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*** HYDROLASE/IMMUNE SYSTEM 30-NOV-15 5F1K ***elNémo ID: 2608152137101473911Job options:ID = 2608152137101473911 JOBID = HYDROLASE/IMMUNE SYSTEM 30-NOV-15 5F1K USERID = unknown PRIVAT = 0 NMODES = 25 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HYDROLASE/IMMUNE SYSTEM 30-NOV-15 5F1K TITLE HUMAN CD38 IN COMPLEX WITH NANOBODY MU1053 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADP-RIBOSYL CYCLASE/CYCLIC ADP-RIBOSE HYDROLASE 1; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: ECTODOMAIN, UNP RESIDUES 45-300; COMPND 5 SYNONYM: CD38; COMPND 6 EC: 3.2.2.6; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NANOBODY MU1053; COMPND 11 CHAIN: C, D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CD38; SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: X33; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 14 ORGANISM_TAXID: 9844; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHEN2 KEYWDS CD38, ADP-RIBOSYL CYCLASE, CYCLIC ADP-RIBOSE, X-CRYSTALLOGRAPHY, KEYWDS 2 CALCIUM SIGNALING, NANOBODY, MU1053, HYDROLASE-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR H.ZHANG,Q.HAO REVDAT 3 30-OCT-24 5F1K 1 REMARK REVDAT 2 08-NOV-23 5F1K 1 REMARK REVDAT 1 15-JUN-16 5F1K 0 JRNL AUTH T.LI,S.QI,M.UNGER,Y.N.HOU,Q.W.DENG,J.LIU,C.M.LAM,X.W.WANG, JRNL AUTH 2 D.XIN,P.ZHANG,F.KOCH-NOLTE,Q.HAO,H.ZHANG,H.C.LEE,Y.J.ZHAO JRNL TITL IMMUNO-TARGETING THE MULTIFUNCTIONAL CD38 USING NANOBODY JRNL REF SCI REP V. 6 27055 2016 JRNL REFN ESSN 2045-2322 JRNL PMID 27251573 JRNL DOI 10.1038/SREP27055 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0135 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.8 REMARK 3 NUMBER OF REFLECTIONS : 42953 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.231 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2259 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1796 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.41 REMARK 3 BIN R VALUE (WORKING SET) : 0.2230 REMARK 3 BIN FREE R VALUE SET COUNT : 98 REMARK 3 BIN FREE R VALUE : 0.2640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5755 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 323 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.65 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.59000 REMARK 3 B22 (A**2) : 0.37000 REMARK 3 B33 (A**2) : 2.22000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.213 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.552 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5922 ; 0.010 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 5496 ; 0.004 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8031 ; 1.383 ; 1.935 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12657 ; 1.181 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 725 ; 5.765 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 278 ;36.191 ;23.741 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 998 ;14.514 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;20.424 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 865 ; 0.082 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6707 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 1419 ; 0.003 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2906 ; 0.507 ; 0.910 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2905 ; 0.507 ; 0.910 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3623 ; 0.658 ; 1.363 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 11418 ; 1.459 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 128 ;30.549 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 11462 ; 3.163 ; 5.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NCS TYPE: LOCAL REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2 REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT REMARK 3 1 A 49 290 B 49 290 28040 0.100 0.050 REMARK 3 2 C 2 124 D 2 124 13206 0.100 0.050 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 25 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 49 A 112 REMARK 3 ORIGIN FOR THE GROUP (A): 61.3840 35.0060 94.5960 REMARK 3 T TENSOR REMARK 3 T11: 0.2824 T22: 0.1620 REMARK 3 T33: 0.3051 T12: 0.0433 REMARK 3 T13: 0.0550 T23: -0.0623 REMARK 3 L TENSOR REMARK 3 L11: 2.3901 L22: 4.6424 REMARK 3 L33: 4.5939 L12: -1.4038 REMARK 3 L13: -1.0861 L23: 3.0267 REMARK 3 S TENSOR REMARK 3 S11: -0.1011 S12: -0.0308 S13: 0.5366 REMARK 3 S21: -0.3099 S22: 0.2572 S23: -0.1770 REMARK 3 S31: -0.5070 S32: -0.0971 S33: -0.1562 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 113 A 160 REMARK 3 ORIGIN FOR THE GROUP (A): 75.1540 26.5270 98.2220 REMARK 3 T TENSOR REMARK 3 T11: 0.3545 T22: 0.1521 REMARK 3 T33: 0.3297 T12: 0.0272 REMARK 3 T13: 0.0259 T23: -0.0934 REMARK 3 L TENSOR REMARK 3 L11: 5.6919 L22: 1.2287 REMARK 3 L33: 1.0490 L12: -2.4999 REMARK 3 L13: -0.2378 L23: 0.4502 REMARK 3 S TENSOR REMARK 3 S11: -0.0299 S12: -0.1823 S13: 0.4546 REMARK 3 S21: 0.0745 S22: 0.0962 S23: -0.2340 REMARK 3 S31: -0.0036 S32: -0.0315 S33: -0.0664 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 161 A 179 REMARK 3 ORIGIN FOR THE GROUP (A): 58.8540 45.6370 106.3190 REMARK 3 T TENSOR REMARK 3 T11: 0.5409 T22: 0.2657 REMARK 3 T33: 0.9486 T12: 0.2195 REMARK 3 T13: -0.0230 T23: -0.2711 REMARK 3 L TENSOR REMARK 3 L11: 9.6443 L22: 8.2096 REMARK 3 L33: 11.8289 L12: 4.3134 REMARK 3 L13: -6.8235 L23: -6.0068 REMARK 3 S TENSOR REMARK 3 S11: -0.2662 S12: -0.6840 S13: 2.2802 REMARK 3 S21: 0.1900 S22: 0.4675 S23: -0.0266 REMARK 3 S31: -0.4452 S32: 0.1195 S33: -0.2014 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 180 A 256 REMARK 3 ORIGIN FOR THE GROUP (A): 74.3340 23.5540 110.3770 REMARK 3 T TENSOR REMARK 3 T11: 0.4137 T22: 0.3198 REMARK 3 T33: 0.2653 T12: 0.1118 REMARK 3 T13: 0.0182 T23: -0.2120 REMARK 3 L TENSOR REMARK 3 L11: 2.2039 L22: 3.4125 REMARK 3 L33: 1.3799 L12: -1.7644 REMARK 3 L13: -0.2937 L23: -0.9359 REMARK 3 S TENSOR REMARK 3 S11: -0.3034 S12: -0.6719 S13: 0.2668 REMARK 3 S21: 0.6434 S22: 0.3644 S23: 0.0359 REMARK 3 S31: -0.1349 S32: 0.0511 S33: -0.0611 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 257 A 296 REMARK 3 ORIGIN FOR THE GROUP (A): 86.5670 18.3110 109.2580 REMARK 3 T TENSOR REMARK 3 T11: 0.4611 T22: 0.2400 REMARK 3 T33: 0.3456 T12: 0.1121 REMARK 3 T13: -0.1198 T23: -0.1560 REMARK 3 L TENSOR REMARK 3 L11: 5.2227 L22: 3.6528 REMARK 3 L33: 3.4066 L12: 1.4427 REMARK 3 L13: -0.8379 L23: -1.7136 REMARK 3 S TENSOR REMARK 3 S11: -0.2401 S12: -0.6870 S13: -0.1400 REMARK 3 S21: 0.6221 S22: -0.1045 S23: -0.6289 REMARK 3 S31: -0.0632 S32: 0.3361 S33: 0.3447 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 49 B 116 REMARK 3 ORIGIN FOR THE GROUP (A): 55.5990 1.4970 88.5250 REMARK 3 T TENSOR REMARK 3 T11: 0.2733 T22: 0.1823 REMARK 3 T33: 0.2013 T12: -0.0168 REMARK 3 T13: 0.0479 T23: 0.1178 REMARK 3 L TENSOR REMARK 3 L11: 3.5367 L22: 3.8691 REMARK 3 L33: 2.7452 L12: 1.2102 REMARK 3 L13: 1.5723 L23: 1.3394 REMARK 3 S TENSOR REMARK 3 S11: 0.1640 S12: -0.3430 S13: -0.1019 REMARK 3 S21: 0.2119 S22: 0.1701 S23: 0.0407 REMARK 3 S31: 0.2799 S32: -0.1587 S33: -0.3342 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 117 B 159 REMARK 3 ORIGIN FOR THE GROUP (A): 69.3160 4.8530 79.2040 REMARK 3 T TENSOR REMARK 3 T11: 0.3167 T22: 0.2047 REMARK 3 T33: 0.2190 T12: 0.0023 REMARK 3 T13: 0.0440 T23: 0.0490 REMARK 3 L TENSOR REMARK 3 L11: 4.0548 L22: 2.5240 REMARK 3 L33: 2.5087 L12: 2.6885 REMARK 3 L13: -1.2788 L23: -2.0824 REMARK 3 S TENSOR REMARK 3 S11: 0.0917 S12: 0.0970 S13: -0.1222 REMARK 3 S21: -0.0573 S22: -0.0346 S23: -0.0237 REMARK 3 S31: 0.0707 S32: 0.1974 S33: -0.0571 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 160 B 176 REMARK 3 ORIGIN FOR THE GROUP (A): 45.6680 -8.1470 81.5040 REMARK 3 T TENSOR REMARK 3 T11: 0.3775 T22: 0.2910 REMARK 3 T33: 0.4792 T12: -0.0933 REMARK 3 T13: -0.0915 T23: 0.1625 REMARK 3 L TENSOR REMARK 3 L11: 3.6795 L22: 4.4158 REMARK 3 L33: 9.0196 L12: -3.8486 REMARK 3 L13: -1.0140 L23: 2.1610 REMARK 3 S TENSOR REMARK 3 S11: 0.1334 S12: 0.0192 S13: -0.6673 REMARK 3 S21: 0.1001 S22: 0.0027 S23: 0.5948 REMARK 3 S31: 0.2482 S32: -0.6620 S33: -0.1361 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 177 B 195 REMARK 3 ORIGIN FOR THE GROUP (A): 52.5800 3.1340 75.2940 REMARK 3 T TENSOR REMARK 3 T11: 0.2994 T22: 0.1801 REMARK 3 T33: 0.3562 T12: 0.0265 REMARK 3 T13: -0.0045 T23: 0.1293 REMARK 3 L TENSOR REMARK 3 L11: 11.2056 L22: 9.4619 REMARK 3 L33: 1.8786 L12: 8.1068 REMARK 3 L13: 2.5435 L23: 0.5614 REMARK 3 S TENSOR REMARK 3 S11: 0.0497 S12: 0.2946 S13: 0.3594 REMARK 3 S21: -0.3636 S22: 0.1132 S23: 0.6353 REMARK 3 S31: 0.0527 S32: 0.0380 S33: -0.1629 REMARK 3 REMARK 3 TLS GROUP : 10 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 196 B 291 REMARK 3 ORIGIN FOR THE GROUP (A): 70.6340 10.7720 65.5320 REMARK 3 T TENSOR REMARK 3 T11: 0.4399 T22: 0.2286 REMARK 3 T33: 0.0601 T12: -0.0243 REMARK 3 T13: 0.0158 T23: 0.0432 REMARK 3 L TENSOR REMARK 3 L11: 4.1620 L22: 6.4119 REMARK 3 L33: 2.0431 L12: -0.6304 REMARK 3 L13: -0.0926 L23: -1.0559 REMARK 3 S TENSOR REMARK 3 S11: 0.0934 S12: 0.4520 S13: -0.1341 REMARK 3 S21: -1.1039 S22: -0.0512 S23: 0.1480 REMARK 3 S31: 0.3897 S32: 0.1196 S33: -0.0421 REMARK 3 REMARK 3 TLS GROUP : 11 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 2 C 15 REMARK 3 ORIGIN FOR THE GROUP (A): 89.3630 -11.2130 103.4970 REMARK 3 T TENSOR REMARK 3 T11: 0.3634 T22: 0.1550 REMARK 3 T33: 0.7596 T12: -0.0058 REMARK 3 T13: -0.2416 T23: 0.0966 REMARK 3 L TENSOR REMARK 3 L11: 4.1269 L22: 5.3826 REMARK 3 L33: 6.4380 L12: -4.0160 REMARK 3 L13: 3.1011 L23: -0.5999 REMARK 3 S TENSOR REMARK 3 S11: 0.1458 S12: 0.0355 S13: 0.4240 REMARK 3 S21: 0.1764 S22: 0.1004 S23: -0.9106 REMARK 3 S31: 0.4839 S32: 0.2941 S33: -0.2462 REMARK 3 REMARK 3 TLS GROUP : 12 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 16 C 30 REMARK 3 ORIGIN FOR THE GROUP (A): 93.5910 -1.7470 103.4820 REMARK 3 T TENSOR REMARK 3 T11: 0.3666 T22: 0.5287 REMARK 3 T33: 0.7182 T12: 0.0141 REMARK 3 T13: -0.2085 T23: -0.2510 REMARK 3 L TENSOR REMARK 3 L11: 12.9107 L22: 17.7841 REMARK 3 L33: 1.8218 L12: 6.9859 REMARK 3 L13: -2.3800 L23: -5.4747 REMARK 3 S TENSOR REMARK 3 S11: -0.1239 S12: -0.4856 S13: -0.2793 REMARK 3 S21: 0.2339 S22: -0.0724 S23: -1.4419 REMARK 3 S31: -0.0374 S32: 0.2444 S33: 0.1963 REMARK 3 REMARK 3 TLS GROUP : 13 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 31 C 39 REMARK 3 ORIGIN FOR THE GROUP (A): 85.6760 0.2170 99.0180 REMARK 3 T TENSOR REMARK 3 T11: 0.2804 T22: 0.1684 REMARK 3 T33: 0.2293 T12: 0.0387 REMARK 3 T13: -0.0292 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 7.3905 L22: 6.5331 REMARK 3 L33: 1.1274 L12: 2.6495 REMARK 3 L13: 0.4427 L23: -0.3183 REMARK 3 S TENSOR REMARK 3 S11: -0.0447 S12: -0.2969 S13: 0.2410 REMARK 3 S21: -0.2665 S22: 0.1483 S23: -0.1940 REMARK 3 S31: 0.0773 S32: -0.1328 S33: -0.1037 REMARK 3 REMARK 3 TLS GROUP : 14 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 40 C 47 REMARK 3 ORIGIN FOR THE GROUP (A): 76.9140 -7.9450 94.6740 REMARK 3 T TENSOR REMARK 3 T11: 0.4502 T22: 0.7239 REMARK 3 T33: 0.4566 T12: 0.1994 REMARK 3 T13: -0.1817 T23: -0.2099 REMARK 3 L TENSOR REMARK 3 L11: 7.7822 L22: 65.6180 REMARK 3 L33: 29.8292 L12: 19.2126 REMARK 3 L13: 13.5274 L23: 31.2731 REMARK 3 S TENSOR REMARK 3 S11: 0.0405 S12: 0.0234 S13: -0.2426 REMARK 3 S21: -2.4142 S22: -0.4862 S23: 0.5530 REMARK 3 S31: -0.0832 S32: -1.7723 S33: 0.4457 REMARK 3 REMARK 3 TLS GROUP : 15 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 48 C 72 REMARK 3 ORIGIN FOR THE GROUP (A): 81.5110 2.4360 107.0910 REMARK 3 T TENSOR REMARK 3 T11: 0.3443 T22: 0.2343 REMARK 3 T33: 0.1388 T12: 0.0665 REMARK 3 T13: -0.0506 T23: -0.0107 REMARK 3 L TENSOR REMARK 3 L11: 3.4199 L22: 7.4105 REMARK 3 L33: 2.1008 L12: 1.6352 REMARK 3 L13: 0.3504 L23: -0.1026 REMARK 3 S TENSOR REMARK 3 S11: -0.0254 S12: -0.5414 S13: 0.3047 REMARK 3 S21: 0.7617 S22: 0.1785 S23: 0.1178 REMARK 3 S31: 0.0387 S32: -0.0984 S33: -0.1532 REMARK 3 REMARK 3 TLS GROUP : 16 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 73 C 89 REMARK 3 ORIGIN FOR THE GROUP (A): 86.8970 -4.9730 108.5790 REMARK 3 T TENSOR REMARK 3 T11: 0.3649 T22: 0.2684 REMARK 3 T33: 0.2371 T12: 0.0706 REMARK 3 T13: -0.0740 T23: 0.0446 REMARK 3 L TENSOR REMARK 3 L11: 4.3423 L22: 7.2461 REMARK 3 L33: 2.2938 L12: 1.2446 REMARK 3 L13: -0.3796 L23: -1.2742 REMARK 3 S TENSOR REMARK 3 S11: -0.0364 S12: -0.5314 S13: 0.0973 REMARK 3 S21: 0.7908 S22: 0.1592 S23: -0.2690 REMARK 3 S31: 0.0988 S32: -0.0112 S33: -0.1229 REMARK 3 REMARK 3 TLS GROUP : 17 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 90 C 109 REMARK 3 ORIGIN FOR THE GROUP (A): 82.6960 -0.0320 97.6460 REMARK 3 T TENSOR REMARK 3 T11: 0.3095 T22: 0.1354 REMARK 3 T33: 0.2383 T12: 0.0245 REMARK 3 T13: -0.0579 T23: -0.0418 REMARK 3 L TENSOR REMARK 3 L11: 3.5425 L22: 10.2796 REMARK 3 L33: 0.2736 L12: 0.7804 REMARK 3 L13: -0.4650 L23: -1.5383 REMARK 3 S TENSOR REMARK 3 S11: 0.0908 S12: -0.1638 S13: -0.1054 REMARK 3 S21: -0.0941 S22: -0.0847 S23: -0.1695 REMARK 3 S31: 0.0265 S32: 0.0483 S33: -0.0061 REMARK 3 REMARK 3 TLS GROUP : 18 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : C 110 C 124 REMARK 3 ORIGIN FOR THE GROUP (A): 85.0050 -8.0330 97.9000 REMARK 3 T TENSOR REMARK 3 T11: 0.2062 T22: 0.1967 REMARK 3 T33: 0.2951 T12: 0.0438 REMARK 3 T13: -0.0680 T23: 0.0415 REMARK 3 L TENSOR REMARK 3 L11: 2.6025 L22: 15.4218 REMARK 3 L33: 4.9365 L12: 1.5230 REMARK 3 L13: 0.7150 L23: -2.7400 REMARK 3 S TENSOR REMARK 3 S11: 0.1347 S12: -0.0525 S13: -0.3359 REMARK 3 S21: -0.6318 S22: 0.1104 S23: -0.0395 REMARK 3 S31: 0.4267 S32: 0.1597 S33: -0.2450 REMARK 3 REMARK 3 TLS GROUP : 19 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 2 D 6 REMARK 3 ORIGIN FOR THE GROUP (A): 96.1120 28.0940 73.3300 REMARK 3 T TENSOR REMARK 3 T11: 0.2538 T22: 0.7665 REMARK 3 T33: 1.1804 T12: 0.0676 REMARK 3 T13: -0.1030 T23: 0.3747 REMARK 3 L TENSOR REMARK 3 L11: 3.1066 L22: 17.1175 REMARK 3 L33: 17.8987 L12: -2.9941 REMARK 3 L13: -2.7674 L23: 17.4868 REMARK 3 S TENSOR REMARK 3 S11: -0.4805 S12: -1.1938 S13: 0.3934 REMARK 3 S21: 0.6436 S22: 1.2313 S23: -0.7881 REMARK 3 S31: 0.6075 S32: 1.1647 S33: -0.7507 REMARK 3 REMARK 3 TLS GROUP : 20 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 7 D 29 REMARK 3 ORIGIN FOR THE GROUP (A): 89.8870 34.2520 66.6330 REMARK 3 T TENSOR REMARK 3 T11: 0.3414 T22: 0.4468 REMARK 3 T33: 0.5761 T12: 0.0746 REMARK 3 T13: 0.2108 T23: 0.3201 REMARK 3 L TENSOR REMARK 3 L11: 7.4798 L22: 19.3433 REMARK 3 L33: 0.3897 L12: -8.9434 REMARK 3 L13: 1.3241 L23: -1.3803 REMARK 3 S TENSOR REMARK 3 S11: -0.3028 S12: -0.7197 S13: 0.0061 REMARK 3 S21: 0.1597 S22: 0.3628 S23: -1.2451 REMARK 3 S31: -0.0208 S32: -0.0256 S33: -0.0600 REMARK 3 REMARK 3 TLS GROUP : 21 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 30 D 43 REMARK 3 ORIGIN FOR THE GROUP (A): 85.4710 29.3380 75.4640 REMARK 3 T TENSOR REMARK 3 T11: 0.2479 T22: 0.3740 REMARK 3 T33: 0.3345 T12: -0.0975 REMARK 3 T13: 0.0080 T23: 0.2265 REMARK 3 L TENSOR REMARK 3 L11: 2.7278 L22: 18.9624 REMARK 3 L33: 2.7180 L12: 0.7686 REMARK 3 L13: 1.0921 L23: -0.1312 REMARK 3 S TENSOR REMARK 3 S11: 0.1913 S12: -0.0565 S13: 0.1567 REMARK 3 S21: 0.4741 S22: -0.7601 S23: -1.4475 REMARK 3 S31: -0.1968 S32: 0.2553 S33: 0.5688 REMARK 3 REMARK 3 TLS GROUP : 22 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 44 D 72 REMARK 3 ORIGIN FOR THE GROUP (A): 78.8690 28.1990 70.4000 REMARK 3 T TENSOR REMARK 3 T11: 0.2398 T22: 0.3073 REMARK 3 T33: 0.1855 T12: -0.0458 REMARK 3 T13: 0.1039 T23: 0.1603 REMARK 3 L TENSOR REMARK 3 L11: 2.8103 L22: 12.5468 REMARK 3 L33: 2.9071 L12: -0.2812 REMARK 3 L13: -0.6083 L23: -0.1024 REMARK 3 S TENSOR REMARK 3 S11: 0.1105 S12: 0.0496 S13: 0.1212 REMARK 3 S21: 0.0614 S22: -0.3701 S23: -0.1485 REMARK 3 S31: 0.0052 S32: 0.1961 S33: 0.2595 REMARK 3 REMARK 3 TLS GROUP : 23 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 73 D 95 REMARK 3 ORIGIN FOR THE GROUP (A): 84.9240 34.4240 67.1680 REMARK 3 T TENSOR REMARK 3 T11: 0.2716 T22: 0.3893 REMARK 3 T33: 0.3184 T12: -0.0154 REMARK 3 T13: 0.1268 T23: 0.2537 REMARK 3 L TENSOR REMARK 3 L11: 5.2033 L22: 10.8471 REMARK 3 L33: 2.0851 L12: -0.4297 REMARK 3 L13: -0.4667 L23: -1.2453 REMARK 3 S TENSOR REMARK 3 S11: 0.1782 S12: 0.4095 S13: 0.1937 REMARK 3 S21: -0.3630 S22: -0.6922 S23: -0.9433 REMARK 3 S31: -0.0305 S32: 0.1842 S33: 0.5140 REMARK 3 REMARK 3 TLS GROUP : 24 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 96 D 109 REMARK 3 ORIGIN FOR THE GROUP (A): 82.7840 22.5600 78.1710 REMARK 3 T TENSOR REMARK 3 T11: 0.9128 T22: 0.5069 REMARK 3 T33: 0.4560 T12: -0.4616 REMARK 3 T13: -0.3287 T23: 0.3920 REMARK 3 L TENSOR REMARK 3 L11: 5.1323 L22: 3.7806 REMARK 3 L33: 12.1466 L12: -3.4631 REMARK 3 L13: -3.9782 L23: -0.7106 REMARK 3 S TENSOR REMARK 3 S11: -0.0651 S12: 0.2624 S13: 0.7853 REMARK 3 S21: 0.4825 S22: -0.6115 S23: -1.1389 REMARK 3 S31: -0.0629 S32: 0.4558 S33: 0.6766 REMARK 3 REMARK 3 TLS GROUP : 25 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : D 110 D 124 REMARK 3 ORIGIN FOR THE GROUP (A): 87.8860 35.2230 75.6590 REMARK 3 T TENSOR REMARK 3 T11: 0.4903 T22: 0.3584 REMARK 3 T33: 0.5500 T12: -0.1585 REMARK 3 T13: 0.0423 T23: 0.2789 REMARK 3 L TENSOR REMARK 3 L11: 0.5705 L22: 9.6704 REMARK 3 L33: 8.3302 L12: -0.5218 REMARK 3 L13: 1.8510 L23: -3.7242 REMARK 3 S TENSOR REMARK 3 S11: 0.1410 S12: 0.0777 S13: 0.2956 REMARK 3 S21: 1.4468 S22: -0.9569 S23: -1.4067 REMARK 3 S31: -0.4685 S32: 0.6952 S33: 0.8159 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 5F1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-15. REMARK 100 THE DEPOSITION ID IS D_1000215840. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-SEP-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51358 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 9.800 REMARK 200 R MERGE (I) : 0.09200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 9.10 REMARK 200 R MERGE FOR SHELL (I) : 0.57600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1YH3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 25% PEG3350, PH 8.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 44.27600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.88850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.12100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.88850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.27600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.12100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17180 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 16910 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ARG A 45 REMARK 465 TRP A 46 REMARK 465 ARG A 47 REMARK 465 GLN A 48 REMARK 465 ARG A 247 REMARK 465 GLU A 248 REMARK 465 ASP A 249 REMARK 465 SER A 250 REMARK 465 THR A 297 REMARK 465 SER A 298 REMARK 465 GLU A 299 REMARK 465 ILE A 300 REMARK 465 ARG B 45 REMARK 465 TRP B 46 REMARK 465 ARG B 47 REMARK 465 GLN B 48 REMARK 465 GLY B 245 REMARK 465 GLY B 246 REMARK 465 ARG B 247 REMARK 465 GLU B 248 REMARK 465 ASP B 249 REMARK 465 SER B 250 REMARK 465 GLU B 292 REMARK 465 ASP B 293 REMARK 465 SER B 294 REMARK 465 SER B 295 REMARK 465 CYS B 296 REMARK 465 THR B 297 REMARK 465 SER B 298 REMARK 465 GLU B 299 REMARK 465 ILE B 300 REMARK 465 ASP C 1 REMARK 465 GLU C 125 REMARK 465 PRO C 126 REMARK 465 LYS C 127 REMARK 465 THR C 128 REMARK 465 PRO C 129 REMARK 465 LYS C 130 REMARK 465 PRO C 131 REMARK 465 GLN C 132 REMARK 465 PRO C 133 REMARK 465 ALA C 134 REMARK 465 ALA C 135 REMARK 465 ALA C 136 REMARK 465 HIS C 137 REMARK 465 HIS C 138 REMARK 465 HIS C 139 REMARK 465 HIS C 140 REMARK 465 HIS C 141 REMARK 465 HIS C 142 REMARK 465 GLY C 143 REMARK 465 ALA C 144 REMARK 465 ALA C 145 REMARK 465 GLU C 146 REMARK 465 GLN C 147 REMARK 465 LYS C 148 REMARK 465 LEU C 149 REMARK 465 ILE C 150 REMARK 465 SER C 151 REMARK 465 GLU C 152 REMARK 465 GLU C 153 REMARK 465 ASP C 154 REMARK 465 LEU C 155 REMARK 465 ASN C 156 REMARK 465 GLY C 157 REMARK 465 ALA C 158 REMARK 465 ALA C 159 REMARK 465 ASP D 1 REMARK 465 GLU D 125 REMARK 465 PRO D 126 REMARK 465 LYS D 127 REMARK 465 THR D 128 REMARK 465 PRO D 129 REMARK 465 LYS D 130 REMARK 465 PRO D 131 REMARK 465 GLN D 132 REMARK 465 PRO D 133 REMARK 465 ALA D 134 REMARK 465 ALA D 135 REMARK 465 ALA D 136 REMARK 465 HIS D 137 REMARK 465 HIS D 138 REMARK 465 HIS D 139 REMARK 465 HIS D 140 REMARK 465 HIS D 141 REMARK 465 HIS D 142 REMARK 465 GLY D 143 REMARK 465 ALA D 144 REMARK 465 ALA D 145 REMARK 465 GLU D 146 REMARK 465 GLN D 147 REMARK 465 LYS D 148 REMARK 465 LEU D 149 REMARK 465 ILE D 150 REMARK 465 SER D 151 REMARK 465 GLU D 152 REMARK 465 GLU D 153 REMARK 465 ASP D 154 REMARK 465 LEU D 155 REMARK 465 ASN D 156 REMARK 465 GLY D 157 REMARK 465 ALA D 158 REMARK 465 ALA D 159 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG B 78 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG B 78 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES REMARK 500 ARG B 280 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 ARG D 67 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 ARG D 67 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ILE A 128 50.90 -152.55 REMARK 500 ASN A 182 60.00 -96.15 REMARK 500 ASP A 202 -116.65 60.95 REMARK 500 LYS A 214 68.90 76.94 REMARK 500 LYS A 234 -23.83 -148.17 REMARK 500 ILE B 128 50.08 -154.68 REMARK 500 ASN B 182 59.74 -96.75 REMARK 500 ASP B 202 -116.85 61.16 REMARK 500 LYS B 234 -23.75 -148.40 REMARK 500 ALA C 92 170.84 179.73 REMARK 500 REMARK 500 REMARK: NULL DBREF 5F1K A 45 300 UNP P28907 CD38_HUMAN 45 300 DBREF 5F1K B 45 300 UNP P28907 CD38_HUMAN 45 300 DBREF 5F1K C 1 159 PDB 5F1K 5F1K 1 159 DBREF 5F1K D 1 159 PDB 5F1K 5F1K 1 159 SEQADV 5F1K THR A 49 UNP P28907 GLN 49 ENGINEERED MUTATION SEQADV 5F1K ASP A 100 UNP P28907 ASN 100 ENGINEERED MUTATION SEQADV 5F1K ASP A 164 UNP P28907 ASN 164 ENGINEERED MUTATION SEQADV 5F1K ASP A 209 UNP P28907 ASN 209 ENGINEERED MUTATION SEQADV 5F1K ASP A 219 UNP P28907 ASN 219 ENGINEERED MUTATION SEQADV 5F1K THR B 49 UNP P28907 GLN 49 ENGINEERED MUTATION SEQADV 5F1K ASP B 100 UNP P28907 ASN 100 ENGINEERED MUTATION SEQADV 5F1K ASP B 164 UNP P28907 ASN 164 ENGINEERED MUTATION SEQADV 5F1K ASP B 209 UNP P28907 ASN 209 ENGINEERED MUTATION SEQADV 5F1K ASP B 219 UNP P28907 ASN 219 ENGINEERED MUTATION SEQRES 1 A 256 ARG TRP ARG GLN THR TRP SER GLY PRO GLY THR THR LYS SEQRES 2 A 256 ARG PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR SEQRES 3 A 256 THR GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN SEQRES 4 A 256 SER VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS SEQRES 5 A 256 HIS PRO CYS ASP ILE THR GLU GLU ASP TYR GLN PRO LEU SEQRES 6 A 256 MET LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE SEQRES 7 A 256 LEU LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE SEQRES 8 A 256 THR GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR SEQRES 9 A 256 LEU LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY SEQRES 10 A 256 GLU PHE ASP THR SER LYS ILE ASN TYR GLN SER CYS PRO SEQRES 11 A 256 ASP TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL SEQRES 12 A 256 PHE TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA SEQRES 13 A 256 CYS ASP VAL VAL HIS VAL MET LEU ASP GLY SER ARG SER SEQRES 14 A 256 LYS ILE PHE ASP LYS ASP SER THR PHE GLY SER VAL GLU SEQRES 15 A 256 VAL HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU SEQRES 16 A 256 ALA TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP SEQRES 17 A 256 LEU CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE SEQRES 18 A 256 ILE SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE SEQRES 19 A 256 TYR ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO SEQRES 20 A 256 GLU ASP SER SER CYS THR SER GLU ILE SEQRES 1 B 256 ARG TRP ARG GLN THR TRP SER GLY PRO GLY THR THR LYS SEQRES 2 B 256 ARG PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR SEQRES 3 B 256 THR GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN SEQRES 4 B 256 SER VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS SEQRES 5 B 256 HIS PRO CYS ASP ILE THR GLU GLU ASP TYR GLN PRO LEU SEQRES 6 B 256 MET LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE SEQRES 7 B 256 LEU LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE SEQRES 8 B 256 THR GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR SEQRES 9 B 256 LEU LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY SEQRES 10 B 256 GLU PHE ASP THR SER LYS ILE ASN TYR GLN SER CYS PRO SEQRES 11 B 256 ASP TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL SEQRES 12 B 256 PHE TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA SEQRES 13 B 256 CYS ASP VAL VAL HIS VAL MET LEU ASP GLY SER ARG SER SEQRES 14 B 256 LYS ILE PHE ASP LYS ASP SER THR PHE GLY SER VAL GLU SEQRES 15 B 256 VAL HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU SEQRES 16 B 256 ALA TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP SEQRES 17 B 256 LEU CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE SEQRES 18 B 256 ILE SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE SEQRES 19 B 256 TYR ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO SEQRES 20 B 256 GLU ASP SER SER CYS THR SER GLU ILE SEQRES 1 C 159 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 159 ALA GLY GLY SER LEU ARG LEU SER CYS THR GLY SER GLY SEQRES 3 C 159 ARG THR PHE ARG ASN TYR PRO MET ALA TRP PHE ARG GLN SEQRES 4 C 159 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLY ILE THR SEQRES 5 C 159 TRP VAL GLY ALA SER THR LEU TYR ALA ASP PHE ALA LYS SEQRES 6 C 159 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 159 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 C 159 ALA VAL TYR SER CYS ALA ALA GLY ARG GLY ILE VAL ALA SEQRES 9 C 159 GLY ARG ILE PRO ALA GLU TYR ALA ASP TRP GLY GLN GLY SEQRES 10 C 159 THR GLN VAL THR VAL SER SER GLU PRO LYS THR PRO LYS SEQRES 11 C 159 PRO GLN PRO ALA ALA ALA HIS HIS HIS HIS HIS HIS GLY SEQRES 12 C 159 ALA ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SEQRES 13 C 159 GLY ALA ALA SEQRES 1 D 159 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 159 ALA GLY GLY SER LEU ARG LEU SER CYS THR GLY SER GLY SEQRES 3 D 159 ARG THR PHE ARG ASN TYR PRO MET ALA TRP PHE ARG GLN SEQRES 4 D 159 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLY ILE THR SEQRES 5 D 159 TRP VAL GLY ALA SER THR LEU TYR ALA ASP PHE ALA LYS SEQRES 6 D 159 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 159 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 D 159 ALA VAL TYR SER CYS ALA ALA GLY ARG GLY ILE VAL ALA SEQRES 9 D 159 GLY ARG ILE PRO ALA GLU TYR ALA ASP TRP GLY GLN GLY SEQRES 10 D 159 THR GLN VAL THR VAL SER SER GLU PRO LYS THR PRO LYS SEQRES 11 D 159 PRO GLN PRO ALA ALA ALA HIS HIS HIS HIS HIS HIS GLY SEQRES 12 D 159 ALA ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SEQRES 13 D 159 GLY ALA ALA FORMUL 5 HOH *323(H2 O) HELIX 1 AA1 ARG A 58 HIS A 74 1 17 HELIX 2 AA2 PRO A 75 ARG A 78 5 4 HELIX 3 AA3 ASP A 81 ILE A 94 1 14 HELIX 4 AA4 GLU A 103 ASP A 105 5 3 HELIX 5 AA5 TYR A 106 GLY A 113 1 8 HELIX 6 AA6 PRO A 118 LYS A 121 5 4 HELIX 7 AA7 ILE A 128 GLN A 139 1 12 HELIX 8 AA8 THR A 144 ASP A 147 5 4 HELIX 9 AA9 THR A 148 ASP A 155 1 8 HELIX 10 AB1 ASN A 183 ALA A 200 1 18 HELIX 11 AB2 SER A 220 VAL A 225 1 6 HELIX 12 AB3 GLU A 226 LEU A 230 5 5 HELIX 13 AB4 ASP A 252 GLN A 255 5 4 HELIX 14 AB5 ASP A 256 ARG A 269 1 14 HELIX 15 AB6 ARG A 280 ASN A 290 1 11 HELIX 16 AB7 ARG B 58 HIS B 74 1 17 HELIX 17 AB8 PRO B 75 ARG B 78 5 4 HELIX 18 AB9 ASP B 81 ILE B 94 1 14 HELIX 19 AC1 GLU B 103 ASP B 105 5 3 HELIX 20 AC2 TYR B 106 GLY B 113 1 8 HELIX 21 AC3 PRO B 118 LYS B 121 5 4 HELIX 22 AC4 ILE B 128 GLN B 139 1 12 HELIX 23 AC5 THR B 144 ASP B 147 5 4 HELIX 24 AC6 THR B 148 ASP B 155 1 8 HELIX 25 AC7 ASN B 183 ALA B 200 1 18 HELIX 26 AC8 SER B 220 VAL B 225 1 6 HELIX 27 AC9 GLU B 226 LEU B 230 5 5 HELIX 28 AD1 ASP B 252 GLN B 255 5 4 HELIX 29 AD2 ASP B 256 ARG B 269 1 14 HELIX 30 AD3 ARG B 280 ASN B 290 1 11 HELIX 31 AD4 LYS C 87 THR C 91 5 5 HELIX 32 AD5 ILE C 107 TYR C 111 5 5 HELIX 33 AD6 LYS D 87 THR D 91 5 5 HELIX 34 AD7 ILE D 107 TYR D 111 5 5 SHEET 1 AA1 2 GLY A 52 PRO A 53 0 SHEET 2 AA1 2 SER A 172 CYS A 173 -1 O CYS A 173 N GLY A 52 SHEET 1 AA2 4 LEU A 123 SER A 126 0 SHEET 2 AA2 4 ASP A 202 ASP A 209 1 O HIS A 205 N LEU A 124 SHEET 3 AA2 4 VAL A 235 ILE A 243 1 O GLU A 239 N VAL A 204 SHEET 4 AA2 4 GLN A 272 ILE A 278 1 O ILE A 278 N VAL A 242 SHEET 1 AA3 2 GLY B 52 PRO B 53 0 SHEET 2 AA3 2 SER B 172 CYS B 173 -1 O CYS B 173 N GLY B 52 SHEET 1 AA4 4 LEU B 123 SER B 126 0 SHEET 2 AA4 4 ASP B 202 ASP B 209 1 O HIS B 205 N LEU B 124 SHEET 3 AA4 4 VAL B 235 ILE B 243 1 O GLU B 239 N VAL B 204 SHEET 4 AA4 4 GLN B 272 ILE B 278 1 O ILE B 278 N VAL B 242 SHEET 1 AA5 4 GLN C 3 SER C 7 0 SHEET 2 AA5 4 LEU C 18 SER C 25 -1 O THR C 23 N GLN C 5 SHEET 3 AA5 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA5 4 PHE C 68 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AA6 6 GLY C 10 GLN C 13 0 SHEET 2 AA6 6 THR C 118 SER C 123 1 O SER C 123 N VAL C 12 SHEET 3 AA6 6 ALA C 92 ALA C 98 -1 N TYR C 94 O THR C 118 SHEET 4 AA6 6 MET C 34 GLN C 39 -1 N PHE C 37 O SER C 95 SHEET 5 AA6 6 GLU C 46 ILE C 51 -1 O ALA C 49 N TRP C 36 SHEET 6 AA6 6 THR C 58 TYR C 60 -1 O LEU C 59 N GLY C 50 SHEET 1 AA7 4 GLY C 10 GLN C 13 0 SHEET 2 AA7 4 THR C 118 SER C 123 1 O SER C 123 N VAL C 12 SHEET 3 AA7 4 ALA C 92 ALA C 98 -1 N TYR C 94 O THR C 118 SHEET 4 AA7 4 ASP C 113 TRP C 114 -1 O ASP C 113 N ALA C 98 SHEET 1 AA8 4 GLN D 3 SER D 7 0 SHEET 2 AA8 4 LEU D 18 SER D 25 -1 O THR D 23 N GLN D 5 SHEET 3 AA8 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA8 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AA9 6 GLY D 10 GLN D 13 0 SHEET 2 AA9 6 THR D 118 SER D 123 1 O SER D 123 N VAL D 12 SHEET 3 AA9 6 ALA D 92 ALA D 98 -1 N TYR D 94 O THR D 118 SHEET 4 AA9 6 MET D 34 GLN D 39 -1 N PHE D 37 O SER D 95 SHEET 5 AA9 6 GLU D 46 ILE D 51 -1 O ALA D 49 N TRP D 36 SHEET 6 AA9 6 THR D 58 TYR D 60 -1 O LEU D 59 N GLY D 50 SHEET 1 AB1 4 GLY D 10 GLN D 13 0 SHEET 2 AB1 4 THR D 118 SER D 123 1 O SER D 123 N VAL D 12 SHEET 3 AB1 4 ALA D 92 ALA D 98 -1 N TYR D 94 O THR D 118 SHEET 4 AB1 4 ASP D 113 TRP D 114 -1 O ASP D 113 N ALA D 98 SSBOND 1 CYS A 67 CYS A 82 1555 1555 2.16 SSBOND 2 CYS A 99 CYS A 180 1555 1555 2.05 SSBOND 3 CYS A 119 CYS A 201 1555 1555 2.06 SSBOND 4 CYS A 160 CYS A 173 1555 1555 2.08 SSBOND 5 CYS A 254 CYS A 275 1555 1555 2.06 SSBOND 6 CYS A 287 CYS A 296 1555 1555 2.05 SSBOND 7 CYS B 67 CYS B 82 1555 1555 2.16 SSBOND 8 CYS B 99 CYS B 180 1555 1555 2.06 SSBOND 9 CYS B 119 CYS B 201 1555 1555 2.02 SSBOND 10 CYS B 160 CYS B 173 1555 1555 2.09 SSBOND 11 CYS B 254 CYS B 275 1555 1555 2.08 SSBOND 12 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 13 CYS D 22 CYS D 96 1555 1555 2.03 CRYST1 88.552 96.242 133.777 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011293 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010390 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007475 0.00000 ATOM 1 N THR A 49 56.938 51.454 110.246 1.00 60.26 N ANISOU 1 N THR A 49 8329 5263 9302 2707 84 -3276 N ATOM 2 CA THR A 49 58.440 51.577 110.232 1.00 60.97 C ANISOU 2 CA THR A 49 8384 5281 9501 2434 111 -3503 C ATOM 3 C THR A 49 59.137 50.508 111.102 1.00 59.75 C ANISOU 3 C THR A 49 8108 5473 9120 2455 24 -3697 C ATOM 4 O THR A 49 58.853 50.375 112.303 1.00 60.99 O ANISOU 4 O THR A 49 8292 5912 8966 2790 -87 -3972 O ATOM 5 CB THR A 49 58.919 52.975 110.691 1.00 64.40 C ANISOU 5 CB THR A 49 8928 5379 10159 2420 124 -3854 C ATOM 6 OG1 THR A 49 58.183 53.982 109.991 1.00 66.59 O ANISOU 6 OG1 THR A 49 9442 5246 10612 2464 255 -3566 O ATOM 7 CG2 THR A 49 60.420 53.184 110.412 1.00 65.53 C ANISOU 7 CG2 THR A 49 9016 5375 10507 2026 119 -4057 C ATOM 8 N TRP A 50 60.060 49.777 110.474 1.00 57.82 N ANISOU 8 N TRP A 50 7745 5321 8900 2225 -42 -3620 N ATOM 9 CA TRP A 50 60.790 48.661 111.094 1.00 56.03 C ANISOU 9 CA TRP A 50 7420 5381 8485 2171 -145 -3807 C ATOM 10 C TRP A 50 62.248 49.056 111.360 1.00 58.16 C ANISOU 10 C TRP A 50 7555 5638 8903 2017 -270 -4158 C ATOM 11 O TRP A 50 62.730 50.084 110.859 1.00 60.76 O ANISOU 11 O TRP A 50 7923 5717 9445 1655 -201 -4253 O ATOM 12 CB TRP A 50 60.744 47.442 110.174 1.00 52.49 C ANISOU 12 CB TRP A 50 6901 5053 7990 2098 -79 -3425 C ATOM 13 CG TRP A 50 59.350 47.092 109.679 1.00 50.42 C ANISOU 13 CG TRP A 50 6738 4838 7578 2267 38 -3105 C ATOM 14 CD1 TRP A 50 58.867 47.268 108.421 1.00 49.19 C ANISOU 14 CD1 TRP A 50 6609 4516 7565 2194 136 -2920 C ATOM 15 CD2 TRP A 50 58.278 46.519 110.444 1.00 49.65 C ANISOU 15 CD2 TRP A 50 6656 4919 7287 2456 15 -3053 C ATOM 16 NE1 TRP A 50 57.568 46.833 108.345 1.00 47.98 N ANISOU 16 NE1 TRP A 50 6515 4392 7322 2342 167 -2698 N ATOM 17 CE2 TRP A 50 57.177 46.382 109.577 1.00 48.24 C ANISOU 17 CE2 TRP A 50 6531 4621 7176 2417 108 -2771 C ATOM 18 CE3 TRP A 50 58.141 46.117 111.782 1.00 50.56 C ANISOU 18 CE3 TRP A 50 6781 5267 7161 2586 40 -3206 C ATOM 19 CZ2 TRP A 50 55.946 45.873 110.003 1.00 48.03 C ANISOU 19 CZ2 TRP A 50 6473 4781 6996 2603 195 -2639 C ATOM 20 CZ3 TRP A 50 56.914 45.603 112.205 1.00 50.12 C ANISOU 20 CZ3 TRP A 50 6816 5321 6905 2641 90 -3084 C ATOM 21 CH2 TRP A 50 55.835 45.492 111.318 1.00 48.92 C ANISOU 21 CH2 TRP A 50 6585 5145 6855 2721 217 -2822 C ATOM 22 N SER A 51 62.935 48.236 112.150 1.00 57.84 N ANISOU 22 N SER A 51 7444 5790 8741 2136 -400 -4392 N ATOM 23 CA SER A 51 64.312 48.498 112.564 1.00 60.46 C ANISOU 23 CA SER A 51 7574 6200 9197 2041 -565 -4820 C ATOM 24 C SER A 51 65.350 48.004 111.559 1.00 59.57 C ANISOU 24 C SER A 51 7295 6086 9253 1736 -535 -4792 C ATOM 25 O SER A 51 66.490 48.446 111.581 1.00 61.87 O ANISOU 25 O SER A 51 7486 6348 9672 1454 -730 -5206 O ATOM 26 CB SER A 51 64.577 47.829 113.915 1.00 61.53 C ANISOU 26 CB SER A 51 7703 6678 8998 2336 -732 -5037 C ATOM 27 OG SER A 51 63.606 48.213 114.880 1.00 63.02 O ANISOU 27 OG SER A 51 8123 6834 8986 2742 -693 -5106 O ATOM 28 N GLY A 52 64.971 47.067 110.698 1.00 56.91 N ANISOU 28 N GLY A 52 6997 5828 8797 1677 -435 -4409 N ATOM 29 CA GLY A 52 65.907 46.479 109.734 1.00 56.07 C ANISOU 29 CA GLY A 52 6750 5744 8807 1430 -359 -4332 C ATOM 30 C GLY A 52 65.991 47.263 108.429 1.00 56.37 C ANISOU 30 C GLY A 52 6814 5429 9173 1175 -96 -4172 C ATOM 31 O GLY A 52 65.097 48.063 108.125 1.00 55.45 O ANISOU 31 O GLY A 52 7029 4951 9086 1208 236 -3992 O ATOM 32 N PRO A 53 67.054 47.016 107.628 1.00 56.67 N ANISOU 32 N PRO A 53 6695 5434 9403 886 -18 -4302 N ATOM 33 CA PRO A 53 67.163 47.657 106.306 1.00 57.25 C ANISOU 33 CA PRO A 53 6901 5125 9724 592 238 -4110 C ATOM 34 C PRO A 53 66.042 47.218 105.364 1.00 54.59 C ANISOU 34 C PRO A 53 6866 4711 9163 685 310 -3623 C ATOM 35 O PRO A 53 65.511 46.115 105.497 1.00 53.00 O ANISOU 35 O PRO A 53 6741 4746 8651 745 216 -3451 O ATOM 36 CB PRO A 53 68.533 47.199 105.783 1.00 57.93 C ANISOU 36 CB PRO A 53 6783 5263 9962 299 320 -4365 C ATOM 37 CG PRO A 53 68.917 46.015 106.602 1.00 57.07 C ANISOU 37 CG PRO A 53 6422 5629 9630 585 13 -4479 C ATOM 38 CD PRO A 53 68.182 46.106 107.908 1.00 56.89 C ANISOU 38 CD PRO A 53 6520 5693 9401 898 -200 -4571 C ATOM 39 N GLY A 54 65.672 48.097 104.443 1.00 55.59 N ANISOU 39 N GLY A 54 7170 4537 9413 522 525 -3399 N ATOM 40 CA GLY A 54 64.557 47.844 103.538 1.00 53.65 C ANISOU 40 CA GLY A 54 7127 4230 9025 596 590 -2949 C ATOM 41 C GLY A 54 64.899 46.886 102.423 1.00 52.15 C ANISOU 41 C GLY A 54 6912 4182 8719 475 683 -2736 C ATOM 42 O GLY A 54 66.040 46.444 102.294 1.00 53.80 O ANISOU 42 O GLY A 54 6651 4877 8913 237 710 -2778 O ATOM 43 N THR A 55 63.899 46.566 101.609 1.00 50.22 N ANISOU 43 N THR A 55 6824 3927 8330 592 744 -2381 N ATOM 44 CA THR A 55 64.092 45.710 100.455 1.00 48.23 C ANISOU 44 CA THR A 55 6662 3632 8029 351 753 -2111 C ATOM 45 C THR A 55 65.254 46.214 99.587 1.00 50.48 C ANISOU 45 C THR A 55 6967 3693 8517 60 1018 -2185 C ATOM 46 O THR A 55 65.382 47.422 99.388 1.00 53.83 O ANISOU 46 O THR A 55 7530 3841 9080 -263 1182 -1947 O ATOM 47 CB THR A 55 62.815 45.657 99.605 1.00 47.28 C ANISOU 47 CB THR A 55 6742 3505 7716 577 767 -1771 C ATOM 48 OG1 THR A 55 61.741 45.100 100.385 1.00 45.15 O ANISOU 48 OG1 THR A 55 6541 3740 6875 918 712 -1966 O ATOM 49 CG2 THR A 55 63.049 44.820 98.321 1.00 46.02 C ANISOU 49 CG2 THR A 55 6652 3396 7437 487 829 -1516 C ATOM 50 N THR A 56 66.099 45.304 99.105 1.00 49.47 N ANISOU 50 N THR A 56 6690 3673 8431 -94 1066 -2218 N ATOM 51 CA THR A 56 67.231 45.664 98.243 1.00 51.84 C ANISOU 51 CA THR A 56 7011 3800 8884 -393 1364 -2341 C ATOM 52 C THR A 56 66.737 46.364 96.988 1.00 52.99 C ANISOU 52 C THR A 56 7528 3601 9002 -430 1619 -2029 C ATOM 53 O THR A 56 65.740 45.944 96.398 1.00 51.06 O ANISOU 53 O THR A 56 7470 3355 8572 -105 1534 -1873 O ATOM 54 CB THR A 56 68.040 44.420 97.806 1.00 50.57 C ANISOU 54 CB THR A 56 6657 3858 8699 -521 1386 -2380 C ATOM 55 OG1 THR A 56 68.212 43.543 98.922 1.00 49.31 O ANISOU 55 OG1 THR A 56 6289 3986 8460 -324 1182 -2551 O ATOM 56 CG2 THR A 56 69.420 44.812 97.263 1.00 53.63 C ANISOU 56 CG2 THR A 56 6910 4129 9338 -858 1691 -2621 C ATOM 57 N LYS A 57 67.434 47.430 96.594 1.00 56.49 N ANISOU 57 N LYS A 57 8173 3620 9671 -743 1932 -2219 N ATOM 58 CA LYS A 57 67.096 48.200 95.377 1.00 59.57 C ANISOU 58 CA LYS A 57 9059 3621 9952 -832 2148 -1829 C ATOM 59 C LYS A 57 67.006 47.260 94.194 1.00 57.46 C ANISOU 59 C LYS A 57 8892 3467 9471 -884 2197 -1475 C ATOM 60 O LYS A 57 67.886 46.425 94.024 1.00 56.41 O ANISOU 60 O LYS A 57 8541 3574 9317 -1054 2277 -1530 O ATOM 61 CB LYS A 57 68.157 49.285 95.005 1.00 64.93 C ANISOU 61 CB LYS A 57 9868 3849 10951 -1308 2557 -2005 C ATOM 62 CG LYS A 57 69.137 49.722 96.092 1.00 67.38 C ANISOU 62 CG LYS A 57 9834 4211 11555 -1506 2538 -2550 C ATOM 63 CD LYS A 57 70.147 50.743 95.523 1.00 72.65 C ANISOU 63 CD LYS A 57 10642 4422 12537 -1976 3007 -2716 C ATOM 64 CE LYS A 57 70.000 52.113 96.117 1.00 76.07 C ANISOU 64 CE LYS A 57 11294 4440 13169 -2027 3113 -2899 C ATOM 65 NZ LYS A 57 70.566 52.182 97.484 1.00 76.63 N ANISOU 65 NZ LYS A 57 10872 4773 13468 -2056 2908 -3402 N ATOM 66 N ARG A 58 65.970 47.423 93.375 1.00 57.47 N ANISOU 66 N ARG A 58 9264 3342 9227 -686 2162 -1091 N ATOM 67 CA ARG A 58 65.795 46.637 92.136 1.00 57.14 C ANISOU 67 CA ARG A 58 9412 3360 8937 -655 2161 -861 C ATOM 68 C ARG A 58 65.687 45.136 92.384 1.00 52.58 C ANISOU 68 C ARG A 58 8405 3356 8215 -535 1937 -856 C ATOM 69 O ARG A 58 66.092 44.329 91.543 1.00 52.75 O ANISOU 69 O ARG A 58 8378 3499 8163 -577 2000 -858 O ATOM 70 CB ARG A 58 66.917 46.942 91.133 1.00 61.02 C ANISOU 70 CB ARG A 58 10019 3694 9468 -1031 2624 -890 C ATOM 71 CG ARG A 58 67.050 48.448 90.956 1.00 66.45 C ANISOU 71 CG ARG A 58 11166 3746 10336 -1111 2899 -838 C ATOM 72 CD ARG A 58 67.509 48.931 89.566 1.00 70.97 C ANISOU 72 CD ARG A 58 12238 4008 10720 -1371 3362 -616 C ATOM 73 NE ARG A 58 68.546 48.128 88.929 1.00 72.07 N ANISOU 73 NE ARG A 58 12128 4386 10866 -1580 3632 -778 N ATOM 74 CZ ARG A 58 69.794 47.973 89.380 1.00 73.50 C ANISOU 74 CZ ARG A 58 11867 4668 11389 -1924 3720 -1236 C ATOM 75 NH1 ARG A 58 70.193 48.517 90.531 1.00 74.80 N ANISOU 75 NH1 ARG A 58 11689 4918 11811 -2021 3646 -1632 N ATOM 76 NH2 ARG A 58 70.650 47.237 88.676 1.00 74.19 N ANISOU 76 NH2 ARG A 58 11835 4849 11501 -2036 3896 -1315 N ATOM 77 N PHE A 59 65.131 44.785 93.542 1.00 49.62 N ANISOU 77 N PHE A 59 7800 3170 7883 -316 1602 -1001 N ATOM 78 CA PHE A 59 64.922 43.396 93.964 1.00 45.46 C ANISOU 78 CA PHE A 59 6915 3134 7220 -177 1397 -1044 C ATOM 79 C PHE A 59 64.155 42.552 92.946 1.00 43.55 C ANISOU 79 C PHE A 59 6802 2996 6749 -88 1342 -691 C ATOM 80 O PHE A 59 64.582 41.452 92.659 1.00 41.63 O ANISOU 80 O PHE A 59 6259 3122 6433 -108 1348 -699 O ATOM 81 CB PHE A 59 64.232 43.381 95.332 1.00 43.99 C ANISOU 81 CB PHE A 59 6554 3087 7070 54 1163 -1156 C ATOM 82 CG PHE A 59 63.820 42.031 95.803 1.00 40.79 C ANISOU 82 CG PHE A 59 5900 3064 6533 199 954 -1202 C ATOM 83 CD1 PHE A 59 64.749 41.178 96.384 1.00 39.89 C ANISOU 83 CD1 PHE A 59 5548 3201 6404 64 858 -1328 C ATOM 84 CD2 PHE A 59 62.506 41.613 95.686 1.00 39.30 C ANISOU 84 CD2 PHE A 59 5754 3009 6169 444 871 -1037 C ATOM 85 CE1 PHE A 59 64.379 39.930 96.828 1.00 37.58 C ANISOU 85 CE1 PHE A 59 5112 3167 5999 207 701 -1322 C ATOM 86 CE2 PHE A 59 62.125 40.362 96.135 1.00 37.17 C ANISOU 86 CE2 PHE A 59 5297 3083 5744 553 728 -925 C ATOM 87 CZ PHE A 59 63.061 39.519 96.707 1.00 36.35 C ANISOU 87 CZ PHE A 59 4979 3164 5667 430 626 -1088 C ATOM 88 N PRO A 60 63.028 43.055 92.395 1.00 44.30 N ANISOU 88 N PRO A 60 7208 2909 6713 121 1253 -498 N ATOM 89 CA PRO A 60 62.334 42.286 91.349 1.00 43.43 C ANISOU 89 CA PRO A 60 7192 2995 6315 258 1167 -264 C ATOM 90 C PRO A 60 63.192 41.937 90.128 1.00 44.17 C ANISOU 90 C PRO A 60 7469 2990 6323 17 1373 -186 C ATOM 91 O PRO A 60 63.180 40.790 89.692 1.00 42.70 O ANISOU 91 O PRO A 60 7232 3024 5966 -52 1336 -186 O ATOM 92 CB PRO A 60 61.170 43.197 90.938 1.00 45.17 C ANISOU 92 CB PRO A 60 7733 3025 6405 528 1060 -87 C ATOM 93 CG PRO A 60 60.924 44.043 92.115 1.00 45.91 C ANISOU 93 CG PRO A 60 7745 3026 6670 634 1019 -249 C ATOM 94 CD PRO A 60 62.274 44.272 92.742 1.00 46.33 C ANISOU 94 CD PRO A 60 7618 3014 6972 354 1237 -483 C ATOM 95 N GLU A 61 63.928 42.915 89.604 1.00 47.12 N ANISOU 95 N GLU A 61 8129 3011 6762 -169 1666 -171 N ATOM 96 CA GLU A 61 64.778 42.713 88.422 1.00 48.48 C ANISOU 96 CA GLU A 61 8464 3070 6884 -359 1929 -99 C ATOM 97 C GLU A 61 65.977 41.828 88.767 1.00 46.57 C ANISOU 97 C GLU A 61 7830 3055 6807 -684 2058 -330 C ATOM 98 O GLU A 61 66.389 41.005 87.960 1.00 45.95 O ANISOU 98 O GLU A 61 7786 2996 6674 -789 2212 -211 O ATOM 99 CB GLU A 61 65.272 44.047 87.819 1.00 52.87 C ANISOU 99 CB GLU A 61 9465 3165 7456 -527 2288 0 C ATOM 100 CG GLU A 61 64.195 45.056 87.398 1.00 55.54 C ANISOU 100 CG GLU A 61 10273 3215 7615 -222 2164 271 C ATOM 101 CD GLU A 61 63.779 46.016 88.507 1.00 56.35 C ANISOU 101 CD GLU A 61 10361 3157 7890 -135 2077 145 C ATOM 102 OE1 GLU A 61 64.093 47.219 88.443 1.00 61.47 O ANISOU 102 OE1 GLU A 61 11421 3121 8812 -136 2123 289 O ATOM 103 OE2 GLU A 61 63.136 45.571 89.469 1.00 54.72 O ANISOU 103 OE2 GLU A 61 9615 3474 7699 -14 1682 264 O ATOM 104 N THR A 62 66.528 41.996 89.968 1.00 45.85 N ANISOU 104 N THR A 62 7386 3037 6995 -737 2037 -589 N ATOM 105 CA THR A 62 67.637 41.163 90.428 1.00 44.74 C ANISOU 105 CA THR A 62 6884 3109 7006 -895 2052 -890 C ATOM 106 C THR A 62 67.236 39.689 90.534 1.00 41.29 C ANISOU 106 C THR A 62 6222 3064 6402 -723 1825 -872 C ATOM 107 O THR A 62 67.972 38.808 90.071 1.00 40.19 O ANISOU 107 O THR A 62 6022 2887 6359 -838 1914 -768 O ATOM 108 CB THR A 62 68.176 41.628 91.798 1.00 45.24 C ANISOU 108 CB THR A 62 6664 3197 7328 -929 1984 -1243 C ATOM 109 OG1 THR A 62 68.664 42.961 91.691 1.00 48.55 O ANISOU 109 OG1 THR A 62 7274 3324 7849 -1200 2222 -1283 O ATOM 110 CG2 THR A 62 69.325 40.732 92.284 1.00 44.76 C ANISOU 110 CG2 THR A 62 6150 3470 7387 -1027 1954 -1575 C ATOM 111 N VAL A 63 66.087 39.429 91.150 1.00 39.25 N ANISOU 111 N VAL A 63 5932 2964 6016 -489 1532 -754 N ATOM 112 CA VAL A 63 65.646 38.049 91.329 1.00 36.75 C ANISOU 112 CA VAL A 63 5432 2927 5602 -335 1303 -705 C ATOM 113 C VAL A 63 65.384 37.427 89.969 1.00 36.52 C ANISOU 113 C VAL A 63 5554 2967 5354 -340 1414 -481 C ATOM 114 O VAL A 63 65.814 36.308 89.698 1.00 35.27 O ANISOU 114 O VAL A 63 5203 2997 5202 -367 1579 -369 O ATOM 115 CB VAL A 63 64.407 37.943 92.234 1.00 35.30 C ANISOU 115 CB VAL A 63 5200 2883 5329 -78 1069 -682 C ATOM 116 CG1 VAL A 63 63.827 36.537 92.210 1.00 33.06 C ANISOU 116 CG1 VAL A 63 4800 2860 4897 45 935 -674 C ATOM 117 CG2 VAL A 63 64.781 38.307 93.665 1.00 35.60 C ANISOU 117 CG2 VAL A 63 5056 2942 5528 -58 955 -929 C ATOM 118 N LEU A 64 64.675 38.158 89.117 1.00 38.10 N ANISOU 118 N LEU A 64 6074 2991 5410 -259 1441 -280 N ATOM 119 CA LEU A 64 64.400 37.684 87.772 1.00 38.76 C ANISOU 119 CA LEU A 64 6379 3092 5252 -271 1429 -84 C ATOM 120 C LEU A 64 65.692 37.401 86.998 1.00 39.71 C ANISOU 120 C LEU A 64 6553 3114 5421 -527 1696 -169 C ATOM 121 O LEU A 64 65.812 36.360 86.365 1.00 38.85 O ANISOU 121 O LEU A 64 6444 3105 5211 -661 1708 -134 O ATOM 122 CB LEU A 64 63.522 38.681 86.998 1.00 41.11 C ANISOU 122 CB LEU A 64 7119 3093 5408 -77 1419 124 C ATOM 123 CG LEU A 64 62.917 38.101 85.707 1.00 41.91 C ANISOU 123 CG LEU A 64 7408 3309 5205 22 1311 307 C ATOM 124 CD1 LEU A 64 61.857 37.061 86.057 1.00 39.84 C ANISOU 124 CD1 LEU A 64 6826 3440 4871 171 998 264 C ATOM 125 CD2 LEU A 64 62.345 39.187 84.807 1.00 45.10 C ANISOU 125 CD2 LEU A 64 8271 3493 5371 225 1335 503 C ATOM 126 N ALA A 65 66.656 38.320 87.066 1.00 42.03 N ANISOU 126 N ALA A 65 6911 3153 5904 -755 1980 -259 N ATOM 127 CA ALA A 65 67.930 38.155 86.344 1.00 43.67 C ANISOU 127 CA ALA A 65 7101 3316 6174 -1023 2268 -400 C ATOM 128 C ALA A 65 68.782 36.995 86.885 1.00 41.75 C ANISOU 128 C ALA A 65 6444 3376 6044 -1093 2218 -639 C ATOM 129 O ALA A 65 69.494 36.344 86.120 1.00 43.07 O ANISOU 129 O ALA A 65 6612 3675 6076 -1144 2389 -697 O ATOM 130 CB ALA A 65 68.725 39.463 86.336 1.00 47.00 C ANISOU 130 CB ALA A 65 7691 3398 6766 -1278 2643 -459 C ATOM 131 N ARG A 66 68.705 36.736 88.189 1.00 39.49 N ANISOU 131 N ARG A 66 5791 3260 5951 -990 2028 -815 N ATOM 132 CA ARG A 66 69.399 35.589 88.776 1.00 38.07 C ANISOU 132 CA ARG A 66 5313 3346 5805 -989 1900 -1017 C ATOM 133 C ARG A 66 68.752 34.272 88.331 1.00 35.96 C ANISOU 133 C ARG A 66 5122 3272 5269 -799 1722 -934 C ATOM 134 O ARG A 66 69.433 33.294 88.056 1.00 35.18 O ANISOU 134 O ARG A 66 4937 3228 5199 -903 1721 -988 O ATOM 135 CB ARG A 66 69.408 35.665 90.301 1.00 36.84 C ANISOU 135 CB ARG A 66 4897 3271 5828 -846 1685 -1265 C ATOM 136 CG ARG A 66 70.423 36.630 90.857 1.00 39.05 C ANISOU 136 CG ARG A 66 5020 3448 6368 -992 1836 -1553 C ATOM 137 CD ARG A 66 70.264 36.755 92.362 1.00 37.99 C ANISOU 137 CD ARG A 66 4664 3425 6343 -816 1573 -1720 C ATOM 138 NE ARG A 66 71.329 37.544 92.966 1.00 40.17 N ANISOU 138 NE ARG A 66 4775 3593 6892 -948 1685 -2131 N ATOM 139 CZ ARG A 66 71.565 37.633 94.272 1.00 40.18 C ANISOU 139 CZ ARG A 66 4515 3745 7006 -813 1488 -2371 C ATOM 140 NH1 ARG A 66 70.815 36.978 95.150 1.00 37.54 N ANISOU 140 NH1 ARG A 66 4212 3499 6551 -501 1191 -2299 N ATOM 141 NH2 ARG A 66 72.561 38.404 94.710 1.00 43.18 N ANISOU 141 NH2 ARG A 66 4631 4130 7643 -987 1562 -2773 N ATOM 142 N CYS A 67 67.431 34.266 88.254 1.00 35.23 N ANISOU 142 N CYS A 67 5139 3295 4950 -670 1567 -666 N ATOM 143 CA CYS A 67 66.729 33.098 87.778 1.00 34.50 C ANISOU 143 CA CYS A 67 5144 3205 4760 -557 1405 -561 C ATOM 144 C CYS A 67 67.103 32.813 86.320 1.00 35.74 C ANISOU 144 C CYS A 67 5403 3399 4777 -727 1591 -461 C ATOM 145 O CYS A 67 67.486 31.689 85.991 1.00 35.03 O ANISOU 145 O CYS A 67 5242 3475 4591 -727 1601 -488 O ATOM 146 CB CYS A 67 65.224 33.289 87.940 1.00 34.71 C ANISOU 146 CB CYS A 67 5202 3384 4602 -226 1217 -397 C ATOM 147 SG CYS A 67 64.278 31.839 87.493 1.00 35.46 S ANISOU 147 SG CYS A 67 5378 3707 4387 -483 1322 -326 S ATOM 148 N VAL A 68 67.000 33.831 85.460 1.00 38.34 N ANISOU 148 N VAL A 68 6127 3441 4998 -748 1688 -346 N ATOM 149 CA VAL A 68 67.390 33.732 84.035 1.00 40.30 C ANISOU 149 CA VAL A 68 6563 3642 5104 -868 1986 -209 C ATOM 150 C VAL A 68 68.826 33.209 83.898 1.00 40.74 C ANISOU 150 C VAL A 68 6438 3760 5280 -1086 2148 -376 C ATOM 151 O VAL A 68 69.093 32.293 83.117 1.00 41.39 O ANISOU 151 O VAL A 68 6580 3938 5206 -1043 2196 -415 O ATOM 152 CB VAL A 68 67.247 35.101 83.301 1.00 43.69 C ANISOU 152 CB VAL A 68 7384 3793 5420 -826 2155 -11 C ATOM 153 CG1 VAL A 68 67.926 35.109 81.917 1.00 46.16 C ANISOU 153 CG1 VAL A 68 7981 3991 5565 -997 2460 67 C ATOM 154 CG2 VAL A 68 65.775 35.490 83.157 1.00 43.76 C ANISOU 154 CG2 VAL A 68 7594 3805 5226 -558 1912 164 C ATOM 155 N LYS A 69 69.729 33.786 84.677 1.00 41.27 N ANISOU 155 N LYS A 69 6295 3780 5604 -1236 2306 -571 N ATOM 156 CA LYS A 69 71.142 33.409 84.665 1.00 42.70 C ANISOU 156 CA LYS A 69 6206 4003 6013 -1386 2542 -891 C ATOM 157 C LYS A 69 71.376 31.959 85.097 1.00 40.00 C ANISOU 157 C LYS A 69 5543 3999 5656 -1297 2363 -1068 C ATOM 158 O LYS A 69 72.083 31.216 84.428 1.00 40.95 O ANISOU 158 O LYS A 69 5551 4194 5812 -1367 2491 -1239 O ATOM 159 CB LYS A 69 71.925 34.381 85.567 1.00 44.77 C ANISOU 159 CB LYS A 69 6262 4192 6557 -1563 2627 -1145 C ATOM 160 CG LYS A 69 73.343 33.975 85.961 1.00 46.27 C ANISOU 160 CG LYS A 69 6012 4526 7041 -1656 2751 -1531 C ATOM 161 CD LYS A 69 74.332 34.238 84.855 1.00 49.98 C ANISOU 161 CD LYS A 69 6520 4912 7555 -1928 3215 -1626 C ATOM 162 CE LYS A 69 75.710 33.755 85.254 1.00 51.70 C ANISOU 162 CE LYS A 69 6220 5329 8092 -2063 3263 -2088 C ATOM 163 NZ LYS A 69 76.605 33.745 84.065 1.00 54.87 N ANISOU 163 NZ LYS A 69 6665 5682 8500 -2386 3701 -2186 N ATOM 164 N TYR A 70 70.795 31.558 86.214 1.00 37.26 N ANISOU 164 N TYR A 70 5052 3759 5345 -1005 2056 -1079 N ATOM 165 CA TYR A 70 70.959 30.186 86.713 1.00 35.29 C ANISOU 165 CA TYR A 70 4569 3742 5096 -900 1902 -1204 C ATOM 166 C TYR A 70 70.337 29.173 85.751 1.00 34.53 C ANISOU 166 C TYR A 70 4656 3713 4751 -888 1895 -1019 C ATOM 167 O TYR A 70 70.928 28.132 85.446 1.00 34.03 O ANISOU 167 O TYR A 70 4253 3880 4795 -944 2199 -1025 O ATOM 168 CB TYR A 70 70.318 30.076 88.099 1.00 32.87 C ANISOU 168 CB TYR A 70 4224 3438 4824 -699 1541 -1201 C ATOM 169 CG TYR A 70 70.594 28.797 88.856 1.00 30.97 C ANISOU 169 CG TYR A 70 3763 3433 4568 -488 1348 -1400 C ATOM 170 CD1 TYR A 70 71.537 28.769 89.867 1.00 31.46 C ANISOU 170 CD1 TYR A 70 3617 3559 4775 -407 1289 -1672 C ATOM 171 CD2 TYR A 70 69.884 27.626 88.581 1.00 29.03 C ANISOU 171 CD2 TYR A 70 3658 3273 4096 -387 1316 -1196 C ATOM 172 CE1 TYR A 70 71.797 27.608 90.574 1.00 30.73 C ANISOU 172 CE1 TYR A 70 3443 3624 4606 -244 1100 -1771 C ATOM 173 CE2 TYR A 70 70.143 26.450 89.281 1.00 28.14 C ANISOU 173 CE2 TYR A 70 3451 3281 3957 -239 1121 -1332 C ATOM 174 CZ TYR A 70 71.103 26.445 90.277 1.00 28.89 C ANISOU 174 CZ TYR A 70 3366 3430 4180 -119 1044 -1543 C ATOM 175 OH TYR A 70 71.374 25.297 90.983 1.00 27.13 O ANISOU 175 OH TYR A 70 3093 3308 3904 -1 866 -1802 O ATOM 176 N THR A 71 69.131 29.469 85.282 1.00 35.13 N ANISOU 176 N THR A 71 4970 3747 4630 -778 1688 -681 N ATOM 177 CA THR A 71 68.369 28.479 84.515 1.00 35.19 C ANISOU 177 CA THR A 71 5156 3784 4429 -713 1551 -646 C ATOM 178 C THR A 71 68.884 28.281 83.118 1.00 37.80 C ANISOU 178 C THR A 71 5652 4119 4589 -830 1894 -597 C ATOM 179 O THR A 71 68.754 27.180 82.575 1.00 39.45 O ANISOU 179 O THR A 71 6112 4115 4762 -823 1695 -570 O ATOM 180 CB THR A 71 66.865 28.813 84.423 1.00 34.45 C ANISOU 180 CB THR A 71 5218 3661 4209 -577 1473 -455 C ATOM 181 OG1 THR A 71 66.668 30.106 83.813 1.00 35.33 O ANISOU 181 OG1 THR A 71 5531 3646 4244 -688 1665 -367 O ATOM 182 CG2 THR A 71 66.243 28.738 85.807 1.00 32.69 C ANISOU 182 CG2 THR A 71 4833 3509 4075 -473 1227 -412 C ATOM 183 N GLU A 72 69.414 29.347 82.521 1.00 40.39 N ANISOU 183 N GLU A 72 6156 4213 4976 -1045 2109 -635 N ATOM 184 CA GLU A 72 69.968 29.261 81.174 1.00 42.50 C ANISOU 184 CA GLU A 72 6538 4505 5105 -1137 2383 -588 C ATOM 185 C GLU A 72 71.340 28.536 81.168 1.00 43.05 C ANISOU 185 C GLU A 72 6366 4717 5274 -1239 2485 -855 C ATOM 186 O GLU A 72 71.732 28.002 80.105 1.00 45.83 O ANISOU 186 O GLU A 72 6576 5404 5431 -1192 2928 -906 O ATOM 187 CB GLU A 72 70.028 30.643 80.496 1.00 45.91 C ANISOU 187 CB GLU A 72 7345 4628 5471 -1193 2567 -385 C ATOM 188 CG GLU A 72 71.280 31.448 80.821 1.00 48.76 C ANISOU 188 CG GLU A 72 7529 4863 6134 -1473 2829 -529 C ATOM 189 CD GLU A 72 71.283 32.881 80.370 1.00 52.52 C ANISOU 189 CD GLU A 72 8271 4920 6762 -1658 3127 -316 C ATOM 190 OE1 GLU A 72 70.248 33.351 79.866 1.00 54.74 O ANISOU 190 OE1 GLU A 72 8848 5228 6719 -1306 3026 90 O ATOM 191 OE2 GLU A 72 72.352 33.516 80.527 1.00 54.70 O ANISOU 191 OE2 GLU A 72 8496 4896 7392 -2006 3541 -284 O ATOM 192 N ILE A 73 72.044 28.490 82.318 1.00 40.76 N ANISOU 192 N ILE A 73 5816 4264 5405 -1271 2505 -1048 N ATOM 193 CA ILE A 73 73.359 27.807 82.395 1.00 41.89 C ANISOU 193 CA ILE A 73 5564 4707 5643 -1336 2620 -1285 C ATOM 194 C ILE A 73 73.399 26.455 83.106 1.00 39.62 C ANISOU 194 C ILE A 73 4989 4586 5476 -1062 2337 -1475 C ATOM 195 O ILE A 73 74.245 25.635 82.751 1.00 39.39 O ANISOU 195 O ILE A 73 4977 4491 5497 -1248 2640 -1685 O ATOM 196 CB ILE A 73 74.524 28.681 82.924 1.00 44.27 C ANISOU 196 CB ILE A 73 5675 4897 6249 -1427 2742 -1698 C ATOM 197 CG1 ILE A 73 74.446 28.860 84.439 1.00 42.99 C ANISOU 197 CG1 ILE A 73 5199 4888 6244 -1283 2510 -1783 C ATOM 198 CG2 ILE A 73 74.620 29.994 82.141 1.00 47.17 C ANISOU 198 CG2 ILE A 73 6238 5059 6623 -1739 3147 -1529 C ATOM 199 CD1 ILE A 73 75.612 29.639 85.024 1.00 45.57 C ANISOU 199 CD1 ILE A 73 5210 5195 6907 -1479 2646 -2109 C ATOM 200 N HIS A 74 72.542 26.234 84.116 1.00 37.07 N ANISOU 200 N HIS A 74 4762 4310 5012 -830 2043 -1436 N ATOM 201 CA HIS A 74 72.473 24.923 84.779 1.00 35.66 C ANISOU 201 CA HIS A 74 4425 4285 4837 -709 1785 -1494 C ATOM 202 C HIS A 74 71.418 24.079 84.102 1.00 33.29 C ANISOU 202 C HIS A 74 4454 4008 4185 -608 1779 -1266 C ATOM 203 O HIS A 74 70.234 24.370 84.221 1.00 31.44 O ANISOU 203 O HIS A 74 4380 3872 3691 -725 1689 -1077 O ATOM 204 CB HIS A 74 72.186 25.017 86.267 1.00 35.39 C ANISOU 204 CB HIS A 74 4371 4260 4814 -490 1580 -1567 C ATOM 205 CG HIS A 74 73.310 25.592 87.048 1.00 38.35 C ANISOU 205 CG HIS A 74 4376 4642 5550 -540 1474 -1859 C ATOM 206 ND1 HIS A 74 73.313 26.899 87.486 1.00 40.55 N ANISOU 206 ND1 HIS A 74 4732 4688 5984 -643 1443 -1967 N ATOM 207 CD2 HIS A 74 74.480 25.051 87.450 1.00 40.49 C ANISOU 207 CD2 HIS A 74 4355 5019 6010 -334 1457 -2091 C ATOM 208 CE1 HIS A 74 74.445 27.138 88.125 1.00 42.41 C ANISOU 208 CE1 HIS A 74 4525 5059 6530 -488 1480 -2294 C ATOM 209 NE2 HIS A 74 75.159 26.029 88.134 1.00 42.65 N ANISOU 209 NE2 HIS A 74 4271 5333 6599 -331 1448 -2430 N ATOM 210 N PRO A 75 71.849 23.033 83.382 1.00 33.16 N ANISOU 210 N PRO A 75 4433 3992 4173 -654 1738 -1304 N ATOM 211 CA PRO A 75 70.918 22.272 82.556 1.00 32.26 C ANISOU 211 CA PRO A 75 4558 3868 3828 -618 1718 -1157 C ATOM 212 C PRO A 75 69.802 21.555 83.338 1.00 29.89 C ANISOU 212 C PRO A 75 4321 3476 3558 -450 1458 -1080 C ATOM 213 O PRO A 75 68.723 21.389 82.814 1.00 28.46 O ANISOU 213 O PRO A 75 4432 3037 3341 -533 1390 -838 O ATOM 214 CB PRO A 75 71.829 21.287 81.805 1.00 33.41 C ANISOU 214 CB PRO A 75 4661 4063 3966 -634 1815 -1347 C ATOM 215 CG PRO A 75 73.087 21.231 82.558 1.00 34.32 C ANISOU 215 CG PRO A 75 4493 4269 4275 -540 1858 -1597 C ATOM 216 CD PRO A 75 73.226 22.512 83.296 1.00 34.73 C ANISOU 216 CD PRO A 75 4441 4262 4492 -621 1860 -1610 C ATOM 217 N GLU A 76 70.045 21.216 84.596 1.00 29.42 N ANISOU 217 N GLU A 76 4145 3476 3555 -298 1390 -1178 N ATOM 218 CA GLU A 76 69.047 20.528 85.419 1.00 28.55 C ANISOU 218 CA GLU A 76 4089 3351 3405 -253 1227 -1091 C ATOM 219 C GLU A 76 67.820 21.393 85.689 1.00 27.33 C ANISOU 219 C GLU A 76 3942 3210 3230 -315 1093 -805 C ATOM 220 O GLU A 76 66.788 20.856 86.020 1.00 26.23 O ANISOU 220 O GLU A 76 3997 2936 3031 -315 940 -621 O ATOM 221 CB GLU A 76 69.616 20.111 86.781 1.00 29.02 C ANISOU 221 CB GLU A 76 4076 3445 3503 -53 1138 -1166 C ATOM 222 CG GLU A 76 70.815 19.188 86.745 1.00 30.98 C ANISOU 222 CG GLU A 76 4276 3684 3809 141 1133 -1365 C ATOM 223 CD GLU A 76 72.141 19.898 86.463 1.00 33.47 C ANISOU 223 CD GLU A 76 4267 4097 4350 28 1196 -1542 C ATOM 224 OE1 GLU A 76 72.181 21.164 86.406 1.00 34.65 O ANISOU 224 OE1 GLU A 76 4607 4107 4450 7 1109 -1501 O ATOM 225 OE2 GLU A 76 73.150 19.176 86.281 1.00 36.31 O ANISOU 225 OE2 GLU A 76 4443 4506 4844 249 1333 -1608 O ATOM 226 N MET A 77 67.942 22.723 85.590 1.00 27.44 N ANISOU 226 N MET A 77 3927 3218 3281 -359 1183 -824 N ATOM 227 CA MET A 77 66.817 23.624 85.818 1.00 26.79 C ANISOU 227 CA MET A 77 3941 3071 3165 -380 1128 -730 C ATOM 228 C MET A 77 66.418 24.453 84.600 1.00 28.05 C ANISOU 228 C MET A 77 4192 3228 3236 -449 1166 -575 C ATOM 229 O MET A 77 65.786 25.506 84.753 1.00 28.96 O ANISOU 229 O MET A 77 4434 3266 3301 -353 1108 -584 O ATOM 230 CB MET A 77 67.145 24.523 87.012 1.00 26.42 C ANISOU 230 CB MET A 77 3791 2963 3281 -327 1078 -764 C ATOM 231 CG MET A 77 67.525 23.747 88.274 1.00 25.77 C ANISOU 231 CG MET A 77 3604 2943 3245 -192 986 -903 C ATOM 232 SD MET A 77 66.162 22.761 88.927 1.00 24.70 S ANISOU 232 SD MET A 77 3631 2861 2890 -87 1004 -840 S ATOM 233 CE MET A 77 65.235 24.039 89.782 1.00 24.14 C ANISOU 233 CE MET A 77 3469 2701 3000 -30 857 -704 C ATOM 234 N ARG A 78 66.770 23.990 83.397 1.00 28.93 N ANISOU 234 N ARG A 78 4440 3274 3276 -557 1203 -662 N ATOM 235 CA ARG A 78 66.442 24.711 82.157 1.00 30.76 C ANISOU 235 CA ARG A 78 4836 3557 3293 -600 1303 -496 C ATOM 236 C ARG A 78 64.941 24.824 81.906 1.00 30.77 C ANISOU 236 C ARG A 78 4914 3557 3217 -485 1118 -387 C ATOM 237 O ARG A 78 64.471 25.777 81.291 1.00 32.09 O ANISOU 237 O ARG A 78 5302 3686 3202 -529 1143 -162 O ATOM 238 CB ARG A 78 67.092 24.042 80.946 1.00 32.06 C ANISOU 238 CB ARG A 78 5078 3737 3365 -681 1479 -545 C ATOM 239 CG ARG A 78 66.934 24.830 79.649 1.00 34.45 C ANISOU 239 CG ARG A 78 5635 4067 3386 -717 1570 -409 C ATOM 240 CD ARG A 78 67.702 26.134 79.658 1.00 36.02 C ANISOU 240 CD ARG A 78 5953 4028 3702 -798 1847 -401 C ATOM 241 NE ARG A 78 69.088 25.851 80.004 1.00 36.50 N ANISOU 241 NE ARG A 78 5779 4108 3979 -1008 2010 -538 N ATOM 242 CZ ARG A 78 70.030 25.381 79.169 1.00 38.57 C ANISOU 242 CZ ARG A 78 6032 4460 4161 -1034 2207 -701 C ATOM 243 NH1 ARG A 78 69.799 25.180 77.857 1.00 39.89 N ANISOU 243 NH1 ARG A 78 6473 4620 4063 -1098 2297 -586 N ATOM 244 NH2 ARG A 78 71.248 25.137 79.661 1.00 39.14 N ANISOU 244 NH2 ARG A 78 5836 4584 4451 -1079 2322 -860 N ATOM 245 N HIS A 79 64.215 23.820 82.379 1.00 29.91 N ANISOU 245 N HIS A 79 4687 3495 3180 -432 985 -426 N ATOM 246 CA HIS A 79 62.754 23.749 82.290 1.00 30.03 C ANISOU 246 CA HIS A 79 4695 3670 3041 -360 835 -366 C ATOM 247 C HIS A 79 61.999 24.879 83.030 1.00 30.07 C ANISOU 247 C HIS A 79 4645 3701 3079 -284 719 -382 C ATOM 248 O HIS A 79 60.831 25.120 82.753 1.00 31.71 O ANISOU 248 O HIS A 79 4730 4132 3185 -68 665 -357 O ATOM 249 CB HIS A 79 62.266 22.383 82.791 1.00 29.04 C ANISOU 249 CB HIS A 79 4443 3592 2998 -418 803 -528 C ATOM 250 CG HIS A 79 62.445 22.186 84.268 1.00 27.99 C ANISOU 250 CG HIS A 79 4215 3421 2998 -374 805 -554 C ATOM 251 ND1 HIS A 79 63.644 21.820 84.834 1.00 27.44 N ANISOU 251 ND1 HIS A 79 4127 3303 2995 -381 901 -588 N ATOM 252 CD2 HIS A 79 61.576 22.323 85.297 1.00 27.65 C ANISOU 252 CD2 HIS A 79 4090 3405 3010 -338 756 -547 C ATOM 253 CE1 HIS A 79 63.509 21.736 86.147 1.00 26.59 C ANISOU 253 CE1 HIS A 79 3972 3134 2997 -328 914 -607 C ATOM 254 NE2 HIS A 79 62.265 22.044 86.454 1.00 26.52 N ANISOU 254 NE2 HIS A 79 3952 3126 2995 -288 847 -531 N ATOM 255 N VAL A 80 62.657 25.545 83.967 1.00 29.25 N ANISOU 255 N VAL A 80 4525 3430 3159 -324 799 -352 N ATOM 256 CA VAL A 80 61.991 26.499 84.851 1.00 28.94 C ANISOU 256 CA VAL A 80 4409 3370 3217 -199 717 -281 C ATOM 257 C VAL A 80 61.576 27.771 84.111 1.00 30.69 C ANISOU 257 C VAL A 80 4802 3566 3291 -118 652 -114 C ATOM 258 O VAL A 80 62.348 28.332 83.333 1.00 31.53 O ANISOU 258 O VAL A 80 4986 3640 3353 -145 677 27 O ATOM 259 CB VAL A 80 62.896 26.863 86.052 1.00 27.94 C ANISOU 259 CB VAL A 80 4215 3163 3234 -221 798 -319 C ATOM 260 CG1 VAL A 80 62.290 27.997 86.884 1.00 27.96 C ANISOU 260 CG1 VAL A 80 4177 3098 3346 -168 746 -287 C ATOM 261 CG2 VAL A 80 63.111 25.637 86.924 1.00 26.64 C ANISOU 261 CG2 VAL A 80 3944 3034 3141 -260 782 -441 C ATOM 262 N ASP A 81 60.353 28.221 84.385 1.00 31.14 N ANISOU 262 N ASP A 81 4803 3657 3370 -14 497 -107 N ATOM 263 CA ASP A 81 59.838 29.462 83.829 1.00 33.04 C ANISOU 263 CA ASP A 81 5246 3818 3489 175 427 -23 C ATOM 264 C ASP A 81 60.081 30.573 84.838 1.00 32.82 C ANISOU 264 C ASP A 81 5201 3634 3632 179 456 20 C ATOM 265 O ASP A 81 59.373 30.678 85.830 1.00 32.06 O ANISOU 265 O ASP A 81 5007 3541 3632 174 348 -192 O ATOM 266 CB ASP A 81 58.344 29.306 83.511 1.00 34.42 C ANISOU 266 CB ASP A 81 5309 4154 3612 318 218 -89 C ATOM 267 CG ASP A 81 57.703 30.582 82.971 1.00 37.35 C ANISOU 267 CG ASP A 81 5834 4415 3940 539 32 95 C ATOM 268 OD1 ASP A 81 58.363 31.620 82.835 1.00 38.91 O ANISOU 268 OD1 ASP A 81 6228 4309 4245 537 34 288 O ATOM 269 OD2 ASP A 81 56.503 30.534 82.688 1.00 40.02 O ANISOU 269 OD2 ASP A 81 5919 5055 4231 839 -199 88 O ATOM 270 N CYS A 82 61.056 31.424 84.555 1.00 34.00 N ANISOU 270 N CYS A 82 5508 3633 3777 90 601 151 N ATOM 271 CA CYS A 82 61.478 32.431 85.508 1.00 34.48 C ANISOU 271 CA CYS A 82 5584 3528 3987 124 709 45 C ATOM 272 C CYS A 82 60.420 33.474 85.864 1.00 34.60 C ANISOU 272 C CYS A 82 5683 3451 4011 225 561 142 C ATOM 273 O CYS A 82 60.418 33.981 86.979 1.00 33.50 O ANISOU 273 O CYS A 82 5431 3143 4151 170 560 24 O ATOM 274 CB CYS A 82 62.778 33.081 85.039 1.00 37.29 C ANISOU 274 CB CYS A 82 6115 3733 4319 -184 1004 172 C ATOM 275 SG CYS A 82 64.200 31.981 85.341 1.00 39.21 S ANISOU 275 SG CYS A 82 6054 4302 4538 -80 966 184 S ATOM 276 N GLN A 83 59.496 33.756 84.952 1.00 36.21 N ANISOU 276 N GLN A 83 6060 3617 4078 444 445 285 N ATOM 277 CA GLN A 83 58.371 34.660 85.268 1.00 37.52 C ANISOU 277 CA GLN A 83 6249 3807 4199 690 294 236 C ATOM 278 C GLN A 83 57.448 34.035 86.318 1.00 36.01 C ANISOU 278 C GLN A 83 5742 3800 4140 735 167 91 C ATOM 279 O GLN A 83 56.989 34.721 87.225 1.00 36.60 O ANISOU 279 O GLN A 83 5994 3676 4235 754 280 133 O ATOM 280 CB GLN A 83 57.587 35.044 83.998 1.00 40.36 C ANISOU 280 CB GLN A 83 6863 4159 4311 963 112 339 C ATOM 281 CG GLN A 83 56.455 36.058 84.196 1.00 42.40 C ANISOU 281 CG GLN A 83 7166 4417 4524 1273 -92 313 C ATOM 282 CD GLN A 83 56.924 37.417 84.728 1.00 43.41 C ANISOU 282 CD GLN A 83 7559 4174 4759 1291 80 435 C ATOM 283 OE1 GLN A 83 57.820 38.044 84.152 1.00 44.64 O ANISOU 283 OE1 GLN A 83 8144 3851 4965 1233 355 536 O ATOM 284 NE2 GLN A 83 56.335 37.865 85.844 1.00 42.71 N ANISOU 284 NE2 GLN A 83 7233 4132 4863 1411 -32 335 N ATOM 285 N SER A 84 57.188 32.735 86.193 1.00 34.55 N ANISOU 285 N SER A 84 5302 3881 3942 638 100 10 N ATOM 286 CA SER A 84 56.403 32.008 87.188 1.00 33.13 C ANISOU 286 CA SER A 84 4803 3876 3906 652 41 -148 C ATOM 287 C SER A 84 57.096 32.015 88.540 1.00 31.33 C ANISOU 287 C SER A 84 4458 3569 3875 517 162 -169 C ATOM 288 O SER A 84 56.433 32.148 89.574 1.00 31.86 O ANISOU 288 O SER A 84 4551 3614 3939 586 205 -181 O ATOM 289 CB SER A 84 56.162 30.557 86.756 1.00 32.54 C ANISOU 289 CB SER A 84 4563 4005 3794 516 10 -258 C ATOM 290 OG SER A 84 55.695 30.518 85.428 1.00 34.38 O ANISOU 290 OG SER A 84 4938 4273 3852 593 -142 -209 O ATOM 291 N VAL A 85 58.417 31.864 88.532 1.00 30.14 N ANISOU 291 N VAL A 85 4409 3336 3703 366 364 -173 N ATOM 292 CA VAL A 85 59.191 31.836 89.767 1.00 28.90 C ANISOU 292 CA VAL A 85 4172 3132 3676 344 464 -232 C ATOM 293 C VAL A 85 59.042 33.158 90.505 1.00 30.05 C ANISOU 293 C VAL A 85 4392 3109 3916 466 442 -247 C ATOM 294 O VAL A 85 58.773 33.165 91.714 1.00 28.69 O ANISOU 294 O VAL A 85 4099 2845 3956 703 511 -504 O ATOM 295 CB VAL A 85 60.676 31.508 89.526 1.00 28.25 C ANISOU 295 CB VAL A 85 4130 2989 3613 147 602 -253 C ATOM 296 CG1 VAL A 85 61.526 31.779 90.759 1.00 27.67 C ANISOU 296 CG1 VAL A 85 3981 2855 3676 203 649 -345 C ATOM 297 CG2 VAL A 85 60.812 30.055 89.125 1.00 27.54 C ANISOU 297 CG2 VAL A 85 3978 3018 3467 90 617 -265 C ATOM 298 N TRP A 86 59.204 34.259 89.770 1.00 32.06 N ANISOU 298 N TRP A 86 4862 3192 4127 444 501 -119 N ATOM 299 CA TRP A 86 59.040 35.588 90.330 1.00 32.86 C ANISOU 299 CA TRP A 86 4992 3163 4330 583 441 -117 C ATOM 300 C TRP A 86 57.619 35.780 90.868 1.00 33.55 C ANISOU 300 C TRP A 86 4919 3389 4438 790 274 -159 C ATOM 301 O TRP A 86 57.456 36.233 91.997 1.00 34.17 O ANISOU 301 O TRP A 86 4889 3555 4540 843 439 -258 O ATOM 302 CB TRP A 86 59.386 36.690 89.316 1.00 34.74 C ANISOU 302 CB TRP A 86 5519 3175 4505 609 499 -3 C ATOM 303 CG TRP A 86 58.999 38.037 89.843 1.00 35.99 C ANISOU 303 CG TRP A 86 5756 3183 4732 745 495 9 C ATOM 304 CD1 TRP A 86 58.078 38.881 89.316 1.00 38.20 C ANISOU 304 CD1 TRP A 86 6269 3330 4913 980 370 122 C ATOM 305 CD2 TRP A 86 59.458 38.645 91.056 1.00 35.66 C ANISOU 305 CD2 TRP A 86 5621 3010 4915 688 529 -117 C ATOM 306 NE1 TRP A 86 57.950 39.998 90.108 1.00 39.40 N ANISOU 306 NE1 TRP A 86 6495 3313 5162 1048 351 74 N ATOM 307 CE2 TRP A 86 58.789 39.876 91.183 1.00 37.65 C ANISOU 307 CE2 TRP A 86 6040 3094 5168 886 471 -83 C ATOM 308 CE3 TRP A 86 60.379 38.273 92.045 1.00 34.21 C ANISOU 308 CE3 TRP A 86 5260 2862 4874 518 605 -277 C ATOM 309 CZ2 TRP A 86 59.008 40.740 92.253 1.00 37.85 C ANISOU 309 CZ2 TRP A 86 6008 3007 5365 897 532 -196 C ATOM 310 CZ3 TRP A 86 60.594 39.140 93.119 1.00 34.70 C ANISOU 310 CZ3 TRP A 86 5301 2826 5058 554 640 -391 C ATOM 311 CH2 TRP A 86 59.912 40.358 93.206 1.00 36.38 C ANISOU 311 CH2 TRP A 86 5640 2907 5272 740 628 -369 C ATOM 312 N ASP A 87 56.606 35.447 90.070 1.00 34.79 N ANISOU 312 N ASP A 87 5074 3665 4478 846 107 -162 N ATOM 313 CA ASP A 87 55.199 35.551 90.513 1.00 35.83 C ANISOU 313 CA ASP A 87 5032 3975 4605 1113 0 -260 C ATOM 314 C ASP A 87 54.930 34.782 91.805 1.00 34.38 C ANISOU 314 C ASP A 87 4586 3890 4586 1023 49 -349 C ATOM 315 O ASP A 87 54.229 35.285 92.697 1.00 34.89 O ANISOU 315 O ASP A 87 4473 4047 4736 1146 96 -308 O ATOM 316 CB ASP A 87 54.227 35.051 89.440 1.00 37.51 C ANISOU 316 CB ASP A 87 5175 4313 4762 1165 -211 -281 C ATOM 317 CG ASP A 87 54.190 35.937 88.208 1.00 40.34 C ANISOU 317 CG ASP A 87 5884 4560 4882 1320 -365 -125 C ATOM 318 OD1 ASP A 87 54.787 37.038 88.240 1.00 42.20 O ANISOU 318 OD1 ASP A 87 6405 4396 5232 1350 -193 -110 O ATOM 319 OD2 ASP A 87 53.565 35.529 87.201 1.00 43.01 O ANISOU 319 OD2 ASP A 87 6117 5182 5043 1223 -567 -155 O ATOM 320 N ALA A 88 55.505 33.593 91.913 1.00 32.30 N ANISOU 320 N ALA A 88 4192 3739 4340 830 161 -395 N ATOM 321 CA ALA A 88 55.380 32.786 93.120 1.00 31.56 C ANISOU 321 CA ALA A 88 3981 3723 4288 740 259 -485 C ATOM 322 C ALA A 88 56.138 33.373 94.318 1.00 30.91 C ANISOU 322 C ALA A 88 4017 3423 4303 818 337 -615 C ATOM 323 O ALA A 88 55.655 33.306 95.442 1.00 31.13 O ANISOU 323 O ALA A 88 4093 3449 4284 834 340 -788 O ATOM 324 CB ALA A 88 55.845 31.356 92.842 1.00 30.40 C ANISOU 324 CB ALA A 88 3817 3667 4066 579 356 -498 C ATOM 325 N PHE A 89 57.321 33.933 94.070 1.00 31.19 N ANISOU 325 N PHE A 89 4178 3378 4292 730 399 -515 N ATOM 326 CA PHE A 89 58.147 34.578 95.116 1.00 31.83 C ANISOU 326 CA PHE A 89 4269 3415 4410 660 398 -570 C ATOM 327 C PHE A 89 57.380 35.798 95.653 1.00 33.44 C ANISOU 327 C PHE A 89 4441 3535 4728 881 287 -594 C ATOM 328 O PHE A 89 57.144 35.932 96.855 1.00 33.93 O ANISOU 328 O PHE A 89 4344 3742 4806 1005 316 -803 O ATOM 329 CB PHE A 89 59.495 35.015 94.525 1.00 32.11 C ANISOU 329 CB PHE A 89 4367 3350 4484 628 481 -537 C ATOM 330 CG PHE A 89 60.629 35.141 95.517 1.00 32.61 C ANISOU 330 CG PHE A 89 4344 3449 4594 580 475 -741 C ATOM 331 CD1 PHE A 89 61.925 34.792 95.131 1.00 33.37 C ANISOU 331 CD1 PHE A 89 4347 3628 4704 519 513 -792 C ATOM 332 CD2 PHE A 89 60.447 35.631 96.799 1.00 32.71 C ANISOU 332 CD2 PHE A 89 4285 3458 4684 681 466 -837 C ATOM 333 CE1 PHE A 89 63.004 34.923 96.004 1.00 33.34 C ANISOU 333 CE1 PHE A 89 4333 3559 4775 457 515 -1020 C ATOM 334 CE2 PHE A 89 61.512 35.749 97.677 1.00 32.83 C ANISOU 334 CE2 PHE A 89 4289 3385 4796 691 427 -1020 C ATOM 335 CZ PHE A 89 62.791 35.393 97.283 1.00 33.07 C ANISOU 335 CZ PHE A 89 4243 3467 4854 537 463 -1155 C ATOM 336 N LYS A 90 56.966 36.653 94.733 1.00 35.18 N ANISOU 336 N LYS A 90 4780 3696 4889 947 211 -453 N ATOM 337 CA LYS A 90 56.216 37.855 95.035 1.00 37.52 C ANISOU 337 CA LYS A 90 5108 3880 5267 1155 210 -555 C ATOM 338 C LYS A 90 54.926 37.527 95.800 1.00 37.39 C ANISOU 338 C LYS A 90 4904 4086 5217 1274 93 -624 C ATOM 339 O LYS A 90 54.594 38.177 96.788 1.00 38.79 O ANISOU 339 O LYS A 90 5088 4284 5366 1619 21 -717 O ATOM 340 CB LYS A 90 55.909 38.570 93.711 1.00 40.33 C ANISOU 340 CB LYS A 90 5693 4122 5506 1226 94 -344 C ATOM 341 CG LYS A 90 55.210 39.895 93.838 1.00 43.34 C ANISOU 341 CG LYS A 90 6133 4346 5986 1509 58 -410 C ATOM 342 CD LYS A 90 55.109 40.649 92.515 1.00 47.26 C ANISOU 342 CD LYS A 90 6952 4775 6230 1536 -33 -128 C ATOM 343 CE LYS A 90 54.373 39.868 91.418 1.00 48.45 C ANISOU 343 CE LYS A 90 6970 5148 6290 1657 -257 -140 C ATOM 344 NZ LYS A 90 54.019 40.748 90.259 1.00 52.49 N ANISOU 344 NZ LYS A 90 7856 5434 6653 1915 -445 119 N ATOM 345 N GLY A 91 54.226 36.478 95.381 1.00 36.96 N ANISOU 345 N GLY A 91 4713 4177 5149 1221 139 -560 N ATOM 346 CA GLY A 91 52.986 36.073 96.042 1.00 37.27 C ANISOU 346 CA GLY A 91 4524 4373 5261 1331 177 -768 C ATOM 347 C GLY A 91 53.151 35.593 97.481 1.00 35.52 C ANISOU 347 C GLY A 91 4208 4184 5104 1235 362 -973 C ATOM 348 O GLY A 91 52.185 35.546 98.221 1.00 35.44 O ANISOU 348 O GLY A 91 4269 4012 5184 1289 485 -1255 O ATOM 349 N ALA A 92 54.370 35.220 97.873 1.00 34.17 N ANISOU 349 N ALA A 92 4207 3941 4833 1105 323 -890 N ATOM 350 CA ALA A 92 54.636 34.795 99.238 1.00 33.74 C ANISOU 350 CA ALA A 92 4148 3900 4770 1088 530 -853 C ATOM 351 C ALA A 92 54.529 35.908 100.268 1.00 34.71 C ANISOU 351 C ALA A 92 4296 4001 4888 1302 559 -940 C ATOM 352 O ALA A 92 54.153 35.628 101.391 1.00 34.45 O ANISOU 352 O ALA A 92 4431 3752 4907 1445 674 -1015 O ATOM 353 CB ALA A 92 56.006 34.150 99.338 1.00 32.63 C ANISOU 353 CB ALA A 92 4085 3761 4550 984 501 -828 C ATOM 354 N PHE A 93 54.869 37.149 99.892 1.00 35.13 N ANISOU 354 N PHE A 93 4369 3966 5010 1269 359 -940 N ATOM 355 CA PHE A 93 54.936 38.270 100.841 1.00 36.20 C ANISOU 355 CA PHE A 93 4541 3968 5246 1500 402 -1052 C ATOM 356 C PHE A 93 54.181 39.557 100.473 1.00 37.73 C ANISOU 356 C PHE A 93 4701 4120 5515 1677 334 -1080 C ATOM 357 O PHE A 93 54.012 40.417 101.328 1.00 37.91 O ANISOU 357 O PHE A 93 4515 3942 5946 1970 482 -1145 O ATOM 358 CB PHE A 93 56.406 38.608 101.145 1.00 36.01 C ANISOU 358 CB PHE A 93 4630 3826 5223 1404 340 -1106 C ATOM 359 CG PHE A 93 57.144 39.250 100.006 1.00 36.48 C ANISOU 359 CG PHE A 93 4824 3691 5344 1270 314 -1026 C ATOM 360 CD1 PHE A 93 57.261 40.628 99.933 1.00 38.23 C ANISOU 360 CD1 PHE A 93 5183 3662 5678 1408 312 -1069 C ATOM 361 CD2 PHE A 93 57.752 38.478 99.017 1.00 35.93 C ANISOU 361 CD2 PHE A 93 4774 3659 5219 1128 374 -938 C ATOM 362 CE1 PHE A 93 57.951 41.236 98.889 1.00 39.30 C ANISOU 362 CE1 PHE A 93 5458 3601 5870 1297 372 -987 C ATOM 363 CE2 PHE A 93 58.439 39.080 97.962 1.00 36.38 C ANISOU 363 CE2 PHE A 93 4940 3500 5380 1006 398 -880 C ATOM 364 CZ PHE A 93 58.538 40.461 97.893 1.00 37.93 C ANISOU 364 CZ PHE A 93 5229 3451 5733 1138 383 -894 C ATOM 365 N ILE A 94 53.767 39.709 99.216 1.00 38.38 N ANISOU 365 N ILE A 94 4736 4213 5631 1672 183 -949 N ATOM 366 CA ILE A 94 53.053 40.901 98.778 1.00 40.29 C ANISOU 366 CA ILE A 94 5143 4240 5925 1898 100 -1027 C ATOM 367 C ILE A 94 51.660 40.905 99.387 1.00 41.56 C ANISOU 367 C ILE A 94 5068 4606 6117 2042 40 -1070 C ATOM 368 O ILE A 94 50.995 39.874 99.426 1.00 41.07 O ANISOU 368 O ILE A 94 4799 4835 5971 1948 -73 -1019 O ATOM 369 CB ILE A 94 52.979 40.998 97.231 1.00 41.29 C ANISOU 369 CB ILE A 94 5401 4317 5968 1944 -24 -803 C ATOM 370 CG1 ILE A 94 54.290 41.547 96.666 1.00 41.48 C ANISOU 370 CG1 ILE A 94 5708 4047 6005 1761 5 -667 C ATOM 371 CG2 ILE A 94 51.856 41.895 96.746 1.00 43.77 C ANISOU 371 CG2 ILE A 94 5726 4626 6278 2229 -178 -820 C ATOM 372 CD1 ILE A 94 54.607 43.001 97.007 1.00 43.44 C ANISOU 372 CD1 ILE A 94 6224 3970 6311 1868 31 -659 C ATOM 373 N SER A 95 51.255 42.085 99.866 1.00 43.46 N ANISOU 373 N SER A 95 5318 4744 6449 2297 9 -1153 N ATOM 374 CA SER A 95 49.924 42.329 100.448 1.00 45.33 C ANISOU 374 CA SER A 95 5373 5180 6667 2390 1 -1319 C ATOM 375 C SER A 95 49.705 41.523 101.726 1.00 43.78 C ANISOU 375 C SER A 95 5010 5111 6512 2319 170 -1516 C ATOM 376 O SER A 95 48.585 41.140 102.042 1.00 44.12 O ANISOU 376 O SER A 95 4934 5335 6493 2526 450 -1760 O ATOM 377 CB SER A 95 48.797 42.095 99.429 1.00 47.33 C ANISOU 377 CB SER A 95 5419 5618 6943 2581 -221 -1275 C ATOM 378 OG SER A 95 49.123 42.679 98.188 1.00 48.48 O ANISOU 378 OG SER A 95 5754 5711 6955 2658 -493 -1056 O ATOM 379 N LYS A 96 50.798 41.279 102.436 1.00 41.67 N ANISOU 379 N LYS A 96 4994 4579 6258 2268 255 -1512 N ATOM 380 CA LYS A 96 50.765 40.513 103.652 1.00 41.98 C ANISOU 380 CA LYS A 96 4905 4930 6115 2120 481 -1539 C ATOM 381 C LYS A 96 51.554 41.221 104.714 1.00 42.03 C ANISOU 381 C LYS A 96 5104 4696 6169 2204 519 -1684 C ATOM 382 O LYS A 96 52.571 41.853 104.427 1.00 41.74 O ANISOU 382 O LYS A 96 5084 4433 6340 2313 538 -1677 O ATOM 383 CB LYS A 96 51.364 39.134 103.406 1.00 40.09 C ANISOU 383 CB LYS A 96 4643 4791 5798 1909 563 -1417 C ATOM 384 CG LYS A 96 50.409 38.244 102.656 1.00 40.42 C ANISOU 384 CG LYS A 96 4533 5038 5785 1838 604 -1446 C ATOM 385 CD LYS A 96 51.068 36.966 102.216 1.00 38.84 C ANISOU 385 CD LYS A 96 4371 4814 5572 1629 665 -1278 C ATOM 386 CE LYS A 96 50.046 36.091 101.480 1.00 39.74 C ANISOU 386 CE LYS A 96 4283 5088 5725 1516 690 -1307 C ATOM 387 NZ LYS A 96 50.737 35.076 100.641 1.00 38.30 N ANISOU 387 NZ LYS A 96 4231 4942 5376 1283 712 -1222 N ATOM 388 N HIS A 97 51.070 41.127 105.946 1.00 43.42 N ANISOU 388 N HIS A 97 5266 4991 6239 2195 657 -1774 N ATOM 389 CA HIS A 97 51.757 41.705 107.086 1.00 44.01 C ANISOU 389 CA HIS A 97 5404 5102 6214 2357 627 -1896 C ATOM 390 C HIS A 97 53.093 40.982 107.213 1.00 42.24 C ANISOU 390 C HIS A 97 5329 4844 5873 2201 661 -1871 C ATOM 391 O HIS A 97 53.117 39.769 107.279 1.00 41.56 O ANISOU 391 O HIS A 97 5401 4836 5552 2145 916 -1902 O ATOM 392 CB HIS A 97 50.896 41.553 108.344 1.00 45.67 C ANISOU 392 CB HIS A 97 5533 5484 6332 2528 810 -2024 C ATOM 393 CG HIS A 97 51.293 42.443 109.475 1.00 47.28 C ANISOU 393 CG HIS A 97 5878 5625 6460 2631 722 -2177 C ATOM 394 ND1 HIS A 97 52.313 42.137 110.343 1.00 46.91 N ANISOU 394 ND1 HIS A 97 6013 5551 6260 2644 733 -2217 N ATOM 395 CD2 HIS A 97 50.780 43.622 109.902 1.00 49.45 C ANISOU 395 CD2 HIS A 97 6127 5841 6819 2850 699 -2369 C ATOM 396 CE1 HIS A 97 52.429 43.092 111.246 1.00 48.95 C ANISOU 396 CE1 HIS A 97 6370 5706 6522 2807 691 -2446 C ATOM 397 NE2 HIS A 97 51.508 44.007 111.001 1.00 50.37 N ANISOU 397 NE2 HIS A 97 6371 5908 6859 2913 641 -2501 N ATOM 398 N PRO A 98 54.212 41.729 107.222 1.00 42.29 N ANISOU 398 N PRO A 98 5374 4718 5976 2212 563 -1891 N ATOM 399 CA PRO A 98 55.510 41.088 107.236 1.00 40.84 C ANISOU 399 CA PRO A 98 5319 4504 5691 2124 430 -1848 C ATOM 400 C PRO A 98 55.943 40.557 108.601 1.00 41.32 C ANISOU 400 C PRO A 98 5478 4728 5493 2160 486 -1997 C ATOM 401 O PRO A 98 57.119 40.285 108.790 1.00 40.40 O ANISOU 401 O PRO A 98 5505 4694 5149 2185 422 -2133 O ATOM 402 CB PRO A 98 56.444 42.211 106.762 1.00 41.30 C ANISOU 402 CB PRO A 98 5387 4369 5933 2036 299 -1986 C ATOM 403 CG PRO A 98 55.813 43.452 107.274 1.00 43.08 C ANISOU 403 CG PRO A 98 5631 4462 6275 2220 273 -2053 C ATOM 404 CD PRO A 98 54.336 43.202 107.183 1.00 43.46 C ANISOU 404 CD PRO A 98 5582 4669 6261 2330 384 -1985 C ATOM 405 N CYS A 99 55.026 40.396 109.544 1.00 42.45 N ANISOU 405 N CYS A 99 5612 4976 5539 2315 623 -2056 N ATOM 406 CA CYS A 99 55.309 39.643 110.775 1.00 43.31 C ANISOU 406 CA CYS A 99 5871 5204 5379 2433 705 -2111 C ATOM 407 C CYS A 99 54.482 38.357 110.874 1.00 42.89 C ANISOU 407 C CYS A 99 5891 5190 5213 2475 941 -1949 C ATOM 408 O CYS A 99 54.558 37.662 111.882 1.00 43.49 O ANISOU 408 O CYS A 99 6213 5287 5024 2781 1197 -2038 O ATOM 409 CB CYS A 99 55.093 40.531 112.015 1.00 45.51 C ANISOU 409 CB CYS A 99 6232 5473 5585 2659 676 -2326 C ATOM 410 SG CYS A 99 56.325 41.840 112.256 1.00 46.49 S ANISOU 410 SG CYS A 99 6251 5522 5888 2729 549 -2742 S ATOM 411 N ASP A 100 53.704 38.043 109.834 1.00 42.75 N ANISOU 411 N ASP A 100 5665 5241 5336 2283 951 -1825 N ATOM 412 CA ASP A 100 52.831 36.865 109.831 1.00 43.83 C ANISOU 412 CA ASP A 100 5863 5405 5383 2103 1195 -1717 C ATOM 413 C ASP A 100 53.063 35.968 108.617 1.00 42.11 C ANISOU 413 C ASP A 100 5540 5278 5178 1951 1218 -1561 C ATOM 414 O ASP A 100 52.150 35.270 108.160 1.00 42.73 O ANISOU 414 O ASP A 100 5295 5520 5419 1874 1401 -1544 O ATOM 415 CB ASP A 100 51.346 37.272 109.923 1.00 46.09 C ANISOU 415 CB ASP A 100 5894 5864 5754 2162 1358 -1810 C ATOM 416 CG ASP A 100 50.461 36.147 110.480 1.00 48.37 C ANISOU 416 CG ASP A 100 6229 6190 5957 2022 1753 -1799 C ATOM 417 OD1 ASP A 100 51.039 35.168 110.974 1.00 49.84 O ANISOU 417 OD1 ASP A 100 6682 6302 5952 2005 1734 -1614 O ATOM 418 OD2 ASP A 100 49.210 36.202 110.415 1.00 52.05 O ANISOU 418 OD2 ASP A 100 6262 7101 6413 2057 1644 -2106 O ATOM 419 N ILE A 101 54.294 35.931 108.127 1.00 40.47 N ANISOU 419 N ILE A 101 5404 5061 4912 1836 997 -1494 N ATOM 420 CA ILE A 101 54.609 35.054 106.996 1.00 38.83 C ANISOU 420 CA ILE A 101 5131 4774 4846 1714 983 -1377 C ATOM 421 C ILE A 101 54.752 33.628 107.506 1.00 39.12 C ANISOU 421 C ILE A 101 5360 4825 4680 1677 1252 -1323 C ATOM 422 O ILE A 101 55.316 33.404 108.582 1.00 41.18 O ANISOU 422 O ILE A 101 5744 5323 4581 1648 1205 -1481 O ATOM 423 CB ILE A 101 55.884 35.496 106.263 1.00 37.53 C ANISOU 423 CB ILE A 101 5031 4471 4757 1667 782 -1359 C ATOM 424 CG1 ILE A 101 55.830 36.991 105.899 1.00 37.74 C ANISOU 424 CG1 ILE A 101 4927 4442 4970 1703 636 -1408 C ATOM 425 CG2 ILE A 101 56.093 34.656 105.010 1.00 36.13 C ANISOU 425 CG2 ILE A 101 4808 4334 4584 1439 749 -1209 C ATOM 426 CD1 ILE A 101 54.641 37.427 105.065 1.00 37.99 C ANISOU 426 CD1 ILE A 101 4804 4453 5175 1702 663 -1358 C ATOM 427 N THR A 102 54.218 32.668 106.752 1.00 39.10 N ANISOU 427 N THR A 102 5289 4880 4687 1480 1309 -1225 N ATOM 428 CA THR A 102 54.346 31.234 107.070 1.00 40.09 C ANISOU 428 CA THR A 102 5697 4904 4631 1390 1491 -1131 C ATOM 429 C THR A 102 55.152 30.525 105.987 1.00 38.33 C ANISOU 429 C THR A 102 5431 4679 4453 1244 1379 -1028 C ATOM 430 O THR A 102 55.369 31.065 104.913 1.00 36.06 O ANISOU 430 O THR A 102 4811 4402 4488 1006 1317 -1088 O ATOM 431 CB THR A 102 52.968 30.527 107.157 1.00 41.51 C ANISOU 431 CB THR A 102 5838 5125 4809 1246 1828 -1126 C ATOM 432 OG1 THR A 102 52.334 30.495 105.865 1.00 39.40 O ANISOU 432 OG1 THR A 102 5059 4984 4927 1127 1876 -1126 O ATOM 433 CG2 THR A 102 52.065 31.231 108.155 1.00 43.95 C ANISOU 433 CG2 THR A 102 6057 5561 5081 1378 2001 -1234 C ATOM 434 N GLU A 103 55.549 29.289 106.265 1.00 39.67 N ANISOU 434 N GLU A 103 5795 4773 4504 1331 1440 -861 N ATOM 435 CA GLU A 103 56.225 28.445 105.260 1.00 39.31 C ANISOU 435 CA GLU A 103 5917 4633 4382 1219 1444 -846 C ATOM 436 C GLU A 103 55.294 28.129 104.086 1.00 38.26 C ANISOU 436 C GLU A 103 5681 4243 4612 1048 1476 -854 C ATOM 437 O GLU A 103 55.729 28.107 102.931 1.00 36.10 O ANISOU 437 O GLU A 103 5373 3762 4580 1271 1316 -826 O ATOM 438 CB GLU A 103 56.768 27.161 105.893 1.00 41.01 C ANISOU 438 CB GLU A 103 6535 4693 4352 1330 1587 -734 C ATOM 439 CG GLU A 103 57.658 27.425 107.117 1.00 43.58 C ANISOU 439 CG GLU A 103 7052 5067 4437 1554 1360 -821 C ATOM 440 CD GLU A 103 58.578 26.279 107.507 1.00 45.31 C ANISOU 440 CD GLU A 103 7619 5308 4289 1788 1154 -705 C ATOM 441 OE1 GLU A 103 58.458 25.185 106.915 1.00 46.85 O ANISOU 441 OE1 GLU A 103 7924 4980 4898 1642 1323 -616 O ATOM 442 OE2 GLU A 103 59.414 26.495 108.423 1.00 50.84 O ANISOU 442 OE2 GLU A 103 8274 6748 4293 1628 870 -444 O ATOM 443 N GLU A 104 54.009 27.961 104.379 1.00 40.87 N ANISOU 443 N GLU A 104 5875 4730 4921 820 1820 -789 N ATOM 444 CA GLU A 104 52.995 27.708 103.354 1.00 43.05 C ANISOU 444 CA GLU A 104 5993 5209 5152 622 1711 -820 C ATOM 445 C GLU A 104 52.941 28.815 102.294 1.00 40.08 C ANISOU 445 C GLU A 104 5212 4889 5127 601 1569 -978 C ATOM 446 O GLU A 104 52.760 28.516 101.109 1.00 38.16 O ANISOU 446 O GLU A 104 5121 4315 5063 518 1523 -757 O ATOM 447 CB GLU A 104 51.609 27.500 104.002 1.00 49.25 C ANISOU 447 CB GLU A 104 6445 6183 6084 430 2291 -977 C ATOM 448 CG GLU A 104 50.496 27.025 103.062 1.00 54.50 C ANISOU 448 CG GLU A 104 6889 6949 6868 -99 2038 -1085 C ATOM 449 CD GLU A 104 50.775 25.691 102.354 1.00 58.66 C ANISOU 449 CD GLU A 104 8312 6918 7057 -287 2505 -990 C ATOM 450 OE1 GLU A 104 50.484 24.626 102.953 1.00 71.35 O ANISOU 450 OE1 GLU A 104 10663 7318 9128 -778 2310 -65 O ATOM 451 OE2 GLU A 104 51.242 25.709 101.181 1.00 60.47 O ANISOU 451 OE2 GLU A 104 7903 7975 7096 -1267 2657 -1414 O ATOM 452 N ASP A 105 53.126 30.073 102.715 1.00 38.16 N ANISOU 452 N ASP A 105 4816 4824 4858 817 1427 -906 N ATOM 453 CA ASP A 105 53.292 31.214 101.786 1.00 36.47 C ANISOU 453 CA ASP A 105 4464 4595 4797 945 1142 -1000 C ATOM 454 C ASP A 105 54.362 30.973 100.709 1.00 35.06 C ANISOU 454 C ASP A 105 4262 4468 4590 858 992 -776 C ATOM 455 O ASP A 105 54.213 31.427 99.568 1.00 35.52 O ANISOU 455 O ASP A 105 4276 4514 4703 937 1050 -609 O ATOM 456 CB ASP A 105 53.642 32.498 102.547 1.00 36.10 C ANISOU 456 CB ASP A 105 4472 4491 4752 1194 1050 -999 C ATOM 457 CG ASP A 105 52.478 33.037 103.367 1.00 37.65 C ANISOU 457 CG ASP A 105 4556 4778 4968 1287 1112 -1192 C ATOM 458 OD1 ASP A 105 51.319 33.005 102.911 1.00 37.93 O ANISOU 458 OD1 ASP A 105 4370 4934 5107 1340 1296 -1433 O ATOM 459 OD2 ASP A 105 52.749 33.497 104.483 1.00 38.30 O ANISOU 459 OD2 ASP A 105 4813 4786 4951 1678 1426 -1473 O ATOM 460 N TYR A 106 55.421 30.250 101.073 1.00 33.35 N ANISOU 460 N TYR A 106 4278 4144 4246 801 1029 -806 N ATOM 461 CA TYR A 106 56.509 29.952 100.148 1.00 31.48 C ANISOU 461 CA TYR A 106 4119 3766 4073 813 836 -752 C ATOM 462 C TYR A 106 56.362 28.616 99.429 1.00 31.76 C ANISOU 462 C TYR A 106 4181 3784 4100 612 940 -733 C ATOM 463 O TYR A 106 57.216 28.257 98.624 1.00 30.37 O ANISOU 463 O TYR A 106 3877 3727 3935 428 828 -664 O ATOM 464 CB TYR A 106 57.851 30.018 100.887 1.00 30.43 C ANISOU 464 CB TYR A 106 4154 3533 3874 862 843 -797 C ATOM 465 CG TYR A 106 58.319 31.421 101.148 1.00 29.32 C ANISOU 465 CG TYR A 106 3861 3474 3803 1030 734 -896 C ATOM 466 CD1 TYR A 106 58.818 32.201 100.109 1.00 28.47 C ANISOU 466 CD1 TYR A 106 3755 3213 3849 992 556 -875 C ATOM 467 CD2 TYR A 106 58.293 31.957 102.423 1.00 29.80 C ANISOU 467 CD2 TYR A 106 3927 3518 3875 1160 806 -1008 C ATOM 468 CE1 TYR A 106 59.269 33.477 100.330 1.00 28.71 C ANISOU 468 CE1 TYR A 106 3701 3236 3971 1008 506 -955 C ATOM 469 CE2 TYR A 106 58.735 33.241 102.661 1.00 29.86 C ANISOU 469 CE2 TYR A 106 3899 3485 3959 1268 702 -1094 C ATOM 470 CZ TYR A 106 59.213 34.003 101.614 1.00 29.34 C ANISOU 470 CZ TYR A 106 3769 3304 4073 1133 552 -1078 C ATOM 471 OH TYR A 106 59.655 35.284 101.843 1.00 29.09 O ANISOU 471 OH TYR A 106 3628 3264 4161 1258 593 -1268 O ATOM 472 N GLN A 107 55.277 27.882 99.677 1.00 33.75 N ANISOU 472 N GLN A 107 4341 4056 4424 468 1131 -705 N ATOM 473 CA GLN A 107 55.153 26.549 99.096 1.00 33.87 C ANISOU 473 CA GLN A 107 4511 4091 4264 373 1249 -719 C ATOM 474 C GLN A 107 55.087 26.578 97.547 1.00 31.37 C ANISOU 474 C GLN A 107 3918 3760 4239 242 1161 -689 C ATOM 475 O GLN A 107 55.749 25.789 96.902 1.00 29.30 O ANISOU 475 O GLN A 107 3622 3673 3838 96 1151 -562 O ATOM 476 CB GLN A 107 53.992 25.770 99.734 1.00 36.97 C ANISOU 476 CB GLN A 107 4833 4545 4669 232 1659 -719 C ATOM 477 CG GLN A 107 53.903 24.298 99.365 1.00 39.76 C ANISOU 477 CG GLN A 107 5383 4696 5026 -106 1772 -848 C ATOM 478 CD GLN A 107 55.207 23.490 99.507 1.00 41.94 C ANISOU 478 CD GLN A 107 5887 5016 5031 252 1573 -785 C ATOM 479 OE1 GLN A 107 56.061 23.720 100.399 1.00 46.22 O ANISOU 479 OE1 GLN A 107 6797 5817 4946 189 1298 -1237 O ATOM 480 NE2 GLN A 107 55.367 22.517 98.599 1.00 44.96 N ANISOU 480 NE2 GLN A 107 6510 5012 5559 -34 1525 -1030 N ATOM 481 N PRO A 108 54.330 27.509 96.948 1.00 31.31 N ANISOU 481 N PRO A 108 3812 3887 4196 217 1043 -684 N ATOM 482 CA PRO A 108 54.329 27.532 95.482 1.00 31.11 C ANISOU 482 CA PRO A 108 3703 3917 4199 186 824 -743 C ATOM 483 C PRO A 108 55.712 27.761 94.851 1.00 29.29 C ANISOU 483 C PRO A 108 3687 3582 3857 287 724 -666 C ATOM 484 O PRO A 108 56.029 27.132 93.845 1.00 27.91 O ANISOU 484 O PRO A 108 3618 3170 3816 345 568 -600 O ATOM 485 CB PRO A 108 53.375 28.678 95.161 1.00 32.51 C ANISOU 485 CB PRO A 108 3718 4202 4431 351 708 -824 C ATOM 486 CG PRO A 108 52.442 28.702 96.333 1.00 33.92 C ANISOU 486 CG PRO A 108 3790 4454 4643 357 873 -867 C ATOM 487 CD PRO A 108 53.357 28.468 97.497 1.00 32.92 C ANISOU 487 CD PRO A 108 3879 4199 4427 386 1012 -778 C ATOM 488 N LEU A 109 56.522 28.634 95.462 1.00 28.60 N ANISOU 488 N LEU A 109 3650 3384 3829 356 689 -579 N ATOM 489 CA LEU A 109 57.914 28.820 95.063 1.00 27.74 C ANISOU 489 CA LEU A 109 3637 3215 3685 389 663 -570 C ATOM 490 C LEU A 109 58.763 27.547 95.249 1.00 27.22 C ANISOU 490 C LEU A 109 3663 3165 3514 367 748 -576 C ATOM 491 O LEU A 109 59.492 27.164 94.334 1.00 26.29 O ANISOU 491 O LEU A 109 3553 2876 3559 614 591 -624 O ATOM 492 CB LEU A 109 58.557 29.979 95.846 1.00 27.59 C ANISOU 492 CB LEU A 109 3615 3155 3710 490 606 -577 C ATOM 493 CG LEU A 109 60.035 30.265 95.581 1.00 26.99 C ANISOU 493 CG LEU A 109 3614 2993 3647 454 565 -574 C ATOM 494 CD1 LEU A 109 60.282 30.601 94.126 1.00 26.85 C ANISOU 494 CD1 LEU A 109 3616 2935 3649 356 526 -541 C ATOM 495 CD2 LEU A 109 60.507 31.387 96.492 1.00 27.70 C ANISOU 495 CD2 LEU A 109 3714 3035 3776 570 554 -693 C ATOM 496 N MET A 110 58.677 26.918 96.423 1.00 27.65 N ANISOU 496 N MET A 110 3747 3223 3533 349 891 -553 N ATOM 497 CA MET A 110 59.370 25.669 96.682 1.00 28.02 C ANISOU 497 CA MET A 110 3992 3151 3500 416 998 -630 C ATOM 498 C MET A 110 59.050 24.668 95.577 1.00 28.21 C ANISOU 498 C MET A 110 3994 3245 3476 235 931 -576 C ATOM 499 O MET A 110 59.952 23.975 95.073 1.00 27.08 O ANISOU 499 O MET A 110 3971 3005 3313 174 785 -733 O ATOM 500 CB MET A 110 58.965 25.039 98.011 1.00 29.82 C ANISOU 500 CB MET A 110 4372 3390 3567 534 1072 -516 C ATOM 501 CG MET A 110 59.347 25.778 99.290 1.00 31.23 C ANISOU 501 CG MET A 110 4674 3468 3721 673 927 -609 C ATOM 502 SD MET A 110 61.071 26.266 99.408 1.00 33.32 S ANISOU 502 SD MET A 110 4900 3436 4321 459 640 -540 S ATOM 503 CE MET A 110 60.916 27.997 98.983 1.00 31.63 C ANISOU 503 CE MET A 110 4487 3507 4024 674 610 -619 C ATOM 504 N LYS A 111 57.781 24.587 95.185 1.00 28.82 N ANISOU 504 N LYS A 111 3917 3446 3587 147 1035 -536 N ATOM 505 CA LYS A 111 57.380 23.607 94.167 1.00 29.81 C ANISOU 505 CA LYS A 111 4126 3512 3685 -53 1032 -556 C ATOM 506 C LYS A 111 58.004 23.903 92.781 1.00 27.60 C ANISOU 506 C LYS A 111 3786 3230 3471 -7 775 -632 C ATOM 507 O LYS A 111 58.560 23.014 92.164 1.00 26.71 O ANISOU 507 O LYS A 111 3611 3430 3107 -65 557 -806 O ATOM 508 CB LYS A 111 55.864 23.485 94.128 1.00 32.77 C ANISOU 508 CB LYS A 111 4187 3994 4269 -190 1025 -601 C ATOM 509 CG LYS A 111 55.362 22.358 93.246 1.00 35.62 C ANISOU 509 CG LYS A 111 4706 4239 4589 -383 1101 -811 C ATOM 510 CD LYS A 111 53.914 22.606 92.801 1.00 39.48 C ANISOU 510 CD LYS A 111 4636 5096 5267 -496 1064 -879 C ATOM 511 CE LYS A 111 53.182 21.352 92.370 1.00 42.42 C ANISOU 511 CE LYS A 111 5134 5325 5656 -815 1214 -982 C ATOM 512 NZ LYS A 111 51.706 21.422 92.600 1.00 46.32 N ANISOU 512 NZ LYS A 111 5148 6132 6317 -854 1333 -1046 N ATOM 513 N LEU A 112 57.971 25.151 92.333 1.00 26.55 N ANISOU 513 N LEU A 112 3472 3264 3350 -15 765 -565 N ATOM 514 CA LEU A 112 58.626 25.539 91.086 1.00 26.04 C ANISOU 514 CA LEU A 112 3492 3132 3267 9 680 -531 C ATOM 515 C LEU A 112 60.132 25.320 91.150 1.00 24.74 C ANISOU 515 C LEU A 112 3487 2864 3049 24 696 -484 C ATOM 516 O LEU A 112 60.736 24.936 90.161 1.00 24.59 O ANISOU 516 O LEU A 112 3376 2938 3030 45 699 -398 O ATOM 517 CB LEU A 112 58.346 27.008 90.743 1.00 26.70 C ANISOU 517 CB LEU A 112 3578 3208 3358 98 593 -467 C ATOM 518 CG LEU A 112 56.887 27.351 90.427 1.00 28.00 C ANISOU 518 CG LEU A 112 3620 3470 3548 111 463 -491 C ATOM 519 CD1 LEU A 112 56.726 28.838 90.144 1.00 28.75 C ANISOU 519 CD1 LEU A 112 3773 3529 3620 260 351 -417 C ATOM 520 CD2 LEU A 112 56.343 26.524 89.277 1.00 28.83 C ANISOU 520 CD2 LEU A 112 3700 3681 3570 30 435 -546 C ATOM 521 N GLY A 113 60.717 25.525 92.328 1.00 32.40 N ANISOU 521 N GLY A 113 4544 3701 4064 513 360 -1102 N ATOM 522 CA GLY A 113 62.140 25.323 92.552 1.00 31.57 C ANISOU 522 CA GLY A 113 4524 3501 3969 419 364 -1015 C ATOM 523 C GLY A 113 62.618 23.909 92.822 1.00 31.21 C ANISOU 523 C GLY A 113 4448 3420 3987 328 343 -1062 C ATOM 524 O GLY A 113 63.766 23.725 93.176 1.00 30.93 O ANISOU 524 O GLY A 113 4492 3322 3935 347 309 -992 O ATOM 525 N THR A 114 61.749 22.920 92.643 1.00 31.83 N ANISOU 525 N THR A 114 4432 3474 4185 333 320 -1218 N ATOM 526 CA THR A 114 62.066 21.529 92.884 1.00 32.27 C ANISOU 526 CA THR A 114 4433 3402 4425 221 265 -1257 C ATOM 527 C THR A 114 63.312 21.137 92.116 1.00 32.06 C ANISOU 527 C THR A 114 4435 3354 4390 248 223 -1310 C ATOM 528 O THR A 114 63.412 21.360 90.917 1.00 31.87 O ANISOU 528 O THR A 114 4358 3405 4345 304 227 -1425 O ATOM 529 CB THR A 114 60.908 20.613 92.441 1.00 33.64 C ANISOU 529 CB THR A 114 4458 3564 4757 187 232 -1432 C ATOM 530 OG1 THR A 114 59.757 20.914 93.219 1.00 33.45 O ANISOU 530 OG1 THR A 114 4440 3479 4787 61 272 -1405 O ATOM 531 CG2 THR A 114 61.245 19.157 92.640 1.00 34.54 C ANISOU 531 CG2 THR A 114 4489 3502 5132 90 219 -1468 C ATOM 532 N GLN A 115 64.241 20.518 92.824 1.00 31.94 N ANISOU 532 N GLN A 115 4457 3223 4454 187 236 -1222 N ATOM 533 CA GLN A 115 65.549 20.227 92.283 1.00 31.81 C ANISOU 533 CA GLN A 115 4460 3213 4412 221 208 -1227 C ATOM 534 C GLN A 115 66.097 18.983 92.972 1.00 32.21 C ANISOU 534 C GLN A 115 4517 3059 4661 124 221 -1210 C ATOM 535 O GLN A 115 66.357 19.014 94.176 1.00 31.85 O ANISOU 535 O GLN A 115 4396 3067 4635 43 270 -991 O ATOM 536 CB GLN A 115 66.445 21.456 92.495 1.00 30.71 C ANISOU 536 CB GLN A 115 4457 3083 4128 268 249 -1090 C ATOM 537 CG GLN A 115 67.799 21.377 91.780 1.00 30.56 C ANISOU 537 CG GLN A 115 4469 3077 4062 330 238 -1063 C ATOM 538 CD GLN A 115 68.548 22.713 91.757 1.00 29.84 C ANISOU 538 CD GLN A 115 4409 3039 3888 386 303 -957 C ATOM 539 OE1 GLN A 115 68.092 23.717 92.310 1.00 29.29 O ANISOU 539 OE1 GLN A 115 4392 2973 3763 381 345 -858 O ATOM 540 NE2 GLN A 115 69.695 22.728 91.089 1.00 29.80 N ANISOU 540 NE2 GLN A 115 4397 3087 3839 451 290 -938 N ATOM 541 N THR A 116 66.263 17.896 92.216 1.00 33.61 N ANISOU 541 N THR A 116 4638 3197 4933 169 156 -1401 N ATOM 542 CA THR A 116 66.663 16.598 92.793 1.00 34.35 C ANISOU 542 CA THR A 116 4670 3093 5289 93 131 -1399 C ATOM 543 C THR A 116 68.186 16.488 92.936 1.00 33.59 C ANISOU 543 C THR A 116 4667 3003 5089 128 152 -1339 C ATOM 544 O THR A 116 68.865 15.894 92.127 1.00 34.77 O ANISOU 544 O THR A 116 4721 3232 5255 175 177 -1412 O ATOM 545 CB THR A 116 66.129 15.407 91.988 1.00 36.18 C ANISOU 545 CB THR A 116 4719 3252 5773 80 42 -1651 C ATOM 546 OG1 THR A 116 66.425 15.605 90.598 1.00 36.49 O ANISOU 546 OG1 THR A 116 4669 3549 5646 287 -32 -1922 O ATOM 547 CG2 THR A 116 64.604 15.250 92.208 1.00 37.32 C ANISOU 547 CG2 THR A 116 4737 3353 6090 43 88 -1699 C ATOM 548 N VAL A 117 68.693 17.057 94.010 1.00 32.50 N ANISOU 548 N VAL A 117 4615 2849 4883 91 194 -1103 N ATOM 549 CA VAL A 117 70.124 17.126 94.276 1.00 31.37 C ANISOU 549 CA VAL A 117 4607 2632 4680 122 209 -1031 C ATOM 550 C VAL A 117 70.655 15.815 94.881 1.00 32.02 C ANISOU 550 C VAL A 117 4655 2567 4944 99 202 -1002 C ATOM 551 O VAL A 117 69.904 15.083 95.541 1.00 32.90 O ANISOU 551 O VAL A 117 4676 2550 5273 126 235 -856 O ATOM 552 CB VAL A 117 70.420 18.311 95.214 1.00 30.44 C ANISOU 552 CB VAL A 117 4597 2565 4403 102 250 -876 C ATOM 553 CG1 VAL A 117 69.830 19.600 94.648 1.00 30.13 C ANISOU 553 CG1 VAL A 117 4541 2673 4232 192 246 -904 C ATOM 554 CG2 VAL A 117 69.923 18.089 96.649 1.00 30.77 C ANISOU 554 CG2 VAL A 117 4647 2565 4477 101 318 -745 C ATOM 555 N PRO A 118 71.939 15.501 94.659 1.00 31.64 N ANISOU 555 N PRO A 118 4659 2476 4887 123 168 -994 N ATOM 556 CA PRO A 118 72.434 14.270 95.319 1.00 32.49 C ANISOU 556 CA PRO A 118 4758 2437 5150 105 184 -932 C ATOM 557 C PRO A 118 72.542 14.414 96.840 1.00 31.94 C ANISOU 557 C PRO A 118 4723 2318 5094 102 251 -708 C ATOM 558 O PRO A 118 73.376 15.161 97.332 1.00 30.81 O ANISOU 558 O PRO A 118 4660 2222 4822 176 210 -679 O ATOM 559 CB PRO A 118 73.801 14.001 94.660 1.00 32.39 C ANISOU 559 CB PRO A 118 4749 2440 5115 172 121 -1008 C ATOM 560 CG PRO A 118 74.101 15.183 93.811 1.00 31.49 C ANISOU 560 CG PRO A 118 4672 2525 4768 205 106 -1072 C ATOM 561 CD PRO A 118 72.836 15.970 93.591 1.00 31.22 C ANISOU 561 CD PRO A 118 4629 2561 4671 190 105 -1084 C ATOM 562 N CYS A 119 71.681 13.686 97.546 1.00 32.92 N ANISOU 562 N CYS A 119 4798 2317 5390 86 338 -578 N ATOM 563 CA CYS A 119 71.564 13.748 99.001 1.00 33.71 C ANISOU 563 CA CYS A 119 4933 2485 5388 117 443 -348 C ATOM 564 C CYS A 119 72.891 13.572 99.752 1.00 33.22 C ANISOU 564 C CYS A 119 4968 2428 5226 178 478 -260 C ATOM 565 O CYS A 119 73.061 14.108 100.841 1.00 32.58 O ANISOU 565 O CYS A 119 4957 2345 5075 331 517 -127 O ATOM 566 CB CYS A 119 70.515 12.714 99.520 1.00 36.11 C ANISOU 566 CB CYS A 119 5070 2707 5941 8 559 -185 C ATOM 567 SG CYS A 119 70.941 10.953 99.430 1.00 38.67 S ANISOU 567 SG CYS A 119 5305 2749 6638 -8 588 -123 S ATOM 568 N ASN A 120 73.801 12.778 99.194 1.00 33.27 N ANISOU 568 N ASN A 120 4948 2363 5327 175 405 -320 N ATOM 569 CA ASN A 120 75.016 12.354 99.904 1.00 33.48 C ANISOU 569 CA ASN A 120 5014 2417 5286 261 439 -223 C ATOM 570 C ASN A 120 76.197 13.316 99.784 1.00 31.76 C ANISOU 570 C ASN A 120 4927 2341 4799 317 360 -342 C ATOM 571 O ASN A 120 77.256 13.049 100.339 1.00 31.80 O ANISOU 571 O ASN A 120 4966 2381 4736 315 347 -318 O ATOM 572 CB ASN A 120 75.447 10.936 99.446 1.00 34.66 C ANISOU 572 CB ASN A 120 5115 2340 5713 243 416 -221 C ATOM 573 CG ASN A 120 75.925 10.901 98.009 1.00 33.72 C ANISOU 573 CG ASN A 120 4984 2186 5642 207 273 -504 C ATOM 574 OD1 ASN A 120 75.526 11.730 97.196 1.00 32.43 O ANISOU 574 OD1 ASN A 120 4820 2156 5344 184 222 -692 O ATOM 575 ND2 ASN A 120 76.766 9.934 97.684 1.00 34.41 N ANISOU 575 ND2 ASN A 120 5017 2177 5878 229 258 -525 N ATOM 576 N LYS A 121 76.026 14.400 99.045 1.00 30.36 N ANISOU 576 N LYS A 121 4752 2257 4525 276 295 -499 N ATOM 577 CA LYS A 121 77.114 15.337 98.771 1.00 29.37 C ANISOU 577 CA LYS A 121 4657 2255 4245 308 240 -582 C ATOM 578 C LYS A 121 76.805 16.782 99.175 1.00 28.26 C ANISOU 578 C LYS A 121 4500 2273 3961 316 233 -581 C ATOM 579 O LYS A 121 77.294 17.717 98.566 1.00 26.90 O ANISOU 579 O LYS A 121 4303 2178 3740 361 204 -711 O ATOM 580 CB LYS A 121 77.477 15.231 97.305 1.00 29.09 C ANISOU 580 CB LYS A 121 4611 2202 4240 263 177 -722 C ATOM 581 CG LYS A 121 78.186 13.929 97.040 1.00 30.12 C ANISOU 581 CG LYS A 121 4728 2199 4516 298 142 -733 C ATOM 582 CD LYS A 121 78.764 13.838 95.654 1.00 30.21 C ANISOU 582 CD LYS A 121 4720 2259 4497 306 85 -881 C ATOM 583 CE LYS A 121 77.674 13.651 94.623 1.00 30.88 C ANISOU 583 CE LYS A 121 4716 2329 4687 273 33 -1019 C ATOM 584 NZ LYS A 121 77.088 12.273 94.623 1.00 32.36 N ANISOU 584 NZ LYS A 121 4849 2318 5126 263 21 -993 N ATOM 585 N ILE A 122 76.051 16.942 100.252 1.00 28.63 N ANISOU 585 N ILE A 122 4555 2360 3963 337 282 -475 N ATOM 586 CA ILE A 122 75.663 18.260 100.749 1.00 28.46 C ANISOU 586 CA ILE A 122 4562 2448 3804 357 295 -529 C ATOM 587 C ILE A 122 76.737 18.814 101.686 1.00 28.71 C ANISOU 587 C ILE A 122 4585 2612 3709 466 265 -591 C ATOM 588 O ILE A 122 77.231 18.106 102.575 1.00 29.62 O ANISOU 588 O ILE A 122 4695 2776 3780 550 237 -527 O ATOM 589 CB ILE A 122 74.270 18.217 101.423 1.00 29.16 C ANISOU 589 CB ILE A 122 4617 2578 3882 371 363 -420 C ATOM 590 CG1 ILE A 122 73.188 18.249 100.341 1.00 28.73 C ANISOU 590 CG1 ILE A 122 4545 2424 3945 261 362 -468 C ATOM 591 CG2 ILE A 122 74.068 19.370 102.421 1.00 29.34 C ANISOU 591 CG2 ILE A 122 4627 2760 3759 444 351 -458 C ATOM 592 CD1 ILE A 122 71.838 17.796 100.835 1.00 29.69 C ANISOU 592 CD1 ILE A 122 4608 2551 4120 241 434 -353 C ATOM 593 N LEU A 123 77.099 20.076 101.458 1.00 28.08 N ANISOU 593 N LEU A 123 4480 2563 3625 471 224 -733 N ATOM 594 CA LEU A 123 77.939 20.813 102.373 1.00 28.83 C ANISOU 594 CA LEU A 123 4542 2758 3653 543 153 -840 C ATOM 595 C LEU A 123 77.117 21.913 103.040 1.00 29.30 C ANISOU 595 C LEU A 123 4533 2918 3681 593 136 -924 C ATOM 596 O LEU A 123 76.770 22.911 102.411 1.00 28.66 O ANISOU 596 O LEU A 123 4401 2739 3746 577 150 -1044 O ATOM 597 CB LEU A 123 79.128 21.428 101.645 1.00 28.40 C ANISOU 597 CB LEU A 123 4459 2634 3697 512 106 -964 C ATOM 598 CG LEU A 123 80.072 22.296 102.502 1.00 29.25 C ANISOU 598 CG LEU A 123 4492 2838 3781 592 39 -1144 C ATOM 599 CD1 LEU A 123 80.773 21.458 103.567 1.00 30.19 C ANISOU 599 CD1 LEU A 123 4617 3115 3738 730 8 -1145 C ATOM 600 CD2 LEU A 123 81.080 22.996 101.618 1.00 28.93 C ANISOU 600 CD2 LEU A 123 4395 2672 3925 512 8 -1241 C ATOM 601 N LEU A 124 76.864 21.735 104.325 1.00 30.54 N ANISOU 601 N LEU A 124 4643 3279 3680 709 148 -890 N ATOM 602 CA LEU A 124 76.319 22.798 105.143 1.00 31.68 C ANISOU 602 CA LEU A 124 4761 3540 3733 817 121 -1028 C ATOM 603 C LEU A 124 77.487 23.715 105.583 1.00 32.82 C ANISOU 603 C LEU A 124 4783 3741 3944 868 3 -1283 C ATOM 604 O LEU A 124 78.656 23.332 105.484 1.00 32.92 O ANISOU 604 O LEU A 124 4777 3726 4003 860 -8 -1381 O ATOM 605 CB LEU A 124 75.572 22.194 106.337 1.00 32.87 C ANISOU 605 CB LEU A 124 4895 3905 3687 965 160 -879 C ATOM 606 CG LEU A 124 74.482 21.184 105.942 1.00 32.50 C ANISOU 606 CG LEU A 124 4896 3778 3674 879 283 -607 C ATOM 607 CD1 LEU A 124 73.902 20.499 107.152 1.00 34.15 C ANISOU 607 CD1 LEU A 124 5053 4199 3720 1054 371 -407 C ATOM 608 CD2 LEU A 124 73.379 21.827 105.104 1.00 31.58 C ANISOU 608 CD2 LEU A 124 4784 3536 3679 745 293 -646 C ATOM 609 N TRP A 125 77.170 24.918 106.059 1.00 33.70 N ANISOU 609 N TRP A 125 4828 3899 4074 949 -38 -1467 N ATOM 610 CA TRP A 125 78.191 25.837 106.547 1.00 35.06 C ANISOU 610 CA TRP A 125 4875 4137 4306 1009 -184 -1759 C ATOM 611 C TRP A 125 77.614 26.871 107.499 1.00 36.80 C ANISOU 611 C TRP A 125 4979 4532 4469 1163 -241 -1988 C ATOM 612 O TRP A 125 76.403 27.102 107.504 1.00 37.31 O ANISOU 612 O TRP A 125 4947 4745 4483 1110 -221 -1874 O ATOM 613 CB TRP A 125 78.888 26.533 105.380 1.00 34.22 C ANISOU 613 CB TRP A 125 4773 3724 4503 848 -181 -1849 C ATOM 614 CG TRP A 125 77.974 27.325 104.518 1.00 33.63 C ANISOU 614 CG TRP A 125 4695 3489 4592 726 -132 -1774 C ATOM 615 CD1 TRP A 125 77.309 26.886 103.418 1.00 32.26 C ANISOU 615 CD1 TRP A 125 4624 3204 4429 615 -34 -1548 C ATOM 616 CD2 TRP A 125 77.616 28.708 104.682 1.00 34.77 C ANISOU 616 CD2 TRP A 125 4737 3558 4915 770 -178 -1973 C ATOM 617 NE1 TRP A 125 76.559 27.910 102.879 1.00 32.30 N ANISOU 617 NE1 TRP A 125 4596 3071 4604 554 -20 -1554 N ATOM 618 CE2 TRP A 125 76.730 29.039 103.640 1.00 33.81 C ANISOU 618 CE2 TRP A 125 4671 3279 4894 633 -102 -1809 C ATOM 619 CE3 TRP A 125 77.971 29.699 105.607 1.00 36.75 C ANISOU 619 CE3 TRP A 125 4826 3860 5277 857 -304 -2289 C ATOM 620 CZ2 TRP A 125 76.176 30.323 103.504 1.00 34.65 C ANISOU 620 CZ2 TRP A 125 4728 3224 5211 592 -124 -1885 C ATOM 621 CZ3 TRP A 125 77.420 30.973 105.484 1.00 37.61 C ANISOU 621 CZ3 TRP A 125 4864 3799 5623 823 -303 -2398 C ATOM 622 CH2 TRP A 125 76.519 31.271 104.439 1.00 36.61 C ANISOU 622 CH2 TRP A 125 4831 3506 5571 682 -213 -2205 C ATOM 623 N SER A 126 78.479 27.495 108.301 1.00 38.70 N ANISOU 623 N SER A 126 5069 4907 4725 1278 -385 -2291 N ATOM 624 CA SER A 126 78.030 28.506 109.241 1.00 40.70 C ANISOU 624 CA SER A 126 5190 5299 4972 1454 -487 -2596 C ATOM 625 C SER A 126 79.084 29.584 109.481 1.00 42.46 C ANISOU 625 C SER A 126 5212 5451 5470 1475 -637 -2968 C ATOM 626 O SER A 126 80.179 29.291 109.999 1.00 43.35 O ANISOU 626 O SER A 126 5275 5594 5600 1632 -700 -3125 O ATOM 627 CB SER A 126 77.638 27.846 110.562 1.00 42.39 C ANISOU 627 CB SER A 126 5383 5945 4776 1708 -499 -2538 C ATOM 628 OG SER A 126 76.766 28.699 111.290 1.00 44.30 O ANISOU 628 OG SER A 126 5505 6366 4960 1918 -561 -2725 O ATOM 629 N ARG A 127 78.728 30.823 109.115 1.00 42.86 N ANISOU 629 N ARG A 127 5140 5276 5868 1437 -668 -3170 N ATOM 630 CA ARG A 127 79.581 32.026 109.250 1.00 44.90 C ANISOU 630 CA ARG A 127 5189 5377 6491 1430 -807 -3593 C ATOM 631 C ARG A 127 80.965 31.906 108.563 1.00 44.68 C ANISOU 631 C ARG A 127 5147 5146 6682 1267 -781 -3607 C ATOM 632 O ARG A 127 81.971 32.425 109.057 1.00 46.48 O ANISOU 632 O ARG A 127 5281 5261 7117 1341 -862 -4130 O ATOM 633 CB ARG A 127 79.712 32.458 110.736 1.00 47.88 C ANISOU 633 CB ARG A 127 5350 6146 6694 1715 -980 -4011 C ATOM 634 CG ARG A 127 78.513 33.227 111.307 1.00 48.92 C ANISOU 634 CG ARG A 127 5440 6351 6795 1838 -1034 -4179 C ATOM 635 CD ARG A 127 77.337 32.297 111.540 1.00 47.80 C ANISOU 635 CD ARG A 127 5477 6480 6203 1890 -918 -3785 C ATOM 636 NE ARG A 127 76.203 32.874 112.271 1.00 49.22 N ANISOU 636 NE ARG A 127 5620 6838 6243 2060 -944 -3921 N ATOM 637 CZ ARG A 127 76.138 33.079 113.596 1.00 51.86 C ANISOU 637 CZ ARG A 127 5755 7639 6308 2377 -1102 -4217 C ATOM 638 NH1 ARG A 127 77.165 32.816 114.412 1.00 53.89 N ANISOU 638 NH1 ARG A 127 5862 8200 6412 2591 -1222 -4418 N ATOM 639 NH2 ARG A 127 75.019 33.586 114.112 1.00 52.85 N ANISOU 639 NH2 ARG A 127 5846 7928 6307 2510 -1098 -4286 N ATOM 640 N ILE A 128 81.001 31.224 107.419 1.00 42.28 N ANISOU 640 N ILE A 128 5039 4607 6418 1044 -632 -3232 N ATOM 641 CA ILE A 128 82.231 30.996 106.665 1.00 41.98 C ANISOU 641 CA ILE A 128 4967 4398 6584 960 -607 -3198 C ATOM 642 C ILE A 128 81.854 30.832 105.184 1.00 39.99 C ANISOU 642 C ILE A 128 4839 3922 6433 741 -433 -2779 C ATOM 643 O ILE A 128 82.234 29.870 104.484 1.00 38.58 O ANISOU 643 O ILE A 128 4834 3692 6129 694 -332 -2513 O ATOM 644 CB ILE A 128 83.024 29.810 107.279 1.00 42.18 C ANISOU 644 CB ILE A 128 5038 4731 6256 1081 -663 -3131 C ATOM 645 CG1 ILE A 128 84.409 29.626 106.623 1.00 42.29 C ANISOU 645 CG1 ILE A 128 4996 4594 6475 992 -637 -3126 C ATOM 646 CG2 ILE A 128 82.219 28.518 107.276 1.00 40.43 C ANISOU 646 CG2 ILE A 128 5035 4671 5652 1129 -560 -2787 C ATOM 647 CD1 ILE A 128 85.426 30.667 107.067 1.00 44.86 C ANISOU 647 CD1 ILE A 128 5053 4836 7153 1018 -765 -3560 C ATOM 648 N LYS A 129 81.079 31.800 104.713 1.00 40.14 N ANISOU 648 N LYS A 129 4859 3674 6714 654 -375 -2771 N ATOM 649 CA LYS A 129 80.400 31.698 103.421 1.00 39.03 C ANISOU 649 CA LYS A 129 4823 3473 6532 539 -224 -2371 C ATOM 650 C LYS A 129 81.369 31.550 102.238 1.00 38.04 C ANISOU 650 C LYS A 129 4752 3078 6621 408 -165 -2252 C ATOM 651 O LYS A 129 81.195 30.676 101.388 1.00 35.65 O ANISOU 651 O LYS A 129 4623 2704 6217 439 -59 -1932 O ATOM 652 CB LYS A 129 79.537 32.940 103.211 1.00 40.35 C ANISOU 652 CB LYS A 129 4940 3388 7000 537 -206 -2433 C ATOM 653 CG LYS A 129 78.575 32.871 102.026 1.00 39.67 C ANISOU 653 CG LYS A 129 4972 3269 6831 407 -111 -2061 C ATOM 654 CD LYS A 129 78.313 34.266 101.448 1.00 41.42 C ANISOU 654 CD LYS A 129 5079 3160 7497 379 -27 -2033 C ATOM 655 CE LYS A 129 76.924 34.437 100.851 1.00 40.89 C ANISOU 655 CE LYS A 129 5062 3143 7328 405 43 -1854 C ATOM 656 NZ LYS A 129 76.049 35.221 101.756 1.00 42.34 N ANISOU 656 NZ LYS A 129 5197 3389 7498 462 -2 -2086 N ATOM 657 N ASP A 130 82.364 32.439 102.191 1.00 39.59 N ANISOU 657 N ASP A 130 4733 3092 7216 393 -140 -2385 N ATOM 658 CA ASP A 130 83.222 32.522 101.034 1.00 39.48 C ANISOU 658 CA ASP A 130 4662 2897 7441 280 -44 -2176 C ATOM 659 C ASP A 130 84.003 31.237 100.814 1.00 38.06 C ANISOU 659 C ASP A 130 4628 2858 6971 256 -69 -2079 C ATOM 660 O ASP A 130 84.088 30.781 99.679 1.00 37.25 O ANISOU 660 O ASP A 130 4718 2630 6805 79 -12 -1823 O ATOM 661 CB ASP A 130 84.188 33.693 101.110 1.00 42.12 C ANISOU 661 CB ASP A 130 4739 2975 8290 218 -63 -2423 C ATOM 662 CG ASP A 130 84.985 33.863 99.810 1.00 42.54 C ANISOU 662 CG ASP A 130 4711 2797 8656 25 117 -2100 C ATOM 663 OD1 ASP A 130 84.351 34.205 98.777 1.00 43.60 O ANISOU 663 OD1 ASP A 130 5038 2867 8659 -236 179 -1659 O ATOM 664 OD2 ASP A 130 86.216 33.635 99.805 1.00 42.73 O ANISOU 664 OD2 ASP A 130 4694 2588 8952 0 76 -2198 O ATOM 665 N LEU A 131 84.541 30.646 101.882 1.00 37.88 N ANISOU 665 N LEU A 131 4559 3033 6797 350 -179 -2339 N ATOM 666 CA LEU A 131 85.323 29.438 101.739 1.00 36.88 C ANISOU 666 CA LEU A 131 4515 3070 6427 379 -169 -2220 C ATOM 667 C LEU A 131 84.447 28.214 101.402 1.00 34.74 C ANISOU 667 C LEU A 131 4484 2940 5774 402 -109 -1966 C ATOM 668 O LEU A 131 84.855 27.373 100.601 1.00 33.32 O ANISOU 668 O LEU A 131 4352 2758 5548 279 -106 -1823 O ATOM 669 CB LEU A 131 86.160 29.164 102.981 1.00 38.16 C ANISOU 669 CB LEU A 131 4607 3424 6467 513 -313 -2526 C ATOM 670 CG LEU A 131 87.146 27.991 102.841 1.00 37.58 C ANISOU 670 CG LEU A 131 4607 3458 6212 543 -313 -2436 C ATOM 671 CD1 LEU A 131 88.284 28.290 101.871 1.00 38.09 C ANISOU 671 CD1 LEU A 131 4541 3367 6564 445 -250 -2383 C ATOM 672 CD2 LEU A 131 87.707 27.617 104.194 1.00 38.87 C ANISOU 672 CD2 LEU A 131 4696 3883 6189 730 -459 -2698 C ATOM 673 N ALA A 132 83.263 28.136 102.012 1.00 34.15 N ANISOU 673 N ALA A 132 4508 2948 5516 462 -141 -1976 N ATOM 674 CA ALA A 132 82.297 27.086 101.722 1.00 32.57 C ANISOU 674 CA ALA A 132 4468 2884 5022 457 -84 -1739 C ATOM 675 C ALA A 132 81.928 27.067 100.232 1.00 31.45 C ANISOU 675 C ALA A 132 4388 2591 4968 353 6 -1496 C ATOM 676 O ALA A 132 81.870 26.003 99.603 1.00 30.23 O ANISOU 676 O ALA A 132 4299 2535 4649 388 14 -1369 O ATOM 677 CB ALA A 132 81.061 27.247 102.581 1.00 32.60 C ANISOU 677 CB ALA A 132 4521 2966 4897 534 -107 -1804 C ATOM 678 N HIS A 133 81.741 28.250 99.667 1.00 32.04 N ANISOU 678 N HIS A 133 4390 2500 5281 301 70 -1484 N ATOM 679 CA HIS A 133 81.442 28.385 98.245 1.00 31.54 C ANISOU 679 CA HIS A 133 4349 2361 5275 242 201 -1241 C ATOM 680 C HIS A 133 82.627 28.141 97.314 1.00 31.45 C ANISOU 680 C HIS A 133 4313 2270 5365 227 243 -1131 C ATOM 681 O HIS A 133 82.447 27.546 96.249 1.00 30.55 O ANISOU 681 O HIS A 133 4382 2034 5192 276 317 -946 O ATOM 682 CB HIS A 133 80.773 29.729 97.972 1.00 32.48 C ANISOU 682 CB HIS A 133 4382 2320 5637 230 250 -1222 C ATOM 683 CG HIS A 133 79.403 29.819 98.562 1.00 32.38 C ANISOU 683 CG HIS A 133 4401 2381 5518 247 238 -1247 C ATOM 684 ND1 HIS A 133 78.680 30.993 98.607 1.00 33.56 N ANISOU 684 ND1 HIS A 133 4464 2405 5881 270 283 -1279 N ATOM 685 CD2 HIS A 133 78.621 28.878 99.142 1.00 31.56 C ANISOU 685 CD2 HIS A 133 4431 2422 5137 292 212 -1232 C ATOM 686 CE1 HIS A 133 77.505 30.764 99.172 1.00 32.92 C ANISOU 686 CE1 HIS A 133 4473 2432 5601 288 240 -1304 C ATOM 687 NE2 HIS A 133 77.447 29.489 99.510 1.00 31.84 N ANISOU 687 NE2 HIS A 133 4445 2472 5179 307 222 -1269 N ATOM 688 N GLN A 134 83.811 28.625 97.685 1.00 32.49 N ANISOU 688 N GLN A 134 4306 2326 5710 224 233 -1261 N ATOM 689 CA GLN A 134 85.033 28.243 96.987 1.00 32.72 C ANISOU 689 CA GLN A 134 4273 2380 5777 189 274 -1184 C ATOM 690 C GLN A 134 85.187 26.729 96.971 1.00 31.33 C ANISOU 690 C GLN A 134 4242 2392 5268 217 225 -1170 C ATOM 691 O GLN A 134 85.614 26.163 95.969 1.00 31.18 O ANISOU 691 O GLN A 134 4227 2444 5172 221 278 -1052 O ATOM 692 CB GLN A 134 86.271 28.806 97.664 1.00 34.25 C ANISOU 692 CB GLN A 134 4299 2478 6235 169 218 -1388 C ATOM 693 CG GLN A 134 86.475 30.289 97.470 1.00 36.12 C ANISOU 693 CG GLN A 134 4328 2473 6921 122 275 -1409 C ATOM 694 CD GLN A 134 87.845 30.746 97.938 1.00 37.87 C ANISOU 694 CD GLN A 134 4328 2593 7467 110 238 -1611 C ATOM 695 OE1 GLN A 134 88.852 30.094 97.689 1.00 37.58 O ANISOU 695 OE1 GLN A 134 4348 2524 7403 111 224 -1591 O ATOM 696 NE2 GLN A 134 87.888 31.889 98.599 1.00 39.79 N ANISOU 696 NE2 GLN A 134 4363 2685 8068 89 179 -1852 N ATOM 697 N PHE A 135 84.855 26.074 98.080 1.00 30.64 N ANISOU 697 N PHE A 135 4223 2406 5011 267 121 -1312 N ATOM 698 CA PHE A 135 85.016 24.648 98.159 1.00 29.80 C ANISOU 698 CA PHE A 135 4250 2424 4647 310 97 -1279 C ATOM 699 C PHE A 135 84.185 23.901 97.092 1.00 28.74 C ANISOU 699 C PHE A 135 4215 2323 4379 304 155 -1098 C ATOM 700 O PHE A 135 84.715 23.013 96.406 1.00 28.11 O ANISOU 700 O PHE A 135 4183 2244 4251 269 103 -1069 O ATOM 701 CB PHE A 135 84.686 24.113 99.550 1.00 29.86 C ANISOU 701 CB PHE A 135 4314 2550 4480 399 19 -1396 C ATOM 702 CG PHE A 135 84.956 22.659 99.681 1.00 29.44 C ANISOU 702 CG PHE A 135 4362 2577 4245 434 0 -1315 C ATOM 703 CD1 PHE A 135 86.197 22.210 100.098 1.00 30.01 C ANISOU 703 CD1 PHE A 135 4396 2712 4294 495 -57 -1420 C ATOM 704 CD2 PHE A 135 83.999 21.728 99.301 1.00 28.65 C ANISOU 704 CD2 PHE A 135 4357 2491 4036 425 35 -1179 C ATOM 705 CE1 PHE A 135 86.459 20.851 100.175 1.00 29.87 C ANISOU 705 CE1 PHE A 135 4470 2741 4137 545 -77 -1320 C ATOM 706 CE2 PHE A 135 84.250 20.378 99.379 1.00 28.58 C ANISOU 706 CE2 PHE A 135 4425 2500 3934 460 15 -1108 C ATOM 707 CZ PHE A 135 85.481 19.936 99.813 1.00 29.18 C ANISOU 707 CZ PHE A 135 4467 2630 3989 529 -29 -1175 C ATOM 708 N THR A 136 82.918 24.289 96.939 1.00 28.26 N ANISOU 708 N THR A 136 4200 2228 4307 276 196 -1034 N ATOM 709 CA THR A 136 82.057 23.641 95.964 1.00 27.62 C ANISOU 709 CA THR A 136 4194 2205 4095 284 223 -899 C ATOM 710 C THR A 136 82.390 24.020 94.525 1.00 27.85 C ANISOU 710 C THR A 136 4159 2226 4196 294 296 -765 C ATOM 711 O THR A 136 81.924 23.364 93.592 1.00 27.63 O ANISOU 711 O THR A 136 4209 2221 4065 361 310 -725 O ATOM 712 CB THR A 136 80.553 23.809 96.282 1.00 27.36 C ANISOU 712 CB THR A 136 4201 2173 4019 265 233 -882 C ATOM 713 OG1 THR A 136 80.196 25.193 96.349 1.00 28.33 O ANISOU 713 OG1 THR A 136 4265 2176 4323 278 219 -859 O ATOM 714 CG2 THR A 136 80.225 23.117 97.612 1.00 27.23 C ANISOU 714 CG2 THR A 136 4240 2212 3892 291 167 -954 C ATOM 715 N GLN A 137 83.195 25.062 94.336 1.00 28.56 N ANISOU 715 N GLN A 137 4150 2241 4458 291 343 -745 N ATOM 716 CA GLN A 137 83.734 25.365 93.013 1.00 29.25 C ANISOU 716 CA GLN A 137 4128 2372 4612 319 459 -591 C ATOM 717 C GLN A 137 84.894 24.457 92.650 1.00 29.09 C ANISOU 717 C GLN A 137 4125 2406 4520 331 432 -611 C ATOM 718 O GLN A 137 85.153 24.252 91.481 1.00 29.26 O ANISOU 718 O GLN A 137 4124 2484 4507 364 476 -524 O ATOM 719 CB GLN A 137 84.136 26.847 92.877 1.00 30.58 C ANISOU 719 CB GLN A 137 4148 2402 5067 285 561 -510 C ATOM 720 CG GLN A 137 82.963 27.821 92.864 1.00 30.92 C ANISOU 720 CG GLN A 137 4182 2367 5196 289 604 -433 C ATOM 721 CD GLN A 137 81.966 27.558 91.735 1.00 30.69 C ANISOU 721 CD GLN A 137 4199 2509 4951 365 672 -271 C ATOM 722 OE1 GLN A 137 82.349 27.498 90.561 1.00 31.76 O ANISOU 722 OE1 GLN A 137 4307 2766 4992 497 776 -138 O ATOM 723 NE2 GLN A 137 80.682 27.412 92.082 1.00 29.70 N ANISOU 723 NE2 GLN A 137 4183 2371 4729 345 625 -350 N ATOM 724 N VAL A 138 85.606 23.958 93.655 1.00 28.91 N ANISOU 724 N VAL A 138 4132 2354 4497 309 343 -758 N ATOM 725 CA VAL A 138 86.713 23.027 93.466 1.00 29.01 C ANISOU 725 CA VAL A 138 4140 2464 4417 352 313 -812 C ATOM 726 C VAL A 138 86.204 21.590 93.421 1.00 28.22 C ANISOU 726 C VAL A 138 4170 2444 4105 376 242 -845 C ATOM 727 O VAL A 138 86.516 20.857 92.480 1.00 28.31 O ANISOU 727 O VAL A 138 4214 2496 4047 434 262 -801 O ATOM 728 CB VAL A 138 87.718 23.157 94.642 1.00 29.39 C ANISOU 728 CB VAL A 138 4132 2459 4575 325 247 -969 C ATOM 729 CG1 VAL A 138 88.842 22.138 94.540 1.00 29.39 C ANISOU 729 CG1 VAL A 138 4164 2524 4479 370 202 -1035 C ATOM 730 CG2 VAL A 138 88.282 24.578 94.759 1.00 30.61 C ANISOU 730 CG2 VAL A 138 4138 2477 5015 289 309 -957 C ATOM 731 N GLN A 139 85.444 21.186 94.432 1.00 27.66 N ANISOU 731 N GLN A 139 4174 2354 3981 349 183 -924 N ATOM 732 CA GLN A 139 84.853 19.836 94.465 1.00 27.26 C ANISOU 732 CA GLN A 139 4233 2310 3815 384 136 -936 C ATOM 733 C GLN A 139 83.436 19.940 93.922 1.00 27.11 C ANISOU 733 C GLN A 139 4220 2281 3796 318 155 -914 C ATOM 734 O GLN A 139 82.467 20.068 94.668 1.00 26.81 O ANISOU 734 O GLN A 139 4237 2161 3787 222 168 -931 O ATOM 735 CB GLN A 139 84.859 19.289 95.870 1.00 27.12 C ANISOU 735 CB GLN A 139 4260 2262 3782 397 73 -984 C ATOM 736 CG GLN A 139 84.426 17.830 95.959 1.00 27.07 C ANISOU 736 CG GLN A 139 4322 2250 3712 410 28 -1008 C ATOM 737 CD GLN A 139 85.287 16.894 95.110 1.00 27.23 C ANISOU 737 CD GLN A 139 4333 2282 3730 452 3 -1024 C ATOM 738 OE1 GLN A 139 86.485 16.814 95.283 1.00 27.25 O ANISOU 738 OE1 GLN A 139 4339 2296 3716 396 -38 -1116 O ATOM 739 NE2 GLN A 139 84.667 16.188 94.200 1.00 27.36 N ANISOU 739 NE2 GLN A 139 4351 2275 3769 476 -4 -1047 N ATOM 740 N ARG A 140 83.317 19.887 92.605 1.00 27.60 N ANISOU 740 N ARG A 140 4252 2444 3787 374 185 -853 N ATOM 741 CA ARG A 140 82.095 20.351 91.940 1.00 27.95 C ANISOU 741 CA ARG A 140 4263 2547 3808 447 226 -809 C ATOM 742 C ARG A 140 80.870 19.420 92.026 1.00 28.05 C ANISOU 742 C ARG A 140 4306 2547 3803 419 176 -851 C ATOM 743 O ARG A 140 79.765 19.855 91.701 1.00 29.06 O ANISOU 743 O ARG A 140 4296 2808 3935 426 168 -786 O ATOM 744 CB ARG A 140 82.387 20.725 90.482 1.00 28.87 C ANISOU 744 CB ARG A 140 4292 2830 3844 530 273 -722 C ATOM 745 CG ARG A 140 83.545 21.734 90.323 1.00 29.46 C ANISOU 745 CG ARG A 140 4294 2883 4014 532 337 -615 C ATOM 746 CD ARG A 140 83.679 22.289 88.925 1.00 30.61 C ANISOU 746 CD ARG A 140 4332 3194 4105 648 447 -449 C ATOM 747 NE ARG A 140 82.461 22.981 88.526 1.00 30.99 N ANISOU 747 NE ARG A 140 4363 3268 4141 713 517 -361 N ATOM 748 CZ ARG A 140 82.131 24.230 88.846 1.00 31.34 C ANISOU 748 CZ ARG A 140 4375 3198 4333 666 589 -255 C ATOM 749 NH1 ARG A 140 82.948 25.000 89.588 1.00 31.71 N ANISOU 749 NH1 ARG A 140 4383 3081 4583 559 610 -222 N ATOM 750 NH2 ARG A 140 80.963 24.720 88.401 1.00 31.61 N ANISOU 750 NH2 ARG A 140 4384 3315 4310 727 633 -185 N ATOM 751 N ASP A 141 81.035 18.177 92.472 1.00 28.00 N ANISOU 751 N ASP A 141 4349 2465 3824 426 101 -958 N ATOM 752 CA ASP A 141 79.875 17.329 92.726 1.00 28.15 C ANISOU 752 CA ASP A 141 4383 2436 3874 392 64 -1014 C ATOM 753 C ASP A 141 79.203 17.606 94.086 1.00 27.80 C ANISOU 753 C ASP A 141 4411 2282 3866 341 97 -940 C ATOM 754 O ASP A 141 78.127 17.085 94.354 1.00 28.39 O ANISOU 754 O ASP A 141 4444 2368 3973 288 89 -923 O ATOM 755 CB ASP A 141 80.183 15.833 92.492 1.00 28.92 C ANISOU 755 CB ASP A 141 4486 2465 4036 405 1 -1140 C ATOM 756 CG ASP A 141 81.241 15.259 93.416 1.00 29.25 C ANISOU 756 CG ASP A 141 4564 2440 4106 413 -21 -1079 C ATOM 757 OD1 ASP A 141 81.799 15.963 94.275 1.00 29.22 O ANISOU 757 OD1 ASP A 141 4655 2400 4046 437 8 -1036 O ATOM 758 OD2 ASP A 141 81.537 14.051 93.283 1.00 30.76 O ANISOU 758 OD2 ASP A 141 4831 2507 4346 496 -91 -1188 O ATOM 759 N MET A 142 79.818 18.429 94.932 1.00 27.43 N ANISOU 759 N MET A 142 4382 2213 3824 321 119 -883 N ATOM 760 CA MET A 142 79.206 18.848 96.213 1.00 27.52 C ANISOU 760 CA MET A 142 4410 2240 3804 283 151 -832 C ATOM 761 C MET A 142 78.488 20.200 96.099 1.00 27.41 C ANISOU 761 C MET A 142 4400 2233 3781 266 169 -837 C ATOM 762 O MET A 142 78.835 21.008 95.241 1.00 27.19 O ANISOU 762 O MET A 142 4344 2166 3821 276 140 -828 O ATOM 763 CB MET A 142 80.257 18.884 97.307 1.00 27.60 C ANISOU 763 CB MET A 142 4461 2251 3775 330 139 -851 C ATOM 764 CG MET A 142 80.790 17.484 97.581 1.00 28.13 C ANISOU 764 CG MET A 142 4541 2295 3851 373 114 -825 C ATOM 765 SD MET A 142 81.903 17.360 98.966 1.00 28.51 S ANISOU 765 SD MET A 142 4604 2359 3868 510 91 -787 S ATOM 766 CE MET A 142 80.756 17.595 100.318 1.00 29.27 C ANISOU 766 CE MET A 142 4695 2570 3855 489 147 -673 C ATOM 767 N PHE A 143 77.488 20.435 96.953 1.00 27.67 N ANISOU 767 N PHE A 143 4431 2298 3784 257 192 -831 N ATOM 768 CA APHE A 143 76.850 21.736 96.888 0.50 27.75 C ANISOU 768 CA APHE A 143 4414 2312 3815 256 233 -808 C ATOM 769 CA BPHE A 143 76.539 21.572 96.880 0.50 27.76 C ANISOU 769 CA BPHE A 143 4431 2321 3794 263 222 -805 C ATOM 770 C PHE A 143 76.358 22.255 98.228 1.00 27.76 C ANISOU 770 C PHE A 143 4403 2342 3800 274 189 -836 C ATOM 771 O PHE A 143 76.121 21.528 99.193 1.00 28.04 O ANISOU 771 O PHE A 143 4380 2525 3747 295 193 -809 O ATOM 772 CB APHE A 143 75.717 21.693 95.872 0.50 27.98 C ANISOU 772 CB APHE A 143 4418 2380 3831 242 229 -786 C ATOM 773 CB BPHE A 143 75.094 21.065 96.576 0.50 28.04 C ANISOU 773 CB BPHE A 143 4459 2339 3853 212 228 -770 C ATOM 774 CG APHE A 143 74.904 20.487 96.009 0.50 28.25 C ANISOU 774 CG APHE A 143 4498 2367 3869 214 217 -790 C ATOM 775 CG BPHE A 143 74.834 20.638 95.163 0.50 28.40 C ANISOU 775 CG BPHE A 143 4495 2404 3891 204 214 -832 C ATOM 776 CD1APHE A 143 73.829 20.469 96.851 0.50 28.55 C ANISOU 776 CD1APHE A 143 4528 2419 3900 212 249 -756 C ATOM 777 CD1BPHE A 143 74.059 21.424 94.313 0.50 28.65 C ANISOU 777 CD1BPHE A 143 4478 2507 3897 239 231 -816 C ATOM 778 CD2APHE A 143 75.297 19.344 95.394 0.50 28.81 C ANISOU 778 CD2APHE A 143 4554 2424 3969 229 200 -857 C ATOM 779 CD2BPHE A 143 75.273 19.425 94.706 0.50 29.02 C ANISOU 779 CD2BPHE A 143 4571 2441 4014 237 190 -867 C ATOM 780 CE1APHE A 143 73.114 19.323 97.033 0.50 29.35 C ANISOU 780 CE1APHE A 143 4614 2475 4063 156 265 -749 C ATOM 781 CE1BPHE A 143 73.779 21.010 93.015 0.50 29.15 C ANISOU 781 CE1BPHE A 143 4494 2668 3912 294 240 -867 C ATOM 782 CE2APHE A 143 74.602 18.192 95.570 0.50 29.60 C ANISOU 782 CE2APHE A 143 4624 2458 4164 179 207 -847 C ATOM 783 CE2BPHE A 143 75.000 19.009 93.412 0.50 29.65 C ANISOU 783 CE2BPHE A 143 4609 2599 4057 252 154 -943 C ATOM 784 CZ APHE A 143 73.504 18.173 96.393 0.50 29.81 C ANISOU 784 CZ APHE A 143 4649 2458 4217 165 245 -782 C ATOM 785 CZ BPHE A 143 74.247 19.797 92.569 0.50 29.59 C ANISOU 785 CZ BPHE A 143 4552 2692 3998 307 190 -957 C ATOM 786 N THR A 144 76.310 23.577 98.268 1.00 27.61 N ANISOU 786 N THR A 144 4320 2339 3831 298 229 -870 N ATOM 787 CA THR A 144 75.713 24.314 99.381 1.00 28.00 C ANISOU 787 CA THR A 144 4370 2419 3848 299 201 -941 C ATOM 788 C THR A 144 74.291 24.688 98.974 1.00 27.54 C ANISOU 788 C THR A 144 4336 2341 3786 273 242 -907 C ATOM 789 O THR A 144 73.932 24.645 97.797 1.00 26.69 O ANISOU 789 O THR A 144 4105 2269 3764 253 306 -905 O ATOM 790 CB THR A 144 76.464 25.624 99.691 1.00 28.54 C ANISOU 790 CB THR A 144 4368 2435 4041 320 191 -1041 C ATOM 791 OG1 THR A 144 76.385 26.509 98.571 1.00 28.12 O ANISOU 791 OG1 THR A 144 4210 2312 4160 273 284 -996 O ATOM 792 CG2 THR A 144 77.923 25.333 100.037 1.00 29.02 C ANISOU 792 CG2 THR A 144 4384 2504 4138 354 154 -1120 C ATOM 793 N LEU A 145 73.512 25.129 99.947 1.00 27.89 N ANISOU 793 N LEU A 145 4353 2460 3782 290 230 -942 N ATOM 794 CA LEU A 145 72.175 25.650 99.692 1.00 27.91 C ANISOU 794 CA LEU A 145 4369 2450 3783 309 256 -905 C ATOM 795 C LEU A 145 72.158 26.698 98.574 1.00 27.65 C ANISOU 795 C LEU A 145 4297 2358 3849 294 289 -914 C ATOM 796 O LEU A 145 71.259 26.707 97.737 1.00 27.54 O ANISOU 796 O LEU A 145 4288 2391 3785 322 322 -890 O ATOM 797 CB LEU A 145 71.609 26.240 100.983 1.00 28.82 C ANISOU 797 CB LEU A 145 4443 2698 3808 378 238 -978 C ATOM 798 CG LEU A 145 70.202 26.841 100.953 1.00 29.01 C ANISOU 798 CG LEU A 145 4437 2765 3820 380 254 -970 C ATOM 799 CD1 LEU A 145 69.182 25.796 100.515 1.00 28.76 C ANISOU 799 CD1 LEU A 145 4449 2745 3731 322 288 -842 C ATOM 800 CD2 LEU A 145 69.860 27.392 102.331 1.00 30.01 C ANISOU 800 CD2 LEU A 145 4530 3011 3858 480 213 -1080 C ATOM 801 N GLU A 146 73.173 27.559 98.558 1.00 28.04 N ANISOU 801 N GLU A 146 4283 2321 4047 314 294 -946 N ATOM 802 CA GLU A 146 73.245 28.672 97.626 1.00 28.43 C ANISOU 802 CA GLU A 146 4275 2278 4248 293 329 -887 C ATOM 803 C GLU A 146 73.726 28.248 96.233 1.00 28.05 C ANISOU 803 C GLU A 146 4213 2219 4224 285 376 -771 C ATOM 804 O GLU A 146 73.701 29.055 95.299 1.00 28.75 O ANISOU 804 O GLU A 146 4194 2351 4379 367 511 -634 O ATOM 805 CB GLU A 146 74.143 29.774 98.185 1.00 29.51 C ANISOU 805 CB GLU A 146 4335 2265 4613 309 297 -1011 C ATOM 806 CG GLU A 146 73.667 30.324 99.526 1.00 30.27 C ANISOU 806 CG GLU A 146 4382 2416 4703 361 246 -1177 C ATOM 807 CD GLU A 146 74.006 29.455 100.735 1.00 30.35 C ANISOU 807 CD GLU A 146 4419 2564 4547 423 161 -1276 C ATOM 808 OE1 GLU A 146 74.944 28.633 100.632 1.00 30.14 O ANISOU 808 OE1 GLU A 146 4405 2588 4456 404 255 -1293 O ATOM 809 OE2 GLU A 146 73.345 29.601 101.801 1.00 31.08 O ANISOU 809 OE2 GLU A 146 4453 2798 4557 605 142 -1326 O ATOM 810 N ASP A 147 74.160 26.999 96.091 1.00 27.42 N ANISOU 810 N ASP A 147 4179 2224 4013 282 353 -760 N ATOM 811 CA ASP A 147 74.395 26.395 94.778 1.00 27.37 C ANISOU 811 CA ASP A 147 4209 2248 3943 291 389 -671 C ATOM 812 C ASP A 147 73.103 25.863 94.125 1.00 27.11 C ANISOU 812 C ASP A 147 4202 2304 3794 307 399 -647 C ATOM 813 O ASP A 147 73.114 25.579 92.916 1.00 27.41 O ANISOU 813 O ASP A 147 4215 2458 3738 354 432 -542 O ATOM 814 CB ASP A 147 75.433 25.272 94.895 1.00 27.07 C ANISOU 814 CB ASP A 147 4198 2228 3858 273 358 -705 C ATOM 815 CG ASP A 147 76.791 25.791 95.279 1.00 27.46 C ANISOU 815 CG ASP A 147 4193 2194 4046 270 367 -730 C ATOM 816 OD1 ASP A 147 77.401 25.311 96.275 1.00 26.97 O ANISOU 816 OD1 ASP A 147 4116 2112 4016 231 349 -794 O ATOM 817 OD2 ASP A 147 77.225 26.713 94.565 1.00 28.35 O ANISOU 817 OD2 ASP A 147 4247 2211 4310 320 499 -643 O ATOM 818 N THR A 148 72.007 25.746 94.895 1.00 26.75 N ANISOU 818 N THR A 148 4206 2248 3710 276 378 -718 N ATOM 819 CA THR A 148 70.685 25.381 94.333 1.00 26.90 C ANISOU 819 CA THR A 148 4188 2396 3636 301 386 -703 C ATOM 820 C THR A 148 70.012 26.647 93.784 1.00 27.38 C ANISOU 820 C THR A 148 4232 2470 3699 359 426 -638 C ATOM 821 O THR A 148 70.356 27.749 94.197 1.00 27.94 O ANISOU 821 O THR A 148 4321 2430 3864 286 429 -564 O ATOM 822 CB THR A 148 69.744 24.718 95.372 1.00 26.64 C ANISOU 822 CB THR A 148 4187 2351 3582 247 346 -746 C ATOM 823 OG1 THR A 148 69.300 25.695 96.322 1.00 26.56 O ANISOU 823 OG1 THR A 148 4151 2369 3570 216 371 -741 O ATOM 824 CG2 THR A 148 70.437 23.608 96.091 1.00 26.52 C ANISOU 824 CG2 THR A 148 4205 2291 3581 210 326 -763 C ATOM 825 N LEU A 149 69.024 26.486 92.901 1.00 27.68 N ANISOU 825 N LEU A 149 4226 2645 3646 415 439 -629 N ATOM 826 CA LEU A 149 68.313 27.638 92.330 1.00 28.25 C ANISOU 826 CA LEU A 149 4270 2758 3704 496 484 -553 C ATOM 827 C LEU A 149 67.736 28.561 93.388 1.00 28.26 C ANISOU 827 C LEU A 149 4275 2661 3800 464 484 -581 C ATOM 828 O LEU A 149 67.922 29.776 93.309 1.00 28.51 O ANISOU 828 O LEU A 149 4256 2664 3910 483 522 -508 O ATOM 829 CB LEU A 149 67.166 27.199 91.416 1.00 28.70 C ANISOU 829 CB LEU A 149 4289 2989 3625 579 462 -599 C ATOM 830 CG LEU A 149 66.243 28.318 90.887 1.00 29.31 C ANISOU 830 CG LEU A 149 4319 3139 3677 689 526 -537 C ATOM 831 CD1 LEU A 149 67.013 29.371 90.099 1.00 30.13 C ANISOU 831 CD1 LEU A 149 4378 3241 3826 805 617 -342 C ATOM 832 CD2 LEU A 149 65.132 27.763 90.014 1.00 29.95 C ANISOU 832 CD2 LEU A 149 4326 3436 3615 775 487 -621 C ATOM 833 N LEU A 150 67.007 27.986 94.347 1.00 28.02 N ANISOU 833 N LEU A 150 4270 2640 3736 390 445 -657 N ATOM 834 CA LEU A 150 66.283 28.790 95.350 1.00 28.32 C ANISOU 834 CA LEU A 150 4306 2662 3789 395 436 -701 C ATOM 835 C LEU A 150 67.222 29.551 96.274 1.00 28.62 C ANISOU 835 C LEU A 150 4362 2551 3962 382 417 -749 C ATOM 836 O LEU A 150 66.980 30.729 96.557 1.00 29.39 O ANISOU 836 O LEU A 150 4367 2639 4158 534 517 -815 O ATOM 837 CB LEU A 150 65.313 27.929 96.165 1.00 28.23 C ANISOU 837 CB LEU A 150 4301 2726 3696 341 406 -751 C ATOM 838 CG LEU A 150 64.097 27.342 95.412 1.00 28.39 C ANISOU 838 CG LEU A 150 4302 2825 3657 347 408 -782 C ATOM 839 CD1 LEU A 150 63.248 26.538 96.382 1.00 28.52 C ANISOU 839 CD1 LEU A 150 4294 2887 3652 283 404 -809 C ATOM 840 CD2 LEU A 150 63.241 28.400 94.739 1.00 28.81 C ANISOU 840 CD2 LEU A 150 4314 2975 3655 436 426 -753 C ATOM 841 N GLY A 151 68.315 28.903 96.689 1.00 28.48 N ANISOU 841 N GLY A 151 4351 2501 3968 347 390 -743 N ATOM 842 CA GLY A 151 69.329 29.570 97.503 1.00 28.98 C ANISOU 842 CA GLY A 151 4364 2486 4161 358 364 -837 C ATOM 843 C GLY A 151 70.048 30.676 96.752 1.00 29.75 C ANISOU 843 C GLY A 151 4369 2458 4475 376 416 -766 C ATOM 844 O GLY A 151 70.340 31.732 97.310 1.00 30.47 O ANISOU 844 O GLY A 151 4378 2446 4751 445 435 -862 O ATOM 845 N TYR A 152 70.325 30.425 95.480 1.00 29.92 N ANISOU 845 N TYR A 152 4423 2515 4431 392 436 -631 N ATOM 846 CA TYR A 152 70.998 31.395 94.616 1.00 31.30 C ANISOU 846 CA TYR A 152 4548 2550 4792 400 554 -503 C ATOM 847 C TYR A 152 70.148 32.668 94.365 1.00 32.31 C ANISOU 847 C TYR A 152 4623 2635 5015 510 626 -486 C ATOM 848 O TYR A 152 70.676 33.786 94.341 1.00 33.29 O ANISOU 848 O TYR A 152 4612 2575 5459 598 702 -455 O ATOM 849 CB TYR A 152 71.363 30.706 93.295 1.00 31.36 C ANISOU 849 CB TYR A 152 4537 2677 4700 484 621 -386 C ATOM 850 CG TYR A 152 72.068 31.584 92.284 1.00 32.93 C ANISOU 850 CG TYR A 152 4658 2796 5057 517 733 -170 C ATOM 851 CD1 TYR A 152 73.452 31.714 92.294 1.00 33.68 C ANISOU 851 CD1 TYR A 152 4672 2812 5312 482 754 -109 C ATOM 852 CD2 TYR A 152 71.348 32.260 91.302 1.00 33.97 C ANISOU 852 CD2 TYR A 152 4739 3003 5164 630 827 23 C ATOM 853 CE1 TYR A 152 74.104 32.510 91.372 1.00 35.55 C ANISOU 853 CE1 TYR A 152 4795 3013 5698 528 881 148 C ATOM 854 CE2 TYR A 152 71.980 33.056 90.376 1.00 35.98 C ANISOU 854 CE2 TYR A 152 4881 3252 5535 705 980 300 C ATOM 855 CZ TYR A 152 73.359 33.187 90.417 1.00 35.75 C ANISOU 855 CZ TYR A 152 4870 3057 5654 555 1116 522 C ATOM 856 OH TYR A 152 73.988 33.985 89.491 1.00 40.36 O ANISOU 856 OH TYR A 152 5461 3669 6205 561 1191 745 O ATOM 857 N LEU A 153 68.843 32.500 94.200 1.00 32.12 N ANISOU 857 N LEU A 153 4634 2731 4837 506 602 -484 N ATOM 858 CA LEU A 153 67.920 33.645 94.004 1.00 33.49 C ANISOU 858 CA LEU A 153 4763 2833 5125 594 630 -354 C ATOM 859 C LEU A 153 67.955 34.660 95.133 1.00 34.32 C ANISOU 859 C LEU A 153 4776 2782 5482 568 602 -523 C ATOM 860 O LEU A 153 67.941 35.871 94.893 1.00 35.52 O ANISOU 860 O LEU A 153 4850 2815 5829 555 599 -380 O ATOM 861 CB LEU A 153 66.468 33.180 93.862 1.00 32.94 C ANISOU 861 CB LEU A 153 4732 2946 4837 631 620 -375 C ATOM 862 CG LEU A 153 66.091 32.374 92.620 1.00 33.10 C ANISOU 862 CG LEU A 153 4758 3201 4615 679 631 -291 C ATOM 863 CD1 LEU A 153 64.631 31.974 92.681 1.00 32.94 C ANISOU 863 CD1 LEU A 153 4734 3370 4411 679 568 -365 C ATOM 864 CD2 LEU A 153 66.367 33.127 91.329 1.00 34.69 C ANISOU 864 CD2 LEU A 153 4899 3427 4853 805 738 -46 C ATOM 865 N ALA A 154 68.007 34.160 96.360 1.00 34.03 N ANISOU 865 N ALA A 154 4780 2787 5361 487 511 -686 N ATOM 866 CA ALA A 154 67.772 34.991 97.536 1.00 35.48 C ANISOU 866 CA ALA A 154 4933 2906 5639 524 449 -921 C ATOM 867 C ALA A 154 69.040 35.450 98.265 1.00 36.98 C ANISOU 867 C ALA A 154 5002 2950 6095 463 369 -1118 C ATOM 868 O ALA A 154 68.949 36.297 99.137 1.00 38.22 O ANISOU 868 O ALA A 154 5024 2982 6513 441 374 -1362 O ATOM 869 CB ALA A 154 66.860 34.249 98.497 1.00 34.55 C ANISOU 869 CB ALA A 154 4871 2985 5270 526 362 -1053 C ATOM 870 N ASP A 155 70.200 34.893 97.906 1.00 37.26 N ANISOU 870 N ASP A 155 5026 2955 6175 465 454 -993 N ATOM 871 CA ASP A 155 71.457 35.117 98.646 1.00 38.44 C ANISOU 871 CA ASP A 155 5099 2968 6536 405 327 -1193 C ATOM 872 C ASP A 155 71.806 36.617 98.718 1.00 40.04 C ANISOU 872 C ASP A 155 5026 2947 7239 468 374 -1225 C ATOM 873 O ASP A 155 71.797 37.312 97.701 1.00 39.23 O ANISOU 873 O ASP A 155 4767 2559 7576 500 489 -1089 O ATOM 874 CB ASP A 155 72.598 34.325 97.976 1.00 38.60 C ANISOU 874 CB ASP A 155 5122 2999 6543 434 384 -1056 C ATOM 875 CG ASP A 155 73.788 34.067 98.902 1.00 39.46 C ANISOU 875 CG ASP A 155 5118 3231 6640 661 298 -1356 C ATOM 876 OD1 ASP A 155 73.761 34.460 100.090 1.00 41.65 O ANISOU 876 OD1 ASP A 155 5607 3304 6911 376 240 -1693 O ATOM 877 OD2 ASP A 155 74.762 33.433 98.426 1.00 42.05 O ANISOU 877 OD2 ASP A 155 5248 3728 6999 575 433 -1306 O ATOM 878 N ASP A 156 72.087 37.076 99.941 1.00 41.90 N ANISOU 878 N ASP A 156 5192 3171 7553 478 205 -1571 N ATOM 879 CA ASP A 156 72.410 38.470 100.279 1.00 44.94 C ANISOU 879 CA ASP A 156 5475 3202 8397 552 147 -1771 C ATOM 880 C ASP A 156 71.291 39.492 100.052 1.00 44.80 C ANISOU 880 C ASP A 156 5409 3115 8499 522 225 -1801 C ATOM 881 O ASP A 156 71.565 40.676 100.113 1.00 46.63 O ANISOU 881 O ASP A 156 5391 3061 9266 598 264 -1838 O ATOM 882 CB ASP A 156 73.682 38.981 99.547 1.00 47.63 C ANISOU 882 CB ASP A 156 5648 3355 9091 404 356 -1647 C ATOM 883 CG ASP A 156 74.927 38.174 99.856 1.00 49.45 C ANISOU 883 CG ASP A 156 5686 3899 9204 488 228 -1603 C ATOM 884 OD1 ASP A 156 75.143 37.786 101.032 1.00 52.99 O ANISOU 884 OD1 ASP A 156 6232 4950 8949 449 220 -1810 O ATOM 885 OD2 ASP A 156 75.717 37.941 98.902 1.00 51.17 O ANISOU 885 OD2 ASP A 156 5913 4253 9274 154 479 -1484 O ATOM 886 N LEU A 157 70.055 39.065 99.801 1.00 43.02 N ANISOU 886 N LEU A 157 5348 3060 7935 588 262 -1625 N ATOM 887 CA LEU A 157 68.969 40.005 99.498 1.00 43.69 C ANISOU 887 CA LEU A 157 5391 3033 8173 609 309 -1529 C ATOM 888 C LEU A 157 68.033 40.163 100.680 1.00 43.52 C ANISOU 888 C LEU A 157 5345 3165 8024 698 142 -1800 C ATOM 889 O LEU A 157 68.026 39.348 101.586 1.00 43.20 O ANISOU 889 O LEU A 157 5322 3456 7632 641 50 -1893 O ATOM 890 CB LEU A 157 68.179 39.563 98.266 1.00 42.42 C ANISOU 890 CB LEU A 157 5367 2963 7787 640 419 -1158 C ATOM 891 CG LEU A 157 68.936 39.410 96.936 1.00 42.50 C ANISOU 891 CG LEU A 157 5390 2877 7880 609 573 -833 C ATOM 892 CD1 LEU A 157 67.956 39.010 95.844 1.00 41.40 C ANISOU 892 CD1 LEU A 157 5385 2905 7438 656 673 -515 C ATOM 893 CD2 LEU A 157 69.671 40.682 96.533 1.00 45.18 C ANISOU 893 CD2 LEU A 157 5487 2933 8746 581 675 -706 C ATOM 894 N THR A 158 67.270 41.249 100.660 1.00 44.46 N ANISOU 894 N THR A 158 5372 3182 8337 729 160 -1858 N ATOM 895 CA THR A 158 66.312 41.593 101.702 1.00 44.77 C ANISOU 895 CA THR A 158 5367 3362 8281 863 12 -2113 C ATOM 896 C THR A 158 65.056 42.024 100.982 1.00 44.26 C ANISOU 896 C THR A 158 5385 3303 8126 896 133 -1914 C ATOM 897 O THR A 158 65.120 42.640 99.925 1.00 44.60 O ANISOU 897 O THR A 158 5445 2986 8512 926 267 -1682 O ATOM 898 CB THR A 158 66.817 42.752 102.592 1.00 47.62 C ANISOU 898 CB THR A 158 5506 3518 9069 941 -108 -2521 C ATOM 899 OG1 THR A 158 68.030 42.365 103.235 1.00 47.98 O ANISOU 899 OG1 THR A 158 5446 3627 9158 832 -227 -2765 O ATOM 900 CG2 THR A 158 65.801 43.110 103.675 1.00 48.46 C ANISOU 900 CG2 THR A 158 5564 3840 9007 1057 -247 -2819 C ATOM 901 N TRP A 159 63.915 41.698 101.565 1.00 43.28 N ANISOU 901 N TRP A 159 5307 3465 7671 983 35 -2001 N ATOM 902 CA TRP A 159 62.638 41.993 100.961 1.00 42.75 C ANISOU 902 CA TRP A 159 5317 3432 7494 1041 125 -1837 C ATOM 903 C TRP A 159 61.524 41.949 102.016 1.00 42.61 C ANISOU 903 C TRP A 159 5303 3678 7208 1126 -2 -2050 C ATOM 904 O TRP A 159 61.614 41.171 102.968 1.00 41.64 O ANISOU 904 O TRP A 159 5197 3765 6857 1136 -55 -2230 O ATOM 905 CB TRP A 159 62.354 41.019 99.802 1.00 40.67 C ANISOU 905 CB TRP A 159 5218 3269 6964 1006 255 -1490 C ATOM 906 CG TRP A 159 62.184 39.606 100.207 1.00 38.65 C ANISOU 906 CG TRP A 159 5073 3349 6263 919 222 -1500 C ATOM 907 CD1 TRP A 159 61.012 38.983 100.514 1.00 37.64 C ANISOU 907 CD1 TRP A 159 5025 3481 5793 964 242 -1501 C ATOM 908 CD2 TRP A 159 63.209 38.611 100.319 1.00 37.59 C ANISOU 908 CD2 TRP A 159 4999 3250 6032 837 203 -1481 C ATOM 909 NE1 TRP A 159 61.239 37.683 100.827 1.00 36.27 N ANISOU 909 NE1 TRP A 159 4945 3478 5357 882 246 -1473 N ATOM 910 CE2 TRP A 159 62.580 37.419 100.720 1.00 36.15 C ANISOU 910 CE2 TRP A 159 4907 3358 5468 815 191 -1466 C ATOM 911 CE3 TRP A 159 64.597 38.616 100.132 1.00 37.96 C ANISOU 911 CE3 TRP A 159 5004 3141 6275 786 227 -1465 C ATOM 912 CZ2 TRP A 159 63.284 36.225 100.929 1.00 35.04 C ANISOU 912 CZ2 TRP A 159 4843 3304 5164 743 198 -1468 C ATOM 913 CZ3 TRP A 159 65.315 37.420 100.345 1.00 36.73 C ANISOU 913 CZ3 TRP A 159 4924 3089 5942 719 240 -1475 C ATOM 914 CH2 TRP A 159 64.650 36.242 100.739 1.00 35.30 C ANISOU 914 CH2 TRP A 159 4843 3181 5386 705 211 -1477 C ATOM 915 N CYS A 160 60.518 42.816 101.852 1.00 43.24 N ANISOU 915 N CYS A 160 5358 3695 7375 1194 34 -2102 N ATOM 916 CA CYS A 160 59.228 42.659 102.523 1.00 42.99 C ANISOU 916 CA CYS A 160 5333 3949 7051 1287 -43 -2174 C ATOM 917 C CYS A 160 58.140 43.496 101.854 1.00 43.39 C ANISOU 917 C CYS A 160 5407 3901 7176 1359 51 -2074 C ATOM 918 O CYS A 160 58.432 44.374 101.036 1.00 44.05 O ANISOU 918 O CYS A 160 5440 3616 7679 1378 123 -1977 O ATOM 919 CB CYS A 160 59.316 43.024 104.001 1.00 44.61 C ANISOU 919 CB CYS A 160 5396 4298 7253 1401 -206 -2596 C ATOM 920 SG CYS A 160 59.778 44.741 104.235 1.00 47.80 S ANISOU 920 SG CYS A 160 5621 4296 8244 1548 -258 -2904 S ATOM 921 N GLY A 161 56.892 43.176 102.190 1.00 49.13 N ANISOU 921 N GLY A 161 6690 3452 8526 1131 -134 -791 N ATOM 922 CA GLY A 161 55.733 43.938 101.750 1.00 52.02 C ANISOU 922 CA GLY A 161 6662 3908 9195 1007 -378 -305 C ATOM 923 C GLY A 161 55.024 44.629 102.902 1.00 53.13 C ANISOU 923 C GLY A 161 6384 3967 9834 1481 -418 -528 C ATOM 924 O GLY A 161 55.582 44.810 103.980 1.00 51.82 O ANISOU 924 O GLY A 161 6139 3654 9895 1868 -259 -1194 O ATOM 925 N GLU A 162 53.778 45.008 102.644 1.00 56.22 N ANISOU 925 N GLU A 162 6410 4531 10418 1458 -531 0 N ATOM 926 CA GLU A 162 52.911 45.690 103.605 1.00 59.04 C ANISOU 926 CA GLU A 162 6325 4833 11273 1935 -416 -79 C ATOM 927 C GLU A 162 51.526 45.048 103.547 1.00 60.39 C ANISOU 927 C GLU A 162 6302 5539 11102 1781 -515 414 C ATOM 928 O GLU A 162 51.083 44.635 102.471 1.00 61.24 O ANISOU 928 O GLU A 162 6372 6032 10861 1293 -711 1029 O ATOM 929 CB GLU A 162 52.786 47.178 103.248 1.00 64.01 C ANISOU 929 CB GLU A 162 6527 4967 12826 2218 -340 282 C ATOM 930 CG GLU A 162 54.096 47.946 103.087 1.00 64.00 C ANISOU 930 CG GLU A 162 6688 4395 13233 2218 -255 -90 C ATOM 931 CD GLU A 162 53.925 49.364 102.529 1.00 69.82 C ANISOU 931 CD GLU A 162 7054 4592 14882 2446 -132 432 C ATOM 932 OE1 GLU A 162 52.793 49.823 102.228 1.00 74.61 O ANISOU 932 OE1 GLU A 162 7155 5327 15867 2644 -75 1152 O ATOM 933 OE2 GLU A 162 54.962 50.035 102.384 1.00 70.43 O ANISOU 933 OE2 GLU A 162 7290 4161 15308 2375 -97 201 O ATOM 934 N PHE A 163 50.834 45.020 104.687 1.00 61.43 N ANISOU 934 N PHE A 163 6241 5778 11319 2160 -337 156 N ATOM 935 CA PHE A 163 49.516 44.348 104.818 1.00 63.30 C ANISOU 935 CA PHE A 163 6229 6619 11202 1994 -401 597 C ATOM 936 C PHE A 163 48.402 45.075 104.017 1.00 69.44 C ANISOU 936 C PHE A 163 6276 7684 12423 1983 -533 1615 C ATOM 937 O PHE A 163 47.508 44.431 103.452 1.00 71.47 O ANISOU 937 O PHE A 163 6316 8629 12208 1452 -740 2226 O ATOM 938 CB PHE A 163 49.178 44.086 106.328 1.00 62.73 C ANISOU 938 CB PHE A 163 6191 6543 11100 2442 -105 5 C ATOM 939 CG PHE A 163 48.432 45.215 107.020 1.00 68.01 C ANISOU 939 CG PHE A 163 6320 6925 12593 3093 214 99 C ATOM 940 CD1 PHE A 163 47.044 45.366 106.875 1.00 73.12 C ANISOU 940 CD1 PHE A 163 6325 7973 13485 3185 281 892 C ATOM 941 CD2 PHE A 163 49.118 46.116 107.843 1.00 68.90 C ANISOU 941 CD2 PHE A 163 6586 6393 13197 3555 540 -605 C ATOM 942 CE1 PHE A 163 46.372 46.412 107.510 1.00 79.12 C ANISOU 942 CE1 PHE A 163 6615 8390 15058 3884 752 1014 C ATOM 943 CE2 PHE A 163 48.449 47.154 108.485 1.00 74.99 C ANISOU 943 CE2 PHE A 163 7032 6782 14676 4087 1041 -633 C ATOM 944 CZ PHE A 163 47.075 47.308 108.315 1.00 80.04 C ANISOU 944 CZ PHE A 163 7043 7698 15671 4357 1198 211 C ATOM 945 N ASP A 164 48.518 46.397 103.876 1.00 73.25 N ANISOU 945 N ASP A 164 6396 7635 13800 2460 -356 1859 N ATOM 946 CA ASP A 164 47.454 47.220 103.260 1.00 80.84 C ANISOU 946 CA ASP A 164 6545 8797 15372 2642 -412 3002 C ATOM 947 C ASP A 164 47.762 47.720 101.828 1.00 83.37 C ANISOU 947 C ASP A 164 6706 9182 15786 2287 -720 3782 C ATOM 948 O ASP A 164 47.049 48.592 101.302 1.00 90.56 O ANISOU 948 O ASP A 164 6918 10147 17342 2573 -712 4791 O ATOM 949 CB ASP A 164 47.060 48.402 104.193 1.00 85.98 C ANISOU 949 CB ASP A 164 6807 8788 17073 3555 190 2905 C ATOM 950 CG ASP A 164 48.276 49.172 104.777 1.00 84.16 C ANISOU 950 CG ASP A 164 7105 7575 17295 3859 557 1908 C ATOM 951 OD1 ASP A 164 48.120 49.893 105.798 1.00 87.85 O ANISOU 951 OD1 ASP A 164 7561 7500 18316 4352 1119 1406 O ATOM 952 OD2 ASP A 164 49.389 49.051 104.230 1.00 79.71 O ANISOU 952 OD2 ASP A 164 6993 6817 16475 3434 289 1534 O ATOM 953 N THR A 165 48.813 47.190 101.199 1.00 78.48 N ANISOU 953 N THR A 165 6718 8514 14584 1737 -949 3382 N ATOM 954 CA THR A 165 49.199 47.599 99.832 1.00 80.86 C ANISOU 954 CA THR A 165 6983 8883 14856 1322 -1207 4050 C ATOM 955 C THR A 165 49.773 46.425 99.046 1.00 76.95 C ANISOU 955 C THR A 165 7201 8779 13258 435 -1481 3839 C ATOM 956 O THR A 165 50.115 45.400 99.613 1.00 72.54 O ANISOU 956 O THR A 165 7273 8180 12107 308 -1372 3101 O ATOM 957 CB THR A 165 50.264 48.736 99.812 1.00 80.85 C ANISOU 957 CB THR A 165 7103 7957 15659 1758 -917 3732 C ATOM 958 OG1 THR A 165 51.547 48.204 100.156 1.00 74.44 O ANISOU 958 OG1 THR A 165 6946 6903 14434 1598 -816 2647 O ATOM 959 CG2 THR A 165 49.922 49.887 100.764 1.00 84.95 C ANISOU 959 CG2 THR A 165 7231 7772 17272 2625 -427 3628 C ATOM 960 N SER A 166 49.913 46.606 97.736 1.00 79.87 N ANISOU 960 N SER A 166 7539 9419 13387 -109 -1752 4526 N ATOM 961 CA SER A 166 50.580 45.621 96.884 1.00 77.27 C ANISOU 961 CA SER A 166 7965 9341 12051 -977 -1858 4284 C ATOM 962 C SER A 166 52.012 46.055 96.551 1.00 74.19 C ANISOU 962 C SER A 166 8010 8231 11946 -819 -1638 3830 C ATOM 963 O SER A 166 52.591 45.580 95.579 1.00 74.14 O ANISOU 963 O SER A 166 8494 8352 11322 -1457 -1677 3839 O ATOM 964 CB SER A 166 49.753 45.382 95.613 1.00 83.75 C ANISOU 964 CB SER A 166 8584 11075 12160 -1890 -2313 5305 C ATOM 965 OG SER A 166 49.490 46.595 94.929 1.00 89.90 O ANISOU 965 OG SER A 166 8685 11901 13571 -1632 -2496 6304 O ATOM 966 N LYS A 167 52.582 46.949 97.362 1.00 72.43 N ANISOU 966 N LYS A 167 7585 7289 12643 -27 -1367 3398 N ATOM 967 CA LYS A 167 53.903 47.525 97.101 1.00 70.73 C ANISOU 967 CA LYS A 167 7624 6433 12815 122 -1177 3066 C ATOM 968 C LYS A 167 54.995 46.836 97.897 1.00 64.59 C ANISOU 968 C LYS A 167 7391 5301 11847 263 -898 2023 C ATOM 969 O LYS A 167 54.756 46.256 98.957 1.00 61.84 O ANISOU 969 O LYS A 167 7126 5028 11339 598 -825 1510 O ATOM 970 CB LYS A 167 53.919 49.027 97.428 1.00 74.40 C ANISOU 970 CB LYS A 167 7554 6271 14443 749 -1018 3241 C ATOM 971 CG LYS A 167 52.939 49.863 96.610 1.00 81.74 C ANISOU 971 CG LYS A 167 7852 7430 15774 788 -1185 4452 C ATOM 972 CD LYS A 167 53.340 51.333 96.542 1.00 86.06 C ANISOU 972 CD LYS A 167 8101 7164 17431 1291 -898 4698 C ATOM 973 CE LYS A 167 53.248 52.015 97.900 1.00 86.66 C ANISOU 973 CE LYS A 167 8049 6516 18361 2025 -464 4044 C ATOM 974 NZ LYS A 167 53.153 53.490 97.741 1.00 93.88 N ANISOU 974 NZ LYS A 167 8592 6666 20409 2534 -97 4576 N ATOM 975 N ILE A 168 56.200 46.901 97.356 1.00 63.23 N ANISOU 975 N ILE A 168 7555 4808 11660 101 -760 1853 N ATOM 976 CA ILE A 168 57.380 46.404 98.028 1.00 59.30 C ANISOU 976 CA ILE A 168 7366 4104 11061 268 -508 1086 C ATOM 977 C ILE A 168 57.881 47.544 98.915 1.00 59.91 C ANISOU 977 C ILE A 168 7073 3649 12037 831 -413 679 C ATOM 978 O ILE A 168 57.994 48.671 98.453 1.00 63.34 O ANISOU 978 O ILE A 168 7249 3738 13077 937 -376 1017 O ATOM 979 CB ILE A 168 58.429 45.898 96.989 1.00 59.03 C ANISOU 979 CB ILE A 168 7814 4031 10582 -132 -303 1151 C ATOM 980 CG1 ILE A 168 57.991 44.527 96.476 1.00 58.60 C ANISOU 980 CG1 ILE A 168 8353 4384 9525 -657 -203 1221 C ATOM 981 CG2 ILE A 168 59.832 45.818 97.572 1.00 56.80 C ANISOU 981 CG2 ILE A 168 7600 3419 10560 198 -25 589 C ATOM 982 CD1 ILE A 168 58.736 44.017 95.266 1.00 60.26 C ANISOU 982 CD1 ILE A 168 9146 4577 9173 -1182 101 1374 C ATOM 983 N ASN A 169 58.184 47.247 100.180 1.00 57.41 N ANISOU 983 N ASN A 169 6778 3299 11734 1121 -327 -22 N ATOM 984 CA ASN A 169 58.753 48.230 101.098 1.00 59.00 C ANISOU 984 CA ASN A 169 6743 3070 12602 1428 -266 -528 C ATOM 985 C ASN A 169 60.281 48.339 100.967 1.00 58.65 C ANISOU 985 C ASN A 169 6775 2864 12646 1266 -201 -811 C ATOM 986 O ASN A 169 61.026 47.516 101.516 1.00 56.22 O ANISOU 986 O ASN A 169 6589 2842 11928 1289 -188 -1188 O ATOM 987 CB ASN A 169 58.359 47.898 102.542 1.00 57.85 C ANISOU 987 CB ASN A 169 6586 3077 12316 1706 -247 -1119 C ATOM 988 CG ASN A 169 58.645 49.037 103.512 1.00 61.50 C ANISOU 988 CG ASN A 169 6880 3101 13386 1880 -129 -1681 C ATOM 989 OD1 ASN A 169 59.368 49.979 103.201 1.00 64.37 O ANISOU 989 OD1 ASN A 169 7195 3055 14205 1729 -38 -1758 O ATOM 990 ND2 ASN A 169 58.082 48.945 104.705 1.00 61.95 N ANISOU 990 ND2 ASN A 169 6945 3239 13355 2108 -56 -2143 N ATOM 991 N TYR A 170 60.734 49.367 100.255 1.00 61.83 N ANISOU 991 N TYR A 170 7034 2821 13636 1162 -167 -540 N ATOM 992 CA TYR A 170 62.161 49.701 100.149 1.00 63.13 C ANISOU 992 CA TYR A 170 7125 2837 14024 981 -76 -735 C ATOM 993 C TYR A 170 62.726 50.547 101.318 1.00 66.19 C ANISOU 993 C TYR A 170 7309 2937 14901 999 -89 -1408 C ATOM 994 O TYR A 170 63.933 50.754 101.388 1.00 67.29 O ANISOU 994 O TYR A 170 7383 3022 15162 770 -83 -1628 O ATOM 995 CB TYR A 170 62.426 50.417 98.822 1.00 65.93 C ANISOU 995 CB TYR A 170 7439 2884 14727 749 -2 -136 C ATOM 996 CG TYR A 170 62.094 49.573 97.617 1.00 64.25 C ANISOU 996 CG TYR A 170 7513 2993 13904 516 2 470 C ATOM 997 CD1 TYR A 170 63.011 48.645 97.128 1.00 62.49 C ANISOU 997 CD1 TYR A 170 7561 3013 13166 343 196 470 C ATOM 998 CD2 TYR A 170 60.864 49.700 96.960 1.00 65.67 C ANISOU 998 CD2 TYR A 170 7675 3292 13982 442 -124 1068 C ATOM 999 CE1 TYR A 170 62.721 47.865 96.022 1.00 62.24 C ANISOU 999 CE1 TYR A 170 7943 3240 12466 35 307 912 C ATOM 1000 CE2 TYR A 170 60.560 48.925 95.848 1.00 65.44 C ANISOU 1000 CE2 TYR A 170 7969 3668 13226 44 -151 1584 C ATOM 1001 CZ TYR A 170 61.495 48.005 95.385 1.00 63.73 C ANISOU 1001 CZ TYR A 170 8168 3603 12442 -191 102 1433 C ATOM 1002 OH TYR A 170 61.227 47.219 94.292 1.00 64.78 O ANISOU 1002 OH TYR A 170 8777 4083 11752 -704 222 1801 O ATOM 1003 N GLN A 171 61.865 51.006 102.232 1.00 68.13 N ANISOU 1003 N GLN A 171 7534 3011 15338 1211 -43 -1766 N ATOM 1004 CA GLN A 171 62.265 51.894 103.333 1.00 72.70 C ANISOU 1004 CA GLN A 171 8068 3257 16295 1100 31 -2492 C ATOM 1005 C GLN A 171 62.857 51.078 104.468 1.00 70.98 C ANISOU 1005 C GLN A 171 7834 3662 15472 1070 -137 -3071 C ATOM 1006 O GLN A 171 63.950 51.374 104.951 1.00 73.31 O ANISOU 1006 O GLN A 171 8085 3968 15801 760 -202 -3556 O ATOM 1007 CB GLN A 171 61.072 52.684 103.895 1.00 76.62 C ANISOU 1007 CB GLN A 171 8601 3272 17239 1392 296 -2663 C ATOM 1008 CG GLN A 171 60.186 53.406 102.884 1.00 79.55 C ANISOU 1008 CG GLN A 171 8872 3156 18195 1606 469 -1875 C ATOM 1009 CD GLN A 171 58.858 53.870 103.500 1.00 83.22 C ANISOU 1009 CD GLN A 171 9313 3262 19043 2061 800 -1888 C ATOM 1010 OE1 GLN A 171 58.017 53.039 103.891 1.00 81.30 O ANISOU 1010 OE1 GLN A 171 8915 3713 18261 2185 742 -1758 O ATOM 1011 NE2 GLN A 171 58.661 55.185 103.583 1.00 90.31 N ANISOU 1011 NE2 GLN A 171 10235 3271 20808 2153 1263 -1927 N ATOM 1012 N SER A 172 62.104 50.065 104.902 1.00 67.18 N ANISOU 1012 N SER A 172 7451 3633 14442 1355 -181 -3046 N ATOM 1013 CA SER A 172 62.498 49.213 106.023 1.00 66.14 C ANISOU 1013 CA SER A 172 7318 4140 13669 1386 -332 -3456 C ATOM 1014 C SER A 172 61.772 47.855 106.006 1.00 61.13 C ANISOU 1014 C SER A 172 6836 3976 12412 1671 -332 -3166 C ATOM 1015 O SER A 172 60.708 47.709 105.396 1.00 59.77 O ANISOU 1015 O SER A 172 6743 3809 12157 1748 -237 -2823 O ATOM 1016 CB SER A 172 62.242 49.939 107.351 1.00 70.67 C ANISOU 1016 CB SER A 172 7939 4581 14328 1286 -312 -4212 C ATOM 1017 OG SER A 172 60.858 50.142 107.569 1.00 70.59 O ANISOU 1017 OG SER A 172 8116 4291 14415 1630 -83 -4271 O ATOM 1018 N CYS A 173 62.379 46.870 106.667 1.00 59.88 N ANISOU 1018 N CYS A 173 6669 4372 11707 1758 -420 -3282 N ATOM 1019 CA CYS A 173 61.804 45.542 106.844 1.00 56.19 C ANISOU 1019 CA CYS A 173 6426 4277 10645 2006 -370 -3087 C ATOM 1020 C CYS A 173 62.103 45.075 108.263 1.00 57.57 C ANISOU 1020 C CYS A 173 6509 5009 10357 2118 -460 -3487 C ATOM 1021 O CYS A 173 63.081 45.534 108.857 1.00 61.20 O ANISOU 1021 O CYS A 173 6689 5720 10843 1940 -612 -3790 O ATOM 1022 CB CYS A 173 62.398 44.540 105.829 1.00 53.74 C ANISOU 1022 CB CYS A 173 6261 4068 10090 2057 -196 -2546 C ATOM 1023 SG CYS A 173 61.855 44.787 104.122 1.00 52.27 S ANISOU 1023 SG CYS A 173 6342 3431 10085 1852 -19 -2129 S ATOM 1024 N PRO A 174 61.283 44.150 108.807 1.00 55.41 N ANISOU 1024 N PRO A 174 6448 4997 9606 2358 -367 -3475 N ATOM 1025 CA PRO A 174 61.468 43.712 110.192 1.00 57.29 C ANISOU 1025 CA PRO A 174 6598 5790 9378 2481 -500 -3773 C ATOM 1026 C PRO A 174 62.828 43.116 110.496 1.00 59.23 C ANISOU 1026 C PRO A 174 6565 6564 9376 2513 -581 -3518 C ATOM 1027 O PRO A 174 63.356 42.364 109.684 1.00 56.97 O ANISOU 1027 O PRO A 174 6321 6238 9086 2619 -457 -3025 O ATOM 1028 CB PRO A 174 60.383 42.650 110.383 1.00 54.12 C ANISOU 1028 CB PRO A 174 6518 5498 8548 2742 -322 -3608 C ATOM 1029 CG PRO A 174 59.354 42.977 109.371 1.00 52.03 C ANISOU 1029 CG PRO A 174 6384 4760 8622 2675 -203 -3388 C ATOM 1030 CD PRO A 174 60.125 43.479 108.189 1.00 52.06 C ANISOU 1030 CD PRO A 174 6295 4445 9039 2470 -223 -3111 C ATOM 1031 N ASP A 175 63.396 43.511 111.636 1.00 64.05 N ANISOU 1031 N ASP A 175 6899 7687 9749 2343 -848 -3899 N ATOM 1032 CA ASP A 175 64.590 42.882 112.198 1.00 67.74 C ANISOU 1032 CA ASP A 175 6958 8932 9844 2409 -1025 -3544 C ATOM 1033 C ASP A 175 64.087 41.754 113.075 1.00 67.20 C ANISOU 1033 C ASP A 175 7042 9343 9146 2762 -921 -3386 C ATOM 1034 O ASP A 175 63.116 41.917 113.807 1.00 66.72 O ANISOU 1034 O ASP A 175 7258 9215 8875 2743 -953 -3866 O ATOM 1035 CB ASP A 175 65.440 43.881 113.000 1.00 74.68 C ANISOU 1035 CB ASP A 175 7432 10273 10668 1845 -1434 -3980 C ATOM 1036 CG ASP A 175 66.764 43.280 113.492 1.00 79.67 C ANISOU 1036 CG ASP A 175 7456 11886 10929 1855 -1694 -3441 C ATOM 1037 OD1 ASP A 175 66.857 42.055 113.720 1.00 79.04 O ANISOU 1037 OD1 ASP A 175 7404 12197 10429 2306 -1539 -2848 O ATOM 1038 OD2 ASP A 175 67.739 44.036 113.656 1.00 85.44 O ANISOU 1038 OD2 ASP A 175 7744 12938 11781 1320 -1968 -3517 O ATOM 1039 N TRP A 176 64.765 40.614 112.996 1.00 67.84 N ANISOU 1039 N TRP A 176 6955 9791 9030 3174 -762 -2694 N ATOM 1040 CA TRP A 176 64.260 39.376 113.594 1.00 67.09 C ANISOU 1040 CA TRP A 176 7096 9966 8429 3585 -529 -2385 C ATOM 1041 C TRP A 176 64.280 39.395 115.138 1.00 71.79 C ANISOU 1041 C TRP A 176 7440 11396 8441 3516 -839 -2623 C ATOM 1042 O TRP A 176 63.423 38.780 115.752 1.00 70.01 O ANISOU 1042 O TRP A 176 7492 11296 7813 3778 -684 -2714 O ATOM 1043 CB TRP A 176 64.941 38.121 112.969 1.00 67.17 C ANISOU 1043 CB TRP A 176 7128 9936 8456 4097 -42 -1546 C ATOM 1044 CG TRP A 176 66.085 37.502 113.710 1.00 73.51 C ANISOU 1044 CG TRP A 176 7328 11581 9021 4454 -89 -882 C ATOM 1045 CD1 TRP A 176 67.427 37.722 113.516 1.00 78.51 C ANISOU 1045 CD1 TRP A 176 7295 12650 9883 4403 -205 -391 C ATOM 1046 CD2 TRP A 176 65.984 36.505 114.740 1.00 76.61 C ANISOU 1046 CD2 TRP A 176 7684 12524 8900 4827 28 -467 C ATOM 1047 NE1 TRP A 176 68.171 36.931 114.381 1.00 84.73 N ANISOU 1047 NE1 TRP A 176 7540 14301 10351 4827 -215 347 N ATOM 1048 CE2 TRP A 176 67.310 36.180 115.145 1.00 83.72 C ANISOU 1048 CE2 TRP A 176 7828 14245 9737 5076 -100 336 C ATOM 1049 CE3 TRP A 176 64.901 35.860 115.371 1.00 74.59 C ANISOU 1049 CE3 TRP A 176 7893 12211 8235 4993 187 -627 C ATOM 1050 CZ2 TRP A 176 67.576 35.239 116.159 1.00 88.97 C ANISOU 1050 CZ2 TRP A 176 8199 15675 9930 5534 -52 1013 C ATOM 1051 CZ3 TRP A 176 65.166 34.927 116.386 1.00 79.32 C ANISOU 1051 CZ3 TRP A 176 8287 13508 8342 5405 270 -40 C ATOM 1052 CH2 TRP A 176 66.493 34.628 116.766 1.00 86.55 C ANISOU 1052 CH2 TRP A 176 8450 15249 9186 5691 126 797 C ATOM 1053 N ARG A 177 65.239 40.112 115.736 1.00 78.00 N ANISOU 1053 N ARG A 177 7705 12817 9113 3115 -1311 -2777 N ATOM 1054 CA ARG A 177 65.311 40.287 117.209 1.00 84.37 C ANISOU 1054 CA ARG A 177 8300 14558 9198 2817 -1714 -3047 C ATOM 1055 C ARG A 177 64.341 41.384 117.651 1.00 84.26 C ANISOU 1055 C ARG A 177 8725 14152 9136 2319 -1785 -4099 C ATOM 1056 O ARG A 177 63.528 41.196 118.555 1.00 84.71 O ANISOU 1056 O ARG A 177 9116 14372 8695 2328 -1742 -4515 O ATOM 1057 CB ARG A 177 66.737 40.663 117.731 1.00 93.01 C ANISOU 1057 CB ARG A 177 8611 16660 10066 2386 -2256 -2777 C ATOM 1058 CG ARG A 177 67.902 40.495 116.758 1.00 93.88 C ANISOU 1058 CG ARG A 177 8184 16774 10709 2560 -2172 -2027 C ATOM 1059 CD ARG A 177 69.220 40.087 117.407 1.00102.81 C ANISOU 1059 CD ARG A 177 8399 19183 11480 2554 -2551 -1185 C ATOM 1060 NE ARG A 177 70.211 39.829 116.354 1.00103.32 N ANISOU 1060 NE ARG A 177 8000 19080 12175 2909 -2263 -408 N ATOM 1061 CZ ARG A 177 70.957 40.753 115.734 1.00105.50 C ANISOU 1061 CZ ARG A 177 7948 19243 12892 2396 -2461 -532 C ATOM 1062 NH1 ARG A 177 71.812 40.376 114.782 1.00105.93 N ANISOU 1062 NH1 ARG A 177 7613 19152 13482 2817 -2108 275 N ATOM 1063 NH2 ARG A 177 70.874 42.047 116.054 1.00108.04 N ANISOU 1063 NH2 ARG A 177 8358 19552 13137 1470 -2922 -1460 N ATOM 1064 N LYS A 178 64.433 42.529 116.987 1.00 84.09 N ANISOU 1064 N LYS A 178 8763 13491 9694 1923 -1837 -4559 N ATOM 1065 CA LYS A 178 63.800 43.755 117.468 1.00 86.96 C ANISOU 1065 CA LYS A 178 9453 13480 10106 1413 -1836 -5528 C ATOM 1066 C LYS A 178 62.330 43.885 117.089 1.00 81.60 C ANISOU 1066 C LYS A 178 9298 11918 9787 1755 -1372 -5809 C ATOM 1067 O LYS A 178 61.582 44.552 117.789 1.00 84.16 O ANISOU 1067 O LYS A 178 9980 12043 9951 1572 -1237 -6551 O ATOM 1068 CB LYS A 178 64.554 44.983 116.954 1.00 90.45 C ANISOU 1068 CB LYS A 178 9735 13574 11058 814 -1990 -5871 C ATOM 1069 CG LYS A 178 65.985 45.118 117.451 1.00 98.03 C ANISOU 1069 CG LYS A 178 10090 15513 11642 250 -2489 -5699 C ATOM 1070 CD LYS A 178 66.603 46.400 116.918 1.00101.75 C ANISOU 1070 CD LYS A 178 10483 15516 12659 -422 -2580 -6109 C ATOM 1071 CE LYS A 178 68.106 46.450 117.121 1.00108.88 C ANISOU 1071 CE LYS A 178 10642 17414 13313 -973 -3100 -5719 C ATOM 1072 NZ LYS A 178 68.670 47.759 116.685 1.00113.51 N ANISOU 1072 NZ LYS A 178 11208 17526 14395 -1765 -3165 -6207 N ATOM 1073 N ASP A 179 61.923 43.281 115.975 1.00 74.74 N ANISOU 1073 N ASP A 179 8514 10528 9355 2197 -1147 -5266 N ATOM 1074 CA ASP A 179 60.568 43.467 115.463 1.00 70.70 C ANISOU 1074 CA ASP A 179 8354 9284 9224 2462 -793 -5376 C ATOM 1075 C ASP A 179 59.767 42.176 115.528 1.00 66.74 C ANISOU 1075 C ASP A 179 8039 8950 8368 2885 -585 -4917 C ATOM 1076 O ASP A 179 58.808 42.096 116.280 1.00 67.23 O ANISOU 1076 O ASP A 179 8325 9039 8179 3126 -424 -5217 O ATOM 1077 CB ASP A 179 60.600 44.041 114.041 1.00 67.58 C ANISOU 1077 CB ASP A 179 7947 8136 9594 2415 -699 -5155 C ATOM 1078 CG ASP A 179 61.245 45.418 113.980 1.00 72.19 C ANISOU 1078 CG ASP A 179 8424 8406 10596 1963 -809 -5635 C ATOM 1079 OD1 ASP A 179 60.955 46.264 114.843 1.00 77.15 O ANISOU 1079 OD1 ASP A 179 9182 8912 11216 1759 -733 -6302 O ATOM 1080 OD2 ASP A 179 62.040 45.661 113.049 1.00 71.13 O ANISOU 1080 OD2 ASP A 179 8101 8050 10871 1890 -879 -5386 O ATOM 1081 N CYS A 180 60.153 41.174 114.739 1.00 58.85 N ANISOU 1081 N CYS A 180 9124 6072 7164 3074 2265 -2736 N ATOM 1082 CA CYS A 180 59.438 39.891 114.699 1.00 58.11 C ANISOU 1082 CA CYS A 180 8851 6126 7102 3082 2406 -2404 C ATOM 1083 C CYS A 180 60.231 38.828 113.940 1.00 54.86 C ANISOU 1083 C CYS A 180 8297 5822 6724 2769 2168 -2358 C ATOM 1084 O CYS A 180 60.862 39.126 112.919 1.00 53.29 O ANISOU 1084 O CYS A 180 7924 5670 6652 2542 2018 -2561 O ATOM 1085 CB CYS A 180 58.043 40.049 114.065 1.00 58.95 C ANISOU 1085 CB CYS A 180 8651 6281 7466 3066 2584 -2095 C ATOM 1086 SG CYS A 180 58.076 40.787 112.412 1.00 58.13 S ANISOU 1086 SG CYS A 180 8223 6285 7578 2860 2266 -1997 S ATOM 1087 N SER A 181 60.179 37.600 114.455 1.00 54.26 N ANISOU 1087 N SER A 181 8212 5897 6504 2844 2210 -2285 N ATOM 1088 CA SER A 181 60.874 36.453 113.880 1.00 51.54 C ANISOU 1088 CA SER A 181 7706 5654 6221 2607 2055 -2172 C ATOM 1089 C SER A 181 60.302 36.046 112.516 1.00 49.17 C ANISOU 1089 C SER A 181 7066 5362 6254 2425 2057 -1922 C ATOM 1090 O SER A 181 61.057 35.616 111.643 1.00 47.20 O ANISOU 1090 O SER A 181 6708 5155 6069 2236 1906 -1840 O ATOM 1091 CB SER A 181 60.801 35.240 114.826 1.00 52.25 C ANISOU 1091 CB SER A 181 7853 5903 6093 2752 2161 -2051 C ATOM 1092 OG SER A 181 59.465 35.014 115.205 1.00 53.99 O ANISOU 1092 OG SER A 181 7981 6191 6342 2842 2424 -1733 O ATOM 1093 N ASN A 182 58.983 36.170 112.337 1.00 49.31 N ANISOU 1093 N ASN A 182 7022 5308 6404 2525 2260 -1719 N ATOM 1094 CA ASN A 182 58.290 35.593 111.180 1.00 47.52 C ANISOU 1094 CA ASN A 182 6507 5074 6475 2338 2260 -1463 C ATOM 1095 C ASN A 182 58.075 36.571 110.039 1.00 46.36 C ANISOU 1095 C ASN A 182 6252 4791 6571 2255 2180 -1532 C ATOM 1096 O ASN A 182 56.958 36.790 109.584 1.00 46.36 O ANISOU 1096 O ASN A 182 6139 4739 6736 2354 2349 -1465 O ATOM 1097 CB ASN A 182 56.991 34.927 111.617 1.00 48.93 C ANISOU 1097 CB ASN A 182 6521 5341 6729 2461 2493 -1203 C ATOM 1098 CG ASN A 182 57.241 33.677 112.441 1.00 49.48 C ANISOU 1098 CG ASN A 182 6632 5553 6615 2483 2530 -1090 C ATOM 1099 OD1 ASN A 182 58.219 32.946 112.214 1.00 48.88 O ANISOU 1099 OD1 ASN A 182 6418 5550 6603 2396 2259 -1113 O ATOM 1100 ND2 ASN A 182 56.357 33.398 113.371 1.00 51.60 N ANISOU 1100 ND2 ASN A 182 6904 5893 6806 2713 2795 -923 N ATOM 1101 N ASN A 183 59.202 37.076 109.538 1.00 45.18 N ANISOU 1101 N ASN A 183 6187 4569 6408 2117 1969 -1703 N ATOM 1102 CA ASN A 183 59.264 38.014 108.419 1.00 44.30 C ANISOU 1102 CA ASN A 183 5991 4355 6483 2004 1897 -1747 C ATOM 1103 C ASN A 183 59.636 37.326 107.109 1.00 41.92 C ANISOU 1103 C ASN A 183 5534 4080 6310 1765 1678 -1667 C ATOM 1104 O ASN A 183 60.168 36.218 107.129 1.00 40.49 O ANISOU 1104 O ASN A 183 5317 4028 6037 1660 1539 -1699 O ATOM 1105 CB ASN A 183 60.257 39.142 108.737 1.00 44.87 C ANISOU 1105 CB ASN A 183 6264 4307 6477 2019 1831 -2016 C ATOM 1106 CG ASN A 183 61.668 38.642 108.954 1.00 43.80 C ANISOU 1106 CG ASN A 183 6240 4177 6224 1898 1633 -2207 C ATOM 1107 OD1 ASN A 183 62.388 38.357 107.998 1.00 42.14 O ANISOU 1107 OD1 ASN A 183 5936 3963 6109 1712 1498 -2175 O ATOM 1108 ND2 ASN A 183 62.066 38.512 110.217 1.00 45.13 N ANISOU 1108 ND2 ASN A 183 6591 4399 6156 2032 1646 -2364 N ATOM 1109 N PRO A 184 59.376 37.984 105.964 1.00 41.44 N ANISOU 1109 N PRO A 184 5384 3925 6434 1699 1658 -1604 N ATOM 1110 CA PRO A 184 59.616 37.351 104.655 1.00 39.62 C ANISOU 1110 CA PRO A 184 5025 3710 6318 1540 1509 -1504 C ATOM 1111 C PRO A 184 60.987 36.691 104.457 1.00 37.99 C ANISOU 1111 C PRO A 184 4908 3514 6009 1399 1336 -1642 C ATOM 1112 O PRO A 184 61.060 35.585 103.927 1.00 36.63 O ANISOU 1112 O PRO A 184 4645 3413 5858 1366 1273 -1520 O ATOM 1113 CB PRO A 184 59.436 38.507 103.675 1.00 39.80 C ANISOU 1113 CB PRO A 184 5011 3617 6491 1534 1510 -1484 C ATOM 1114 CG PRO A 184 58.407 39.371 104.339 1.00 41.82 C ANISOU 1114 CG PRO A 184 5274 3832 6783 1698 1719 -1459 C ATOM 1115 CD PRO A 184 58.694 39.284 105.809 1.00 42.82 C ANISOU 1115 CD PRO A 184 5557 3992 6720 1825 1812 -1612 C ATOM 1116 N VAL A 185 62.044 37.376 104.898 1.00 38.25 N ANISOU 1116 N VAL A 185 5058 3490 5985 1399 1308 -1838 N ATOM 1117 CA VAL A 185 63.405 36.887 104.754 1.00 36.87 C ANISOU 1117 CA VAL A 185 4965 3317 5725 1275 1163 -1962 C ATOM 1118 C VAL A 185 63.678 35.705 105.679 1.00 36.73 C ANISOU 1118 C VAL A 185 5008 3453 5493 1296 1135 -1984 C ATOM 1119 O VAL A 185 64.151 34.650 105.225 1.00 35.81 O ANISOU 1119 O VAL A 185 4859 3331 5413 1203 998 -1957 O ATOM 1120 CB VAL A 185 64.443 37.997 105.023 1.00 37.46 C ANISOU 1120 CB VAL A 185 5157 3263 5810 1279 1114 -2194 C ATOM 1121 CG1 VAL A 185 65.853 37.429 105.053 1.00 36.53 C ANISOU 1121 CG1 VAL A 185 5069 3180 5630 1144 936 -2299 C ATOM 1122 CG2 VAL A 185 64.353 39.077 103.952 1.00 37.52 C ANISOU 1122 CG2 VAL A 185 5103 3130 6020 1250 1155 -2151 C ATOM 1123 N SER A 186 63.431 35.889 106.971 1.00 38.03 N ANISOU 1123 N SER A 186 5248 3663 5538 1431 1241 -2043 N ATOM 1124 CA SER A 186 63.696 34.827 107.953 1.00 38.06 C ANISOU 1124 CA SER A 186 5328 3780 5352 1465 1234 -2065 C ATOM 1125 C SER A 186 62.934 33.545 107.664 1.00 37.07 C ANISOU 1125 C SER A 186 5100 3773 5210 1449 1277 -1873 C ATOM 1126 O SER A 186 63.474 32.447 107.817 1.00 36.13 O ANISOU 1126 O SER A 186 5019 3752 4956 1389 1246 -1875 O ATOM 1127 CB SER A 186 63.329 35.306 109.360 1.00 40.25 C ANISOU 1127 CB SER A 186 5764 4079 5450 1686 1349 -2157 C ATOM 1128 OG SER A 186 64.166 36.374 109.745 1.00 41.13 O ANISOU 1128 OG SER A 186 5961 4138 5528 1698 1299 -2402 O ATOM 1129 N VAL A 187 61.674 33.686 107.272 1.00 37.45 N ANISOU 1129 N VAL A 187 5026 3779 5422 1480 1388 -1697 N ATOM 1130 CA VAL A 187 60.814 32.540 107.019 1.00 37.36 C ANISOU 1130 CA VAL A 187 4825 3839 5530 1430 1410 -1430 C ATOM 1131 C VAL A 187 61.241 31.812 105.737 1.00 35.55 C ANISOU 1131 C VAL A 187 4497 3596 5414 1264 1218 -1393 C ATOM 1132 O VAL A 187 61.148 30.599 105.657 1.00 35.25 O ANISOU 1132 O VAL A 187 4439 3592 5361 1242 1188 -1287 O ATOM 1133 CB VAL A 187 59.322 32.944 106.964 1.00 38.73 C ANISOU 1133 CB VAL A 187 4858 3979 5876 1531 1567 -1241 C ATOM 1134 CG1 VAL A 187 58.438 31.755 106.602 1.00 38.69 C ANISOU 1134 CG1 VAL A 187 4661 4014 6026 1473 1577 -1011 C ATOM 1135 CG2 VAL A 187 58.871 33.508 108.311 1.00 40.83 C ANISOU 1135 CG2 VAL A 187 5226 4282 6005 1742 1771 -1260 C ATOM 1136 N PHE A 188 61.705 32.553 104.735 1.00 34.80 N ANISOU 1136 N PHE A 188 4419 3416 5387 1184 1102 -1461 N ATOM 1137 CA PHE A 188 62.216 31.946 103.512 1.00 33.41 C ANISOU 1137 CA PHE A 188 4213 3229 5250 1018 952 -1429 C ATOM 1138 C PHE A 188 63.388 31.030 103.857 1.00 32.60 C ANISOU 1138 C PHE A 188 4216 3153 5015 968 874 -1531 C ATOM 1139 O PHE A 188 63.370 29.846 103.562 1.00 32.01 O ANISOU 1139 O PHE A 188 4165 3141 4853 903 819 -1509 O ATOM 1140 CB PHE A 188 62.652 33.013 102.504 1.00 32.84 C ANISOU 1140 CB PHE A 188 4168 3044 5265 999 887 -1500 C ATOM 1141 CG PHE A 188 63.403 32.452 101.327 1.00 31.33 C ANISOU 1141 CG PHE A 188 3996 2807 5097 907 722 -1481 C ATOM 1142 CD1 PHE A 188 62.726 32.003 100.196 1.00 31.10 C ANISOU 1142 CD1 PHE A 188 3883 2769 5163 860 639 -1356 C ATOM 1143 CD2 PHE A 188 64.784 32.360 101.363 1.00 30.53 C ANISOU 1143 CD2 PHE A 188 3989 2717 4894 834 666 -1601 C ATOM 1144 CE1 PHE A 188 63.425 31.460 99.124 1.00 30.17 C ANISOU 1144 CE1 PHE A 188 3792 2690 4981 761 507 -1347 C ATOM 1145 CE2 PHE A 188 65.494 31.812 100.298 1.00 29.63 C ANISOU 1145 CE2 PHE A 188 3882 2613 4760 768 550 -1590 C ATOM 1146 CZ PHE A 188 64.808 31.362 99.177 1.00 29.34 C ANISOU 1146 CZ PHE A 188 3793 2564 4791 753 487 -1471 C ATOM 1147 N TRP A 189 64.390 31.604 104.524 1.00 33.07 N ANISOU 1147 N TRP A 189 4376 3244 4943 987 846 -1704 N ATOM 1148 CA TRP A 189 65.618 30.881 104.829 1.00 32.47 C ANISOU 1148 CA TRP A 189 4369 3217 4750 949 759 -1787 C ATOM 1149 C TRP A 189 65.344 29.685 105.716 1.00 33.07 C ANISOU 1149 C TRP A 189 4476 3374 4714 976 819 -1701 C ATOM 1150 O TRP A 189 65.957 28.635 105.551 1.00 32.16 O ANISOU 1150 O TRP A 189 4363 3335 4521 895 768 -1752 O ATOM 1151 CB TRP A 189 66.680 31.821 105.446 1.00 32.81 C ANISOU 1151 CB TRP A 189 4555 3193 4717 991 739 -1996 C ATOM 1152 CG TRP A 189 67.312 32.672 104.404 1.00 32.10 C ANISOU 1152 CG TRP A 189 4429 2989 4777 910 664 -2059 C ATOM 1153 CD1 TRP A 189 67.254 34.013 104.309 1.00 32.76 C ANISOU 1153 CD1 TRP A 189 4501 2971 4973 920 715 -2146 C ATOM 1154 CD2 TRP A 189 68.043 32.215 103.254 1.00 30.73 C ANISOU 1154 CD2 TRP A 189 4194 2801 4680 793 582 -1990 C ATOM 1155 NE1 TRP A 189 67.900 34.439 103.185 1.00 32.08 N ANISOU 1155 NE1 TRP A 189 4391 2782 5015 830 670 -2141 N ATOM 1156 CE2 TRP A 189 68.409 33.356 102.521 1.00 30.91 C ANISOU 1156 CE2 TRP A 189 4225 2687 4830 761 583 -2047 C ATOM 1157 CE3 TRP A 189 68.421 30.963 102.782 1.00 29.66 C ANISOU 1157 CE3 TRP A 189 4075 2709 4485 702 499 -1928 C ATOM 1158 CZ2 TRP A 189 69.153 33.281 101.328 1.00 30.09 C ANISOU 1158 CZ2 TRP A 189 4101 2530 4801 690 531 -2009 C ATOM 1159 CZ3 TRP A 189 69.175 30.885 101.599 1.00 28.86 C ANISOU 1159 CZ3 TRP A 189 3983 2554 4429 636 430 -1876 C ATOM 1160 CH2 TRP A 189 69.532 32.041 100.895 1.00 29.00 C ANISOU 1160 CH2 TRP A 189 3978 2458 4582 634 455 -1918 C ATOM 1161 N LYS A 190 64.412 29.858 106.645 1.00 34.92 N ANISOU 1161 N LYS A 190 4672 3681 4915 1147 993 -1685 N ATOM 1162 CA LYS A 190 63.986 28.790 107.533 1.00 36.15 C ANISOU 1162 CA LYS A 190 4849 3875 5008 1191 1059 -1525 C ATOM 1163 C LYS A 190 63.319 27.675 106.731 1.00 35.62 C ANISOU 1163 C LYS A 190 4635 3818 5081 1092 1034 -1355 C ATOM 1164 O LYS A 190 63.645 26.523 106.939 1.00 35.46 O ANISOU 1164 O LYS A 190 4625 3819 5027 1037 925 -1257 O ATOM 1165 CB LYS A 190 63.065 29.363 108.626 1.00 38.50 C ANISOU 1165 CB LYS A 190 5162 4246 5218 1376 1268 -1498 C ATOM 1166 CG LYS A 190 62.362 28.365 109.528 1.00 40.00 C ANISOU 1166 CG LYS A 190 5330 4506 5361 1474 1423 -1289 C ATOM 1167 CD LYS A 190 61.580 29.082 110.635 1.00 42.52 C ANISOU 1167 CD LYS A 190 5727 4837 5591 1717 1635 -1310 C ATOM 1168 CE LYS A 190 60.151 29.448 110.197 1.00 43.46 C ANISOU 1168 CE LYS A 190 5657 4907 5949 1732 1765 -1116 C ATOM 1169 NZ LYS A 190 59.527 30.573 110.962 1.00 45.45 N ANISOU 1169 NZ LYS A 190 5997 5138 6131 1940 1958 -1147 N ATOM 1170 N THR A 191 62.442 28.021 105.786 1.00 35.72 N ANISOU 1170 N THR A 191 4480 3808 5283 1086 1034 -1268 N ATOM 1171 CA THR A 191 61.798 27.014 104.928 1.00 35.87 C ANISOU 1171 CA THR A 191 4404 3751 5471 907 948 -1100 C ATOM 1172 C THR A 191 62.794 26.239 104.042 1.00 34.71 C ANISOU 1172 C THR A 191 4360 3576 5252 819 763 -1187 C ATOM 1173 O THR A 191 62.777 24.995 104.035 1.00 34.19 O ANISOU 1173 O THR A 191 4253 3560 5175 849 770 -1126 O ATOM 1174 CB THR A 191 60.704 27.629 104.037 1.00 36.59 C ANISOU 1174 CB THR A 191 4363 3788 5752 884 912 -988 C ATOM 1175 OG1 THR A 191 59.795 28.388 104.847 1.00 38.12 O ANISOU 1175 OG1 THR A 191 4518 3941 6026 999 1139 -859 O ATOM 1176 CG2 THR A 191 59.905 26.550 103.322 1.00 37.16 C ANISOU 1176 CG2 THR A 191 4279 3820 6018 768 816 -847 C ATOM 1177 N VAL A 192 63.637 26.960 103.290 1.00 34.10 N ANISOU 1177 N VAL A 192 4313 3475 5168 714 633 -1289 N ATOM 1178 CA VAL A 192 64.579 26.293 102.375 1.00 33.47 C ANISOU 1178 CA VAL A 192 4255 3425 5037 653 508 -1329 C ATOM 1179 C VAL A 192 65.668 25.532 103.099 1.00 33.07 C ANISOU 1179 C VAL A 192 4315 3407 4840 637 490 -1346 C ATOM 1180 O VAL A 192 66.074 24.499 102.609 1.00 33.02 O ANISOU 1180 O VAL A 192 4457 3231 4856 539 307 -1319 O ATOM 1181 CB VAL A 192 65.251 27.202 101.298 1.00 33.10 C ANISOU 1181 CB VAL A 192 4276 3237 5063 578 391 -1358 C ATOM 1182 CG1 VAL A 192 64.248 27.600 100.245 1.00 34.11 C ANISOU 1182 CG1 VAL A 192 4370 3318 5270 543 295 -1229 C ATOM 1183 CG2 VAL A 192 65.938 28.419 101.896 1.00 33.11 C ANISOU 1183 CG2 VAL A 192 4401 3235 4944 686 486 -1539 C ATOM 1184 N SER A 193 66.157 26.052 104.223 1.00 33.49 N ANISOU 1184 N SER A 193 4415 3584 4725 731 649 -1478 N ATOM 1185 CA SER A 193 67.198 25.354 105.003 1.00 33.73 C ANISOU 1185 CA SER A 193 4570 3632 4613 761 561 -1560 C ATOM 1186 C SER A 193 66.714 24.053 105.603 1.00 34.48 C ANISOU 1186 C SER A 193 4692 3736 4672 770 597 -1425 C ATOM 1187 O SER A 193 67.448 23.074 105.629 1.00 34.22 O ANISOU 1187 O SER A 193 4878 3515 4607 696 606 -1547 O ATOM 1188 CB SER A 193 67.738 26.225 106.135 1.00 34.49 C ANISOU 1188 CB SER A 193 4776 3763 4565 894 634 -1734 C ATOM 1189 OG SER A 193 68.429 27.341 105.617 1.00 34.38 O ANISOU 1189 OG SER A 193 4910 3779 4374 739 589 -1911 O ATOM 1190 N ARG A 194 65.489 24.069 106.106 1.00 36.37 N ANISOU 1190 N ARG A 194 4789 3997 5031 852 771 -1364 N ATOM 1191 CA ARG A 194 64.859 22.887 106.675 1.00 38.12 C ANISOU 1191 CA ARG A 194 5028 4166 5290 888 848 -1090 C ATOM 1192 C ARG A 194 64.737 21.791 105.623 1.00 37.65 C ANISOU 1192 C ARG A 194 4911 4080 5315 799 747 -1031 C ATOM 1193 O ARG A 194 65.067 20.641 105.888 1.00 38.18 O ANISOU 1193 O ARG A 194 4987 4134 5384 878 782 -1027 O ATOM 1194 CB ARG A 194 63.465 23.217 107.206 1.00 40.45 C ANISOU 1194 CB ARG A 194 5164 4535 5668 1048 1054 -1015 C ATOM 1195 CG ARG A 194 62.921 22.218 108.197 1.00 43.01 C ANISOU 1195 CG ARG A 194 5559 4826 5955 1048 1163 -751 C ATOM 1196 CD ARG A 194 61.421 22.387 108.434 1.00 46.04 C ANISOU 1196 CD ARG A 194 5629 5206 6659 1010 1271 -506 C ATOM 1197 NE ARG A 194 60.671 21.623 107.435 1.00 48.45 N ANISOU 1197 NE ARG A 194 6019 5273 7114 732 1054 -511 N ATOM 1198 CZ ARG A 194 59.983 22.110 106.396 1.00 49.70 C ANISOU 1198 CZ ARG A 194 6043 5420 7420 671 937 -362 C ATOM 1199 NH1 ARG A 194 59.871 23.418 106.165 1.00 49.56 N ANISOU 1199 NH1 ARG A 194 5960 5392 7476 911 1037 -645 N ATOM 1200 NH2 ARG A 194 59.385 21.253 105.563 1.00 52.45 N ANISOU 1200 NH2 ARG A 194 6287 5587 8052 196 742 -281 N ATOM 1201 N ARG A 195 64.263 22.160 104.439 1.00 36.76 N ANISOU 1201 N ARG A 195 4692 3845 5430 739 642 -1033 N ATOM 1202 CA ARG A 195 64.080 21.216 103.348 1.00 36.58 C ANISOU 1202 CA ARG A 195 4608 3748 5541 544 470 -999 C ATOM 1203 C ARG A 195 65.396 20.672 102.816 1.00 34.86 C ANISOU 1203 C ARG A 195 4510 3564 5168 464 326 -1014 C ATOM 1204 O ARG A 195 65.497 19.495 102.478 1.00 34.17 O ANISOU 1204 O ARG A 195 4307 3475 5201 815 63 -805 O ATOM 1205 CB ARG A 195 63.257 21.825 102.228 1.00 37.12 C ANISOU 1205 CB ARG A 195 4688 3665 5751 501 329 -953 C ATOM 1206 CG ARG A 195 61.792 21.956 102.631 1.00 39.82 C ANISOU 1206 CG ARG A 195 4749 4107 6273 448 473 -865 C ATOM 1207 CD ARG A 195 61.064 22.952 101.745 1.00 41.36 C ANISOU 1207 CD ARG A 195 4903 4255 6557 473 338 -790 C ATOM 1208 NE ARG A 195 61.162 22.520 100.345 1.00 42.20 N ANISOU 1208 NE ARG A 195 5054 4469 6508 177 71 -777 N ATOM 1209 CZ ARG A 195 60.257 21.798 99.684 1.00 42.68 C ANISOU 1209 CZ ARG A 195 4984 4329 6904 148 -12 -695 C ATOM 1210 NH1 ARG A 195 59.109 21.423 100.259 1.00 44.27 N ANISOU 1210 NH1 ARG A 195 4967 4478 7373 167 58 -425 N ATOM 1211 NH2 ARG A 195 60.503 21.472 98.416 1.00 42.05 N ANISOU 1211 NH2 ARG A 195 5133 3912 6933 253 -203 -831 N ATOM 1212 N PHE A 196 66.399 21.532 102.759 1.00 33.79 N ANISOU 1212 N PHE A 196 4438 3448 4950 562 348 -1134 N ATOM 1213 CA PHE A 196 67.735 21.131 102.327 1.00 32.26 C ANISOU 1213 CA PHE A 196 4409 3274 4572 460 284 -1208 C ATOM 1214 C PHE A 196 68.322 20.109 103.299 1.00 32.04 C ANISOU 1214 C PHE A 196 4476 3291 4405 555 361 -1265 C ATOM 1215 O PHE A 196 68.835 19.082 102.885 1.00 31.37 O ANISOU 1215 O PHE A 196 4441 3197 4279 438 409 -1260 O ATOM 1216 CB PHE A 196 68.635 22.362 102.249 1.00 31.28 C ANISOU 1216 CB PHE A 196 4370 3170 4342 493 297 -1414 C ATOM 1217 CG PHE A 196 69.903 22.146 101.477 1.00 29.85 C ANISOU 1217 CG PHE A 196 4289 2861 4189 495 173 -1482 C ATOM 1218 CD1 PHE A 196 69.861 21.793 100.124 1.00 29.49 C ANISOU 1218 CD1 PHE A 196 4267 2770 4168 466 109 -1428 C ATOM 1219 CD2 PHE A 196 71.141 22.341 102.079 1.00 29.08 C ANISOU 1219 CD2 PHE A 196 4291 2752 4006 537 195 -1600 C ATOM 1220 CE1 PHE A 196 71.039 21.619 99.405 1.00 28.80 C ANISOU 1220 CE1 PHE A 196 4260 2683 3999 434 57 -1435 C ATOM 1221 CE2 PHE A 196 72.313 22.178 101.361 1.00 28.28 C ANISOU 1221 CE2 PHE A 196 4227 2615 3901 469 135 -1589 C ATOM 1222 CZ PHE A 196 72.264 21.815 100.028 1.00 28.09 C ANISOU 1222 CZ PHE A 196 4219 2615 3839 437 121 -1452 C ATOM 1223 N ALA A 197 68.220 20.402 104.594 1.00 32.62 N ANISOU 1223 N ALA A 197 4581 3428 4383 650 435 -1241 N ATOM 1224 CA ALA A 197 68.692 19.502 105.637 1.00 32.52 C ANISOU 1224 CA ALA A 197 4549 3531 4276 667 509 -1223 C ATOM 1225 C ALA A 197 67.933 18.179 105.642 1.00 33.02 C ANISOU 1225 C ALA A 197 4538 3593 4414 610 527 -1067 C ATOM 1226 O ALA A 197 68.552 17.129 105.842 1.00 33.44 O ANISOU 1226 O ALA A 197 4647 3648 4411 639 406 -1007 O ATOM 1227 CB ALA A 197 68.610 20.168 107.001 1.00 33.32 C ANISOU 1227 CB ALA A 197 4654 3733 4272 858 646 -1248 C ATOM 1228 N GLU A 198 66.620 18.225 105.392 1.00 33.13 N ANISOU 1228 N GLU A 198 4462 3512 4614 623 670 -944 N ATOM 1229 CA GLU A 198 65.787 17.014 105.271 1.00 34.13 C ANISOU 1229 CA GLU A 198 4473 3568 4926 549 643 -792 C ATOM 1230 C GLU A 198 66.145 16.142 104.065 1.00 33.34 C ANISOU 1230 C GLU A 198 4407 3358 4902 404 487 -800 C ATOM 1231 O GLU A 198 65.917 14.917 104.089 1.00 33.57 O ANISOU 1231 O GLU A 198 4374 3316 5066 490 589 -603 O ATOM 1232 CB GLU A 198 64.287 17.359 105.234 1.00 35.36 C ANISOU 1232 CB GLU A 198 4463 3631 5340 533 680 -665 C ATOM 1233 CG GLU A 198 63.733 17.738 106.604 1.00 37.03 C ANISOU 1233 CG GLU A 198 4603 3972 5494 661 936 -573 C ATOM 1234 CD GLU A 198 62.289 18.235 106.594 1.00 38.51 C ANISOU 1234 CD GLU A 198 4617 4133 5881 693 1006 -485 C ATOM 1235 OE1 GLU A 198 61.723 18.472 105.504 1.00 39.30 O ANISOU 1235 OE1 GLU A 198 4669 4137 6126 504 715 -472 O ATOM 1236 OE2 GLU A 198 61.723 18.378 107.698 1.00 39.74 O ANISOU 1236 OE2 GLU A 198 4678 4322 6099 782 1276 -382 O ATOM 1237 N ALA A 199 66.679 16.773 103.016 1.00 31.87 N ANISOU 1237 N ALA A 199 4308 3124 4675 378 293 -924 N ATOM 1238 CA ALA A 199 67.114 16.054 101.820 1.00 31.28 C ANISOU 1238 CA ALA A 199 4274 2974 4635 313 174 -945 C ATOM 1239 C ALA A 199 68.405 15.293 102.044 1.00 30.38 C ANISOU 1239 C ALA A 199 4281 2924 4335 320 205 -1023 C ATOM 1240 O ALA A 199 68.705 14.386 101.282 1.00 29.90 O ANISOU 1240 O ALA A 199 4272 2701 4388 201 83 -1025 O ATOM 1241 CB ALA A 199 67.284 17.012 100.653 1.00 30.53 C ANISOU 1241 CB ALA A 199 4242 2854 4504 291 41 -1059 C ATOM 1242 N ALA A 200 69.183 15.683 103.056 1.00 30.10 N ANISOU 1242 N ALA A 200 4270 3024 4141 437 276 -1020 N ATOM 1243 CA ALA A 200 70.526 15.127 103.235 1.00 29.21 C ANISOU 1243 CA ALA A 200 4300 2911 3886 459 285 -1055 C ATOM 1244 C ALA A 200 70.479 13.658 103.608 1.00 29.76 C ANISOU 1244 C ALA A 200 4355 2936 4016 462 338 -963 C ATOM 1245 O ALA A 200 69.568 13.220 104.297 1.00 30.85 O ANISOU 1245 O ALA A 200 4406 2982 4332 433 453 -894 O ATOM 1246 CB ALA A 200 71.283 15.898 104.300 1.00 29.10 C ANISOU 1246 CB ALA A 200 4279 3033 3743 551 366 -1150 C ATOM 1247 N CYS A 201 71.493 12.922 103.168 1.00 28.82 N ANISOU 1247 N CYS A 201 4386 2797 3766 437 286 -986 N ATOM 1248 CA CYS A 201 71.680 11.536 103.568 1.00 29.58 C ANISOU 1248 CA CYS A 201 4495 2868 3873 484 374 -855 C ATOM 1249 C CYS A 201 73.171 11.189 103.715 1.00 28.72 C ANISOU 1249 C CYS A 201 4528 2810 3574 555 375 -892 C ATOM 1250 O CYS A 201 74.046 11.991 103.375 1.00 27.51 O ANISOU 1250 O CYS A 201 4362 2743 3344 641 331 -976 O ATOM 1251 CB CYS A 201 71.046 10.620 102.519 1.00 30.21 C ANISOU 1251 CB CYS A 201 4612 2773 4092 401 237 -813 C ATOM 1252 SG CYS A 201 72.100 10.496 101.067 1.00 30.13 S ANISOU 1252 SG CYS A 201 4664 2864 3918 505 94 -923 S ATOM 1253 N ASP A 202 73.423 9.960 104.175 1.00 29.54 N ANISOU 1253 N ASP A 202 4648 2908 3669 601 439 -753 N ATOM 1254 CA ASP A 202 74.756 9.323 104.224 1.00 29.11 C ANISOU 1254 CA ASP A 202 4713 2866 3481 677 450 -741 C ATOM 1255 C ASP A 202 75.701 10.134 105.114 1.00 28.75 C ANISOU 1255 C ASP A 202 4661 2981 3281 805 478 -805 C ATOM 1256 O ASP A 202 75.430 10.264 106.305 1.00 29.81 O ANISOU 1256 O ASP A 202 4919 3083 3322 980 605 -773 O ATOM 1257 CB ASP A 202 75.309 9.051 102.812 1.00 28.39 C ANISOU 1257 CB ASP A 202 4724 2639 3422 646 345 -812 C ATOM 1258 CG ASP A 202 74.539 7.973 102.073 1.00 29.23 C ANISOU 1258 CG ASP A 202 4856 2570 3679 549 297 -751 C ATOM 1259 OD1 ASP A 202 73.550 7.472 102.621 1.00 30.40 O ANISOU 1259 OD1 ASP A 202 4801 2818 3929 498 339 -748 O ATOM 1260 OD2 ASP A 202 74.933 7.564 100.950 1.00 29.29 O ANISOU 1260 OD2 ASP A 202 5054 2429 3643 532 210 -791 O ATOM 1261 N VAL A 203 76.780 10.691 104.562 1.00 28.07 N ANISOU 1261 N VAL A 203 4564 2965 3133 806 390 -890 N ATOM 1262 CA VAL A 203 77.651 11.582 105.308 1.00 28.05 C ANISOU 1262 CA VAL A 203 4530 3113 3013 878 390 -1006 C ATOM 1263 C VAL A 203 77.326 12.992 104.857 1.00 27.52 C ANISOU 1263 C VAL A 203 4401 3041 3011 791 307 -1085 C ATOM 1264 O VAL A 203 77.383 13.314 103.679 1.00 26.23 O ANISOU 1264 O VAL A 203 4307 2692 2966 740 274 -1196 O ATOM 1265 CB VAL A 203 79.139 11.287 105.082 1.00 27.93 C ANISOU 1265 CB VAL A 203 4532 3143 2936 907 359 -979 C ATOM 1266 CG1 VAL A 203 80.011 12.246 105.886 1.00 28.25 C ANISOU 1266 CG1 VAL A 203 4513 3334 2885 971 298 -1070 C ATOM 1267 CG2 VAL A 203 79.461 9.836 105.449 1.00 28.54 C ANISOU 1267 CG2 VAL A 203 4667 3220 2955 975 455 -847 C ATOM 1268 N VAL A 204 76.972 13.826 105.826 1.00 28.34 N ANISOU 1268 N VAL A 204 4451 3242 3075 845 310 -1176 N ATOM 1269 CA VAL A 204 76.714 15.249 105.575 1.00 28.18 C ANISOU 1269 CA VAL A 204 4396 3202 3109 782 258 -1245 C ATOM 1270 C VAL A 204 77.900 15.998 106.195 1.00 28.83 C ANISOU 1270 C VAL A 204 4439 3391 3121 823 174 -1363 C ATOM 1271 O VAL A 204 78.442 15.606 107.233 1.00 29.73 O ANISOU 1271 O VAL A 204 4514 3703 3079 837 222 -1268 O ATOM 1272 CB VAL A 204 75.298 15.678 105.998 1.00 28.68 C ANISOU 1272 CB VAL A 204 4415 3261 3218 789 317 -1254 C ATOM 1273 CG1 VAL A 204 75.045 15.393 107.452 1.00 30.08 C ANISOU 1273 CG1 VAL A 204 4607 3559 3260 912 401 -1201 C ATOM 1274 CG2 VAL A 204 75.034 17.153 105.742 1.00 28.60 C ANISOU 1274 CG2 VAL A 204 4348 3244 3273 738 266 -1323 C ATOM 1275 N HIS A 205 78.373 17.004 105.477 1.00 28.53 N ANISOU 1275 N HIS A 205 4375 3291 3172 779 128 -1444 N ATOM 1276 CA HIS A 205 79.534 17.778 105.892 1.00 29.36 C ANISOU 1276 CA HIS A 205 4386 3494 3275 788 33 -1560 C ATOM 1277 C HIS A 205 79.084 19.179 106.314 1.00 30.15 C ANISOU 1277 C HIS A 205 4476 3546 3431 780 -35 -1718 C ATOM 1278 O HIS A 205 78.137 19.732 105.716 1.00 30.54 O ANISOU 1278 O HIS A 205 4394 3655 3552 670 -44 -1653 O ATOM 1279 CB HIS A 205 80.531 17.859 104.743 1.00 28.83 C ANISOU 1279 CB HIS A 205 4316 3311 3327 734 21 -1530 C ATOM 1280 CG HIS A 205 81.216 16.561 104.440 1.00 28.77 C ANISOU 1280 CG HIS A 205 4307 3332 3289 789 78 -1411 C ATOM 1281 ND1 HIS A 205 80.656 15.585 103.635 1.00 28.05 N ANISOU 1281 ND1 HIS A 205 4303 3183 3171 782 126 -1305 N ATOM 1282 CD2 HIS A 205 82.409 16.070 104.852 1.00 29.48 C ANISOU 1282 CD2 HIS A 205 4360 3522 3316 846 21 -1387 C ATOM 1283 CE1 HIS A 205 81.481 14.557 103.559 1.00 28.11 C ANISOU 1283 CE1 HIS A 205 4396 3143 3138 803 165 -1233 C ATOM 1284 NE2 HIS A 205 82.553 14.824 104.284 1.00 29.09 N ANISOU 1284 NE2 HIS A 205 4404 3364 3285 883 67 -1206 N ATOM 1285 N VAL A 206 79.727 19.744 107.339 1.00 31.29 N ANISOU 1285 N VAL A 206 4553 3827 3509 855 -129 -1826 N ATOM 1286 CA VAL A 206 79.502 21.157 107.704 1.00 32.18 C ANISOU 1286 CA VAL A 206 4673 3885 3667 825 -177 -2002 C ATOM 1287 C VAL A 206 80.829 21.889 107.895 1.00 33.42 C ANISOU 1287 C VAL A 206 4750 4013 3934 802 -353 -2157 C ATOM 1288 O VAL A 206 81.736 21.405 108.582 1.00 33.97 O ANISOU 1288 O VAL A 206 4847 4121 3938 781 -511 -2258 O ATOM 1289 CB VAL A 206 78.619 21.321 108.960 1.00 33.44 C ANISOU 1289 CB VAL A 206 4901 4148 3655 941 -139 -2062 C ATOM 1290 CG1 VAL A 206 79.250 20.707 110.202 1.00 34.80 C ANISOU 1290 CG1 VAL A 206 5142 4472 3606 1082 -209 -2107 C ATOM 1291 CG2 VAL A 206 78.292 22.787 109.193 1.00 34.46 C ANISOU 1291 CG2 VAL A 206 5031 4200 3861 918 -196 -2217 C ATOM 1292 N MET A 207 80.936 23.060 107.277 1.00 33.79 N ANISOU 1292 N MET A 207 4778 3975 4082 725 -373 -2180 N ATOM 1293 CA MET A 207 82.089 23.923 107.465 1.00 35.36 C ANISOU 1293 CA MET A 207 4789 4157 4487 688 -490 -2294 C ATOM 1294 C MET A 207 81.771 24.949 108.554 1.00 37.01 C ANISOU 1294 C MET A 207 5085 4341 4633 714 -589 -2502 C ATOM 1295 O MET A 207 80.722 25.604 108.515 1.00 36.52 O ANISOU 1295 O MET A 207 5086 4283 4506 707 -341 -2520 O ATOM 1296 CB MET A 207 82.449 24.596 106.153 1.00 34.89 C ANISOU 1296 CB MET A 207 4652 3934 4668 611 -472 -2217 C ATOM 1297 CG MET A 207 83.823 25.236 106.164 1.00 36.59 C ANISOU 1297 CG MET A 207 4691 4086 5124 551 -623 -2306 C ATOM 1298 SD MET A 207 84.248 25.893 104.549 1.00 36.77 S ANISOU 1298 SD MET A 207 4580 3930 5457 451 -475 -2092 S ATOM 1299 CE MET A 207 84.849 24.457 103.666 1.00 35.59 C ANISOU 1299 CE MET A 207 4476 3852 5191 471 -372 -1936 C ATOM 1300 N LEU A 208 82.665 25.071 109.529 1.00 39.02 N ANISOU 1300 N LEU A 208 5293 4697 4833 777 -793 -2634 N ATOM 1301 CA LEU A 208 82.510 26.036 110.630 1.00 41.30 C ANISOU 1301 CA LEU A 208 5669 4964 5058 844 -876 -2887 C ATOM 1302 C LEU A 208 83.731 26.944 110.742 1.00 43.51 C ANISOU 1302 C LEU A 208 5759 5182 5590 750 -1112 -3061 C ATOM 1303 O LEU A 208 84.849 26.533 110.424 1.00 42.73 O ANISOU 1303 O LEU A 208 5642 4821 5771 684 -1260 -3092 O ATOM 1304 CB LEU A 208 82.323 25.301 111.952 1.00 42.53 C ANISOU 1304 CB LEU A 208 5958 5334 4865 1022 -915 -2916 C ATOM 1305 CG LEU A 208 81.099 24.388 112.065 1.00 41.40 C ANISOU 1305 CG LEU A 208 5923 5271 4533 1104 -753 -2735 C ATOM 1306 CD1 LEU A 208 81.148 23.593 113.356 1.00 42.92 C ANISOU 1306 CD1 LEU A 208 6237 5690 4379 1268 -826 -2744 C ATOM 1307 CD2 LEU A 208 79.813 25.185 112.008 1.00 41.09 C ANISOU 1307 CD2 LEU A 208 5965 5158 4487 1127 -616 -2784 C ATOM 1308 N ASP A 209 83.489 28.180 111.190 1.00 45.53 N ANISOU 1308 N ASP A 209 6107 5310 5880 761 -1176 -3273 N ATOM 1309 CA ASP A 209 84.533 29.192 111.380 1.00 48.06 C ANISOU 1309 CA ASP A 209 6258 5533 6468 663 -1446 -3484 C ATOM 1310 C ASP A 209 85.159 29.027 112.758 1.00 51.20 C ANISOU 1310 C ASP A 209 6781 6060 6610 762 -1751 -3626 C ATOM 1311 O ASP A 209 84.576 29.409 113.765 1.00 52.49 O ANISOU 1311 O ASP A 209 7076 6304 6561 873 -1826 -3754 O ATOM 1312 CB ASP A 209 83.939 30.596 111.213 1.00 48.67 C ANISOU 1312 CB ASP A 209 6424 5423 6645 602 -1436 -3616 C ATOM 1313 CG ASP A 209 84.999 31.705 111.168 1.00 50.38 C ANISOU 1313 CG ASP A 209 6493 5498 7150 513 -1648 -3797 C ATOM 1314 OD1 ASP A 209 86.133 31.525 111.666 1.00 51.41 O ANISOU 1314 OD1 ASP A 209 6654 5647 7233 469 -1915 -3978 O ATOM 1315 OD2 ASP A 209 84.667 32.781 110.626 1.00 50.75 O ANISOU 1315 OD2 ASP A 209 6703 5137 7440 402 -1458 -3914 O ATOM 1316 N GLY A 210 86.362 28.467 112.787 1.00 53.09 N ANISOU 1316 N GLY A 210 6740 6436 6993 761 -1856 -3548 N ATOM 1317 CA GLY A 210 87.094 28.239 114.035 1.00 56.60 C ANISOU 1317 CA GLY A 210 7315 7036 7151 869 -2180 -3715 C ATOM 1318 C GLY A 210 87.779 29.454 114.654 1.00 60.91 C ANISOU 1318 C GLY A 210 7954 7343 7846 780 -2494 -4099 C ATOM 1319 O GLY A 210 88.247 29.388 115.792 1.00 64.17 O ANISOU 1319 O GLY A 210 8496 7874 8009 788 -2865 -4438 O ATOM 1320 N SER A 211 87.866 30.553 113.909 1.00 61.83 N ANISOU 1320 N SER A 211 7956 7168 8366 662 -2453 -4073 N ATOM 1321 CA SER A 211 88.487 31.771 114.412 1.00 65.89 C ANISOU 1321 CA SER A 211 8355 7567 9111 499 -2867 -4393 C ATOM 1322 C SER A 211 87.551 32.597 115.300 1.00 68.45 C ANISOU 1322 C SER A 211 8950 7789 9269 798 -2872 -4586 C ATOM 1323 O SER A 211 88.021 33.508 115.975 1.00 73.46 O ANISOU 1323 O SER A 211 9801 8180 9931 676 -3297 -4815 O ATOM 1324 CB SER A 211 89.013 32.634 113.256 1.00 65.39 C ANISOU 1324 CB SER A 211 8008 7174 9661 343 -2764 -4364 C ATOM 1325 OG SER A 211 87.967 33.341 112.608 1.00 62.91 O ANISOU 1325 OG SER A 211 7962 6444 9497 327 -2576 -4585 O ATOM 1326 N ARG A 212 86.252 32.297 115.321 1.00 68.35 N ANISOU 1326 N ARG A 212 8997 7956 9014 761 -2633 -4441 N ATOM 1327 CA ARG A 212 85.306 33.131 116.067 1.00 72.29 C ANISOU 1327 CA ARG A 212 9860 8364 9241 995 -2443 -4837 C ATOM 1328 C ARG A 212 84.882 32.528 117.406 1.00 73.65 C ANISOU 1328 C ARG A 212 10328 8766 8887 1163 -2642 -4907 C ATOM 1329 O ARG A 212 85.077 31.339 117.650 1.00 72.46 O ANISOU 1329 O ARG A 212 10269 8726 8536 1102 -2476 -5042 O ATOM 1330 CB ARG A 212 84.093 33.490 115.195 1.00 72.16 C ANISOU 1330 CB ARG A 212 9711 8437 9268 941 -2258 -4596 C ATOM 1331 CG ARG A 212 83.118 32.373 114.867 1.00 71.19 C ANISOU 1331 CG ARG A 212 9876 8206 8966 824 -1844 -4374 C ATOM 1332 CD ARG A 212 81.787 32.970 114.436 1.00 74.46 C ANISOU 1332 CD ARG A 212 10190 8641 9458 1132 -1779 -4166 C ATOM 1333 NE ARG A 212 81.952 33.878 113.290 1.00 80.05 N ANISOU 1333 NE ARG A 212 11001 9108 10305 878 -1245 -3663 N ATOM 1334 CZ ARG A 212 81.376 35.081 113.130 1.00 83.21 C ANISOU 1334 CZ ARG A 212 11353 9175 11086 1192 -1141 -4124 C ATOM 1335 NH1 ARG A 212 80.570 35.615 114.053 1.00 83.09 N ANISOU 1335 NH1 ARG A 212 11937 9029 10605 1145 -1403 -4645 N ATOM 1336 NH2 ARG A 212 81.627 35.772 112.014 1.00 85.25 N ANISOU 1336 NH2 ARG A 212 11403 9070 11915 846 -1081 -3592 N ATOM 1337 N SER A 213 84.307 33.373 118.265 1.00 75.76 N ANISOU 1337 N SER A 213 10634 9088 9064 1266 -2666 -5138 N ATOM 1338 CA SER A 213 83.805 32.966 119.574 1.00 77.26 C ANISOU 1338 CA SER A 213 11170 9420 8764 1638 -2710 -5234 C ATOM 1339 C SER A 213 82.452 32.358 119.252 1.00 75.38 C ANISOU 1339 C SER A 213 10903 9180 8557 1651 -2181 -4851 C ATOM 1340 O SER A 213 81.636 33.000 118.586 1.00 77.00 O ANISOU 1340 O SER A 213 10867 9771 8618 1638 -1969 -4575 O ATOM 1341 CB SER A 213 83.683 34.159 120.529 1.00 80.65 C ANISOU 1341 CB SER A 213 11855 9847 8938 1730 -2948 -5579 C ATOM 1342 OG SER A 213 82.868 35.185 119.985 1.00 80.16 O ANISOU 1342 OG SER A 213 11732 9469 9255 1623 -2655 -5565 O ATOM 1343 N LYS A 214 82.252 31.117 119.682 1.00 73.74 N ANISOU 1343 N LYS A 214 10642 9283 8090 1949 -2173 -4653 N ATOM 1344 CA LYS A 214 81.107 30.256 119.277 1.00 69.55 C ANISOU 1344 CA LYS A 214 10549 8775 7101 1961 -1758 -4460 C ATOM 1345 C LYS A 214 81.275 29.655 117.861 1.00 63.60 C ANISOU 1345 C LYS A 214 9445 7860 6860 1773 -1604 -3978 C ATOM 1346 O LYS A 214 80.550 29.970 116.894 1.00 58.31 O ANISOU 1346 O LYS A 214 9109 6332 6713 1512 -1319 -3819 O ATOM 1347 CB LYS A 214 79.725 30.914 119.455 1.00 70.33 C ANISOU 1347 CB LYS A 214 10680 8867 7173 2046 -1588 -4503 C ATOM 1348 CG LYS A 214 79.331 31.106 120.908 1.00 74.40 C ANISOU 1348 CG LYS A 214 11551 9539 7176 2357 -1587 -4690 C ATOM 1349 CD LYS A 214 78.002 31.818 121.035 1.00 75.71 C ANISOU 1349 CD LYS A 214 11742 9675 7348 2538 -1352 -4666 C ATOM 1350 CE LYS A 214 77.300 31.482 122.344 1.00 78.96 C ANISOU 1350 CE LYS A 214 12499 10262 7237 2835 -1191 -4595 C ATOM 1351 NZ LYS A 214 75.903 31.994 122.327 1.00 79.27 N ANISOU 1351 NZ LYS A 214 12666 10151 7302 3033 -813 -4520 N ATOM 1352 N ILE A 215 82.240 28.749 117.782 1.00 62.17 N ANISOU 1352 N ILE A 215 9113 7989 6517 1676 -1671 -4087 N ATOM 1353 CA ILE A 215 82.534 28.001 116.557 1.00 58.44 C ANISOU 1353 CA ILE A 215 8435 7390 6377 1472 -1645 -3850 C ATOM 1354 C ILE A 215 81.256 27.360 116.007 1.00 54.37 C ANISOU 1354 C ILE A 215 8136 6715 5804 1613 -1257 -3644 C ATOM 1355 O ILE A 215 80.973 27.435 114.810 1.00 48.63 O ANISOU 1355 O ILE A 215 7448 5282 5745 1506 -1161 -3895 O ATOM 1356 CB ILE A 215 83.598 26.919 116.807 1.00 58.54 C ANISOU 1356 CB ILE A 215 8386 7632 6224 1511 -1764 -3745 C ATOM 1357 CG1 ILE A 215 84.937 27.556 117.209 1.00 60.72 C ANISOU 1357 CG1 ILE A 215 8642 7865 6561 1462 -2150 -4028 C ATOM 1358 CG2 ILE A 215 83.774 26.047 115.558 1.00 56.15 C ANISOU 1358 CG2 ILE A 215 7898 7366 6067 1323 -1539 -3482 C ATOM 1359 CD1 ILE A 215 85.974 26.558 117.681 1.00 61.83 C ANISOU 1359 CD1 ILE A 215 8681 8197 6614 1502 -2352 -3961 C ATOM 1360 N PHE A 216 80.505 26.728 116.903 1.00 55.25 N ANISOU 1360 N PHE A 216 8334 7069 5589 1831 -1101 -3574 N ATOM 1361 CA PHE A 216 79.133 26.311 116.646 1.00 54.58 C ANISOU 1361 CA PHE A 216 8274 7152 5309 1753 -911 -3320 C ATOM 1362 C PHE A 216 78.219 27.212 117.477 1.00 57.03 C ANISOU 1362 C PHE A 216 8655 7558 5455 1942 -819 -3478 C ATOM 1363 O PHE A 216 78.363 27.302 118.697 1.00 60.26 O ANISOU 1363 O PHE A 216 9070 8356 5468 1946 -938 -3554 O ATOM 1364 CB PHE A 216 78.932 24.847 117.030 1.00 53.50 C ANISOU 1364 CB PHE A 216 8146 7225 4956 1948 -729 -3109 C ATOM 1365 CG PHE A 216 77.491 24.425 117.086 1.00 52.32 C ANISOU 1365 CG PHE A 216 8142 6988 4750 2012 -443 -2903 C ATOM 1366 CD1 PHE A 216 76.763 24.248 115.922 1.00 49.78 C ANISOU 1366 CD1 PHE A 216 7688 6542 4682 1838 -267 -2643 C ATOM 1367 CD2 PHE A 216 76.856 24.210 118.308 1.00 54.56 C ANISOU 1367 CD2 PHE A 216 8562 7475 4693 2261 -307 -2970 C ATOM 1368 CE1 PHE A 216 75.427 23.867 115.972 1.00 49.63 C ANISOU 1368 CE1 PHE A 216 7687 6564 4606 1890 -29 -2457 C ATOM 1369 CE2 PHE A 216 75.523 23.825 118.364 1.00 53.89 C ANISOU 1369 CE2 PHE A 216 8544 7376 4553 2358 19 -2809 C ATOM 1370 CZ PHE A 216 74.804 23.653 117.195 1.00 51.36 C ANISOU 1370 CZ PHE A 216 8052 6897 4563 2232 133 -2561 C ATOM 1371 N ASP A 217 77.286 27.881 116.811 1.00 56.57 N ANISOU 1371 N ASP A 217 8588 7319 5585 1895 -683 -3347 N ATOM 1372 CA ASP A 217 76.345 28.775 117.472 1.00 58.52 C ANISOU 1372 CA ASP A 217 9036 7534 5666 2041 -557 -3528 C ATOM 1373 C ASP A 217 74.965 28.139 117.337 1.00 56.84 C ANISOU 1373 C ASP A 217 8896 7294 5405 2122 -189 -3317 C ATOM 1374 O ASP A 217 74.410 28.062 116.246 1.00 53.82 O ANISOU 1374 O ASP A 217 8288 6709 5450 1736 -31 -3385 O ATOM 1375 CB ASP A 217 76.405 30.164 116.813 1.00 58.83 C ANISOU 1375 CB ASP A 217 9054 7293 6005 1834 -653 -3736 C ATOM 1376 CG ASP A 217 75.635 31.246 117.583 1.00 61.57 C ANISOU 1376 CG ASP A 217 9708 7544 6141 2057 -633 -3964 C ATOM 1377 OD1 ASP A 217 75.054 30.975 118.664 1.00 63.60 O ANISOU 1377 OD1 ASP A 217 10153 7826 6187 2344 -405 -3910 O ATOM 1378 OD2 ASP A 217 75.630 32.399 117.082 1.00 61.86 O ANISOU 1378 OD2 ASP A 217 9791 7382 6330 2142 -1000 -4127 O ATOM 1379 N LYS A 218 74.403 27.719 118.461 1.00 58.95 N ANISOU 1379 N LYS A 218 9318 7706 5372 2338 -74 -3210 N ATOM 1380 CA LYS A 218 73.076 27.085 118.485 1.00 58.89 C ANISOU 1380 CA LYS A 218 9300 7703 5373 2392 92 -2968 C ATOM 1381 C LYS A 218 71.926 28.019 118.054 1.00 58.37 C ANISOU 1381 C LYS A 218 9186 7494 5496 2362 263 -3021 C ATOM 1382 O LYS A 218 70.838 27.550 117.726 1.00 56.72 O ANISOU 1382 O LYS A 218 9119 6764 5666 2371 517 -2951 O ATOM 1383 CB LYS A 218 72.795 26.481 119.875 1.00 62.09 C ANISOU 1383 CB LYS A 218 9938 8302 5350 2698 302 -2869 C ATOM 1384 CG LYS A 218 72.844 27.512 121.005 1.00 65.27 C ANISOU 1384 CG LYS A 218 10583 8745 5469 3038 211 -3170 C ATOM 1385 CD LYS A 218 71.665 27.482 121.986 1.00 68.31 C ANISOU 1385 CD LYS A 218 11119 9240 5592 3248 535 -2917 C ATOM 1386 CE LYS A 218 72.089 27.175 123.420 1.00 72.29 C ANISOU 1386 CE LYS A 218 11902 9957 5605 3585 407 -3005 C ATOM 1387 NZ LYS A 218 70.958 26.594 124.198 1.00 74.15 N ANISOU 1387 NZ LYS A 218 12203 10315 5656 3931 911 -2865 N ATOM 1388 N ASP A 219 72.174 29.330 118.058 1.00 58.65 N ANISOU 1388 N ASP A 219 9272 7483 5529 2427 190 -3196 N ATOM 1389 CA ASP A 219 71.199 30.317 117.598 1.00 57.95 C ANISOU 1389 CA ASP A 219 9215 7269 5534 2385 399 -3190 C ATOM 1390 C ASP A 219 71.344 30.677 116.106 1.00 54.21 C ANISOU 1390 C ASP A 219 8466 6514 5616 2199 253 -3156 C ATOM 1391 O ASP A 219 70.547 31.462 115.597 1.00 52.62 O ANISOU 1391 O ASP A 219 8022 6142 5829 2241 352 -3122 O ATOM 1392 CB ASP A 219 71.294 31.582 118.460 1.00 61.64 C ANISOU 1392 CB ASP A 219 9873 7635 5909 2471 281 -3579 C ATOM 1393 CG ASP A 219 71.223 31.280 119.969 1.00 62.73 C ANISOU 1393 CG ASP A 219 10214 7801 5816 2489 426 -3692 C ATOM 1394 OD1 ASP A 219 70.346 30.493 120.397 1.00 66.87 O ANISOU 1394 OD1 ASP A 219 10560 8327 6517 2907 986 -3707 O ATOM 1395 OD2 ASP A 219 72.055 31.830 120.727 1.00 68.82 O ANISOU 1395 OD2 ASP A 219 11365 8771 6010 2837 130 -4210 O ATOM 1396 N SER A 220 72.334 30.111 115.401 1.00 52.02 N ANISOU 1396 N SER A 220 7988 6391 5383 1936 166 -3122 N ATOM 1397 CA SER A 220 72.461 30.325 113.944 1.00 49.35 C ANISOU 1397 CA SER A 220 7486 5858 5407 1667 142 -3117 C ATOM 1398 C SER A 220 71.431 29.472 113.207 1.00 46.76 C ANISOU 1398 C SER A 220 7120 5464 5182 1710 453 -2878 C ATOM 1399 O SER A 220 70.767 28.622 113.810 1.00 46.25 O ANISOU 1399 O SER A 220 6972 5381 5218 2018 731 -2796 O ATOM 1400 CB SER A 220 73.870 29.997 113.449 1.00 48.37 C ANISOU 1400 CB SER A 220 7279 5769 5328 1455 -63 -3182 C ATOM 1401 OG SER A 220 74.146 28.615 113.577 1.00 47.39 O ANISOU 1401 OG SER A 220 6968 5785 5252 1354 -112 -2964 O ATOM 1402 N THR A 221 71.293 29.699 111.906 1.00 45.15 N ANISOU 1402 N THR A 221 6816 5151 5188 1573 480 -2847 N ATOM 1403 CA THR A 221 70.400 28.873 111.081 1.00 44.50 C ANISOU 1403 CA THR A 221 6529 5198 5179 1358 490 -2466 C ATOM 1404 C THR A 221 70.809 27.387 111.117 1.00 44.80 C ANISOU 1404 C THR A 221 6492 5223 5305 1335 527 -2401 C ATOM 1405 O THR A 221 69.937 26.503 111.144 1.00 46.10 O ANISOU 1405 O THR A 221 6444 5402 5668 1294 728 -2159 O ATOM 1406 CB THR A 221 70.381 29.342 109.616 1.00 42.53 C ANISOU 1406 CB THR A 221 6124 4783 5251 1223 393 -2388 C ATOM 1407 OG1 THR A 221 69.983 30.712 109.574 1.00 43.50 O ANISOU 1407 OG1 THR A 221 6443 4708 5375 1190 419 -2783 O ATOM 1408 CG2 THR A 221 69.398 28.510 108.785 1.00 41.10 C ANISOU 1408 CG2 THR A 221 5946 4577 5092 1164 587 -2225 C ATOM 1409 N PHE A 222 72.122 27.120 111.083 1.00 44.30 N ANISOU 1409 N PHE A 222 6443 5235 5155 1266 257 -2442 N ATOM 1410 CA PHE A 222 72.635 25.756 111.167 1.00 43.05 C ANISOU 1410 CA PHE A 222 6310 5242 4802 1247 233 -2272 C ATOM 1411 C PHE A 222 72.297 25.147 112.513 1.00 44.21 C ANISOU 1411 C PHE A 222 6566 5509 4720 1443 254 -2207 C ATOM 1412 O PHE A 222 71.845 24.017 112.595 1.00 43.63 O ANISOU 1412 O PHE A 222 6522 5468 4584 1524 176 -2035 O ATOM 1413 CB PHE A 222 74.145 25.714 110.948 1.00 42.91 C ANISOU 1413 CB PHE A 222 6300 5185 4816 1166 172 -2496 C ATOM 1414 CG PHE A 222 74.751 24.373 111.245 1.00 43.34 C ANISOU 1414 CG PHE A 222 6397 5382 4689 1173 25 -2251 C ATOM 1415 CD1 PHE A 222 74.526 23.289 110.394 1.00 41.48 C ANISOU 1415 CD1 PHE A 222 6111 5089 4560 1163 209 -2089 C ATOM 1416 CD2 PHE A 222 75.527 24.178 112.382 1.00 44.86 C ANISOU 1416 CD2 PHE A 222 6690 5713 4640 1274 -48 -2303 C ATOM 1417 CE1 PHE A 222 75.058 22.054 110.671 1.00 40.97 C ANISOU 1417 CE1 PHE A 222 5970 5216 4377 1265 219 -2012 C ATOM 1418 CE2 PHE A 222 76.077 22.936 112.652 1.00 44.83 C ANISOU 1418 CE2 PHE A 222 6686 5750 4597 1399 41 -2345 C ATOM 1419 CZ PHE A 222 75.837 21.877 111.797 1.00 42.98 C ANISOU 1419 CZ PHE A 222 6412 5560 4358 1326 72 -2112 C ATOM 1420 N GLY A 223 72.521 25.925 113.561 1.00 46.35 N ANISOU 1420 N GLY A 223 6961 5835 4814 1602 317 -2416 N ATOM 1421 CA GLY A 223 72.326 25.473 114.937 1.00 48.84 C ANISOU 1421 CA GLY A 223 7433 6308 4812 1830 375 -2336 C ATOM 1422 C GLY A 223 70.886 25.283 115.383 1.00 49.66 C ANISOU 1422 C GLY A 223 7588 6402 4878 1942 662 -2195 C ATOM 1423 O GLY A 223 70.614 24.410 116.209 1.00 51.59 O ANISOU 1423 O GLY A 223 8030 6927 4643 2050 674 -1988 O ATOM 1424 N SER A 224 69.967 26.085 114.840 1.00 48.69 N ANISOU 1424 N SER A 224 7419 6073 5005 1914 845 -2276 N ATOM 1425 CA SER A 224 68.570 26.055 115.266 1.00 49.96 C ANISOU 1425 CA SER A 224 7527 6341 5115 2036 1019 -2054 C ATOM 1426 C SER A 224 67.611 25.359 114.287 1.00 47.93 C ANISOU 1426 C SER A 224 7182 5937 5089 1946 1249 -1897 C ATOM 1427 O SER A 224 66.539 24.920 114.710 1.00 50.71 O ANISOU 1427 O SER A 224 7285 6326 5656 1897 1477 -1791 O ATOM 1428 CB SER A 224 68.076 27.482 115.569 1.00 51.53 C ANISOU 1428 CB SER A 224 7866 6403 5310 2132 1066 -2189 C ATOM 1429 OG SER A 224 67.747 28.177 114.377 1.00 50.68 O ANISOU 1429 OG SER A 224 7747 5957 5552 1830 923 -2123 O ATOM 1430 N VAL A 225 67.965 25.279 113.005 1.00 44.82 N ANISOU 1430 N VAL A 225 6654 5370 5004 1803 1080 -1902 N ATOM 1431 CA VAL A 225 67.094 24.648 112.006 1.00 44.19 C ANISOU 1431 CA VAL A 225 6328 5390 5070 1560 1081 -1560 C ATOM 1432 C VAL A 225 67.717 23.393 111.369 1.00 42.77 C ANISOU 1432 C VAL A 225 6064 5209 4977 1421 966 -1468 C ATOM 1433 O VAL A 225 67.160 22.298 111.463 1.00 43.71 O ANISOU 1433 O VAL A 225 6277 5240 5089 1396 820 -1047 O ATOM 1434 CB VAL A 225 66.720 25.627 110.878 1.00 42.98 C ANISOU 1434 CB VAL A 225 6087 5084 5157 1405 1031 -1621 C ATOM 1435 CG1 VAL A 225 65.698 24.996 109.941 1.00 42.11 C ANISOU 1435 CG1 VAL A 225 5823 4910 5266 1299 1089 -1393 C ATOM 1436 CG2 VAL A 225 66.173 26.927 111.448 1.00 44.41 C ANISOU 1436 CG2 VAL A 225 6308 5328 5237 1535 1137 -1769 C ATOM 1437 N GLU A 226 68.853 23.570 110.701 1.00 41.48 N ANISOU 1437 N GLU A 226 5940 5058 4759 1372 801 -1631 N ATOM 1438 CA GLU A 226 69.461 22.515 109.885 1.00 39.99 C ANISOU 1438 CA GLU A 226 5719 4828 4648 1197 731 -1580 C ATOM 1439 C GLU A 226 69.809 21.273 110.691 1.00 40.19 C ANISOU 1439 C GLU A 226 5773 4938 4558 1263 833 -1501 C ATOM 1440 O GLU A 226 69.449 20.163 110.299 1.00 40.29 O ANISOU 1440 O GLU A 226 5593 4956 4758 1009 720 -1262 O ATOM 1441 CB GLU A 226 70.720 23.033 109.160 1.00 39.04 C ANISOU 1441 CB GLU A 226 5609 4652 4569 1093 585 -1723 C ATOM 1442 CG GLU A 226 70.428 24.007 108.033 1.00 38.03 C ANISOU 1442 CG GLU A 226 5373 4356 4719 1018 561 -1755 C ATOM 1443 CD GLU A 226 71.663 24.794 107.569 1.00 37.99 C ANISOU 1443 CD GLU A 226 5326 4321 4785 963 553 -1984 C ATOM 1444 OE1 GLU A 226 72.636 24.208 107.066 1.00 35.74 O ANISOU 1444 OE1 GLU A 226 5069 4088 4421 789 412 -1890 O ATOM 1445 OE2 GLU A 226 71.666 26.029 107.698 1.00 39.52 O ANISOU 1445 OE2 GLU A 226 5746 4344 4923 917 955 -2053 O ATOM 1446 N VAL A 227 70.494 21.457 111.815 1.00 40.97 N ANISOU 1446 N VAL A 227 5984 5135 4445 1496 852 -1671 N ATOM 1447 CA VAL A 227 70.987 20.321 112.579 1.00 42.52 C ANISOU 1447 CA VAL A 227 6314 5480 4361 1516 835 -1454 C ATOM 1448 C VAL A 227 69.854 19.455 113.173 1.00 43.62 C ANISOU 1448 C VAL A 227 6364 5660 4548 1623 1073 -1311 C ATOM 1449 O VAL A 227 70.000 18.232 113.307 1.00 44.00 O ANISOU 1449 O VAL A 227 6650 5647 4419 1692 1308 -1397 O ATOM 1450 CB VAL A 227 72.016 20.767 113.646 1.00 44.45 C ANISOU 1450 CB VAL A 227 6668 5790 4428 1620 691 -1709 C ATOM 1451 CG1 VAL A 227 71.337 21.391 114.855 1.00 47.01 C ANISOU 1451 CG1 VAL A 227 7115 6244 4499 1838 842 -1716 C ATOM 1452 CG2 VAL A 227 72.897 19.596 114.060 1.00 45.24 C ANISOU 1452 CG2 VAL A 227 6748 6067 4372 1710 613 -1560 C ATOM 1453 N HIS A 228 68.732 20.090 113.502 1.00 44.13 N ANISOU 1453 N HIS A 228 6432 5665 4671 1701 1152 -1236 N ATOM 1454 CA HIS A 228 67.540 19.397 114.009 1.00 45.49 C ANISOU 1454 CA HIS A 228 6575 5819 4888 1777 1420 -986 C ATOM 1455 C HIS A 228 66.647 18.790 112.918 1.00 44.28 C ANISOU 1455 C HIS A 228 6212 5498 5115 1560 1518 -855 C ATOM 1456 O HIS A 228 65.632 18.167 113.234 1.00 45.82 O ANISOU 1456 O HIS A 228 6226 5665 5519 1617 1798 -808 O ATOM 1457 CB HIS A 228 66.716 20.352 114.877 1.00 47.17 C ANISOU 1457 CB HIS A 228 6811 6066 5046 1944 1604 -967 C ATOM 1458 CG HIS A 228 67.476 20.880 116.049 1.00 48.89 C ANISOU 1458 CG HIS A 228 7294 6407 4875 2166 1543 -1125 C ATOM 1459 ND1 HIS A 228 67.912 20.070 117.074 1.00 50.39 N ANISOU 1459 ND1 HIS A 228 7638 6701 4804 2346 1594 -1061 N ATOM 1460 CD2 HIS A 228 67.921 22.125 116.336 1.00 49.72 C ANISOU 1460 CD2 HIS A 228 7602 6500 4788 2232 1377 -1402 C ATOM 1461 CE1 HIS A 228 68.579 20.798 117.952 1.00 51.92 C ANISOU 1461 CE1 HIS A 228 8079 6969 4678 2544 1481 -1290 C ATOM 1462 NE2 HIS A 228 68.603 22.047 117.524 1.00 51.53 N ANISOU 1462 NE2 HIS A 228 8097 6834 4647 2445 1347 -1499 N ATOM 1463 N ASN A 229 67.012 18.957 111.648 1.00 42.73 N ANISOU 1463 N ASN A 229 5944 5284 5007 1353 1289 -936 N ATOM 1464 CA ASN A 229 66.272 18.336 110.540 1.00 41.76 C ANISOU 1464 CA ASN A 229 5662 4980 5223 1221 1257 -777 C ATOM 1465 C ASN A 229 67.037 17.302 109.724 1.00 40.30 C ANISOU 1465 C ASN A 229 5547 4640 5124 1085 1067 -783 C ATOM 1466 O ASN A 229 66.514 16.776 108.733 1.00 38.84 O ANISOU 1466 O ASN A 229 5248 4245 5264 1024 1019 -679 O ATOM 1467 CB ASN A 229 65.689 19.424 109.656 1.00 41.26 C ANISOU 1467 CB ASN A 229 5514 4830 5332 1158 1174 -848 C ATOM 1468 CG ASN A 229 64.467 20.043 110.290 1.00 42.99 C ANISOU 1468 CG ASN A 229 5602 4994 5738 1250 1362 -769 C ATOM 1469 OD1 ASN A 229 63.382 19.459 110.253 1.00 43.68 O ANISOU 1469 OD1 ASN A 229 5553 4756 6285 1326 1584 -659 O ATOM 1470 ND2 ASN A 229 64.652 21.189 110.943 1.00 43.23 N ANISOU 1470 ND2 ASN A 229 5735 5059 5628 1448 1407 -860 N ATOM 1471 N LEU A 230 68.252 16.991 110.167 1.00 40.46 N ANISOU 1471 N LEU A 230 5638 4808 4927 1160 986 -825 N ATOM 1472 CA LEU A 230 68.981 15.844 109.644 1.00 39.72 C ANISOU 1472 CA LEU A 230 5523 4755 4813 1111 952 -793 C ATOM 1473 C LEU A 230 68.240 14.591 110.119 1.00 41.47 C ANISOU 1473 C LEU A 230 5692 4856 5207 1156 1057 -508 C ATOM 1474 O LEU A 230 68.127 14.343 111.317 1.00 43.75 O ANISOU 1474 O LEU A 230 6085 5358 5180 1157 1293 -652 O ATOM 1475 CB LEU A 230 70.430 15.870 110.131 1.00 39.18 C ANISOU 1475 CB LEU A 230 5611 4773 4502 1150 873 -868 C ATOM 1476 CG LEU A 230 71.240 17.087 109.672 1.00 38.02 C ANISOU 1476 CG LEU A 230 5506 4613 4323 1097 722 -1163 C ATOM 1477 CD1 LEU A 230 72.600 17.140 110.343 1.00 38.48 C ANISOU 1477 CD1 LEU A 230 5664 4792 4163 1160 623 -1369 C ATOM 1478 CD2 LEU A 230 71.423 17.097 108.165 1.00 36.62 C ANISOU 1478 CD2 LEU A 230 5275 4333 4305 894 604 -1111 C ATOM 1479 N GLN A 231 67.692 13.831 109.176 1.00 41.82 N ANISOU 1479 N GLN A 231 5648 4806 5434 1004 978 -445 N ATOM 1480 CA GLN A 231 66.891 12.653 109.503 1.00 44.29 C ANISOU 1480 CA GLN A 231 5909 4988 5930 909 1257 -230 C ATOM 1481 C GLN A 231 67.825 11.489 109.817 1.00 44.23 C ANISOU 1481 C GLN A 231 5939 5058 5809 949 1246 -210 C ATOM 1482 O GLN A 231 68.688 11.183 109.003 1.00 43.66 O ANISOU 1482 O GLN A 231 6081 4833 5673 939 1138 -417 O ATOM 1483 CB GLN A 231 65.970 12.293 108.338 1.00 45.07 C ANISOU 1483 CB GLN A 231 5838 4998 6290 695 1120 -178 C ATOM 1484 CG GLN A 231 64.993 13.400 107.992 1.00 46.33 C ANISOU 1484 CG GLN A 231 5846 5106 6648 672 1054 -83 C ATOM 1485 CD GLN A 231 63.916 12.946 107.020 1.00 48.51 C ANISOU 1485 CD GLN A 231 5879 5322 7228 312 831 45 C ATOM 1486 OE1 GLN A 231 63.043 12.152 107.381 1.00 54.78 O ANISOU 1486 OE1 GLN A 231 6222 5987 8605 61 836 399 O ATOM 1487 NE2 GLN A 231 63.943 13.475 105.796 1.00 47.47 N ANISOU 1487 NE2 GLN A 231 5674 5331 7030 286 825 -265 N ATOM 1488 N PRO A 232 67.678 10.847 110.996 1.00 46.05 N ANISOU 1488 N PRO A 232 6140 5429 5926 1131 1430 -14 N ATOM 1489 CA PRO A 232 68.512 9.670 111.302 1.00 46.53 C ANISOU 1489 CA PRO A 232 6384 5408 5884 1194 1521 118 C ATOM 1490 C PRO A 232 68.247 8.406 110.462 1.00 46.59 C ANISOU 1490 C PRO A 232 6412 5330 5959 995 1471 245 C ATOM 1491 O PRO A 232 69.110 7.524 110.364 1.00 46.14 O ANISOU 1491 O PRO A 232 6591 5166 5774 1076 1472 658 O ATOM 1492 CB PRO A 232 68.189 9.386 112.771 1.00 48.83 C ANISOU 1492 CB PRO A 232 6678 5839 6034 1424 1771 224 C ATOM 1493 CG PRO A 232 66.914 10.100 113.073 1.00 49.55 C ANISOU 1493 CG PRO A 232 6664 5895 6267 1427 1908 321 C ATOM 1494 CD PRO A 232 66.866 11.272 112.159 1.00 47.85 C ANISOU 1494 CD PRO A 232 6413 5660 6106 1354 1650 91 C ATOM 1495 N GLU A 233 67.072 8.334 109.850 1.00 48.38 N ANISOU 1495 N GLU A 233 6304 5483 6594 752 1462 309 N ATOM 1496 CA GLU A 233 66.720 7.224 108.926 1.00 50.19 C ANISOU 1496 CA GLU A 233 6638 5249 7181 707 1509 198 C ATOM 1497 C GLU A 233 67.579 7.199 107.638 1.00 47.45 C ANISOU 1497 C GLU A 233 6521 4657 6849 558 1236 7 C ATOM 1498 O GLU A 233 67.495 6.244 106.861 1.00 49.18 O ANISOU 1498 O GLU A 233 6998 4445 7241 913 1171 -43 O ATOM 1499 CB GLU A 233 65.222 7.277 108.511 1.00 53.14 C ANISOU 1499 CB GLU A 233 6672 5496 8022 598 1315 297 C ATOM 1500 CG GLU A 233 64.186 7.306 109.654 1.00 56.17 C ANISOU 1500 CG GLU A 233 6851 5991 8499 692 1631 589 C ATOM 1501 CD GLU A 233 63.812 8.758 110.049 1.00 56.36 C ANISOU 1501 CD GLU A 233 6663 6268 8483 1001 1528 261 C ATOM 1502 OE1 GLU A 233 64.644 9.438 110.697 1.00 56.33 O ANISOU 1502 OE1 GLU A 233 7026 6242 8134 1128 1655 241 O ATOM 1503 OE2 GLU A 233 62.717 9.259 109.659 1.00 63.68 O ANISOU 1503 OE2 GLU A 233 6695 8047 9450 1152 1339 208 O ATOM 1504 N LYS A 234 68.360 8.249 107.383 1.00 43.28 N ANISOU 1504 N LYS A 234 5948 4508 5987 705 1100 -307 N ATOM 1505 CA LYS A 234 69.176 8.318 106.182 1.00 40.92 C ANISOU 1505 CA LYS A 234 5688 4125 5734 461 793 -330 C ATOM 1506 C LYS A 234 70.503 9.075 106.304 1.00 37.55 C ANISOU 1506 C LYS A 234 5505 3843 4918 686 742 -490 C ATOM 1507 O LYS A 234 71.403 8.822 105.518 1.00 35.46 O ANISOU 1507 O LYS A 234 5233 3546 4693 449 567 -544 O ATOM 1508 CB LYS A 234 68.335 8.816 104.986 1.00 41.33 C ANISOU 1508 CB LYS A 234 5710 4030 5961 407 621 -329 C ATOM 1509 CG LYS A 234 67.801 10.233 105.055 1.00 40.89 C ANISOU 1509 CG LYS A 234 5588 4065 5883 415 619 -521 C ATOM 1510 CD LYS A 234 67.054 10.570 103.757 1.00 40.88 C ANISOU 1510 CD LYS A 234 5515 3930 6085 249 427 -547 C ATOM 1511 CE LYS A 234 66.327 11.901 103.850 1.00 40.95 C ANISOU 1511 CE LYS A 234 5357 4052 6149 294 469 -562 C ATOM 1512 NZ LYS A 234 65.676 12.378 102.581 1.00 41.72 N ANISOU 1512 NZ LYS A 234 5464 4116 6269 171 258 -637 N ATOM 1513 N VAL A 235 70.634 9.995 107.254 1.00 36.53 N ANISOU 1513 N VAL A 235 5259 3863 4755 769 859 -471 N ATOM 1514 CA VAL A 235 71.940 10.547 107.600 1.00 35.72 C ANISOU 1514 CA VAL A 235 5300 3922 4347 825 766 -563 C ATOM 1515 C VAL A 235 72.580 9.618 108.617 1.00 35.89 C ANISOU 1515 C VAL A 235 5351 4025 4260 937 899 -526 C ATOM 1516 O VAL A 235 71.978 9.340 109.652 1.00 37.45 O ANISOU 1516 O VAL A 235 5577 4270 4382 905 1054 -475 O ATOM 1517 CB VAL A 235 71.845 11.984 108.166 1.00 35.53 C ANISOU 1517 CB VAL A 235 5202 4059 4236 920 776 -709 C ATOM 1518 CG1 VAL A 235 73.220 12.499 108.594 1.00 34.78 C ANISOU 1518 CG1 VAL A 235 5212 4087 3916 1035 717 -852 C ATOM 1519 CG2 VAL A 235 71.251 12.913 107.115 1.00 34.73 C ANISOU 1519 CG2 VAL A 235 5050 3829 4315 783 667 -793 C ATOM 1520 N GLN A 236 73.791 9.155 108.325 1.00 34.81 N ANISOU 1520 N GLN A 236 5322 3896 4008 946 820 -550 N ATOM 1521 CA GLN A 236 74.556 8.331 109.263 1.00 35.81 C ANISOU 1521 CA GLN A 236 5483 4166 3957 1114 940 -432 C ATOM 1522 C GLN A 236 75.656 9.096 110.019 1.00 36.32 C ANISOU 1522 C GLN A 236 5605 4464 3729 1184 861 -573 C ATOM 1523 O GLN A 236 75.971 8.727 111.153 1.00 38.39 O ANISOU 1523 O GLN A 236 5980 4858 3746 1281 792 -526 O ATOM 1524 CB GLN A 236 75.141 7.121 108.542 1.00 35.24 C ANISOU 1524 CB GLN A 236 5474 3955 3958 1063 897 -334 C ATOM 1525 CG GLN A 236 74.052 6.237 107.966 1.00 35.59 C ANISOU 1525 CG GLN A 236 5466 3793 4262 976 968 -229 C ATOM 1526 CD GLN A 236 74.541 4.909 107.424 1.00 35.75 C ANISOU 1526 CD GLN A 236 5573 3702 4308 935 978 -189 C ATOM 1527 OE1 GLN A 236 75.483 4.312 107.953 1.00 36.43 O ANISOU 1527 OE1 GLN A 236 5686 3878 4275 1088 958 -261 O ATOM 1528 NE2 GLN A 236 73.880 4.418 106.379 1.00 35.53 N ANISOU 1528 NE2 GLN A 236 5576 3459 4464 841 910 -156 N ATOM 1529 N THR A 237 76.222 10.154 109.419 1.00 35.24 N ANISOU 1529 N THR A 237 5447 4342 3597 1140 708 -721 N ATOM 1530 CA THR A 237 77.328 10.900 110.041 1.00 35.21 C ANISOU 1530 CA THR A 237 5438 4475 3461 1258 650 -838 C ATOM 1531 C THR A 237 77.355 12.352 109.620 1.00 34.31 C ANISOU 1531 C THR A 237 5257 4371 3406 1170 563 -1008 C ATOM 1532 O THR A 237 77.212 12.647 108.454 1.00 31.94 O ANISOU 1532 O THR A 237 4850 3977 3306 1027 538 -1271 O ATOM 1533 CB THR A 237 78.699 10.285 109.671 1.00 34.94 C ANISOU 1533 CB THR A 237 5438 4463 3372 1277 600 -830 C ATOM 1534 OG1 THR A 237 78.694 8.871 109.925 1.00 35.36 O ANISOU 1534 OG1 THR A 237 5721 4458 3253 1296 856 -744 O ATOM 1535 CG2 THR A 237 79.838 10.939 110.474 1.00 35.76 C ANISOU 1535 CG2 THR A 237 5525 4741 3320 1366 484 -943 C ATOM 1536 N LEU A 238 77.557 13.244 110.585 1.00 35.44 N ANISOU 1536 N LEU A 238 5415 4658 3393 1248 496 -1116 N ATOM 1537 CA LEU A 238 77.889 14.644 110.326 1.00 35.14 C ANISOU 1537 CA LEU A 238 5366 4590 3396 1232 316 -1274 C ATOM 1538 C LEU A 238 79.397 14.815 110.524 1.00 35.44 C ANISOU 1538 C LEU A 238 5406 4669 3388 1282 161 -1387 C ATOM 1539 O LEU A 238 79.913 14.527 111.607 1.00 36.78 O ANISOU 1539 O LEU A 238 5619 4910 3443 1518 92 -1421 O ATOM 1540 CB LEU A 238 77.132 15.571 111.275 1.00 36.48 C ANISOU 1540 CB LEU A 238 5537 4836 3486 1348 359 -1358 C ATOM 1541 CG LEU A 238 77.446 17.083 111.202 1.00 36.74 C ANISOU 1541 CG LEU A 238 5564 4865 3529 1259 222 -1545 C ATOM 1542 CD1 LEU A 238 76.873 17.714 109.945 1.00 35.50 C ANISOU 1542 CD1 LEU A 238 5317 4546 3624 1117 117 -1609 C ATOM 1543 CD2 LEU A 238 76.922 17.824 112.417 1.00 38.34 C ANISOU 1543 CD2 LEU A 238 5820 5135 3612 1450 239 -1642 C ATOM 1544 N GLU A 239 80.090 15.282 109.486 1.00 34.54 N ANISOU 1544 N GLU A 239 5198 4553 3371 1181 98 -1496 N ATOM 1545 CA GLU A 239 81.505 15.610 109.559 1.00 35.30 C ANISOU 1545 CA GLU A 239 5219 4735 3458 1161 -100 -1533 C ATOM 1546 C GLU A 239 81.716 17.135 109.597 1.00 36.04 C ANISOU 1546 C GLU A 239 5272 4760 3661 1118 -211 -1656 C ATOM 1547 O GLU A 239 81.390 17.842 108.651 1.00 35.90 O ANISOU 1547 O GLU A 239 4965 4882 3792 1075 -282 -1581 O ATOM 1548 CB GLU A 239 82.275 14.986 108.382 1.00 34.25 C ANISOU 1548 CB GLU A 239 5045 4462 3505 1098 -66 -1413 C ATOM 1549 CG GLU A 239 83.783 15.199 108.475 1.00 35.01 C ANISOU 1549 CG GLU A 239 5040 4620 3640 1146 -124 -1455 C ATOM 1550 CD GLU A 239 84.609 14.304 107.572 1.00 34.34 C ANISOU 1550 CD GLU A 239 4951 4419 3676 1108 -59 -1316 C ATOM 1551 OE1 GLU A 239 84.386 13.089 107.559 1.00 34.23 O ANISOU 1551 OE1 GLU A 239 4882 4358 3764 1223 97 -1143 O ATOM 1552 OE2 GLU A 239 85.514 14.817 106.886 1.00 33.04 O ANISOU 1552 OE2 GLU A 239 4618 4204 3729 1109 -171 -1407 O ATOM 1553 N ALA A 240 82.313 17.625 110.684 1.00 37.81 N ANISOU 1553 N ALA A 240 5545 5053 3766 1176 -320 -1824 N ATOM 1554 CA ALA A 240 82.628 19.048 110.861 1.00 38.14 C ANISOU 1554 CA ALA A 240 5457 5089 3945 1211 -453 -2016 C ATOM 1555 C ALA A 240 84.064 19.374 110.440 1.00 38.40 C ANISOU 1555 C ALA A 240 5388 5075 4124 1098 -626 -2033 C ATOM 1556 O ALA A 240 85.009 18.701 110.841 1.00 39.97 O ANISOU 1556 O ALA A 240 5367 5532 4284 1140 -843 -2079 O ATOM 1557 CB ALA A 240 82.419 19.447 112.318 1.00 40.14 C ANISOU 1557 CB ALA A 240 5801 5482 3968 1340 -578 -2166 C ATOM 1558 N TRP A 241 84.216 20.405 109.628 1.00 37.63 N ANISOU 1558 N TRP A 241 5154 4810 4332 984 -645 -2122 N ATOM 1559 CA TRP A 241 85.509 20.929 109.272 1.00 38.09 C ANISOU 1559 CA TRP A 241 5069 4866 4536 952 -757 -2175 C ATOM 1560 C TRP A 241 85.646 22.299 109.930 1.00 40.14 C ANISOU 1560 C TRP A 241 5320 5088 4843 878 -1001 -2423 C ATOM 1561 O TRP A 241 84.974 23.266 109.523 1.00 39.33 O ANISOU 1561 O TRP A 241 5286 4818 4836 790 -1025 -2587 O ATOM 1562 CB TRP A 241 85.592 21.072 107.765 1.00 36.43 C ANISOU 1562 CB TRP A 241 4771 4502 4566 829 -642 -2060 C ATOM 1563 CG TRP A 241 85.508 19.787 106.994 1.00 34.94 C ANISOU 1563 CG TRP A 241 4661 4322 4293 804 -547 -1820 C ATOM 1564 CD1 TRP A 241 85.701 18.528 107.458 1.00 34.65 C ANISOU 1564 CD1 TRP A 241 4613 4408 4143 919 -525 -1757 C ATOM 1565 CD2 TRP A 241 85.266 19.666 105.594 1.00 33.64 C ANISOU 1565 CD2 TRP A 241 4586 3984 4210 768 -339 -1750 C ATOM 1566 NE1 TRP A 241 85.579 17.633 106.440 1.00 33.49 N ANISOU 1566 NE1 TRP A 241 4556 4201 3967 878 -351 -1571 N ATOM 1567 CE2 TRP A 241 85.304 18.299 105.283 1.00 32.62 C ANISOU 1567 CE2 TRP A 241 4485 3906 4000 804 -210 -1546 C ATOM 1568 CE3 TRP A 241 85.005 20.585 104.575 1.00 33.06 C ANISOU 1568 CE3 TRP A 241 4467 3774 4320 752 -275 -1761 C ATOM 1569 CZ2 TRP A 241 85.096 17.818 103.992 1.00 31.51 C ANISOU 1569 CZ2 TRP A 241 4411 3624 3935 730 -122 -1437 C ATOM 1570 CZ3 TRP A 241 84.790 20.114 103.293 1.00 31.96 C ANISOU 1570 CZ3 TRP A 241 4373 3547 4220 732 -184 -1590 C ATOM 1571 CH2 TRP A 241 84.837 18.737 103.010 1.00 31.31 C ANISOU 1571 CH2 TRP A 241 4363 3502 4030 730 -129 -1460 C ATOM 1572 N VAL A 242 86.482 22.385 110.962 1.00 42.28 N ANISOU 1572 N VAL A 242 5496 5503 5063 947 -1207 -2514 N ATOM 1573 CA VAL A 242 86.724 23.681 111.637 1.00 44.29 C ANISOU 1573 CA VAL A 242 5726 5693 5408 937 -1388 -2758 C ATOM 1574 C VAL A 242 87.881 24.394 110.941 1.00 45.01 C ANISOU 1574 C VAL A 242 5604 5642 5857 792 -1484 -2799 C ATOM 1575 O VAL A 242 89.008 23.904 110.951 1.00 46.07 O ANISOU 1575 O VAL A 242 5536 6045 5923 781 -1711 -2685 O ATOM 1576 CB VAL A 242 86.930 23.575 113.172 1.00 46.59 C ANISOU 1576 CB VAL A 242 6116 6155 5428 1088 -1595 -2917 C ATOM 1577 CG1 VAL A 242 85.706 22.950 113.823 1.00 45.92 C ANISOU 1577 CG1 VAL A 242 6275 6192 4980 1269 -1407 -2877 C ATOM 1578 CG2 VAL A 242 88.165 22.778 113.544 1.00 48.04 C ANISOU 1578 CG2 VAL A 242 6211 6450 5591 1152 -1740 -2836 C ATOM 1579 N ILE A 243 87.581 25.528 110.319 1.00 44.53 N ANISOU 1579 N ILE A 243 5486 5383 6050 662 -1470 -2915 N ATOM 1580 CA ILE A 243 88.571 26.305 109.578 1.00 45.87 C ANISOU 1580 CA ILE A 243 5432 5405 6592 533 -1490 -2857 C ATOM 1581 C ILE A 243 89.294 27.287 110.533 1.00 49.41 C ANISOU 1581 C ILE A 243 5760 5847 7165 473 -1814 -3161 C ATOM 1582 O ILE A 243 88.647 27.992 111.315 1.00 50.19 O ANISOU 1582 O ILE A 243 6210 5702 7157 442 -1983 -3489 O ATOM 1583 CB ILE A 243 87.919 27.116 108.433 1.00 44.60 C ANISOU 1583 CB ILE A 243 5218 5075 6653 436 -1319 -2786 C ATOM 1584 CG1 ILE A 243 86.952 26.263 107.597 1.00 41.91 C ANISOU 1584 CG1 ILE A 243 5032 4743 6146 480 -1048 -2592 C ATOM 1585 CG2 ILE A 243 88.987 27.722 107.532 1.00 45.45 C ANISOU 1585 CG2 ILE A 243 5061 5022 7184 336 -1323 -2673 C ATOM 1586 CD1 ILE A 243 87.565 25.042 106.927 1.00 40.91 C ANISOU 1586 CD1 ILE A 243 4864 4670 6007 522 -951 -2357 C ATOM 1587 N HIS A 244 90.623 27.329 110.449 1.00 51.14 N ANISOU 1587 N HIS A 244 5737 6023 7668 431 -1999 -3126 N ATOM 1588 CA HIS A 244 91.441 28.187 111.309 1.00 54.55 C ANISOU 1588 CA HIS A 244 6089 6357 8279 404 -2341 -3390 C ATOM 1589 C HIS A 244 91.779 29.532 110.650 1.00 56.44 C ANISOU 1589 C HIS A 244 6167 6332 8945 169 -2326 -3383 C ATOM 1590 O HIS A 244 91.737 29.658 109.428 1.00 54.94 O ANISOU 1590 O HIS A 244 5843 6100 8932 73 -2110 -3348 O ATOM 1591 CB HIS A 244 92.738 27.478 111.680 1.00 56.08 C ANISOU 1591 CB HIS A 244 6120 6654 8534 435 -2525 -3322 C ATOM 1592 CG HIS A 244 92.547 26.308 112.599 1.00 55.92 C ANISOU 1592 CG HIS A 244 6280 6900 8067 614 -2543 -3305 C ATOM 1593 ND1 HIS A 244 93.258 26.158 113.768 1.00 58.72 N ANISOU 1593 ND1 HIS A 244 6572 7417 8320 690 -2863 -3438 N ATOM 1594 CD2 HIS A 244 91.725 25.234 112.523 1.00 53.70 C ANISOU 1594 CD2 HIS A 244 6224 6743 7434 719 -2288 -3140 C ATOM 1595 CE1 HIS A 244 92.899 25.035 114.364 1.00 58.26 C ANISOU 1595 CE1 HIS A 244 6748 7556 7832 868 -2807 -3340 C ATOM 1596 NE2 HIS A 244 91.967 24.456 113.632 1.00 55.17 N ANISOU 1596 NE2 HIS A 244 6542 7145 7273 879 -2451 -3187 N ATOM 1597 N GLY A 245 92.117 30.525 111.482 1.00 59.74 N ANISOU 1597 N GLY A 245 6578 6610 9507 135 -2634 -3687 N ATOM 1598 CA GLY A 245 92.591 31.831 111.011 1.00 61.36 C ANISOU 1598 CA GLY A 245 6530 6562 10222 -5 -2725 -3754 C ATOM 1599 C GLY A 245 94.019 32.137 111.426 1.00 65.28 C ANISOU 1599 C GLY A 245 6668 7015 11119 -84 -3048 -3801 C ATOM 1600 O GLY A 245 94.379 33.317 111.540 1.00 69.16 O ANISOU 1600 O GLY A 245 7269 6935 12072 -45 -2996 -3857 O ATOM 1601 N GLY A 246 94.838 31.098 111.650 1.00 65.32 N ANISOU 1601 N GLY A 246 6616 7172 11029 -43 -3131 -3735 N ATOM 1602 CA GLY A 246 96.189 31.276 112.234 1.00 69.08 C ANISOU 1602 CA GLY A 246 6817 7649 11778 -63 -3500 -3818 C ATOM 1603 C GLY A 246 96.258 32.226 113.434 1.00 72.59 C ANISOU 1603 C GLY A 246 7335 7997 12249 -262 -3963 -4234 C ATOM 1604 O GLY A 246 97.127 32.098 114.297 1.00 75.11 O ANISOU 1604 O GLY A 246 7573 8332 12632 -365 -4304 -4362 O ATOM 1605 N ARG A 251 96.412 24.929 118.074 1.00 85.20 N ANISOU 1605 N ARG A 251 9451 11835 11086 850 -4374 -4130 N ATOM 1606 CA ARG A 251 95.507 24.263 119.011 1.00 85.25 C ANISOU 1606 CA ARG A 251 10167 11749 10471 1323 -4161 -3989 C ATOM 1607 C ARG A 251 94.428 23.362 118.355 1.00 81.95 C ANISOU 1607 C ARG A 251 10046 11314 9775 1205 -3704 -3587 C ATOM 1608 O ARG A 251 94.109 23.503 117.168 1.00 82.65 O ANISOU 1608 O ARG A 251 10039 11594 9771 907 -3554 -3251 O ATOM 1609 CB ARG A 251 94.835 25.273 119.932 1.00 87.76 C ANISOU 1609 CB ARG A 251 10763 11891 10690 1436 -4402 -4407 C ATOM 1610 CG ARG A 251 94.646 26.694 119.412 1.00 88.58 C ANISOU 1610 CG ARG A 251 10743 11754 11160 1337 -4448 -4476 C ATOM 1611 CD ARG A 251 93.393 27.309 119.982 1.00 88.57 C ANISOU 1611 CD ARG A 251 11139 11688 10824 1515 -4370 -4664 C ATOM 1612 NE ARG A 251 93.297 27.231 121.453 1.00 91.45 N ANISOU 1612 NE ARG A 251 11774 12236 10735 1893 -4553 -4992 N ATOM 1613 CZ ARG A 251 92.156 27.131 122.150 1.00 90.62 C ANISOU 1613 CZ ARG A 251 12030 12260 10141 2017 -4486 -4978 C ATOM 1614 NH1 ARG A 251 90.958 27.088 121.554 1.00 86.28 N ANISOU 1614 NH1 ARG A 251 11701 11522 9557 2009 -4055 -4945 N ATOM 1615 NH2 ARG A 251 92.212 27.064 123.479 1.00 94.00 N ANISOU 1615 NH2 ARG A 251 12655 12902 10158 2289 -4747 -5016 N ATOM 1616 N ASP A 252 93.868 22.447 119.155 1.00 80.72 N ANISOU 1616 N ASP A 252 10216 11281 9172 1536 -3614 -3613 N ATOM 1617 CA ASP A 252 92.805 21.508 118.717 1.00 75.47 C ANISOU 1617 CA ASP A 252 9576 10712 8386 1837 -3140 -3340 C ATOM 1618 C ASP A 252 91.399 22.048 118.999 1.00 72.69 C ANISOU 1618 C ASP A 252 9606 10246 7764 1756 -3070 -3535 C ATOM 1619 O ASP A 252 90.864 21.871 120.094 1.00 72.71 O ANISOU 1619 O ASP A 252 9775 10376 7474 2008 -3230 -3668 O ATOM 1620 CB ASP A 252 92.992 20.130 119.387 1.00 76.77 C ANISOU 1620 CB ASP A 252 9903 11069 8195 1988 -3132 -3080 C ATOM 1621 CG ASP A 252 91.997 19.061 118.881 1.00 74.62 C ANISOU 1621 CG ASP A 252 9675 10779 7898 1954 -2724 -2774 C ATOM 1622 OD1 ASP A 252 91.117 19.350 118.037 1.00 72.83 O ANISOU 1622 OD1 ASP A 252 9384 10613 7675 1676 -2532 -2692 O ATOM 1623 OD2 ASP A 252 92.108 17.907 119.343 1.00 78.29 O ANISOU 1623 OD2 ASP A 252 10420 10907 8418 1993 -2550 -2512 O ATOM 1624 N LEU A 253 90.793 22.652 117.979 1.00 69.41 N ANISOU 1624 N LEU A 253 9006 9673 7690 1581 -2820 -3585 N ATOM 1625 CA LEU A 253 89.473 23.284 118.099 1.00 68.09 C ANISOU 1625 CA LEU A 253 9109 9359 7403 1634 -2643 -3599 C ATOM 1626 C LEU A 253 88.303 22.300 118.152 1.00 65.01 C ANISOU 1626 C LEU A 253 8833 9166 6700 1890 -2322 -3423 C ATOM 1627 O LEU A 253 87.225 22.679 118.589 1.00 62.50 O ANISOU 1627 O LEU A 253 9059 8523 6162 1874 -2316 -3727 O ATOM 1628 CB LEU A 253 89.242 24.303 116.972 1.00 67.53 C ANISOU 1628 CB LEU A 253 8838 9134 7684 1485 -2507 -3514 C ATOM 1629 CG LEU A 253 89.828 25.709 117.160 1.00 70.71 C ANISOU 1629 CG LEU A 253 9119 9413 8332 1246 -2820 -3771 C ATOM 1630 CD1 LEU A 253 91.213 25.675 117.784 1.00 74.18 C ANISOU 1630 CD1 LEU A 253 9356 9966 8862 1343 -3172 -3813 C ATOM 1631 CD2 LEU A 253 89.874 26.471 115.848 1.00 68.88 C ANISOU 1631 CD2 LEU A 253 8680 8992 8498 1021 -2729 -3742 C ATOM 1632 N CYS A 254 88.505 21.045 117.741 1.00 63.34 N ANISOU 1632 N CYS A 254 8559 9051 6456 1774 -2185 -3183 N ATOM 1633 CA CYS A 254 87.477 20.003 117.925 1.00 61.51 C ANISOU 1633 CA CYS A 254 8552 8932 5886 1955 -1880 -2877 C ATOM 1634 C CYS A 254 87.179 19.687 119.394 1.00 64.03 C ANISOU 1634 C CYS A 254 9078 9486 5761 2248 -1984 -2872 C ATOM 1635 O CYS A 254 86.171 19.035 119.688 1.00 62.56 O ANISOU 1635 O CYS A 254 9067 9413 5287 2370 -1894 -2817 O ATOM 1636 CB CYS A 254 87.856 18.711 117.198 1.00 59.86 C ANISOU 1636 CB CYS A 254 8240 8773 5731 1874 -1738 -2617 C ATOM 1637 SG CYS A 254 87.829 18.856 115.398 1.00 57.96 S ANISOU 1637 SG CYS A 254 7677 8620 5722 1452 -1797 -2654 S ATOM 1638 N GLN A 255 88.059 20.126 120.300 1.00 66.60 N ANISOU 1638 N GLN A 255 9386 9908 6010 2357 -2312 -2990 N ATOM 1639 CA GLN A 255 87.811 20.047 121.747 1.00 69.04 C ANISOU 1639 CA GLN A 255 10010 10262 5958 2712 -2289 -3245 C ATOM 1640 C GLN A 255 86.983 21.201 122.305 1.00 69.40 C ANISOU 1640 C GLN A 255 10307 10270 5789 2755 -2373 -3427 C ATOM 1641 O GLN A 255 86.500 21.092 123.424 1.00 70.84 O ANISOU 1641 O GLN A 255 10960 10344 5609 3286 -2334 -3636 O ATOM 1642 CB GLN A 255 89.135 19.945 122.542 1.00 72.76 C ANISOU 1642 CB GLN A 255 10392 10961 6291 2720 -2710 -3395 C ATOM 1643 CG GLN A 255 89.971 18.679 122.312 1.00 73.08 C ANISOU 1643 CG GLN A 255 10326 11040 6399 2820 -2682 -3039 C ATOM 1644 CD GLN A 255 89.149 17.458 121.896 1.00 71.25 C ANISOU 1644 CD GLN A 255 10289 10757 6023 2788 -2196 -2782 C ATOM 1645 OE1 GLN A 255 88.438 16.866 122.712 1.00 73.73 O ANISOU 1645 OE1 GLN A 255 10929 11437 5645 3158 -1901 -2570 O ATOM 1646 NE2 GLN A 255 89.237 17.082 120.617 1.00 69.19 N ANISOU 1646 NE2 GLN A 255 9938 10323 6027 2597 -1947 -2644 N ATOM 1647 N ASP A 256 86.810 22.285 121.539 1.00 67.90 N ANISOU 1647 N ASP A 256 9941 9896 5962 2551 -2318 -3585 N ATOM 1648 CA ASP A 256 86.070 23.478 121.993 1.00 68.41 C ANISOU 1648 CA ASP A 256 10162 9931 5900 2517 -2385 -3885 C ATOM 1649 C ASP A 256 84.684 23.078 122.528 1.00 67.11 C ANISOU 1649 C ASP A 256 10296 9800 5402 2789 -2151 -3769 C ATOM 1650 O ASP A 256 84.040 22.202 121.943 1.00 63.65 O ANISOU 1650 O ASP A 256 9880 9379 4924 2781 -1734 -3548 O ATOM 1651 CB ASP A 256 85.980 24.539 120.859 1.00 66.95 C ANISOU 1651 CB ASP A 256 9816 9461 6159 2219 -2380 -3965 C ATOM 1652 CG ASP A 256 85.125 25.776 121.231 1.00 68.70 C ANISOU 1652 CG ASP A 256 10222 9597 6282 2305 -2302 -4204 C ATOM 1653 OD1 ASP A 256 83.940 25.595 121.551 1.00 68.42 O ANISOU 1653 OD1 ASP A 256 10327 9795 5871 2312 -2148 -4309 O ATOM 1654 OD2 ASP A 256 85.610 26.938 121.190 1.00 70.73 O ANISOU 1654 OD2 ASP A 256 10529 9734 6609 2069 -2157 -4547 O ATOM 1655 N PRO A 257 84.237 23.700 123.655 1.00 75.79 N ANISOU 1655 N PRO A 257 13068 10559 5167 360 -2190 -3367 N ATOM 1656 CA PRO A 257 82.927 23.383 124.250 1.00 76.14 C ANISOU 1656 CA PRO A 257 13283 10743 4901 533 -1885 -3427 C ATOM 1657 C PRO A 257 81.742 23.379 123.271 1.00 71.48 C ANISOU 1657 C PRO A 257 12637 9831 4689 777 -1418 -3457 C ATOM 1658 O PRO A 257 80.863 22.527 123.400 1.00 70.85 O ANISOU 1658 O PRO A 257 12434 9858 4626 946 -1102 -3250 O ATOM 1659 CB PRO A 257 82.742 24.474 125.334 1.00 81.29 C ANISOU 1659 CB PRO A 257 14305 11518 5060 365 -1850 -3926 C ATOM 1660 CG PRO A 257 83.869 25.438 125.161 1.00 82.68 C ANISOU 1660 CG PRO A 257 14512 11564 5338 123 -2197 -4165 C ATOM 1661 CD PRO A 257 84.966 24.678 124.490 1.00 80.28 C ANISOU 1661 CD PRO A 257 13853 11287 5363 103 -2493 -3690 C ATOM 1662 N THR A 258 81.732 24.303 122.309 1.00 68.77 N ANISOU 1662 N THR A 258 12216 9164 4750 798 -1421 -3730 N ATOM 1663 CA THR A 258 80.648 24.386 121.319 1.00 65.27 C ANISOU 1663 CA THR A 258 11664 8420 4712 1014 -1083 -3696 C ATOM 1664 C THR A 258 80.626 23.216 120.317 1.00 60.52 C ANISOU 1664 C THR A 258 10742 7833 4418 1125 -1065 -3250 C ATOM 1665 O THR A 258 79.556 22.863 119.817 1.00 57.33 O ANISOU 1665 O THR A 258 10426 7300 4055 1353 -752 -3259 O ATOM 1666 CB THR A 258 80.673 25.699 120.518 1.00 64.84 C ANISOU 1666 CB THR A 258 11618 7985 5031 1024 -1079 -3958 C ATOM 1667 OG1 THR A 258 81.847 25.750 119.699 1.00 63.39 O ANISOU 1667 OG1 THR A 258 11153 7723 5207 867 -1376 -3819 O ATOM 1668 CG2 THR A 258 80.615 26.919 121.441 1.00 69.41 C ANISOU 1668 CG2 THR A 258 12526 8558 5288 941 -1058 -4447 C ATOM 1669 N ILE A 259 81.790 22.625 120.031 1.00 59.24 N ANISOU 1669 N ILE A 259 10454 7699 4355 1006 -1353 -3014 N ATOM 1670 CA ILE A 259 81.861 21.407 119.202 1.00 55.94 C ANISOU 1670 CA ILE A 259 9786 7230 4236 1103 -1322 -2609 C ATOM 1671 C ILE A 259 81.318 20.200 119.974 1.00 56.77 C ANISOU 1671 C ILE A 259 9915 7568 4085 1201 -1176 -2367 C ATOM 1672 O ILE A 259 80.641 19.355 119.385 1.00 54.12 O ANISOU 1672 O ILE A 259 9380 7188 3994 1329 -908 -2204 O ATOM 1673 CB ILE A 259 83.295 21.110 118.688 1.00 55.07 C ANISOU 1673 CB ILE A 259 9482 7062 4377 1008 -1642 -2407 C ATOM 1674 CG1 ILE A 259 83.840 22.271 117.843 1.00 54.08 C ANISOU 1674 CG1 ILE A 259 9333 6693 4520 960 -1745 -2614 C ATOM 1675 CG2 ILE A 259 83.343 19.824 117.867 1.00 52.33 C ANISOU 1675 CG2 ILE A 259 8936 6647 4300 1095 -1548 -2038 C ATOM 1676 CD1 ILE A 259 83.075 22.573 116.567 1.00 50.96 C ANISOU 1676 CD1 ILE A 259 8836 6031 4491 1075 -1519 -2668 C ATOM 1677 N LYS A 260 81.603 20.128 121.278 1.00 60.58 N ANISOU 1677 N LYS A 260 10536 8362 4119 1109 -1352 -2346 N ATOM 1678 CA LYS A 260 81.014 19.090 122.152 1.00 62.45 C ANISOU 1678 CA LYS A 260 10828 8873 4025 1129 -1203 -2098 C ATOM 1679 C LYS A 260 79.494 19.233 122.266 1.00 61.98 C ANISOU 1679 C LYS A 260 10917 8865 3766 1242 -796 -2295 C ATOM 1680 O LYS A 260 78.784 18.238 122.410 1.00 61.56 O ANISOU 1680 O LYS A 260 10918 8912 3560 1285 -581 -2129 O ATOM 1681 CB LYS A 260 81.622 19.110 123.571 1.00 67.27 C ANISOU 1681 CB LYS A 260 11618 9856 4082 982 -1425 -2054 C ATOM 1682 CG LYS A 260 83.140 18.952 123.667 1.00 68.74 C ANISOU 1682 CG LYS A 260 11650 10136 4329 816 -1847 -1827 C ATOM 1683 CD LYS A 260 83.672 17.766 122.848 1.00 66.31 C ANISOU 1683 CD LYS A 260 11058 9647 4491 920 -1901 -1378 C ATOM 1684 CE LYS A 260 85.138 17.457 123.143 1.00 68.51 C ANISOU 1684 CE LYS A 260 11156 10092 4783 792 -2309 -1097 C ATOM 1685 NZ LYS A 260 85.324 16.311 124.083 1.00 71.51 N ANISOU 1685 NZ LYS A 260 11487 10779 4904 795 -2420 -631 N ATOM 1686 N GLU A 261 79.005 20.473 122.226 1.00 62.58 N ANISOU 1686 N GLU A 261 11109 8833 3836 1267 -681 -2633 N ATOM 1687 CA GLU A 261 77.568 20.738 122.222 1.00 62.94 C ANISOU 1687 CA GLU A 261 11160 8806 3946 1413 -299 -2788 C ATOM 1688 C GLU A 261 76.948 20.165 120.956 1.00 58.83 C ANISOU 1688 C GLU A 261 10387 8041 3922 1520 -155 -2591 C ATOM 1689 O GLU A 261 75.940 19.464 121.019 1.00 58.60 O ANISOU 1689 O GLU A 261 10295 8100 3868 1604 142 -2482 O ATOM 1690 CB GLU A 261 77.278 22.243 122.318 1.00 64.77 C ANISOU 1690 CB GLU A 261 11567 8859 4181 1432 -210 -3240 C ATOM 1691 CG GLU A 261 75.835 22.567 122.704 1.00 66.66 C ANISOU 1691 CG GLU A 261 11871 9117 4340 1616 202 -3416 C ATOM 1692 CD GLU A 261 75.497 24.053 122.726 1.00 69.00 C ANISOU 1692 CD GLU A 261 12256 9137 4821 1681 313 -3961 C ATOM 1693 OE1 GLU A 261 76.425 24.874 122.865 1.00 70.32 O ANISOU 1693 OE1 GLU A 261 12604 9062 5050 1584 85 -4217 O ATOM 1694 OE2 GLU A 261 74.290 24.390 122.624 1.00 69.45 O ANISOU 1694 OE2 GLU A 261 12329 8906 5150 1919 648 -4171 O ATOM 1695 N LEU A 262 77.565 20.469 119.815 1.00 55.81 N ANISOU 1695 N LEU A 262 9894 7360 3950 1506 -323 -2579 N ATOM 1696 CA LEU A 262 77.131 19.951 118.522 1.00 52.42 C ANISOU 1696 CA LEU A 262 9248 6788 3879 1566 -242 -2373 C ATOM 1697 C LEU A 262 77.145 18.426 118.484 1.00 51.55 C ANISOU 1697 C LEU A 262 9044 6776 3764 1507 -224 -1991 C ATOM 1698 O LEU A 262 76.185 17.804 118.017 1.00 49.73 O ANISOU 1698 O LEU A 262 8776 6550 3567 1569 -52 -1754 O ATOM 1699 CB LEU A 262 78.027 20.492 117.401 1.00 50.13 C ANISOU 1699 CB LEU A 262 8832 6251 3965 1501 -422 -2456 C ATOM 1700 CG LEU A 262 77.745 19.993 115.974 1.00 46.73 C ANISOU 1700 CG LEU A 262 8192 5640 3922 1491 -346 -2305 C ATOM 1701 CD1 LEU A 262 76.339 20.364 115.519 1.00 46.19 C ANISOU 1701 CD1 LEU A 262 8073 5536 3941 1581 -105 -2375 C ATOM 1702 CD2 LEU A 262 78.774 20.576 115.029 1.00 45.15 C ANISOU 1702 CD2 LEU A 262 7899 5271 3982 1419 -565 -2357 C ATOM 1703 N GLU A 263 78.237 17.841 118.978 1.00 52.90 N ANISOU 1703 N GLU A 263 9190 7066 3842 1458 -467 -1846 N ATOM 1704 CA GLU A 263 78.383 16.389 119.081 1.00 53.09 C ANISOU 1704 CA GLU A 263 9138 7109 3924 1448 -441 -1475 C ATOM 1705 C GLU A 263 77.235 15.792 119.882 1.00 54.64 C ANISOU 1705 C GLU A 263 9401 7501 3855 1497 -249 -1312 C ATOM 1706 O GLU A 263 76.645 14.795 119.472 1.00 52.85 O ANISOU 1706 O GLU A 263 9112 7250 3718 1592 -147 -1056 O ATOM 1707 CB GLU A 263 79.731 16.029 119.723 1.00 55.42 C ANISOU 1707 CB GLU A 263 9396 7548 4111 1373 -759 -1294 C ATOM 1708 CG GLU A 263 79.969 14.537 119.922 1.00 56.53 C ANISOU 1708 CG GLU A 263 9485 7648 4346 1351 -753 -861 C ATOM 1709 CD GLU A 263 81.410 14.178 120.270 1.00 59.24 C ANISOU 1709 CD GLU A 263 9617 7996 4896 1335 -1058 -628 C ATOM 1710 OE1 GLU A 263 82.198 15.057 120.695 1.00 61.56 O ANISOU 1710 OE1 GLU A 263 10126 8195 5067 1182 -1178 -798 O ATOM 1711 OE2 GLU A 263 81.761 12.986 120.128 1.00 61.27 O ANISOU 1711 OE2 GLU A 263 9745 7961 5572 1435 -954 -234 O ATOM 1712 N SER A 264 76.917 16.426 121.010 1.00 57.92 N ANISOU 1712 N SER A 264 9993 8171 3842 1478 -180 -1507 N ATOM 1713 CA SER A 264 75.819 15.999 121.886 1.00 60.53 C ANISOU 1713 CA SER A 264 10349 8751 3896 1512 100 -1430 C ATOM 1714 C SER A 264 74.447 16.094 121.204 1.00 58.87 C ANISOU 1714 C SER A 264 10078 8439 3848 1572 384 -1491 C ATOM 1715 O SER A 264 73.651 15.157 121.283 1.00 59.44 O ANISOU 1715 O SER A 264 10062 8543 3976 1558 515 -1172 O ATOM 1716 CB SER A 264 75.831 16.816 123.198 1.00 64.75 C ANISOU 1716 CB SER A 264 11137 9578 3885 1481 86 -1671 C ATOM 1717 OG SER A 264 74.593 16.733 123.889 1.00 67.46 O ANISOU 1717 OG SER A 264 11561 10211 3857 1502 466 -1711 O ATOM 1718 N ILE A 265 74.176 17.225 120.550 1.00 57.71 N ANISOU 1718 N ILE A 265 9926 8121 3880 1634 450 -1783 N ATOM 1719 CA ILE A 265 72.925 17.420 119.786 1.00 56.56 C ANISOU 1719 CA ILE A 265 9596 7866 4026 1729 699 -1798 C ATOM 1720 C ILE A 265 72.767 16.314 118.739 1.00 53.78 C ANISOU 1720 C ILE A 265 9033 7356 4045 1656 676 -1519 C ATOM 1721 O ILE A 265 71.686 15.758 118.578 1.00 54.89 O ANISOU 1721 O ILE A 265 9020 7611 4222 1573 694 -1331 O ATOM 1722 CB ILE A 265 72.887 18.791 119.057 1.00 55.45 C ANISOU 1722 CB ILE A 265 9439 7481 4147 1830 703 -2129 C ATOM 1723 CG1 ILE A 265 72.745 19.942 120.051 1.00 58.72 C ANISOU 1723 CG1 ILE A 265 10055 8008 4248 1894 807 -2462 C ATOM 1724 CG2 ILE A 265 71.729 18.861 118.058 1.00 54.02 C ANISOU 1724 CG2 ILE A 265 9005 7179 4338 1933 893 -2046 C ATOM 1725 CD1 ILE A 265 73.188 21.277 119.488 1.00 58.05 C ANISOU 1725 CD1 ILE A 265 10013 7632 4410 1978 718 -2780 C ATOM 1726 N ILE A 266 73.865 16.009 118.054 1.00 51.74 N ANISOU 1726 N ILE A 266 8728 6963 3968 1601 430 -1477 N ATOM 1727 CA ILE A 266 73.908 15.012 116.978 1.00 49.37 C ANISOU 1727 CA ILE A 266 8290 6467 4002 1524 442 -1259 C ATOM 1728 C ILE A 266 73.760 13.587 117.489 1.00 50.51 C ANISOU 1728 C ILE A 266 8402 6672 4116 1461 515 -962 C ATOM 1729 O ILE A 266 73.047 12.791 116.869 1.00 50.77 O ANISOU 1729 O ILE A 266 8180 6754 4356 1364 689 -952 O ATOM 1730 CB ILE A 266 75.211 15.188 116.131 1.00 47.29 C ANISOU 1730 CB ILE A 266 8010 6004 3954 1508 217 -1326 C ATOM 1731 CG1 ILE A 266 75.054 16.361 115.156 1.00 45.59 C ANISOU 1731 CG1 ILE A 266 7739 5666 3917 1514 223 -1563 C ATOM 1732 CG2 ILE A 266 75.627 13.926 115.382 1.00 45.88 C ANISOU 1732 CG2 ILE A 266 7759 5665 4007 1362 190 -1120 C ATOM 1733 CD1 ILE A 266 73.837 16.297 114.241 1.00 44.63 C ANISOU 1733 CD1 ILE A 266 7477 5529 3948 1441 389 -1526 C ATOM 1734 N SER A 267 74.454 13.258 118.581 1.00 52.52 N ANISOU 1734 N SER A 267 8805 7073 4075 1446 438 -840 N ATOM 1735 CA SER A 267 74.347 11.939 119.207 1.00 54.28 C ANISOU 1735 CA SER A 267 9015 7385 4221 1431 493 -467 C ATOM 1736 C SER A 267 72.919 11.606 119.538 1.00 55.43 C ANISOU 1736 C SER A 267 9138 7678 4243 1406 748 -365 C ATOM 1737 O SER A 267 72.466 10.503 119.265 1.00 55.48 O ANISOU 1737 O SER A 267 9082 7597 4398 1418 897 -283 O ATOM 1738 CB SER A 267 75.144 11.879 120.504 1.00 57.43 C ANISOU 1738 CB SER A 267 9517 8005 4297 1436 310 -335 C ATOM 1739 OG SER A 267 76.517 12.043 120.255 1.00 57.53 O ANISOU 1739 OG SER A 267 9459 7839 4559 1422 164 -408 O ATOM 1740 N LYS A 268 72.210 12.572 120.117 1.00 57.19 N ANISOU 1740 N LYS A 268 9402 8069 4259 1493 885 -601 N ATOM 1741 CA LYS A 268 70.825 12.358 120.575 1.00 59.31 C ANISOU 1741 CA LYS A 268 9583 8544 4405 1468 1172 -484 C ATOM 1742 C LYS A 268 69.850 12.058 119.440 1.00 56.94 C ANISOU 1742 C LYS A 268 9136 8072 4424 1440 1371 -506 C ATOM 1743 O LYS A 268 68.829 11.415 119.650 1.00 57.64 O ANISOU 1743 O LYS A 268 9275 8174 4449 1365 1520 -440 O ATOM 1744 CB LYS A 268 70.332 13.550 121.415 1.00 61.68 C ANISOU 1744 CB LYS A 268 10018 9079 4336 1548 1315 -777 C ATOM 1745 CG LYS A 268 70.948 13.540 122.800 1.00 65.12 C ANISOU 1745 CG LYS A 268 10670 9820 4251 1555 1264 -706 C ATOM 1746 CD LYS A 268 70.770 14.852 123.547 1.00 67.66 C ANISOU 1746 CD LYS A 268 11151 10290 4266 1653 1360 -1089 C ATOM 1747 CE LYS A 268 71.564 14.824 124.852 1.00 71.29 C ANISOU 1747 CE LYS A 268 11820 11035 4229 1572 1182 -1077 C ATOM 1748 NZ LYS A 268 71.027 15.767 125.875 1.00 75.25 N ANISOU 1748 NZ LYS A 268 12507 11784 4300 1645 1396 -1391 N ATOM 1749 N ARG A 269 70.188 12.493 118.238 1.00 54.19 N ANISOU 1749 N ARG A 269 8746 7445 4397 1432 1192 -561 N ATOM 1750 CA ARG A 269 69.427 12.127 117.053 1.00 53.18 C ANISOU 1750 CA ARG A 269 8376 7216 4610 1270 1226 -535 C ATOM 1751 C ARG A 269 69.856 10.784 116.447 1.00 52.27 C ANISOU 1751 C ARG A 269 8239 6934 4685 1131 1194 -337 C ATOM 1752 O ARG A 269 69.336 10.409 115.414 1.00 51.58 O ANISOU 1752 O ARG A 269 7981 6793 4823 898 1288 -422 O ATOM 1753 CB ARG A 269 69.548 13.218 115.987 1.00 51.22 C ANISOU 1753 CB ARG A 269 8085 6853 4520 1334 1143 -764 C ATOM 1754 CG ARG A 269 69.326 14.636 116.496 1.00 52.60 C ANISOU 1754 CG ARG A 269 8328 7104 4551 1514 1226 -1044 C ATOM 1755 CD ARG A 269 69.061 15.612 115.353 1.00 50.82 C ANISOU 1755 CD ARG A 269 7934 6751 4621 1615 1149 -1212 C ATOM 1756 NE ARG A 269 68.025 15.227 114.412 1.00 49.92 N ANISOU 1756 NE ARG A 269 7624 6553 4789 1597 1232 -1148 N ATOM 1757 CZ ARG A 269 66.728 15.441 114.546 1.00 51.88 C ANISOU 1757 CZ ARG A 269 7635 7049 5026 1543 1463 -977 C ATOM 1758 NH1 ARG A 269 66.225 16.091 115.596 1.00 54.65 N ANISOU 1758 NH1 ARG A 269 8027 7731 5003 1636 1713 -975 N ATOM 1759 NH2 ARG A 269 65.931 15.016 113.582 1.00 51.33 N ANISOU 1759 NH2 ARG A 269 7376 6915 5208 1398 1481 -861 N ATOM 1760 N ASN A 270 70.778 10.066 117.088 1.00 53.21 N ANISOU 1760 N ASN A 270 8457 7067 4693 1168 1129 -171 N ATOM 1761 CA ASN A 270 71.266 8.774 116.615 1.00 53.57 C ANISOU 1761 CA ASN A 270 8517 6799 5037 1049 1067 -2 C ATOM 1762 C ASN A 270 72.062 8.871 115.295 1.00 50.53 C ANISOU 1762 C ASN A 270 8128 6102 4967 967 910 -188 C ATOM 1763 O ASN A 270 71.976 8.006 114.414 1.00 50.18 O ANISOU 1763 O ASN A 270 8001 5957 5108 935 1045 -212 O ATOM 1764 CB ASN A 270 70.118 7.762 116.527 1.00 55.99 C ANISOU 1764 CB ASN A 270 8633 7104 5534 824 1235 174 C ATOM 1765 CG ASN A 270 70.602 6.325 116.509 1.00 59.27 C ANISOU 1765 CG ASN A 270 9034 7076 6410 791 1229 332 C ATOM 1766 OD1 ASN A 270 71.784 6.039 116.716 1.00 61.98 O ANISOU 1766 OD1 ASN A 270 9034 7595 6921 811 1084 113 O ATOM 1767 ND2 ASN A 270 69.682 5.404 116.253 1.00 61.75 N ANISOU 1767 ND2 ASN A 270 9162 7319 6981 526 1377 419 N ATOM 1768 N ILE A 271 72.861 9.931 115.208 1.00 48.39 N ANISOU 1768 N ILE A 271 7898 5917 4570 1136 770 -342 N ATOM 1769 CA ILE A 271 73.738 10.201 114.085 1.00 45.67 C ANISOU 1769 CA ILE A 271 7525 5317 4508 1091 613 -523 C ATOM 1770 C ILE A 271 75.151 10.262 114.664 1.00 45.55 C ANISOU 1770 C ILE A 271 7636 5252 4419 1130 485 -489 C ATOM 1771 O ILE A 271 75.346 10.827 115.733 1.00 46.72 O ANISOU 1771 O ILE A 271 7851 5650 4247 1033 396 -396 O ATOM 1772 CB ILE A 271 73.343 11.539 113.414 1.00 43.80 C ANISOU 1772 CB ILE A 271 7246 5110 4283 1101 613 -807 C ATOM 1773 CG1 ILE A 271 71.961 11.410 112.767 1.00 43.70 C ANISOU 1773 CG1 ILE A 271 7104 5138 4361 997 765 -794 C ATOM 1774 CG2 ILE A 271 74.367 11.973 112.367 1.00 41.57 C ANISOU 1774 CG2 ILE A 271 6958 4669 4166 1131 464 -967 C ATOM 1775 CD1 ILE A 271 71.315 12.732 112.410 1.00 43.15 C ANISOU 1775 CD1 ILE A 271 6929 5219 4246 1085 801 -927 C ATOM 1776 N GLN A 272 76.112 9.659 113.968 1.00 44.64 N ANISOU 1776 N GLN A 272 7478 4854 4627 1135 387 -457 N ATOM 1777 CA GLN A 272 77.525 9.712 114.350 1.00 45.60 C ANISOU 1777 CA GLN A 272 7577 5032 4717 1249 181 -393 C ATOM 1778 C GLN A 272 78.098 11.123 114.117 1.00 44.00 C ANISOU 1778 C GLN A 272 7359 4896 4461 1362 66 -647 C ATOM 1779 O GLN A 272 77.543 11.906 113.336 1.00 41.85 O ANISOU 1779 O GLN A 272 6998 4639 4263 1357 161 -877 O ATOM 1780 CB GLN A 272 78.360 8.698 113.539 1.00 45.77 C ANISOU 1780 CB GLN A 272 7527 4748 5113 1293 225 -279 C ATOM 1781 CG GLN A 272 78.004 7.235 113.725 1.00 48.09 C ANISOU 1781 CG GLN A 272 7823 4845 5603 1222 392 -7 C ATOM 1782 CD GLN A 272 78.824 6.307 112.820 1.00 49.23 C ANISOU 1782 CD GLN A 272 7889 4719 6095 1280 541 17 C ATOM 1783 OE1 GLN A 272 79.557 5.429 113.311 1.00 52.81 O ANISOU 1783 OE1 GLN A 272 8091 4984 6990 1336 509 465 O ATOM 1784 NE2 GLN A 272 78.709 6.490 111.493 1.00 47.53 N ANISOU 1784 NE2 GLN A 272 7690 4344 6022 1234 634 -149 N ATOM 1785 N PHE A 273 79.229 11.423 114.764 1.00 44.86 N ANISOU 1785 N PHE A 273 7519 5070 4456 1414 -128 -605 N ATOM 1786 CA PHE A 273 79.896 12.717 114.610 1.00 44.00 C ANISOU 1786 CA PHE A 273 7387 5037 4292 1411 -339 -837 C ATOM 1787 C PHE A 273 81.399 12.571 114.418 1.00 44.39 C ANISOU 1787 C PHE A 273 7336 4985 4543 1448 -612 -754 C ATOM 1788 O PHE A 273 82.039 11.850 115.160 1.00 45.15 O ANISOU 1788 O PHE A 273 7565 4966 4622 1523 -783 -689 O ATOM 1789 CB PHE A 273 79.633 13.581 115.821 1.00 45.55 C ANISOU 1789 CB PHE A 273 7696 5478 4133 1434 -443 -925 C ATOM 1790 CG PHE A 273 80.232 14.944 115.721 1.00 45.34 C ANISOU 1790 CG PHE A 273 7672 5517 4038 1370 -596 -1133 C ATOM 1791 CD1 PHE A 273 79.701 15.892 114.846 1.00 43.52 C ANISOU 1791 CD1 PHE A 273 7445 5142 3949 1402 -521 -1390 C ATOM 1792 CD2 PHE A 273 81.322 15.298 116.506 1.00 47.42 C ANISOU 1792 CD2 PHE A 273 7934 5918 4165 1345 -850 -1109 C ATOM 1793 CE1 PHE A 273 80.254 17.162 114.757 1.00 43.25 C ANISOU 1793 CE1 PHE A 273 7449 5091 3890 1396 -696 -1647 C ATOM 1794 CE2 PHE A 273 81.872 16.570 116.426 1.00 47.22 C ANISOU 1794 CE2 PHE A 273 8011 5833 4097 1362 -1010 -1409 C ATOM 1795 CZ PHE A 273 81.343 17.498 115.545 1.00 45.11 C ANISOU 1795 CZ PHE A 273 7707 5409 4022 1371 -912 -1682 C ATOM 1796 N SER A 274 81.933 13.252 113.402 1.00 43.22 N ANISOU 1796 N SER A 274 7119 4700 4601 1365 -597 -902 N ATOM 1797 CA SER A 274 83.373 13.404 113.190 1.00 43.91 C ANISOU 1797 CA SER A 274 7060 4791 4832 1440 -769 -849 C ATOM 1798 C SER A 274 83.682 14.886 113.151 1.00 43.84 C ANISOU 1798 C SER A 274 7108 4828 4720 1383 -940 -1057 C ATOM 1799 O SER A 274 82.842 15.683 112.727 1.00 42.23 O ANISOU 1799 O SER A 274 7016 4756 4273 1409 -898 -1298 O ATOM 1800 CB SER A 274 83.817 12.799 111.863 1.00 42.51 C ANISOU 1800 CB SER A 274 6789 4339 5022 1466 -586 -788 C ATOM 1801 OG SER A 274 83.366 11.472 111.714 1.00 43.08 O ANISOU 1801 OG SER A 274 6909 4322 5137 1428 -368 -610 O ATOM 1802 N CYS A 275 84.897 15.239 113.562 1.00 45.65 N ANISOU 1802 N CYS A 275 7243 5189 4912 1342 -1203 -1015 N ATOM 1803 CA CYS A 275 85.372 16.605 113.497 1.00 46.10 C ANISOU 1803 CA CYS A 275 7310 5195 5009 1252 -1348 -1248 C ATOM 1804 C CYS A 275 86.810 16.621 113.008 1.00 45.49 C ANISOU 1804 C CYS A 275 7135 5010 5138 1285 -1582 -1174 C ATOM 1805 O CYS A 275 87.590 15.760 113.359 1.00 47.22 O ANISOU 1805 O CYS A 275 7161 5254 5523 1336 -1734 -910 O ATOM 1806 CB CYS A 275 85.285 17.248 114.874 1.00 50.06 C ANISOU 1806 CB CYS A 275 7974 6042 5002 1198 -1503 -1402 C ATOM 1807 SG CYS A 275 85.830 18.975 114.902 1.00 52.48 S ANISOU 1807 SG CYS A 275 8463 6174 5301 1011 -1631 -1751 S ATOM 1808 N LYS A 276 87.156 17.618 112.205 1.00 44.02 N ANISOU 1808 N LYS A 276 6830 4811 5083 1145 -1564 -1404 N ATOM 1809 CA LYS A 276 88.506 17.751 111.671 1.00 44.73 C ANISOU 1809 CA LYS A 276 6666 4876 5451 1126 -1701 -1279 C ATOM 1810 C LYS A 276 88.977 19.208 111.724 1.00 45.10 C ANISOU 1810 C LYS A 276 6702 4958 5473 1028 -1857 -1439 C ATOM 1811 O LYS A 276 88.255 20.114 111.305 1.00 43.57 O ANISOU 1811 O LYS A 276 6800 4715 5040 1004 -1736 -1633 O ATOM 1812 CB LYS A 276 88.529 17.258 110.231 1.00 42.69 C ANISOU 1812 CB LYS A 276 6292 4429 5498 1159 -1430 -1254 C ATOM 1813 CG LYS A 276 89.883 17.319 109.549 1.00 43.43 C ANISOU 1813 CG LYS A 276 6138 4474 5887 1152 -1510 -1119 C ATOM 1814 CD LYS A 276 90.834 16.283 110.101 1.00 45.66 C ANISOU 1814 CD LYS A 276 6225 4789 6334 1244 -1595 -878 C ATOM 1815 CE LYS A 276 92.164 16.353 109.376 1.00 46.81 C ANISOU 1815 CE LYS A 276 6127 4884 6772 1302 -1562 -756 C ATOM 1816 NZ LYS A 276 93.047 15.268 109.869 1.00 49.56 N ANISOU 1816 NZ LYS A 276 6236 5282 7312 1456 -1601 -401 N ATOM 1817 N ASN A 277 90.195 19.408 112.224 1.00 47.01 N ANISOU 1817 N ASN A 277 6855 5221 5784 972 -2140 -1344 N ATOM 1818 CA ASN A 277 90.879 20.684 112.143 1.00 47.74 C ANISOU 1818 CA ASN A 277 6895 5365 5877 800 -2346 -1466 C ATOM 1819 C ASN A 277 91.415 20.916 110.743 1.00 45.71 C ANISOU 1819 C ASN A 277 6418 4953 5996 796 -2321 -1453 C ATOM 1820 O ASN A 277 92.196 20.120 110.248 1.00 44.81 O ANISOU 1820 O ASN A 277 6208 4830 5986 756 -2353 -1450 O ATOM 1821 CB ASN A 277 92.047 20.724 113.134 1.00 51.44 C ANISOU 1821 CB ASN A 277 7256 6032 6257 677 -2705 -1313 C ATOM 1822 CG ASN A 277 91.582 20.789 114.564 1.00 53.87 C ANISOU 1822 CG ASN A 277 7833 6527 6105 640 -2843 -1326 C ATOM 1823 OD1 ASN A 277 91.270 21.866 115.064 1.00 55.46 O ANISOU 1823 OD1 ASN A 277 8368 6776 5926 472 -2915 -1709 O ATOM 1824 ND2 ASN A 277 91.510 19.646 115.224 1.00 55.10 N ANISOU 1824 ND2 ASN A 277 7996 6776 6164 778 -2825 -1079 N ATOM 1825 N ILE A 278 90.993 22.003 110.107 1.00 44.53 N ANISOU 1825 N ILE A 278 6393 4685 5840 663 -2232 -1591 N ATOM 1826 CA ILE A 278 91.616 22.461 108.861 1.00 43.54 C ANISOU 1826 CA ILE A 278 6039 4466 6039 575 -2185 -1596 C ATOM 1827 C ILE A 278 92.512 23.662 109.231 1.00 45.18 C ANISOU 1827 C ILE A 278 6216 4712 6235 440 -2493 -1663 C ATOM 1828 O ILE A 278 92.050 24.796 109.356 1.00 44.87 O ANISOU 1828 O ILE A 278 6443 4588 6016 268 -2589 -1925 O ATOM 1829 CB ILE A 278 90.581 22.864 107.780 1.00 41.22 C ANISOU 1829 CB ILE A 278 5847 4058 5757 610 -1950 -1729 C ATOM 1830 CG1 ILE A 278 89.525 21.756 107.546 1.00 39.37 C ANISOU 1830 CG1 ILE A 278 5743 3743 5473 762 -1664 -1689 C ATOM 1831 CG2 ILE A 278 91.286 23.232 106.480 1.00 40.88 C ANISOU 1831 CG2 ILE A 278 5617 3945 5967 514 -1886 -1662 C ATOM 1832 CD1 ILE A 278 90.050 20.456 106.966 1.00 39.26 C ANISOU 1832 CD1 ILE A 278 5542 3770 5604 840 -1496 -1550 C ATOM 1833 N TYR A 279 93.793 23.378 109.423 1.00 46.82 N ANISOU 1833 N TYR A 279 6197 4996 6595 348 -2642 -1493 N ATOM 1834 CA TYR A 279 94.781 24.383 109.836 1.00 49.22 C ANISOU 1834 CA TYR A 279 6414 5314 6972 152 -2951 -1439 C ATOM 1835 C TYR A 279 95.153 25.339 108.717 1.00 48.42 C ANISOU 1835 C TYR A 279 6176 5080 7140 43 -2917 -1499 C ATOM 1836 O TYR A 279 95.430 26.510 108.977 1.00 49.87 O ANISOU 1836 O TYR A 279 6346 5292 7307 -229 -3187 -1642 O ATOM 1837 CB TYR A 279 96.046 23.699 110.348 1.00 51.92 C ANISOU 1837 CB TYR A 279 6446 5893 7388 108 -3206 -1159 C ATOM 1838 CG TYR A 279 95.814 22.887 111.595 1.00 53.48 C ANISOU 1838 CG TYR A 279 6752 6261 7307 181 -3276 -1065 C ATOM 1839 CD1 TYR A 279 95.554 23.517 112.815 1.00 55.77 C ANISOU 1839 CD1 TYR A 279 7297 6651 7238 0 -3529 -1263 C ATOM 1840 CD2 TYR A 279 95.850 21.487 111.572 1.00 53.19 C ANISOU 1840 CD2 TYR A 279 6625 6253 7332 456 -3102 -812 C ATOM 1841 CE1 TYR A 279 95.347 22.782 113.976 1.00 57.47 C ANISOU 1841 CE1 TYR A 279 7629 7065 7140 67 -3634 -1157 C ATOM 1842 CE2 TYR A 279 95.635 20.752 112.731 1.00 54.95 C ANISOU 1842 CE2 TYR A 279 6964 6623 7291 529 -3190 -680 C ATOM 1843 CZ TYR A 279 95.388 21.408 113.926 1.00 56.91 C ANISOU 1843 CZ TYR A 279 7416 7053 7152 362 -3470 -821 C ATOM 1844 OH TYR A 279 95.171 20.702 115.074 1.00 59.08 O ANISOU 1844 OH TYR A 279 7757 7592 7096 423 -3587 -645 O ATOM 1845 N ARG A 280 95.171 24.825 107.489 1.00 45.96 N ANISOU 1845 N ARG A 280 5696 4694 7072 147 -2672 -1337 N ATOM 1846 CA ARG A 280 95.658 25.542 106.327 1.00 45.82 C ANISOU 1846 CA ARG A 280 5546 4585 7278 15 -2619 -1308 C ATOM 1847 C ARG A 280 94.649 25.441 105.191 1.00 42.60 C ANISOU 1847 C ARG A 280 5250 4051 6882 86 -2269 -1371 C ATOM 1848 O ARG A 280 94.783 24.591 104.320 1.00 41.00 O ANISOU 1848 O ARG A 280 4854 3914 6807 179 -2034 -1215 O ATOM 1849 CB ARG A 280 97.009 24.978 105.908 1.00 47.59 C ANISOU 1849 CB ARG A 280 5389 4957 7736 7 -2589 -1034 C ATOM 1850 CG ARG A 280 98.146 25.430 106.798 1.00 51.14 C ANISOU 1850 CG ARG A 280 5661 5530 8240 -180 -2965 -930 C ATOM 1851 CD ARG A 280 98.648 26.813 106.398 1.00 52.71 C ANISOU 1851 CD ARG A 280 5813 5617 8594 -436 -3127 -961 C ATOM 1852 NE ARG A 280 99.181 26.833 105.028 1.00 52.27 N ANISOU 1852 NE ARG A 280 5500 5534 8826 -436 -2898 -801 N ATOM 1853 CZ ARG A 280 100.464 26.945 104.674 1.00 54.77 C ANISOU 1853 CZ ARG A 280 5430 5989 9391 -529 -2980 -568 C ATOM 1854 NH1 ARG A 280 101.448 27.085 105.565 1.00 58.27 N ANISOU 1854 NH1 ARG A 280 5649 6621 9867 -664 -3324 -448 N ATOM 1855 NH2 ARG A 280 100.763 26.939 103.380 1.00 54.17 N ANISOU 1855 NH2 ARG A 280 5186 5868 9527 -491 -2706 -454 N ATOM 1856 N PRO A 281 93.625 26.312 105.207 1.00 41.69 N ANISOU 1856 N PRO A 281 5361 3849 6629 62 -2289 -1555 N ATOM 1857 CA PRO A 281 92.578 26.302 104.180 1.00 39.45 C ANISOU 1857 CA PRO A 281 5169 3478 6340 113 -2047 -1613 C ATOM 1858 C PRO A 281 93.130 26.290 102.737 1.00 39.20 C ANISOU 1858 C PRO A 281 4928 3455 6510 54 -1866 -1437 C ATOM 1859 O PRO A 281 92.555 25.632 101.853 1.00 37.79 O ANISOU 1859 O PRO A 281 4847 3282 6227 97 -1562 -1447 O ATOM 1860 CB PRO A 281 91.782 27.595 104.445 1.00 39.75 C ANISOU 1860 CB PRO A 281 5410 3349 6340 45 -2138 -1770 C ATOM 1861 CG PRO A 281 92.215 28.104 105.765 1.00 41.98 C ANISOU 1861 CG PRO A 281 5782 3599 6568 -50 -2406 -1905 C ATOM 1862 CD PRO A 281 93.415 27.350 106.232 1.00 43.33 C ANISOU 1862 CD PRO A 281 5767 3940 6753 -69 -2555 -1757 C ATOM 1863 N ASP A 282 94.214 27.034 102.517 1.00 41.24 N ANISOU 1863 N ASP A 282 4970 3718 6978 -98 -2038 -1328 N ATOM 1864 CA ASP A 282 94.912 27.068 101.220 1.00 41.95 C ANISOU 1864 CA ASP A 282 4837 3894 7205 -191 -1878 -1160 C ATOM 1865 C ASP A 282 95.414 25.678 100.755 1.00 41.97 C ANISOU 1865 C ASP A 282 4691 4017 7238 -38 -1626 -1050 C ATOM 1866 O ASP A 282 95.154 25.288 99.621 1.00 41.72 O ANISOU 1866 O ASP A 282 4653 4075 7123 -69 -1338 -1060 O ATOM 1867 CB ASP A 282 96.057 28.109 101.217 1.00 44.60 C ANISOU 1867 CB ASP A 282 4987 4188 7772 -405 -2089 -1042 C ATOM 1868 CG ASP A 282 97.128 27.831 102.281 1.00 47.05 C ANISOU 1868 CG ASP A 282 5081 4686 8110 -485 -2337 -1010 C ATOM 1869 OD1 ASP A 282 96.778 27.700 103.482 1.00 47.28 O ANISOU 1869 OD1 ASP A 282 5177 4839 7945 -618 -2596 -1065 O ATOM 1870 OD2 ASP A 282 98.322 27.763 101.920 1.00 49.22 O ANISOU 1870 OD2 ASP A 282 5018 5156 8526 -518 -2369 -846 O ATOM 1871 N LYS A 283 96.077 24.924 101.628 1.00 43.10 N ANISOU 1871 N LYS A 283 4704 4250 7422 54 -1737 -997 N ATOM 1872 CA LYS A 283 96.580 23.576 101.290 1.00 43.58 C ANISOU 1872 CA LYS A 283 4618 4376 7563 199 -1454 -913 C ATOM 1873 C LYS A 283 95.417 22.609 101.128 1.00 41.06 C ANISOU 1873 C LYS A 283 4536 4025 7038 367 -1239 -1037 C ATOM 1874 O LYS A 283 95.413 21.798 100.217 1.00 40.17 O ANISOU 1874 O LYS A 283 4363 3780 7116 395 -888 -973 O ATOM 1875 CB LYS A 283 97.523 23.035 102.399 1.00 45.93 C ANISOU 1875 CB LYS A 283 4729 4749 7973 316 -1640 -739 C ATOM 1876 CG LYS A 283 98.864 23.791 102.554 1.00 49.18 C ANISOU 1876 CG LYS A 283 4843 5236 8607 126 -1890 -583 C ATOM 1877 CD LYS A 283 100.032 23.052 101.909 1.00 51.62 C ANISOU 1877 CD LYS A 283 4772 5664 9177 228 -1631 -351 C ATOM 1878 CE LYS A 283 101.341 23.838 102.059 1.00 55.09 C ANISOU 1878 CE LYS A 283 4886 6196 9849 10 -1869 -152 C ATOM 1879 NZ LYS A 283 101.760 24.605 100.842 1.00 55.72 N ANISOU 1879 NZ LYS A 283 4854 6240 10074 -133 -1699 -99 N ATOM 1880 N PHE A 284 94.423 22.734 101.999 1.00 39.84 N ANISOU 1880 N PHE A 284 4623 3833 6682 391 -1369 -1167 N ATOM 1881 CA PHE A 284 93.211 21.926 101.918 1.00 38.19 C ANISOU 1881 CA PHE A 284 4642 3540 6328 477 -1141 -1306 C ATOM 1882 C PHE A 284 92.540 22.031 100.534 1.00 36.93 C ANISOU 1882 C PHE A 284 4517 3402 6111 387 -896 -1341 C ATOM 1883 O PHE A 284 92.299 21.014 99.902 1.00 37.11 O ANISOU 1883 O PHE A 284 4584 3408 6105 358 -593 -1404 O ATOM 1884 CB PHE A 284 92.238 22.293 103.055 1.00 37.45 C ANISOU 1884 CB PHE A 284 4788 3428 6012 519 -1322 -1395 C ATOM 1885 CG PHE A 284 90.994 21.436 103.109 1.00 36.05 C ANISOU 1885 CG PHE A 284 4775 3203 5716 620 -1138 -1496 C ATOM 1886 CD1 PHE A 284 91.079 20.046 103.117 1.00 36.49 C ANISOU 1886 CD1 PHE A 284 4777 3230 5856 741 -944 -1376 C ATOM 1887 CD2 PHE A 284 89.732 22.015 103.185 1.00 34.86 C ANISOU 1887 CD2 PHE A 284 4800 3021 5423 590 -1184 -1600 C ATOM 1888 CE1 PHE A 284 89.931 19.257 103.166 1.00 35.19 C ANISOU 1888 CE1 PHE A 284 4774 3035 5559 810 -828 -1449 C ATOM 1889 CE2 PHE A 284 88.588 21.229 103.245 1.00 33.66 C ANISOU 1889 CE2 PHE A 284 4779 2859 5150 666 -1011 -1661 C ATOM 1890 CZ PHE A 284 88.687 19.848 103.247 1.00 33.65 C ANISOU 1890 CZ PHE A 284 4759 2854 5173 759 -883 -1595 C ATOM 1891 N LEU A 285 92.292 23.234 100.030 1.00 36.66 N ANISOU 1891 N LEU A 285 4485 3370 6073 270 -983 -1349 N ATOM 1892 CA LEU A 285 91.719 23.337 98.688 1.00 36.33 C ANISOU 1892 CA LEU A 285 4498 3381 5923 168 -817 -1380 C ATOM 1893 C LEU A 285 92.629 22.715 97.621 1.00 37.73 C ANISOU 1893 C LEU A 285 4498 3650 6188 166 -591 -1342 C ATOM 1894 O LEU A 285 92.139 22.053 96.715 1.00 36.13 O ANISOU 1894 O LEU A 285 4221 3451 6054 217 -264 -1470 O ATOM 1895 CB LEU A 285 91.403 24.776 98.302 1.00 36.49 C ANISOU 1895 CB LEU A 285 4521 3370 5972 23 -984 -1312 C ATOM 1896 CG LEU A 285 90.259 25.453 99.055 1.00 35.80 C ANISOU 1896 CG LEU A 285 4641 3161 5798 68 -1115 -1400 C ATOM 1897 CD1 LEU A 285 90.223 26.961 98.855 1.00 36.79 C ANISOU 1897 CD1 LEU A 285 4746 3177 6056 -23 -1281 -1313 C ATOM 1898 CD2 LEU A 285 88.899 24.854 98.709 1.00 34.53 C ANISOU 1898 CD2 LEU A 285 4606 3064 5447 121 -976 -1468 C ATOM 1899 N GLN A 286 93.939 22.940 97.736 1.00 39.93 N ANISOU 1899 N GLN A 286 4516 3967 6686 104 -649 -1176 N ATOM 1900 CA GLN A 286 94.918 22.345 96.817 1.00 41.95 C ANISOU 1900 CA GLN A 286 4571 4310 7054 142 -376 -1118 C ATOM 1901 C GLN A 286 94.881 20.826 96.815 1.00 42.14 C ANISOU 1901 C GLN A 286 4528 4302 7180 300 -154 -1201 C ATOM 1902 O GLN A 286 94.919 20.228 95.746 1.00 42.04 O ANISOU 1902 O GLN A 286 4484 4255 7234 276 132 -1232 O ATOM 1903 CB GLN A 286 96.346 22.825 97.106 1.00 44.14 C ANISOU 1903 CB GLN A 286 4558 4608 7603 119 -505 -926 C ATOM 1904 CG GLN A 286 96.640 24.191 96.531 1.00 45.05 C ANISOU 1904 CG GLN A 286 4582 4763 7773 -79 -641 -788 C ATOM 1905 CD GLN A 286 98.039 24.684 96.844 1.00 47.75 C ANISOU 1905 CD GLN A 286 4548 5214 8379 -113 -764 -613 C ATOM 1906 OE1 GLN A 286 98.322 25.147 97.950 1.00 48.23 O ANISOU 1906 OE1 GLN A 286 4356 5407 8561 -160 -1159 -603 O ATOM 1907 NE2 GLN A 286 98.917 24.602 95.866 1.00 49.88 N ANISOU 1907 NE2 GLN A 286 4591 5607 8752 -181 -514 -437 N ATOM 1908 N CYS A 287 94.789 20.222 98.000 1.00 42.52 N ANISOU 1908 N CYS A 287 4598 4360 7196 434 -295 -1161 N ATOM 1909 CA CYS A 287 94.789 18.752 98.130 1.00 44.50 C ANISOU 1909 CA CYS A 287 4988 4351 7567 695 40 -1281 C ATOM 1910 C CYS A 287 93.472 18.094 97.701 1.00 42.60 C ANISOU 1910 C CYS A 287 5055 4059 7070 642 256 -1391 C ATOM 1911 O CYS A 287 93.488 17.019 97.124 1.00 43.06 O ANISOU 1911 O CYS A 287 4991 4045 7322 654 495 -1427 O ATOM 1912 CB CYS A 287 95.181 18.316 99.544 1.00 47.21 C ANISOU 1912 CB CYS A 287 5524 4624 7789 1050 -65 -1063 C ATOM 1913 SG CYS A 287 96.923 18.709 99.928 1.00 53.14 S ANISOU 1913 SG CYS A 287 5803 5190 9196 983 -408 -920 S ATOM 1914 N VAL A 288 92.347 18.761 97.941 1.00 40.31 N ANISOU 1914 N VAL A 288 4957 3805 6554 502 70 -1492 N ATOM 1915 CA VAL A 288 91.051 18.316 97.430 1.00 38.76 C ANISOU 1915 CA VAL A 288 5011 3627 6087 473 180 -1628 C ATOM 1916 C VAL A 288 91.062 18.301 95.894 1.00 39.25 C ANISOU 1916 C VAL A 288 4958 3859 6094 353 497 -1683 C ATOM 1917 O VAL A 288 90.531 17.380 95.278 1.00 40.13 O ANISOU 1917 O VAL A 288 5206 4026 6015 304 662 -1840 O ATOM 1918 CB VAL A 288 89.903 19.210 97.947 1.00 36.98 C ANISOU 1918 CB VAL A 288 4905 3485 5659 374 -3 -1627 C ATOM 1919 CG1 VAL A 288 88.574 18.840 97.288 1.00 36.21 C ANISOU 1919 CG1 VAL A 288 4986 3441 5331 295 108 -1760 C ATOM 1920 CG2 VAL A 288 89.781 19.082 99.453 1.00 36.46 C ANISOU 1920 CG2 VAL A 288 4921 3301 5630 537 -247 -1617 C ATOM 1921 N LYS A 289 91.665 19.319 95.292 1.00 39.56 N ANISOU 1921 N LYS A 289 4904 3928 6199 259 431 -1641 N ATOM 1922 CA LYS A 289 91.809 19.424 93.833 1.00 41.46 C ANISOU 1922 CA LYS A 289 5168 4349 6237 2 601 -1679 C ATOM 1923 C LYS A 289 92.732 18.353 93.246 1.00 43.21 C ANISOU 1923 C LYS A 289 5393 4465 6558 -23 994 -1731 C ATOM 1924 O LYS A 289 92.416 17.761 92.222 1.00 42.94 O ANISOU 1924 O LYS A 289 5614 4122 6576 -220 1429 -1855 O ATOM 1925 CB LYS A 289 92.341 20.824 93.466 1.00 42.47 C ANISOU 1925 CB LYS A 289 5131 4563 6439 -154 441 -1468 C ATOM 1926 CG LYS A 289 92.584 21.116 91.994 1.00 44.56 C ANISOU 1926 CG LYS A 289 5385 5059 6484 -362 622 -1477 C ATOM 1927 CD LYS A 289 91.273 21.237 91.236 1.00 44.57 C ANISOU 1927 CD LYS A 289 5534 5189 6211 -481 581 -1486 C ATOM 1928 CE LYS A 289 91.515 21.271 89.729 1.00 47.46 C ANISOU 1928 CE LYS A 289 5899 5830 6302 -746 787 -1381 C ATOM 1929 NZ LYS A 289 90.292 20.828 89.003 1.00 47.81 N ANISOU 1929 NZ LYS A 289 6081 6033 6052 -919 810 -1447 N ATOM 1930 N ASN A 290 93.883 18.154 93.880 1.00 44.64 N ANISOU 1930 N ASN A 290 5337 4542 7081 204 998 -1571 N ATOM 1931 CA ASN A 290 94.838 17.168 93.445 1.00 48.11 C ANISOU 1931 CA ASN A 290 5599 5002 7677 380 1380 -1684 C ATOM 1932 C ASN A 290 95.383 16.384 94.657 1.00 48.96 C ANISOU 1932 C ASN A 290 5598 4961 8043 655 1300 -1596 C ATOM 1933 O ASN A 290 96.416 16.733 95.222 1.00 49.38 O ANISOU 1933 O ASN A 290 5456 4960 8344 798 1216 -1463 O ATOM 1934 CB ASN A 290 95.958 17.813 92.622 1.00 50.71 C ANISOU 1934 CB ASN A 290 5655 5527 8084 264 1477 -1490 C ATOM 1935 CG ASN A 290 96.915 16.769 92.030 1.00 54.71 C ANISOU 1935 CG ASN A 290 6027 6017 8742 401 1998 -1624 C ATOM 1936 OD1 ASN A 290 96.521 15.630 91.733 1.00 55.57 O ANISOU 1936 OD1 ASN A 290 6381 6020 8713 372 2398 -1839 O ATOM 1937 ND2 ASN A 290 98.191 17.141 91.888 1.00 57.40 N ANISOU 1937 ND2 ASN A 290 5989 6470 9348 418 1992 -1410 N ATOM 1938 N PRO A 291 94.682 15.306 95.054 1.00 48.95 N ANISOU 1938 N PRO A 291 5768 4737 8090 766 1412 -1678 N ATOM 1939 CA PRO A 291 95.131 14.476 96.175 1.00 50.08 C ANISOU 1939 CA PRO A 291 5855 4712 8460 978 1356 -1550 C ATOM 1940 C PRO A 291 96.432 13.683 95.928 1.00 53.42 C ANISOU 1940 C PRO A 291 6130 4789 9378 1201 1617 -1487 C ATOM 1941 O PRO A 291 97.021 13.206 96.887 1.00 52.70 O ANISOU 1941 O PRO A 291 6111 4136 9775 1511 1588 -1459 O ATOM 1942 CB PRO A 291 93.955 13.511 96.390 1.00 49.45 C ANISOU 1942 CB PRO A 291 6017 4558 8211 971 1489 -1679 C ATOM 1943 CG PRO A 291 92.802 14.104 95.661 1.00 47.53 C ANISOU 1943 CG PRO A 291 6037 4430 7590 733 1417 -1871 C ATOM 1944 CD PRO A 291 93.412 14.808 94.497 1.00 48.36 C ANISOU 1944 CD PRO A 291 6003 4666 7705 565 1525 -1891 C ATOM 1945 N GLU A 292 96.885 13.593 94.673 1.00 56.54 N ANISOU 1945 N GLU A 292 6559 5268 9656 1114 2019 -1676 N ATOM 1946 CA GLU A 292 98.136 12.899 94.317 1.00 62.38 C ANISOU 1946 CA GLU A 292 6773 6157 10769 1409 2443 -1534 C ATOM 1947 C GLU A 292 99.396 13.642 94.780 1.00 65.53 C ANISOU 1947 C GLU A 292 6766 6677 11453 1344 2117 -1281 C ATOM 1948 O GLU A 292 100.486 13.075 94.723 1.00 70.01 O ANISOU 1948 O GLU A 292 7030 7117 12452 1636 2516 -1347 O ATOM 1949 CB GLU A 292 98.250 12.655 92.794 1.00 64.82 C ANISOU 1949 CB GLU A 292 7163 6558 10906 1229 2866 -1823 C ATOM 1950 CG GLU A 292 97.305 11.606 92.222 1.00 65.91 C ANISOU 1950 CG GLU A 292 7736 6478 10828 1097 3166 -2192 C ATOM 1951 CD GLU A 292 95.834 12.024 92.248 1.00 63.32 C ANISOU 1951 CD GLU A 292 7649 6244 10167 877 2730 -2349 C ATOM 1952 OE1 GLU A 292 95.553 13.249 92.271 1.00 62.87 O ANISOU 1952 OE1 GLU A 292 7863 6181 9841 748 2221 -2276 O ATOM 1953 OE2 GLU A 292 94.944 11.135 92.264 1.00 62.97 O ANISOU 1953 OE2 GLU A 292 7977 5969 9978 821 2827 -2558 O ATOM 1954 N ASP A 293 99.270 14.899 95.213 1.00 64.50 N ANISOU 1954 N ASP A 293 6693 6649 11164 1269 1772 -1175 N ATOM 1955 CA ASP A 293 100.433 15.679 95.674 1.00 66.67 C ANISOU 1955 CA ASP A 293 6544 7138 11648 1202 1492 -819 C ATOM 1956 C ASP A 293 101.068 15.072 96.952 1.00 68.85 C ANISOU 1956 C ASP A 293 6597 7388 12172 1516 1261 -595 C ATOM 1957 O ASP A 293 100.354 14.724 97.906 1.00 67.39 O ANISOU 1957 O ASP A 293 6470 7259 11877 1594 1013 -545 O ATOM 1958 CB ASP A 293 100.018 17.142 95.899 1.00 64.36 C ANISOU 1958 CB ASP A 293 6354 6999 11098 1011 1096 -757 C ATOM 1959 CG ASP A 293 101.185 18.117 95.858 1.00 67.25 C ANISOU 1959 CG ASP A 293 6335 7535 11679 826 981 -383 C ATOM 1960 OD1 ASP A 293 102.349 17.729 95.603 1.00 70.60 O ANISOU 1960 OD1 ASP A 293 6388 7832 12605 1031 1024 -195 O ATOM 1961 OD2 ASP A 293 100.914 19.312 96.096 1.00 67.77 O ANISOU 1961 OD2 ASP A 293 7084 7292 11371 377 813 -234 O ATOM 1962 N SER A 294 102.402 14.937 96.950 1.00 72.96 N ANISOU 1962 N SER A 294 6668 8005 13049 1707 1397 -389 N ATOM 1963 CA SER A 294 103.148 14.314 98.072 1.00 75.43 C ANISOU 1963 CA SER A 294 6740 8151 13768 1962 1218 -55 C ATOM 1964 C SER A 294 103.150 15.163 99.357 1.00 73.86 C ANISOU 1964 C SER A 294 6414 8190 13459 1832 462 186 C ATOM 1965 O SER A 294 103.389 14.624 100.448 1.00 73.52 O ANISOU 1965 O SER A 294 5700 8250 13981 2243 34 449 O ATOM 1966 CB SER A 294 104.589 13.961 97.661 1.00 80.04 C ANISOU 1966 CB SER A 294 6814 8812 14785 2023 1560 208 C ATOM 1967 OG SER A 294 105.291 15.099 97.204 1.00 81.08 O ANISOU 1967 OG SER A 294 6832 9146 14828 1674 1542 88 O ATOM 1968 N SER A 295 102.881 16.472 99.219 1.00 71.85 N ANISOU 1968 N SER A 295 6387 7999 12915 1404 303 79 N ATOM 1969 CA SER A 295 102.643 17.386 100.356 1.00 69.73 C ANISOU 1969 CA SER A 295 6157 7747 12587 1270 -184 213 C ATOM 1970 C SER A 295 101.409 17.049 101.224 1.00 66.06 C ANISOU 1970 C SER A 295 6166 7104 11829 1397 -355 -18 C ATOM 1971 O SER A 295 101.393 17.352 102.418 1.00 65.28 O ANISOU 1971 O SER A 295 6380 6620 11803 1386 -943 14 O ATOM 1972 CB SER A 295 102.545 18.838 99.857 1.00 68.15 C ANISOU 1972 CB SER A 295 6020 7761 12113 1001 -443 194 C ATOM 1973 OG SER A 295 101.821 18.909 98.649 1.00 66.57 O ANISOU 1973 OG SER A 295 6202 7339 11751 976 -225 232 O ATOM 1974 N CYS A 296 100.388 16.429 100.636 1.00 64.02 N ANISOU 1974 N CYS A 296 6079 6827 11419 1467 -45 -168 N ATOM 1975 CA CYS A 296 99.183 16.035 101.383 1.00 61.83 C ANISOU 1975 CA CYS A 296 6158 6475 10858 1459 -150 -271 C ATOM 1976 C CYS A 296 99.387 14.687 102.083 1.00 64.53 C ANISOU 1976 C CYS A 296 6576 6592 11350 1706 -25 -84 C ATOM 1977 O CYS A 296 99.527 14.601 103.310 1.00 67.08 O ANISOU 1977 O CYS A 296 7048 6986 11453 1677 -320 179 O ATOM 1978 CB CYS A 296 98.006 15.923 100.428 1.00 58.95 C ANISOU 1978 CB CYS A 296 6085 5992 10319 1505 151 -651 C ATOM 1979 SG CYS A 296 98.017 17.168 99.133 1.00 58.90 S ANISOU 1979 SG CYS A 296 6266 6058 10054 1596 323 -836 S TER 1980 CYS A 296 If you find results from this site helpful for your research, please cite one of our 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