZ PHE A 641 1825 1462 2063 353 276 -82 A C ATOM 5192 N GLN A 642 12.668 15.306 51.917 1.00 13.63 A N ANISOU 5192 N GLN A 642 1728 1375 2076 228 515 85 A N ATOM 5193 CA GLN A 642 12.168 16.228 52.945 1.00 16.15 A C ANISOU 5193 CA GLN A 642 2155 1389 2589 192 429 -230 A C ATOM 5194 C GLN A 642 10.706 15.913 53.290 1.00 14.55 A C ANISOU 5194 C GLN A 642 2170 842 2514 229 283 -358 A C ATOM 5195 O GLN A 642 10.355 15.792 54.480 1.00 16.06 A O ANISOU 5195 O GLN A 642 2094 1381 2626 442 556 -66 A O ATOM 5196 CB GLN A 642 12.353 17.669 52.473 1.00 15.28 A C ANISOU 5196 CB GLN A 642 2087 1401 2316 350 408 -48 A C ATOM 5197 CG GLN A 642 13.822 18.065 52.394 1.00 16.25 A C ANISOU 5197 CG GLN A 642 2137 1451 2585 223 375 -85 A C ATOM 5198 CD GLN A 642 14.062 19.328 51.604 1.00 16.56 A C ANISOU 5198 CD GLN A 642 1949 1482 2859 77 249 -13 A C ATOM 5199 NE2 GLN A 642 15.331 19.692 51.498 1.00 14.98 A N ANISOU 5199 NE2 GLN A 642 1722 1446 2524 300 374 -232 A N ATOM 5200 OE1 GLN A 642 13.133 19.922 51.057 1.00 18.43 A O ANISOU 5200 OE1 GLN A 642 2219 1724 3059 51 294 309 A O ATOM 5201 N LYS A 643 9.869 15.759 52.260 1.00 14.93 A N ANISOU 5201 N LYS A 643 2017 1388 2266 250 478 -47 A N ATOM 5202 CA LYS A 643 8.463 15.449 52.483 1.00 17.82 A C ANISOU 5202 CA LYS A 643 2039 1799 2933 78 430 -62 A C ATOM 5203 C LYS A 643 8.296 14.160 53.290 1.00 16.23 A C ANISOU 5203 C LYS A 643 1777 2029 2362 263 450 -110 A C ATOM 5204 O LYS A 643 7.409 14.071 54.134 1.00 18.34 A O ANISOU 5204 O LYS A 643 1970 2060 2937 306 849 155 A O ATOM 5205 CB LYS A 643 7.714 15.336 51.155 1.00 18.06 A C ANISOU 5205 CB LYS A 643 1906 2190 2766 368 450 116 A C ATOM 5206 CG LYS A 643 7.486 16.667 50.459 1.00 22.42 A C ANISOU 5206 CG LYS A 643 2683 2533 3301 273 814 567 A C ATOM 5207 CD LYS A 643 7.138 16.560 48.991 1.00 29.27 A C ANISOU 5207 CD LYS A 643 3373 4062 3683 928 251 22 A C ATOM 5208 CE LYS A 643 5.790 15.942 48.724 1.00 41.94 A C ANISOU 5208 CE LYS A 643 5076 4942 5915 109 -1364 -423 A C ATOM 5209 NZ LYS A 643 5.507 15.973 47.263 1.00 55.53 A N ANISOU 5209 NZ LYS A 643 7402 7396 6298 571 -2000 -1268 A N ATOM 5210 N ALA A 644 9.126 13.156 52.984 1.00 15.61 A N ANISOU 5210 N ALA A 644 1695 1820 2415 128 564 153 A N ATOM 5211 CA ALA A 644 8.977 11.857 53.611 1.00 15.37 A C ANISOU 5211 CA ALA A 644 1784 1544 2509 -213 461 -14 A C ATOM 5212 C ALA A 644 9.518 11.811 55.053 1.00 15.91 A C ANISOU 5212 C ALA A 644 1995 1567 2481 42 453 -219 A C ATOM 5213 O ALA A 644 8.918 11.128 55.905 1.00 18.02 A O ANISOU 5213 O ALA A 644 2019 2057 2771 188 684 229 A O ATOM 5214 CB ALA A 644 9.652 10.812 52.759 1.00 18.39 A C ANISOU 5214 CB ALA A 644 2195 1891 2900 184 498 -89 A C ATOM 5215 N TRP A 645 10.644 12.492 55.331 1.00 15.33 A N ANISOU 5215 N TRP A 645 2069 1067 2688 45 466 -115 A N ATOM 5216 CA TRP A 645 11.465 12.197 56.499 1.00 15.44 A C ANISOU 5216 CA TRP A 645 1945 1792 2129 91 669 -166 A C ATOM 5217 C TRP A 645 11.781 13.392 57.400 1.00 15.15 A C ANISOU 5217 C TRP A 645 2120 1472 2163 237 596 -45 A C ATOM 5218 O TRP A 645 12.319 13.189 58.486 1.00 15.97 A O ANISOU 5218 O TRP A 645 2259 1444 2361 125 419 -31 A O ATOM 5219 CB TRP A 645 12.782 11.527 56.069 1.00 14.29 A C ANISOU 5219 CB TRP A 645 1977 1151 2298 382 270 -82 A C ATOM 5220 CG TRP A 645 12.559 10.270 55.283 1.00 14.34 A C ANISOU 5220 CG TRP A 645 1933 1167 2346 263 493 -75 A C ATOM 5221 CD1 TRP A 645 12.937 10.056 53.994 1.00 13.30 A C ANISOU 5221 CD1 TRP A 645 1940 919 2191 154 336 -27 A C ATOM 5222 CD2 TRP A 645 11.872 9.066 55.705 1.00 15.11 A C ANISOU 5222 CD2 TRP A 645 1928 1411 2401 66 675 -149 A C ATOM 5223 CE2 TRP A 645 11.895 8.185 54.602 1.00 14.63 A C ANISOU 5223 CE2 TRP A 645 1803 1455 2298 169 479 -78 A C ATOM 5224 CE3 TRP A 645 11.216 8.656 56.877 1.00 16.01 A C ANISOU 5224 CE3 TRP A 645 2046 1542 2493 -5 568 -68 A C ATOM 5225 NE1 TRP A 645 12.586 8.801 53.594 1.00 13.89 A N ANISOU 5225 NE1 TRP A 645 1951 1079 2245 177 394 -206 A N ATOM 5226 CZ2 TRP A 645 11.357 6.902 54.653 1.00 15.48 A C ANISOU 5226 CZ2 TRP A 645 2142 1160 2577 353 355 -149 A C ATOM 5227 CZ3 TRP A 645 10.680 7.384 56.926 1.00 17.16 A C ANISOU 5227 CZ3 TRP A 645 2233 1660 2626 -66 802 -98 A C ATOM 5228 CH2 TRP A 645 10.709 6.544 55.815 1.00 17.23 A C ANISOU 5228 CH2 TRP A 645 2281 1605 2658 102 471 -195 A C ATOM 5229 N ILE A 646 11.472 14.617 56.968 1.00 14.84 A N ANISOU 5229 N ILE A 646 2090 1639 1906 246 502 17 A N ATOM 5230 CA ILE A 646 11.821 15.816 57.743 1.00 16.47 A C ANISOU 5230 CA ILE A 646 1925 1931 2402 261 554 -446 A C ATOM 5231 C ILE A 646 10.536 16.604 58.000 1.00 14.61 A C ANISOU 5231 C ILE A 646 1788 1296 2467 10 341 -233 A C ATOM 5232 O ILE A 646 9.808 16.946 57.047 1.00 17.33 A O ANISOU 5232 O ILE A 646 2340 1895 2348 539 488 -178 A O ATOM 5233 CB ILE A 646 12.867 16.693 57.037 1.00 17.29 A C ANISOU 5233 CB ILE A 646 2348 1699 2521 421 675 -256 A C ATOM 5234 CG1 ILE A 646 14.086 15.894 56.592 1.00 14.96 A C ANISOU 5234 CG1 ILE A 646 1962 1572 2149 349 432 41 A C ATOM 5235 CG2 ILE A 646 13.271 17.807 57.973 1.00 19.49 A C ANISOU 5235 CG2 ILE A 646 2972 1805 2626 48 719 -332 A C ATOM 5236 CD1 ILE A 646 15.205 16.680 56.003 1.00 16.46 A C ANISOU 5236 CD1 ILE A 646 2108 1574 2572 270 439 62 A C ATOM 5237 N THR A 647 10.245 16.875 59.274 1.00 15.34 A N ANISOU 5237 N THR A 647 2014 1520 2295 157 294 -58 A N ATOM 5238 CA THR A 647 9.050 17.673 59.597 1.00 16.83 A C ANISOU 5238 CA THR A 647 2470 1580 2345 272 563 -446 A C ATOM 5239 C THR A 647 9.260 19.113 59.126 1.00 17.78 A C ANISOU 5239 C THR A 647 2461 1755 2537 120 609 -332 A C ATOM 5240 O THR A 647 10.385 19.525 58.879 1.00 17.63 A O ANISOU 5240 O THR A 647 2292 1433 2972 416 700 -331 A O ATOM 5241 CB THR A 647 8.757 17.673 61.105 1.00 16.74 A C ANISOU 5241 CB THR A 647 2179 1882 2297 506 378 -135 A C ATOM 5242 CG2 THR A 647 8.667 16.278 61.658 1.00 18.73 A C ANISOU 5242 CG2 THR A 647 2570 1936 2608 243 547 -96 A C ATOM 5243 OG1 THR A 647 9.787 18.379 61.800 1.00 18.34 A O ANISOU 5243 OG1 THR A 647 2252 1841 2874 328 538 -362 A O ATOM 5244 N SER A 648 8.168 19.879 59.095 1.00 17.86 A N ANISOU 5244 N SER A 648 2408 1737 2638 119 746 -276 A N ATOM 5245 CA ASER A 648 8.219 21.252 58.615 0.50 18.25 A C ANISOU 5245 CA ASER A 648 2543 1707 2682 282 450 -296 A C ATOM 5246 CA BSER A 648 8.199 21.261 58.640 0.50 18.40 A C ANISOU 5246 CA BSER A 648 2605 1693 2692 221 463 -345 A C ATOM 5247 C SER A 648 9.255 22.074 59.395 1.00 18.34 A C ANISOU 5247 C SER A 648 2353 1859 2754 507 373 -461 A C ATOM 5248 O SER A 648 9.950 22.892 58.785 1.00 18.09 A O ANISOU 5248 O SER A 648 2461 1703 2710 405 202 -332 A O ATOM 5249 CB ASER A 648 6.862 21.896 58.657 0.50 20.47 A C ANISOU 5249 CB ASER A 648 2380 2243 3154 332 107 156 A C ATOM 5250 CB BSER A 648 6.841 21.889 58.752 0.50 20.19 A C ANISOU 5250 CB BSER A 648 2326 2232 3111 190 53 -70 A C ATOM 5251 OG ASER A 648 6.398 21.976 59.990 0.50 22.79 A O ANISOU 5251 OG ASER A 648 2648 2616 3392 762 418 -74 A O ATOM 5252 OG BSER A 648 5.954 21.272 57.837 0.50 24.15 A O ANISOU 5252 OG BSER A 648 2677 2645 3854 206 -173 -706 A O ATOM 5253 N ASN A 649 9.373 21.839 60.702 1.00 17.91 A N ANISOU 5253 N ASN A 649 2428 1636 2739 639 468 -663 A N ATOM 5254 CA ASN A 649 10.311 22.593 61.534 1.00 19.07 A C ANISOU 5254 CA ASN A 649 2507 1803 2936 482 276 -450 A C ATOM 5255 C ASN A 649 11.738 22.031 61.527 1.00 17.93 A C ANISOU 5255 C ASN A 649 2711 1287 2815 546 132 -375 A C ATOM 5256 O ASN A 649 12.593 22.528 62.265 1.00 19.49 A O ANISOU 5256 O ASN A 649 2760 1830 2815 540 12 -309 A O ATOM 5257 CB ASN A 649 9.822 22.767 62.975 1.00 19.73 A C ANISOU 5257 CB ASN A 649 2963 1703 2828 669 290 -479 A C ATOM 5258 CG ASN A 649 9.803 21.508 63.802 1.00 19.48 A C ANISOU 5258 CG ASN A 649 2751 1958 2691 703 800 -482 A C ATOM 5259 ND2 ASN A 649 9.104 21.579 64.920 1.00 21.62 A N ANISOU 5259 ND2 ASN A 649 3454 2016 2744 810 1048 -384 A N ATOM 5260 OD1 ASN A 649 10.424 20.505 63.471 1.00 21.40 A O ANISOU 5260 OD1 ASN A 649 2962 1834 3335 882 775 -335 A O ATOM 5261 N GLY A 650 12.013 20.977 60.749 1.00 16.19 A N ANISOU 5261 N GLY A 650 2265 940 2944 283 419 -253 A N ATOM 5262 CA GLY A 650 13.382 20.513 60.568 1.00 16.24 A C ANISOU 5262 CA GLY A 650 2245 1024 2901 204 647 -233 A C ATOM 5263 C GLY A 650 13.779 19.309 61.421 1.00 15.85 A C ANISOU 5263 C GLY A 650 2254 1170 2597 287 641 -274 A C ATOM 5264 O GLY A 650 14.981 19.071 61.564 1.00 18.46 A O ANISOU 5264 O GLY A 650 2195 1832 2985 292 631 -88 A O ATOM 5265 N THR A 651 12.800 18.630 62.046 1.00 16.53 A N ANISOU 5265 N THR A 651 1964 1688 2627 479 712 -260 A N ATOM 5266 CA THR A 651 13.039 17.448 62.868 1.00 17.64 A C ANISOU 5266 CA THR A 651 2467 1373 2861 164 636 -207 A C ATOM 5267 C THR A 651 13.024 16.175 62.009 1.00 15.97 A C ANISOU 5267 C THR A 651 2026 1562 2481 -33 326 -121 A C ATOM 5268 O THR A 651 12.167 15.999 61.168 1.00 16.03 A O ANISOU 5268 O THR A 651 2432 1369 2286 436 252 -23 A O ATOM 5269 CB THR A 651 11.968 17.344 63.967 1.00 17.99 A C ANISOU 5269 CB THR A 651 2797 1388 2647 418 600 -141 A C ATOM 5270 CG2 THR A 651 12.238 16.205 64.922 1.00 19.75 A C ANISOU 5270 CG2 THR A 651 3115 1619 2770 584 683 37 A C ATOM 5271 OG1 THR A 651 11.941 18.583 64.679 1.00 19.24 A O ANISOU 5271 OG1 THR A 651 3028 1698 2582 495 678 -425 A O ATOM 5272 N MET A 652 14.003 15.293 62.236 1.00 15.76 A N ANISOU 5272 N MET A 652 2142 1427 2417 45 185 -325 A N ATOM 5273 CA MET A 652 14.034 14.035 61.509 1.00 15.89 A C ANISOU 5273 CA MET A 652 2207 1461 2368 86 153 -383 A C ATOM 5274 C MET A 652 12.977 13.072 62.074 1.00 16.93 A C ANISOU 5274 C MET A 652 2775 1355 2300 215 520 -139 A C ATOM 5275 O MET A 652 12.701 13.082 63.287 1.00 17.80 A O ANISOU 5275 O MET A 652 2883 1535 2342 264 619 -239 A O ATOM 5276 CB MET A 652 15.405 13.384 61.642 1.00 17.35 A C ANISOU 5276 CB MET A 652 2390 1601 2600 453 566 -190 A C ATOM 5277 CG MET A 652 16.514 14.182 60.967 1.00 16.22 A C ANISOU 5277 CG MET A 652 1896 1391 2875 419 387 -440 A C ATOM 5278 SD MET A 652 16.212 14.639 59.243 1.00 16.87 A S ANISOU 5278 SD MET A 652 2382 1216 2810 183 624 -200 A S ATOM 5279 CE MET A 652 15.942 13.025 58.540 1.00 15.12 A C ANISOU 5279 CE MET A 652 2318 973 2451 316 585 41 A C ATOM 5280 N ALA A 653 12.450 12.195 61.204 1.00 17.62 A N ANISOU 5280 N ALA A 653 2445 1679 2568 -3 724 -196 A N ATOM 5281 CA ALA A 653 11.497 11.172 61.631 1.00 17.96 A C ANISOU 5281 CA ALA A 653 2452 1888 2482 24 908 -119 A C ATOM 5282 C ALA A 653 12.095 10.328 62.775 1.00 17.35 A C ANISOU 5282 C ALA A 653 2349 1607 2635 110 796 -246 A C ATOM 5283 O ALA A 653 11.388 9.973 63.727 1.00 19.62 A O ANISOU 5283 O ALA A 653 2514 1962 2975 87 1234 -124 A O ATOM 5284 CB ALA A 653 11.098 10.309 60.455 1.00 18.96 A C ANISOU 5284 CB ALA A 653 2916 1776 2509 38 593 -96 A C ATOM 5285 N ASN A 654 13.392 10.037 62.683 1.00 17.52 A N ANISOU 5285 N ASN A 654 2327 1862 2466 168 749 -313 A N ATOM 5286 CA ASN A 654 14.155 9.393 63.770 1.00 17.77 A C ANISOU 5286 CA ASN A 654 2330 1737 2682 474 496 -320 A C ATOM 5287 C ASN A 654 15.340 10.285 64.148 1.00 18.71 A C ANISOU 5287 C ASN A 654 2628 1982 2499 210 331 -29 A C ATOM 5288 O ASN A 654 16.276 10.457 63.370 1.00 17.14 A O ANISOU 5288 O ASN A 654 2790 1188 2532 143 305 -150 A O ATOM 5289 CB ASN A 654 14.646 7.993 63.373 1.00 17.33 A C ANISOU 5289 CB ASN A 654 2539 1666 2377 200 728 -305 A C ATOM 5290 CG ASN A 654 13.570 7.156 62.733 1.00 19.71 A C ANISOU 5290 CG ASN A 654 2661 2172 2656 -55 604 -208 A C ATOM 5291 ND2 ASN A 654 12.430 7.003 63.410 1.00 21.06 A N ANISOU 5291 ND2 ASN A 654 2912 1729 3360 -114 1001 -81 A N ATOM 5292 OD1 ASN A 654 13.769 6.673 61.639 1.00 19.72 A O ANISOU 5292 OD1 ASN A 654 2713 1855 2924 110 433 -398 A O ATOM 5293 N GLU A 655 15.300 10.830 65.366 1.00 18.89 A N ANISOU 5293 N GLU A 655 2593 1908 2676 66 861 -210 A N ATOM 5294 CA GLU A 655 16.371 11.681 65.882 1.00 18.42 A C ANISOU 5294 CA GLU A 655 3046 1540 2413 166 570 -388 A C ATOM 5295 C GLU A 655 17.432 10.813 66.576 1.00 18.86 A C ANISOU 5295 C GLU A 655 3036 1688 2442 273 783 -93 A C ATOM 5296 O GLU A 655 17.528 10.730 67.782 1.00 20.84 A O ANISOU 5296 O GLU A 655 3429 1910 2578 539 497 -504 A O ATOM 5297 CB GLU A 655 15.783 12.735 66.820 1.00 19.35 A C ANISOU 5297 CB GLU A 655 3087 1572 2691 475 629 -391 A C ATOM 5298 CG GLU A 655 15.004 13.838 66.116 1.00 18.94 A C ANISOU 5298 CG GLU A 655 2666 1741 2788 231 730 -219 A C ATOM 5299 CD GLU A 655 15.842 15.044 65.690 1.00 19.87 A C ANISOU 5299 CD GLU A 655 2556 2015 2979 257 425 94 A C ATOM 5300 OE1 GLU A 655 16.607 15.520 66.526 1.00 20.60 A O ANISOU 5300 OE1 GLU A 655 3011 1874 2941 193 349 -305 A O ATOM 5301 OE2 GLU A 655 15.753 15.450 64.476 1.00 18.48 A O ANISOU 5301 OE2 GLU A 655 2740 1355 2927 400 515 -187 A O ATOM 5302 N THR A 656 18.208 10.140 65.731 1.00 16.24 A N ANISOU 5302 N THR A 656 2432 1749 1990 92 527 -30 A N ATOM 5303 CA THR A 656 19.255 9.209 66.088 1.00 15.84 A C ANISOU 5303 CA THR A 656 2616 1285 2115 87 379 -295 A C ATOM 5304 C THR A 656 20.561 9.681 65.458 1.00 15.56 A C ANISOU 5304 C THR A 656 2540 1308 2063 37 99 -40 A C ATOM 5305 O THR A 656 20.573 10.585 64.611 1.00 14.99 A O ANISOU 5305 O THR A 656 2447 1161 2085 284 558 -7 A O ATOM 5306 CB THR A 656 18.929 7.815 65.558 1.00 14.74 A C ANISOU 5306 CB THR A 656 2382 1133 2082 59 399 -177 A C ATOM 5307 CG2 THR A 656 17.642 7.274 66.150 1.00 15.74 A C ANISOU 5307 CG2 THR A 656 2287 1372 2319 132 359 -179 A C ATOM 5308 OG1 THR A 656 18.828 7.873 64.123 1.00 15.69 A O ANISOU 5308 OG1 THR A 656 2612 1324 2025 -87 382 97 A O ATOM 5309 N GLN A 657 21.673 9.114 65.904 1.00 15.15 A N ANISOU 5309 N GLN A 657 2512 1345 1896 41 293 -21 A N ATOM 5310 CA GLN A 657 22.948 9.495 65.355 1.00 14.98 A C ANISOU 5310 CA GLN A 657 2414 1178 2100 143 224 -254 A C ATOM 5311 C GLN A 657 22.932 9.329 63.833 1.00 14.95 A C ANISOU 5311 C GLN A 657 2419 1306 1954 43 339 -203 A C ATOM 5312 O GLN A 657 23.365 10.230 63.115 1.00 14.93 A O ANISOU 5312 O GLN A 657 2480 1257 1936 160 283 -169 A O ATOM 5313 CB GLN A 657 24.085 8.751 66.035 1.00 16.06 A C ANISOU 5313 CB GLN A 657 2320 1515 2265 278 68 -336 A C ATOM 5314 CG GLN A 657 24.292 9.185 67.473 1.00 16.97 A C ANISOU 5314 CG GLN A 657 2630 1519 2298 45 -24 -325 A C ATOM 5315 CD GLN A 657 25.496 8.540 68.111 1.00 16.62 A C ANISOU 5315 CD GLN A 657 2619 1369 2324 -94 141 -94 A C ATOM 5316 NE2 GLN A 657 25.418 8.386 69.433 1.00 17.83 A N ANISOU 5316 NE2 GLN A 657 3599 1059 2115 178 143 -384 A N ATOM 5317 OE1 GLN A 657 26.463 8.168 67.433 1.00 16.96 A O ANISOU 5317 OE1 GLN A 657 2813 1687 1945 -103 234 -32 A O ATOM 5318 N THR A 658 22.504 8.157 63.336 1.00 14.11 A N ANISOU 5318 N THR A 658 2444 1177 1740 139 203 -150 A N ATOM 5319 CA THR A 658 22.475 7.959 61.880 1.00 12.95 A C ANISOU 5319 CA THR A 658 2054 1095 1770 -57 231 -1 A C ATOM 5320 C THR A 658 21.395 8.824 61.203 1.00 14.01 A C ANISOU 5320 C THR A 658 2018 1273 2029 84 280 -162 A C ATOM 5321 O THR A 658 21.625 9.375 60.108 1.00 14.24 A O ANISOU 5321 O THR A 658 2224 1083 2100 64 465 -237 A O ATOM 5322 CB THR A 658 22.287 6.480 61.543 1.00 14.17 A C ANISOU 5322 CB THR A 658 2117 1182 2083 -148 170 -241 A C ATOM 5323 CG2 THR A 658 22.100 6.221 60.070 1.00 13.86 A C ANISOU 5323 CG2 THR A 658 2078 1073 2113 118 205 -103 A C ATOM 5324 OG1 THR A 658 23.448 5.809 62.025 1.00 14.88 A O ANISOU 5324 OG1 THR A 658 2337 1456 1859 215 55 -207 A O ATOM 5325 N GLY A 659 20.218 8.910 61.822 1.00 13.84 A N ANISOU 5325 N GLY A 659 1937 1622 1697 -69 442 118 A N ATOM 5326 CA GLY A 659 19.113 9.654 61.246 1.00 14.15 A C ANISOU 5326 CA GLY A 659 2267 1148 1961 223 509 -161 A C ATOM 5327 C GLY A 659 19.393 11.145 61.040 1.00 14.15 A C ANISOU 5327 C GLY A 659 1956 1235 2182 112 506 -177 A C ATOM 5328 O GLY A 659 18.879 11.724 60.065 1.00 14.98 A O ANISOU 5328 O GLY A 659 2139 1254 2296 105 222 -338 A O ATOM 5329 N LEU A 660 20.239 11.712 61.907 1.00 14.31 A N ANISOU 5329 N LEU A 660 2173 1263 2001 -66 656 26 A N ATOM 5330 CA LEU A 660 20.699 13.079 61.743 1.00 14.31 A C ANISOU 5330 CA LEU A 660 2239 1125 2072 -37 223 -15 A C ATOM 5331 C LEU A 660 21.953 13.135 60.861 1.00 14.12 A C ANISOU 5331 C LEU A 660 2088 1249 2029 129 239 -83 A C ATOM 5332 O LEU A 660 22.112 14.035 60.058 1.00 13.98 A O ANISOU 5332 O LEU A 660 2212 989 2109 142 314 -184 A O ATOM 5333 CB LEU A 660 20.968 13.682 63.116 1.00 14.67 A C ANISOU 5333 CB LEU A 660 2054 1296 2223 146 247 -142 A C ATOM 5334 CG LEU A 660 19.705 14.079 63.871 1.00 15.81 A C ANISOU 5334 CG LEU A 660 1930 1632 2442 297 147 -361 A C ATOM 5335 CD1 LEU A 660 19.973 14.076 65.353 1.00 17.62 A C ANISOU 5335 CD1 LEU A 660 2269 2056 2369 485 566 -361 A C ATOM 5336 CD2 LEU A 660 19.185 15.420 63.396 1.00 19.45 A C ANISOU 5336 CD2 LEU A 660 2313 1693 3382 350 511 -64 A C ATOM 5337 N ALA A 661 22.917 12.233 61.070 1.00 13.80 A N ANISOU 5337 N ALA A 661 2067 1071 2102 86 480 -239 A N ATOM 5338 CA ALA A 661 24.214 12.367 60.381 1.00 12.97 A C ANISOU 5338 CA ALA A 661 1763 1060 2105 64 180 -241 A C ATOM 5339 C ALA A 661 24.030 12.293 58.858 1.00 13.81 A C ANISOU 5339 C ALA A 661 1869 1391 1985 162 220 -325 A C ATOM 5340 O ALA A 661 24.668 13.022 58.091 1.00 13.59 A O ANISOU 5340 O ALA A 661 1964 1115 2085 233 113 -118 A O ATOM 5341 CB ALA A 661 25.190 11.327 60.850 1.00 14.87 A C ANISOU 5341 CB ALA A 661 1923 1544 2182 326 201 -115 A C ATOM 5342 N LEU A 662 23.178 11.381 58.381 1.00 13.41 A N ANISOU 5342 N LEU A 662 2091 956 2046 115 287 -170 A N ATOM 5343 CA LEU A 662 23.043 11.233 56.916 1.00 12.80 A C ANISOU 5343 CA LEU A 662 1675 1227 1958 207 212 -232 A C ATOM 5344 C LEU A 662 22.527 12.494 56.226 1.00 11.93 A C ANISOU 5344 C LEU A 662 1715 1311 1506 114 229 -253 A C ATOM 5345 O LEU A 662 23.176 12.943 55.259 1.00 12.88 A O ANISOU 5345 O LEU A 662 1896 1092 1902 134 408 -121 A O ATOM 5346 CB LEU A 662 22.228 9.990 56.561 1.00 12.93 A C ANISOU 5346 CB LEU A 662 1735 1056 2122 234 339 -168 A C ATOM 5347 CG LEU A 662 22.783 8.664 57.048 1.00 13.45 A C ANISOU 5347 CG LEU A 662 2011 1065 2032 151 165 -79 A C ATOM 5348 CD1 LEU A 662 21.897 7.516 56.603 1.00 14.57 A C ANISOU 5348 CD1 LEU A 662 2057 1255 2223 18 348 -259 A C ATOM 5349 CD2 LEU A 662 24.214 8.455 56.564 1.00 13.42 A C ANISOU 5349 CD2 LEU A 662 2051 937 2110 23 24 23 A C ATOM 5350 N PRO A 663 21.369 13.075 56.623 1.00 12.78 A N ANISOU 5350 N PRO A 663 1866 1020 1967 265 300 -1 A N ATOM 5351 CA PRO A 663 20.956 14.301 55.950 1.00 12.71 A C ANISOU 5351 CA PRO A 663 2019 856 1952 276 473 -46 A C ATOM 5352 C PRO A 663 21.912 15.491 56.172 1.00 13.80 A C ANISOU 5352 C PRO A 663 1939 1481 1823 206 284 -368 A C ATOM 5353 O PRO A 663 21.990 16.337 55.314 1.00 14.21 A O ANISOU 5353 O PRO A 663 2055 1374 1967 365 195 -196 A O ATOM 5354 CB PRO A 663 19.548 14.537 56.507 1.00 12.95 A C ANISOU 5354 CB PRO A 663 1958 1078 1885 362 443 -142 A C ATOM 5355 CG PRO A 663 19.589 13.876 57.865 1.00 13.60 A C ANISOU 5355 CG PRO A 663 1948 1307 1912 340 628 -46 A C ATOM 5356 CD PRO A 663 20.390 12.619 57.634 1.00 12.95 A C ANISOU 5356 CD PRO A 663 2063 847 2009 16 374 -341 A C ATOM 5357 N LEU A 664 22.665 15.507 57.273 1.00 13.55 A N ANISOU 5357 N LEU A 664 2045 1244 1859 228 169 -151 A N ATOM 5358 CA LEU A 664 23.676 16.524 57.463 1.00 14.16 A C ANISOU 5358 CA LEU A 664 2020 1283 2074 119 221 -147 A C ATOM 5359 C LEU A 664 24.820 16.346 56.465 1.00 14.50 A C ANISOU 5359 C LEU A 664 2108 1331 2069 166 240 -106 A C ATOM 5360 O LEU A 664 25.228 17.294 55.793 1.00 16.18 A O ANISOU 5360 O LEU A 664 2247 1374 2525 174 572 19 A O ATOM 5361 CB LEU A 664 24.190 16.498 58.901 1.00 14.06 A C ANISOU 5361 CB LEU A 664 1968 1394 1977 338 305 -237 A C ATOM 5362 CG LEU A 664 23.213 17.065 59.938 1.00 13.41 A C ANISOU 5362 CG LEU A 664 2013 928 2152 221 285 -383 A C ATOM 5363 CD1 LEU A 664 23.703 16.757 61.349 1.00 15.65 A C ANISOU 5363 CD1 LEU A 664 2605 1379 1961 484 247 -679 A C ATOM 5364 CD2 LEU A 664 23.029 18.559 59.743 1.00 14.39 A C ANISOU 5364 CD2 LEU A 664 1993 968 2505 351 306 -377 A C ATOM 5365 N TYR A 665 25.353 15.132 56.333 1.00 13.57 A N ANISOU 5365 N TYR A 665 1985 1222 1949 76 271 -181 A N ATOM 5366 CA TYR A 665 26.507 14.945 55.452 1.00 12.36 A C ANISOU 5366 CA TYR A 665 1868 821 2006 10 235 -59 A C ATOM 5367 C TYR A 665 26.096 15.085 53.979 1.00 11.81 A C ANISOU 5367 C TYR A 665 1504 945 2039 445 283 -34 A C ATOM 5368 O TYR A 665 26.887 15.569 53.136 1.00 13.88 A O ANISOU 5368 O TYR A 665 1814 1418 2041 84 366 -2 A O ATOM 5369 CB TYR A 665 27.141 13.570 55.680 1.00 13.50 A C ANISOU 5369 CB TYR A 665 2082 1022 2023 272 73 -116 A C ATOM 5370 CG TYR A 665 28.523 13.478 55.116 1.00 15.76 A C ANISOU 5370 CG TYR A 665 1908 1560 2519 316 55 9 A C ATOM 5371 CD1 TYR A 665 29.561 14.164 55.702 1.00 17.45 A C ANISOU 5371 CD1 TYR A 665 2013 2370 2247 204 184 -199 A C ATOM 5372 CD2 TYR A 665 28.771 12.774 53.950 1.00 18.00 A C ANISOU 5372 CD2 TYR A 665 2052 1684 3101 77 324 -287 A C ATOM 5373 CE1 TYR A 665 30.829 14.143 55.151 1.00 18.11 A C ANISOU 5373 CE1 TYR A 665 1798 2666 2415 -401 -50 50 A C ATOM 5374 CE2 TYR A 665 30.033 12.739 53.385 1.00 18.94 A C ANISOU 5374 CE2 TYR A 665 2291 1971 2933 172 609 -334 A C ATOM 5375 CZ TYR A 665 31.071 13.413 54.009 1.00 17.33 A C ANISOU 5375 CZ TYR A 665 2038 1699 2847 230 448 143 A C ATOM 5376 OH TYR A 665 32.322 13.441 53.491 1.00 21.44 A O ANISOU 5376 OH TYR A 665 2200 2095 3851 647 840 149 A O ATOM 5377 N PHE A 666 24.874 14.623 53.654 1.00 12.48 A N ANISOU 5377 N PHE A 666 1627 1159 1952 67 425 -165 A N ATOM 5378 CA PHE A 666 24.380 14.619 52.286 1.00 13.43 A C ANISOU 5378 CA PHE A 666 1822 1186 2094 152 193 -90 A C ATOM 5379 C PHE A 666 23.666 15.931 51.900 1.00 13.55 A C ANISOU 5379 C PHE A 666 1697 1323 2125 149 210 -33 A C ATOM 5380 O PHE A 666 23.198 16.063 50.766 1.00 14.25 A O ANISOU 5380 O PHE A 666 1703 1367 2342 299 113 -47 A O ATOM 5381 CB PHE A 666 23.479 13.403 52.042 1.00 13.56 A C ANISOU 5381 CB PHE A 666 1821 1250 2081 225 236 -372 A C ATOM 5382 CG PHE A 666 24.125 12.036 52.212 1.00 13.64 A C ANISOU 5382 CG PHE A 666 1831 1258 2093 179 360 -167 A C ATOM 5383 CD1 PHE A 666 25.488 11.822 52.084 1.00 13.09 A C ANISOU 5383 CD1 PHE A 666 1941 1067 1965 444 134 -369 A C ATOM 5384 CD2 PHE A 666 23.323 10.961 52.522 1.00 13.79 A C ANISOU 5384 CD2 PHE A 666 1724 1220 2293 267 349 -22 A C ATOM 5385 CE1 PHE A 666 26.033 10.553 52.236 1.00 13.90 A C ANISOU 5385 CE1 PHE A 666 1919 1104 2259 364 223 -242 A C ATOM 5386 CE2 PHE A 666 23.857 9.699 52.699 1.00 14.19 A C ANISOU 5386 CE2 PHE A 666 2122 1080 2187 274 155 -162 A C ATOM 5387 CZ PHE A 666 25.209 9.507 52.560 1.00 15.00 A C ANISOU 5387 CZ PHE A 666 2076 1211 2410 118 129 -224 A C ATOM 5388 N ASP A 667 23.591 16.879 52.842 1.00 13.70 A N ANISOU 5388 N ASP A 667 1843 1102 2259 123 204 -84 A N ATOM 5389 CA ASP A 667 23.073 18.258 52.604 1.00 15.16 A C ANISOU 5389 CA ASP A 667 2187 1033 2538 12 235 189 A C ATOM 5390 C ASP A 667 21.608 18.206 52.132 1.00 14.73 A C ANISOU 5390 C ASP A 667 2155 1258 2183 211 317 -170 A C ATOM 5391 O ASP A 667 21.227 18.780 51.106 1.00 16.42 A O ANISOU 5391 O ASP A 667 1986 1544 2710 186 209 28 A O ATOM 5392 CB ASP A 667 23.971 19.034 51.633 1.00 16.22 A C ANISOU 5392 CB ASP A 667 2209 1004 2948 103 458 -59 A C ATOM 5393 CG ASP A 667 25.368 19.306 52.140 1.00 20.37 A C ANISOU 5393 CG ASP A 667 2502 1927 3309 -410 332 273 A C ATOM 5394 OD1 ASP A 667 25.497 19.802 53.282 1.00 28.12 A O ANISOU 5394 OD1 ASP A 667 2941 3964 3780 -522 290 -468 A O ATOM 5395 OD2 ASP A 667 26.321 19.075 51.372 1.00 37.08 A O ANISOU 5395 OD2 ASP A 667 3523 4996 5567 213 1349 -1292 A O ATOM 5396 N LEU A 668 20.757 17.537 52.922 1.00 13.17 A N ANISOU 5396 N LEU A 668 1806 1126 2069 304 222 -203 A N ATOM 5397 CA LEU A 668 19.370 17.278 52.531 1.00 13.33 A C ANISOU 5397 CA LEU A 668 1870 1044 2150 -29 110 -117 A C ATOM 5398 C LEU A 668 18.348 18.162 53.275 1.00 15.89 A C ANISOU 5398 C LEU A 668 1993 1446 2598 183 27 -374 A C ATOM 5399 O LEU A 668 17.169 18.035 53.011 1.00 14.76 A O ANISOU 5399 O LEU A 668 1881 1251 2474 144 360 -177 A O ATOM 5400 CB LEU A 668 19.034 15.795 52.779 1.00 14.31 A C ANISOU 5400 CB LEU A 668 1954 1007 2476 132 193 -6 A C ATOM 5401 CG LEU A 668 19.917 14.812 52.007 1.00 15.06 A C ANISOU 5401 CG LEU A 668 2148 1214 2360 283 64 -108 A C ATOM 5402 CD1 LEU A 668 19.499 13.373 52.255 1.00 15.75 A C ANISOU 5402 CD1 LEU A 668 1812 1163 3007 222 -112 -249 A C ATOM 5403 CD2 LEU A 668 19.890 15.113 50.519 1.00 13.85 A C ANISOU 5403 CD2 LEU A 668 1713 1265 2282 -2 390 -305 A C ATOM 5404 N PHE A 669 18.801 19.061 54.160 1.00 15.45 A N ANISOU 5404 N PHE A 669 1922 1441 2504 304 82 -422 A N ATOM 5405 CA PHE A 669 17.876 19.979 54.857 1.00 16.41 A C ANISOU 5405 CA PHE A 669 2230 1500 2503 340 340 -429 A C ATOM 5406 C PHE A 669 17.513 21.099 53.896 1.00 16.33 A C ANISOU 5406 C PHE A 669 2246 1261 2694 156 570 -375 A C ATOM 5407 O PHE A 669 18.283 21.427 52.996 1.00 17.24 A O ANISOU 5407 O PHE A 669 2481 1286 2781 396 600 -31 A O ATOM 5408 CB PHE A 669 18.487 20.523 56.155 1.00 15.62 A C ANISOU 5408 CB PHE A 669 2093 1436 2406 393 385 -461 A C ATOM 5409 CG PHE A 669 18.523 19.504 57.258 1.00 15.83 A C ANISOU 5409 CG PHE A 669 2065 1553 2394 71 505 -346 A C ATOM 5410 CD1 PHE A 669 17.432 19.301 58.083 1.00 16.56 A C ANISOU 5410 CD1 PHE A 669 2249 1462 2579 196 598 -141 A C ATOM 5411 CD2 PHE A 669 19.637 18.689 57.427 1.00 16.55 A C ANISOU 5411 CD2 PHE A 669 1877 1828 2582 71 433 -40 A C ATOM 5412 CE1 PHE A 669 17.443 18.302 59.046 1.00 17.52 A C ANISOU 5412 CE1 PHE A 669 2339 1981 2337 24 160 37 A C ATOM 5413 CE2 PHE A 669 19.638 17.709 58.403 1.00 17.12 A C ANISOU 5413 CE2 PHE A 669 2332 1524 2646 251 265 -310 A C ATOM 5414 CZ PHE A 669 18.564 17.542 59.234 1.00 17.70 A C ANISOU 5414 CZ PHE A 669 2636 1458 2630 118 373 -43 A C ATOM 5415 N PRO A 670 16.316 21.690 54.032 1.00 17.51 A N ANISOU 5415 N PRO A 670 2359 1592 2701 569 435 -71 A N ATOM 5416 CA PRO A 670 15.909 22.768 53.130 1.00 17.78 A C ANISOU 5416 CA PRO A 670 2579 1446 2730 427 255 -226 A C ATOM 5417 C PRO A 670 16.598 24.120 53.334 1.00 17.64 A C ANISOU 5417 C PRO A 670 2563 1493 2646 471 58 -336 A C ATOM 5418 O PRO A 670 16.431 24.987 52.501 1.00 22.03 A O ANISOU 5418 O PRO A 670 3045 2250 3073 252 78 157 A O ATOM 5419 CB PRO A 670 14.402 22.878 53.381 1.00 19.03 A C ANISOU 5419 CB PRO A 670 2466 1570 3194 522 -294 -428 A C ATOM 5420 CG PRO A 670 14.186 22.366 54.763 1.00 22.10 A C ANISOU 5420 CG PRO A 670 2332 2625 3438 608 392 1 A C ATOM 5421 CD PRO A 670 15.258 21.305 54.981 1.00 17.93 A C ANISOU 5421 CD PRO A 670 2583 1712 2516 371 388 -435 A C ATOM 5422 N SER A 671 17.351 24.279 54.416 1.00 17.29 A N ANISOU 5422 N SER A 671 2714 1265 2589 458 126 -301 A N ATOM 5423 CA SER A 671 18.054 25.525 54.646 1.00 16.59 A C ANISOU 5423 CA SER A 671 2451 1548 2303 316 129 -344 A C ATOM 5424 C SER A 671 19.285 25.270 55.506 1.00 18.24 A C ANISOU 5424 C SER A 671 2220 2000 2711 385 210 193 A C ATOM 5425 O SER A 671 19.346 24.290 56.267 1.00 17.63 A O ANISOU 5425 O SER A 671 2440 1290 2967 484 301 -3 A O ATOM 5426 CB SER A 671 17.172 26.556 55.328 1.00 18.85 A C ANISOU 5426 CB SER A 671 2908 1480 2770 544 111 -376 A C ATOM 5427 OG SER A 671 16.996 26.268 56.693 1.00 18.86 A O ANISOU 5427 OG SER A 671 2566 1658 2942 347 405 -105 A O ATOM 5428 N ALA A 672 20.266 26.171 55.362 1.00 19.75 A N ANISOU 5428 N ALA A 672 2611 1535 3357 274 188 -144 A N ATOM 5429 CA ALA A 672 21.502 26.099 56.129 1.00 19.61 A C ANISOU 5429 CA ALA A 672 2796 1870 2785 -404 202 -219 A C ATOM 5430 C ALA A 672 21.153 26.180 57.622 1.00 18.38 A C ANISOU 5430 C ALA A 672 2259 1741 2981 223 301 -82 A C ATOM 5431 O ALA A 672 21.822 25.565 58.466 1.00 20.28 A O ANISOU 5431 O ALA A 672 2918 1521 3265 -84 28 207 A O ATOM 5432 CB ALA A 672 22.428 27.209 55.718 1.00 22.18 A C ANISOU 5432 CB ALA A 672 2986 2347 3094 -419 439 740 A C ATOM 5433 N GLU A 673 20.134 26.988 57.953 1.00 19.72 A N ANISOU 5433 N GLU A 673 2725 1549 3217 87 347 1 A N ATOM 5434 CA AGLU A 673 19.676 27.149 59.350 0.60 19.52 A C ANISOU 5434 CA AGLU A 673 3228 649 3539 186 557 -177 A C ATOM 5435 CA BGLU A 673 19.689 27.139 59.365 0.40 19.77 A C ANISOU 5435 CA BGLU A 673 3256 794 3462 107 541 -183 A C ATOM 5436 C GLU A 673 19.106 25.844 60.042 1.00 16.97 A C ANISOU 5436 C GLU A 673 2655 1148 2644 -97 919 -641 A C ATOM 5437 O GLU A 673 19.232 25.442 61.274 1.00 21.09 A O ANISOU 5437 O GLU A 673 3303 1530 3177 37 -46 -53 A O ATOM 5438 CB AGLU A 673 18.721 28.347 59.408 0.60 23.76 A C ANISOU 5438 CB AGLU A 673 3954 764 4306 471 118 58 A C ATOM 5439 CB BGLU A 673 18.738 28.335 59.456 0.40 24.45 A C ANISOU 5439 CB BGLU A 673 3976 1142 4170 508 263 -377 A C ATOM 5440 CG AGLU A 673 19.418 29.686 59.140 0.60 31.04 A C ANISOU 5440 CG AGLU A 673 5229 1386 5175 -81 320 769 A C ATOM 5441 CG BGLU A 673 19.435 29.664 59.191 0.40 30.56 A C ANISOU 5441 CG BGLU A 673 5184 1578 4847 9 503 -181 A C ATOM 5442 CD AGLU A 673 19.832 29.999 57.698 0.60 34.24 A C ANISOU 5442 CD AGLU A 673 4525 3474 5010 -621 -30 852 A C ATOM 5443 CD BGLU A 673 20.096 30.290 60.407 0.40 37.21 A C ANISOU 5443 CD BGLU A 673 5510 3200 5426 344 540 -1515 A C ATOM 5444 OE1AGLU A 673 19.191 29.477 56.738 0.60 24.62 A O ANISOU 5444 OE1AGLU A 673 3415 383 5555 489 -742 1042 A O ATOM 5445 OE1BGLU A 673 20.336 29.563 61.396 0.40 36.10 A O ANISOU 5445 OE1BGLU A 673 5836 3260 4620 298 298 -2355 A O ATOM 5446 OE2AGLU A 673 20.803 30.798 57.526 0.60 45.14 A O ANISOU 5446 OE2AGLU A 673 5959 4494 6697 -1928 -785 403 A O ATOM 5447 OE2BGLU A 673 20.363 31.511 60.366 0.40 46.47 A O ANISOU 5447 OE2BGLU A 673 7056 3752 6848 -681 1759 -286 A O ATOM 5448 N GLN A 674 18.317 25.164 59.216 1.00 17.40 A N ANISOU 5448 N GLN A 674 2732 1254 2624 359 119 -132 A N ATOM 5449 CA GLN A 674 17.722 23.880 59.679 1.00 16.59 A C ANISOU 5449 CA GLN A 674 2247 1511 2544 201 549 -100 A C ATOM 5450 C GLN A 674 18.837 22.843 59.820 1.00 16.08 A C ANISOU 5450 C GLN A 674 2123 1582 2405 165 423 -92 A C ATOM 5451 O GLN A 674 18.767 22.047 60.755 1.00 15.87 A O ANISOU 5451 O GLN A 674 2240 1531 2256 392 309 -151 A O ATOM 5452 CB GLN A 674 16.601 23.419 58.739 1.00 16.59 A C ANISOU 5452 CB GLN A 674 2006 1449 2847 299 344 -6 A C ATOM 5453 CG GLN A 674 15.310 24.205 58.936 1.00 17.41 A C ANISOU 5453 CG GLN A 674 2021 1567 3028 275 321 -229 A C ATOM 5454 CD GLN A 674 14.086 23.391 58.612 1.00 16.95 A C ANISOU 5454 CD GLN A 674 2088 1564 2786 302 344 -282 A C ATOM 5455 NE2 GLN A 674 12.947 23.841 59.130 1.00 18.93 A N ANISOU 5455 NE2 GLN A 674 2347 1541 3303 411 442 -329 A N ATOM 5456 OE1 GLN A 674 14.156 22.384 57.904 1.00 17.53 A O ANISOU 5456 OE1 GLN A 674 2260 1608 2791 271 413 -529 A O ATOM 5457 N ALA A 675 19.828 22.875 58.910 1.00 14.34 A N ANISOU 5457 N ALA A 675 1961 1221 2265 129 160 -16 A N ATOM 5458 CA ALA A 675 20.963 21.964 59.020 1.00 15.32 A C ANISOU 5458 CA ALA A 675 2122 1306 2392 374 172 -175 A C ATOM 5459 C ALA A 675 21.777 22.296 60.274 1.00 15.13 A C ANISOU 5459 C ALA A 675 2134 1334 2279 143 291 -289 A C ATOM 5460 O ALA A 675 22.136 21.423 61.040 1.00 16.46 A O ANISOU 5460 O ALA A 675 2230 1411 2610 129 351 -244 A O ATOM 5461 CB ALA A 675 21.825 22.030 57.785 1.00 15.82 A C ANISOU 5461 CB ALA A 675 2088 1410 2511 129 129 -244 A C ATOM 5462 N GLN A 676 22.048 23.592 60.520 1.00 15.86 A N ANISOU 5462 N GLN A 676 2153 1299 2572 133 282 -273 A N ATOM 5463 CA GLN A 676 22.845 23.961 61.688 1.00 17.60 A C ANISOU 5463 CA GLN A 676 2637 1500 2549 417 238 -339 A C ATOM 5464 C GLN A 676 22.101 23.540 62.984 1.00 16.38 A C ANISOU 5464 C GLN A 676 2284 1321 2618 177 152 -339 A C ATOM 5465 O GLN A 676 22.713 23.083 63.948 1.00 17.29 A O ANISOU 5465 O GLN A 676 2569 1242 2758 370 31 -304 A O ATOM 5466 CB GLN A 676 23.141 25.477 61.698 1.00 19.97 A C ANISOU 5466 CB GLN A 676 2763 1461 3362 443 620 -29 A C ATOM 5467 CG GLN A 676 24.083 25.927 60.582 1.00 24.17 A C ANISOU 5467 CG GLN A 676 3718 1950 3516 -401 637 20 A C ATOM 5468 CD GLN A 676 24.137 27.417 60.279 1.00 32.74 A C ANISOU 5468 CD GLN A 676 5551 1795 5092 -822 1240 -300 A C ATOM 5469 NE2 GLN A 676 24.836 27.762 59.202 1.00 41.21 A N ANISOU 5469 NE2 GLN A 676 5879 4289 5489 -1111 1690 -152 A N ATOM 5470 OE1 GLN A 676 23.560 28.263 60.973 1.00 45.76 A O ANISOU 5470 OE1 GLN A 676 6387 4346 6653 -259 1673 -1659 A O ATOM 5471 N SER A 677 20.777 23.728 63.034 1.00 16.10 A N ANISOU 5471 N SER A 677 2356 1110 2652 479 88 -399 A N ATOM 5472 CA SER A 677 19.982 23.323 64.190 1.00 18.07 A C ANISOU 5472 CA SER A 677 2541 1389 2935 106 162 -422 A C ATOM 5473 C SER A 677 20.097 21.809 64.392 1.00 16.33 A C ANISOU 5473 C SER A 677 2274 1530 2398 85 191 -30 A C ATOM 5474 O SER A 677 20.264 21.354 65.515 1.00 16.70 A O ANISOU 5474 O SER A 677 2676 1358 2311 338 335 -145 A O ATOM 5475 CB SER A 677 18.519 23.739 64.050 1.00 18.94 A C ANISOU 5475 CB SER A 677 2600 1301 3294 540 157 -535 A C ATOM 5476 OG SER A 677 18.419 25.146 64.102 1.00 23.60 A O ANISOU 5476 OG SER A 677 3532 1497 3937 698 539 -539 A O ATOM 5477 N ALA A 678 19.997 21.054 63.285 1.00 15.88 A N ANISOU 5477 N ALA A 678 2447 1389 2194 461 243 99 A N ATOM 5478 CA ALA A 678 20.112 19.570 63.345 1.00 15.80 A C ANISOU 5478 CA ALA A 678 2220 1383 2397 416 170 -50 A C ATOM 5479 C ALA A 678 21.497 19.147 63.868 1.00 14.84 A C ANISOU 5479 C ALA A 678 2089 1755 1795 196 92 -496 A C ATOM 5480 O ALA A 678 21.620 18.203 64.683 1.00 17.58 A O ANISOU 5480 O ALA A 678 2442 1556 2681 334 147 -303 A O ATOM 5481 CB ALA A 678 19.787 19.024 61.988 1.00 16.39 A C ANISOU 5481 CB ALA A 678 2312 1234 2679 245 266 -246 A C ATOM 5482 N ALA A 679 22.552 19.828 63.432 1.00 14.82 A N ANISOU 5482 N ALA A 679 2375 1172 2081 238 288 -400 A N ATOM 5483 CA ALA A 679 23.942 19.535 63.923 1.00 15.36 A C ANISOU 5483 CA ALA A 679 2428 1097 2309 54 194 -389 A C ATOM 5484 C ALA A 679 24.016 19.703 65.441 1.00 16.83 A C ANISOU 5484 C ALA A 679 2599 1483 2310 254 98 -398 A C ATOM 5485 O ALA A 679 24.617 18.897 66.148 1.00 16.67 A O ANISOU 5485 O ALA A 679 2755 1269 2310 204 250 -427 A O ATOM 5486 CB ALA A 679 24.996 20.343 63.213 1.00 16.60 A C ANISOU 5486 CB ALA A 679 2461 1495 2352 -11 139 -171 A C ATOM 5487 N LYS A 680 23.439 20.790 65.963 1.00 16.87 A N ANISOU 5487 N LYS A 680 2533 1409 2469 115 381 -394 A N ATOM 5488 CA LYS A 680 23.453 20.975 67.425 1.00 17.57 A C ANISOU 5488 CA LYS A 680 2660 1546 2468 348 244 -398 A C ATOM 5489 C LYS A 680 22.630 19.876 68.135 1.00 16.29 A C ANISOU 5489 C LYS A 680 2610 1296 2281 308 139 -704 A C ATOM 5490 O LYS A 680 23.020 19.430 69.240 1.00 18.96 A O ANISOU 5490 O LYS A 680 3104 1744 2355 432 669 -237 A O ATOM 5491 CB LYS A 680 22.986 22.388 67.772 1.00 19.20 A C ANISOU 5491 CB LYS A 680 2785 1593 2916 250 412 -688 A C ATOM 5492 CG LYS A 680 23.909 23.508 67.318 1.00 22.36 A C ANISOU 5492 CG LYS A 680 3088 1875 3530 11 265 -438 A C ATOM 5493 CD LYS A 680 25.234 23.474 68.011 1.00 27.40 A C ANISOU 5493 CD LYS A 680 3179 2539 4692 -91 291 -1044 A C ATOM 5494 CE LYS A 680 26.109 24.670 67.709 1.00 33.04 A C ANISOU 5494 CE LYS A 680 3994 3189 5370 -734 227 -909 A C ATOM 5495 NZ LYS A 680 27.428 24.479 68.370 1.00 33.96 A N ANISOU 5495 NZ LYS A 680 4138 3344 5421 -450 -4 -1895 A N ATOM 5496 N ARG A 681 21.515 19.440 67.543 1.00 15.86 A N ANISOU 5496 N ARG A 681 2189 1369 2467 336 323 -329 A N ATOM 5497 CA ARG A 681 20.750 18.350 68.143 1.00 17.09 A C ANISOU 5497 CA ARG A 681 2821 1462 2210 189 422 -282 A C ATOM 5498 C ARG A 681 21.530 17.036 68.107 1.00 17.61 A C ANISOU 5498 C ARG A 681 2604 1768 2316 315 337 -354 A C ATOM 5499 O ARG A 681 21.452 16.267 69.072 1.00 18.50 A O ANISOU 5499 O ARG A 681 2938 1852 2237 455 675 -428 A O ATOM 5500 CB ARG A 681 19.404 18.143 67.445 1.00 17.39 A C ANISOU 5500 CB ARG A 681 2677 1363 2566 346 423 -124 A C ATOM 5501 CG ARG A 681 18.459 19.311 67.627 1.00 18.79 A C ANISOU 5501 CG ARG A 681 2925 1487 2726 560 266 -128 A C ATOM 5502 CD ARG A 681 17.012 18.951 67.371 1.00 19.27 A C ANISOU 5502 CD ARG A 681 2991 1869 2463 390 679 -253 A C ATOM 5503 NE ARG A 681 16.778 18.321 66.090 1.00 18.33 A N ANISOU 5503 NE ARG A 681 2457 1889 2618 122 371 -353 A N ATOM 5504 CZ ARG A 681 16.710 18.912 64.914 1.00 18.32 A C ANISOU 5504 CZ ARG A 681 2611 1561 2790 208 446 -197 A C ATOM 5505 NH1 ARG A 681 16.786 20.241 64.836 1.00 19.92 A N ANISOU 5505 NH1 ARG A 681 2657 1437 3472 145 694 -49 A N ATOM 5506 NH2 ARG A 681 16.602 18.165 63.819 1.00 17.57 A N ANISOU 5506 NH2 ARG A 681 2388 1728 2560 282 534 -186 A N ATOM 5507 N LEU A 682 22.303 16.815 67.034 1.00 16.79 A N ANISOU 5507 N LEU A 682 2823 1187 2369 317 357 -317 A N ATOM 5508 CA LEU A 682 23.154 15.616 66.949 1.00 14.87 A C ANISOU 5508 CA LEU A 682 2364 1253 2031 274 406 -416 A C ATOM 5509 C LEU A 682 24.153 15.600 68.117 1.00 16.04 A C ANISOU 5509 C LEU A 682 2587 1401 2104 245 252 -321 A C ATOM 5510 O LEU A 682 24.340 14.577 68.828 1.00 17.56 A O ANISOU 5510 O LEU A 682 2673 1661 2334 592 557 -168 A O ATOM 5511 CB LEU A 682 23.847 15.547 65.577 1.00 15.35 A C ANISOU 5511 CB LEU A 682 1947 1527 2357 174 569 -396 A C ATOM 5512 CG LEU A 682 24.852 14.399 65.432 1.00 15.89 A C ANISOU 5512 CG LEU A 682 2431 1184 2422 199 433 -371 A C ATOM 5513 CD1 LEU A 682 24.249 13.005 65.723 1.00 16.97 A C ANISOU 5513 CD1 LEU A 682 2549 1493 2405 45 344 -156 A C ATOM 5514 CD2 LEU A 682 25.454 14.414 64.009 1.00 17.50 A C ANISOU 5514 CD2 LEU A 682 2566 1545 2538 229 648 -153 A C ATOM 5515 N VAL A 683 24.812 16.738 68.338 1.00 16.05 A N ANISOU 5515 N VAL A 683 2608 1369 2118 296 301 -475 A N ATOM 5516 CA VAL A 683 25.814 16.851 69.421 1.00 16.98 A C ANISOU 5516 CA VAL A 683 2692 1492 2267 381 287 -562 A C ATOM 5517 C VAL A 683 25.132 16.594 70.776 1.00 19.23 A C ANISOU 5517 C VAL A 683 2776 2141 2389 421 247 -378 A C ATOM 5518 O VAL A 683 25.726 15.925 71.635 1.00 19.29 A O ANISOU 5518 O VAL A 683 3247 1595 2487 377 534 -326 A O ATOM 5519 CB VAL A 683 26.517 18.217 69.403 1.00 18.54 A C ANISOU 5519 CB VAL A 683 2898 1635 2510 93 217 -394 A C ATOM 5520 CG1 VAL A 683 27.340 18.444 70.668 1.00 21.23 A C ANISOU 5520 CG1 VAL A 683 3242 2243 2581 -133 301 -492 A C ATOM 5521 CG2 VAL A 683 27.383 18.369 68.167 1.00 19.96 A C ANISOU 5521 CG2 VAL A 683 2703 1942 2936 -113 415 69 A C ATOM 5522 N ASN A 684 23.912 17.113 70.958 1.00 18.30 A N ANISOU 5522 N ASN A 684 2820 1949 2184 385 309 -348 A N ATOM 5523 CA ASN A 684 23.174 16.935 72.202 1.00 21.08 A C ANISOU 5523 CA ASN A 684 3123 2467 2420 501 467 -319 A C ATOM 5524 C ASN A 684 22.846 15.453 72.432 1.00 20.19 A C ANISOU 5524 C ASN A 684 2729 2395 2545 661 422 -312 A C ATOM 5525 O ASN A 684 23.033 14.984 73.570 1.00 21.45 A O ANISOU 5525 O ASN A 684 3411 2295 2442 545 486 -454 A O ATOM 5526 CB ASN A 684 21.905 17.788 72.229 1.00 27.65 A C ANISOU 5526 CB ASN A 684 3577 3227 3701 365 84 -40 A C ATOM 5527 CG ASN A 684 21.199 17.717 73.564 1.00 30.78 A C ANISOU 5527 CG ASN A 684 3882 4007 3803 -5 -190 -250 A C ATOM 5528 ND2 ASN A 684 19.979 17.214 73.575 1.00 31.71 A N ANISOU 5528 ND2 ASN A 684 3785 4152 4112 62 399 6 A N ATOM 5529 OD1 ASN A 684 21.776 18.087 74.581 1.00 31.92 A O ANISOU 5529 OD1 ASN A 684 4259 4188 3682 207 -56 -328 A O ATOM 5530 N ILE A 685 22.373 14.750 71.389 1.00 19.95 A N ANISOU 5530 N ILE A 685 3263 2068 2247 330 654 -64 A N ATOM 5531 CA ILE A 685 22.054 13.299 71.486 1.00 17.91 A C ANISOU 5531 CA ILE A 685 2398 2253 2152 37 751 -56 A C ATOM 5532 C ILE A 685 23.320 12.513 71.863 1.00 19.31 A C ANISOU 5532 C ILE A 685 2707 2480 2150 130 579 -257 A C ATOM 5533 O ILE A 685 23.245 11.610 72.705 1.00 20.34 A O ANISOU 5533 O ILE A 685 3187 2092 2449 493 686 -205 A O ATOM 5534 CB ILE A 685 21.433 12.781 70.168 1.00 22.44 A C ANISOU 5534 CB ILE A 685 2496 2325 3703 -406 -724 136 A C ATOM 5535 CG1 ILE A 685 19.972 13.220 70.047 1.00 26.37 A C ANISOU 5535 CG1 ILE A 685 2645 3426 3946 -122 -421 87 A C ATOM 5536 CG2 ILE A 685 21.590 11.272 70.049 1.00 28.93 A C ANISOU 5536 CG2 ILE A 685 3349 2756 4885 -466 322 34 A C ATOM 5537 CD1 ILE A 685 19.504 13.413 68.613 1.00 36.90 A C ANISOU 5537 CD1 ILE A 685 4655 5489 3876 -263 -430 459 A C ATOM 5538 N ILE A 686 24.455 12.863 71.245 1.00 17.68 A N ANISOU 5538 N ILE A 686 2706 1938 2071 32 528 -472 A N ATOM 5539 CA ILE A 686 25.725 12.210 71.529 1.00 17.79 A C ANISOU 5539 CA ILE A 686 2569 2071 2116 103 312 -497 A C ATOM 5540 C ILE A 686 26.124 12.440 72.995 1.00 19.79 A C ANISOU 5540 C ILE A 686 3295 2155 2067 259 249 -281 A C ATOM 5541 O ILE A 686 26.532 11.521 73.692 1.00 18.22 A O ANISOU 5541 O ILE A 686 2832 2220 1869 303 374 -368 A O ATOM 5542 CB ILE A 686 26.790 12.681 70.529 1.00 16.67 A C ANISOU 5542 CB ILE A 686 2593 1450 2289 180 301 -414 A C ATOM 5543 CG1 ILE A 686 26.477 12.145 69.127 1.00 16.18 A C ANISOU 5543 CG1 ILE A 686 2697 1312 2138 515 188 -111 A C ATOM 5544 CG2 ILE A 686 28.186 12.334 71.002 1.00 18.31 A C ANISOU 5544 CG2 ILE A 686 2709 1858 2388 240 295 -377 A C ATOM 5545 CD1 ILE A 686 27.252 12.841 68.002 1.00 18.01 A C ANISOU 5545 CD1 ILE A 686 2811 1745 2286 92 348 -240 A C ATOM 5546 N LYS A 687 26.005 13.690 73.450 1.00 19.82 A N ANISOU 5546 N LYS A 687 3399 2044 2086 240 365 -237 A N ATOM 5547 CA LYS A 687 26.372 14.061 74.828 1.00 21.53 A C ANISOU 5547 CA LYS A 687 4153 1644 2382 515 40 -402 A C ATOM 5548 C LYS A 687 25.489 13.316 75.843 1.00 20.63 A C ANISOU 5548 C LYS A 687 3631 2002 2203 424 126 -876 A C ATOM 5549 O LYS A 687 26.001 12.816 76.870 1.00 23.47 A O ANISOU 5549 O LYS A 687 4261 2289 2365 693 342 -242 A O ATOM 5550 CB LYS A 687 26.358 15.587 74.993 1.00 22.74 A C ANISOU 5550 CB LYS A 687 4461 1614 2562 1095 -260 -683 A C ATOM 5551 CG LYS A 687 26.639 16.092 76.395 1.00 31.03 A C ANISOU 5551 CG LYS A 687 5920 2457 3412 24 -398 -1331 A C ATOM 5552 CD LYS A 687 26.568 17.611 76.518 1.00 39.80 A C ANISOU 5552 CD LYS A 687 7272 2441 5407 574 -664 -1836 A C ATOM 5553 CE LYS A 687 26.781 18.060 77.959 1.00 50.46 A C ANISOU 5553 CE LYS A 687 9354 3789 6027 582 -1384 -2825 A C ATOM 5554 NZ LYS A 687 27.003 19.523 78.089 1.00 55.36 A N ANISOU 5554 NZ LYS A 687 10161 3903 6970 954 -1204 -2744 A N ATOM 5555 N GLN A 688 24.189 13.214 75.557 1.00 20.55 A N ANISOU 5555 N GLN A 688 3563 2096 2149 326 473 -487 A N ATOM 5556 CA GLN A 688 23.243 12.552 76.453 1.00 23.24 A C ANISOU 5556 CA GLN A 688 3957 2475 2396 260 796 -482 A C ATOM 5557 C GLN A 688 23.494 11.038 76.462 1.00 23.73 A C ANISOU 5557 C GLN A 688 4183 2444 2389 101 1617 -183 A C ATOM 5558 O GLN A 688 23.166 10.387 77.415 1.00 24.81 A O ANISOU 5558 O GLN A 688 3992 2952 2480 201 1507 176 A O ATOM 5559 CB GLN A 688 21.806 12.922 76.089 1.00 28.22 A C ANISOU 5559 CB GLN A 688 4152 3088 3482 513 662 98 A C ATOM 5560 CG GLN A 688 21.487 14.397 76.317 1.00 33.94 A C ANISOU 5560 CG GLN A 688 5234 3121 4541 512 1175 170 A C ATOM 5561 CD GLN A 688 21.894 14.949 77.668 1.00 46.90 A C ANISOU 5561 CD GLN A 688 7767 5602 4450 133 1502 185 A C ATOM 5562 NE2 GLN A 688 21.414 14.306 78.724 1.00 50.14 A N ANISOU 5562 NE2 GLN A 688 8111 5868 5069 578 2583 518 A N ATOM 5563 OE1 GLN A 688 22.625 15.946 77.777 1.00 57.22 A O ANISOU 5563 OE1 GLN A 688 7842 5392 8506 592 1851 -2691 A O ATOM 5564 N ASN A 689 24.158 10.525 75.422 1.00 21.83 A N ANISOU 5564 N ASN A 689 3762 2145 2384 332 1282 -191 A N ATOM 5565 CA ASN A 689 24.563 9.123 75.362 1.00 19.67 A C ANISOU 5565 CA ASN A 689 3119 2091 2263 315 593 -227 A C ATOM 5566 C ASN A 689 25.964 8.899 75.931 1.00 18.35 A C ANISOU 5566 C ASN A 689 2960 1952 2059 139 635 -217 A C ATOM 5567 O ASN A 689 26.565 7.858 75.675 1.00 19.04 A O ANISOU 5567 O ASN A 689 3423 1745 2065 184 423 -306 A O ATOM 5568 CB ASN A 689 24.529 8.652 73.903 1.00 19.72 A C ANISOU 5568 CB ASN A 689 3117 2028 2348 0 525 -325 A C ATOM 5569 CG ASN A 689 24.381 7.151 73.760 1.00 19.98 A C ANISOU 5569 CG ASN A 689 3147 1893 2548 166 597 -299 A C ATOM 5570 ND2 ASN A 689 25.123 6.538 72.836 1.00 19.01 A N ANISOU 5570 ND2 ASN A 689 2847 2319 2055 229 390 -32 A N ATOM 5571 OD1 ASN A 689 23.563 6.566 74.464 1.00 23.92 A O ANISOU 5571 OD1 ASN A 689 3627 2710 2748 -313 1018 -611 A O ATOM 5572 N ASP A 690 26.509 9.841 76.702 1.00 19.78 A N ANISOU 5572 N ASP A 690 3232 2323 1959 286 785 -411 A N ATOM 5573 CA ASP A 690 27.858 9.760 77.287 1.00 19.59 A C ANISOU 5573 CA ASP A 690 3562 2022 1857 399 260 -321 A C ATOM 5574 C ASP A 690 28.910 9.516 76.198 1.00 19.91 A C ANISOU 5574 C ASP A 690 3182 2344 2039 311 117 -444 A C ATOM 5575 O ASP A 690 29.917 8.845 76.421 1.00 20.35 A O ANISOU 5575 O ASP A 690 3267 2241 2221 372 136 -486 A O ATOM 5576 CB ASP A 690 27.909 8.708 78.397 1.00 24.50 A C ANISOU 5576 CB ASP A 690 4457 2556 2293 458 623 49 A C ATOM 5577 CG ASP A 690 27.152 9.075 79.658 1.00 36.97 A C ANISOU 5577 CG ASP A 690 5968 4570 3506 513 1737 -378 A C ATOM 5578 OD1 ASP A 690 27.091 10.281 79.985 1.00 41.17 A O ANISOU 5578 OD1 ASP A 690 7605 4641 3394 1006 358 -453 A O ATOM 5579 OD2 ASP A 690 26.629 8.149 80.287 1.00 47.82 A O ANISOU 5579 OD2 ASP A 690 6965 7217 3985 -667 3516 62 A O ATOM 5580 N TYR A 691 28.674 10.110 75.019 1.00 17.63 A N ANISOU 5580 N TYR A 691 3037 1581 2079 138 312 -484 A N ATOM 5581 CA TYR A 691 29.601 10.103 73.878 1.00 17.87 A C ANISOU 5581 CA TYR A 691 3047 1796 1947 369 351 -375 A C ATOM 5582 C TYR A 691 29.842 8.694 73.310 1.00 17.13 A C ANISOU 5582 C TYR A 691 2850 1593 2065 217 61 -98 A C ATOM 5583 O TYR A 691 30.766 8.508 72.520 1.00 18.79 A O ANISOU 5583 O TYR A 691 2846 1865 2427 202 294 -427 A O ATOM 5584 CB TYR A 691 30.935 10.779 74.210 1.00 18.10 A C ANISOU 5584 CB TYR A 691 3255 1822 1798 442 178 -689 A C ATOM 5585 CG TYR A 691 30.767 12.255 74.500 1.00 20.26 A C ANISOU 5585 CG TYR A 691 3565 1810 2321 425 216 -722 A C ATOM 5586 CD1 TYR A 691 30.717 13.192 73.477 1.00 21.33 A C ANISOU 5586 CD1 TYR A 691 3578 1832 2692 187 225 -647 A C ATOM 5587 CD2 TYR A 691 30.610 12.721 75.803 1.00 22.81 A C ANISOU 5587 CD2 TYR A 691 4178 1889 2599 170 622 -1081 A C ATOM 5588 CE1 TYR A 691 30.558 14.548 73.728 1.00 21.00 A C ANISOU 5588 CE1 TYR A 691 3343 1714 2920 272 288 -302 A C ATOM 5589 CE2 TYR A 691 30.444 14.078 76.065 1.00 22.78 A C ANISOU 5589 CE2 TYR A 691 4412 1766 2477 -82 479 -971 A C ATOM 5590 CZ TYR A 691 30.433 14.992 75.024 1.00 23.25 A C ANISOU 5590 CZ TYR A 691 4033 1555 3245 179 385 -688 A C ATOM 5591 OH TYR A 691 30.309 16.344 75.238 1.00 25.44 A O ANISOU 5591 OH TYR A 691 4885 1585 3195 435 294 -613 A O ATOM 5592 N LYS A 692 28.989 7.744 73.651 1.00 17.23 A N ANISOU 5592 N LYS A 692 3158 1696 1691 -75 322 -660 A N ATOM 5593 CA LYS A 692 29.072 6.395 73.088 1.00 17.05 A C ANISOU 5593 CA LYS A 692 3180 1498 1798 301 457 -456 A C ATOM 5594 C LYS A 692 28.510 6.416 71.670 1.00 16.87 A C ANISOU 5594 C LYS A 692 2949 1556 1903 182 253 -439 A C ATOM 5595 O LYS A 692 27.548 7.128 71.339 1.00 16.27 A O ANISOU 5595 O LYS A 692 2765 1575 1839 83 214 -459 A O ATOM 5596 CB LYS A 692 28.294 5.403 73.945 1.00 18.43 A C ANISOU 5596 CB LYS A 692 3248 1830 1924 54 291 -407 A C ATOM 5597 CG ALYS A 692 28.871 5.235 75.337 0.50 21.35 A C ANISOU 5597 CG ALYS A 692 3825 2395 1889 74 76 -599 A C ATOM 5598 CG BLYS A 692 28.830 5.218 75.351 0.50 21.47 A C ANISOU 5598 CG BLYS A 692 3705 2395 2056 396 -118 -750 A C ATOM 5599 CD ALYS A 692 28.007 4.439 76.280 0.50 22.88 A C ANISOU 5599 CD ALYS A 692 4259 2432 2000 -271 99 -559 A C ATOM 5600 CD BLYS A 692 30.331 5.118 75.416 0.50 22.71 A C ANISOU 5600 CD BLYS A 692 3689 2649 2289 534 -64 -625 A C ATOM 5601 CE ALYS A 692 28.725 4.172 77.585 0.50 30.08 A C ANISOU 5601 CE ALYS A 692 4815 3893 2718 -84 -474 -365 A C ATOM 5602 CE BLYS A 692 30.828 4.870 76.822 0.50 24.80 A C ANISOU 5602 CE BLYS A 692 3777 3111 2534 804 -525 -817 A C ATOM 5603 NZ ALYS A 692 28.073 4.866 78.718 0.50 34.29 A N ANISOU 5603 NZ ALYS A 692 5132 5381 2512 245 -56 -259 A N ATOM 5604 NZ BLYS A 692 30.564 6.037 77.696 0.50 27.75 A N ANISOU 5604 NZ BLYS A 692 4652 3519 2373 1238 -1222 -1100 A N ATOM 5605 N VAL A 693 29.140 5.632 70.805 1.00 16.07 A N ANISOU 5605 N VAL A 693 2783 1586 1736 318 276 -237 A N ATOM 5606 CA AVAL A 693 28.757 5.566 69.389 0.50 16.55 A C ANISOU 5606 CA AVAL A 693 2593 1888 1805 125 261 -194 A C ATOM 5607 CA BVAL A 693 28.757 5.610 69.398 0.50 15.33 A C ANISOU 5607 CA BVAL A 693 2570 1528 1726 164 312 -211 A C ATOM 5608 C VAL A 693 27.364 4.965 69.289 1.00 15.82 A C ANISOU 5608 C VAL A 693 2545 1685 1779 133 252 -229 A C ATOM 5609 O VAL A 693 27.032 4.005 70.013 1.00 16.16 A O ANISOU 5609 O VAL A 693 2669 1585 1884 129 247 -175 A O ATOM 5610 CB AVAL A 693 29.738 4.727 68.554 0.50 19.85 A C ANISOU 5610 CB AVAL A 693 3005 1977 2559 634 199 -357 A C ATOM 5611 CB BVAL A 693 29.867 4.947 68.544 0.50 14.01 A C ANISOU 5611 CB BVAL A 693 2704 922 1697 277 68 -376 A C ATOM 5612 CG1AVAL A 693 31.168 5.156 68.752 0.50 23.27 A C ANISOU 5612 CG1AVAL A 693 3136 2823 2880 203 223 -466 A C ATOM 5613 CG1BVAL A 693 30.100 3.488 68.913 0.50 14.14 A C ANISOU 5613 CG1BVAL A 693 2833 887 1651 -115 54 -161 A C ATOM 5614 CG2AVAL A 693 29.585 3.243 68.826 0.50 20.41 A C ANISOU 5614 CG2AVAL A 693 2810 2106 2838 287 439 -183 A C ATOM 5615 CG2BVAL A 693 29.610 5.089 67.043 0.50 13.32 A C ANISOU 5615 CG2BVAL A 693 2727 839 1493 438 543 -321 A C ATOM 5616 N GLY A 694 26.564 5.487 68.366 1.00 15.50 A N ANISOU 5616 N GLY A 694 2383 1573 1932 176 255 -343 A N ATOM 5617 CA GLY A 694 25.202 5.082 68.187 1.00 14.14 A C ANISOU 5617 CA GLY A 694 2336 1369 1665 171 351 -162 A C ATOM 5618 C GLY A 694 24.848 4.676 66.763 1.00 14.89 A C ANISOU 5618 C GLY A 694 2327 1467 1863 2 142 -188 A C ATOM 5619 O GLY A 694 23.706 4.409 66.482 1.00 15.38 A O ANISOU 5619 O GLY A 694 2461 1691 1690 -218 219 -220 A O ATOM 5620 N THR A 695 25.870 4.583 65.912 1.00 14.76 A N ANISOU 5620 N THR A 695 2658 1481 1468 -238 358 -38 A N ATOM 5621 CA THR A 695 25.724 4.292 64.475 1.00 14.65 A C ANISOU 5621 CA THR A 695 2683 1268 1615 -143 191 -33 A C ATOM 5622 C THR A 695 26.052 2.824 64.166 1.00 14.55 A C ANISOU 5622 C THR A 695 2318 1435 1774 -93 -54 -255 A C ATOM 5623 O THR A 695 26.951 2.271 64.755 1.00 15.26 A O ANISOU 5623 O THR A 695 2493 1310 1992 -27 181 12 A O ATOM 5624 CB THR A 695 26.633 5.242 63.693 1.00 13.86 A C ANISOU 5624 CB THR A 695 2513 950 1803 9 324 -82 A C ATOM 5625 CG2 THR A 695 26.174 6.687 63.719 1.00 15.45 A C ANISOU 5625 CG2 THR A 695 2758 959 2153 25 301 -258 A C ATOM 5626 OG1 THR A 695 27.967 5.156 64.217 1.00 14.52 A O ANISOU 5626 OG1 THR A 695 2275 1209 2030 -92 380 -39 A O ATOM 5627 N GLY A 696 25.370 2.291 63.137 1.00 14.00 A N ANISOU 5627 N GLY A 696 2428 1011 1877 -37 -147 -90 A N ATOM 5628 CA GLY A 696 25.778 1.049 62.483 1.00 13.74 A C ANISOU 5628 CA GLY A 696 2342 840 2039 -221 46 -81 A C ATOM 5629 C GLY A 696 26.572 1.319 61.210 1.00 14.11 A C ANISOU 5629 C GLY A 696 2151 1329 1880 -28 -31 23 A C ATOM 5630 O GLY A 696 27.222 2.365 61.070 1.00 14.23 A O ANISOU 5630 O GLY A 696 2302 1183 1920 -33 8 72 A O ATOM 5631 N PHE A 697 26.466 0.415 60.227 1.00 13.23 A N ANISOU 5631 N PHE A 697 1873 1008 2144 -76 209 -49 A N ATOM 5632 CA PHE A 697 27.309 0.490 59.039 1.00 14.06 A C ANISOU 5632 CA PHE A 697 2112 804 2423 -40 256 -80 A C ATOM 5633 C PHE A 697 26.952 1.722 58.203 1.00 13.38 A C ANISOU 5633 C PHE A 697 1940 1047 2094 63 119 -103 A C ATOM 5634 O PHE A 697 27.782 2.173 57.420 1.00 14.04 A O ANISOU 5634 O PHE A 697 1907 1186 2241 127 23 11 A O ATOM 5635 CB PHE A 697 27.231 -0.808 58.211 1.00 13.04 A C ANISOU 5635 CB PHE A 697 1774 920 2258 -114 -28 -165 A C ATOM 5636 CG PHE A 697 28.061 -1.991 58.653 1.00 14.61 A C ANISOU 5636 CG PHE A 697 1981 1375 2195 197 210 -89 A C ATOM 5637 CD1 PHE A 697 28.424 -2.172 59.982 1.00 14.64 A C ANISOU 5637 CD1 PHE A 697 2124 1130 2307 -9 106 -199 A C ATOM 5638 CD2 PHE A 697 28.460 -2.932 57.731 1.00 15.52 A C ANISOU 5638 CD2 PHE A 697 2174 1538 2184 72 -35 -354 A C ATOM 5639 CE1 PHE A 697 29.158 -3.270 60.396 1.00 16.72 A C ANISOU 5639 CE1 PHE A 697 2506 1396 2449 197 193 75 A C ATOM 5640 CE2 PHE A 697 29.176 -4.050 58.142 1.00 17.14 A C ANISOU 5640 CE2 PHE A 697 2460 1444 2607 99 280 -215 A C ATOM 5641 CZ PHE A 697 29.545 -4.212 59.456 1.00 16.80 A C ANISOU 5641 CZ PHE A 697 2294 1519 2568 68 224 -114 A C ATOM 5642 N ALA A 698 25.692 2.161 58.290 1.00 12.96 A N ANISOU 5642 N ALA A 698 2013 940 1969 175 172 -4 A N ATOM 5643 CA ALA A 698 25.266 3.285 57.436 1.00 12.83 A C ANISOU 5643 CA ALA A 698 2004 1153 1717 466 70 -92 A C ATOM 5644 C ALA A 698 25.843 4.619 57.930 1.00 13.31 A C ANISOU 5644 C ALA A 698 1743 1368 1946 177 257 -120 A C ATOM 5645 O ALA A 698 26.081 5.495 57.122 1.00 13.79 A O ANISOU 5645 O ALA A 698 2176 1337 1726 20 283 -242 A O ATOM 5646 CB ALA A 698 23.751 3.384 57.362 1.00 13.23 A C ANISOU 5646 CB ALA A 698 1993 1230 1800 209 -33 138 A C ATOM 5647 N GLY A 699 25.980 4.757 59.259 1.00 12.95 A N ANISOU 5647 N GLY A 699 2115 676 2129 145 24 -122 A N ATOM 5648 CA GLY A 699 26.353 6.024 59.865 1.00 12.69 A C ANISOU 5648 CA GLY A 699 1979 839 2004 106 323 -360 A C ATOM 5649 C GLY A 699 27.822 6.120 60.269 1.00 13.40 A C ANISOU 5649 C GLY A 699 2150 1154 1785 59 -32 -61 A C ATOM 5650 O GLY A 699 28.377 7.221 60.308 1.00 13.80 A O ANISOU 5650 O GLY A 699 1942 1160 2139 21 339 -244 A O ATOM 5651 N THR A 700 28.460 5.008 60.613 1.00 13.58 A N ANISOU 5651 N THR A 700 2097 1129 1930 210 4 -252 A N ATOM 5652 CA THR A 700 29.746 5.058 61.322 1.00 12.74 A C ANISOU 5652 CA THR A 700 2044 872 1923 446 108 -339 A C ATOM 5653 C THR A 700 30.846 5.724 60.482 1.00 13.77 A C ANISOU 5653 C THR A 700 1985 1371 1876 104 -58 -383 A C ATOM 5654 O THR A 700 31.562 6.638 60.979 1.00 13.53 A O ANISOU 5654 O THR A 700 1992 1087 2061 71 -44 -295 A O ATOM 5655 CB THR A 700 30.190 3.668 61.755 1.00 13.58 A C ANISOU 5655 CB THR A 700 2213 861 2085 357 79 -203 A C ATOM 5656 CG2 THR A 700 31.545 3.705 62.423 1.00 15.46 A C ANISOU 5656 CG2 THR A 700 2166 1323 2382 42 -2 86 A C ATOM 5657 OG1 THR A 700 29.223 3.191 62.692 1.00 14.10 A O ANISOU 5657 OG1 THR A 700 2398 1109 1847 117 95 -203 A O ATOM 5658 N HIS A 701 30.951 5.356 59.191 1.00 12.54 A N ANISOU 5658 N HIS A 701 1906 1099 1757 -41 -18 -408 A N ATOM 5659 CA HIS A 701 32.040 5.856 58.368 1.00 11.92 A C ANISOU 5659 CA HIS A 701 1762 935 1829 242 114 -561 A C ATOM 5660 C HIS A 701 31.956 7.367 58.133 1.00 11.66 A C ANISOU 5660 C HIS A 701 1720 988 1721 0 91 -449 A C ATOM 5661 O HIS A 701 32.994 7.988 57.755 1.00 13.67 A O ANISOU 5661 O HIS A 701 1822 1036 2335 6 254 -469 A O ATOM 5662 CB HIS A 701 32.159 5.107 57.035 1.00 12.72 A C ANISOU 5662 CB HIS A 701 2055 1210 1567 171 17 -433 A C ATOM 5663 CG HIS A 701 31.045 5.356 56.076 1.00 12.15 A C ANISOU 5663 CG HIS A 701 1934 999 1680 102 69 -442 A C ATOM 5664 CD2 HIS A 701 29.741 4.983 56.067 1.00 12.79 A C ANISOU 5664 CD2 HIS A 701 1842 1088 1926 158 125 -195 A C ATOM 5665 ND1 HIS A 701 31.258 6.047 54.901 1.00 13.85 A N ANISOU 5665 ND1 HIS A 701 1972 1400 1889 226 83 -67 A N ATOM 5666 CE1 HIS A 701 30.126 6.090 54.211 1.00 14.33 A C ANISOU 5666 CE1 HIS A 701 1838 1470 2136 136 36 81 A C ATOM 5667 NE2 HIS A 701 29.177 5.439 54.903 1.00 13.31 A N ANISOU 5667 NE2 HIS A 701 1676 1433 1946 46 165 -196 A N ATOM 5668 N LEU A 702 30.768 7.944 58.340 1.00 12.07 A N ANISOU 5668 N LEU A 702 1835 960 1790 90 247 -327 A N ATOM 5669 CA LEU A 702 30.563 9.369 58.058 1.00 12.95 A C ANISOU 5669 CA LEU A 702 1967 973 1979 308 223 -301 A C ATOM 5670 C LEU A 702 30.423 10.211 59.329 1.00 12.70 A C ANISOU 5670 C LEU A 702 2035 993 1798 287 228 -184 A C ATOM 5671 O LEU A 702 30.417 11.441 59.260 1.00 14.31 A O ANISOU 5671 O LEU A 702 2234 896 2307 121 184 -264 A O ATOM 5672 CB LEU A 702 29.309 9.523 57.199 1.00 14.28 A C ANISOU 5672 CB LEU A 702 2582 1047 1795 399 -22 -28 A C ATOM 5673 CG LEU A 702 29.318 8.910 55.825 1.00 16.82 A C ANISOU 5673 CG LEU A 702 2761 1304 2326 51 -348 -407 A C ATOM 5674 CD1 LEU A 702 27.913 9.070 55.223 1.00 17.49 A C ANISOU 5674 CD1 LEU A 702 2687 1512 2444 257 -466 -324 A C ATOM 5675 CD2 LEU A 702 30.425 9.539 54.981 1.00 19.06 A C ANISOU 5675 CD2 LEU A 702 2633 1715 2893 409 -268 185 A C ATOM 5676 N LEU A 703 30.303 9.598 60.494 1.00 12.28 A N ANISOU 5676 N LEU A 703 1886 1043 1736 210 66 -178 A N ATOM 5677 CA LEU A 703 29.919 10.334 61.705 1.00 14.07 A C ANISOU 5677 CA LEU A 703 2114 1553 1677 53 236 -235 A C ATOM 5678 C LEU A 703 30.943 11.421 62.050 1.00 12.77 A C ANISOU 5678 C LEU A 703 2141 915 1792 336 13 -163 A C ATOM 5679 O LEU A 703 30.593 12.579 62.287 1.00 13.22 A O ANISOU 5679 O LEU A 703 2078 884 2059 285 80 -255 A O ATOM 5680 CB LEU A 703 29.719 9.365 62.872 1.00 15.21 A C ANISOU 5680 CB LEU A 703 2380 1604 1792 -204 240 -99 A C ATOM 5681 CG LEU A 703 29.274 10.007 64.181 1.00 17.09 A C ANISOU 5681 CG LEU A 703 2277 2219 1997 -294 177 -434 A C ATOM 5682 CD1 LEU A 703 27.942 10.739 64.007 1.00 20.10 A C ANISOU 5682 CD1 LEU A 703 2747 2215 2675 -120 197 -618 A C ATOM 5683 CD2 LEU A 703 29.168 8.951 65.274 1.00 19.06 A C ANISOU 5683 CD2 LEU A 703 2931 2263 2045 -131 -203 -289 A C ATOM 5684 N GLY A 704 32.233 11.099 62.115 1.00 12.31 A N ANISOU 5684 N GLY A 704 2014 959 1702 102 -179 -299 A N ATOM 5685 CA GLY A 704 33.243 12.080 62.455 1.00 13.36 A C ANISOU 5685 CA GLY A 704 1967 1451 1656 -136 195 -480 A C ATOM 5686 C GLY A 704 33.308 13.189 61.428 1.00 12.97 A C ANISOU 5686 C GLY A 704 1869 1158 1898 24 -37 -473 A C ATOM 5687 O GLY A 704 33.451 14.370 61.781 1.00 13.57 A O ANISOU 5687 O GLY A 704 2197 971 1986 132 202 -392 A O ATOM 5688 N HIS A 705 33.223 12.841 60.149 1.00 12.76 A N ANISOU 5688 N HIS A 705 1961 1119 1765 125 -2 -270 A N ATOM 5689 CA HIS A 705 33.295 13.823 59.082 1.00 13.62 A C ANISOU 5689 CA HIS A 705 1770 1453 1952 77 7 -128 A C ATOM 5690 C HIS A 705 32.096 14.756 59.134 1.00 13.29 A C ANISOU 5690 C HIS A 705 1881 1024 2143 31 54 -195 A C ATOM 5691 O HIS A 705 32.227 15.952 58.812 1.00 14.54 A O ANISOU 5691 O HIS A 705 2295 859 2371 62 141 -188 A O ATOM 5692 CB HIS A 705 33.408 13.172 57.712 1.00 14.05 A C ANISOU 5692 CB HIS A 705 2016 1429 1891 171 46 -114 A C ATOM 5693 CG HIS A 705 34.664 12.398 57.587 1.00 13.03 A C ANISOU 5693 CG HIS A 705 1878 1303 1769 174 -133 -22 A C ATOM 5694 CD2 HIS A 705 34.885 11.070 57.461 1.00 15.13 A C ANISOU 5694 CD2 HIS A 705 2057 1165 2524 -143 72 -1 A C ATOM 5695 ND1 HIS A 705 35.900 12.999 57.659 1.00 15.87 A N ANISOU 5695 ND1 HIS A 705 1782 1826 2419 143 -113 -283 A N ATOM 5696 CE1 HIS A 705 36.841 12.068 57.545 1.00 13.50 A C ANISOU 5696 CE1 HIS A 705 1540 1645 1945 -100 -81 -284 A C ATOM 5697 NE2 HIS A 705 36.239 10.875 57.442 1.00 14.18 A N ANISOU 5697 NE2 HIS A 705 2046 1353 1986 5 -34 -112 A N ATOM 5698 N THR A 706 30.942 14.246 59.551 1.00 12.82 A N ANISOU 5698 N THR A 706 1742 1222 1908 184 73 -210 A N ATOM 5699 CA THR A 706 29.741 15.034 59.636 1.00 12.92 A C ANISOU 5699 CA THR A 706 1697 1400 1810 324 5 -367 A C ATOM 5700 C THR A 706 29.915 16.064 60.754 1.00 13.21 A C ANISOU 5700 C THR A 706 2077 946 1993 -53 163 -194 A C ATOM 5701 O THR A 706 29.598 17.270 60.600 1.00 14.31 A O ANISOU 5701 O THR A 706 2160 991 2285 103 298 -334 A O ATOM 5702 CB THR A 706 28.500 14.173 59.892 1.00 14.78 A C ANISOU 5702 CB THR A 706 1910 1366 2338 277 -15 -477 A C ATOM 5703 CG2 THR A 706 27.252 15.012 60.054 1.00 14.54 A C ANISOU 5703 CG2 THR A 706 2036 1089 2396 229 51 -232 A C ATOM 5704 OG1 THR A 706 28.321 13.248 58.811 1.00 15.55 A O ANISOU 5704 OG1 THR A 706 2243 1210 2455 90 22 -429 A O ATOM 5705 N LEU A 707 30.398 15.617 61.922 1.00 13.63 A N ANISOU 5705 N LEU A 707 2318 998 1862 237 165 -308 A N ATOM 5706 CA LEU A 707 30.554 16.513 63.050 1.00 14.54 A C ANISOU 5706 CA LEU A 707 2007 1543 1975 97 154 -508 A C ATOM 5707 C LEU A 707 31.587 17.583 62.709 1.00 14.58 A C ANISOU 5707 C LEU A 707 2215 1150 2174 169 40 -469 A C ATOM 5708 O LEU A 707 31.370 18.785 62.978 1.00 14.84 A O ANISOU 5708 O LEU A 707 2461 885 2292 22 81 -295 A O ATOM 5709 CB LEU A 707 30.925 15.720 64.313 1.00 15.27 A C ANISOU 5709 CB LEU A 707 2090 1666 2044 228 78 -540 A C ATOM 5710 CG LEU A 707 29.776 14.911 64.901 1.00 16.28 A C ANISOU 5710 CG LEU A 707 2491 1725 1969 198 209 -261 A C ATOM 5711 CD1 LEU A 707 30.317 13.850 65.839 1.00 19.10 A C ANISOU 5711 CD1 LEU A 707 2923 2001 2330 305 336 -74 A C ATOM 5712 CD2 LEU A 707 28.795 15.817 65.623 1.00 18.15 A C ANISOU 5712 CD2 LEU A 707 2838 2020 2035 304 201 -381 A C ATOM 5713 N SER A 708 32.700 17.215 62.097 1.00 14.25 A N ANISOU 5713 N SER A 708 2107 962 2344 107 87 -378 A N ATOM 5714 CA SER A 708 33.730 18.192 61.723 1.00 14.46 A C ANISOU 5714 CA SER A 708 2094 1386 2013 15 199 -375 A C ATOM 5715 C SER A 708 33.203 19.177 60.670 1.00 14.37 A C ANISOU 5715 C SER A 708 2363 812 2284 177 179 -445 A C ATOM 5716 O SER A 708 33.533 20.362 60.719 1.00 15.64 A O ANISOU 5716 O SER A 708 2421 849 2672 -42 205 -452 A O ATOM 5717 CB SER A 708 34.982 17.494 61.237 1.00 14.41 A C ANISOU 5717 CB SER A 708 1935 1555 1984 27 212 -209 A C ATOM 5718 OG SER A 708 35.575 16.762 62.301 1.00 15.43 A O ANISOU 5718 OG SER A 708 2160 1389 2314 293 66 -383 A O ATOM 5719 N LYS A 709 32.362 18.739 59.736 1.00 15.48 A N ANISOU 5719 N LYS A 709 2268 1236 2376 27 54 -176 A N ATOM 5720 CA LYS A 709 31.778 19.589 58.693 1.00 15.94 A C ANISOU 5720 CA LYS A 709 2217 1798 2041 152 235 -14 A C ATOM 5721 C LYS A 709 31.034 20.765 59.344 1.00 17.19 A C ANISOU 5721 C LYS A 709 2643 1433 2455 61 208 -61 A C ATOM 5722 O LYS A 709 31.040 21.880 58.787 1.00 18.86 A O ANISOU 5722 O LYS A 709 2922 1268 2974 175 327 -117 A O ATOM 5723 CB LYS A 709 30.816 18.757 57.836 1.00 17.23 A C ANISOU 5723 CB LYS A 709 1812 1964 2771 430 76 -85 A C ATOM 5724 CG LYS A 709 30.005 19.516 56.792 1.00 18.77 A C ANISOU 5724 CG LYS A 709 2407 2126 2598 527 -41 -181 A C ATOM 5725 CD LYS A 709 29.180 18.576 55.941 1.00 22.21 A C ANISOU 5725 CD LYS A 709 2944 2749 2744 13 -82 -30 A C ATOM 5726 CE LYS A 709 28.351 19.283 54.886 1.00 24.99 A C ANISOU 5726 CE LYS A 709 3128 2924 3442 316 -363 125 A C ATOM 5727 NZ LYS A 709 27.852 18.320 53.880 1.00 30.12 A N ANISOU 5727 NZ LYS A 709 4416 3142 3886 -468 -572 514 A N ATOM 5728 N TYR A 710 30.467 20.543 60.538 1.00 15.09 A N ANISOU 5728 N TYR A 710 2371 974 2385 303 139 -52 A N ATOM 5729 CA ATYR A 710 29.665 21.553 61.270 0.50 15.98 A C ANISOU 5729 CA ATYR A 710 2507 1293 2271 353 221 -115 A C ATOM 5730 CA BTYR A 710 29.643 21.570 61.255 0.50 15.62 A C ANISOU 5730 CA BTYR A 710 2446 1298 2190 322 272 -94 A C ATOM 5731 C TYR A 710 30.408 22.148 62.461 1.00 17.56 A C ANISOU 5731 C TYR A 710 2544 1888 2240 259 162 -132 A C ATOM 5732 O TYR A 710 29.786 22.808 63.337 1.00 21.63 A O ANISOU 5732 O TYR A 710 3016 1961 3242 440 342 -757 A O ATOM 5733 CB ATYR A 710 28.329 20.937 61.687 0.50 17.54 A C ANISOU 5733 CB ATYR A 710 2337 1852 2472 292 182 -65 A C ATOM 5734 CB BTYR A 710 28.270 20.983 61.629 0.50 15.52 A C ANISOU 5734 CB BTYR A 710 2218 1612 2064 438 365 -197 A C ATOM 5735 CG ATYR A 710 27.395 21.067 60.531 0.50 17.64 A C ANISOU 5735 CG ATYR A 710 2358 1934 2411 321 247 240 A C ATOM 5736 CG BTYR A 710 27.382 20.683 60.446 0.50 16.17 A C ANISOU 5736 CG BTYR A 710 2404 1829 1908 267 411 22 A C ATOM 5737 CD1ATYR A 710 26.786 22.278 60.270 0.50 19.82 A C ANISOU 5737 CD1ATYR A 710 2869 1753 2907 305 234 110 A C ATOM 5738 CD1BTYR A 710 27.454 19.464 59.794 0.50 16.48 A C ANISOU 5738 CD1BTYR A 710 2443 1928 1889 -15 599 -37 A C ATOM 5739 CD2ATYR A 710 27.271 20.053 59.606 0.50 18.92 A C ANISOU 5739 CD2ATYR A 710 2490 2023 2674 636 209 31 A C ATOM 5740 CD2BTYR A 710 26.470 21.616 59.971 0.50 17.35 A C ANISOU 5740 CD2BTYR A 710 2476 1881 2236 278 332 -49 A C ATOM 5741 CE1ATYR A 710 25.982 22.451 59.160 0.50 19.57 A C ANISOU 5741 CE1ATYR A 710 2582 1592 3261 383 -21 -133 A C ATOM 5742 CE1BTYR A 710 26.664 19.194 58.690 0.50 16.56 A C ANISOU 5742 CE1BTYR A 710 2379 1837 2074 214 574 -321 A C ATOM 5743 CE2ATYR A 710 26.479 20.206 58.487 0.50 17.27 A C ANISOU 5743 CE2ATYR A 710 2498 1282 2781 642 198 158 A C ATOM 5744 CE2BTYR A 710 25.653 21.353 58.882 0.50 16.18 A C ANISOU 5744 CE2BTYR A 710 2108 1538 2501 278 419 -264 A C ATOM 5745 CZ ATYR A 710 25.826 21.406 58.271 0.50 17.99 A C ANISOU 5745 CZ ATYR A 710 2504 1377 2953 766 100 -1 A C ATOM 5746 CZ BTYR A 710 25.761 20.140 58.233 0.50 17.22 A C ANISOU 5746 CZ BTYR A 710 2496 1484 2564 67 420 -259 A C ATOM 5747 OH ATYR A 710 25.077 21.551 57.159 0.50 18.58 A O ANISOU 5747 OH ATYR A 710 2197 1694 3166 515 -8 -128 A O ATOM 5748 OH BTYR A 710 24.988 19.896 57.141 0.50 16.50 A O ANISOU 5748 OH BTYR A 710 2497 787 2982 144 99 -62 A O ATOM 5749 N GLY A 711 31.739 21.992 62.468 1.00 17.25 A N ANISOU 5749 N GLY A 711 2595 1249 2708 88 169 -225 A N ATOM 5750 CA GLY A 711 32.583 22.643 63.478 1.00 18.71 A C ANISOU 5750 CA GLY A 711 2790 1543 2775 22 206 -517 A C ATOM 5751 C GLY A 711 32.533 21.982 64.838 1.00 18.66 A C ANISOU 5751 C GLY A 711 3016 1354 2718 10 31 -729 A C ATOM 5752 O GLY A 711 32.904 22.595 65.860 1.00 20.74 A O ANISOU 5752 O GLY A 711 3548 1629 2703 -321 -5 -676 A O ATOM 5753 N GLU A 712 32.116 20.704 64.854 1.00 16.27 A N ANISOU 5753 N GLU A 712 2745 1164 2269 166 123 -711 A N ATOM 5754 CA GLU A 712 31.933 19.995 66.110 1.00 17.08 A C ANISOU 5754 CA GLU A 712 2411 1791 2287 217 241 -486 A C ATOM 5755 C GLU A 712 32.980 18.884 66.282 1.00 15.87 A C ANISOU 5755 C GLU A 712 2260 1531 2238 -24 282 -206 A C ATOM 5756 O GLU A 712 32.657 17.812 66.820 1.00 15.44 A O ANISOU 5756 O GLU A 712 2447 1333 2084 79 245 -287 A O ATOM 5757 CB GLU A 712 30.516 19.450 66.183 1.00 17.12 A C ANISOU 5757 CB GLU A 712 2537 1434 2533 208 101 -261 A C ATOM 5758 CG GLU A 712 29.444 20.515 66.051 1.00 18.08 A C ANISOU 5758 CG GLU A 712 2524 1563 2781 309 154 -400 A C ATOM 5759 CD GLU A 712 29.227 21.399 67.261 1.00 22.61 A C ANISOU 5759 CD GLU A 712 3346 2020 3223 86 -301 -978 A C ATOM 5760 OE1 GLU A 712 29.793 21.089 68.347 1.00 22.22 A O ANISOU 5760 OE1 GLU A 712 3293 1977 3171 234 82 -832 A O ATOM 5761 OE2 GLU A 712 28.444 22.377 67.121 1.00 24.12 A O ANISOU 5761 OE2 GLU A 712 2935 2703 3525 537 4 -1072 A O ATOM 5762 N SER A 713 34.225 19.135 65.859 1.00 15.72 A N ANISOU 5762 N SER A 713 2237 1162 2573 144 451 -343 A N ATOM 5763 CA SER A 713 35.293 18.173 66.063 1.00 16.27 A C ANISOU 5763 CA SER A 713 2504 1081 2595 203 277 -728 A C ATOM 5764 C SER A 713 35.489 17.814 67.543 1.00 18.60 A C ANISOU 5764 C SER A 713 2823 1593 2651 137 -189 -602 A C ATOM 5765 O SER A 713 35.864 16.695 67.836 1.00 17.89 A O ANISOU 5765 O SER A 713 2850 1525 2420 171 132 -239 A O ATOM 5766 CB SER A 713 36.613 18.596 65.423 1.00 17.32 A C ANISOU 5766 CB SER A 713 2631 1268 2679 -36 158 -291 A C ATOM 5767 OG SER A 713 36.515 18.670 64.012 1.00 18.25 A O ANISOU 5767 OG SER A 713 2602 1700 2632 87 276 -587 A O ATOM 5768 N ASP A 714 35.319 18.752 68.477 1.00 17.74 A N ANISOU 5768 N ASP A 714 3010 1195 2533 194 -71 -345 A N ATOM 5769 CA ASP A 714 35.524 18.447 69.910 1.00 18.90 A C ANISOU 5769 CA ASP A 714 3271 1370 2537 221 -169 -758 A C ATOM 5770 C ASP A 714 34.563 17.350 70.376 1.00 17.46 A C ANISOU 5770 C ASP A 714 3070 1798 1765 226 92 -617 A C ATOM 5771 O ASP A 714 34.968 16.454 71.123 1.00 19.09 A O ANISOU 5771 O ASP A 714 3335 1694 2224 174 -104 -440 A O ATOM 5772 CB ASP A 714 35.341 19.704 70.772 1.00 20.39 A C ANISOU 5772 CB ASP A 714 3655 1232 2858 299 -202 -790 A C ATOM 5773 CG ASP A 714 36.503 20.649 70.630 1.00 28.44 A C ANISOU 5773 CG ASP A 714 4344 1721 4739 -28 -401 -1449 A C ATOM 5774 OD1 ASP A 714 37.659 20.209 70.444 1.00 30.49 A O ANISOU 5774 OD1 ASP A 714 4120 2835 4628 2 -189 -447 A O ATOM 5775 OD2 ASP A 714 36.235 21.849 70.738 1.00 37.76 A O ANISOU 5775 OD2 ASP A 714 5559 1598 7187 87 -197 -1483 A O ATOM 5776 N ALA A 715 33.315 17.378 69.903 1.00 17.19 A N ANISOU 5776 N ALA A 715 2740 1520 2270 46 390 -757 A N ATOM 5777 CA ALA A 715 32.356 16.326 70.232 1.00 17.01 A C ANISOU 5777 CA ALA A 715 2813 1595 2051 -35 237 -642 A C ATOM 5778 C ALA A 715 32.854 14.962 69.734 1.00 16.40 A C ANISOU 5778 C ALA A 715 2682 1697 1852 184 205 -501 A C ATOM 5779 O ALA A 715 32.728 13.974 70.427 1.00 17.10 A O ANISOU 5779 O ALA A 715 3132 1823 1541 230 356 -443 A O ATOM 5780 CB ALA A 715 30.985 16.641 69.664 1.00 18.48 A C ANISOU 5780 CB ALA A 715 2754 1624 2641 219 305 -448 A C ATOM 5781 N PHE A 716 33.418 14.930 68.532 1.00 14.86 A N ANISOU 5781 N PHE A 716 2448 1159 2039 9 368 -378 A N ATOM 5782 CA PHE A 716 33.866 13.644 67.987 1.00 14.55 A C ANISOU 5782 CA PHE A 716 2645 1374 1508 106 28 -637 A C ATOM 5783 C PHE A 716 35.091 13.174 68.763 1.00 14.88 A C ANISOU 5783 C PHE A 716 2333 1472 1846 72 161 -349 A C ATOM 5784 O PHE A 716 35.243 11.981 69.007 1.00 15.46 A O ANISOU 5784 O PHE A 716 2708 1386 1780 258 237 -474 A O ATOM 5785 CB PHE A 716 34.133 13.672 66.475 1.00 13.94 A C ANISOU 5785 CB PHE A 716 2286 1390 1617 91 270 -382 A C ATOM 5786 CG PHE A 716 34.268 12.262 65.943 1.00 14.57 A C ANISOU 5786 CG PHE A 716 2541 1441 1552 141 65 -392 A C ATOM 5787 CD1 PHE A 716 33.156 11.433 65.928 1.00 14.67 A C ANISOU 5787 CD1 PHE A 716 2276 1585 1711 175 144 -487 A C ATOM 5788 CD2 PHE A 716 35.479 11.762 65.516 1.00 14.50 A C ANISOU 5788 CD2 PHE A 716 2359 1331 1816 -42 85 -278 A C ATOM 5789 CE1 PHE A 716 33.271 10.121 65.483 1.00 14.99 A C ANISOU 5789 CE1 PHE A 716 2118 1552 2025 148 219 -479 A C ATOM 5790 CE2 PHE A 716 35.586 10.461 65.025 1.00 15.16 A C ANISOU 5790 CE2 PHE A 716 2145 1553 2062 229 119 -553 A C ATOM 5791 CZ PHE A 716 34.474 9.652 65.007 1.00 16.24 A C ANISOU 5791 CZ PHE A 716 2225 1767 2177 224 311 -137 A C ATOM 5792 N TYR A 717 36.008 14.098 69.088 1.00 15.60 A N ANISOU 5792 N TYR A 717 2438 1543 1943 153 -34 -555 A N ATOM 5793 CA TYR A 717 37.157 13.719 69.909 1.00 14.78 A C ANISOU 5793 CA TYR A 717 2246 1370 1998 -65 34 -611 A C ATOM 5794 C TYR A 717 36.668 13.042 71.204 1.00 17.04 A C ANISOU 5794 C TYR A 717 2692 1952 1830 318 -27 -485 A C ATOM 5795 O TYR A 717 37.306 12.085 71.701 1.00 17.26 A O ANISOU 5795 O TYR A 717 3139 1425 1992 175 -133 -478 A O ATOM 5796 CB TYR A 717 38.050 14.925 70.218 1.00 14.82 A C ANISOU 5796 CB TYR A 717 2224 1248 2158 15 181 -653 A C ATOM 5797 CG TYR A 717 39.174 15.194 69.246 1.00 14.10 A C ANISOU 5797 CG TYR A 717 2023 1244 2088 -254 -21 -493 A C ATOM 5798 CD1 TYR A 717 40.235 14.310 69.062 1.00 15.88 A C ANISOU 5798 CD1 TYR A 717 2388 1541 2102 -32 -34 -762 A C ATOM 5799 CD2 TYR A 717 39.220 16.376 68.542 1.00 14.64 A C ANISOU 5799 CD2 TYR A 717 2448 1227 1887 -24 -266 -565 A C ATOM 5800 CE1 TYR A 717 41.282 14.601 68.197 1.00 16.41 A C ANISOU 5800 CE1 TYR A 717 2641 1354 2240 -167 10 -496 A C ATOM 5801 CE2 TYR A 717 40.276 16.693 67.691 1.00 16.69 A C ANISOU 5801 CE2 TYR A 717 2495 1667 2177 -12 -47 -394 A C ATOM 5802 CZ TYR A 717 41.327 15.819 67.527 1.00 15.21 A C ANISOU 5802 CZ TYR A 717 2660 1167 1950 -124 -16 -728 A C ATOM 5803 OH TYR A 717 42.379 16.128 66.706 1.00 17.65 A O ANISOU 5803 OH TYR A 717 2753 1486 2465 -133 50 -883 A O ATOM 5804 N SER A 718 35.591 13.576 71.794 1.00 16.06 A N ANISOU 5804 N SER A 718 2752 1617 1732 205 165 -407 A N ATOM 5805 CA SER A 718 35.077 12.997 73.045 1.00 16.77 A C ANISOU 5805 CA SER A 718 2567 1990 1813 -53 54 -357 A C ATOM 5806 C SER A 718 34.548 11.582 72.786 1.00 17.51 A C ANISOU 5806 C SER A 718 2671 1972 2009 0 -113 -281 A C ATOM 5807 O SER A 718 34.750 10.712 73.619 1.00 18.85 A O ANISOU 5807 O SER A 718 3288 2006 1866 39 -77 -373 A O ATOM 5808 CB SER A 718 34.051 13.881 73.684 1.00 17.77 A C ANISOU 5808 CB SER A 718 2954 1941 1857 65 103 -297 A C ATOM 5809 OG SER A 718 34.646 15.101 74.103 1.00 21.55 A O ANISOU 5809 OG SER A 718 3803 2312 2072 -109 31 -1024 A O ATOM 5810 N MET A 719 33.876 11.369 71.635 1.00 16.04 A N ANISOU 5810 N MET A 719 2852 1489 1752 146 100 -264 A N ATOM 5811 CA MET A 719 33.469 10.008 71.256 1.00 15.06 A C ANISOU 5811 CA MET A 719 2426 1576 1719 137 39 -224 A C ATOM 5812 C MET A 719 34.696 9.112 71.069 1.00 15.19 A C ANISOU 5812 C MET A 719 2268 1857 1644 146 -133 -50 A C ATOM 5813 O MET A 719 34.722 7.959 71.551 1.00 16.89 A O ANISOU 5813 O MET A 719 2992 1416 2006 46 101 -265 A O ATOM 5814 CB MET A 719 32.677 10.018 69.946 1.00 16.34 A C ANISOU 5814 CB MET A 719 2505 1704 1997 208 -231 -294 A C ATOM 5815 CG MET A 719 31.418 10.844 70.005 1.00 15.93 A C ANISOU 5815 CG MET A 719 2402 1573 2077 -26 177 -49 A C ATOM 5816 SD MET A 719 30.357 10.594 68.565 1.00 17.00 A S ANISOU 5816 SD MET A 719 2729 1471 2257 89 42 -317 A S ATOM 5817 CE MET A 719 29.684 9.005 68.976 1.00 17.81 A C ANISOU 5817 CE MET A 719 3059 1554 2153 -224 -154 -116 A C ATOM 5818 N LEU A 720 35.704 9.609 70.369 1.00 14.82 A N ANISOU 5818 N LEU A 720 2429 1431 1769 60 -23 -409 A N ATOM 5819 CA LEU A 720 36.889 8.808 70.030 1.00 15.73 A C ANISOU 5819 CA LEU A 720 2325 1736 1914 168 -20 -389 A C ATOM 5820 C LEU A 720 37.665 8.389 71.276 1.00 17.08 A C ANISOU 5820 C LEU A 720 2851 1805 1834 486 -91 -513 A C ATOM 5821 O LEU A 720 38.227 7.290 71.295 1.00 18.08 A O ANISOU 5821 O LEU A 720 3015 1680 2175 256 -144 -183 A O ATOM 5822 CB LEU A 720 37.771 9.600 69.066 1.00 17.16 A C ANISOU 5822 CB LEU A 720 2371 1764 2382 32 133 -279 A C ATOM 5823 CG LEU A 720 39.015 8.888 68.550 1.00 17.08 A C ANISOU 5823 CG LEU A 720 2677 1478 2333 110 90 -437 A C ATOM 5824 CD1 LEU A 720 38.629 7.650 67.747 1.00 18.43 A C ANISOU 5824 CD1 LEU A 720 2928 1544 2531 93 250 -679 A C ATOM 5825 CD2 LEU A 720 39.863 9.816 67.714 1.00 19.13 A C ANISOU 5825 CD2 LEU A 720 2929 2081 2258 36 186 -326 A C ATOM 5826 N ARG A 721 37.601 9.190 72.343 1.00 18.58 A N ANISOU 5826 N ARG A 721 3299 1833 1925 25 -92 -589 A N ATOM 5827 CA ARG A 721 38.334 8.897 73.575 1.00 18.83 A C ANISOU 5827 CA ARG A 721 3145 2046 1961 9 -135 -421 A C ATOM 5828 C ARG A 721 37.546 7.979 74.520 1.00 19.61 A C ANISOU 5828 C ARG A 721 3235 1904 2311 -101 -70 -446 A C ATOM 5829 O ARG A 721 38.138 7.528 75.518 1.00 21.36 A O ANISOU 5829 O ARG A 721 3729 1994 2392 -90 -229 -136 A O ATOM 5830 CB ARG A 721 38.700 10.205 74.281 1.00 20.27 A C ANISOU 5830 CB ARG A 721 3147 2182 2371 -102 -244 -631 A C ATOM 5831 CG ARG A 721 39.690 11.047 73.502 1.00 22.17 A C ANISOU 5831 CG ARG A 721 3686 2650 2084 -111 -14 -444 A C ATOM 5832 CD ARG A 721 39.943 12.381 74.162 1.00 27.06 A C ANISOU 5832 CD ARG A 721 4663 2975 2644 -736 -325 -719 A C ATOM 5833 NE ARG A 721 40.384 12.227 75.541 1.00 31.62 A N ANISOU 5833 NE ARG A 721 5314 3902 2798 -1067 -1049 -1095 A N ATOM 5834 CZ ARG A 721 40.561 13.237 76.377 1.00 33.78 A C ANISOU 5834 CZ ARG A 721 5754 3778 3301 -954 -451 -1496 A C ATOM 5835 NH1 ARG A 721 40.002 14.408 76.119 1.00 33.59 A N ANISOU 5835 NH1 ARG A 721 4436 3994 4330 -786 613 -1276 A N ATOM 5836 NH2 ARG A 721 41.318 13.069 77.448 1.00 40.88 A N ANISOU 5836 NH2 ARG A 721 6805 5149 3579 -1376 -1220 -922 A N ATOM 5837 N GLN A 722 36.274 7.687 74.218 1.00 18.54 A N ANISOU 5837 N GLN A 722 2983 1830 2230 297 -26 -303 A N ATOM 5838 CA GLN A 722 35.476 6.815 75.120 1.00 20.71 A C ANISOU 5838 CA GLN A 722 3513 1841 2514 7 78 -307 A C ATOM 5839 C GLN A 722 36.077 5.405 75.119 1.00 19.63 A C ANISOU 5839 C GLN A 722 3526 1874 2057 -35 203 -329 A C ATOM 5840 O GLN A 722 36.471 4.922 74.075 1.00 20.17 A O ANISOU 5840 O GLN A 722 3420 2286 1956 6 66 -345 A O ATOM 5841 CB GLN A 722 34.028 6.685 74.661 1.00 22.69 A C ANISOU 5841 CB GLN A 722 3738 2689 2192 305 -238 -807 A C ATOM 5842 CG GLN A 722 33.216 7.938 74.839 1.00 27.18 A C ANISOU 5842 CG GLN A 722 4248 3576 2504 900 93 -475 A C ATOM 5843 CD GLN A 722 33.330 8.479 76.241 1.00 33.04 A C ANISOU 5843 CD GLN A 722 5745 4207 2599 396 -771 -525 A C ATOM 5844 NE2 GLN A 722 33.769 9.733 76.342 1.00 36.23 A N ANISOU 5844 NE2 GLN A 722 5456 3944 4362 435 -132 2 A N ATOM 5845 OE1 GLN A 722 33.012 7.781 77.212 1.00 37.21 A O ANISOU 5845 OE1 GLN A 722 7677 4693 1768 2161 581 -410 A O ATOM 5846 N THR A 723 36.137 4.782 76.299 1.00 18.56 A N ANISOU 5846 N THR A 723 3469 2040 1540 186 72 -592 A N ATOM 5847 CA THR A 723 36.669 3.443 76.409 1.00 20.32 A C ANISOU 5847 CA THR A 723 3709 1961 2049 157 -67 -468 A C ATOM 5848 C THR A 723 35.627 2.423 76.851 1.00 18.68 A C ANISOU 5848 C THR A 723 3304 2136 1657 134 -12 -618 A C ATOM 5849 O THR A 723 35.971 1.223 76.892 1.00 19.91 A O ANISOU 5849 O THR A 723 3579 1991 1993 143 327 -332 A O ATOM 5850 CB THR A 723 37.875 3.395 77.345 1.00 19.47 A C ANISOU 5850 CB THR A 723 3566 1876 1954 263 -44 -592 A C ATOM 5851 CG2 THR A 723 39.025 4.212 76.807 1.00 21.33 A C ANISOU 5851 CG2 THR A 723 3120 2829 2155 194 -240 -532 A C ATOM 5852 OG1 THR A 723 37.459 3.881 78.622 1.00 22.83 A O ANISOU 5852 OG1 THR A 723 4283 2889 1498 -110 -198 -542 A O ATOM 5853 N GLU A 724 34.409 2.865 77.186 1.00 19.91 A N ANISOU 5853 N GLU A 724 3311 2077 2177 -34 -91 -641 A N ATOM 5854 CA GLU A 724 33.329 1.955 77.540 1.00 20.58 A C ANISOU 5854 CA GLU A 724 3315 2408 2095 -84 -38 -258 A C ATOM 5855 C GLU A 724 32.540 1.564 76.294 1.00 19.24 A C ANISOU 5855 C GLU A 724 3554 1841 1912 -26 86 -245 A C ATOM 5856 O GLU A 724 32.514 2.263 75.326 1.00 19.22 A O ANISOU 5856 O GLU A 724 3433 1904 1963 140 -77 -192 A O ATOM 5857 CB GLU A 724 32.410 2.563 78.611 1.00 26.69 A C ANISOU 5857 CB GLU A 724 4183 3679 2276 -11 204 -692 A C ATOM 5858 CG GLU A 724 33.105 2.801 79.934 1.00 35.74 A C ANISOU 5858 CG GLU A 724 5538 5466 2576 -279 -166 -1457 A C ATOM 5859 CD GLU A 724 32.134 2.938 81.097 1.00 50.53 A C ANISOU 5859 CD GLU A 724 7841 8107 3250 249 1119 -470 A C ATOM 5860 OE1 GLU A 724 30.942 3.340 80.863 1.00 54.15 A O ANISOU 5860 OE1 GLU A 724 8633 7281 4658 1742 2002 -881 A O ATOM 5861 OE2 GLU A 724 32.551 2.631 82.238 1.00 71.75 A O ANISOU 5861 OE2 GLU A 724 11649 10374 5237 780 -1954 188 A O ATOM 5862 N VAL A 725 31.926 0.380 76.327 1.00 17.83 A N ANISOU 5862 N VAL A 725 3226 1732 1814 71 -85 -97 A N ATOM 5863 CA VAL A 725 31.158 -0.114 75.201 1.00 17.04 A C ANISOU 5863 CA VAL A 725 2948 1761 1765 184 318 -349 A C ATOM 5864 C VAL A 725 29.860 0.677 75.082 1.00 17.37 A C ANISOU 5864 C VAL A 725 2724 1893 1980 -45 231 -229 A C ATOM 5865 O VAL A 725 29.243 1.011 76.110 1.00 19.61 A O ANISOU 5865 O VAL A 725 3455 2212 1784 120 471 -56 A O ATOM 5866 CB VAL A 725 30.913 -1.623 75.369 1.00 19.06 A C ANISOU 5866 CB VAL A 725 3282 1684 2275 159 153 -297 A C ATOM 5867 CG1 VAL A 725 29.957 -1.943 76.504 1.00 21.80 A C ANISOU 5867 CG1 VAL A 725 3239 2522 2522 104 51 -64 A C ATOM 5868 CG2 VAL A 725 30.401 -2.271 74.093 1.00 18.97 A C ANISOU 5868 CG2 VAL A 725 3259 1455 2493 -91 355 -466 A C ATOM 5869 N PRO A 726 29.360 1.001 73.868 1.00 17.09 A N ANISOU 5869 N PRO A 726 2925 1603 1964 42 462 -63 A N ATOM 5870 CA PRO A 726 30.056 0.842 72.582 1.00 16.31 A C ANISOU 5870 CA PRO A 726 2651 1594 1951 233 304 -109 A C ATOM 5871 C PRO A 726 30.941 2.043 72.213 1.00 16.46 A C ANISOU 5871 C PRO A 726 2639 1625 1989 178 204 -80 A C ATOM 5872 O PRO A 726 30.511 3.213 72.353 1.00 17.44 A O ANISOU 5872 O PRO A 726 3116 1613 1894 206 395 -344 A O ATOM 5873 CB PRO A 726 28.857 0.741 71.621 1.00 15.68 A C ANISOU 5873 CB PRO A 726 2847 1507 1603 74 421 -314 A C ATOM 5874 CG PRO A 726 27.837 1.673 72.172 1.00 16.25 A C ANISOU 5874 CG PRO A 726 2663 1618 1894 255 302 -88 A C ATOM 5875 CD PRO A 726 27.994 1.524 73.674 1.00 16.94 A C ANISOU 5875 CD PRO A 726 2988 1568 1881 209 215 -177 A C ATOM 5876 N SER A 727 32.136 1.770 71.696 1.00 15.85 A N ANISOU 5876 N SER A 727 2536 1708 1778 120 83 -425 A N ATOM 5877 CA SER A 727 33.098 2.774 71.277 1.00 16.01 A C ANISOU 5877 CA SER A 727 2494 1787 1798 114 18 -288 A C ATOM 5878 C SER A 727 34.248 2.064 70.559 1.00 14.21 A C ANISOU 5878 C SER A 727 2285 1484 1627 -7 -97 -349 A C ATOM 5879 O SER A 727 34.350 0.831 70.591 1.00 16.44 A O ANISOU 5879 O SER A 727 2984 1397 1863 52 476 -299 A O ATOM 5880 CB SER A 727 33.649 3.565 72.456 1.00 16.70 A C ANISOU 5880 CB SER A 727 2611 1376 2358 100 -220 -419 A C ATOM 5881 OG SER A 727 34.404 2.708 73.294 1.00 16.74 A O ANISOU 5881 OG SER A 727 2840 1650 1868 127 -129 -383 A O ATOM 5882 N TRP A 728 35.118 2.812 69.908 1.00 16.07 A N ANISOU 5882 N TRP A 728 2406 1927 1773 59 61 -336 A N ATOM 5883 CA TRP A 728 36.312 2.218 69.289 1.00 14.48 A C ANISOU 5883 CA TRP A 728 2239 1601 1660 -76 -73 -300 A C ATOM 5884 C TRP A 728 37.343 1.738 70.320 1.00 15.53 A C ANISOU 5884 C TRP A 728 2685 1657 1556 132 -219 -377 A C ATOM 5885 O TRP A 728 37.855 0.624 70.229 1.00 15.52 A O ANISOU 5885 O TRP A 728 2837 1471 1585 154 211 -89 A O ATOM 5886 CB TRP A 728 36.957 3.194 68.326 1.00 14.00 A C ANISOU 5886 CB TRP A 728 2290 1178 1848 -148 -45 -345 A C ATOM 5887 CG TRP A 728 36.115 3.507 67.139 1.00 15.05 A C ANISOU 5887 CG TRP A 728 2355 1656 1704 26 64 -188 A C ATOM 5888 CD1 TRP A 728 36.075 2.815 65.970 1.00 15.40 A C ANISOU 5888 CD1 TRP A 728 2359 1585 1906 -328 10 -319 A C ATOM 5889 CD2 TRP A 728 35.234 4.629 66.962 1.00 14.53 A C ANISOU 5889 CD2 TRP A 728 2434 1344 1742 -73 109 -117 A C ATOM 5890 CE2 TRP A 728 34.669 4.516 65.677 1.00 14.93 A C ANISOU 5890 CE2 TRP A 728 2461 1275 1934 136 43 -283 A C ATOM 5891 CE3 TRP A 728 34.847 5.694 67.775 1.00 16.56 A C ANISOU 5891 CE3 TRP A 728 2668 1826 1798 236 -50 -336 A C ATOM 5892 NE1 TRP A 728 35.179 3.379 65.106 1.00 14.53 A N ANISOU 5892 NE1 TRP A 728 2361 1373 1786 29 -5 -567 A N ATOM 5893 CZ2 TRP A 728 33.738 5.428 65.184 1.00 14.81 A C ANISOU 5893 CZ2 TRP A 728 2254 1493 1877 6 -70 -134 A C ATOM 5894 CZ3 TRP A 728 33.921 6.593 67.293 1.00 17.32 A C ANISOU 5894 CZ3 TRP A 728 2913 1835 1830 266 177 -106 A C ATOM 5895 CH2 TRP A 728 33.384 6.463 66.013 1.00 15.91 A C ANISOU 5895 CH2 TRP A 728 2409 1727 1906 279 112 -12 A C ATOM 5896 N LEU A 729 37.649 2.571 71.318 1.00 15.50 A N ANISOU 5896 N LEU A 729 2560 1525 1804 165 -240 -523 A N ATOM 5897 CA LEU A 729 38.741 2.240 72.233 1.00 15.23 A C ANISOU 5897 CA LEU A 729 2324 1654 1808 131 -122 -397 A C ATOM 5898 C LEU A 729 38.325 1.174 73.235 1.00 16.30 A C ANISOU 5898 C LEU A 729 2729 1791 1670 -202 -230 -637 A C ATOM 5899 O LEU A 729 39.209 0.568 73.839 1.00 17.14 A O ANISOU 5899 O LEU A 729 2752 1948 1812 18 -171 -202 A O ATOM 5900 CB LEU A 729 39.245 3.498 72.956 1.00 16.18 A C ANISOU 5900 CB LEU A 729 2695 1674 1776 228 -328 -367 A C ATOM 5901 CG LEU A 729 39.856 4.549 72.059 1.00 17.57 A C ANISOU 5901 CG LEU A 729 2215 1890 2568 -65 -39 -323 A C ATOM 5902 CD1 LEU A 729 40.500 5.658 72.889 1.00 17.27 A C ANISOU 5902 CD1 LEU A 729 2838 1605 2118 3 84 -325 A C ATOM 5903 CD2 LEU A 729 40.833 3.973 71.059 1.00 16.11 A C ANISOU 5903 CD2 LEU A 729 2359 1682 2080 -194 -76 -103 A C ATOM 5904 N TYR A 730 37.024 0.919 73.387 1.00 15.87 A N ANISOU 5904 N TYR A 730 2741 1712 1576 0 16 -26 A N ATOM 5905 CA TYR A 730 36.624 -0.256 74.174 1.00 15.51 A C ANISOU 5905 CA TYR A 730 3032 1489 1369 25 -12 -230 A C ATOM 5906 C TYR A 730 37.309 -1.494 73.601 1.00 15.63 A C ANISOU 5906 C TYR A 730 2791 1682 1466 227 -239 -265 A C ATOM 5907 O TYR A 730 37.802 -2.335 74.330 1.00 16.26 A O ANISOU 5907 O TYR A 730 2911 1592 1673 243 -12 -114 A O ATOM 5908 CB TYR A 730 35.112 -0.425 74.161 1.00 16.34 A C ANISOU 5908 CB TYR A 730 2936 1548 1721 171 112 -152 A C ATOM 5909 CG TYR A 730 34.630 -1.763 74.642 1.00 15.40 A C ANISOU 5909 CG TYR A 730 2893 1316 1640 199 48 -359 A C ATOM 5910 CD1 TYR A 730 34.657 -2.062 75.982 1.00 16.50 A C ANISOU 5910 CD1 TYR A 730 2852 1706 1711 16 -34 -106 A C ATOM 5911 CD2 TYR A 730 34.149 -2.718 73.766 1.00 16.93 A C ANISOU 5911 CD2 TYR A 730 3154 1592 1685 -290 298 -375 A C ATOM 5912 CE1 TYR A 730 34.217 -3.291 76.443 1.00 17.64 A C ANISOU 5912 CE1 TYR A 730 3537 1509 1655 121 145 -17 A C ATOM 5913 CE2 TYR A 730 33.702 -3.953 74.195 1.00 18.12 A C ANISOU 5913 CE2 TYR A 730 3390 1282 2211 -125 284 -325 A C ATOM 5914 CZ TYR A 730 33.737 -4.242 75.551 1.00 20.33 A C ANISOU 5914 CZ TYR A 730 3604 1939 2180 -347 138 -262 A C ATOM 5915 OH TYR A 730 33.300 -5.458 75.994 1.00 21.30 A O ANISOU 5915 OH TYR A 730 4045 1687 2361 6 436 -321 A O ATOM 5916 N GLN A 731 37.283 -1.611 72.270 1.00 15.28 A N ANISOU 5916 N GLN A 731 2916 1430 1456 348 -206 -355 A N ATOM 5917 CA GLN A 731 37.847 -2.818 71.655 1.00 14.03 A C ANISOU 5917 CA GLN A 731 2514 1405 1410 234 185 -205 A C ATOM 5918 C GLN A 731 39.361 -2.881 71.920 1.00 15.02 A C ANISOU 5918 C GLN A 731 2616 1496 1593 151 -96 -222 A C ATOM 5919 O GLN A 731 39.895 -3.954 72.173 1.00 16.51 A O ANISOU 5919 O GLN A 731 2781 1522 1968 356 -246 -250 A O ATOM 5920 CB GLN A 731 37.523 -2.872 70.151 1.00 14.94 A C ANISOU 5920 CB GLN A 731 2710 1381 1582 76 -231 -407 A C ATOM 5921 CG GLN A 731 36.051 -2.684 69.854 1.00 16.04 A C ANISOU 5921 CG GLN A 731 2465 1588 2039 -296 -45 -288 A C ATOM 5922 CD GLN A 731 35.639 -2.922 68.421 1.00 15.73 A C ANISOU 5922 CD GLN A 731 2501 1414 2061 24 114 -343 A C ATOM 5923 NE2 GLN A 731 34.352 -3.202 68.206 1.00 15.88 A N ANISOU 5923 NE2 GLN A 731 2405 1433 2194 155 -20 -455 A N ATOM 5924 OE1 GLN A 731 36.462 -2.844 67.507 1.00 14.98 A O ANISOU 5924 OE1 GLN A 731 2456 1305 1931 42 100 -318 A O ATOM 5925 N VAL A 732 40.023 -1.718 72.000 1.00 15.05 A N ANISOU 5925 N VAL A 732 2558 1617 1542 36 13 -336 A N ATOM 5926 CA VAL A 732 41.456 -1.624 72.264 1.00 15.53 A C ANISOU 5926 CA VAL A 732 2731 1503 1663 181 115 -314 A C ATOM 5927 C VAL A 732 41.769 -2.049 73.723 1.00 16.96 A C ANISOU 5927 C VAL A 732 2698 1905 1840 84 -181 -165 A C ATOM 5928 O VAL A 732 42.700 -2.836 74.000 1.00 18.08 A O ANISOU 5928 O VAL A 732 2979 2286 1605 285 -205 -1 A O ATOM 5929 CB VAL A 732 41.967 -0.194 71.967 1.00 16.70 A C ANISOU 5929 CB VAL A 732 2973 1567 1805 -88 4 -450 A C ATOM 5930 CG1 VAL A 732 43.414 -0.047 72.387 1.00 17.85 A C ANISOU 5930 CG1 VAL A 732 2954 1621 2205 -54 -42 -153 A C ATOM 5931 CG2 VAL A 732 41.837 0.118 70.466 1.00 15.97 A C ANISOU 5931 CG2 VAL A 732 2602 1624 1840 76 -17 -483 A C ATOM 5932 N VAL A 733 41.012 -1.523 74.678 1.00 17.56 A N ANISOU 5932 N VAL A 733 3130 1824 1719 299 -160 -81 A N ATOM 5933 CA VAL A 733 41.297 -1.792 76.084 1.00 18.47 A C ANISOU 5933 CA VAL A 733 3087 2238 1693 421 -91 -92 A C ATOM 5934 C VAL A 733 40.885 -3.226 76.435 1.00 19.88 A C ANISOU 5934 C VAL A 733 3503 2428 1620 91 -247 -197 A C ATOM 5935 O VAL A 733 41.350 -3.712 77.455 1.00 22.54 A O ANISOU 5935 O VAL A 733 4072 2488 2004 203 -630 -162 A O ATOM 5936 CB VAL A 733 40.712 -0.729 77.035 1.00 19.99 A C ANISOU 5936 CB VAL A 733 3613 1959 2022 169 -271 -299 A C ATOM 5937 CG1 VAL A 733 41.220 0.668 76.702 1.00 20.73 A C ANISOU 5937 CG1 VAL A 733 3387 2256 2231 -42 -380 -264 A C ATOM 5938 CG2 VAL A 733 39.196 -0.772 77.125 1.00 22.63 A C ANISOU 5938 CG2 VAL A 733 3779 2687 2130 603 82 -298 A C ATOM 5939 N MET A 734 40.080 -3.896 75.591 1.00 17.66 A N ANISOU 5939 N MET A 734 3425 1668 1617 267 -334 168 A N ATOM 5940 CA MET A 734 39.755 -5.325 75.761 1.00 16.51 A C ANISOU 5940 CA MET A 734 3205 1678 1389 56 -122 99 A C ATOM 5941 C MET A 734 40.800 -6.215 75.065 1.00 18.72 A C ANISOU 5941 C MET A 734 3187 2176 1747 4 11 -132 A C ATOM 5942 O MET A 734 40.596 -7.415 74.913 1.00 21.63 A O ANISOU 5942 O MET A 734 4003 2064 2150 109 273 103 A O ATOM 5943 CB MET A 734 38.367 -5.607 75.197 1.00 18.08 A C ANISOU 5943 CB MET A 734 3358 1657 1854 -59 -134 4 A C ATOM 5944 CG MET A 734 37.252 -4.986 76.006 1.00 20.74 A C ANISOU 5944 CG MET A 734 2981 2285 2612 -57 197 263 A C ATOM 5945 SD MET A 734 37.090 -5.711 77.649 1.00 22.98 A S ANISOU 5945 SD MET A 734 4017 2204 2508 208 421 -23 A S ATOM 5946 CE MET A 734 36.511 -7.349 77.236 1.00 25.61 A C ANISOU 5946 CE MET A 734 4900 1696 3133 347 1205 92 A C ATOM 5947 N ASN A 735 41.939 -5.634 74.707 1.00 17.84 A N ANISOU 5947 N ASN A 735 2934 2024 1820 224 -230 -151 A N ATOM 5948 CA ASN A 735 43.113 -6.306 74.106 1.00 18.74 A C ANISOU 5948 CA ASN A 735 3479 2092 1549 457 -176 327 A C ATOM 5949 C ASN A 735 42.827 -6.676 72.662 1.00 18.13 A C ANISOU 5949 C ASN A 735 3288 2019 1581 632 70 -100 A C ATOM 5950 O ASN A 735 43.476 -7.558 72.107 1.00 18.64 A O ANISOU 5950 O ASN A 735 3035 2057 1987 512 -20 -173 A O ATOM 5951 CB ASN A 735 43.575 -7.558 74.854 1.00 19.72 A C ANISOU 5951 CB ASN A 735 3911 1637 1942 354 -444 18 A C ATOM 5952 CG ASN A 735 43.997 -7.229 76.249 1.00 28.72 A C ANISOU 5952 CG ASN A 735 4895 3713 2304 -201 -1275 -81 A C ATOM 5953 ND2 ASN A 735 43.737 -8.159 77.158 1.00 34.22 A N ANISOU 5953 ND2 ASN A 735 5947 4587 2466 502 -903 535 A N ATOM 5954 OD1 ASN A 735 44.527 -6.138 76.458 1.00 28.99 A O ANISOU 5954 OD1 ASN A 735 4834 3550 2629 -192 -1121 89 A O ATOM 5955 N GLY A 736 41.868 -6.010 72.044 1.00 16.76 A N ANISOU 5955 N GLY A 736 2878 2076 1414 323 161 -249 A N ATOM 5956 CA GLY A 736 41.710 -6.111 70.609 1.00 15.22 A C ANISOU 5956 CA GLY A 736 2535 1671 1576 280 -303 -195 A C ATOM 5957 C GLY A 736 42.934 -5.628 69.856 1.00 15.20 A C ANISOU 5957 C GLY A 736 2566 1591 1617 350 -196 -266 A C ATOM 5958 O GLY A 736 43.552 -4.631 70.261 1.00 16.48 A O ANISOU 5958 O GLY A 736 2922 1719 1618 -39 -263 -40 A O ATOM 5959 N THR A 737 43.274 -6.330 68.768 1.00 13.35 A N ANISOU 5959 N THR A 737 2136 1286 1647 151 -360 -327 A N ATOM 5960 CA THR A 737 44.395 -5.989 67.910 1.00 15.07 A C ANISOU 5960 CA THR A 737 2242 1757 1723 -25 -276 -127 A C ATOM 5961 C THR A 737 43.947 -5.807 66.444 1.00 13.05 A C ANISOU 5961 C THR A 737 2203 968 1787 19 -234 -307 A C ATOM 5962 O THR A 737 44.782 -5.641 65.550 1.00 13.52 A O ANISOU 5962 O THR A 737 2128 1192 1814 48 -180 -282 A O ATOM 5963 CB THR A 737 45.517 -7.028 68.033 1.00 15.24 A C ANISOU 5963 CB THR A 737 2330 1567 1893 -12 -356 -299 A C ATOM 5964 CG2 THR A 737 46.148 -7.022 69.408 1.00 16.72 A C ANISOU 5964 CG2 THR A 737 2817 1630 1902 60 -479 -200 A C ATOM 5965 OG1 THR A 737 45.030 -8.335 67.736 1.00 13.89 A O ANISOU 5965 OG1 THR A 737 2456 1266 1555 107 -266 -94 A O ATOM 5966 N THR A 738 42.629 -5.785 66.264 1.00 12.79 A N ANISOU 5966 N THR A 738 2039 1308 1512 9 -69 -196 A N ATOM 5967 CA THR A 738 41.920 -5.622 65.008 1.00 12.79 A C ANISOU 5967 CA THR A 738 1996 1270 1590 50 -77 -90 A C ATOM 5968 C THR A 738 40.622 -4.914 65.374 1.00 13.68 A C ANISOU 5968 C THR A 738 1970 1409 1817 -70 -19 -63 A C ATOM 5969 O THR A 738 40.257 -4.910 66.536 1.00 14.65 A O ANISOU 5969 O THR A 738 2459 1405 1701 348 40 -150 A O ATOM 5970 CB THR A 738 41.630 -6.967 64.333 1.00 14.22 A C ANISOU 5970 CB THR A 738 2185 1401 1816 -131 -91 -143 A C ATOM 5971 CG2 THR A 738 42.850 -7.539 63.656 1.00 15.70 A C ANISOU 5971 CG2 THR A 738 2039 1676 2248 -207 -48 -225 A C ATOM 5972 OG1 THR A 738 41.101 -7.891 65.275 1.00 14.40 A O ANISOU 5972 OG1 THR A 738 2425 1130 1916 117 -100 -200 A O ATOM 5973 N THR A 739 39.927 -4.361 64.383 1.00 13.55 A N ANISOU 5973 N THR A 739 2066 1399 1682 113 -92 -182 A N ATOM 5974 CA THR A 739 38.578 -3.860 64.622 1.00 13.25 A C ANISOU 5974 CA THR A 739 1916 1659 1459 -47 -280 -307 A C ATOM 5975 C THR A 739 37.604 -5.029 64.506 1.00 13.29 A C ANISOU 5975 C THR A 739 2293 1181 1574 -4 67 -257 A C ATOM 5976 O THR A 739 37.787 -5.954 63.722 1.00 13.25 A O ANISOU 5976 O THR A 739 2169 1124 1739 192 -74 -301 A O ATOM 5977 CB THR A 739 38.250 -2.686 63.686 1.00 14.15 A C ANISOU 5977 CB THR A 739 2086 1658 1631 -13 9 -139 A C ATOM 5978 CG2 THR A 739 39.051 -1.453 64.043 1.00 13.46 A C ANISOU 5978 CG2 THR A 739 2203 1434 1476 200 10 -231 A C ATOM 5979 OG1 THR A 739 38.474 -2.993 62.302 1.00 14.00 A O ANISOU 5979 OG1 THR A 739 2181 1413 1725 241 -47 -277 A O ATOM 5980 N TRP A 740 36.517 -4.954 65.287 1.00 13.77 A N ANISOU 5980 N TRP A 740 2257 1258 1717 114 97 -376 A N ATOM 5981 CA TRP A 740 35.558 -6.074 65.398 1.00 14.50 A C ANISOU 5981 CA TRP A 740 2291 1485 1730 -56 -8 -230 A C ATOM 5982 C TRP A 740 34.299 -5.759 64.589 1.00 14.21 A C ANISOU 5982 C TRP A 740 2159 1263 1974 103 -100 -245 A C ATOM 5983 O TRP A 740 33.941 -4.607 64.364 1.00 15.56 A O ANISOU 5983 O TRP A 740 2099 1333 2479 342 81 -117 A O ATOM 5984 CB TRP A 740 35.183 -6.339 66.859 1.00 13.84 A C ANISOU 5984 CB TRP A 740 2313 1158 1787 108 16 -201 A C ATOM 5985 CG TRP A 740 36.345 -6.536 67.777 1.00 13.96 A C ANISOU 5985 CG TRP A 740 2303 1411 1590 81 95 -86 A C ATOM 5986 CD1 TRP A 740 37.630 -6.890 67.484 1.00 14.67 A C ANISOU 5986 CD1 TRP A 740 2245 1427 1899 12 -53 -247 A C ATOM 5987 CD2 TRP A 740 36.264 -6.480 69.209 1.00 14.50 A C ANISOU 5987 CD2 TRP A 740 2550 1436 1523 -150 62 -76 A C ATOM 5988 CE2 TRP A 740 37.548 -6.772 69.714 1.00 15.26 A C ANISOU 5988 CE2 TRP A 740 2648 1367 1780 -12 122 -191 A C ATOM 5989 CE3 TRP A 740 35.235 -6.144 70.092 1.00 16.34 A C ANISOU 5989 CE3 TRP A 740 2252 1667 2287 -203 141 -191 A C ATOM 5990 NE1 TRP A 740 38.360 -7.036 68.640 1.00 14.76 A N ANISOU 5990 NE1 TRP A 740 2475 1379 1754 243 7 -213 A N ATOM 5991 CZ2 TRP A 740 37.821 -6.807 71.087 1.00 17.74 A C ANISOU 5991 CZ2 TRP A 740 2835 2094 1810 -174 55 -140 A C ATOM 5992 CZ3 TRP A 740 35.498 -6.163 71.446 1.00 17.12 A C ANISOU 5992 CZ3 TRP A 740 2569 1863 2073 -118 348 -504 A C ATOM 5993 CH2 TRP A 740 36.771 -6.496 71.934 1.00 17.04 A C ANISOU 5993 CH2 TRP A 740 2850 1953 1670 -171 -25 -486 A C ATOM 5994 N GLU A 741 33.597 -6.792 64.162 1.00 13.23 A N ANISOU 5994 N GLU A 741 1865 1407 1752 147 232 -354 A N ATOM 5995 CA GLU A 741 32.347 -6.671 63.419 1.00 12.51 A C ANISOU 5995 CA GLU A 741 2146 1114 1492 105 184 -62 A C ATOM 5996 C GLU A 741 31.304 -5.875 64.200 1.00 15.24 A C ANISOU 5996 C GLU A 741 2137 1856 1797 511 17 -141 A C ATOM 5997 O GLU A 741 30.660 -4.984 63.637 1.00 14.48 A O ANISOU 5997 O GLU A 741 2272 1524 1706 369 -35 -267 A O ATOM 5998 CB GLU A 741 31.852 -8.076 63.118 1.00 14.01 A C ANISOU 5998 CB GLU A 741 2177 1079 2066 8 236 81 A C ATOM 5999 CG GLU A 741 30.536 -8.187 62.377 1.00 14.21 A C ANISOU 5999 CG GLU A 741 1877 1381 2138 270 407 -443 A C ATOM 6000 CD GLU A 741 30.126 -9.609 62.028 1.00 14.97 A C ANISOU 6000 CD GLU A 741 1973 1487 2228 232 225 -386 A C ATOM 6001 OE1 GLU A 741 30.446 -10.529 62.822 1.00 15.27 A O ANISOU 6001 OE1 GLU A 741 2349 1406 2045 35 100 -532 A O ATOM 6002 OE2 GLU A 741 29.462 -9.756 60.960 1.00 14.52 A O ANISOU 6002 OE2 GLU A 741 2181 1257 2079 161 160 54 A O ATOM 6003 N ARG A 742 31.065 -6.298 65.441 1.00 13.90 A N ANISOU 6003 N ARG A 742 2108 1412 1762 48 241 -325 A N ATOM 6004 CA ARG A 742 30.140 -5.660 66.323 1.00 15.69 A C ANISOU 6004 CA ARG A 742 2110 1859 1992 72 267 -276 A C ATOM 6005 C ARG A 742 30.906 -4.738 67.281 1.00 16.33 A C ANISOU 6005 C ARG A 742 2444 1652 2107 159 60 -269 A C ATOM 6006 O ARG A 742 32.019 -5.039 67.703 1.00 16.17 A O ANISOU 6006 O ARG A 742 2435 1693 2014 302 290 -621 A O ATOM 6007 CB ARG A 742 29.470 -6.694 67.216 1.00 14.62 A C ANISOU 6007 CB ARG A 742 2368 1600 1586 217 343 -251 A C ATOM 6008 CG ARG A 742 28.707 -7.764 66.457 1.00 15.17 A C ANISOU 6008 CG ARG A 742 2372 1662 1727 36 264 -86 A C ATOM 6009 CD ARG A 742 28.241 -8.864 67.383 1.00 15.78 A C ANISOU 6009 CD ARG A 742 2479 1799 1718 -96 414 -175 A C ATOM 6010 NE ARG A 742 27.296 -9.787 66.747 1.00 15.03 A N ANISOU 6010 NE ARG A 742 2130 1613 1968 -108 17 153 A N ATOM 6011 CZ ARG A 742 25.995 -9.543 66.548 1.00 15.63 A C ANISOU 6011 CZ ARG A 742 2074 1875 1987 -62 185 -175 A C ATOM 6012 NH1 ARG A 742 25.409 -8.437 67.040 1.00 15.91 A N ANISOU 6012 NH1 ARG A 742 2165 1828 2052 114 300 -20 A N ATOM 6013 NH2 ARG A 742 25.278 -10.417 65.855 1.00 15.91 A N ANISOU 6013 NH2 ARG A 742 2240 1742 2061 -356 -9 -60 A N ATOM 6014 N TRP A 743 30.265 -3.641 67.680 1.00 15.66 A N ANISOU 6014 N TRP A 743 2420 1592 1936 205 22 -193 A N ATOM 6015 CA TRP A 743 30.866 -2.805 68.733 1.00 15.47 A C ANISOU 6015 CA TRP A 743 2262 1498 2117 167 162 -363 A C ATOM 6016 C TRP A 743 31.224 -3.702 69.933 1.00 14.55 A C ANISOU 6016 C TRP A 743 2372 829 2325 383 321 -322 A C ATOM 6017 O TRP A 743 32.319 -3.587 70.552 1.00 16.58 A O ANISOU 6017 O TRP A 743 2679 1757 1863 70 345 -173 A O ATOM 6018 CB TRP A 743 29.933 -1.643 69.121 1.00 15.57 A C ANISOU 6018 CB TRP A 743 2460 1374 2082 202 246 -225 A C ATOM 6019 CG TRP A 743 29.693 -0.698 67.981 1.00 14.37 A C ANISOU 6019 CG TRP A 743 2194 1402 1864 236 279 -357 A C ATOM 6020 CD1 TRP A 743 28.560 -0.516 67.265 1.00 13.49 A C ANISOU 6020 CD1 TRP A 743 2076 974 2072 -184 201 -94 A C ATOM 6021 CD2 TRP A 743 30.650 0.221 67.459 1.00 14.46 A C ANISOU 6021 CD2 TRP A 743 2139 1443 1909 174 79 -362 A C ATOM 6022 CE2 TRP A 743 30.037 0.878 66.375 1.00 13.03 A C ANISOU 6022 CE2 TRP A 743 1938 1221 1791 135 18 -362 A C ATOM 6023 CE3 TRP A 743 31.996 0.491 67.754 1.00 14.60 A C ANISOU 6023 CE3 TRP A 743 2078 1510 1958 128 147 -427 A C ATOM 6024 NE1 TRP A 743 28.746 0.440 66.295 1.00 14.54 A N ANISOU 6024 NE1 TRP A 743 2210 1205 2109 40 266 -81 A N ATOM 6025 CZ2 TRP A 743 30.681 1.880 65.666 1.00 14.38 A C ANISOU 6025 CZ2 TRP A 743 2315 1324 1822 172 52 -345 A C ATOM 6026 CZ3 TRP A 743 32.632 1.478 67.040 1.00 15.75 A C ANISOU 6026 CZ3 TRP A 743 2319 1640 2023 -111 97 -372 A C ATOM 6027 CH2 TRP A 743 31.987 2.130 65.987 1.00 15.84 A C ANISOU 6027 CH2 TRP A 743 2251 1430 2338 93 62 -401 A C ATOM 6028 N ASP A 744 30.332 -4.655 70.210 1.00 16.84 A N ANISOU 6028 N ASP A 744 2741 1488 2168 98 442 -330 A N ATOM 6029 CA ASP A 744 30.445 -5.542 71.382 1.00 16.48 A C ANISOU 6029 CA ASP A 744 2795 1850 1614 345 345 -363 A C ATOM 6030 C ASP A 744 30.687 -7.000 70.944 1.00 16.94 A C ANISOU 6030 C ASP A 744 2352 1818 2265 -272 562 -471 A C ATOM 6031 O ASP A 744 30.064 -7.904 71.496 1.00 16.59 A O ANISOU 6031 O ASP A 744 2555 1529 2219 -20 420 -187 A O ATOM 6032 CB ASP A 744 29.179 -5.437 72.270 1.00 16.95 A C ANISOU 6032 CB ASP A 744 2794 1739 1906 270 352 -54 A C ATOM 6033 CG ASP A 744 27.862 -5.699 71.543 1.00 18.65 A C ANISOU 6033 CG ASP A 744 2840 1612 2634 202 403 -196 A C ATOM 6034 OD1 ASP A 744 27.875 -5.855 70.283 1.00 20.49 A O ANISOU 6034 OD1 ASP A 744 3198 2062 2524 411 221 -241 A O ATOM 6035 OD2 ASP A 744 26.815 -5.630 72.192 1.00 25.10 A O ANISOU 6035 OD2 ASP A 744 3579 3264 2691 -40 893 -500 A O ATOM 6036 N SER A 745 31.605 -7.269 70.003 1.00 15.19 A N ANISOU 6036 N SER A 745 2688 1303 1779 -46 448 44 A N ATOM 6037 CA SER A 745 31.858 -8.668 69.632 1.00 16.09 A C ANISOU 6037 CA SER A 745 2649 1505 1958 92 -37 -413 A C ATOM 6038 C SER A 745 32.265 -9.440 70.885 1.00 16.30 A C ANISOU 6038 C SER A 745 2785 1774 1634 -141 424 -243 A C ATOM 6039 O SER A 745 31.949 -10.625 71.005 1.00 17.81 A O ANISOU 6039 O SER A 745 3082 1511 2171 113 670 -308 A O ATOM 6040 CB SER A 745 32.900 -8.802 68.554 1.00 16.78 A C ANISOU 6040 CB SER A 745 2760 1526 2090 265 64 15 A C ATOM 6041 OG SER A 745 32.359 -8.562 67.253 1.00 15.92 A O ANISOU 6041 OG SER A 745 2495 1511 2040 181 95 136 A O ATOM 6042 N MET A 746 33.029 -8.796 71.778 1.00 16.04 A N ANISOU 6042 N MET A 746 2479 2156 1457 -170 523 -148 A N ATOM 6043 CA MET A 746 33.261 -9.332 73.145 1.00 16.61 A C ANISOU 6043 CA MET A 746 3112 1764 1435 323 601 -145 A C ATOM 6044 C MET A 746 32.573 -8.406 74.157 1.00 17.78 A C ANISOU 6044 C MET A 746 3535 1470 1750 389 593 -229 A C ATOM 6045 O MET A 746 32.653 -7.173 74.013 1.00 19.03 A O ANISOU 6045 O MET A 746 3494 1500 2237 -42 500 -330 A O ATOM 6046 CB MET A 746 34.756 -9.395 73.477 1.00 19.75 A C ANISOU 6046 CB MET A 746 3213 2373 1917 230 638 2 A C ATOM 6047 CG MET A 746 35.106 -10.027 74.823 1.00 21.29 A C ANISOU 6047 CG MET A 746 4034 2007 2047 271 339 -325 A C ATOM 6048 SD MET A 746 36.898 -10.347 74.962 1.00 28.95 A S ANISOU 6048 SD MET A 746 4625 3621 2751 816 362 -154 A S ATOM 6049 CE MET A 746 37.043 -11.762 73.853 1.00 26.31 A C ANISOU 6049 CE MET A 746 3619 3591 2786 988 1012 -146 A C ATOM 6050 N LEU A 747 31.918 -9.000 75.157 1.00 20.23 A N ANISOU 6050 N LEU A 747 3730 2245 1710 326 756 -406 A N ATOM 6051 CA LEU A 747 31.260 -8.256 76.216 1.00 20.17 A C ANISOU 6051 CA LEU A 747 3519 2162 1983 106 1056 -368 A C ATOM 6052 C LEU A 747 32.288 -7.927 77.303 1.00 22.17 A C ANISOU 6052 C LEU A 747 3796 2441 2187 397 549 -279 A C ATOM 6053 O LEU A 747 33.365 -8.506 77.378 1.00 20.89 A O ANISOU 6053 O LEU A 747 4229 1784 1923 248 608 -18 A O ATOM 6054 CB LEU A 747 30.090 -9.094 76.745 1.00 22.42 A C ANISOU 6054 CB LEU A 747 3337 2808 2371 100 1295 -376 A C ATOM 6055 CG LEU A 747 29.136 -9.636 75.682 1.00 25.13 A C ANISOU 6055 CG LEU A 747 4114 2767 2665 79 800 -249 A C ATOM 6056 CD1 LEU A 747 28.029 -10.441 76.339 1.00 30.95 A C ANISOU 6056 CD1 LEU A 747 4243 4362 3151 -258 1156 -138 A C ATOM 6057 CD2 LEU A 747 28.543 -8.525 74.823 1.00 26.17 A C ANISOU 6057 CD2 LEU A 747 4552 2694 2696 7 769 -329 A C ATOM 6058 N PRO A 748 32.054 -6.914 78.167 1.00 23.31 A N ANISOU 6058 N PRO A 748 4351 2137 2367 -17 782 -145 A N ATOM 6059 CA PRO A 748 33.091 -6.485 79.109 1.00 25.34 A C ANISOU 6059 CA PRO A 748 4744 2407 2474 464 252 -302 A C ATOM 6060 C PRO A 748 33.692 -7.522 80.068 1.00 26.78 A C ANISOU 6060 C PRO A 748 4773 2820 2581 404 224 -43 A C ATOM 6061 O PRO A 748 34.852 -7.354 80.477 1.00 30.69 A O ANISOU 6061 O PRO A 748 5066 3862 2734 -158 74 -326 A O ATOM 6062 CB PRO A 748 32.422 -5.333 79.891 1.00 25.93 A C ANISOU 6062 CB PRO A 748 4752 2448 2651 202 588 -542 A C ATOM 6063 CG PRO A 748 31.336 -4.835 78.937 1.00 26.00 A C ANISOU 6063 CG PRO A 748 5298 2061 2517 229 486 -384 A C ATOM 6064 CD PRO A 748 30.855 -6.072 78.197 1.00 25.28 A C ANISOU 6064 CD PRO A 748 4318 2714 2571 154 757 -673 A C ATOM 6065 N ASN A 749 32.984 -8.618 80.350 1.00 26.53 A N ANISOU 6065 N ASN A 749 5167 2960 1953 47 646 -367 A N ATOM 6066 CA ASN A 749 33.554 -9.666 81.256 1.00 30.73 A C ANISOU 6066 CA ASN A 749 5521 3656 2498 715 430 -58 A C ATOM 6067 C ASN A 749 34.347 -10.703 80.459 1.00 29.19 A C ANISOU 6067 C ASN A 749 5284 3339 2465 776 -173 -4 A C ATOM 6068 O ASN A 749 34.875 -11.640 81.032 1.00 32.17 A O ANISOU 6068 O ASN A 749 6476 2759 2986 1017 642 221 A O ATOM 6069 CB ASN A 749 32.496 -10.417 82.060 1.00 35.24 A C ANISOU 6069 CB ASN A 749 5286 4605 3495 353 155 569 A C ATOM 6070 CG ASN A 749 31.411 -10.988 81.181 1.00 33.12 A C ANISOU 6070 CG ASN A 749 5043 4926 2614 80 676 357 A C ATOM 6071 ND2 ASN A 749 30.312 -11.351 81.813 1.00 35.76 A N ANISOU 6071 ND2 ASN A 749 5439 5331 2816 117 1329 -165 A N ATOM 6072 OD1 ASN A 749 31.558 -11.095 79.953 1.00 32.65 A O ANISOU 6072 OD1 ASN A 749 6638 2929 2835 664 1202 -124 A O ATOM 6073 N GLY A 750 34.389 -10.569 79.133 1.00 27.31 A N ANISOU 6073 N GLY A 750 5097 2687 2592 720 -82 275 A N ATOM 6074 CA GLY A 750 35.226 -11.448 78.334 1.00 29.62 A C ANISOU 6074 CA GLY A 750 5051 3339 2862 809 90 47 A C ATOM 6075 C GLY A 750 34.429 -12.443 77.524 1.00 26.79 A C ANISOU 6075 C GLY A 750 3411 2762 4004 928 292 173 A C ATOM 6076 O GLY A 750 35.026 -13.153 76.721 1.00 29.34 A O ANISOU 6076 O GLY A 750 4652 2864 3631 747 105 -243 A O ATOM 6077 N SER A 751 33.126 -12.569 77.787 1.00 23.74 A N ANISOU 6077 N SER A 751 3686 2539 2793 210 599 33 A N ATOM 6078 CA SER A 751 32.260 -13.474 77.017 1.00 23.86 A C ANISOU 6078 CA SER A 751 3967 2835 2260 -101 259 661 A C ATOM 6079 C SER A 751 32.058 -12.945 75.597 1.00 20.35 A C ANISOU 6079 C SER A 751 4297 1598 1838 -142 309 -30 A C ATOM 6080 O SER A 751 32.000 -11.729 75.395 1.00 22.14 A O ANISOU 6080 O SER A 751 4228 1675 2508 4 500 224 A O ATOM 6081 CB SER A 751 30.923 -13.636 77.681 1.00 28.18 A C ANISOU 6081 CB SER A 751 4653 3374 2676 -394 989 1025 A C ATOM 6082 OG SER A 751 31.072 -14.391 78.865 1.00 31.05 A O ANISOU 6082 OG SER A 751 5357 3827 2613 133 556 1001 A O ATOM 6083 N ILE A 752 31.946 -13.872 74.632 1.00 19.56 A N ANISOU 6083 N ILE A 752 4006 1648 1776 115 311 -164 A N ATOM 6084 CA ILE A 752 31.680 -13.516 73.253 1.00 18.11 A C ANISOU 6084 CA ILE A 752 3452 1361 2067 68 -106 -203 A C ATOM 6085 C ILE A 752 30.196 -13.170 73.119 1.00 18.20 A C ANISOU 6085 C ILE A 752 3263 2076 1573 284 483 -53 A C ATOM 6086 O ILE A 752 29.352 -13.746 73.770 1.00 21.51 A O ANISOU 6086 O ILE A 752 3442 2632 2099 -285 348 63 A O ATOM 6087 CB ILE A 752 32.143 -14.633 72.283 1.00 20.01 A C ANISOU 6087 CB ILE A 752 3465 1761 2375 -16 384 -428 A C ATOM 6088 CG1 ILE A 752 33.642 -14.896 72.425 1.00 21.90 A C ANISOU 6088 CG1 ILE A 752 3419 2073 2826 -45 100 -391 A C ATOM 6089 CG2 ILE A 752 31.770 -14.325 70.833 1.00 20.62 A C ANISOU 6089 CG2 ILE A 752 3603 1623 2608 -22 494 -317 A C ATOM 6090 CD1 ILE A 752 34.133 -16.090 71.584 1.00 22.96 A C ANISOU 6090 CD1 ILE A 752 3703 2206 2813 430 360 62 A C ATOM 6091 N ASN A 753 29.900 -12.170 72.273 1.00 18.23 A N ANISOU 6091 N ASN A 753 3072 2015 1839 -311 619 175 A N ATOM 6092 CA ASN A 753 28.541 -11.812 71.953 1.00 18.20 A C ANISOU 6092 CA ASN A 753 3341 1623 1951 -373 445 45 A C ATOM 6093 C ASN A 753 27.754 -13.080 71.615 1.00 18.72 A C ANISOU 6093 C ASN A 753 2985 1985 2141 -354 417 -238 A C ATOM 6094 O ASN A 753 28.251 -13.924 70.871 1.00 19.55 A O ANISOU 6094 O ASN A 753 3496 1778 2152 -25 759 188 A O ATOM 6095 CB ASN A 753 28.517 -10.847 70.780 1.00 17.34 A C ANISOU 6095 CB ASN A 753 2686 1633 2267 -185 508 229 A C ATOM 6096 CG ASN A 753 27.160 -10.232 70.554 1.00 17.47 A C ANISOU 6096 CG ASN A 753 2857 1496 2283 140 540 -306 A C ATOM 6097 ND2 ASN A 753 27.079 -8.928 70.803 1.00 18.80 A N ANISOU 6097 ND2 ASN A 753 3447 1300 2394 174 693 -59 A N ATOM 6098 OD1 ASN A 753 26.211 -10.898 70.142 1.00 20.20 A O ANISOU 6098 OD1 ASN A 753 2533 2114 3026 168 639 -234 A O ATOM 6099 N PRO A 754 26.505 -13.250 72.117 1.00 19.43 A N ANISOU 6099 N PRO A 754 3164 2072 2145 -256 738 -97 A N ATOM 6100 CA PRO A 754 25.756 -14.474 71.844 1.00 20.56 A C ANISOU 6100 CA PRO A 754 2830 2479 2502 -542 289 36 A C ATOM 6101 C PRO A 754 25.286 -14.613 70.395 1.00 20.09 A C ANISOU 6101 C PRO A 754 3233 1979 2418 -14 506 38 A C ATOM 6102 O PRO A 754 24.894 -15.687 69.971 1.00 23.76 A O ANISOU 6102 O PRO A 754 3826 2375 2824 -653 267 -59 A O ATOM 6103 CB PRO A 754 24.563 -14.371 72.808 1.00 25.18 A C ANISOU 6103 CB PRO A 754 3172 3308 3085 -180 692 359 A C ATOM 6104 CG PRO A 754 24.348 -12.864 72.960 1.00 26.86 A C ANISOU 6104 CG PRO A 754 3425 3748 3029 -104 1163 -168 A C ATOM 6105 CD PRO A 754 25.773 -12.310 73.002 1.00 24.29 A C ANISOU 6105 CD PRO A 754 3055 3185 2988 195 906 -373 A C ATOM 6106 N GLY A 755 25.371 -13.533 69.627 1.00 20.08 A N ANISOU 6106 N GLY A 755 3095 2263 2270 -31 500 164 A N ATOM 6107 CA GLY A 755 24.963 -13.607 68.255 1.00 19.47 A C ANISOU 6107 CA GLY A 755 3088 1582 2726 -83 194 -307 A C ATOM 6108 C GLY A 755 25.780 -14.635 67.489 1.00 17.55 A C ANISOU 6108 C GLY A 755 2796 1226 2645 89 263 120 A C ATOM 6109 O GLY A 755 26.983 -14.701 67.622 1.00 18.80 A O ANISOU 6109 O GLY A 755 3100 1810 2231 139 449 117 A O ATOM 6110 N GLN A 756 25.088 -15.375 66.617 1.00 18.15 A N ANISOU 6110 N GLN A 756 2998 1637 2258 -118 658 10 A N ATOM 6111 CA GLN A 756 25.711 -16.416 65.839 1.00 17.58 A C ANISOU 6111 CA GLN A 756 2388 1834 2455 -104 736 -86 A C ATOM 6112 C GLN A 756 26.715 -15.788 64.862 1.00 15.78 A C ANISOU 6112 C GLN A 756 2361 1515 2117 81 467 145 A C ATOM 6113 O GLN A 756 27.725 -16.413 64.475 1.00 17.54 A O ANISOU 6113 O GLN A 756 2450 1790 2422 -29 679 -200 A O ATOM 6114 CB GLN A 756 24.663 -17.225 65.055 1.00 19.18 A C ANISOU 6114 CB GLN A 756 2732 1785 2767 -861 919 -68 A C ATOM 6115 N MET A 757 26.417 -14.558 64.436 1.00 16.43 A N ANISOU 6115 N MET A 757 2564 1275 2403 4 566 82 A N ATOM 6116 CA MET A 757 27.278 -13.769 63.542 1.00 16.20 A C ANISOU 6116 CA MET A 757 2052 1826 2276 -60 490 -168 A C ATOM 6117 C MET A 757 28.124 -12.837 64.417 1.00 15.10 A C ANISOU 6117 C MET A 757 2192 1362 2181 4 395 -57 A C ATOM 6118 O MET A 757 27.650 -11.768 64.819 1.00 16.19 A O ANISOU 6118 O MET A 757 2359 1312 2479 80 584 -59 A O ATOM 6119 CB MET A 757 26.432 -12.966 62.561 1.00 15.68 A C ANISOU 6119 CB MET A 757 2221 1924 1810 -388 183 -315 A C ATOM 6120 CG MET A 757 27.195 -12.182 61.543 1.00 15.13 A C ANISOU 6120 CG MET A 757 1739 1724 2285 31 301 1 A C ATOM 6121 SD MET A 757 26.197 -10.896 60.771 1.00 17.56 A S ANISOU 6121 SD MET A 757 2711 1474 2484 47 332 48 A S ATOM 6122 CE MET A 757 26.239 -9.643 62.040 1.00 17.29 A C ANISOU 6122 CE MET A 757 2563 1365 2641 202 527 -100 A C ATOM 6123 N THR A 758 29.350 -13.261 64.737 1.00 14.07 A N ANISOU 6123 N THR A 758 2295 1031 2018 -65 399 172 A N ATOM 6124 CA THR A 758 30.284 -12.464 65.533 1.00 15.14 A C ANISOU 6124 CA THR A 758 2378 1269 2105 -44 425 -14 A C ATOM 6125 C THR A 758 31.716 -12.704 65.069 1.00 14.34 A C ANISOU 6125 C THR A 758 2407 1402 1638 164 417 325 A C ATOM 6126 O THR A 758 32.201 -13.841 65.156 1.00 17.64 A O ANISOU 6126 O THR A 758 2492 1459 2747 308 702 301 A O ATOM 6127 CB THR A 758 30.158 -12.761 67.028 1.00 15.54 A C ANISOU 6127 CB THR A 758 2389 1414 2100 1 134 371 A C ATOM 6128 CG2 THR A 758 31.134 -11.977 67.865 1.00 16.55 A C ANISOU 6128 CG2 THR A 758 2395 2130 1763 -270 450 176 A C ATOM 6129 OG1 THR A 758 28.824 -12.454 67.450 1.00 16.99 A O ANISOU 6129 OG1 THR A 758 2858 1707 1890 182 545 48 A O ATOM 6130 N SER A 759 32.380 -11.661 64.586 1.00 14.92 A N ANISOU 6130 N SER A 759 2157 1397 2115 -260 209 -37 A N ATOM 6131 CA SER A 759 33.745 -11.703 64.116 1.00 13.81 A C ANISOU 6131 CA SER A 759 2086 1366 1794 -208 -55 -116 A C ATOM 6132 C SER A 759 34.580 -10.660 64.874 1.00 12.42 A C ANISOU 6132 C SER A 759 2124 1095 1499 -22 143 -286 A C ATOM 6133 O SER A 759 34.098 -9.552 65.204 1.00 14.52 A O ANISOU 6133 O SER A 759 2479 1187 1851 141 186 -263 A O ATOM 6134 CB SER A 759 33.785 -11.471 62.617 1.00 13.93 A C ANISOU 6134 CB SER A 759 2069 1478 1744 -300 102 -265 A C ATOM 6135 OG SER A 759 34.908 -10.718 62.211 1.00 12.49 A O ANISOU 6135 OG SER A 759 1790 1287 1668 -119 92 -202 A O ATOM 6136 N PHE A 760 35.870 -10.963 65.068 1.00 13.16 A N ANISOU 6136 N PHE A 760 2247 1273 1481 -104 104 -91 A N ATOM 6137 CA PHE A 760 36.817 -10.043 65.668 1.00 13.34 A C ANISOU 6137 CA PHE A 760 2076 1378 1612 -118 159 -152 A C ATOM 6138 C PHE A 760 37.757 -9.433 64.608 1.00 11.70 A C ANISOU 6138 C PHE A 760 1823 988 1633 225 39 120 A C ATOM 6139 O PHE A 760 38.838 -8.932 64.970 1.00 13.91 A O ANISOU 6139 O PHE A 760 1937 1501 1845 -162 107 16 A O ATOM 6140 CB PHE A 760 37.615 -10.707 66.804 1.00 13.20 A C ANISOU 6140 CB PHE A 760 2126 1315 1571 64 286 -264 A C ATOM 6141 CG PHE A 760 36.732 -11.072 67.959 1.00 13.34 A C ANISOU 6141 CG PHE A 760 2284 1194 1589 -60 291 -148 A C ATOM 6142 CD1 PHE A 760 36.515 -10.150 68.958 1.00 14.91 A C ANISOU 6142 CD1 PHE A 760 2807 1115 1740 170 315 -211 A C ATOM 6143 CD2 PHE A 760 36.085 -12.302 68.033 1.00 14.74 A C ANISOU 6143 CD2 PHE A 760 2347 1400 1852 -297 364 -66 A C ATOM 6144 CE1 PHE A 760 35.679 -10.457 70.022 1.00 16.52 A C ANISOU 6144 CE1 PHE A 760 2697 1810 1768 99 394 -149 A C ATOM 6145 CE2 PHE A 760 35.258 -12.600 69.098 1.00 16.60 A C ANISOU 6145 CE2 PHE A 760 2724 1937 1644 -52 317 291 A C ATOM 6146 CZ PHE A 760 35.053 -11.680 70.087 1.00 16.93 A C ANISOU 6146 CZ PHE A 760 2752 2020 1661 -36 279 255 A C ATOM 6147 N ASN A 761 37.369 -9.444 63.328 1.00 12.99 A N ANISOU 6147 N ASN A 761 2012 1230 1693 -37 -54 -118 A N ATOM 6148 CA ASN A 761 38.258 -8.908 62.305 1.00 11.71 A C ANISOU 6148 CA ASN A 761 1866 1080 1503 97 -12 -281 A C ATOM 6149 C ASN A 761 37.467 -8.483 61.065 1.00 12.87 A C ANISOU 6149 C ASN A 761 1918 1203 1768 176 -25 -88 A C ATOM 6150 O ASN A 761 37.508 -9.132 60.025 1.00 13.13 A O ANISOU 6150 O ASN A 761 2323 1040 1626 149 30 25 A O ATOM 6151 CB ASN A 761 39.340 -9.916 61.939 1.00 11.69 A C ANISOU 6151 CB ASN A 761 1940 960 1541 110 2 -159 A C ATOM 6152 CG ASN A 761 40.564 -9.297 61.316 1.00 12.57 A C ANISOU 6152 CG ASN A 761 1890 1101 1785 71 69 34 A C ATOM 6153 ND2 ASN A 761 41.627 -10.064 61.126 1.00 12.20 A N ANISOU 6153 ND2 ASN A 761 1796 1256 1582 197 -115 -361 A N ATOM 6154 OD1 ASN A 761 40.559 -8.097 60.987 1.00 13.23 A O ANISOU 6154 OD1 ASN A 761 2328 1008 1689 148 85 38 A O ATOM 6155 N HIS A 762 36.765 -7.355 61.204 1.00 13.14 A N ANISOU 6155 N HIS A 762 2087 1363 1543 417 140 -303 A N ATOM 6156 CA HIS A 762 35.993 -6.683 60.133 1.00 13.23 A C ANISOU 6156 CA HIS A 762 1869 1365 1793 140 -190 -368 A C ATOM 6157 C HIS A 762 36.475 -5.239 60.056 1.00 13.66 A C ANISOU 6157 C HIS A 762 1958 1603 1628 1 -305 -42 A C ATOM 6158 O HIS A 762 36.566 -4.629 61.116 1.00 13.95 A O ANISOU 6158 O HIS A 762 2343 1549 1407 140 107 -79 A O ATOM 6159 CB HIS A 762 34.500 -6.637 60.510 1.00 13.11 A C ANISOU 6159 CB HIS A 762 1916 1139 1924 56 -35 -350 A C ATOM 6160 CG HIS A 762 33.595 -7.699 60.004 1.00 12.92 A C ANISOU 6160 CG HIS A 762 1828 1106 1972 101 -24 -295 A C ATOM 6161 CD2 HIS A 762 32.521 -7.620 59.179 1.00 12.16 A C ANISOU 6161 CD2 HIS A 762 1919 1073 1625 0 134 -37 A C ATOM 6162 ND1 HIS A 762 33.680 -9.013 60.433 1.00 13.24 A N ANISOU 6162 ND1 HIS A 762 1764 1280 1985 306 47 -102 A N ATOM 6163 CE1 HIS A 762 32.717 -9.703 59.849 1.00 14.84 A C ANISOU 6163 CE1 HIS A 762 2092 1566 1978 237 52 -436 A C ATOM 6164 NE2 HIS A 762 31.984 -8.875 59.046 1.00 13.40 A N ANISOU 6164 NE2 HIS A 762 1922 1267 1902 -66 207 -313 A N ATOM 6165 N TYR A 763 36.792 -4.722 58.860 1.00 12.97 A N ANISOU 6165 N TYR A 763 1919 1505 1503 -131 9 -382 A N ATOM 6166 CA TYR A 763 37.233 -3.309 58.758 1.00 12.44 A C ANISOU 6166 CA TYR A 763 1810 1536 1378 -116 -95 44 A C ATOM 6167 C TYR A 763 36.138 -2.263 58.853 1.00 12.62 A C ANISOU 6167 C TYR A 763 1822 1416 1556 -332 -116 -249 A C ATOM 6168 O TYR A 763 36.496 -1.076 58.992 1.00 13.87 A O ANISOU 6168 O TYR A 763 1951 1360 1956 -481 139 -367 A O ATOM 6169 CB TYR A 763 38.099 -3.089 57.506 1.00 12.52 A C ANISOU 6169 CB TYR A 763 2064 1123 1567 -288 -64 76 A C ATOM 6170 CG TYR A 763 37.585 -3.551 56.166 1.00 11.23 A C ANISOU 6170 CG TYR A 763 1636 1042 1588 124 -95 -87 A C ATOM 6171 CD1 TYR A 763 36.328 -3.242 55.706 1.00 11.17 A C ANISOU 6171 CD1 TYR A 763 1824 729 1689 -8 -245 -60 A C ATOM 6172 CD2 TYR A 763 38.379 -4.341 55.348 1.00 11.65 A C ANISOU 6172 CD2 TYR A 763 1529 1340 1557 208 -155 -160 A C ATOM 6173 CE1 TYR A 763 35.889 -3.625 54.451 1.00 11.81 A C ANISOU 6173 CE1 TYR A 763 1802 1088 1594 56 -226 76 A C ATOM 6174 CE2 TYR A 763 37.949 -4.756 54.095 1.00 11.33 A C ANISOU 6174 CE2 TYR A 763 1808 937 1557 -128 -53 77 A C ATOM 6175 CZ TYR A 763 36.665 -4.462 53.671 1.00 12.04 A C ANISOU 6175 CZ TYR A 763 1898 1083 1594 -20 -240 -78 A C ATOM 6176 OH TYR A 763 36.258 -4.875 52.429 1.00 12.56 A O ANISOU 6176 OH TYR A 763 2135 1027 1608 -208 -234 80 A O ATOM 6177 N ALA A 764 34.845 -2.593 58.829 1.00 13.78 A N ANISOU 6177 N ALA A 764 1621 1377 2235 -179 -166 -43 A N ATOM 6178 CA ALA A 764 33.821 -1.536 58.778 1.00 14.74 A C ANISOU 6178 CA ALA A 764 1733 1579 2288 -29 -118 -430 A C ATOM 6179 C ALA A 764 33.990 -0.511 59.886 1.00 13.65 A C ANISOU 6179 C ALA A 764 1879 1150 2156 -63 49 -198 A C ATOM 6180 O ALA A 764 33.928 0.669 59.579 1.00 14.25 A O ANISOU 6180 O ALA A 764 2024 1087 2302 -51 86 -105 A O ATOM 6181 CB ALA A 764 32.419 -2.143 58.815 1.00 15.83 A C ANISOU 6181 CB ALA A 764 1616 1563 2833 2 -168 -379 A C ATOM 6182 N VAL A 765 34.106 -0.932 61.156 1.00 15.46 A N ANISOU 6182 N VAL A 765 2258 1343 2273 -114 156 -118 A N ATOM 6183 CA VAL A 765 34.246 0.011 62.330 1.00 16.37 A C ANISOU 6183 CA VAL A 765 2031 2083 2103 -229 247 -176 A C ATOM 6184 C VAL A 765 35.541 0.807 62.170 1.00 12.91 A C ANISOU 6184 C VAL A 765 1956 1121 1826 41 185 -309 A C ATOM 6185 O VAL A 765 35.647 1.981 62.629 1.00 14.83 A O ANISOU 6185 O VAL A 765 2370 1271 1993 211 -63 -442 A O ATOM 6186 CB VAL A 765 34.214 -0.850 63.621 1.00 20.94 A C ANISOU 6186 CB VAL A 765 3239 2828 1886 -614 1113 -244 A C ATOM 6187 CG1 VAL A 765 34.990 -0.318 64.771 1.00 25.97 A C ANISOU 6187 CG1 VAL A 765 3387 3959 2520 -506 349 11 A C ATOM 6188 CG2 VAL A 765 32.761 -1.200 63.976 1.00 21.60 A C ANISOU 6188 CG2 VAL A 765 3134 2930 2143 -643 699 -549 A C ATOM 6189 N GLY A 766 36.507 0.233 61.433 1.00 12.79 A N ANISOU 6189 N GLY A 766 1788 1384 1686 309 52 -111 A N ATOM 6190 CA GLY A 766 37.779 0.861 61.171 1.00 12.14 A C ANISOU 6190 CA GLY A 766 1765 1263 1583 135 119 -332 A C ATOM 6191 C GLY A 766 37.664 2.021 60.181 1.00 11.42 A C ANISOU 6191 C GLY A 766 1551 1054 1734 69 -89 -349 A C ATOM 6192 O GLY A 766 38.666 2.678 59.925 1.00 11.93 A O ANISOU 6192 O GLY A 766 1569 1086 1876 105 -51 -223 A O ATOM 6193 N SER A 767 36.467 2.271 59.639 1.00 11.25 A N ANISOU 6193 N SER A 767 1539 919 1815 193 1 -376 A N ATOM 6194 CA ASER A 767 36.200 3.449 58.783 0.50 11.95 A C ANISOU 6194 CA ASER A 767 1659 1120 1760 233 115 -259 A C ATOM 6195 CA BSER A 767 36.217 3.445 58.775 0.50 13.16 A C ANISOU 6195 CA BSER A 767 1937 1031 2028 301 73 -250 A C ATOM 6196 C SER A 767 36.450 4.786 59.492 1.00 12.22 A C ANISOU 6196 C SER A 767 1604 1251 1785 25 76 -255 A C ATOM 6197 O SER A 767 36.562 5.799 58.822 1.00 13.25 A O ANISOU 6197 O SER A 767 1956 1326 1752 47 56 -178 A O ATOM 6198 CB ASER A 767 34.800 3.398 58.223 0.50 10.62 A C ANISOU 6198 CB ASER A 767 1593 547 1893 245 173 -211 A C ATOM 6199 CB BSER A 767 34.833 3.362 58.170 0.50 14.71 A C ANISOU 6199 CB BSER A 767 2083 676 2829 460 -224 -45 A C ATOM 6200 OG ASER A 767 33.827 3.420 59.250 0.50 10.05 A O ANISOU 6200 OG ASER A 767 1238 1116 1464 105 -78 -271 A O ATOM 6201 OG BSER A 767 34.677 2.138 57.442 0.50 18.22 A O ANISOU 6201 OG BSER A 767 2627 1120 3177 484 -86 -449 A O ATOM 6202 N VAL A 768 36.546 4.764 60.818 1.00 12.49 A N ANISOU 6202 N VAL A 768 2095 900 1747 45 77 -247 A N ATOM 6203 CA VAL A 768 36.990 5.938 61.580 1.00 12.39 A C ANISOU 6203 CA VAL A 768 1970 983 1754 123 -64 -309 A C ATOM 6204 C VAL A 768 38.424 6.332 61.207 1.00 12.59 A C ANISOU 6204 C VAL A 768 1936 950 1898 117 -26 -275 A C ATOM 6205 O VAL A 768 38.827 7.476 61.445 1.00 12.70 A O ANISOU 6205 O VAL A 768 1890 999 1934 29 94 -493 A O ATOM 6206 CB VAL A 768 36.851 5.728 63.098 1.00 12.88 A C ANISOU 6206 CB VAL A 768 1939 1211 1743 -31 -57 -306 A C ATOM 6207 CG1 VAL A 768 37.871 4.745 63.636 1.00 14.77 A C ANISOU 6207 CG1 VAL A 768 2324 1542 1745 185 -93 -285 A C ATOM 6208 CG2 VAL A 768 36.919 7.049 63.850 1.00 13.61 A C ANISOU 6208 CG2 VAL A 768 2021 1291 1857 -15 51 -427 A C ATOM 6209 N GLY A 769 39.212 5.451 60.580 1.00 12.40 A N ANISOU 6209 N GLY A 769 1736 952 2022 52 120 -184 A N ATOM 6210 CA GLY A 769 40.578 5.739 60.227 1.00 11.37 A C ANISOU 6210 CA GLY A 769 1613 1006 1699 117 -179 -229 A C ATOM 6211 C GLY A 769 40.696 6.999 59.386 1.00 11.05 A C ANISOU 6211 C GLY A 769 1414 1054 1729 155 124 -156 A C ATOM 6212 O GLY A 769 41.660 7.779 59.536 1.00 11.97 A O ANISOU 6212 O GLY A 769 1696 1136 1714 40 -218 -417 A O ATOM 6213 N SER A 770 39.760 7.204 58.462 1.00 11.27 A N ANISOU 6213 N SER A 770 1568 1067 1647 71 76 -197 A N ATOM 6214 CA SER A 770 39.812 8.403 57.606 1.00 11.43 A C ANISOU 6214 CA SER A 770 1553 1070 1718 256 -134 -102 A C ATOM 6215 C SER A 770 39.734 9.691 58.409 1.00 10.99 A C ANISOU 6215 C SER A 770 1479 1160 1536 68 -41 -81 A C ATOM 6216 O SER A 770 40.267 10.699 57.960 1.00 12.40 A O ANISOU 6216 O SER A 770 1639 1291 1782 -157 -11 -43 A O ATOM 6217 CB SER A 770 38.754 8.390 56.525 1.00 11.76 A C ANISOU 6217 CB SER A 770 1831 996 1640 33 -149 -216 A C ATOM 6218 OG SER A 770 37.451 8.390 57.050 1.00 12.77 A O ANISOU 6218 OG SER A 770 1608 1330 1912 -22 -252 -239 A O ATOM 6219 N TRP A 771 39.038 9.657 59.546 1.00 11.07 A N ANISOU 6219 N TRP A 771 1710 826 1667 68 91 -286 A N ATOM 6220 CA TRP A 771 38.973 10.853 60.396 1.00 11.47 A C ANISOU 6220 CA TRP A 771 1792 848 1715 59 27 -340 A C ATOM 6221 C TRP A 771 40.339 11.079 61.053 1.00 12.85 A C ANISOU 6221 C TRP A 771 1775 1292 1815 10 -30 -337 A C ATOM 6222 O TRP A 771 40.806 12.229 61.209 1.00 13.28 A O ANISOU 6222 O TRP A 771 2153 1162 1727 -66 -83 -421 A O ATOM 6223 CB TRP A 771 37.857 10.743 61.439 1.00 11.42 A C ANISOU 6223 CB TRP A 771 1577 929 1830 -67 9 -341 A C ATOM 6224 CG TRP A 771 37.484 12.046 62.073 1.00 13.39 A C ANISOU 6224 CG TRP A 771 2233 835 2019 -85 37 -316 A C ATOM 6225 CD1 TRP A 771 36.570 12.920 61.583 1.00 12.88 A C ANISOU 6225 CD1 TRP A 771 1927 1387 1578 -69 20 -537 A C ATOM 6226 CD2 TRP A 771 37.954 12.565 63.324 1.00 14.09 A C ANISOU 6226 CD2 TRP A 771 2020 1136 2196 166 -63 -313 A C ATOM 6227 CE2 TRP A 771 37.336 13.828 63.472 1.00 12.81 A C ANISOU 6227 CE2 TRP A 771 1901 1109 1855 147 8 -417 A C ATOM 6228 CE3 TRP A 771 38.867 12.142 64.299 1.00 14.86 A C ANISOU 6228 CE3 TRP A 771 2039 1696 1909 19 171 -245 A C ATOM 6229 NE1 TRP A 771 36.481 13.994 62.417 1.00 14.43 A N ANISOU 6229 NE1 TRP A 771 2323 1335 1823 104 -43 -561 A N ATOM 6230 CZ2 TRP A 771 37.563 14.634 64.584 1.00 15.72 A C ANISOU 6230 CZ2 TRP A 771 2307 1655 2008 -15 -32 -705 A C ATOM 6231 CZ3 TRP A 771 39.089 12.948 65.393 1.00 16.90 A C ANISOU 6231 CZ3 TRP A 771 2528 1879 2012 14 -300 -213 A C ATOM 6232 CH2 TRP A 771 38.437 14.172 65.536 1.00 15.82 A C ANISOU 6232 CH2 TRP A 771 2553 1638 1818 -219 44 -602 A C ATOM 6233 N LEU A 772 40.997 10.011 61.494 1.00 12.30 A N ANISOU 6233 N LEU A 772 1687 1255 1730 85 2 -373 A N ATOM 6234 CA LEU A 772 42.364 10.132 62.014 1.00 12.50 A C ANISOU 6234 CA LEU A 772 1972 980 1796 -38 -77 -594 A C ATOM 6235 C LEU A 772 43.282 10.758 60.959 1.00 12.39 A C ANISOU 6235 C LEU A 772 1802 1355 1551 -114 -365 -283 A C ATOM 6236 O LEU A 772 44.055 11.679 61.229 1.00 13.99 A O ANISOU 6236 O LEU A 772 2203 1205 1905 -259 -108 -516 A O ATOM 6237 CB LEU A 772 42.908 8.771 62.436 1.00 12.99 A C ANISOU 6237 CB LEU A 772 2008 1018 1909 -27 -363 -503 A C ATOM 6238 CG LEU A 772 42.064 7.951 63.411 1.00 16.53 A C ANISOU 6238 CG LEU A 772 2748 1448 2083 270 0 -100 A C ATOM 6239 CD1 LEU A 772 42.769 6.649 63.780 1.00 15.76 A C ANISOU 6239 CD1 LEU A 772 2651 1368 1966 441 261 -229 A C ATOM 6240 CD2 LEU A 772 41.619 8.636 64.646 1.00 18.25 A C ANISOU 6240 CD2 LEU A 772 3167 1538 2229 274 377 -53 A C ATOM 6241 N HIS A 773 43.150 10.310 59.723 1.00 12.12 A N ANISOU 6241 N HIS A 773 1864 1112 1627 -127 -188 -472 A N ATOM 6242 CA HIS A 773 44.029 10.763 58.656 1.00 12.59 A C ANISOU 6242 CA HIS A 773 1902 1231 1649 245 -147 -388 A C ATOM 6243 C HIS A 773 43.741 12.231 58.320 1.00 11.72 A C ANISOU 6243 C HIS A 773 1857 1258 1334 -35 -146 -182 A C ATOM 6244 O HIS A 773 44.700 13.011 58.075 1.00 13.35 A O ANISOU 6244 O HIS A 773 1927 1238 1907 -149 -258 -260 A O ATOM 6245 CB HIS A 773 43.877 9.905 57.383 1.00 12.63 A C ANISOU 6245 CB HIS A 773 1895 1246 1656 316 6 -428 A C ATOM 6246 CG HIS A 773 44.094 8.434 57.571 1.00 11.80 A C ANISOU 6246 CG HIS A 773 1582 1255 1643 -21 -60 -244 A C ATOM 6247 CD2 HIS A 773 44.890 7.736 58.414 1.00 12.44 A C ANISOU 6247 CD2 HIS A 773 1914 963 1848 -86 -164 -302 A C ATOM 6248 ND1 HIS A 773 43.414 7.524 56.794 1.00 11.88 A N ANISOU 6248 ND1 HIS A 773 1629 1098 1784 -22 -47 -210 A N ATOM 6249 CE1 HIS A 773 43.819 6.314 57.166 1.00 13.15 A C ANISOU 6249 CE1 HIS A 773 2161 911 1924 -38 -143 -270 A C ATOM 6250 NE2 HIS A 773 44.725 6.409 58.155 1.00 12.45 A N ANISOU 6250 NE2 HIS A 773 1740 934 2055 109 144 -410 A N ATOM 6251 N GLU A 774 42.449 12.532 58.112 1.00 11.76 A N ANISOU 6251 N GLU A 774 1760 1018 1689 -187 3 -114 A N ATOM 6252 CA GLU A 774 42.063 13.807 57.472 1.00 11.96 A C ANISOU 6252 CA GLU A 774 1869 1022 1650 -139 -146 -97 A C ATOM 6253 C GLU A 774 41.877 14.956 58.469 1.00 13.32 A C ANISOU 6253 C GLU A 774 1865 1279 1915 -347 -56 -335 A C ATOM 6254 O GLU A 774 42.011 16.110 58.074 1.00 14.80 A O ANISOU 6254 O GLU A 774 2163 1221 2238 -180 -5 -173 A O ATOM 6255 CB GLU A 774 40.751 13.672 56.701 1.00 13.43 A C ANISOU 6255 CB GLU A 774 1893 949 2258 -228 -357 -193 A C ATOM 6256 CG GLU A 774 40.815 12.638 55.579 1.00 14.52 A C ANISOU 6256 CG GLU A 774 2190 1192 2132 -431 -364 -176 A C ATOM 6257 CD GLU A 774 39.550 12.581 54.732 1.00 16.88 A C ANISOU 6257 CD GLU A 774 1854 1874 2684 -304 -272 -481 A C ATOM 6258 OE1 GLU A 774 38.673 13.479 54.873 1.00 19.14 A O ANISOU 6258 OE1 GLU A 774 2071 2090 3110 7 -530 -284 A O ATOM 6259 OE2 GLU A 774 39.402 11.594 53.990 1.00 20.10 A O ANISOU 6259 OE2 GLU A 774 2612 2074 2949 -349 -419 -791 A O ATOM 6260 N VAL A 775 41.533 14.657 59.709 1.00 11.76 A N ANISOU 6260 N VAL A 775 1825 861 1779 150 -60 -373 A N ATOM 6261 CA VAL A 775 41.199 15.700 60.666 1.00 12.46 A C ANISOU 6261 CA VAL A 775 2016 829 1887 108 -84 -414 A C ATOM 6262 C VAL A 775 42.293 15.800 61.734 1.00 12.76 A C ANISOU 6262 C VAL A 775 1778 1195 1872 -32 16 -236 A C ATOM 6263 O VAL A 775 42.857 16.875 61.947 1.00 14.84 A O ANISOU 6263 O VAL A 775 2270 1283 2085 -245 -210 -525 A O ATOM 6264 CB VAL A 775 39.791 15.503 61.264 1.00 13.65 A C ANISOU 6264 CB VAL A 775 1993 901 2292 282 5 -458 A C ATOM 6265 CG1 VAL A 775 39.503 16.582 62.265 1.00 15.02 A C ANISOU 6265 CG1 VAL A 775 2046 1091 2568 127 185 -690 A C ATOM 6266 CG2 VAL A 775 38.726 15.515 60.173 1.00 15.26 A C ANISOU 6266 CG2 VAL A 775 2024 1393 2378 116 -22 -516 A C ATOM 6267 N ILE A 776 42.641 14.697 62.396 1.00 12.79 A N ANISOU 6267 N ILE A 776 2091 1096 1669 -43 -188 -302 A N ATOM 6268 CA ILE A 776 43.792 14.735 63.345 1.00 14.41 A C ANISOU 6268 CA ILE A 776 2223 1359 1892 -32 -166 -355 A C ATOM 6269 C ILE A 776 45.072 15.018 62.549 1.00 13.85 A C ANISOU 6269 C ILE A 776 2021 1330 1909 -200 -198 -392 A C ATOM 6270 O ILE A 776 45.866 15.895 62.905 1.00 15.88 A O ANISOU 6270 O ILE A 776 2544 1237 2250 -376 -244 -440 A O ATOM 6271 CB ILE A 776 43.935 13.452 64.178 1.00 14.90 A C ANISOU 6271 CB ILE A 776 2145 1388 2127 1 -93 -229 A C ATOM 6272 CG1 ILE A 776 42.647 13.118 64.940 1.00 14.09 A C ANISOU 6272 CG1 ILE A 776 2136 1347 1869 67 -39 -514 A C ATOM 6273 CG2 ILE A 776 45.128 13.588 65.123 1.00 16.08 A C ANISOU 6273 CG2 ILE A 776 2360 1523 2225 -317 -180 -396 A C ATOM 6274 CD1 ILE A 776 42.758 11.877 65.798 1.00 15.56 A C ANISOU 6274 CD1 ILE A 776 2347 1564 1998 144 51 -316 A C ATOM 6275 N GLY A 777 45.253 14.292 61.440 1.00 13.79 A N ANISOU 6275 N GLY A 777 2016 1342 1878 -120 -121 -434 A N ATOM 6276 CA GLY A 777 46.426 14.454 60.583 1.00 14.90 A C ANISOU 6276 CA GLY A 777 1989 1474 2198 -172 -184 -322 A C ATOM 6277 C GLY A 777 46.288 15.578 59.580 1.00 13.15 A C ANISOU 6277 C GLY A 777 1916 1443 1634 -102 -30 -575 A C ATOM 6278 O GLY A 777 47.283 15.986 58.980 1.00 14.70 A O ANISOU 6278 O GLY A 777 1928 1634 2020 -87 -213 -279 A O ATOM 6279 N GLY A 778 45.050 16.019 59.343 1.00 12.98 A N ANISOU 6279 N GLY A 778 2123 1023 1784 -245 -231 -204 A N ATOM 6280 CA GLY A 778 44.787 17.140 58.489 1.00 13.30 A C ANISOU 6280 CA GLY A 778 2025 1093 1935 -162 -171 -97 A C ATOM 6281 C GLY A 778 44.784 16.880 56.994 1.00 14.65 A C ANISOU 6281 C GLY A 778 2097 1418 2049 -350 -156 -203 A C ATOM 6282 O GLY A 778 44.504 17.809 56.246 1.00 14.45 A O ANISOU 6282 O GLY A 778 2201 1241 2046 -306 -265 -271 A O ATOM 6283 N LEU A 779 45.106 15.669 56.515 1.00 13.89 A N ANISOU 6283 N LEU A 779 1868 1578 1829 -88 -212 -362 A N ATOM 6284 CA LEU A 779 45.422 15.478 55.100 1.00 13.45 A C ANISOU 6284 CA LEU A 779 1811 1414 1885 -230 -335 10 A C ATOM 6285 C LEU A 779 44.211 14.959 54.321 1.00 13.18 A C ANISOU 6285 C LEU A 779 1611 1626 1770 -138 -167 -173 A C ATOM 6286 O LEU A 779 43.664 13.887 54.633 1.00 15.06 A O ANISOU 6286 O LEU A 779 2080 1781 1861 -526 -240 -117 A O ATOM 6287 CB LEU A 779 46.553 14.466 54.992 1.00 13.88 A C ANISOU 6287 CB LEU A 779 1931 1446 1893 -120 -398 -145 A C ATOM 6288 CG LEU A 779 47.929 14.948 55.422 1.00 14.90 A C ANISOU 6288 CG LEU A 779 1938 1391 2330 -190 -247 -194 A C ATOM 6289 CD1 LEU A 779 48.878 13.780 55.515 1.00 19.07 A C ANISOU 6289 CD1 LEU A 779 2154 2051 3040 209 -794 11 A C ATOM 6290 CD2 LEU A 779 48.443 15.965 54.444 1.00 16.09 A C ANISOU 6290 CD2 LEU A 779 2090 1321 2700 -116 -347 54 A C ATOM 6291 N SER A 780 43.869 15.632 53.229 1.00 13.30 A N ANISOU 6291 N SER A 780 1869 1563 1622 -280 -157 -237 A N ATOM 6292 CA SER A 780 42.828 15.144 52.304 1.00 14.05 A C ANISOU 6292 CA SER A 780 1869 1672 1795 -276 -184 -227 A C ATOM 6293 C SER A 780 43.152 15.667 50.920 1.00 14.06 A C ANISOU 6293 C SER A 780 2019 1605 1715 -340 -46 -312 A C ATOM 6294 O SER A 780 43.811 16.699 50.763 1.00 13.79 A O ANISOU 6294 O SER A 780 2056 1335 1849 -291 -193 -353 A O ATOM 6295 CB SER A 780 41.414 15.538 52.716 1.00 15.73 A C ANISOU 6295 CB SER A 780 1807 1808 2361 -275 -330 -320 A C ATOM 6296 OG SER A 780 41.260 16.956 52.675 1.00 16.67 A O ANISOU 6296 OG SER A 780 2139 1908 2284 -169 51 -489 A O ATOM 6297 N PRO A 781 42.654 15.009 49.862 1.00 12.45 A N ANISOU 6297 N PRO A 781 1951 1040 1737 -409 -55 -151 A N ATOM 6298 CA PRO A 781 42.860 15.498 48.501 1.00 12.94 A C ANISOU 6298 CA PRO A 781 1593 1443 1877 -237 -36 -140 A C ATOM 6299 C PRO A 781 41.943 16.681 48.182 1.00 14.70 A C ANISOU 6299 C PRO A 781 1611 1583 2388 -154 -156 -29 A C ATOM 6300 O PRO A 781 40.741 16.614 48.390 1.00 16.62 A O ANISOU 6300 O PRO A 781 1659 1695 2959 -33 -17 151 A O ATOM 6301 CB PRO A 781 42.593 14.259 47.636 1.00 13.47 A C ANISOU 6301 CB PRO A 781 1943 1240 1934 -177 117 -144 A C ATOM 6302 CG PRO A 781 41.581 13.468 48.442 1.00 14.10 A C ANISOU 6302 CG PRO A 781 2065 1393 1898 -310 -11 -109 A C ATOM 6303 CD PRO A 781 41.947 13.706 49.896 1.00 13.33 A C ANISOU 6303 CD PRO A 781 2123 1102 1838 -466 -15 163 A C ATOM 6304 N ALA A 782 42.538 17.743 47.661 1.00 13.48 A N ANISOU 6304 N ALA A 782 1540 1618 1964 -248 -109 -347 A N ATOM 6305 CA ALA A 782 41.772 18.909 47.209 1.00 14.90 A C ANISOU 6305 CA ALA A 782 1997 1460 2203 -84 -64 -245 A C ATOM 6306 C ALA A 782 41.414 18.803 45.730 1.00 14.19 A C ANISOU 6306 C ALA A 782 1987 1353 2050 -58 84 -42 A C ATOM 6307 O ALA A 782 40.565 19.523 45.251 1.00 18.78 A O ANISOU 6307 O ALA A 782 2829 1733 2571 345 -600 -393 A O ATOM 6308 CB ALA A 782 42.497 20.207 47.498 1.00 14.90 A C ANISOU 6308 CB ALA A 782 2146 1433 2080 -37 -124 -368 A C ATOM 6309 N GLU A 783 42.091 17.902 45.009 1.00 14.33 A N ANISOU 6309 N GLU A 783 2209 1329 1904 -48 -2 -87 A N ATOM 6310 CA GLU A 783 41.802 17.548 43.634 1.00 13.41 A C ANISOU 6310 CA GLU A 783 2219 1045 1831 -35 60 129 A C ATOM 6311 C GLU A 783 41.906 16.028 43.598 1.00 13.02 A C ANISOU 6311 C GLU A 783 2021 1029 1897 -207 -69 66 A C ATOM 6312 O GLU A 783 42.795 15.470 44.260 1.00 12.86 A O ANISOU 6312 O GLU A 783 1705 1243 1938 -256 -226 -59 A O ATOM 6313 CB GLU A 783 42.834 18.141 42.666 1.00 13.94 A C ANISOU 6313 CB GLU A 783 2368 1086 1839 -375 -79 17 A C ATOM 6314 CG GLU A 783 42.647 17.814 41.219 1.00 14.91 A C ANISOU 6314 CG GLU A 783 2167 1530 1966 -20 165 -150 A C ATOM 6315 CD GLU A 783 43.751 18.420 40.365 1.00 16.56 A C ANISOU 6315 CD GLU A 783 2524 1494 2274 -137 182 342 A C ATOM 6316 OE1 GLU A 783 43.664 19.620 40.100 1.00 19.48 A O ANISOU 6316 OE1 GLU A 783 3051 1291 3057 -427 -278 369 A O ATOM 6317 OE2 GLU A 783 44.736 17.717 40.031 1.00 18.79 A O ANISOU 6317 OE2 GLU A 783 2574 1788 2778 8 156 150 A O ATOM 6318 N PRO A 784 41.036 15.336 42.842 1.00 13.27 A N ANISOU 6318 N PRO A 784 2138 762 2138 -71 -388 100 A N ATOM 6319 CA PRO A 784 41.153 13.877 42.749 1.00 12.22 A C ANISOU 6319 CA PRO A 784 1993 759 1890 -60 -224 106 A C ATOM 6320 C PRO A 784 42.575 13.467 42.362 1.00 13.12 A C ANISOU 6320 C PRO A 784 1987 1179 1816 -28 -225 -220 A C ATOM 6321 O PRO A 784 43.083 13.944 41.382 1.00 16.48 A O ANISOU 6321 O PRO A 784 3049 1089 2121 108 100 -205 A O ATOM 6322 CB PRO A 784 40.129 13.505 41.652 1.00 14.29 A C ANISOU 6322 CB PRO A 784 2208 1130 2090 1 -467 -63 A C ATOM 6323 CG PRO A 784 39.106 14.588 41.738 1.00 17.39 A C ANISOU 6323 CG PRO A 784 2441 1061 3106 -44 -452 -52 A C ATOM 6324 CD PRO A 784 39.863 15.842 42.118 1.00 14.66 A C ANISOU 6324 CD PRO A 784 1959 1235 2374 -220 -339 162 A C ATOM 6325 N GLY A 785 43.175 12.548 43.145 1.00 12.21 A N ANISOU 6325 N GLY A 785 1758 971 1910 -197 25 -37 A N ATOM 6326 CA GLY A 785 44.514 12.114 42.871 1.00 12.35 A C ANISOU 6326 CA GLY A 785 1748 1039 1905 -225 -69 -282 A C ATOM 6327 C GLY A 785 45.634 12.829 43.616 1.00 11.27 A C ANISOU 6327 C GLY A 785 1508 1017 1755 -336 126 -123 A C ATOM 6328 O GLY A 785 46.807 12.530 43.361 1.00 11.53 A O ANISOU 6328 O GLY A 785 1527 835 2019 -162 -20 -168 A O ATOM 6329 N TRP A 786 45.297 13.826 44.456 1.00 11.92 A N ANISOU 6329 N TRP A 786 1552 1055 1922 28 57 -125 A N ATOM 6330 CA TRP A 786 46.229 14.460 45.396 1.00 12.69 A C ANISOU 6330 CA TRP A 786 1821 1269 1729 -14 -17 -87 A C ATOM 6331 C TRP A 786 47.244 15.409 44.739 1.00 11.84 A C ANISOU 6331 C TRP A 786 1727 1080 1690 119 -118 -206 A C ATOM 6332 O TRP A 786 48.192 15.786 45.422 1.00 13.29 A O ANISOU 6332 O TRP A 786 1667 1253 2128 -121 -152 -142 A O ATOM 6333 CB TRP A 786 46.949 13.431 46.259 1.00 12.61 A C ANISOU 6333 CB TRP A 786 1795 1199 1798 -162 -337 -204 A C ATOM 6334 CG TRP A 786 46.090 12.669 47.226 1.00 12.60 A C ANISOU 6334 CG TRP A 786 1932 849 2006 -137 -213 -115 A C ATOM 6335 CD1 TRP A 786 45.379 11.523 46.997 1.00 13.30 A C ANISOU 6335 CD1 TRP A 786 2200 1011 1841 -222 -313 -193 A C ATOM 6336 CD2 TRP A 786 45.972 12.911 48.631 1.00 12.88 A C ANISOU 6336 CD2 TRP A 786 2011 941 1940 -219 -228 53 A C ATOM 6337 CE2 TRP A 786 45.140 11.911 49.174 1.00 13.02 A C ANISOU 6337 CE2 TRP A 786 2129 1110 1707 -296 -179 48 A C ATOM 6338 CE3 TRP A 786 46.527 13.854 49.500 1.00 12.80 A C ANISOU 6338 CE3 TRP A 786 1701 1274 1886 -339 -122 -96 A C ATOM 6339 NE1 TRP A 786 44.775 11.101 48.140 1.00 14.68 A N ANISOU 6339 NE1 TRP A 786 2386 1301 1890 -390 -331 -42 A N ATOM 6340 CZ2 TRP A 786 44.824 11.843 50.519 1.00 14.49 A C ANISOU 6340 CZ2 TRP A 786 2091 1617 1794 -259 -87 -19 A C ATOM 6341 CZ3 TRP A 786 46.214 13.799 50.831 1.00 13.53 A C ANISOU 6341 CZ3 TRP A 786 2202 1085 1850 -11 -80 -240 A C ATOM 6342 CH2 TRP A 786 45.397 12.789 51.339 1.00 15.08 A C ANISOU 6342 CH2 TRP A 786 2384 1673 1670 -292 -130 -71 A C ATOM 6343 N ARG A 787 47.004 15.888 43.516 1.00 11.85 A N ANISOU 6343 N ARG A 787 1864 960 1679 -159 -42 25 A N ATOM 6344 CA ARG A 787 47.919 16.893 42.971 1.00 12.79 A C ANISOU 6344 CA ARG A 787 1900 952 2006 -56 46 126 A C ATOM 6345 C ARG A 787 47.716 18.243 43.671 1.00 12.70 A C ANISOU 6345 C ARG A 787 1656 1330 1838 18 91 -131 A C ATOM 6346 O ARG A 787 48.620 19.119 43.646 1.00 14.26 A O ANISOU 6346 O ARG A 787 1701 1583 2131 -90 90 -4 A O ATOM 6347 CB ARG A 787 47.661 17.065 41.474 1.00 13.61 A C ANISOU 6347 CB ARG A 787 2334 965 1871 82 169 2 A C ATOM 6348 CG ARG A 787 48.727 17.839 40.711 1.00 14.64 A C ANISOU 6348 CG ARG A 787 2788 955 1816 -15 365 190 A C ATOM 6349 CD ARG A 787 48.248 18.115 39.280 1.00 17.58 A C ANISOU 6349 CD ARG A 787 2877 1719 2082 151 -88 -240 A C ATOM 6350 NE ARG A 787 47.095 19.034 39.273 1.00 17.18 A N ANISOU 6350 NE ARG A 787 2715 1502 2308 -26 -9 45 A N ATOM 6351 CZ ARG A 787 47.136 20.355 39.107 1.00 17.03 A C ANISOU 6351 CZ ARG A 787 2670 1558 2242 -172 142 260 A C ATOM 6352 NH1 ARG A 787 48.293 20.944 38.817 1.00 18.75 A N ANISOU 6352 NH1 ARG A 787 2576 2013 2532 -299 13 -3 A N ATOM 6353 NH2 ARG A 787 46.014 21.034 39.297 1.00 18.10 A N ANISOU 6353 NH2 ARG A 787 2629 1896 2351 -141 -193 179 A N ATOM 6354 N ARG A 788 46.540 18.408 44.294 1.00 12.47 A N ANISOU 6354 N ARG A 788 1754 991 1994 -290 281 -194 A N ATOM 6355 CA ARG A 788 46.294 19.521 45.191 1.00 12.64 A C ANISOU 6355 CA ARG A 788 1813 1247 1742 -230 -57 -362 A C ATOM 6356 C ARG A 788 45.838 18.914 46.515 1.00 11.85 A C ANISOU 6356 C ARG A 788 1787 941 1773 -172 48 -326 A C ATOM 6357 O ARG A 788 45.107 17.891 46.498 1.00 12.69 A O ANISOU 6357 O ARG A 788 1778 1052 1992 -257 65 -212 A O ATOM 6358 CB ARG A 788 45.180 20.446 44.670 1.00 14.70 A C ANISOU 6358 CB ARG A 788 2005 1256 2325 -187 -161 -240 A C ATOM 6359 CG ARG A 788 45.505 21.133 43.361 1.00 16.73 A C ANISOU 6359 CG ARG A 788 2510 1286 2558 18 -171 -85 A C ATOM 6360 CD ARG A 788 46.540 22.193 43.707 1.00 19.47 A C ANISOU 6360 CD ARG A 788 3016 1755 2625 -527 -85 58 A C ATOM 6361 NE ARG A 788 46.988 23.008 42.575 1.00 19.51 A N ANISOU 6361 NE ARG A 788 3004 1902 2506 -631 104 -68 A N ATOM 6362 CZ ARG A 788 48.064 22.743 41.851 1.00 20.67 A C ANISOU 6362 CZ ARG A 788 3261 1906 2686 -207 374 271 A C ATOM 6363 NH1 ARG A 788 48.740 21.628 42.091 1.00 19.80 A N ANISOU 6363 NH1 ARG A 788 2882 1414 3226 -512 -389 -235 A N ATOM 6364 NH2 ARG A 788 48.425 23.576 40.882 1.00 23.33 A N ANISOU 6364 NH2 ARG A 788 4290 2062 2510 -595 -71 413 A N ATOM 6365 N ILE A 789 46.416 19.372 47.612 1.00 13.15 A N ANISOU 6365 N ILE A 789 1821 1183 1990 -330 -26 -328 A N ATOM 6366 CA ILE A 789 46.280 18.789 48.916 1.00 13.81 A C ANISOU 6366 CA ILE A 789 1851 1420 1976 -455 -31 -418 A C ATOM 6367 C ILE A 789 45.683 19.811 49.883 1.00 13.99 A C ANISOU 6367 C ILE A 789 2262 1110 1941 -353 -12 -335 A C ATOM 6368 O ILE A 789 46.118 20.976 49.887 1.00 16.21 A O ANISOU 6368 O ILE A 789 2465 1147 2546 -540 244 -521 A O ATOM 6369 CB ILE A 789 47.646 18.286 49.419 1.00 13.85 A C ANISOU 6369 CB ILE A 789 1802 1284 2175 -335 -23 -403 A C ATOM 6370 CG1 ILE A 789 48.288 17.400 48.351 1.00 15.29 A C ANISOU 6370 CG1 ILE A 789 2130 1279 2398 -217 44 -322 A C ATOM 6371 CG2 ILE A 789 47.517 17.591 50.766 1.00 15.78 A C ANISOU 6371 CG2 ILE A 789 2223 1446 2326 -190 -39 -282 A C ATOM 6372 CD1 ILE A 789 49.670 16.904 48.690 1.00 17.58 A C ANISOU 6372 CD1 ILE A 789 2352 1778 2549 96 -168 -293 A C ATOM 6373 N ASN A 790 44.735 19.404 50.727 1.00 13.71 A N ANISOU 6373 N ASN A 790 1895 1408 1906 -276 -245 -316 A N ATOM 6374 CA AASN A 790 44.273 20.270 51.850 0.60 14.48 A C ANISOU 6374 CA AASN A 790 1859 1539 2101 -388 -74 -448 A C ATOM 6375 CA BASN A 790 44.249 20.207 51.860 0.40 14.95 A C ANISOU 6375 CA BASN A 790 1957 1623 2097 -305 -36 -437 A C ATOM 6376 C ASN A 790 44.997 19.769 53.104 1.00 14.51 A C ANISOU 6376 C ASN A 790 2312 1256 1945 -352 58 -434 A C ATOM 6377 O ASN A 790 45.091 18.544 53.320 1.00 15.48 A O ANISOU 6377 O ASN A 790 2412 1299 2168 -383 -163 -242 A O ATOM 6378 CB AASN A 790 42.733 20.308 51.910 0.60 17.02 A C ANISOU 6378 CB AASN A 790 1920 2310 2235 -253 41 -508 A C ATOM 6379 CB BASN A 790 42.772 19.951 52.153 0.40 16.68 A C ANISOU 6379 CB BASN A 790 1939 2236 2159 -93 118 -749 A C ATOM 6380 CG AASN A 790 42.136 21.413 52.769 0.60 18.49 A C ANISOU 6380 CG AASN A 790 2284 1730 3008 -66 -173 -432 A C ATOM 6381 CG BASN A 790 41.873 20.455 51.056 0.40 18.11 A C ANISOU 6381 CG BASN A 790 1834 2962 2084 -229 -69 -916 A C ATOM 6382 ND2AASN A 790 41.480 21.037 53.872 0.60 20.58 A N ANISOU 6382 ND2AASN A 790 3124 2407 2287 -35 -572 -481 A N ATOM 6383 ND2BASN A 790 40.954 19.613 50.611 0.40 26.33 A N ANISOU 6383 ND2BASN A 790 2158 4110 3733 -1501 378 -629 A N ATOM 6384 OD1AASN A 790 42.203 22.608 52.416 0.60 23.16 A O ANISOU 6384 OD1AASN A 790 3161 2397 3239 216 -138 592 A O ATOM 6385 OD1BASN A 790 42.031 21.579 50.607 0.40 19.70 A O ANISOU 6385 OD1BASN A 790 2310 3038 2137 1092 -233 -443 A O ATOM 6386 N ILE A 791 45.535 20.713 53.874 1.00 13.63 A N ANISOU 6386 N ILE A 791 1990 1140 2047 -74 -116 -459 A N ATOM 6387 CA ILE A 791 46.239 20.433 55.100 1.00 14.34 A C ANISOU 6387 CA ILE A 791 2033 1306 2109 15 -75 -257 A C ATOM 6388 C ILE A 791 45.566 21.227 56.210 1.00 14.42 A C ANISOU 6388 C ILE A 791 2296 1238 1945 -270 -100 -397 A C ATOM 6389 O ILE A 791 45.844 22.448 56.361 1.00 14.83 A O ANISOU 6389 O ILE A 791 2514 1072 2045 -237 27 -355 A O ATOM 6390 CB ILE A 791 47.746 20.711 55.008 1.00 14.75 A C ANISOU 6390 CB ILE A 791 2210 1179 2213 -67 84 -136 A C ATOM 6391 CG1 ILE A 791 48.333 19.956 53.817 1.00 15.57 A C ANISOU 6391 CG1 ILE A 791 2106 1569 2238 -72 47 -391 A C ATOM 6392 CG2 ILE A 791 48.398 20.321 56.321 1.00 16.63 A C ANISOU 6392 CG2 ILE A 791 1972 1663 2682 123 -234 -168 A C ATOM 6393 CD1 ILE A 791 49.821 20.060 53.659 1.00 17.57 A C ANISOU 6393 CD1 ILE A 791 2085 1838 2753 20 19 -186 A C ATOM 6394 N GLU A 792 44.632 20.590 56.907 1.00 14.38 A N ANISOU 6394 N GLU A 792 1972 1236 2256 -91 -87 -515 A N ATOM 6395 CA GLU A 792 43.708 21.267 57.827 1.00 14.25 A C ANISOU 6395 CA GLU A 792 2131 1242 2040 -2 15 -390 A C ATOM 6396 C GLU A 792 43.639 20.419 59.105 1.00 15.16 A C ANISOU 6396 C GLU A 792 1870 1620 2270 249 -198 -193 A C ATOM 6397 O GLU A 792 42.670 19.713 59.338 1.00 15.32 A O ANISOU 6397 O GLU A 792 2030 1582 2207 87 -105 -413 A O ATOM 6398 CB GLU A 792 42.347 21.499 57.131 1.00 16.43 A C ANISOU 6398 CB GLU A 792 2220 1466 2557 121 20 -226 A C ATOM 6399 CG GLU A 792 41.299 22.272 57.937 1.00 18.65 A C ANISOU 6399 CG GLU A 792 2314 1978 2792 346 200 -54 A C ATOM 6400 CD GLU A 792 40.010 22.608 57.179 1.00 25.23 A C ANISOU 6400 CD GLU A 792 2749 3651 3184 1029 -91 -26 A C ATOM 6401 OE1 GLU A 792 39.912 22.331 55.981 1.00 32.90 A O ANISOU 6401 OE1 GLU A 792 4057 4895 3546 1542 -1459 -1037 A O ATOM 6402 OE2 GLU A 792 39.054 23.113 57.766 1.00 33.16 A O ANISOU 6402 OE2 GLU A 792 3797 4950 3853 1320 762 -757 A O ATOM 6403 N VAL A 793 44.706 20.511 59.914 1.00 13.42 A N ANISOU 6403 N VAL A 793 1813 1232 2052 -254 -79 -264 A N ATOM 6404 CA VAL A 793 44.775 19.865 61.182 1.00 14.85 A C ANISOU 6404 CA VAL A 793 2057 1534 2052 -306 -201 -233 A C ATOM 6405 C VAL A 793 43.806 20.519 62.167 1.00 15.11 A C ANISOU 6405 C VAL A 793 2514 1169 2057 -113 -243 -478 A C ATOM 6406 O VAL A 793 43.834 21.743 62.328 1.00 16.50 A O ANISOU 6406 O VAL A 793 2893 1085 2290 -136 -187 -489 A O ATOM 6407 CB VAL A 793 46.194 19.894 61.769 1.00 16.48 A C ANISOU 6407 CB VAL A 793 2116 1518 2625 -140 -345 -200 A C ATOM 6408 CG1 VAL A 793 46.180 19.433 63.228 1.00 17.79 A C ANISOU 6408 CG1 VAL A 793 2388 1847 2524 -115 -144 -438 A C ATOM 6409 CG2 VAL A 793 47.167 19.117 60.904 1.00 17.46 A C ANISOU 6409 CG2 VAL A 793 2197 1537 2898 42 -517 -282 A C ATOM 6410 N VAL A 794 42.986 19.727 62.848 1.00 15.20 A N ANISOU 6410 N VAL A 794 2384 1378 2013 -193 -48 -615 A N ATOM 6411 CA VAL A 794 42.100 20.206 63.903 1.00 15.22 A C ANISOU 6411 CA VAL A 794 2392 1279 2111 -186 -49 -619 A C ATOM 6412 C VAL A 794 42.503 19.543 65.212 1.00 17.05 A C ANISOU 6412 C VAL A 794 2406 1859 2212 -332 -142 -468 A C ATOM 6413 O VAL A 794 42.089 18.418 65.486 1.00 17.66 A O ANISOU 6413 O VAL A 794 2499 1645 2563 -306 -115 -542 A O ATOM 6414 CB VAL A 794 40.613 19.983 63.573 1.00 17.65 A C ANISOU 6414 CB VAL A 794 2450 1700 2554 -234 -153 -424 A C ATOM 6415 CG1 VAL A 794 39.714 20.616 64.632 1.00 21.62 A C ANISOU 6415 CG1 VAL A 794 2751 2476 2987 -195 224 -435 A C ATOM 6416 CG2 VAL A 794 40.250 20.524 62.197 1.00 19.97 A C ANISOU 6416 CG2 VAL A 794 2713 2159 2716 -212 -348 -427 A C ATOM 6417 N PRO A 795 43.354 20.185 66.041 1.00 18.68 A N ANISOU 6417 N PRO A 795 2585 1721 2790 -346 -463 -519 A N ATOM 6418 CA PRO A 795 43.775 19.584 67.297 1.00 21.04 A C ANISOU 6418 CA PRO A 795 2957 2308 2727 -320 -214 -654 A C ATOM 6419 C PRO A 795 42.590 19.533 68.268 1.00 19.39 A C ANISOU 6419 C PRO A 795 2744 2275 2345 -283 -405 -417 A C ATOM 6420 O PRO A 795 41.652 20.304 68.156 1.00 21.64 A O ANISOU 6420 O PRO A 795 3274 2719 2227 358 -249 -483 A O ATOM 6421 CB PRO A 795 44.901 20.486 67.838 1.00 21.85 A C ANISOU 6421 CB PRO A 795 3418 2114 2768 -178 -827 -628 A C ATOM 6422 CG PRO A 795 44.921 21.699 66.964 1.00 25.52 A C ANISOU 6422 CG PRO A 795 3368 2937 3390 -332 -961 65 A C ATOM 6423 CD PRO A 795 43.929 21.517 65.833 1.00 19.39 A C ANISOU 6423 CD PRO A 795 2816 1809 2740 -356 -346 -319 A C ATOM 6424 N GLY A 796 42.686 18.601 69.215 1.00 18.60 A N ANISOU 6424 N GLY A 796 2929 1815 2321 30 -242 -658 A N ATOM 6425 CA GLY A 796 41.680 18.413 70.204 1.00 20.14 A C ANISOU 6425 CA GLY A 796 3279 1903 2469 -142 -184 -379 A C ATOM 6426 C GLY A 796 41.941 17.138 70.962 1.00 17.79 A C ANISOU 6426 C GLY A 796 2852 1875 2033 -182 -403 -544 A C ATOM 6427 O GLY A 796 42.996 16.536 70.830 1.00 19.09 A O ANISOU 6427 O GLY A 796 2709 2191 2351 -247 -192 -591 A O ATOM 6428 N GLY A 797 40.984 16.774 71.799 1.00 19.33 A N ANISOU 6428 N GLY A 797 2914 1958 2471 -224 -325 -622 A N ATOM 6429 CA GLY A 797 41.026 15.522 72.518 1.00 21.54 A C ANISOU 6429 CA GLY A 797 3481 2104 2598 -367 -291 -247 A C ATOM 6430 C GLY A 797 42.210 15.402 73.460 1.00 22.42 A C ANISOU 6430 C GLY A 797 3139 2599 2778 -228 -182 -448 A C ATOM 6431 O GLY A 797 42.662 14.288 73.748 1.00 24.47 A O ANISOU 6431 O GLY A 797 3634 2981 2680 283 -60 -203 A O ATOM 6432 N ASP A 798 42.718 16.528 73.969 1.00 24.05 A N ANISOU 6432 N ASP A 798 3534 3125 2479 -733 -61 -567 A N ATOM 6433 CA ASP A 798 43.926 16.461 74.831 1.00 25.85 A C ANISOU 6433 CA ASP A 798 3478 3493 2850 -664 -163 -617 A C ATOM 6434 C ASP A 798 45.145 15.811 74.130 1.00 25.29 A C ANISOU 6434 C ASP A 798 3984 3541 2082 215 -601 -317 A C ATOM 6435 O ASP A 798 46.121 15.432 74.808 1.00 25.42 A O ANISOU 6435 O ASP A 798 3495 4241 1923 -240 -457 113 A O ATOM 6436 CB ASP A 798 43.613 15.771 76.162 1.00 31.80 A C ANISOU 6436 CB ASP A 798 4801 4122 3157 -92 -159 -67 A C ATOM 6437 CG ASP A 798 42.780 16.622 77.116 1.00 45.09 A C ANISOU 6437 CG ASP A 798 7503 4846 4781 -165 886 -1406 A C ATOM 6438 OD1 ASP A 798 42.934 17.844 77.077 1.00 49.63 A O ANISOU 6438 OD1 ASP A 798 9251 5053 4551 -961 1299 -886 A O ATOM 6439 OD2 ASP A 798 41.983 16.045 77.906 1.00 54.24 A O ANISOU 6439 OD2 ASP A 798 7988 6103 6517 -1873 1798 -3063 A O ATOM 6440 N LEU A 799 45.168 15.743 72.789 1.00 23.08 A N ANISOU 6440 N LEU A 799 3390 3273 2106 -292 -43 -355 A N ATOM 6441 CA LEU A 799 46.384 15.327 72.086 1.00 18.39 A C ANISOU 6441 CA LEU A 799 2954 2302 1730 -522 -424 -478 A C ATOM 6442 C LEU A 799 47.444 16.420 72.206 1.00 18.86 A C ANISOU 6442 C LEU A 799 2975 1866 2323 -278 -512 -633 A C ATOM 6443 O LEU A 799 47.123 17.619 72.092 1.00 22.76 A O ANISOU 6443 O LEU A 799 3571 1851 3223 -43 -377 -436 A O ATOM 6444 CB LEU A 799 46.097 15.086 70.599 1.00 18.43 A C ANISOU 6444 CB LEU A 799 2918 2350 1731 -126 -427 -672 A C ATOM 6445 CG LEU A 799 45.195 13.911 70.249 1.00 22.19 A C ANISOU 6445 CG LEU A 799 3694 2514 2223 -314 -739 -533 A C ATOM 6446 CD1 LEU A 799 45.103 13.748 68.736 1.00 21.64 A C ANISOU 6446 CD1 LEU A 799 3487 2646 2086 -464 -616 -353 A C ATOM 6447 CD2 LEU A 799 45.688 12.647 70.879 1.00 25.36 A C ANISOU 6447 CD2 LEU A 799 4945 2480 2209 135 -746 -683 A C ATOM 6448 N GLN A 800 48.692 16.003 72.411 1.00 18.57 A N ANISOU 6448 N GLN A 800 2900 1968 2186 -323 -209 -650 A N ATOM 6449 CA AGLN A 800 49.824 16.899 72.466 0.50 21.51 A C ANISOU 6449 CA AGLN A 800 2924 2612 2634 -525 -72 -549 A C ATOM 6450 CA BGLN A 800 49.813 16.917 72.452 0.50 20.20 A C ANISOU 6450 CA BGLN A 800 2901 2426 2347 -450 -302 -553 A C ATOM 6451 C GLN A 800 50.566 16.921 71.120 1.00 18.18 A C ANISOU 6451 C GLN A 800 2855 1895 2156 -420 -432 -540 A C ATOM 6452 O GLN A 800 51.303 17.835 70.854 1.00 19.20 A O ANISOU 6452 O GLN A 800 3089 2096 2109 -388 -285 -214 A O ATOM 6453 CB AGLN A 800 50.757 16.478 73.606 0.50 26.18 A C ANISOU 6453 CB AGLN A 800 3165 3543 3236 -438 -601 -330 A C ATOM 6454 CB BGLN A 800 50.783 16.541 73.572 0.50 21.72 A C ANISOU 6454 CB BGLN A 800 3193 2745 2315 -441 -535 -409 A C ATOM 6455 CG AGLN A 800 50.160 16.641 75.001 0.50 33.47 A C ANISOU 6455 CG AGLN A 800 4094 4891 3730 -394 19 -382 A C ATOM 6456 CG BGLN A 800 51.877 17.576 73.800 0.50 23.05 A C ANISOU 6456 CG BGLN A 800 3583 2869 2303 -594 -644 -656 A C ATOM 6457 CD AGLN A 800 49.658 15.353 75.621 0.50 41.83 A C ANISOU 6457 CD AGLN A 800 5222 5253 5416 -68 45 315 A C ATOM 6458 CD BGLN A 800 53.156 17.361 73.025 0.50 24.26 A C ANISOU 6458 CD BGLN A 800 4016 3246 1955 86 -803 -831 A C ATOM 6459 NE2AGLN A 800 48.462 15.414 76.192 0.50 45.62 A N ANISOU 6459 NE2AGLN A 800 4615 8326 4391 -924 -726 522 A N ATOM 6460 NE2BGLN A 800 53.843 18.459 72.736 0.50 25.07 A N ANISOU 6460 NE2BGLN A 800 4057 3931 1537 -181 -374 -82 A N ATOM 6461 OE1AGLN A 800 50.334 14.319 75.618 0.50 47.97 A O ANISOU 6461 OE1AGLN A 800 5779 6291 6156 1049 -569 -1901 A O ATOM 6462 OE1BGLN A 800 53.552 16.235 72.719 0.50 28.49 A O ANISOU 6462 OE1BGLN A 800 4928 3667 2228 573 -1026 -1596 A O ATOM 6463 N GLN A 801 50.421 15.863 70.315 1.00 18.74 A N ANISOU 6463 N GLN A 801 3408 1663 2046 -187 -386 -417 A N ATOM 6464 CA GLN A 801 51.109 15.775 69.026 1.00 17.67 A C ANISOU 6464 CA GLN A 801 2886 1647 2180 -392 -363 -336 A C ATOM 6465 C GLN A 801 50.510 14.665 68.165 1.00 17.87 A C ANISOU 6465 C GLN A 801 2776 1937 2075 -530 -256 -417 A C ATOM 6466 O GLN A 801 49.883 13.740 68.688 1.00 16.78 A O ANISOU 6466 O GLN A 801 2838 1720 1815 -405 -438 -355 A O ATOM 6467 CB GLN A 801 52.602 15.516 69.136 1.00 21.33 A C ANISOU 6467 CB GLN A 801 2974 2636 2492 -768 -565 -496 A C ATOM 6468 CG GLN A 801 53.027 14.335 69.953 1.00 23.87 A C ANISOU 6468 CG GLN A 801 3533 2628 2908 -536 -114 -780 A C ATOM 6469 CD GLN A 801 54.534 14.227 69.828 1.00 35.04 A C ANISOU 6469 CD GLN A 801 3566 5090 4658 60 -526 -1110 A C ATOM 6470 NE2 GLN A 801 55.239 14.877 70.732 1.00 45.24 A N ANISOU 6470 NE2 GLN A 801 5994 5087 6105 -1256 -1450 -1161 A N ATOM 6471 OE1 GLN A 801 55.065 13.649 68.875 1.00 45.72 A O ANISOU 6471 OE1 GLN A 801 5623 6144 5602 1970 -751 -1874 A O ATOM 6472 N ALA A 802 50.714 14.788 66.846 1.00 15.17 A N ANISOU 6472 N ALA A 802 2569 1207 1986 -315 -286 -491 A N ATOM 6473 CA ALA A 802 50.377 13.691 65.935 1.00 13.78 A C ANISOU 6473 CA ALA A 802 2409 994 1830 -23 -225 -405 A C ATOM 6474 C ALA A 802 51.234 13.787 64.685 1.00 14.75 A C ANISOU 6474 C ALA A 802 2376 1499 1728 -258 -213 -51 A C ATOM 6475 O ALA A 802 51.622 14.878 64.255 1.00 15.96 A O ANISOU 6475 O ALA A 802 2481 1508 2073 -532 -326 -4 A O ATOM 6476 CB ALA A 802 48.917 13.712 65.590 1.00 14.64 A C ANISOU 6476 CB ALA A 802 2508 1130 1923 -184 -169 -230 A C ATOM 6477 N SER A 803 51.525 12.615 64.115 1.00 15.17 A N ANISOU 6477 N SER A 803 2307 1537 1918 -123 -569 -125 A N ATOM 6478 CA ASER A 803 52.314 12.498 62.907 0.50 15.52 A C ANISOU 6478 CA ASER A 803 2050 1528 2319 -450 -345 -343 A C ATOM 6479 CA BSER A 803 52.345 12.443 62.933 0.50 15.35 A C ANISOU 6479 CA BSER A 803 2039 1530 2261 -378 -399 -290 A C ATOM 6480 C SER A 803 51.566 11.612 61.914 1.00 13.86 A C ANISOU 6480 C SER A 803 2113 1295 1856 -168 -205 -332 A C ATOM 6481 O SER A 803 51.218 10.457 62.212 1.00 15.18 A O ANISOU 6481 O SER A 803 2455 1289 2023 -227 -423 -131 A O ATOM 6482 CB ASER A 803 53.699 11.941 63.185 0.50 17.70 A C ANISOU 6482 CB ASER A 803 2055 2188 2480 -306 -365 -712 A C ATOM 6483 CB BSER A 803 53.660 11.760 63.298 0.50 16.61 A C ANISOU 6483 CB BSER A 803 2172 2004 2134 -214 -583 -447 A C ATOM 6484 OG ASER A 803 54.410 12.771 64.087 0.50 20.32 A O ANISOU 6484 OG ASER A 803 2321 2431 2968 -675 -731 -569 A O ATOM 6485 OG BSER A 803 54.395 11.398 62.136 0.50 20.14 A O ANISOU 6485 OG BSER A 803 2458 2642 2551 100 -138 38 A O ATOM 6486 N THR A 804 51.389 12.124 60.704 1.00 13.43 A N ANISOU 6486 N THR A 804 1933 1062 2105 -297 -270 -283 A N ATOM 6487 CA THR A 804 50.667 11.459 59.644 1.00 13.47 A C ANISOU 6487 CA THR A 804 2063 1197 1856 -366 -218 -217 A C ATOM 6488 C THR A 804 51.488 11.577 58.369 1.00 13.67 A C ANISOU 6488 C THR A 804 2132 1133 1927 -275 -65 -308 A C ATOM 6489 O THR A 804 51.932 12.653 58.042 1.00 14.50 A O ANISOU 6489 O THR A 804 2454 1249 1805 -415 -7 -273 A O ATOM 6490 CB THR A 804 49.265 12.081 59.484 1.00 15.25 A C ANISOU 6490 CB THR A 804 2138 1385 2269 -281 -271 -471 A C ATOM 6491 CG2 THR A 804 48.407 11.299 58.503 1.00 16.13 A C ANISOU 6491 CG2 THR A 804 2232 1561 2334 -95 -527 -492 A C ATOM 6492 OG1 THR A 804 48.628 12.180 60.773 1.00 15.51 A O ANISOU 6492 OG1 THR A 804 2093 1502 2297 -65 -324 -334 A O ATOM 6493 N LYS A 805 51.595 10.492 57.589 1.00 13.75 A N ANISOU 6493 N LYS A 805 2172 1186 1863 12 -88 -303 A N ATOM 6494 CA LYS A 805 52.327 10.465 56.357 1.00 14.85 A C ANISOU 6494 CA LYS A 805 2400 1501 1738 -445 -236 -423 A C ATOM 6495 C LYS A 805 51.464 9.785 55.291 1.00 12.75 A C ANISOU 6495 C LYS A 805 2147 1042 1654 -298 -156 -255 A C ATOM 6496 O LYS A 805 50.816 8.767 55.588 1.00 13.02 A O ANISOU 6496 O LYS A 805 2309 964 1674 -405 -172 -192 A O ATOM 6497 CB LYS A 805 53.643 9.673 56.508 1.00 17.81 A C ANISOU 6497 CB LYS A 805 2462 2191 2111 -230 -181 -463 A C ATOM 6498 CG LYS A 805 54.588 10.158 57.590 1.00 22.28 A C ANISOU 6498 CG LYS A 805 2631 2735 3098 -358 -780 -128 A C ATOM 6499 CD LYS A 805 55.916 9.430 57.595 1.00 27.75 A C ANISOU 6499 CD LYS A 805 2714 3468 4359 51 -664 315 A C ATOM 6500 CE LYS A 805 56.769 9.842 58.774 1.00 35.76 A C ANISOU 6500 CE LYS A 805 3797 4500 5289 -63 -1400 -30 A C ATOM 6501 NZ LYS A 805 58.009 9.034 58.892 1.00 40.79 A N ANISOU 6501 NZ LYS A 805 4089 5840 5567 624 -1623 1430 A N ATOM 6502 N PHE A 806 51.535 10.279 54.061 1.00 12.77 A N ANISOU 6502 N PHE A 806 2211 1073 1564 -416 -70 -187 A N ATOM 6503 CA PHE A 806 50.823 9.696 52.946 1.00 12.30 A C ANISOU 6503 CA PHE A 806 1904 970 1798 -212 -131 -157 A C ATOM 6504 C PHE A 806 51.659 9.794 51.683 1.00 12.22 A C ANISOU 6504 C PHE A 806 1868 1010 1764 -62 -134 -250 A C ATOM 6505 O PHE A 806 51.988 10.905 51.231 1.00 12.84 A O ANISOU 6505 O PHE A 806 1755 1207 1916 -194 -201 -37 A O ATOM 6506 CB PHE A 806 49.446 10.333 52.734 1.00 13.18 A C ANISOU 6506 CB PHE A 806 1943 1087 1975 -76 15 -268 A C ATOM 6507 CG PHE A 806 48.709 9.754 51.567 1.00 12.48 A C ANISOU 6507 CG PHE A 806 1875 1016 1850 -125 -5 -67 A C ATOM 6508 CD1 PHE A 806 48.415 8.397 51.549 1.00 11.71 A C ANISOU 6508 CD1 PHE A 806 1844 929 1677 -2 3 -89 A C ATOM 6509 CD2 PHE A 806 48.363 10.519 50.482 1.00 13.28 A C ANISOU 6509 CD2 PHE A 806 2046 1171 1827 -11 104 -22 A C ATOM 6510 CE1 PHE A 806 47.794 7.835 50.455 1.00 12.93 A C ANISOU 6510 CE1 PHE A 806 1728 1347 1835 -126 -187 -79 A C ATOM 6511 CE2 PHE A 806 47.743 9.959 49.386 1.00 13.22 A C ANISOU 6511 CE2 PHE A 806 1736 1331 1956 -118 -121 88 A C ATOM 6512 CZ PHE A 806 47.493 8.591 49.360 1.00 12.18 A C ANISOU 6512 CZ PHE A 806 1447 1328 1851 -87 -12 -31 A C ATOM 6513 N LEU A 807 51.951 8.618 51.097 1.00 12.13 A N ANISOU 6513 N LEU A 807 1851 968 1787 -136 -63 -216 A N ATOM 6514 CA LEU A 807 52.682 8.547 49.843 1.00 11.08 A C ANISOU 6514 CA LEU A 807 1721 718 1768 -304 -166 1 A C ATOM 6515 C LEU A 807 51.720 8.723 48.677 1.00 10.67 A C ANISOU 6515 C LEU A 807 1632 1000 1421 -98 -78 -198 A C ATOM 6516 O LEU A 807 51.085 7.803 48.203 1.00 13.66 A O ANISOU 6516 O LEU A 807 1984 1169 2034 -230 -259 -327 A O ATOM 6517 CB LEU A 807 53.430 7.224 49.772 1.00 13.39 A C ANISOU 6517 CB LEU A 807 2098 638 2349 -274 2 -174 A C ATOM 6518 CG LEU A 807 54.432 7.070 48.636 1.00 16.45 A C ANISOU 6518 CG LEU A 807 2352 1269 2628 44 -24 -159 A C ATOM 6519 CD1 LEU A 807 55.544 8.107 48.739 1.00 18.75 A C ANISOU 6519 CD1 LEU A 807 2214 1794 3116 -182 400 188 A C ATOM 6520 CD2 LEU A 807 55.006 5.663 48.685 1.00 17.68 A C ANISOU 6520 CD2 LEU A 807 2342 1161 3215 0 395 -114 A C ATOM 6521 N THR A 808 51.567 9.975 48.278 1.00 11.49 A N ANISOU 6521 N THR A 808 1497 1077 1790 -178 -113 -50 A N ATOM 6522 CA THR A 808 50.748 10.367 47.166 1.00 11.89 A C ANISOU 6522 CA THR A 808 1701 1069 1744 -9 -182 -168 A C ATOM 6523 C THR A 808 51.342 9.823 45.873 1.00 12.08 A C ANISOU 6523 C THR A 808 1825 817 1948 -249 -46 -214 A C ATOM 6524 O THR A 808 52.526 9.433 45.851 1.00 12.62 A O ANISOU 6524 O THR A 808 1976 796 2021 51 30 -269 A O ATOM 6525 CB THR A 808 50.637 11.901 47.019 1.00 12.47 A C ANISOU 6525 CB THR A 808 1756 1098 1884 10 -260 -36 A C ATOM 6526 CG2 THR A 808 50.340 12.644 48.300 1.00 12.73 A C ANISOU 6526 CG2 THR A 808 1732 1353 1750 -121 -152 27 A C ATOM 6527 OG1 THR A 808 51.812 12.417 46.395 1.00 12.59 A O ANISOU 6527 OG1 THR A 808 2130 718 1935 -81 73 -275 A O ATOM 6528 N PRO A 809 50.573 9.855 44.760 1.00 13.94 A N ANISOU 6528 N PRO A 809 2402 901 1991 -174 -102 -126 A N ATOM 6529 CA PRO A 809 51.144 9.571 43.451 1.00 15.47 A C ANISOU 6529 CA PRO A 809 2584 1366 1926 -123 91 -50 A C ATOM 6530 C PRO A 809 52.340 10.436 43.006 1.00 15.55 A C ANISOU 6530 C PRO A 809 2776 1484 1646 -272 71 -253 A C ATOM 6531 O PRO A 809 52.995 10.114 42.016 1.00 17.13 A O ANISOU 6531 O PRO A 809 3304 923 2278 -206 634 -97 A O ATOM 6532 CB PRO A 809 49.922 9.755 42.531 1.00 16.66 A C ANISOU 6532 CB PRO A 809 2738 1694 1898 -386 -34 109 A C ATOM 6533 CG PRO A 809 48.700 9.495 43.387 1.00 17.33 A C ANISOU 6533 CG PRO A 809 2704 2015 1863 -110 -165 -401 A C ATOM 6534 CD PRO A 809 49.124 10.123 44.695 1.00 16.64 A C ANISOU 6534 CD PRO A 809 2629 1680 2013 12 -401 -425 A C ATOM 6535 N TYR A 810 52.614 11.519 43.747 1.00 13.20 A N ANISOU 6535 N TYR A 810 1966 1334 1714 -112 66 -252 A N ATOM 6536 CA TYR A 810 53.700 12.468 43.473 1.00 12.79 A C ANISOU 6536 CA TYR A 810 2062 923 1873 -29 37 -362 A C ATOM 6537 C TYR A 810 54.908 12.292 44.401 1.00 13.09 A C ANISOU 6537 C TYR A 810 2039 997 1936 -75 -26 -138 A C ATOM 6538 O TYR A 810 55.991 12.863 44.115 1.00 16.35 A O ANISOU 6538 O TYR A 810 2185 1389 2636 -44 150 210 A O ATOM 6539 CB TYR A 810 53.186 13.902 43.576 1.00 12.15 A C ANISOU 6539 CB TYR A 810 2010 806 1799 -217 -94 -418 A C ATOM 6540 CG TYR A 810 52.090 14.145 42.580 1.00 11.48 A C ANISOU 6540 CG TYR A 810 1760 818 1782 -208 8 -197 A C ATOM 6541 CD1 TYR A 810 52.394 14.595 41.302 1.00 12.16 A C ANISOU 6541 CD1 TYR A 810 1947 898 1772 -172 132 -268 A C ATOM 6542 CD2 TYR A 810 50.758 13.901 42.888 1.00 11.71 A C ANISOU 6542 CD2 TYR A 810 2055 708 1685 -309 410 24 A C ATOM 6543 CE1 TYR A 810 51.415 14.732 40.333 1.00 11.33 A C ANISOU 6543 CE1 TYR A 810 1818 845 1640 -301 143 -121 A C ATOM 6544 CE2 TYR A 810 49.763 14.037 41.945 1.00 13.30 A C ANISOU 6544 CE2 TYR A 810 2143 851 2056 -80 209 -244 A C ATOM 6545 CZ TYR A 810 50.086 14.452 40.654 1.00 12.07 A C ANISOU 6545 CZ TYR A 810 1822 762 1999 -193 136 -293 A C ATOM 6546 OH TYR A 810 49.136 14.562 39.679 1.00 13.77 A O ANISOU 6546 OH TYR A 810 1847 1176 2206 13 4 -373 A O ATOM 6547 N GLY A 811 54.728 11.601 45.528 1.00 13.14 A N ANISOU 6547 N GLY A 811 1761 1245 1984 -258 -101 -60 A N ATOM 6548 CA GLY A 811 55.709 11.563 46.578 1.00 13.09 A C ANISOU 6548 CA GLY A 811 2019 932 2023 -282 -93 -142 A C ATOM 6549 C GLY A 811 55.084 11.835 47.939 1.00 12.26 A C ANISOU 6549 C GLY A 811 1955 747 1955 -201 -166 -150 A C ATOM 6550 O GLY A 811 53.842 11.949 48.088 1.00 13.14 A O ANISOU 6550 O GLY A 811 1914 1048 2028 -273 -86 -288 A O ATOM 6551 N MET A 812 55.936 11.868 48.963 1.00 13.79 A N ANISOU 6551 N MET A 812 1707 1360 2170 -370 -276 -81 A N ATOM 6552 CA MET A 812 55.448 11.899 50.329 1.00 14.55 A C ANISOU 6552 CA MET A 812 2010 1519 1999 -3 -497 -144 A C ATOM 6553 C MET A 812 54.841 13.255 50.699 1.00 14.02 A C ANISOU 6553 C MET A 812 1883 1298 2144 -292 -133 -123 A C ATOM 6554 O MET A 812 55.450 14.322 50.468 1.00 15.37 A O ANISOU 6554 O MET A 812 1858 1578 2403 -490 -91 -117 A O ATOM 6555 CB MET A 812 56.575 11.575 51.306 1.00 17.24 A C ANISOU 6555 CB MET A 812 1970 2142 2436 -82 -799 -233 A C ATOM 6556 CG MET A 812 56.087 11.307 52.714 1.00 22.59 A C ANISOU 6556 CG MET A 812 3343 2652 2586 331 -611 -561 A C ATOM 6557 SD MET A 812 55.052 9.828 52.852 1.00 27.52 A S ANISOU 6557 SD MET A 812 2969 3781 3706 167 -92 893 A S ATOM 6558 CE MET A 812 56.272 8.592 52.446 1.00 32.84 A C ANISOU 6558 CE MET A 812 2880 3795 5800 -304 -142 -1548 A C ATOM 6559 N ALA A 813 53.622 13.203 51.253 1.00 13.44 A N ANISOU 6559 N ALA A 813 1821 1176 2109 -157 -320 -317 A N ATOM 6560 CA ALA A 813 53.016 14.305 51.980 1.00 13.65 A C ANISOU 6560 CA ALA A 813 2056 1061 2066 -227 -246 -307 A C ATOM 6561 C ALA A 813 53.004 13.949 53.462 1.00 14.18 A C ANISOU 6561 C ALA A 813 2280 1126 1981 -302 -275 -295 A C ATOM 6562 O ALA A 813 52.844 12.778 53.812 1.00 14.58 A O ANISOU 6562 O ALA A 813 2570 1133 1837 -474 -140 -144 A O ATOM 6563 CB ALA A 813 51.608 14.576 51.514 1.00 13.28 A C ANISOU 6563 CB ALA A 813 2104 1053 1886 -7 -73 -313 A C ATOM 6564 N SER A 814 53.162 14.917 54.354 1.00 13.53 A N ANISOU 6564 N SER A 814 1801 1421 1915 -425 -278 -407 A N ATOM 6565 CA SER A 814 53.112 14.567 55.773 1.00 13.86 A C ANISOU 6565 CA SER A 814 2066 1365 1836 -271 -239 -456 A C ATOM 6566 C SER A 814 52.759 15.780 56.599 1.00 12.78 A C ANISOU 6566 C SER A 814 1935 1167 1751 -290 -170 -305 A C ATOM 6567 O SER A 814 53.034 16.930 56.193 1.00 14.47 A O ANISOU 6567 O SER A 814 2172 1357 1967 -363 -254 -9 A O ATOM 6568 CB SER A 814 54.409 13.969 56.274 1.00 15.06 A C ANISOU 6568 CB SER A 814 2067 1493 2162 -184 -32 -225 A C ATOM 6569 OG SER A 814 55.473 14.901 56.278 1.00 17.21 A O ANISOU 6569 OG SER A 814 2030 1828 2679 -289 -269 -403 A O ATOM 6570 N THR A 815 52.245 15.505 57.799 1.00 12.74 A N ANISOU 6570 N THR A 815 2010 1108 1720 -268 -311 -319 A N ATOM 6571 CA THR A 815 52.100 16.510 58.840 1.00 13.94 A C ANISOU 6571 CA THR A 815 2299 1413 1584 -465 -238 -395 A C ATOM 6572 C THR A 815 52.715 15.961 60.128 1.00 14.45 A C ANISOU 6572 C THR A 815 2148 1451 1891 -369 -291 -147 A C ATOM 6573 O THR A 815 52.587 14.793 60.474 1.00 14.69 A O ANISOU 6573 O THR A 815 2440 1267 1872 -196 -368 -174 A O ATOM 6574 CB THR A 815 50.634 16.892 59.071 1.00 15.40 A C ANISOU 6574 CB THR A 815 2303 1265 2280 -433 -424 -301 A C ATOM 6575 CG2 THR A 815 50.032 17.514 57.836 1.00 15.69 A C ANISOU 6575 CG2 THR A 815 1932 1508 2521 -129 -366 -136 A C ATOM 6576 OG1 THR A 815 49.906 15.711 59.438 1.00 15.11 A O ANISOU 6576 OG1 THR A 815 2480 1067 2195 -316 -320 -414 A O ATOM 6577 N LYS A 816 53.391 16.836 60.851 1.00 15.69 A N ANISOU 6577 N LYS A 816 2261 1532 2166 -525 -570 -122 A N ATOM 6578 CA ALYS A 816 53.820 16.590 62.211 0.50 15.75 A C ANISOU 6578 CA ALYS A 816 2352 1557 2075 -171 -444 -281 A C ATOM 6579 CA BLYS A 816 53.822 16.593 62.207 0.50 16.06 A C ANISOU 6579 CA BLYS A 816 2550 1532 2019 -244 -403 -267 A C ATOM 6580 C LYS A 816 53.478 17.861 62.985 1.00 15.97 A C ANISOU 6580 C LYS A 816 2298 1517 2251 -410 -267 -359 A C ATOM 6581 O LYS A 816 53.970 18.929 62.646 1.00 17.39 A O ANISOU 6581 O LYS A 816 2863 1449 2295 -547 -494 -196 A O ATOM 6582 CB ALYS A 816 55.321 16.299 62.309 0.50 18.47 A C ANISOU 6582 CB ALYS A 816 2409 1895 2713 -56 -498 -338 A C ATOM 6583 CB BLYS A 816 55.324 16.306 62.286 0.50 18.78 A C ANISOU 6583 CB BLYS A 816 2633 1928 2573 -208 -485 -215 A C ATOM 6584 CG ALYS A 816 55.853 16.029 63.716 0.50 24.36 A C ANISOU 6584 CG ALYS A 816 3129 2773 3354 375 -1067 -87 A C ATOM 6585 CG BLYS A 816 55.893 16.128 63.689 0.50 26.28 A C ANISOU 6585 CG BLYS A 816 3956 2901 3126 43 -1066 216 A C ATOM 6586 CD ALYS A 816 57.380 15.899 63.797 0.50 29.32 A C ANISOU 6586 CD ALYS A 816 3123 3623 4391 778 -1324 -328 A C ATOM 6587 CD BLYS A 816 55.259 15.015 64.485 0.50 30.88 A C ANISOU 6587 CD BLYS A 816 4129 3704 3899 -289 -1114 881 A C ATOM 6588 CE ALYS A 816 58.113 17.113 63.262 0.50 35.09 A C ANISOU 6588 CE ALYS A 816 3204 4668 5458 386 -1442 224 A C ATOM 6589 CE BLYS A 816 55.823 14.878 65.887 0.50 36.79 A C ANISOU 6589 CE BLYS A 816 5359 4794 3823 -3 -1310 571 A C ATOM 6590 NZ ALYS A 816 59.590 16.989 63.356 0.50 40.66 A N ANISOU 6590 NZ ALYS A 816 3101 5927 6418 1280 127 -157 A N ATOM 6591 NZ BLYS A 816 57.289 14.627 65.899 0.50 38.94 A N ANISOU 6591 NZ BLYS A 816 5240 4834 4721 8 -1697 1577 A N ATOM 6592 N TRP A 817 52.598 17.743 63.966 1.00 15.04 A N ANISOU 6592 N TRP A 817 2379 1220 2113 -389 -403 -546 A N ATOM 6593 CA TRP A 817 52.226 18.908 64.763 1.00 15.31 A C ANISOU 6593 CA TRP A 817 2693 1204 1920 -402 -435 -571 A C ATOM 6594 C TRP A 817 52.334 18.596 66.246 1.00 16.02 A C ANISOU 6594 C TRP A 817 2618 1504 1964 -365 -379 -271 A C ATOM 6595 O TRP A 817 52.291 17.445 66.668 1.00 16.43 A O ANISOU 6595 O TRP A 817 2886 1516 1839 -264 -314 -312 A O ATOM 6596 CB TRP A 817 50.837 19.444 64.406 1.00 15.98 A C ANISOU 6596 CB TRP A 817 2472 1719 1879 -462 -174 -453 A C ATOM 6597 CG TRP A 817 49.699 18.500 64.609 1.00 14.67 A C ANISOU 6597 CG TRP A 817 2391 1390 1790 -318 -171 -443 A C ATOM 6598 CD1 TRP A 817 49.154 17.651 63.682 1.00 15.78 A C ANISOU 6598 CD1 TRP A 817 2730 1361 1905 -399 -481 -224 A C ATOM 6599 CD2 TRP A 817 48.947 18.313 65.821 1.00 15.83 A C ANISOU 6599 CD2 TRP A 817 2515 1397 2100 -517 -8 -431 A C ATOM 6600 CE2 TRP A 817 47.954 17.344 65.548 1.00 16.37 A C ANISOU 6600 CE2 TRP A 817 2562 1273 2384 -405 -277 -249 A C ATOM 6601 CE3 TRP A 817 48.985 18.888 67.098 1.00 18.37 A C ANISOU 6601 CE3 TRP A 817 2966 1967 2043 -321 -309 -520 A C ATOM 6602 NE1 TRP A 817 48.112 16.965 64.241 1.00 16.60 A N ANISOU 6602 NE1 TRP A 817 2523 1400 2382 -407 -240 -520 A N ATOM 6603 CZ2 TRP A 817 47.007 16.965 66.492 1.00 17.23 A C ANISOU 6603 CZ2 TRP A 817 2686 1491 2368 -359 -207 -141 A C ATOM 6604 CZ3 TRP A 817 48.053 18.500 68.041 1.00 17.48 A C ANISOU 6604 CZ3 TRP A 817 3015 2042 1584 -494 -560 -387 A C ATOM 6605 CH2 TRP A 817 47.087 17.532 67.741 1.00 18.88 A C ANISOU 6605 CH2 TRP A 817 2808 1998 2368 -538 0 -275 A C ATOM 6606 N TRP A 818 52.499 19.653 67.036 1.00 16.69 A N ANISOU 6606 N TRP A 818 2927 1622 1792 -415 -393 -377 A N ATOM 6607 CA TRP A 818 52.557 19.498 68.458 1.00 17.87 A C ANISOU 6607 CA TRP A 818 3214 1510 2062 -373 -386 -539 A C ATOM 6608 C TRP A 818 52.104 20.796 69.110 1.00 17.48 A C ANISOU 6608 C TRP A 818 3120 1189 2330 -482 -536 -529 A C ATOM 6609 O TRP A 818 52.098 21.872 68.464 1.00 19.63 A O ANISOU 6609 O TRP A 818 3169 1556 2733 -383 -541 -206 A O ATOM 6610 CB TRP A 818 53.960 19.055 68.923 1.00 18.88 A C ANISOU 6610 CB TRP A 818 3113 1983 2074 -421 -693 -411 A C ATOM 6611 CG TRP A 818 55.080 20.031 68.694 1.00 20.27 A C ANISOU 6611 CG TRP A 818 2922 2068 2711 -416 -786 -396 A C ATOM 6612 CD1 TRP A 818 55.644 20.878 69.615 1.00 23.31 A C ANISOU 6612 CD1 TRP A 818 3468 2720 2668 -760 -862 -424 A C ATOM 6613 CD2 TRP A 818 55.803 20.250 67.474 1.00 21.33 A C ANISOU 6613 CD2 TRP A 818 2803 2240 3058 -638 -583 -641 A C ATOM 6614 CE2 TRP A 818 56.781 21.244 67.735 1.00 21.84 A C ANISOU 6614 CE2 TRP A 818 2771 2107 3418 -491 -862 -272 A C ATOM 6615 CE3 TRP A 818 55.730 19.711 66.186 1.00 22.00 A C ANISOU 6615 CE3 TRP A 818 2580 2693 3082 -393 -133 -867 A C ATOM 6616 NE1 TRP A 818 56.643 21.624 69.043 1.00 24.61 A N ANISOU 6616 NE1 TRP A 818 3377 2672 3298 -545 -908 -201 A N ATOM 6617 CZ2 TRP A 818 57.656 21.700 66.752 1.00 25.25 A C ANISOU 6617 CZ2 TRP A 818 2934 2659 3999 -301 -271 -299 A C ATOM 6618 CZ3 TRP A 818 56.586 20.172 65.212 1.00 25.33 A C ANISOU 6618 CZ3 TRP A 818 3146 3260 3217 -360 57 -621 A C ATOM 6619 CH2 TRP A 818 57.533 21.160 65.491 1.00 26.97 A C ANISOU 6619 CH2 TRP A 818 3445 2939 3863 -494 89 -280 A C ATOM 6620 N LEU A 819 51.688 20.671 70.369 1.00 20.47 A N ANISOU 6620 N LEU A 819 3421 1840 2516 -413 -122 -850 A N ATOM 6621 CA LEU A 819 51.236 21.809 71.146 1.00 21.43 A C ANISOU 6621 CA LEU A 819 3992 1592 2556 -407 -155 -820 A C ATOM 6622 C LEU A 819 52.130 22.031 72.361 1.00 25.70 A C ANISOU 6622 C LEU A 819 4622 2719 2421 -324 -338 -766 A C ATOM 6623 O LEU A 819 52.608 21.085 72.960 1.00 29.69 A O ANISOU 6623 O LEU A 819 5367 3040 2873 -176 -898 -853 A O ATOM 6624 CB LEU A 819 49.833 21.523 71.675 1.00 24.67 A C ANISOU 6624 CB LEU A 819 3743 2007 3621 -75 -39 -738 A C ATOM 6625 CG LEU A 819 48.735 21.401 70.638 1.00 25.96 A C ANISOU 6625 CG LEU A 819 3833 2596 3434 -423 -177 -940 A C ATOM 6626 CD1 LEU A 819 47.473 20.902 71.282 1.00 29.47 A C ANISOU 6626 CD1 LEU A 819 4745 2204 4246 -763 243 -512 A C ATOM 6627 CD2 LEU A 819 48.456 22.748 70.027 1.00 35.82 A C ANISOU 6627 CD2 LEU A 819 4886 3952 4770 -626 -143 827 A C ATOM 6628 N ASP A 820 52.230 23.290 72.783 1.00 26.35 A N ANISOU 6628 N ASP A 820 4255 2892 2862 -944 -407 -987 A N ATOM 6629 CA ASP A 820 52.817 23.635 74.083 1.00 31.61 A C ANISOU 6629 CA ASP A 820 4647 4036 3327 -848 -1103 -1012 A C ATOM 6630 C ASP A 820 52.408 25.079 74.412 1.00 33.04 A C ANISOU 6630 C ASP A 820 5647 3926 2980 -538 -872 -529 A C ATOM 6631 O ASP A 820 51.471 25.595 73.822 1.00 35.87 A O ANISOU 6631 O ASP A 820 6393 3103 4130 96 -559 -303 A O ATOM 6632 CB ASP A 820 54.321 23.353 74.066 1.00 35.30 A C ANISOU 6632 CB ASP A 820 4926 4907 3577 -205 -858 -665 A C ATOM 6633 CG ASP A 820 55.078 24.087 72.979 1.00 38.98 A C ANISOU 6633 CG ASP A 820 5423 5657 3729 70 -709 -44 A C ATOM 6634 OD1 ASP A 820 54.661 25.230 72.633 1.00 34.15 A O ANISOU 6634 OD1 ASP A 820 5098 4169 3706 -536 -889 -1060 A O ATOM 6635 OD2 ASP A 820 56.100 23.515 72.507 1.00 42.46 A O ANISOU 6635 OD2 ASP A 820 5284 6967 3881 201 -613 176 A O ATOM 6636 N GLY A 821 53.065 25.705 75.386 1.00 40.02 A N ANISOU 6636 N GLY A 821 6599 4687 3916 -357 -1328 -1341 A N ATOM 6637 CA GLY A 821 52.720 27.098 75.808 1.00 43.64 A C ANISOU 6637 CA GLY A 821 7408 4439 4735 -1229 -864 -1878 A C ATOM 6638 C GLY A 821 51.239 27.269 76.163 1.00 55.88 A C ANISOU 6638 C GLY A 821 7754 8194 5283 203 -494 -2049 A C ATOM 6639 O GLY A 821 50.635 26.471 76.931 1.00 58.70 A O ANISOU 6639 O GLY A 821 8120 10427 3754 -225 429 -1708 A O ATOM 6640 N GLY A 828 45.741 30.986 74.826 1.00 64.09 A N ANISOU 6640 N GLY A 828 7826 7606 8916 128 -2393 -690 A N ATOM 6641 CA GLY A 828 45.493 29.580 74.525 1.00 70.07 A C ANISOU 6641 CA GLY A 828 8987 8211 9424 300 -2258 -2005 A C ATOM 6642 C GLY A 828 46.794 28.801 74.458 1.00 70.01 A C ANISOU 6642 C GLY A 828 9889 7620 9091 376 822 -2562 A C ATOM 6643 O GLY A 828 47.676 28.991 75.290 1.00 74.59 A O ANISOU 6643 O GLY A 828 9889 14185 4264 208 128 -3955 A O ATOM 6644 N PHE A 829 46.923 27.945 73.443 1.00 53.96 A N ANISOU 6644 N PHE A 829 5771 6844 7884 -27 249 -1277 A N ATOM 6645 CA PHE A 829 48.106 27.119 73.248 1.00 47.05 A C ANISOU 6645 CA PHE A 829 6022 5692 6162 136 -58 124 A C ATOM 6646 C PHE A 829 48.909 27.658 72.053 1.00 36.29 A C ANISOU 6646 C PHE A 829 4227 4549 5013 -35 -673 -908 A C ATOM 6647 O PHE A 829 48.388 28.390 71.212 1.00 35.01 A O ANISOU 6647 O PHE A 829 4646 4833 3823 -36 459 -766 A O ATOM 6648 CB PHE A 829 47.691 25.653 73.065 1.00 56.40 A C ANISOU 6648 CB PHE A 829 8180 5776 7472 70 491 -726 A C ATOM 6649 CG PHE A 829 47.491 24.860 74.339 1.00 67.86 A C ANISOU 6649 CG PHE A 829 9583 8203 7997 392 724 226 A C ATOM 6650 CD1 PHE A 829 48.560 24.211 74.954 1.00 70.21 A C ANISOU 6650 CD1 PHE A 829 9594 8366 8715 1325 994 -209 A C ATOM 6651 CD2 PHE A 829 46.233 24.736 74.919 1.00 76.20 A C ANISOU 6651 CD2 PHE A 829 9451 10569 8929 436 557 1357 A C ATOM 6652 CE1 PHE A 829 48.379 23.476 76.119 1.00 74.21 A C ANISOU 6652 CE1 PHE A 829 9409 9722 9063 1913 934 927 A C ATOM 6653 CE2 PHE A 829 46.051 23.997 76.082 1.00 74.45 A C ANISOU 6653 CE2 PHE A 829 9490 10843 7954 -442 894 727 A C ATOM 6654 CZ PHE A 829 47.124 23.368 76.680 1.00 76.08 A C ANISOU 6654 CZ PHE A 829 10548 9717 8639 721 1760 1324 A C ATOM 6655 N ASP A 830 50.194 27.298 72.006 1.00 28.73 A N ANISOU 6655 N ASP A 830 4677 2354 3884 46 -286 -1564 A N ATOM 6656 CA ASP A 830 51.023 27.479 70.867 1.00 26.36 A C ANISOU 6656 CA ASP A 830 3878 2088 4047 -207 -132 -1168 A C ATOM 6657 C ASP A 830 50.954 26.194 70.026 1.00 24.07 A C ANISOU 6657 C ASP A 830 3515 2026 3604 -19 -79 -824 A C ATOM 6658 O ASP A 830 51.103 25.098 70.573 1.00 26.32 A O ANISOU 6658 O ASP A 830 4893 2179 2928 -576 -121 -723 A O ATOM 6659 CB ASP A 830 52.476 27.737 71.270 1.00 28.85 A C ANISOU 6659 CB ASP A 830 4223 2656 4083 -808 -173 -1386 A C ATOM 6660 CG ASP A 830 52.672 29.070 71.938 1.00 38.57 A C ANISOU 6660 CG ASP A 830 6095 2768 5789 -998 -610 -2431 A C ATOM 6661 OD1 ASP A 830 51.761 29.909 71.784 1.00 38.53 A O ANISOU 6661 OD1 ASP A 830 4858 4290 5492 -637 -285 -1546 A O ATOM 6662 OD2 ASP A 830 53.719 29.174 72.599 1.00 41.87 A O ANISOU 6662 OD2 ASP A 830 6177 4664 5065 -472 -410 94 A O ATOM 6663 N PHE A 831 50.705 26.358 68.722 1.00 21.38 A N ANISOU 6663 N PHE A 831 3738 1093 3293 -439 187 -779 A N ATOM 6664 CA PHE A 831 50.562 25.255 67.776 1.00 18.78 A C ANISOU 6664 CA PHE A 831 3031 1154 2949 -489 189 -592 A C ATOM 6665 C PHE A 831 51.752 25.298 66.818 1.00 20.09 A C ANISOU 6665 C PHE A 831 3012 1925 2696 -86 131 -467 A C ATOM 6666 O PHE A 831 52.075 26.335 66.264 1.00 23.72 A O ANISOU 6666 O PHE A 831 3840 1850 3321 -373 570 -324 A O ATOM 6667 CB PHE A 831 49.240 25.393 67.014 1.00 20.91 A C ANISOU 6667 CB PHE A 831 2848 2375 2721 -195 135 -736 A C ATOM 6668 CG PHE A 831 49.040 24.394 65.903 1.00 20.07 A C ANISOU 6668 CG PHE A 831 2762 2156 2705 -92 -282 -400 A C ATOM 6669 CD1 PHE A 831 48.631 23.095 66.183 1.00 19.59 A C ANISOU 6669 CD1 PHE A 831 2784 2133 2525 -181 30 -341 A C ATOM 6670 CD2 PHE A 831 49.268 24.743 64.586 1.00 20.88 A C ANISOU 6670 CD2 PHE A 831 2805 2362 2765 -211 -75 -344 A C ATOM 6671 CE1 PHE A 831 48.434 22.175 65.167 1.00 20.76 A C ANISOU 6671 CE1 PHE A 831 2920 2247 2721 -169 -199 -348 A C ATOM 6672 CE2 PHE A 831 49.050 23.825 63.576 1.00 20.82 A C ANISOU 6672 CE2 PHE A 831 2765 2548 2597 49 -193 -311 A C ATOM 6673 CZ PHE A 831 48.649 22.538 63.865 1.00 20.46 A C ANISOU 6673 CZ PHE A 831 2830 2323 2621 103 -240 -324 A C ATOM 6674 N HIS A 832 52.362 24.148 66.603 1.00 17.09 A N ANISOU 6674 N HIS A 832 2389 1673 2431 -350 -458 -536 A N ATOM 6675 CA HIS A 832 53.522 24.021 65.733 1.00 17.24 A C ANISOU 6675 CA HIS A 832 2645 1510 2394 -493 -301 -544 A C ATOM 6676 C HIS A 832 53.220 22.939 64.707 1.00 16.14 A C ANISOU 6676 C HIS A 832 2519 1471 2143 -461 7 -489 A C ATOM 6677 O HIS A 832 52.765 21.852 65.096 1.00 16.65 A O ANISOU 6677 O HIS A 832 2943 1496 1886 -426 -156 -282 A O ATOM 6678 CB HIS A 832 54.755 23.627 66.550 1.00 17.38 A C ANISOU 6678 CB HIS A 832 2714 1659 2229 -607 -329 -406 A C ATOM 6679 CG HIS A 832 54.923 24.466 67.767 1.00 19.26 A C ANISOU 6679 CG HIS A 832 2769 2115 2432 -800 -313 -715 A C ATOM 6680 CD2 HIS A 832 54.534 24.229 69.038 1.00 23.07 A C ANISOU 6680 CD2 HIS A 832 4129 2341 2293 -624 -227 -932 A C ATOM 6681 ND1 HIS A 832 55.517 25.723 67.760 1.00 22.86 A N ANISOU 6681 ND1 HIS A 832 3505 2205 2974 -1029 -195 -973 A N ATOM 6682 CE1 HIS A 832 55.517 26.196 68.999 1.00 27.48 A C ANISOU 6682 CE1 HIS A 832 4628 2751 3060 -1050 -137 -819 A C ATOM 6683 NE2 HIS A 832 54.892 25.318 69.794 1.00 25.47 A N ANISOU 6683 NE2 HIS A 832 4479 2537 2659 -1038 -306 -969 A N ATOM 6684 N LEU A 833 53.507 23.223 63.436 1.00 14.92 A N ANISOU 6684 N LEU A 833 2390 1290 1987 -457 -84 -619 A N ATOM 6685 CA LEU A 833 53.244 22.269 62.353 1.00 14.94 A C ANISOU 6685 CA LEU A 833 2469 1068 2139 -376 -233 -577 A C ATOM 6686 C LEU A 833 54.404 22.267 61.366 1.00 15.78 A C ANISOU 6686 C LEU A 833 2326 1461 2205 -272 -245 -345 A C ATOM 6687 O LEU A 833 54.825 23.315 60.859 1.00 16.92 A O ANISOU 6687 O LEU A 833 2522 1498 2407 -599 -476 -318 A O ATOM 6688 CB LEU A 833 51.949 22.690 61.643 1.00 16.76 A C ANISOU 6688 CB LEU A 833 2474 1844 2049 -290 -293 -461 A C ATOM 6689 CG LEU A 833 51.631 21.985 60.330 1.00 15.71 A C ANISOU 6689 CG LEU A 833 2261 1443 2264 -206 -495 -501 A C ATOM 6690 CD1 LEU A 833 51.311 20.511 60.550 1.00 17.54 A C ANISOU 6690 CD1 LEU A 833 2703 1604 2358 -446 -545 -217 A C ATOM 6691 CD2 LEU A 833 50.452 22.628 59.588 1.00 18.02 A C ANISOU 6691 CD2 LEU A 833 2593 1591 2663 -277 -824 -461 A C ATOM 6692 N VAL A 834 54.856 21.062 61.016 1.00 16.17 A N ANISOU 6692 N VAL A 834 2093 1516 2533 -221 -495 -407 A N ATOM 6693 CA VAL A 834 55.732 20.835 59.893 1.00 16.59 A C ANISOU 6693 CA VAL A 834 2409 1472 2421 -395 -438 -474 A C ATOM 6694 C VAL A 834 54.947 20.062 58.841 1.00 15.44 A C ANISOU 6694 C VAL A 834 2350 1332 2182 -367 -386 -344 A C ATOM 6695 O VAL A 834 54.465 18.949 59.124 1.00 16.34 A O ANISOU 6695 O VAL A 834 2526 1207 2475 -342 -496 -436 A O ATOM 6696 CB VAL A 834 56.990 20.064 60.317 1.00 17.81 A C ANISOU 6696 CB VAL A 834 2578 1599 2589 -276 -461 -264 A C ATOM 6697 CG1 VAL A 834 57.903 19.760 59.132 1.00 20.83 A C ANISOU 6697 CG1 VAL A 834 2547 2503 2865 -394 -420 -393 A C ATOM 6698 CG2 VAL A 834 57.757 20.832 61.386 1.00 20.27 A C ANISOU 6698 CG2 VAL A 834 2404 2777 2519 -197 -340 -755 A C ATOM 6699 N ALA A 835 54.808 20.653 57.650 1.00 16.33 A N ANISOU 6699 N ALA A 835 2918 1226 2060 -649 -406 -584 A N ATOM 6700 CA ALA A 835 54.029 20.082 56.566 1.00 15.98 A C ANISOU 6700 CA ALA A 835 2639 1241 2192 -665 -357 -618 A C ATOM 6701 C ALA A 835 54.967 19.848 55.384 1.00 17.42 A C ANISOU 6701 C ALA A 835 2703 1405 2510 -506 -160 -442 A C ATOM 6702 O ALA A 835 55.672 20.745 54.966 1.00 20.28 A O ANISOU 6702 O ALA A 835 3147 2043 2515 -1016 396 -740 A O ATOM 6703 CB ALA A 835 52.918 21.011 56.171 1.00 18.45 A C ANISOU 6703 CB ALA A 835 2631 2213 2164 -324 -345 -656 A C ATOM 6704 N GLU A 836 54.988 18.610 54.905 1.00 14.56 A N ANISOU 6704 N GLU A 836 2303 1328 1899 -383 -232 -306 A N ATOM 6705 CA GLU A 836 55.759 18.221 53.734 1.00 14.67 A C ANISOU 6705 CA GLU A 836 2175 1501 1896 -466 -182 28 A C ATOM 6706 C GLU A 836 54.812 18.076 52.549 1.00 13.91 A C ANISOU 6706 C GLU A 836 1943 1366 1974 -463 -152 -25 A C ATOM 6707 O GLU A 836 53.804 17.374 52.664 1.00 14.79 A O ANISOU 6707 O GLU A 836 1912 1334 2373 -494 -141 -195 A O ATOM 6708 CB GLU A 836 56.415 16.888 54.035 1.00 19.06 A C ANISOU 6708 CB GLU A 836 2957 1773 2511 -95 -590 -333 A C ATOM 6709 CG GLU A 836 57.287 16.327 52.971 1.00 23.25 A C ANISOU 6709 CG GLU A 836 2849 2730 3252 -167 -146 -328 A C ATOM 6710 CD GLU A 836 57.859 14.960 53.366 1.00 28.07 A C ANISOU 6710 CD GLU A 836 3611 3022 4032 296 257 180 A C ATOM 6711 OE1 GLU A 836 57.384 14.346 54.411 1.00 25.95 A O ANISOU 6711 OE1 GLU A 836 2903 2789 4164 517 809 -273 A O ATOM 6712 OE2 GLU A 836 58.772 14.506 52.650 1.00 31.22 A O ANISOU 6712 OE2 GLU A 836 3100 3764 4997 246 359 -540 A O ATOM 6713 N VAL A 837 55.130 18.763 51.457 1.00 12.60 A N ANISOU 6713 N VAL A 837 1922 1031 1831 -387 -5 -261 A N ATOM 6714 CA VAL A 837 54.318 18.827 50.233 1.00 13.92 A C ANISOU 6714 CA VAL A 837 2248 988 2052 -392 -98 -85 A C ATOM 6715 C VAL A 837 55.196 18.319 49.105 1.00 14.95 A C ANISOU 6715 C VAL A 837 1974 1334 2372 -345 0 -203 A C ATOM 6716 O VAL A 837 56.288 18.832 48.896 1.00 14.21 A O ANISOU 6716 O VAL A 837 1977 1168 2253 -360 46 -215 A O ATOM 6717 CB VAL A 837 53.793 20.253 49.985 1.00 15.74 A C ANISOU 6717 CB VAL A 837 2251 1241 2487 -111 -134 15 A C ATOM 6718 CG1 VAL A 837 53.043 20.415 48.662 1.00 15.77 A C ANISOU 6718 CG1 VAL A 837 2332 1402 2256 -237 94 256 A C ATOM 6719 CG2 VAL A 837 52.929 20.687 51.159 1.00 15.79 A C ANISOU 6719 CG2 VAL A 837 2429 1142 2427 -86 -73 -92 A C ATOM 6720 N PRO A 838 54.785 17.263 48.368 1.00 14.54 A N ANISOU 6720 N PRO A 838 1951 1440 2132 -335 20 -243 A N ATOM 6721 CA PRO A 838 55.685 16.692 47.384 1.00 12.51 A C ANISOU 6721 CA PRO A 838 1548 1165 2039 -508 -40 -118 A C ATOM 6722 C PRO A 838 55.859 17.513 46.118 1.00 13.22 A C ANISOU 6722 C PRO A 838 1698 1263 2062 -382 -79 -146 A C ATOM 6723 O PRO A 838 54.991 18.337 45.742 1.00 14.02 A O ANISOU 6723 O PRO A 838 1976 1195 2154 -327 -237 -85 A O ATOM 6724 CB PRO A 838 55.066 15.304 47.093 1.00 13.59 A C ANISOU 6724 CB PRO A 838 2119 1026 2017 -416 -206 -220 A C ATOM 6725 CG PRO A 838 53.593 15.479 47.428 1.00 14.15 A C ANISOU 6725 CG PRO A 838 1948 1099 2329 -341 -379 -277 A C ATOM 6726 CD PRO A 838 53.520 16.532 48.509 1.00 14.43 A C ANISOU 6726 CD PRO A 838 2076 1197 2209 -341 -12 -214 A C ATOM 6727 N PRO A 839 56.991 17.267 45.412 1.00 12.60 A N ANISOU 6727 N PRO A 839 1713 1198 1877 -391 -179 -334 A N ATOM 6728 CA PRO A 839 57.232 17.887 44.121 1.00 13.24 A C ANISOU 6728 CA PRO A 839 1809 1157 2063 -112 -309 -42 A C ATOM 6729 C PRO A 839 56.000 17.731 43.220 1.00 13.51 A C ANISOU 6729 C PRO A 839 1796 1315 2022 -216 -321 -86 A C ATOM 6730 O PRO A 839 55.379 16.673 43.160 1.00 13.59 A O ANISOU 6730 O PRO A 839 1903 1066 2192 -115 -224 -135 A O ATOM 6731 CB PRO A 839 58.480 17.164 43.587 1.00 14.62 A C ANISOU 6731 CB PRO A 839 1847 1428 2278 -257 -24 -24 A C ATOM 6732 CG PRO A 839 59.184 16.688 44.833 1.00 14.97 A C ANISOU 6732 CG PRO A 839 1770 1565 2351 -173 -61 -289 A C ATOM 6733 CD PRO A 839 58.073 16.332 45.787 1.00 15.37 A C ANISOU 6733 CD PRO A 839 1956 1635 2246 11 111 -410 A C ATOM 6734 N ASN A 840 55.728 18.762 42.427 1.00 13.81 A N ANISOU 6734 N ASN A 840 2050 1295 1899 -93 -183 -51 A N ATOM 6735 CA ASN A 840 54.684 18.791 41.398 1.00 12.09 A C ANISOU 6735 CA ASN A 840 1942 1032 1617 -91 -9 -116 A C ATOM 6736 C ASN A 840 53.273 18.932 41.980 1.00 13.03 A C ANISOU 6736 C ASN A 840 2009 1098 1843 -213 -20 60 A C ATOM 6737 O ASN A 840 52.294 18.774 41.226 1.00 15.88 A O ANISOU 6737 O ASN A 840 1924 1780 2328 -216 -139 -185 A O ATOM 6738 CB ASN A 840 54.779 17.584 40.452 1.00 13.12 A C ANISOU 6738 CB ASN A 840 1893 1114 1977 -222 -226 -266 A C ATOM 6739 CG ASN A 840 54.437 17.965 39.025 1.00 12.17 A C ANISOU 6739 CG ASN A 840 1772 943 1907 -142 -57 26 A C ATOM 6740 ND2 ASN A 840 54.051 17.004 38.196 1.00 14.23 A N ANISOU 6740 ND2 ASN A 840 2009 1294 2103 -222 62 -337 A N ATOM 6741 OD1 ASN A 840 54.542 19.155 38.653 1.00 13.63 A O ANISOU 6741 OD1 ASN A 840 2002 922 2255 -332 24 101 A O ATOM 6742 N THR A 841 53.163 19.197 43.294 1.00 13.04 A N ANISOU 6742 N THR A 841 1869 1146 1939 -406 28 -273 A N ATOM 6743 CA THR A 841 51.860 19.427 43.929 1.00 13.42 A C ANISOU 6743 CA THR A 841 1890 1021 2184 -155 5 -163 A C ATOM 6744 C THR A 841 51.851 20.807 44.604 1.00 13.45 A C ANISOU 6744 C THR A 841 1806 1105 2197 -261 -90 -251 A C ATOM 6745 O THR A 841 52.908 21.414 44.816 1.00 14.18 A O ANISOU 6745 O THR A 841 1924 978 2485 -354 -46 -187 A O ATOM 6746 CB THR A 841 51.513 18.328 44.941 1.00 12.65 A C ANISOU 6746 CB THR A 841 1858 943 2004 27 -139 -167 A C ATOM 6747 CG2 THR A 841 51.671 16.944 44.343 1.00 14.45 A C ANISOU 6747 CG2 THR A 841 2133 956 2401 -71 -6 -335 A C ATOM 6748 OG1 THR A 841 52.299 18.458 46.141 1.00 13.96 A O ANISOU 6748 OG1 THR A 841 2122 1031 2150 -358 -201 -106 A O ATOM 6749 N ARG A 842 50.647 21.191 45.033 1.00 13.25 A N ANISOU 6749 N ARG A 842 1772 1187 2074 -264 -168 -359 A N ATOM 6750 CA ARG A 842 50.450 22.386 45.844 1.00 13.65 A C ANISOU 6750 CA ARG A 842 1785 958 2442 -225 25 -299 A C ATOM 6751 C ARG A 842 49.451 22.043 46.942 1.00 13.96 A C ANISOU 6751 C ARG A 842 1936 1360 2005 -412 -72 -239 A C ATOM 6752 O ARG A 842 48.677 21.063 46.809 1.00 14.97 A O ANISOU 6752 O ARG A 842 2034 1220 2434 -474 53 -322 A O ATOM 6753 CB ARG A 842 49.981 23.612 45.060 1.00 15.19 A C ANISOU 6753 CB ARG A 842 2205 1264 2300 -298 -106 -113 A C ATOM 6754 CG ARG A 842 50.961 24.088 44.000 1.00 16.68 A C ANISOU 6754 CG ARG A 842 2242 1276 2817 -97 216 -208 A C ATOM 6755 CD ARG A 842 50.595 25.399 43.376 1.00 20.18 A C ANISOU 6755 CD ARG A 842 3137 1195 3335 107 196 -145 A C ATOM 6756 NE ARG A 842 50.525 26.507 44.338 1.00 23.29 A N ANISOU 6756 NE ARG A 842 3506 1820 3523 -184 241 -511 A N ATOM 6757 CZ ARG A 842 51.591 27.174 44.813 1.00 20.99 A C ANISOU 6757 CZ ARG A 842 3884 1261 2826 -198 -18 -326 A C ATOM 6758 NH1 ARG A 842 52.821 26.889 44.406 1.00 23.23 A N ANISOU 6758 NH1 ARG A 842 3447 1816 3563 -404 -108 340 A N ATOM 6759 NH2 ARG A 842 51.420 28.182 45.652 1.00 27.82 A N ANISOU 6759 NH2 ARG A 842 6052 1453 3063 -718 474 -635 A N ATOM 6760 N ALA A 843 49.499 22.783 48.040 1.00 15.69 A N ANISOU 6760 N ALA A 843 2285 1352 2322 -483 7 -456 A N ATOM 6761 CA ALA A 843 48.603 22.551 49.139 1.00 15.06 A C ANISOU 6761 CA ALA A 843 2152 1330 2240 -198 64 -531 A C ATOM 6762 C ALA A 843 47.994 23.874 49.627 1.00 14.11 A C ANISOU 6762 C ALA A 843 2244 1032 2084 -245 0 -222 A C ATOM 6763 O ALA A 843 48.542 24.963 49.415 1.00 16.80 A O ANISOU 6763 O ALA A 843 2235 1093 3054 -290 63 -211 A O ATOM 6764 CB ALA A 843 49.333 21.861 50.261 1.00 16.28 A C ANISOU 6764 CB ALA A 843 2144 1435 2606 -127 255 -302 A C ATOM 6765 N THR A 844 46.850 23.747 50.289 1.00 14.45 A N ANISOU 6765 N THR A 844 2104 1266 2117 -127 -43 -511 A N ATOM 6766 CA THR A 844 46.267 24.806 51.073 1.00 15.52 A C ANISOU 6766 CA THR A 844 2341 1398 2157 -76 183 -491 A C ATOM 6767 C THR A 844 46.373 24.401 52.544 1.00 16.53 A C ANISOU 6767 C THR A 844 2145 1692 2441 -147 -2 -57 A C ATOM 6768 O THR A 844 45.806 23.375 52.939 1.00 16.25 A O ANISOU 6768 O THR A 844 2635 1368 2170 -205 -231 -123 A O ATOM 6769 CB THR A 844 44.805 25.083 50.702 1.00 20.25 A C ANISOU 6769 CB THR A 844 2698 2309 2685 269 -108 -284 A C ATOM 6770 CG2 THR A 844 44.200 26.214 51.508 1.00 22.44 A C ANISOU 6770 CG2 THR A 844 2562 2766 3198 832 271 -70 A C ATOM 6771 OG1 THR A 844 44.782 25.453 49.332 1.00 23.22 A O ANISOU 6771 OG1 THR A 844 2404 3468 2948 771 -335 250 A O ATOM 6772 N VAL A 845 47.164 25.164 53.300 1.00 16.25 A N ANISOU 6772 N VAL A 845 2533 1221 2418 -275 46 82 A N ATOM 6773 CA VAL A 845 47.321 24.948 54.703 1.00 15.93 A C ANISOU 6773 CA VAL A 845 2316 1386 2349 -173 -163 -151 A C ATOM 6774 C VAL A 845 46.320 25.849 55.421 1.00 17.00 A C ANISOU 6774 C VAL A 845 2759 1302 2397 -151 137 -23 A C ATOM 6775 O VAL A 845 46.339 27.074 55.237 1.00 18.93 A O ANISOU 6775 O VAL A 845 3000 1152 3038 -57 31 -74 A O ATOM 6776 CB VAL A 845 48.766 25.220 55.145 1.00 17.02 A C ANISOU 6776 CB VAL A 845 2366 1301 2798 -259 -205 -394 A C ATOM 6777 CG1 VAL A 845 48.933 25.032 56.645 1.00 18.13 A C ANISOU 6777 CG1 VAL A 845 2593 1694 2600 -260 -230 -501 A C ATOM 6778 CG2 VAL A 845 49.765 24.393 54.347 1.00 18.10 A C ANISOU 6778 CG2 VAL A 845 2574 1518 2783 -241 -107 -455 A C ATOM 6779 N VAL A 846 45.432 25.264 56.209 1.00 16.41 A N ANISOU 6779 N VAL A 846 2590 1355 2290 -91 225 -346 A N ATOM 6780 CA VAL A 846 44.452 25.999 57.007 1.00 16.84 A C ANISOU 6780 CA VAL A 846 2400 1671 2326 -14 117 -396 A C ATOM 6781 C VAL A 846 44.869 25.859 58.472 1.00 18.37 A C ANISOU 6781 C VAL A 846 2700 1654 2624 -177 -287 -308 A C ATOM 6782 O VAL A 846 44.755 24.765 59.048 1.00 18.68 A O ANISOU 6782 O VAL A 846 2891 1720 2485 299 85 -251 A O ATOM 6783 CB VAL A 846 43.034 25.432 56.779 1.00 19.33 A C ANISOU 6783 CB VAL A 846 2254 2182 2908 102 -22 -178 A C ATOM 6784 CG1 VAL A 846 41.999 26.194 57.591 1.00 21.84 A C ANISOU 6784 CG1 VAL A 846 1920 2623 3754 -26 -41 -641 A C ATOM 6785 CG2 VAL A 846 42.677 25.401 55.301 1.00 23.85 A C ANISOU 6785 CG2 VAL A 846 3081 2939 3040 -312 -5 -74 A C ATOM 6786 N LEU A 847 45.393 26.944 59.051 1.00 16.89 A N ANISOU 6786 N LEU A 847 2417 1620 2380 -688 287 -36 A N ATOM 6787 CA LEU A 847 45.893 26.853 60.414 1.00 19.34 A C ANISOU 6787 CA LEU A 847 2237 2215 2896 -385 -293 -401 A C ATOM 6788 C LEU A 847 44.714 26.897 61.368 1.00 19.30 A C ANISOU 6788 C LEU A 847 2778 1910 2644 -151 -83 -487 A C ATOM 6789 O LEU A 847 43.680 27.503 61.044 1.00 22.21 A O ANISOU 6789 O LEU A 847 3167 2209 3063 249 84 -399 A O ATOM 6790 CB LEU A 847 46.930 27.949 60.654 1.00 21.68 A C ANISOU 6790 CB LEU A 847 2477 2759 3001 -686 -417 -738 A C ATOM 6791 CG LEU A 847 48.165 27.814 59.755 1.00 22.10 A C ANISOU 6791 CG LEU A 847 2571 2942 2884 -541 -436 -525 A C ATOM 6792 CD1 LEU A 847 49.023 29.050 59.842 1.00 26.82 A C ANISOU 6792 CD1 LEU A 847 3457 3363 3370 -1072 -601 -690 A C ATOM 6793 CD2 LEU A 847 49.003 26.610 60.131 1.00 23.55 A C ANISOU 6793 CD2 LEU A 847 2647 3309 2991 -627 -726 -595 A C ATOM 6794 N PRO A 848 44.833 26.223 62.528 1.00 20.27 A N ANISOU 6794 N PRO A 848 2684 2580 2436 66 -309 -409 A N ATOM 6795 CA PRO A 848 43.724 26.073 63.450 1.00 23.38 A C ANISOU 6795 CA PRO A 848 3078 3289 2514 474 -26 -334 A C ATOM 6796 C PRO A 848 43.301 27.357 64.141 1.00 29.05 A C ANISOU 6796 C PRO A 848 4257 3601 3177 -301 195 -1220 A C ATOM 6797 O PRO A 848 44.092 28.305 64.243 1.00 31.68 A O ANISOU 6797 O PRO A 848 5700 3154 3180 -920 346 -1059 A O ATOM 6798 CB PRO A 848 44.182 25.038 64.491 1.00 27.36 A C ANISOU 6798 CB PRO A 848 3471 4108 2814 447 137 238 A C ATOM 6799 CG PRO A 848 45.662 24.910 64.311 1.00 24.36 A C ANISOU 6799 CG PRO A 848 3132 3762 2361 164 -332 150 A C ATOM 6800 CD PRO A 848 46.008 25.452 62.939 1.00 23.12 A C ANISOU 6800 CD PRO A 848 3193 3421 2169 142 -766 41 A C ATOM 6801 N GLY A 849 42.044 27.334 64.608 1.00 32.91 A N ANISOU 6801 N GLY A 849 4276 3581 4645 208 459 -1178 A N ATOM 6802 CA GLY A 849 41.481 28.377 65.427 1.00 41.25 A C ANISOU 6802 CA GLY A 849 5823 5039 4809 1804 252 -1554 A C ATOM 6803 C GLY A 849 40.565 29.297 64.639 1.00 37.16 A C ANISOU 6803 C GLY A 849 3990 6096 4033 1314 450 -1313 A C ATOM 6804 O GLY A 849 40.463 29.193 63.400 1.00 40.23 A O ANISOU 6804 O GLY A 849 5504 5764 4017 1748 -114 -858 A O ATOM 6805 N LYS A 850 39.902 30.191 65.386 1.00 43.93 A N ANISOU 6805 N LYS A 850 5670 5853 5166 1751 1507 -1132 A N ATOM 6806 CA LYS A 850 39.001 31.236 64.862 1.00 47.29 A C ANISOU 6806 CA LYS A 850 6940 6367 4662 1956 1522 -397 A C ATOM 6807 C LYS A 850 39.835 32.195 64.011 1.00 47.93 A C ANISOU 6807 C LYS A 850 6831 5505 5875 1232 1665 -826 A C ATOM 6808 O LYS A 850 40.854 32.697 64.483 1.00 51.38 A O ANISOU 6808 O LYS A 850 7542 4217 7763 684 1104 -1021 A O ATOM 6809 CB LYS A 850 38.306 32.003 66.000 1.00 47.43 A C ANISOU 6809 CB LYS A 850 7175 6012 4832 1462 1724 -718 A C ATOM 6810 N GLY A 851 39.416 32.384 62.752 1.00 54.18 A N ANISOU 6810 N GLY A 851 6881 6311 7393 2622 1003 1543 A N ATOM 6811 CA GLY A 851 40.112 33.242 61.788 1.00 58.24 A C ANISOU 6811 CA GLY A 851 7219 7010 7900 1412 1976 915 A C ATOM 6812 C GLY A 851 41.498 32.720 61.443 1.00 47.96 A C ANISOU 6812 C GLY A 851 7064 3273 7885 891 1280 497 A C ATOM 6813 O GLY A 851 42.378 33.468 61.005 1.00 48.75 A O ANISOU 6813 O GLY A 851 6632 4797 7093 140 1026 158 A O ATOM 6814 N GLY A 852 41.697 31.419 61.642 1.00 39.66 A N ANISOU 6814 N GLY A 852 6547 3004 5519 1474 937 -1037 A N ATOM 6815 CA GLY A 852 42.911 30.760 61.216 1.00 42.75 A C ANISOU 6815 CA GLY A 852 5786 4494 5962 1312 1063 475 A C ATOM 6816 C GLY A 852 43.242 31.096 59.767 1.00 34.40 A C ANISOU 6816 C GLY A 852 4329 2855 5884 -97 1181 -311 A C ATOM 6817 O GLY A 852 42.352 31.099 58.878 1.00 45.95 A O ANISOU 6817 O GLY A 852 4669 5566 7223 1035 143 2 A O ATOM 6818 N GLU A 853 44.518 31.423 59.549 1.00 32.42 A N ANISOU 6818 N GLU A 853 3863 2463 5990 104 1045 -658 A N ATOM 6819 CA GLU A 853 45.080 31.783 58.247 1.00 32.05 A C ANISOU 6819 CA GLU A 853 4594 2579 5003 -166 473 -919 A C ATOM 6820 C GLU A 853 45.033 30.572 57.321 1.00 26.57 A C ANISOU 6820 C GLU A 853 3629 2128 4338 -329 -537 -164 A C ATOM 6821 O GLU A 853 45.348 29.433 57.745 1.00 26.90 A O ANISOU 6821 O GLU A 853 4347 1855 4017 -582 -319 249 A O ATOM 6822 CB GLU A 853 46.542 32.237 58.399 1.00 36.16 A C ANISOU 6822 CB GLU A 853 4900 3222 5614 -1004 -181 -703 A C ATOM 6823 CG GLU A 853 46.693 33.560 59.135 1.00 56.28 A C ANISOU 6823 CG GLU A 853 9437 4229 7717 -549 -160 -2015 A C ATOM 6824 CD GLU A 853 46.278 34.795 58.348 1.00 68.00 A C ANISOU 6824 CD GLU A 853 11514 5793 8528 1403 976 -1007 A C ATOM 6825 OE1 GLU A 853 46.212 34.710 57.096 1.00 90.01 A O ANISOU 6825 OE1 GLU A 853 14643 10976 8580 -263 2369 -1384 A O ATOM 6826 OE2 GLU A 853 46.020 35.843 58.986 1.00 81.11 A O ANISOU 6826 OE2 GLU A 853 14433 6155 10230 2764 329 -1796 A O ATOM 6827 N LYS A 854 44.669 30.845 56.061 1.00 28.52 A N ANISOU 6827 N LYS A 854 3998 2975 3862 814 338 -181 A N ATOM 6828 CA LYS A 854 44.740 29.919 54.948 1.00 27.89 A C ANISOU 6828 CA LYS A 854 3945 2563 4086 240 751 -141 A C ATOM 6829 C LYS A 854 45.872 30.384 54.037 1.00 26.25 A C ANISOU 6829 C LYS A 854 4163 1762 4046 203 790 39 A C ATOM 6830 O LYS A 854 45.960 31.584 53.741 1.00 35.12 A O ANISOU 6830 O LYS A 854 6071 1956 5316 274 1399 706 A O ATOM 6831 CB LYS A 854 43.455 29.936 54.120 1.00 35.01 A C ANISOU 6831 CB LYS A 854 4371 3951 4977 107 -354 810 A C ATOM 6832 CG LYS A 854 42.244 29.275 54.768 1.00 40.47 A C ANISOU 6832 CG LYS A 854 4949 4432 5994 114 48 453 A C ATOM 6833 CD LYS A 854 41.082 29.067 53.818 1.00 46.53 A C ANISOU 6833 CD LYS A 854 6362 5168 6147 124 -1172 88 A C ATOM 6834 CE LYS A 854 41.501 28.754 52.392 1.00 51.62 A C ANISOU 6834 CE LYS A 854 6655 6026 6930 870 -547 -541 A C ATOM 6835 NZ LYS A 854 40.355 28.293 51.566 1.00 62.58 A N ANISOU 6835 NZ LYS A 854 8723 8678 6374 529 -2057 -178 A N ATOM 6836 N VAL A 855 46.725 29.455 53.633 1.00 21.75 A N ANISOU 6836 N VAL A 855 3713 1550 2999 1 486 -151 A N ATOM 6837 CA VAL A 855 47.975 29.719 52.946 1.00 22.67 A C ANISOU 6837 CA VAL A 855 4000 1925 2688 -266 597 -72 A C ATOM 6838 C VAL A 855 48.121 28.727 51.792 1.00 18.89 A C ANISOU 6838 C VAL A 855 2970 1294 2913 -135 -42 -60 A C ATOM 6839 O VAL A 855 48.063 27.523 52.026 1.00 20.05 A O ANISOU 6839 O VAL A 855 3324 1239 3052 -273 253 -24 A O ATOM 6840 CB VAL A 855 49.155 29.533 53.921 1.00 28.11 A C ANISOU 6840 CB VAL A 855 4442 2617 3622 -728 -196 -1149 A C ATOM 6841 CG1 VAL A 855 50.460 29.924 53.287 1.00 31.93 A C ANISOU 6841 CG1 VAL A 855 3840 4298 3994 -380 -764 -1058 A C ATOM 6842 CG2 VAL A 855 48.931 30.279 55.220 1.00 38.99 A C ANISOU 6842 CG2 VAL A 855 6248 5353 3213 -1189 -738 -1489 A C ATOM 6843 N ASP A 856 48.381 29.213 50.568 1.00 19.02 A N ANISOU 6843 N ASP A 856 3089 1096 3042 12 283 -256 A N ATOM 6844 CA ASP A 856 48.683 28.370 49.386 1.00 18.25 A C ANISOU 6844 CA ASP A 856 2490 1166 3276 -342 322 -406 A C ATOM 6845 C ASP A 856 50.197 28.151 49.403 1.00 16.54 A C ANISOU 6845 C ASP A 856 2334 1162 2786 -376 60 39 A C ATOM 6846 O ASP A 856 50.965 29.128 49.495 1.00 19.89 A O ANISOU 6846 O ASP A 856 2721 1474 3363 -612 -201 -256 A O ATOM 6847 CB ASP A 856 48.223 29.082 48.100 1.00 25.10 A C ANISOU 6847 CB ASP A 856 2917 2940 3679 132 -37 259 A C ATOM 6848 CG ASP A 856 48.476 28.403 46.746 1.00 37.19 A C ANISOU 6848 CG ASP A 856 5206 4331 4592 38 158 -496 A C ATOM 6849 OD1 ASP A 856 48.687 27.170 46.729 1.00 45.88 A O ANISOU 6849 OD1 ASP A 856 5977 4970 6484 833 717 1078 A O ATOM 6850 OD2 ASP A 856 48.437 29.123 45.669 1.00 53.22 A O ANISOU 6850 OD2 ASP A 856 9211 5753 5255 -620 250 326 A O ATOM 6851 N VAL A 857 50.644 26.910 49.247 1.00 15.33 A N ANISOU 6851 N VAL A 857 2426 1235 2162 -412 -60 -116 A N ATOM 6852 CA VAL A 857 52.045 26.610 49.204 1.00 16.60 A C ANISOU 6852 CA VAL A 857 2330 1605 2372 -558 58 -212 A C ATOM 6853 C VAL A 857 52.331 25.620 48.077 1.00 16.66 A C ANISOU 6853 C VAL A 857 2192 1477 2660 -680 -33 -310 A C ATOM 6854 O VAL A 857 51.460 24.811 47.757 1.00 18.71 A O ANISOU 6854 O VAL A 857 2285 1551 3274 -885 303 -529 A O ATOM 6855 CB VAL A 857 52.557 26.014 50.529 1.00 17.75 A C ANISOU 6855 CB VAL A 857 2243 1916 2583 -397 -77 -104 A C ATOM 6856 CG1 VAL A 857 52.433 26.959 51.671 1.00 23.20 A C ANISOU 6856 CG1 VAL A 857 3648 2326 2839 -427 -46 -388 A C ATOM 6857 CG2 VAL A 857 51.901 24.700 50.907 1.00 19.11 A C ANISOU 6857 CG2 VAL A 857 2963 1577 2720 -96 138 49 A C ATOM 6858 N GLY A 858 53.595 25.644 47.607 1.00 16.46 A N ANISOU 6858 N GLY A 858 2196 1016 3042 -397 -103 -600 A N ATOM 6859 CA GLY A 858 54.115 24.641 46.712 1.00 16.18 A C ANISOU 6859 CA GLY A 858 1929 1403 2815 -618 59 -656 A C ATOM 6860 C GLY A 858 54.938 23.605 47.464 1.00 17.00 A C ANISOU 6860 C GLY A 858 2173 1740 2546 -599 0 -380 A C ATOM 6861 O GLY A 858 54.848 23.466 48.701 1.00 17.72 A O ANISOU 6861 O GLY A 858 2832 1294 2605 -516 0 -350 A O ATOM 6862 N SER A 859 55.688 22.814 46.703 1.00 15.08 A N ANISOU 6862 N SER A 859 2164 1273 2293 -559 178 -18 A N ATOM 6863 CA SER A 859 56.416 21.683 47.285 1.00 14.53 A C ANISOU 6863 CA SER A 859 2033 1565 1920 -328 14 -226 A C ATOM 6864 C SER A 859 57.455 22.155 48.308 1.00 16.49 A C ANISOU 6864 C SER A 859 2164 1861 2241 -820 -52 -142 A C ATOM 6865 O SER A 859 57.907 23.334 48.301 1.00 17.54 A O ANISOU 6865 O SER A 859 2238 1703 2721 -775 76 -561 A O ATOM 6866 CB SER A 859 57.105 20.846 46.224 1.00 13.94 A C ANISOU 6866 CB SER A 859 1979 1403 1913 -479 21 -319 A C ATOM 6867 OG SER A 859 58.184 21.547 45.598 1.00 16.02 A O ANISOU 6867 OG SER A 859 2158 1362 2567 -661 183 -322 A O ATOM 6868 N GLY A 860 57.819 21.243 49.208 1.00 16.44 A N ANISOU 6868 N GLY A 860 2326 1368 2553 -604 -262 -326 A N ATOM 6869 CA GLY A 860 58.893 21.445 50.164 1.00 17.35 A C ANISOU 6869 CA GLY A 860 2456 1770 2367 -335 -353 -214 A C ATOM 6870 C GLY A 860 58.428 21.167 51.575 1.00 17.49 A C ANISOU 6870 C GLY A 860 2255 1877 2513 -551 -415 -53 A C ATOM 6871 O GLY A 860 57.373 20.580 51.782 1.00 20.56 A O ANISOU 6871 O GLY A 860 2584 2647 2580 -1228 -354 -534 A O ATOM 6872 N VAL A 861 59.247 21.577 52.539 1.00 20.26 A N ANISOU 6872 N VAL A 861 2344 2537 2813 -1145 -377 -393 A N ATOM 6873 CA VAL A 861 58.966 21.371 53.940 1.00 19.99 A C ANISOU 6873 CA VAL A 861 2608 2252 2733 -624 -306 -554 A C ATOM 6874 C VAL A 861 58.674 22.750 54.519 1.00 20.45 A C ANISOU 6874 C VAL A 861 2339 2275 3154 -1141 9 -940 A C ATOM 6875 O VAL A 861 59.517 23.663 54.437 1.00 27.52 A O ANISOU 6875 O VAL A 861 3015 3350 4092 -1982 319 -969 A O ATOM 6876 CB VAL A 861 60.136 20.693 54.678 1.00 22.17 A C ANISOU 6876 CB VAL A 861 2412 3270 2740 -617 -380 -586 A C ATOM 6877 CG1 VAL A 861 59.849 20.532 56.168 1.00 26.43 A C ANISOU 6877 CG1 VAL A 861 3122 4029 2890 -267 97 -565 A C ATOM 6878 CG2 VAL A 861 60.471 19.338 54.062 1.00 23.78 A C ANISOU 6878 CG2 VAL A 861 2801 3375 2856 -144 -189 -394 A C ATOM 6879 N HIS A 862 57.448 22.910 55.019 1.00 17.99 A N ANISOU 6879 N HIS A 862 2723 1752 2358 -612 29 -723 A N ATOM 6880 CA HIS A 862 56.957 24.160 55.528 1.00 18.34 A C ANISOU 6880 CA HIS A 862 3206 1363 2397 -602 70 -463 A C ATOM 6881 C HIS A 862 56.733 24.067 57.038 1.00 19.39 A C ANISOU 6881 C HIS A 862 3122 1893 2350 -794 190 -372 A C ATOM 6882 O HIS A 862 56.107 23.130 57.489 1.00 19.42 A O ANISOU 6882 O HIS A 862 3377 1721 2278 -1102 101 -583 A O ATOM 6883 CB HIS A 862 55.656 24.564 54.816 1.00 21.73 A C ANISOU 6883 CB HIS A 862 3417 2176 2662 -262 2 -266 A C ATOM 6884 CG HIS A 862 55.768 24.580 53.331 1.00 21.85 A C ANISOU 6884 CG HIS A 862 3989 1699 2614 -697 -129 -464 A C ATOM 6885 CD2 HIS A 862 55.489 23.629 52.415 1.00 22.13 A C ANISOU 6885 CD2 HIS A 862 3594 1996 2816 -461 -151 -661 A C ATOM 6886 ND1 HIS A 862 56.248 25.674 52.635 1.00 27.35 A N ANISOU 6886 ND1 HIS A 862 5208 2257 2924 -809 105 184 A N ATOM 6887 CE1 HIS A 862 56.249 25.391 51.342 1.00 31.00 A C ANISOU 6887 CE1 HIS A 862 6286 2362 3129 -1783 -212 -307 A C ATOM 6888 NE2 HIS A 862 55.788 24.137 51.184 1.00 22.49 A N ANISOU 6888 NE2 HIS A 862 3548 2115 2881 -989 -504 -549 A N ATOM 6889 N GLU A 863 57.190 25.051 57.783 1.00 20.05 A N ANISOU 6889 N GLU A 863 3284 1439 2895 -833 -287 -267 A N ATOM 6890 CA GLU A 863 57.074 25.078 59.241 1.00 18.55 A C ANISOU 6890 CA GLU A 863 2687 1491 2869 -233 -23 -301 A C ATOM 6891 C GLU A 863 56.179 26.263 59.619 1.00 15.89 A C ANISOU 6891 C GLU A 863 2419 1219 2399 -314 -541 -178 A C ATOM 6892 O GLU A 863 56.427 27.401 59.129 1.00 17.94 A O ANISOU 6892 O GLU A 863 2610 1323 2880 -492 -456 -123 A O ATOM 6893 CB GLU A 863 58.450 25.217 59.877 1.00 21.90 A C ANISOU 6893 CB GLU A 863 2509 2064 3746 -384 -705 25 A C ATOM 6894 CG GLU A 863 58.467 24.882 61.337 1.00 26.68 A C ANISOU 6894 CG GLU A 863 3444 2925 3767 -697 -617 -153 A C ATOM 6895 CD GLU A 863 59.870 24.716 61.864 1.00 31.10 A C ANISOU 6895 CD GLU A 863 2706 4667 4443 -701 -910 -62 A C ATOM 6896 OE1 GLU A 863 60.579 23.806 61.372 1.00 31.61 A O ANISOU 6896 OE1 GLU A 863 3238 4615 4154 -1398 -345 -325 A O ATOM 6897 OE2 GLU A 863 60.199 25.455 62.759 1.00 31.81 A O ANISOU 6897 OE2 GLU A 863 3681 3978 4427 -1078 -510 187 A O ATOM 6898 N TYR A 864 55.193 26.013 60.477 1.00 16.49 A N ANISOU 6898 N TYR A 864 2344 1493 2428 -264 -384 -384 A N ATOM 6899 CA TYR A 864 54.266 27.044 60.950 1.00 16.75 A C ANISOU 6899 CA TYR A 864 2510 1209 2646 -372 -386 -377 A C ATOM 6900 C TYR A 864 54.249 27.075 62.481 1.00 16.65 A C ANISOU 6900 C TYR A 864 2545 1170 2608 -658 -475 -68 A C ATOM 6901 O TYR A 864 54.103 26.048 63.128 1.00 17.39 A O ANISOU 6901 O TYR A 864 2972 1415 2218 -442 -286 -117 A O ATOM 6902 CB TYR A 864 52.856 26.800 60.403 1.00 18.21 A C ANISOU 6902 CB TYR A 864 2493 1517 2908 -547 -375 -242 A C ATOM 6903 CG TYR A 864 52.762 26.725 58.899 1.00 17.29 A C ANISOU 6903 CG TYR A 864 2395 1624 2550 -712 -778 -252 A C ATOM 6904 CD1 TYR A 864 52.942 25.536 58.213 1.00 18.69 A C ANISOU 6904 CD1 TYR A 864 2638 1464 3000 -1434 -557 -546 A C ATOM 6905 CD2 TYR A 864 52.522 27.869 58.158 1.00 17.78 A C ANISOU 6905 CD2 TYR A 864 2073 1628 3053 -603 -311 4 A C ATOM 6906 CE1 TYR A 864 52.875 25.498 56.832 1.00 19.47 A C ANISOU 6906 CE1 TYR A 864 2489 2174 2733 -897 -498 -629 A C ATOM 6907 CE2 TYR A 864 52.448 27.839 56.779 1.00 20.09 A C ANISOU 6907 CE2 TYR A 864 2321 2406 2906 -598 -586 -592 A C ATOM 6908 CZ TYR A 864 52.618 26.645 56.111 1.00 19.97 A C ANISOU 6908 CZ TYR A 864 2635 2005 2945 -815 -570 -539 A C ATOM 6909 OH TYR A 864 52.560 26.613 54.755 1.00 22.87 A O ANISOU 6909 OH TYR A 864 3337 2619 2733 -979 -646 -700 A O ATOM 6910 N HIS A 865 54.379 28.283 63.045 1.00 17.58 A N ANISOU 6910 N HIS A 865 2576 1583 2520 -520 -248 -512 A N ATOM 6911 CA HIS A 865 54.299 28.437 64.472 1.00 18.55 A C ANISOU 6911 CA HIS A 865 2749 1731 2565 -533 -232 -146 A C ATOM 6912 C HIS A 865 53.190 29.430 64.759 1.00 18.66 A C ANISOU 6912 C HIS A 865 2997 1538 2554 -389 -477 -319 A C ATOM 6913 O HIS A 865 53.316 30.585 64.362 1.00 24.08 A O ANISOU 6913 O HIS A 865 4347 1628 3171 -537 -127 -79 A O ATOM 6914 CB HIS A 865 55.644 28.870 65.072 1.00 20.48 A C ANISOU 6914 CB HIS A 865 3078 1741 2962 -446 -818 -435 A C ATOM 6915 CG HIS A 865 56.721 27.873 64.856 1.00 21.36 A C ANISOU 6915 CG HIS A 865 2593 2618 2902 -545 -484 -501 A C ATOM 6916 CD2 HIS A 865 57.602 27.726 63.853 1.00 21.83 A C ANISOU 6916 CD2 HIS A 865 2915 2432 2948 -1168 -212 -105 A C ATOM 6917 ND1 HIS A 865 56.886 26.769 65.680 1.00 25.12 A N ANISOU 6917 ND1 HIS A 865 2814 2924 3804 -330 -750 -318 A N ATOM 6918 CE1 HIS A 865 57.866 26.020 65.199 1.00 25.90 A C ANISOU 6918 CE1 HIS A 865 2516 3917 3404 -121 -531 267 A C ATOM 6919 NE2 HIS A 865 58.321 26.586 64.084 1.00 25.82 A N ANISOU 6919 NE2 HIS A 865 2811 3342 3655 -774 -673 373 A N ATOM 6920 N VAL A 866 52.101 28.961 65.364 1.00 19.45 A N ANISOU 6920 N VAL A 866 2964 1697 2730 -277 -132 -575 A N ATOM 6921 CA VAL A 866 50.942 29.780 65.626 1.00 23.05 A C ANISOU 6921 CA VAL A 866 2975 1881 3901 -124 -78 -145 A C ATOM 6922 C VAL A 866 50.837 29.972 67.124 1.00 23.73 A C ANISOU 6922 C VAL A 866 3149 1783 4084 -107 69 -620 A C ATOM 6923 O VAL A 866 50.552 29.036 67.868 1.00 23.63 A O ANISOU 6923 O VAL A 866 3572 2054 3350 -365 -182 -908 A O ATOM 6924 CB VAL A 866 49.627 29.225 65.052 1.00 27.81 A C ANISOU 6924 CB VAL A 866 3078 3429 4058 -182 -155 -232 A C ATOM 6925 CG1 VAL A 866 48.531 30.271 65.170 1.00 34.23 A C ANISOU 6925 CG1 VAL A 866 4017 4138 4850 605 -491 658 A C ATOM 6926 CG2 VAL A 866 49.797 28.786 63.612 1.00 28.39 A C ANISOU 6926 CG2 VAL A 866 3248 3770 3768 -744 -891 -52 A C ATOM 6927 N ARG A 867 51.037 31.220 67.554 1.00 29.21 A N ANISOU 6927 N ARG A 867 4277 1740 5079 169 -299 -811 A N ATOM 6928 CA AARG A 867 51.088 31.535 68.962 0.50 31.22 A C ANISOU 6928 CA AARG A 867 3859 2758 5244 -95 -250 -1222 A C ATOM 6929 CA BARG A 867 51.091 31.529 68.945 0.50 30.82 A C ANISOU 6929 CA BARG A 867 3751 2668 5288 -229 -466 -1309 A C ATOM 6930 C ARG A 867 49.672 31.889 69.413 1.00 33.11 A C ANISOU 6930 C ARG A 867 3830 3642 5106 121 -404 -1423 A C ATOM 6931 O ARG A 867 48.939 32.523 68.681 1.00 37.87 A O ANISOU 6931 O ARG A 867 4474 3931 5982 632 -756 -1731 A O ATOM 6932 CB AARG A 867 52.025 32.712 69.261 0.50 31.17 A C ANISOU 6932 CB AARG A 867 3333 2665 5845 -46 108 -985 A C ATOM 6933 CB BARG A 867 52.160 32.614 69.108 0.50 33.70 A C ANISOU 6933 CB BARG A 867 4147 2620 6037 -428 -574 -1237 A C ATOM 6934 CG AARG A 867 53.513 32.415 69.118 0.50 31.95 A C ANISOU 6934 CG AARG A 867 3381 3542 5217 88 788 -203 A C ATOM 6935 CG BARG A 867 53.502 32.198 68.512 0.50 33.40 A C ANISOU 6935 CG BARG A 867 3488 3397 5803 -711 -894 -388 A C ATOM 6936 CD AARG A 867 54.154 31.645 70.260 0.50 31.63 A C ANISOU 6936 CD AARG A 867 3791 3873 4352 -351 772 -381 A C ATOM 6937 CD BARG A 867 54.438 33.344 68.174 0.50 33.32 A C ANISOU 6937 CD BARG A 867 4142 3166 5351 -666 -1070 139 A C ATOM 6938 NE AARG A 867 55.605 31.623 70.103 0.50 31.39 A N ANISOU 6938 NE AARG A 867 3737 3234 4955 -20 209 -298 A N ATOM 6939 NE BARG A 867 54.162 33.983 66.895 0.50 28.45 A N ANISOU 6939 NE BARG A 867 3885 2997 3925 -844 -1175 -1144 A N ATOM 6940 CZ AARG A 867 56.477 31.382 71.072 0.50 32.71 A C ANISOU 6940 CZ AARG A 867 4964 3010 4452 -456 119 785 A C ATOM 6941 CZ BARG A 867 54.704 33.669 65.714 0.50 27.72 A C ANISOU 6941 CZ BARG A 867 3702 3177 3650 -35 -696 345 A C ATOM 6942 NH1AARG A 867 56.056 30.979 72.262 0.50 32.61 A N ANISOU 6942 NH1AARG A 867 5855 2868 3666 -843 157 -434 A N ATOM 6943 NH1BARG A 867 55.400 32.553 65.521 0.50 24.97 A N ANISOU 6943 NH1BARG A 867 5709 765 3010 -955 -828 582 A N ATOM 6944 NH2AARG A 867 57.773 31.540 70.842 0.50 31.66 A N ANISOU 6944 NH2AARG A 867 5091 2753 4185 743 680 2510 A N ATOM 6945 NH2BARG A 867 54.524 34.509 64.716 0.50 21.27 A N ANISOU 6945 NH2BARG A 867 2706 2002 3373 -921 -903 5 A N ATOM 6946 N CYS A 868 49.301 31.438 70.612 1.00 35.13 A N ANISOU 6946 N CYS A 868 4619 3177 5549 -1268 7 -2073 A N ATOM 6947 CA CYS A 868 48.051 31.861 71.290 1.00 43.04 A C ANISOU 6947 CA CYS A 868 4532 5205 6616 -1063 194 -2328 A C ATOM 6948 C CYS A 868 46.815 31.533 70.433 1.00 40.46 A C ANISOU 6948 C CYS A 868 4125 4658 6587 -56 -38 -1991 A C ATOM 6949 O CYS A 868 45.963 32.394 70.158 1.00 43.91 A O ANISOU 6949 O CYS A 868 4945 4954 6784 464 303 -1432 A O ATOM 6950 CB CYS A 868 48.085 33.347 71.635 1.00 52.12 A C ANISOU 6950 CB CYS A 868 6297 5406 8101 -2425 119 -2761 A C ATOM 6951 SG CYS A 868 49.560 33.847 72.572 1.00 54.24 A S ANISOU 6951 SG CYS A 868 6139 6651 7816 -598 199 -3420 A S ATOM 6952 N VAL A 869 46.728 30.269 70.021 1.00 41.12 A N ANISOU 6952 N VAL A 869 4538 5048 6039 -522 359 -2561 A N ATOM 6953 CA VAL A 869 45.577 29.756 69.264 1.00 41.00 A C ANISOU 6953 CA VAL A 869 4149 5346 6082 -225 -130 -2104 A C ATOM 6954 C VAL A 869 44.400 29.587 70.217 1.00 42.58 A C ANISOU 6954 C VAL A 869 5197 5980 5000 962 250 -1721 A C ATOM 6955 O VAL A 869 44.552 28.924 71.242 1.00 42.76 A O ANISOU 6955 O VAL A 869 5739 6656 3849 -100 -68 -1941 A O ATOM 6956 CB VAL A 869 45.857 28.389 68.614 1.00 40.00 A C ANISOU 6956 CB VAL A 869 4410 5745 5041 -724 438 -2378 A C ATOM 6957 CG1 VAL A 869 44.599 27.816 67.964 1.00 43.47 A C ANISOU 6957 CG1 VAL A 869 4443 6519 5552 -467 -340 -1515 A C ATOM 6958 CG2 VAL A 869 46.979 28.460 67.604 1.00 41.11 A C ANISOU 6958 CG2 VAL A 869 2752 5987 6878 374 436 -2010 A C ATOM 6959 N LYS A 870 43.227 30.072 69.799 1.00 45.94 A N ANISOU 6959 N LYS A 870 5827 4885 6741 1408 -161 -650 A N ATOM 6960 CA LYS A 870 42.006 30.051 70.606 1.00 56.43 A C ANISOU 6960 CA LYS A 870 5771 7993 7676 752 32 -1449 A C ATOM 6961 C LYS A 870 40.985 29.096 69.965 1.00 56.40 A C ANISOU 6961 C LYS A 870 5720 10694 5013 0 1087 -2568 A C ATOM 6962 O LYS A 870 40.713 29.134 68.745 1.00 54.16 A O ANISOU 6962 O LYS A 870 4660 10556 5363 -1532 194 -4036 A O ATOM 6963 CB LYS A 870 41.454 31.475 70.762 1.00 65.36 A C ANISOU 6963 CB LYS A 870 5108 9110 10613 2103 1077 -1366 A C TER END If you find results from this site helpful for your research, please cite one of our papers:
elNémo
is maintained by Yves-Henri Sanejouand. |