HEADER MEMBRANE PROTEIN 13-APR-20 6WJC TITLE MUSCARINIC ACETYLCHOLINE RECEPTOR 1 - MUSCARINIC TOXIN 7 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUSCARINIC ACETYLCHOLINE RECEPTOR M1,ENDOLYSIN FUSION; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LYSIS PROTEIN,LYSOZYME,MURAMIDASE; COMPND 5 EC: 3.2.1.17; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: MUSCARINIC TOXIN 7; COMPND 9 CHAIN: C; COMPND 10 SYNONYM: MT7,MUSCARINIC TOXIN 1,M1-TOXIN; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: CHRM1, E, T4TP126; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS; SOURCE 11 ORGANISM_COMMON: EASTERN GREEN MAMBA; SOURCE 12 ORGANISM_TAXID: 8618; SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS GPCR, NATURAL TOXIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.MAEDA,B.K.KOBILKA REVDAT 2 22-JUL-20 6WJC 1 JRNL REVDAT 1 08-JUL-20 6WJC 0 JRNL AUTH S.MAEDA,J.XU,F.M.N KADJI,M.J.CLARK,J.ZHAO,N.TSUTSUMI,J.AOKI, JRNL AUTH 2 R.K.SUNAHARA,A.INOUE,K.C.GARCIA,B.K.KOBILKA JRNL TITL STRUCTURE AND SELECTIVITY ENGINEERING OF THE M1MUSCARINIC JRNL TITL 2 RECEPTOR TOXIN COMPLEX. JRNL REF SCIENCE V. 369 161 2020 JRNL REFN ESSN 1095-9203 JRNL PMID 32646996 JRNL DOI 10.1126/SCIENCE.AAX2517 REMARK 2 REMARK 2 RESOLUTION. 2.55 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17_3644 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.11 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 44346 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.245 REMARK 3 R VALUE (WORKING SET) : 0.245 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500 REMARK 3 FREE R VALUE TEST SET COUNT : 1997 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 44.1100 - 6.1400 0.98 3031 143 0.2023 0.2093 REMARK 3 2 6.1400 - 4.8800 0.99 3035 143 0.2317 0.2476 REMARK 3 3 4.8800 - 4.2600 0.99 3048 144 0.1992 0.2165 REMARK 3 4 4.2600 - 3.8700 0.99 3010 142 0.2117 0.2429 REMARK 3 5 3.8700 - 3.5900 0.97 2953 138 0.2641 0.2527 REMARK 3 6 3.5900 - 3.3800 0.99 3043 144 0.2626 0.3034 REMARK 3 7 3.3800 - 3.2100 1.00 3037 143 0.2869 0.2805 REMARK 3 8 3.2100 - 3.0700 1.00 3019 143 0.3119 0.3850 REMARK 3 9 3.0700 - 2.9500 1.00 3036 142 0.3292 0.3926 REMARK 3 10 2.9500 - 2.8500 1.00 3013 143 0.3516 0.4162 REMARK 3 11 2.8500 - 2.7600 1.00 3028 143 0.3829 0.5063 REMARK 3 12 2.7600 - 2.6800 1.00 3025 143 0.4354 0.4720 REMARK 3 13 2.6800 - 2.6100 1.00 3045 143 0.4513 0.4754 REMARK 3 14 2.6100 - 2.5500 1.00 3026 143 0.4763 0.4545 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.270 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 123.9 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 17:57) REMARK 3 ORIGIN FOR THE GROUP (A): 8.8651 29.2188 1.6213 REMARK 3 T TENSOR REMARK 3 T11: 0.8221 T22: 0.5314 REMARK 3 T33: 1.2026 T12: 0.0270 REMARK 3 T13: -0.1571 T23: -0.0621 REMARK 3 L TENSOR REMARK 3 L11: 4.5721 L22: 0.9084 REMARK 3 L33: 5.0992 L12: -1.7351 REMARK 3 L13: -0.1128 L23: -1.1007 REMARK 3 S TENSOR REMARK 3 S11: -0.2325 S12: 0.3464 S13: 0.0201 REMARK 3 S21: 0.3635 S22: -0.0194 S23: -1.1833 REMARK 3 S31: -0.0781 S32: 0.1308 S33: 0.1539 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 58:207) REMARK 3 ORIGIN FOR THE GROUP (A): 25.5817 22.6029 -0.1616 REMARK 3 T TENSOR REMARK 3 T11: 0.6111 T22: 0.5441 REMARK 3 T33: 1.0541 T12: -0.1006 REMARK 3 T13: -0.0055 T23: 0.0656 REMARK 3 L TENSOR REMARK 3 L11: 3.2695 L22: 0.6772 REMARK 3 L33: 3.4122 L12: -0.5758 REMARK 3 L13: 1.5237 L23: 1.0013 REMARK 3 S TENSOR REMARK 3 S11: -0.3016 S12: 0.2592 S13: 0.3595 REMARK 3 S21: -0.2444 S22: 0.1153 S23: -0.0201 REMARK 3 S31: -0.3876 S32: 0.4028 S33: 0.1382 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 208:218) REMARK 3 ORIGIN FOR THE GROUP (A): 44.1170 50.2151 29.3401 REMARK 3 T TENSOR REMARK 3 T11: 0.9733 T22: 0.7644 REMARK 3 T33: 1.5621 T12: -0.0704 REMARK 3 T13: -0.2447 T23: 0.0113 REMARK 3 L TENSOR REMARK 3 L11: 4.0827 L22: 1.3483 REMARK 3 L33: 5.2304 L12: -0.4081 REMARK 3 L13: -0.0174 L23: 0.2534 REMARK 3 S TENSOR REMARK 3 S11: -0.4206 S12: -0.0762 S13: 0.4470 REMARK 3 S21: -0.2062 S22: 0.0650 S23: 0.2880 REMARK 3 S31: -0.3952 S32: 0.0052 S33: 0.2965 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 386:414) REMARK 3 ORIGIN FOR THE GROUP (A): 21.0455 22.5727 13.5449 REMARK 3 T TENSOR REMARK 3 T11: 0.7510 T22: 0.6077 REMARK 3 T33: 0.2767 T12: -0.0647 REMARK 3 T13: 0.0708 T23: 0.0168 REMARK 3 L TENSOR REMARK 3 L11: 5.2250 L22: 2.2219 REMARK 3 L33: 2.2960 L12: 3.0924 REMARK 3 L13: -0.3621 L23: 0.4381 REMARK 3 S TENSOR REMARK 3 S11: -0.1633 S12: -0.1635 S13: 0.0954 REMARK 3 S21: -1.0391 S22: -0.4185 S23: -0.8394 REMARK 3 S31: -0.1520 S32: -0.0683 S33: 0.6310 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 415:461) REMARK 3 ORIGIN FOR THE GROUP (A): 12.1295 29.8458 7.1791 REMARK 3 T TENSOR REMARK 3 T11: 0.5029 T22: 0.7019 REMARK 3 T33: 1.0353 T12: -0.0228 REMARK 3 T13: 0.0085 T23: -0.0450 REMARK 3 L TENSOR REMARK 3 L11: 7.0035 L22: 8.5929 REMARK 3 L33: 6.0509 L12: 3.7664 REMARK 3 L13: 0.9743 L23: -3.1240 REMARK 3 S TENSOR REMARK 3 S11: -0.4881 S12: -0.1455 S13: 1.2585 REMARK 3 S21: -0.4042 S22: 0.1617 S23: -0.4105 REMARK 3 S31: -0.5997 S32: -0.1786 S33: 0.3156 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN A AND RESID 219:221) REMARK 3 ORIGIN FOR THE GROUP (A): 28.4864 -20.7685 -13.4884 REMARK 3 T TENSOR REMARK 3 T11: 1.5296 T22: 0.8082 REMARK 3 T33: 1.8931 T12: 0.2698 REMARK 3 T13: -0.4744 T23: -0.1925 REMARK 3 L TENSOR REMARK 3 L11: 8.8469 L22: 7.0459 REMARK 3 L33: 4.0081 L12: 7.7797 REMARK 3 L13: 5.4025 L23: 5.1322 REMARK 3 S TENSOR REMARK 3 S11: 1.1796 S12: 0.1587 S13: -0.6268 REMARK 3 S21: 1.7918 S22: -0.3519 S23: -2.6974 REMARK 3 S31: 2.3523 S32: 1.9268 S33: -0.7494 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN A AND RESID 222:235) REMARK 3 ORIGIN FOR THE GROUP (A): 31.9440 -7.1579 -7.1824 REMARK 3 T TENSOR REMARK 3 T11: 1.1765 T22: 1.2459 REMARK 3 T33: 1.3725 T12: 0.1552 REMARK 3 T13: -0.2109 T23: -0.1634 REMARK 3 L TENSOR REMARK 3 L11: 6.9851 L22: 3.7238 REMARK 3 L33: 3.7407 L12: -3.8963 REMARK 3 L13: -4.0841 L23: 3.6457 REMARK 3 S TENSOR REMARK 3 S11: 0.1816 S12: -0.3020 S13: -1.4364 REMARK 3 S21: 0.7023 S22: 0.3688 S23: -1.0235 REMARK 3 S31: 0.4392 S32: 2.3483 S33: -0.5824 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN A AND RESID 236:246) REMARK 3 ORIGIN FOR THE GROUP (A): 23.0405 -14.8998 -5.5463 REMARK 3 T TENSOR REMARK 3 T11: 1.4549 T22: 0.7521 REMARK 3 T33: 1.8325 T12: 0.2320 REMARK 3 T13: -0.1699 T23: -0.0599 REMARK 3 L TENSOR REMARK 3 L11: 9.1039 L22: 4.3082 REMARK 3 L33: 3.6760 L12: -6.2620 REMARK 3 L13: -1.1535 L23: 0.8753 REMARK 3 S TENSOR REMARK 3 S11: -0.0268 S12: 0.6180 S13: -1.2266 REMARK 3 S21: 1.8275 S22: -0.4248 S23: 1.1886 REMARK 3 S31: 1.3864 S32: 0.7450 S33: 0.4446 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN A AND RESID 247:254) REMARK 3 ORIGIN FOR THE GROUP (A): 16.4425 2.7318 2.3528 REMARK 3 T TENSOR REMARK 3 T11: 1.1390 T22: 0.6001 REMARK 3 T33: 1.7483 T12: 0.1158 REMARK 3 T13: -0.0000 T23: -0.1891 REMARK 3 L TENSOR REMARK 3 L11: 5.5471 L22: 5.5979 REMARK 3 L33: 9.0637 L12: -1.7634 REMARK 3 L13: -3.6372 L23: 6.9562 REMARK 3 S TENSOR REMARK 3 S11: 0.1171 S12: 0.0159 S13: 0.0947 REMARK 3 S21: 1.4979 S22: -0.1309 S23: -0.4817 REMARK 3 S31: -0.7411 S32: 1.1651 S33: 0.0040 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN A AND RESID 255:264) REMARK 3 ORIGIN FOR THE GROUP (A): 22.9690 -10.7631 -3.7265 REMARK 3 T TENSOR REMARK 3 T11: 1.2643 T22: 0.9079 REMARK 3 T33: 1.8020 T12: 0.1867 REMARK 3 T13: -0.3607 T23: -0.1578 REMARK 3 L TENSOR REMARK 3 L11: 5.5537 L22: 3.8444 REMARK 3 L33: 3.5776 L12: 4.3504 REMARK 3 L13: -2.6680 L23: -2.8353 REMARK 3 S TENSOR REMARK 3 S11: -0.3017 S12: -0.0846 S13: -0.9003 REMARK 3 S21: 1.4960 S22: 0.6674 S23: -0.7815 REMARK 3 S31: 1.2907 S32: -0.3518 S33: -0.2729 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN A AND RESID 265:273) REMARK 3 ORIGIN FOR THE GROUP (A): 12.4620 -6.6756 1.0015 REMARK 3 T TENSOR REMARK 3 T11: 1.1321 T22: 0.9019 REMARK 3 T33: 2.1543 T12: -0.0143 REMARK 3 T13: 0.1295 T23: 0.0345 REMARK 3 L TENSOR REMARK 3 L11: 5.1968 L22: 4.9199 REMARK 3 L33: 9.6765 L12: -4.9325 REMARK 3 L13: -1.3699 L23: -0.1048 REMARK 3 S TENSOR REMARK 3 S11: -1.4873 S12: -0.9696 S13: 0.7256 REMARK 3 S21: 0.9461 S22: 0.7708 S23: -0.2582 REMARK 3 S31: 1.7947 S32: -0.4202 S33: 0.8179 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN A AND RESID 274:283) REMARK 3 ORIGIN FOR THE GROUP (A): 22.5449 -12.7633 -13.0452 REMARK 3 T TENSOR REMARK 3 T11: 1.4385 T22: 1.0848 REMARK 3 T33: 2.0051 T12: 0.1704 REMARK 3 T13: -0.0865 T23: -0.1254 REMARK 3 L TENSOR REMARK 3 L11: 5.9287 L22: 4.1007 REMARK 3 L33: 3.6392 L12: -4.9300 REMARK 3 L13: -4.6422 L23: 3.8612 REMARK 3 S TENSOR REMARK 3 S11: -0.1106 S12: 1.5639 S13: -1.6055 REMARK 3 S21: -0.1366 S22: 0.2344 S23: 1.3915 REMARK 3 S31: 1.4575 S32: -0.3625 S33: -0.1546 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6WJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-20. REMARK 100 THE DEPOSITION ID IS D_1000240752. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-DEC-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44412 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 REMARK 200 RESOLUTION RANGE LOW (A) : 46.310 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.50 REMARK 200 R MERGE FOR SHELL (I) : 1.09300 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 2.8.2 REMARK 200 STARTING MODEL: 5CXV, 2VLW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 22-27% SOKALAN, HEPES(7.5), 0.1M NACL, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 61.07400 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.21450 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.07400 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 75.21450 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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: 2870 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26030 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ALA A -1 REMARK 465 ALA A 0 REMARK 465 ALA A 1 REMARK 465 GLN A 2 REMARK 465 THR A 3 REMARK 465 SER A 4 REMARK 465 ALA A 5 REMARK 465 PRO A 6 REMARK 465 PRO A 7 REMARK 465 ALA A 8 REMARK 465 VAL A 9 REMARK 465 SER A 10 REMARK 465 PRO A 11 REMARK 465 GLN A 12 REMARK 465 ILE A 13 REMARK 465 THR A 14 REMARK 465 VAL A 15 REMARK 465 LEU A 16 REMARK 465 ASP A 438 REMARK 465 LYS A 439 REMARK 465 ARG A 440 REMARK 465 ARG A 441 REMARK 465 TRP A 442 REMARK 465 ARG A 443 REMARK 465 LYS A 444 REMARK 465 ILE A 445 REMARK 465 PRO A 446 REMARK 465 LYS A 447 REMARK 465 ARG A 448 REMARK 465 PRO A 449 REMARK 465 GLY A 450 REMARK 465 SER A 451 REMARK 465 VAL A 452 REMARK 465 HIS A 453 REMARK 465 ARG A 454 REMARK 465 THR A 455 REMARK 465 PRO A 456 REMARK 465 SER A 457 REMARK 465 ARG A 458 REMARK 465 GLN A 459 REMARK 465 CYS A 460 REMARK 465 HIS A 461 REMARK 465 HIS A 462 REMARK 465 HIS A 463 REMARK 465 HIS A 464 REMARK 465 HIS A 465 REMARK 465 HIS A 466 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 20 CG CD CE NZ REMARK 470 LYS A 51 CG CD CE NZ REMARK 470 LYS A 136 CG CD CE NZ REMARK 470 ARG A 213 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1015 CG CD CE NZ REMARK 470 LYS A1018 CG CD CE NZ REMARK 470 GLU A1021 CG CD OE1 OE2 REMARK 470 LYS A1047 CG CD CE NZ REMARK 470 ILE A1049 CD1 REMARK 470 ASN A1052 CG OD1 ND2 REMARK 470 LYS A1064 CG CD CE NZ REMARK 470 LYS A1123 CG CD CE NZ REMARK 470 ASN A1143 CG OD1 ND2 REMARK 470 LYS A 392 CG CD CE NZ REMARK 470 ASP A 393 CG OD1 OD2 REMARK 470 TRP A 437 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 437 CZ3 CH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OD1 ASP A 71 NH2 ARG A 112 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ACM A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OIN A 506 DBREF 6WJC A 2 218 UNP P11229 ACM1_HUMAN 2 218 DBREF 6WJC A 1001 1160 UNP D9IEF7 D9IEF7_BPT4 2 161 DBREF 6WJC A 355 460 UNP P11229 ACM1_HUMAN 355 460 DBREF 6WJC C 1 65 UNP Q8QGR0 3SIM7_DENAN 22 86 SEQADV 6WJC ASP A -8 UNP P11229 EXPRESSION TAG SEQADV 6WJC TYR A -7 UNP P11229 EXPRESSION TAG SEQADV 6WJC LYS A -6 UNP P11229 EXPRESSION TAG SEQADV 6WJC ASP A -5 UNP P11229 EXPRESSION TAG SEQADV 6WJC ASP A -4 UNP P11229 EXPRESSION TAG SEQADV 6WJC ASP A -3 UNP P11229 EXPRESSION TAG SEQADV 6WJC ASP A -2 UNP P11229 EXPRESSION TAG SEQADV 6WJC ALA A -1 UNP P11229 EXPRESSION TAG SEQADV 6WJC ALA A 0 UNP P11229 EXPRESSION TAG SEQADV 6WJC ALA A 1 UNP P11229 EXPRESSION TAG SEQADV 6WJC GLN A 2 UNP P11229 ASN 2 CONFLICT SEQADV 6WJC GLN A 12 UNP P11229 ASN 12 CONFLICT SEQADV 6WJC GLN A 110 UNP P11229 ASN 110 CONFLICT SEQADV 6WJC ARG A 112 UNP P11229 SER 112 CONFLICT SEQADV 6WJC THR A 1053 UNP D9IEF7 CYS 54 CONFLICT SEQADV 6WJC ALA A 1096 UNP D9IEF7 CYS 97 CONFLICT SEQADV 6WJC HIS A 461 UNP P11229 EXPRESSION TAG SEQADV 6WJC HIS A 462 UNP P11229 EXPRESSION TAG SEQADV 6WJC HIS A 463 UNP P11229 EXPRESSION TAG SEQADV 6WJC HIS A 464 UNP P11229 EXPRESSION TAG SEQADV 6WJC HIS A 465 UNP P11229 EXPRESSION TAG SEQADV 6WJC HIS A 466 UNP P11229 EXPRESSION TAG SEQADV 6WJC GLY C -3 UNP Q8QGR0 EXPRESSION TAG SEQADV 6WJC PRO C -2 UNP Q8QGR0 EXPRESSION TAG SEQADV 6WJC GLY C -1 UNP Q8QGR0 EXPRESSION TAG SEQADV 6WJC SER C 0 UNP Q8QGR0 EXPRESSION TAG SEQRES 1 A 499 ASP TYR LYS ASP ASP ASP ASP ALA ALA ALA GLN THR SER SEQRES 2 A 499 ALA PRO PRO ALA VAL SER PRO GLN ILE THR VAL LEU ALA SEQRES 3 A 499 PRO GLY LYS GLY PRO TRP GLN VAL ALA PHE ILE GLY ILE SEQRES 4 A 499 THR THR GLY LEU LEU SER LEU ALA THR VAL THR GLY ASN SEQRES 5 A 499 LEU LEU VAL LEU ILE SER PHE LYS VAL ASN THR GLU LEU SEQRES 6 A 499 LYS THR VAL ASN ASN TYR PHE LEU LEU SER LEU ALA CYS SEQRES 7 A 499 ALA ASP LEU ILE ILE GLY THR PHE SER MET ASN LEU TYR SEQRES 8 A 499 THR THR TYR LEU LEU MET GLY HIS TRP ALA LEU GLY THR SEQRES 9 A 499 LEU ALA CYS ASP LEU TRP LEU ALA LEU ASP TYR VAL ALA SEQRES 10 A 499 SER GLN ALA ARG VAL MET ASN LEU LEU LEU ILE SER PHE SEQRES 11 A 499 ASP ARG TYR PHE SER VAL THR ARG PRO LEU SER TYR ARG SEQRES 12 A 499 ALA LYS ARG THR PRO ARG ARG ALA ALA LEU MET ILE GLY SEQRES 13 A 499 LEU ALA TRP LEU VAL SER PHE VAL LEU TRP ALA PRO ALA SEQRES 14 A 499 ILE LEU PHE TRP GLN TYR LEU VAL GLY GLU ARG THR VAL SEQRES 15 A 499 LEU ALA GLY GLN CYS TYR ILE GLN PHE LEU SER GLN PRO SEQRES 16 A 499 ILE ILE THR PHE GLY THR ALA MET ALA ALA PHE TYR LEU SEQRES 17 A 499 PRO VAL THR VAL MET CYS THR LEU TYR TRP ARG ILE TYR SEQRES 18 A 499 ARG GLU THR GLU ASN ARG ASN ILE PHE GLU MET LEU ARG SEQRES 19 A 499 ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR SEQRES 20 A 499 GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR SEQRES 21 A 499 LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP SEQRES 22 A 499 LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS SEQRES 23 A 499 ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA SEQRES 24 A 499 ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO SEQRES 25 A 499 VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU SEQRES 26 A 499 ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA SEQRES 27 A 499 GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG SEQRES 28 A 499 TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP SEQRES 29 A 499 TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR SEQRES 30 A 499 THR PHE ARG THR GLY THR TRP ASP ALA TYR PHE SER LEU SEQRES 31 A 499 VAL LYS GLU LYS LYS ALA ALA ARG THR LEU SER ALA ILE SEQRES 32 A 499 LEU LEU ALA PHE ILE LEU THR TRP THR PRO TYR ASN ILE SEQRES 33 A 499 MET VAL LEU VAL SER THR PHE CYS LYS ASP CYS VAL PRO SEQRES 34 A 499 GLU THR LEU TRP GLU LEU GLY TYR TRP LEU CYS TYR VAL SEQRES 35 A 499 ASN SER THR ILE ASN PRO MET CYS TYR ALA LEU CYS ASN SEQRES 36 A 499 LYS ALA PHE ARG ASP THR PHE ARG LEU LEU LEU LEU CYS SEQRES 37 A 499 ARG TRP ASP LYS ARG ARG TRP ARG LYS ILE PRO LYS ARG SEQRES 38 A 499 PRO GLY SER VAL HIS ARG THR PRO SER ARG GLN CYS HIS SEQRES 39 A 499 HIS HIS HIS HIS HIS SEQRES 1 C 69 GLY PRO GLY SER LEU THR CYS VAL LYS SER ASN SER ILE SEQRES 2 C 69 TRP PHE PRO THR SER GLU ASP CYS PRO ASP GLY GLN ASN SEQRES 3 C 69 LEU CYS PHE LYS ARG TRP GLN TYR ILE SER PRO ARG MET SEQRES 4 C 69 TYR ASP PHE THR ARG GLY CYS ALA ALA THR CYS PRO LYS SEQRES 5 C 69 ALA GLU TYR ARG ASP VAL ILE ASN CYS CYS GLY THR ASP SEQRES 6 C 69 LYS CYS ASN LYS HET ACM A 501 4 HET Y01 A 502 35 HET Y01 A 503 35 HET Y01 A 504 35 HET Y01 A 505 35 HET OIN A 506 21 HETNAM ACM ACETAMIDE HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM OIN (1R,5S)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL (2R)-3- HETNAM 2 OIN HYDROXY-2-PHENYLPROPANOATE HETSYN OIN ATROPINE FORMUL 3 ACM C2 H5 N O FORMUL 4 Y01 4(C31 H50 O4) FORMUL 8 OIN C17 H23 N O3 FORMUL 9 HOH *7(H2 O) HELIX 1 AA1 PRO A 22 ASN A 53 1 32 HELIX 2 AA2 THR A 58 PHE A 77 1 20 HELIX 3 AA3 PHE A 77 GLY A 89 1 13 HELIX 4 AA4 LEU A 93 ARG A 129 1 37 HELIX 5 AA5 TYR A 133 ARG A 137 5 5 HELIX 6 AA6 ARG A 140 VAL A 168 1 29 HELIX 7 AA7 ILE A 180 SER A 184 5 5 HELIX 8 AA8 GLN A 185 PHE A 197 1 13 HELIX 9 AA9 PHE A 197 GLY A 1011 1 33 HELIX 10 AB1 SER A 1037 ILE A 1049 1 13 HELIX 11 AB2 THR A 1058 ARG A 1079 1 22 HELIX 12 AB3 LYS A 1082 LEU A 1090 1 9 HELIX 13 AB4 ASP A 1091 MET A 1105 1 15 HELIX 14 AB5 GLY A 1106 ALA A 1111 1 6 HELIX 15 AB6 PHE A 1113 GLN A 1121 1 9 HELIX 16 AB7 ARG A 1124 LYS A 1134 1 11 HELIX 17 AB8 SER A 1135 THR A 1141 1 7 HELIX 18 AB9 ASN A 1143 GLY A 1155 1 13 HELIX 19 AC1 VAL A 358 CYS A 391 1 34 HELIX 20 AC2 PRO A 396 ASN A 422 1 27 HELIX 21 AC3 ASN A 422 LEU A 434 1 13 SHEET 1 AA1 3 ARG A1013 LYS A1018 0 SHEET 2 AA1 3 TYR A1024 GLY A1027 -1 O THR A1025 N TYR A1017 SHEET 3 AA1 3 HIS A1030 THR A1033 -1 O LEU A1032 N TYR A1024 SHEET 1 AA2 2 THR C 2 LYS C 5 0 SHEET 2 AA2 2 THR C 13 ASP C 16 -1 O THR C 13 N LYS C 5 SHEET 1 AA3 3 TYR C 36 ALA C 43 0 SHEET 2 AA3 3 LEU C 23 TYR C 30 -1 N ARG C 27 O THR C 39 SHEET 3 AA3 3 VAL C 54 CYS C 58 -1 O CYS C 58 N CYS C 24 SSBOND 1 CYS A 98 CYS A 178 1555 1555 2.03 SSBOND 2 CYS A 391 CYS A 394 1555 1555 2.03 SSBOND 3 CYS C 3 CYS C 24 1555 1555 2.03 SSBOND 4 CYS C 17 CYS C 42 1555 1555 2.03 SSBOND 5 CYS C 46 CYS C 57 1555 1555 2.03 SSBOND 6 CYS C 58 CYS C 63 1555 1555 2.03 LINK SG CYS A 421 C2 ACM A 501 1555 1555 1.77 SITE 1 AC1 3 ARG A 365 LEU A 420 CYS A 421 SITE 1 AC2 5 THR A 31 GLY A 33 THR A 84 ALA A 92 SITE 2 AC2 5 LEU A 93 SITE 1 AC3 6 GLN A 24 PHE A 27 LEU A 35 THR A 398 SITE 2 AC3 6 LEU A 399 LEU A 402 SITE 1 AC4 5 TYR A 62 PRO A 139 ALA A 143 ILE A 146 SITE 2 AC4 5 Y01 A 505 SITE 1 AC5 6 LEU A 47 PHE A 50 LYS A 51 LYS A 57 SITE 2 AC5 6 CYS A 69 Y01 A 504 SITE 1 AC6 9 ASP A 105 TYR A 106 SER A 109 GLN A 110 SITE 2 AC6 9 ALA A 193 TRP A 378 TYR A 381 ASN A 382 SITE 3 AC6 9 TYR A 404 CRYST1 122.148 150.429 76.927 90.00 98.77 90.00 C 1 2 1 4 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 0.008187 0.000000 0.001263 0.00000 SCALE2 0.000000 0.006648 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013153 0.00000 ATOM 1 N ALA A 17 -3.829 -4.101 -2.014 1.00210.61 N ANISOU 1 N ALA A 17 31316 15944 32763 -4944 386 -4061 N ATOM 2 CA ALA A 17 -3.723 -3.766 -0.600 1.00208.90 C ANISOU 2 CA ALA A 17 31040 15682 32650 -4839 430 -3424 C ATOM 3 C ALA A 17 -3.764 -2.255 -0.394 1.00193.41 C ANISOU 3 C ALA A 17 28686 14421 30379 -4717 491 -3307 C ATOM 4 O ALA A 17 -2.936 -1.528 -0.943 1.00199.53 O ANISOU 4 O ALA A 17 29362 15455 30994 -4300 545 -3534 O ATOM 5 CB ALA A 17 -2.448 -4.350 -0.010 1.00211.16 C ANISOU 5 CB ALA A 17 31645 15401 33184 -4284 481 -3186 C ATOM 6 N PRO A 18 -4.731 -1.785 0.392 1.00170.78 N ANISOU 6 N PRO A 18 25595 11859 27433 -5084 485 -2945 N ATOM 7 CA PRO A 18 -4.839 -0.342 0.640 1.00165.44 C ANISOU 7 CA PRO A 18 24575 11826 26459 -4987 536 -2829 C ATOM 8 C PRO A 18 -3.750 0.146 1.583 1.00155.03 C ANISOU 8 C PRO A 18 23288 10372 25246 -4424 587 -2445 C ATOM 9 O PRO A 18 -3.432 -0.499 2.585 1.00152.29 O ANISOU 9 O PRO A 18 23137 9572 25156 -4288 595 -2019 O ATOM 10 CB PRO A 18 -6.230 -0.196 1.267 1.00163.01 C ANISOU 10 CB PRO A 18 24069 11820 26046 -5565 521 -2527 C ATOM 11 CG PRO A 18 -6.482 -1.515 1.913 1.00163.17 C ANISOU 11 CG PRO A 18 24350 11216 26432 -5788 483 -2224 C ATOM 12 CD PRO A 18 -5.819 -2.542 1.034 1.00177.04 C ANISOU 12 CD PRO A 18 26426 12447 28395 -5629 433 -2637 C ATOM 13 N GLY A 19 -3.179 1.301 1.252 1.00154.27 N ANISOU 13 N GLY A 19 22979 10692 24946 -4090 616 -2591 N ATOM 14 CA GLY A 19 -2.117 1.876 2.054 1.00169.83 C ANISOU 14 CA GLY A 19 24918 12601 27006 -3545 633 -2268 C ATOM 15 C GLY A 19 -2.597 2.950 3.008 1.00176.52 C ANISOU 15 C GLY A 19 25482 14002 27586 -3523 555 -1829 C ATOM 16 O GLY A 19 -3.001 4.035 2.579 1.00186.30 O ANISOU 16 O GLY A 19 26434 15935 28416 -3548 488 -1944 O ATOM 17 N LYS A 20 -2.555 2.661 4.307 1.00169.22 N ANISOU 17 N LYS A 20 24626 12865 26804 -3414 531 -1289 N ATOM 18 CA LYS A 20 -2.985 3.606 5.337 1.00144.94 C ANISOU 18 CA LYS A 20 21295 10379 23397 -3306 411 -819 C ATOM 19 C LYS A 20 -1.775 4.428 5.771 1.00136.21 C ANISOU 19 C LYS A 20 20096 9416 22239 -2688 336 -683 C ATOM 20 O LYS A 20 -0.943 3.968 6.556 1.00144.69 O ANISOU 20 O LYS A 20 21311 10087 23579 -2350 348 -401 O ATOM 21 CB LYS A 20 -3.615 2.866 6.513 1.00125.95 C ANISOU 21 CB LYS A 20 18983 7735 21137 -3509 425 -296 C ATOM 22 N GLY A 21 -1.680 5.654 5.262 1.00136.52 N ANISOU 22 N GLY A 21 19892 10043 21938 -2544 256 -873 N ATOM 23 CA GLY A 21 -0.561 6.517 5.557 1.00127.37 C ANISOU 23 CA GLY A 21 18619 9048 20728 -2023 168 -789 C ATOM 24 C GLY A 21 -0.670 7.200 6.907 1.00129.04 C ANISOU 24 C GLY A 21 18701 9589 20739 -1805 21 -303 C ATOM 25 O GLY A 21 -1.759 7.342 7.473 1.00136.81 O ANISOU 25 O GLY A 21 19609 10882 21491 -2045 -22 -58 O ATOM 26 N PRO A 22 0.464 7.632 7.449 1.00119.52 N ANISOU 26 N PRO A 22 17455 8357 19602 -1336 -64 -159 N ATOM 27 CA PRO A 22 0.455 8.341 8.732 1.00101.45 C ANISOU 27 CA PRO A 22 15041 6405 17101 -1083 -230 254 C ATOM 28 C PRO A 22 0.090 9.806 8.547 1.00107.34 C ANISOU 28 C PRO A 22 15556 7800 17429 -1052 -366 159 C ATOM 29 O PRO A 22 0.157 10.359 7.449 1.00114.15 O ANISOU 29 O PRO A 22 16334 8834 18202 -1128 -335 -198 O ATOM 30 CB PRO A 22 1.899 8.194 9.219 1.00101.16 C ANISOU 30 CB PRO A 22 15044 6076 17317 -610 -269 368 C ATOM 31 CG PRO A 22 2.692 8.124 7.950 1.00110.45 C ANISOU 31 CG PRO A 22 16240 7054 18671 -563 -173 -62 C ATOM 32 CD PRO A 22 1.831 7.397 6.952 1.00100.09 C ANISOU 32 CD PRO A 22 15059 5549 17421 -1006 -13 -361 C ATOM 33 N TRP A 23 -0.289 10.446 9.656 1.00104.60 N ANISOU 33 N TRP A 23 15113 7818 16813 -907 -517 494 N ATOM 34 CA TRP A 23 -0.706 11.839 9.549 1.00 90.78 C ANISOU 34 CA TRP A 23 13182 6653 14657 -858 -647 417 C ATOM 35 C TRP A 23 0.456 12.764 9.217 1.00119.22 C ANISOU 35 C TRP A 23 16696 10303 18299 -544 -749 227 C ATOM 36 O TRP A 23 0.220 13.902 8.797 1.00115.33 O ANISOU 36 O TRP A 23 16079 10204 17538 -534 -820 82 O ATOM 37 CB TRP A 23 -1.392 12.318 10.832 1.00 97.56 C ANISOU 37 CB TRP A 23 13976 7903 15192 -736 -793 800 C ATOM 38 CG TRP A 23 -0.501 12.401 12.035 1.00101.81 C ANISOU 38 CG TRP A 23 14523 8354 15807 -317 -941 1077 C ATOM 39 CD1 TRP A 23 -0.349 11.460 13.009 1.00109.02 C ANISOU 39 CD1 TRP A 23 15522 9009 16892 -210 -918 1428 C ATOM 40 CD2 TRP A 23 0.372 13.486 12.383 1.00113.31 C ANISOU 40 CD2 TRP A 23 15888 9997 17168 47 -1140 1025 C ATOM 41 NE1 TRP A 23 0.554 11.895 13.950 1.00114.50 N ANISOU 41 NE1 TRP A 23 16168 9769 17569 221 -1093 1593 N ATOM 42 CE2 TRP A 23 1.012 13.135 13.587 1.00113.10 C ANISOU 42 CE2 TRP A 23 15883 9855 17236 365 -1242 1333 C ATOM 43 CE3 TRP A 23 0.669 14.721 11.796 1.00111.52 C ANISOU 43 CE3 TRP A 23 15561 10020 16790 123 -1242 758 C ATOM 44 CZ2 TRP A 23 1.935 13.970 14.212 1.00105.57 C ANISOU 44 CZ2 TRP A 23 14843 9047 16223 736 -1461 1344 C ATOM 45 CZ3 TRP A 23 1.586 15.549 12.419 1.00115.63 C ANISOU 45 CZ3 TRP A 23 16016 10632 17287 468 -1455 784 C ATOM 46 CH2 TRP A 23 2.208 15.170 13.615 1.00106.46 C ANISOU 46 CH2 TRP A 23 14867 9371 16212 761 -1572 1057 C ATOM 47 N GLN A 24 1.699 12.306 9.391 1.00110.59 N ANISOU 47 N GLN A 24 15655 8829 17535 -289 -751 245 N ATOM 48 CA GLN A 24 2.847 13.163 9.109 1.00 99.98 C ANISOU 48 CA GLN A 24 14191 7552 16244 -15 -854 98 C ATOM 49 C GLN A 24 2.950 13.483 7.622 1.00 99.99 C ANISOU 49 C GLN A 24 14128 7601 16264 -171 -734 -286 C ATOM 50 O GLN A 24 3.159 14.641 7.245 1.00 97.88 O ANISOU 50 O GLN A 24 13716 7638 15836 -99 -822 -401 O ATOM 51 CB GLN A 24 4.140 12.517 9.610 1.00118.43 C ANISOU 51 CB GLN A 24 16568 9517 18913 297 -868 223 C ATOM 52 CG GLN A 24 4.302 12.492 11.124 1.00133.10 C ANISOU 52 CG GLN A 24 18427 11434 20711 559 -1030 605 C ATOM 53 CD GLN A 24 3.605 11.315 11.773 1.00145.27 C ANISOU 53 CD GLN A 24 20130 12739 22328 451 -917 886 C ATOM 54 OE1 GLN A 24 3.223 10.357 11.102 1.00141.83 O ANISOU 54 OE1 GLN A 24 19836 11971 22082 193 -718 781 O ATOM 55 NE2 GLN A 24 3.453 11.371 13.090 1.00150.25 N ANISOU 55 NE2 GLN A 24 20739 13535 22815 651 -1048 1247 N ATOM 56 N VAL A 25 2.807 12.471 6.757 1.00 91.58 N ANISOU 56 N VAL A 25 13171 6235 15389 -377 -535 -488 N ATOM 57 CA VAL A 25 2.884 12.733 5.320 1.00101.15 C ANISOU 57 CA VAL A 25 14308 7542 16583 -499 -415 -862 C ATOM 58 C VAL A 25 1.735 13.629 4.877 1.00115.37 C ANISOU 58 C VAL A 25 15998 9842 17997 -731 -430 -951 C ATOM 59 O VAL A 25 1.894 14.457 3.971 1.00112.43 O ANISOU 59 O VAL A 25 15485 9733 17501 -713 -408 -1155 O ATOM 60 CB VAL A 25 2.913 11.418 4.514 1.00 92.96 C ANISOU 60 CB VAL A 25 13434 6080 15806 -661 -212 -1099 C ATOM 61 CG1 VAL A 25 4.138 10.590 4.883 1.00106.69 C ANISOU 61 CG1 VAL A 25 15286 7335 17915 -358 -182 -1010 C ATOM 62 CG2 VAL A 25 1.635 10.621 4.716 1.00127.05 C ANISOU 62 CG2 VAL A 25 17893 10313 20066 -1035 -145 -1050 C ATOM 63 N ALA A 26 0.563 13.486 5.503 1.00114.21 N ANISOU 63 N ALA A 26 15896 9859 17639 -933 -457 -772 N ATOM 64 CA ALA A 26 -0.529 14.413 5.236 1.00105.67 C ANISOU 64 CA ALA A 26 14693 9313 16144 -1089 -484 -801 C ATOM 65 C ALA A 26 -0.151 15.823 5.664 1.00101.82 C ANISOU 65 C ALA A 26 14091 9133 15462 -800 -658 -694 C ATOM 66 O ALA A 26 -0.490 16.799 4.986 1.00 90.17 O ANISOU 66 O ALA A 26 12501 8021 13738 -819 -651 -825 O ATOM 67 CB ALA A 26 -1.796 13.952 5.954 1.00113.05 C ANISOU 67 CB ALA A 26 15675 10391 16889 -1326 -487 -574 C ATOM 68 N PHE A 27 0.556 15.946 6.788 1.00107.74 N ANISOU 68 N PHE A 27 14876 9736 16323 -526 -817 -460 N ATOM 69 CA PHE A 27 1.045 17.250 7.219 1.00 97.12 C ANISOU 69 CA PHE A 27 13444 8614 14843 -260 -1008 -397 C ATOM 70 C PHE A 27 2.072 17.802 6.236 1.00 86.14 C ANISOU 70 C PHE A 27 11946 7159 13623 -174 -978 -622 C ATOM 71 O PHE A 27 2.013 18.976 5.851 1.00 98.20 O ANISOU 71 O PHE A 27 13380 8962 14970 -129 -1034 -690 O ATOM 72 CB PHE A 27 1.646 17.143 8.620 1.00101.10 C ANISOU 72 CB PHE A 27 13996 8978 15439 8 -1193 -129 C ATOM 73 CG PHE A 27 2.163 18.443 9.146 1.00112.08 C ANISOU 73 CG PHE A 27 15314 10566 16703 262 -1423 -95 C ATOM 74 CD1 PHE A 27 1.298 19.387 9.674 1.00122.15 C ANISOU 74 CD1 PHE A 27 16598 12219 17596 316 -1552 -11 C ATOM 75 CD2 PHE A 27 3.512 18.738 9.083 1.00121.53 C ANISOU 75 CD2 PHE A 27 16435 11578 18161 443 -1513 -158 C ATOM 76 CE1 PHE A 27 1.773 20.591 10.151 1.00111.76 C ANISOU 76 CE1 PHE A 27 15252 11032 16179 543 -1777 -16 C ATOM 77 CE2 PHE A 27 3.990 19.938 9.551 1.00121.92 C ANISOU 77 CE2 PHE A 27 16422 11781 18120 628 -1741 -148 C ATOM 78 CZ PHE A 27 3.119 20.868 10.088 1.00121.71 C ANISOU 78 CZ PHE A 27 16442 12073 17731 675 -1878 -92 C ATOM 79 N ILE A 28 3.028 16.964 5.823 1.00100.11 N ANISOU 79 N ILE A 28 13727 8569 15742 -132 -881 -717 N ATOM 80 CA ILE A 28 4.069 17.411 4.901 1.00100.64 C ANISOU 80 CA ILE A 28 13660 8605 15976 -30 -839 -894 C ATOM 81 C ILE A 28 3.465 17.782 3.553 1.00106.96 C ANISOU 81 C ILE A 28 14378 9662 16600 -220 -677 -1136 C ATOM 82 O ILE A 28 3.809 18.814 2.964 1.00132.58 O ANISOU 82 O ILE A 28 17479 13117 19778 -153 -694 -1196 O ATOM 83 CB ILE A 28 5.147 16.321 4.745 1.00105.65 C ANISOU 83 CB ILE A 28 14327 8831 16983 91 -748 -936 C ATOM 84 CG1 ILE A 28 5.690 15.888 6.109 1.00110.89 C ANISOU 84 CG1 ILE A 28 15064 9276 17794 302 -895 -666 C ATOM 85 CG2 ILE A 28 6.271 16.805 3.838 1.00 80.57 C ANISOU 85 CG2 ILE A 28 10972 5683 13959 226 -708 -1077 C ATOM 86 CD1 ILE A 28 6.258 17.003 6.929 1.00114.64 C ANISOU 86 CD1 ILE A 28 15421 9941 18196 505 -1144 -514 C ATOM 87 N GLY A 29 2.552 16.949 3.045 1.00102.87 N ANISOU 87 N GLY A 29 13940 9142 16005 -467 -518 -1269 N ATOM 88 CA GLY A 29 2.025 17.162 1.706 1.00 88.54 C ANISOU 88 CA GLY A 29 12030 7594 14018 -637 -355 -1529 C ATOM 89 C GLY A 29 1.242 18.453 1.570 1.00 99.07 C ANISOU 89 C GLY A 29 13257 9408 14976 -658 -406 -1476 C ATOM 90 O GLY A 29 1.379 19.171 0.577 1.00117.88 O ANISOU 90 O GLY A 29 15497 12031 17261 -630 -326 -1605 O ATOM 91 N ILE A 30 0.417 18.771 2.567 1.00 88.13 N ANISOU 91 N ILE A 30 11939 8182 13366 -677 -531 -1267 N ATOM 92 CA ILE A 30 -0.447 19.943 2.461 1.00112.15 C ANISOU 92 CA ILE A 30 14909 11688 16014 -669 -567 -1215 C ATOM 93 C ILE A 30 0.352 21.229 2.619 1.00100.11 C ANISOU 93 C ILE A 30 13326 10195 14518 -414 -702 -1135 C ATOM 94 O ILE A 30 0.171 22.185 1.854 1.00108.76 O ANISOU 94 O ILE A 30 14321 11568 15436 -384 -647 -1193 O ATOM 95 CB ILE A 30 -1.594 19.854 3.483 1.00107.82 C ANISOU 95 CB ILE A 30 14445 11334 15188 -736 -652 -1010 C ATOM 96 CG1 ILE A 30 -2.522 18.700 3.117 1.00111.71 C ANISOU 96 CG1 ILE A 30 14956 11860 15628 -1065 -502 -1099 C ATOM 97 CG2 ILE A 30 -2.361 21.166 3.555 1.00105.60 C ANISOU 97 CG2 ILE A 30 14113 11517 14494 -627 -716 -923 C ATOM 98 CD1 ILE A 30 -3.552 18.410 4.154 1.00107.45 C ANISOU 98 CD1 ILE A 30 14474 11481 14871 -1156 -571 -853 C ATOM 99 N THR A 31 1.250 21.278 3.600 1.00 92.51 N ANISOU 99 N THR A 31 12418 8950 13781 -234 -882 -997 N ATOM 100 CA THR A 31 1.946 22.517 3.921 1.00 91.25 C ANISOU 100 CA THR A 31 12217 8806 13648 -31 -1055 -919 C ATOM 101 C THR A 31 3.133 22.808 3.011 1.00 87.02 C ANISOU 101 C THR A 31 11531 8141 13390 16 -992 -1021 C ATOM 102 O THR A 31 3.650 23.929 3.048 1.00101.68 O ANISOU 102 O THR A 31 13330 10032 15274 125 -1110 -967 O ATOM 103 CB THR A 31 2.419 22.490 5.378 1.00 93.12 C ANISOU 103 CB THR A 31 12548 8853 13982 142 -1298 -742 C ATOM 104 OG1 THR A 31 3.305 21.379 5.572 1.00 94.24 O ANISOU 104 OG1 THR A 31 12687 8654 14465 162 -1272 -736 O ATOM 105 CG2 THR A 31 1.231 22.370 6.324 1.00 87.72 C ANISOU 105 CG2 THR A 31 11986 8368 12974 142 -1368 -598 C ATOM 106 N THR A 32 3.573 21.848 2.195 1.00 94.86 N ANISOU 106 N THR A 32 12462 8994 14588 -60 -812 -1164 N ATOM 107 CA THR A 32 4.779 22.062 1.396 1.00121.28 C ANISOU 107 CA THR A 32 15639 12251 18192 23 -752 -1228 C ATOM 108 C THR A 32 4.566 23.136 0.336 1.00115.14 C ANISOU 108 C THR A 32 14719 11783 17246 1 -650 -1273 C ATOM 109 O THR A 32 5.398 24.036 0.178 1.00126.56 O ANISOU 109 O THR A 32 16040 13221 18826 95 -719 -1190 O ATOM 110 CB THR A 32 5.232 20.756 0.747 1.00 88.86 C ANISOU 110 CB THR A 32 11517 7946 14299 -6 -571 -1388 C ATOM 111 OG1 THR A 32 5.597 19.825 1.770 1.00118.50 O ANISOU 111 OG1 THR A 32 15403 11371 18251 60 -664 -1297 O ATOM 112 CG2 THR A 32 6.430 21.005 -0.158 1.00 82.34 C ANISOU 112 CG2 THR A 32 10483 7115 13687 111 -488 -1440 C ATOM 113 N GLY A 33 3.469 23.043 -0.417 1.00113.10 N ANISOU 113 N GLY A 33 14462 11812 16698 -128 -481 -1390 N ATOM 114 CA GLY A 33 3.156 24.093 -1.372 1.00105.31 C ANISOU 114 CA GLY A 33 13344 11165 15504 -116 -375 -1396 C ATOM 115 C GLY A 33 3.022 25.449 -0.709 1.00100.90 C ANISOU 115 C GLY A 33 12839 10667 14833 -13 -554 -1205 C ATOM 116 O GLY A 33 3.425 26.472 -1.268 1.00 75.74 O ANISOU 116 O GLY A 33 9539 7568 11671 56 -530 -1134 O ATOM 117 N LEU A 34 2.478 25.472 0.507 1.00 97.73 N ANISOU 117 N LEU A 34 12616 10203 14313 11 -736 -1114 N ATOM 118 CA LEU A 34 2.314 26.729 1.224 1.00 83.85 C ANISOU 118 CA LEU A 34 10952 8480 12426 140 -928 -970 C ATOM 119 C LEU A 34 3.663 27.269 1.697 1.00 89.49 C ANISOU 119 C LEU A 34 11628 8881 13492 232 -1123 -894 C ATOM 120 O LEU A 34 3.937 28.468 1.574 1.00 87.11 O ANISOU 120 O LEU A 34 11311 8580 13207 295 -1198 -821 O ATOM 121 CB LEU A 34 1.352 26.514 2.393 1.00 92.85 C ANISOU 121 CB LEU A 34 12278 9691 13308 171 -1064 -901 C ATOM 122 CG LEU A 34 0.770 27.714 3.132 1.00104.91 C ANISOU 122 CG LEU A 34 13947 11353 14563 336 -1236 -789 C ATOM 123 CD1 LEU A 34 -0.062 28.533 2.168 1.00110.35 C ANISOU 123 CD1 LEU A 34 14593 12395 14941 351 -1064 -791 C ATOM 124 CD2 LEU A 34 -0.082 27.242 4.300 1.00106.11 C ANISOU 124 CD2 LEU A 34 14244 11601 14472 382 -1353 -711 C ATOM 125 N LEU A 35 4.525 26.397 2.227 1.00106.12 N ANISOU 125 N LEU A 35 13714 10720 15887 237 -1204 -903 N ATOM 126 CA LEU A 35 5.855 26.830 2.644 1.00 96.42 C ANISOU 126 CA LEU A 35 12401 9247 14987 309 -1390 -834 C ATOM 127 C LEU A 35 6.748 27.151 1.452 1.00104.37 C ANISOU 127 C LEU A 35 13171 10268 16215 271 -1243 -839 C ATOM 128 O LEU A 35 7.621 28.023 1.552 1.00108.44 O ANISOU 128 O LEU A 35 13591 10679 16933 289 -1382 -749 O ATOM 129 CB LEU A 35 6.510 25.761 3.515 1.00101.78 C ANISOU 129 CB LEU A 35 13100 9692 15878 361 -1497 -818 C ATOM 130 CG LEU A 35 5.855 25.514 4.872 1.00110.87 C ANISOU 130 CG LEU A 35 14453 10824 16850 436 -1680 -753 C ATOM 131 CD1 LEU A 35 6.519 24.345 5.574 1.00 91.57 C ANISOU 131 CD1 LEU A 35 12007 8161 14624 503 -1729 -709 C ATOM 132 CD2 LEU A 35 5.917 26.765 5.729 1.00110.15 C ANISOU 132 CD2 LEU A 35 14442 10739 16670 540 -1960 -693 C ATOM 133 N SER A 36 6.565 26.449 0.332 1.00 86.40 N ANISOU 133 N SER A 36 10790 8133 13906 216 -970 -943 N ATOM 134 CA SER A 36 7.318 26.768 -0.877 1.00 94.27 C ANISOU 134 CA SER A 36 11541 9225 15053 213 -803 -933 C ATOM 135 C SER A 36 7.052 28.200 -1.323 1.00107.73 C ANISOU 135 C SER A 36 13205 11088 16638 207 -798 -818 C ATOM 136 O SER A 36 7.981 28.935 -1.677 1.00 88.24 O ANISOU 136 O SER A 36 10563 8569 14396 210 -824 -695 O ATOM 137 CB SER A 36 6.964 25.784 -1.991 1.00 96.61 C ANISOU 137 CB SER A 36 11762 9697 15250 181 -516 -1106 C ATOM 138 OG SER A 36 7.638 26.110 -3.193 1.00104.43 O ANISOU 138 OG SER A 36 12497 10849 16334 217 -341 -1086 O ATOM 139 N LEU A 37 5.781 28.613 -1.312 1.00102.04 N ANISOU 139 N LEU A 37 12638 10567 15564 203 -759 -835 N ATOM 140 CA LEU A 37 5.447 29.981 -1.691 1.00 91.77 C ANISOU 140 CA LEU A 37 11341 9398 14129 238 -744 -710 C ATOM 141 C LEU A 37 6.010 30.984 -0.692 1.00 88.46 C ANISOU 141 C LEU A 37 11030 8689 13891 269 -1040 -591 C ATOM 142 O LEU A 37 6.518 32.041 -1.085 1.00 94.02 O ANISOU 142 O LEU A 37 11653 9332 14738 260 -1054 -459 O ATOM 143 CB LEU A 37 3.932 30.138 -1.816 1.00101.89 C ANISOU 143 CB LEU A 37 12765 10990 14957 266 -640 -750 C ATOM 144 CG LEU A 37 3.446 31.521 -2.258 1.00104.86 C ANISOU 144 CG LEU A 37 13169 11530 15141 353 -588 -609 C ATOM 145 CD1 LEU A 37 3.987 31.863 -3.639 1.00102.40 C ANISOU 145 CD1 LEU A 37 12594 11378 14934 346 -350 -532 C ATOM 146 CD2 LEU A 37 1.927 31.590 -2.244 1.00 83.49 C ANISOU 146 CD2 LEU A 37 10598 9175 11950 415 -502 -640 C ATOM 147 N ALA A 38 5.933 30.671 0.604 1.00 81.06 N ANISOU 147 N ALA A 38 10276 7573 12952 301 -1283 -634 N ATOM 148 CA ALA A 38 6.510 31.552 1.613 1.00 90.71 C ANISOU 148 CA ALA A 38 11602 8528 14337 334 -1597 -571 C ATOM 149 C ALA A 38 8.024 31.641 1.482 1.00 95.04 C ANISOU 149 C ALA A 38 11922 8868 15322 253 -1683 -507 C ATOM 150 O ALA A 38 8.604 32.708 1.718 1.00 92.36 O ANISOU 150 O ALA A 38 11579 8352 15162 212 -1864 -427 O ATOM 151 CB ALA A 38 6.130 31.072 3.013 1.00 87.97 C ANISOU 151 CB ALA A 38 11462 8100 13863 418 -1827 -633 C ATOM 152 N THR A 39 8.679 30.541 1.106 1.00 98.97 N ANISOU 152 N THR A 39 12227 9385 15993 229 -1560 -539 N ATOM 153 CA THR A 39 10.130 30.557 0.951 1.00 85.43 C ANISOU 153 CA THR A 39 10254 7542 14664 177 -1624 -456 C ATOM 154 C THR A 39 10.551 31.423 -0.231 1.00 97.44 C ANISOU 154 C THR A 39 11557 9159 16306 100 -1462 -320 C ATOM 155 O THR A 39 11.473 32.239 -0.116 1.00100.74 O ANISOU 155 O THR A 39 11843 9433 16999 12 -1616 -192 O ATOM 156 CB THR A 39 10.660 29.131 0.788 1.00 96.26 C ANISOU 156 CB THR A 39 11492 8932 16151 228 -1501 -521 C ATOM 157 OG1 THR A 39 10.383 28.372 1.972 1.00 93.29 O ANISOU 157 OG1 THR A 39 11307 8434 15705 301 -1663 -592 O ATOM 158 CG2 THR A 39 12.161 29.143 0.538 1.00 75.13 C ANISOU 158 CG2 THR A 39 8508 6201 13837 209 -1540 -412 C ATOM 159 N VAL A 40 9.880 31.271 -1.376 1.00 99.14 N ANISOU 159 N VAL A 40 11718 9635 16316 126 -1154 -334 N ATOM 160 CA VAL A 40 10.315 31.981 -2.576 1.00113.24 C ANISOU 160 CA VAL A 40 13257 11566 18202 87 -962 -172 C ATOM 161 C VAL A 40 10.002 33.471 -2.471 1.00116.43 C ANISOU 161 C VAL A 40 13783 11867 18588 41 -1063 -26 C ATOM 162 O VAL A 40 10.828 34.313 -2.840 1.00128.84 O ANISOU 162 O VAL A 40 15176 13351 20427 -52 -1085 168 O ATOM 163 CB VAL A 40 9.697 31.350 -3.839 1.00105.94 C ANISOU 163 CB VAL A 40 12223 10997 17030 157 -606 -246 C ATOM 164 CG1 VAL A 40 10.163 29.905 -3.990 1.00110.40 C ANISOU 164 CG1 VAL A 40 12680 11596 17672 207 -515 -401 C ATOM 165 CG2 VAL A 40 8.179 31.423 -3.809 1.00106.04 C ANISOU 165 CG2 VAL A 40 12486 11178 16628 198 -533 -352 C ATOM 166 N THR A 41 8.822 33.826 -1.956 1.00101.63 N ANISOU 166 N THR A 41 12217 9994 16404 109 -1124 -103 N ATOM 167 CA THR A 41 8.463 35.238 -1.852 1.00110.08 C ANISOU 167 CA THR A 41 13452 10939 17433 113 -1210 21 C ATOM 168 C THR A 41 9.339 35.951 -0.831 1.00108.01 C ANISOU 168 C THR A 41 13264 10280 17495 11 -1568 52 C ATOM 169 O THR A 41 9.850 37.045 -1.093 1.00110.52 O ANISOU 169 O THR A 41 13534 10419 18041 -87 -1620 219 O ATOM 170 CB THR A 41 6.983 35.390 -1.492 1.00 92.61 C ANISOU 170 CB THR A 41 11548 8864 14774 258 -1193 -74 C ATOM 171 OG1 THR A 41 6.718 34.724 -0.251 1.00112.36 O ANISOU 171 OG1 THR A 41 14242 11264 17186 296 -1420 -242 O ATOM 172 CG2 THR A 41 6.104 34.803 -2.583 1.00 79.98 C ANISOU 172 CG2 THR A 41 9844 7698 12846 326 -845 -103 C ATOM 173 N GLY A 42 9.526 35.339 0.340 1.00 95.03 N ANISOU 173 N GLY A 42 11729 8499 15878 25 -1823 -102 N ATOM 174 CA GLY A 42 10.393 35.929 1.346 1.00 97.02 C ANISOU 174 CA GLY A 42 12025 8424 16415 -71 -2186 -110 C ATOM 175 C GLY A 42 11.830 36.058 0.881 1.00107.82 C ANISOU 175 C GLY A 42 13036 9711 18218 -257 -2203 40 C ATOM 176 O GLY A 42 12.507 37.039 1.194 1.00118.90 O ANISOU 176 O GLY A 42 14425 10858 19893 -409 -2427 115 O ATOM 177 N ASN A 43 12.317 35.077 0.120 1.00107.09 N ANISOU 177 N ASN A 43 12648 9845 18196 -248 -1970 85 N ATOM 178 CA ASN A 43 13.674 35.185 -0.395 1.00112.22 C ANISOU 178 CA ASN A 43 12918 10494 19225 -394 -1958 261 C ATOM 179 C ASN A 43 13.764 36.037 -1.652 1.00103.51 C ANISOU 179 C ASN A 43 11635 9487 18206 -475 -1716 499 C ATOM 180 O ASN A 43 14.851 36.522 -1.970 1.00109.52 O ANISOU 180 O ASN A 43 12107 10198 19309 -641 -1757 700 O ATOM 181 CB ASN A 43 14.275 33.806 -0.666 1.00109.37 C ANISOU 181 CB ASN A 43 12307 10338 18910 -306 -1816 221 C ATOM 182 CG ASN A 43 14.571 33.037 0.611 1.00102.48 C ANISOU 182 CG ASN A 43 11530 9343 18063 -245 -2079 69 C ATOM 183 OD1 ASN A 43 14.006 31.969 0.851 1.00152.63 O ANISOU 183 OD1 ASN A 43 18014 15769 24208 -94 -1993 -75 O ATOM 184 ND2 ASN A 43 15.458 33.576 1.436 1.00121.04 N ANISOU 184 ND2 ASN A 43 13806 11513 20669 -367 -2401 109 N ATOM 185 N LEU A 44 12.673 36.212 -2.397 1.00111.35 N ANISOU 185 N LEU A 44 12760 10656 18893 -358 -1455 508 N ATOM 186 CA LEU A 44 12.723 37.212 -3.456 1.00109.91 C ANISOU 186 CA LEU A 44 12440 10535 18786 -417 -1256 771 C ATOM 187 C LEU A 44 12.754 38.619 -2.882 1.00111.22 C ANISOU 187 C LEU A 44 12820 10311 19127 -552 -1503 867 C ATOM 188 O LEU A 44 13.324 39.523 -3.502 1.00125.50 O ANISOU 188 O LEU A 44 14456 12033 21196 -696 -1442 1138 O ATOM 189 CB LEU A 44 11.549 37.051 -4.421 1.00 96.45 C ANISOU 189 CB LEU A 44 10797 9170 16679 -233 -910 762 C ATOM 190 CG LEU A 44 11.673 35.889 -5.406 1.00 91.88 C ANISOU 190 CG LEU A 44 9933 8997 15981 -129 -607 717 C ATOM 191 CD1 LEU A 44 10.400 35.729 -6.216 1.00 89.21 C ANISOU 191 CD1 LEU A 44 9684 9010 15202 37 -316 651 C ATOM 192 CD2 LEU A 44 12.872 36.109 -6.320 1.00 90.49 C ANISOU 192 CD2 LEU A 44 9327 8945 16108 -207 -467 987 C ATOM 193 N LEU A 45 12.170 38.820 -1.697 1.00 98.43 N ANISOU 193 N LEU A 45 11576 8448 17374 -504 -1783 655 N ATOM 194 CA LEU A 45 12.177 40.143 -1.080 1.00120.06 C ANISOU 194 CA LEU A 45 14572 10779 20267 -608 -2046 688 C ATOM 195 C LEU A 45 13.597 40.597 -0.759 1.00134.70 C ANISOU 195 C LEU A 45 16199 12362 22619 -902 -2303 792 C ATOM 196 O LEU A 45 14.003 41.702 -1.134 1.00147.41 O ANISOU 196 O LEU A 45 17769 13735 24504 -1084 -2324 1007 O ATOM 197 CB LEU A 45 11.308 40.147 0.177 1.00108.77 C ANISOU 197 CB LEU A 45 13572 9201 18555 -453 -2307 409 C ATOM 198 CG LEU A 45 9.802 40.027 -0.055 1.00102.68 C ANISOU 198 CG LEU A 45 13061 8669 17283 -182 -2092 343 C ATOM 199 CD1 LEU A 45 9.057 39.926 1.265 1.00112.15 C ANISOU 199 CD1 LEU A 45 14629 9775 18205 -20 -2362 89 C ATOM 200 CD2 LEU A 45 9.303 41.204 -0.869 1.00114.72 C ANISOU 200 CD2 LEU A 45 14692 10136 18760 -137 -1905 553 C ATOM 201 N VAL A 46 14.370 39.755 -0.066 1.00119.77 N ANISOU 201 N VAL A 46 14144 10511 20854 -957 -2499 661 N ATOM 202 CA VAL A 46 15.752 40.111 0.253 1.00118.45 C ANISOU 202 CA VAL A 46 13705 10163 21136 -1242 -2752 759 C ATOM 203 C VAL A 46 16.546 40.378 -1.022 1.00120.91 C ANISOU 203 C VAL A 46 13588 10628 21723 -1403 -2488 1113 C ATOM 204 O VAL A 46 17.372 41.297 -1.074 1.00128.98 O ANISOU 204 O VAL A 46 14460 11422 23126 -1691 -2634 1303 O ATOM 205 CB VAL A 46 16.412 39.017 1.116 1.00116.13 C ANISOU 205 CB VAL A 46 13265 9988 20871 -1208 -2952 585 C ATOM 206 CG1 VAL A 46 15.767 38.941 2.485 1.00108.17 C ANISOU 206 CG1 VAL A 46 12653 8811 19634 -1075 -3262 279 C ATOM 207 CG2 VAL A 46 16.279 37.690 0.451 1.00137.76 C ANISOU 207 CG2 VAL A 46 15809 13116 23418 -1003 -2625 593 C ATOM 208 N LEU A 47 16.304 39.588 -2.073 1.00105.68 N ANISOU 208 N LEU A 47 11453 9098 19604 -1226 -2100 1209 N ATOM 209 CA LEU A 47 16.982 39.814 -3.347 1.00118.69 C ANISOU 209 CA LEU A 47 12679 10966 21449 -1319 -1816 1559 C ATOM 210 C LEU A 47 16.630 41.178 -3.932 1.00126.98 C ANISOU 210 C LEU A 47 13839 11813 22593 -1427 -1720 1812 C ATOM 211 O LEU A 47 17.520 41.973 -4.256 1.00112.15 O ANISOU 211 O LEU A 47 11712 9800 21100 -1693 -1762 2106 O ATOM 212 CB LEU A 47 16.635 38.701 -4.337 1.00126.72 C ANISOU 212 CB LEU A 47 13512 12463 22173 -1056 -1424 1549 C ATOM 213 CG LEU A 47 17.542 37.470 -4.438 1.00125.92 C ANISOU 213 CG LEU A 47 13059 12646 22139 -986 -1374 1512 C ATOM 214 CD1 LEU A 47 18.896 37.878 -4.980 1.00142.15 C ANISOU 214 CD1 LEU A 47 14628 14802 24578 -1187 -1356 1854 C ATOM 215 CD2 LEU A 47 17.702 36.759 -3.110 1.00113.97 C ANISOU 215 CD2 LEU A 47 11713 10967 20622 -962 -1691 1226 C ATOM 216 N ILE A 48 15.335 41.469 -4.078 1.00124.27 N ANISOU 216 N ILE A 48 13860 11452 21904 -1221 -1583 1726 N ATOM 217 CA ILE A 48 14.940 42.702 -4.754 1.00142.22 C ANISOU 217 CA ILE A 48 16238 13574 24228 -1255 -1430 2001 C ATOM 218 C ILE A 48 15.173 43.912 -3.854 1.00151.92 C ANISOU 218 C ILE A 48 17754 14208 25762 -1492 -1798 1990 C ATOM 219 O ILE A 48 15.576 44.981 -4.328 1.00152.86 O ANISOU 219 O ILE A 48 17803 14085 26191 -1692 -1764 2302 O ATOM 220 CB ILE A 48 13.479 42.614 -5.238 1.00142.78 C ANISOU 220 CB ILE A 48 16576 13877 23796 -927 -1152 1928 C ATOM 221 CG1 ILE A 48 12.511 42.448 -4.064 1.00144.42 C ANISOU 221 CG1 ILE A 48 17261 13908 23706 -776 -1393 1556 C ATOM 222 CG2 ILE A 48 13.315 41.475 -6.235 1.00139.90 C ANISOU 222 CG2 ILE A 48 15901 14095 23158 -733 -792 1932 C ATOM 223 CD1 ILE A 48 11.058 42.577 -4.451 1.00142.51 C ANISOU 223 CD1 ILE A 48 17291 13874 22980 -478 -1157 1518 C ATOM 224 N SER A 49 14.939 43.768 -2.546 1.00135.35 N ANISOU 224 N SER A 49 15983 11858 23586 -1475 -2159 1632 N ATOM 225 CA SER A 49 15.197 44.870 -1.627 1.00111.21 C ANISOU 225 CA SER A 49 13212 8236 20805 -1691 -2547 1553 C ATOM 226 C SER A 49 16.677 45.211 -1.557 1.00107.54 C ANISOU 226 C SER A 49 12381 7595 20884 -2106 -2756 1727 C ATOM 227 O SER A 49 17.029 46.351 -1.234 1.00132.64 O ANISOU 227 O SER A 49 15707 10293 24397 -2373 -2993 1791 O ATOM 228 CB SER A 49 14.674 44.534 -0.230 1.00109.19 C ANISOU 228 CB SER A 49 13339 7841 20307 -1545 -2890 1121 C ATOM 229 OG SER A 49 15.411 43.474 0.350 1.00131.80 O ANISOU 229 OG SER A 49 15946 10908 23223 -1598 -3053 963 O ATOM 230 N PHE A 50 17.545 44.246 -1.857 1.00114.38 N ANISOU 230 N PHE A 50 12773 8843 21843 -2163 -2674 1806 N ATOM 231 CA PHE A 50 18.974 44.517 -1.891 1.00123.96 C ANISOU 231 CA PHE A 50 13561 9995 23545 -2547 -2836 2020 C ATOM 232 C PHE A 50 19.338 45.378 -3.093 1.00136.45 C ANISOU 232 C PHE A 50 14883 11555 25408 -2736 -2566 2500 C ATOM 233 O PHE A 50 20.267 46.190 -3.018 1.00150.46 O ANISOU 233 O PHE A 50 16473 13051 27644 -3133 -2758 2706 O ATOM 234 CB PHE A 50 19.743 43.198 -1.918 1.00131.29 C ANISOU 234 CB PHE A 50 14057 11390 24439 -2478 -2787 1988 C ATOM 235 CG PHE A 50 21.214 43.346 -1.687 1.00140.31 C ANISOU 235 CG PHE A 50 14759 12527 26027 -2842 -3022 2148 C ATOM 236 CD1 PHE A 50 21.707 43.511 -0.404 1.00130.99 C ANISOU 236 CD1 PHE A 50 13679 11082 25008 -3038 -3496 1889 C ATOM 237 CD2 PHE A 50 22.104 43.321 -2.746 1.00154.91 C ANISOU 237 CD2 PHE A 50 16068 14683 28109 -2979 -2773 2560 C ATOM 238 CE1 PHE A 50 23.056 43.643 -0.180 1.00152.55 C ANISOU 238 CE1 PHE A 50 15974 13858 28129 -3387 -3725 2031 C ATOM 239 CE2 PHE A 50 23.457 43.456 -2.527 1.00171.47 C ANISOU 239 CE2 PHE A 50 17722 16827 30601 -3320 -2991 2730 C ATOM 240 CZ PHE A 50 23.931 43.617 -1.241 1.00173.34 C ANISOU 240 CZ PHE A 50 18059 16801 31001 -3538 -3472 2461 C ATOM 241 N LYS A 51 18.613 45.219 -4.203 1.00137.46 N ANISOU 241 N LYS A 51 14980 11990 25259 -2465 -2124 2691 N ATOM 242 CA LYS A 51 18.859 46.026 -5.394 1.00150.77 C ANISOU 242 CA LYS A 51 16421 13706 27157 -2584 -1826 3182 C ATOM 243 C LYS A 51 18.179 47.387 -5.301 1.00152.57 C ANISOU 243 C LYS A 51 17101 13394 27473 -2644 -1879 3268 C ATOM 244 O LYS A 51 18.736 48.394 -5.752 1.00155.59 O ANISOU 244 O LYS A 51 17352 13508 28259 -2936 -1855 3647 O ATOM 245 CB LYS A 51 18.383 45.277 -6.640 1.00125.42 C ANISOU 245 CB LYS A 51 12969 11105 23581 -2237 -1331 3344 C ATOM 246 N VAL A 52 16.978 47.435 -4.718 1.00139.52 N ANISOU 246 N VAL A 52 15984 11578 25451 -2363 -1945 2937 N ATOM 247 CA VAL A 52 16.242 48.692 -4.622 1.00126.55 C ANISOU 247 CA VAL A 52 14814 9435 23832 -2336 -1977 2997 C ATOM 248 C VAL A 52 16.905 49.635 -3.624 1.00133.08 C ANISOU 248 C VAL A 52 15856 9586 25121 -2726 -2448 2887 C ATOM 249 O VAL A 52 17.070 50.830 -3.897 1.00143.79 O ANISOU 249 O VAL A 52 17335 10481 26819 -2941 -2457 3158 O ATOM 250 CB VAL A 52 14.772 48.418 -4.255 1.00109.27 C ANISOU 250 CB VAL A 52 13106 7337 21073 -1891 -1916 2673 C ATOM 251 CG1 VAL A 52 14.051 49.720 -3.948 1.00165.87 C ANISOU 251 CG1 VAL A 52 20816 13949 28258 -1827 -2012 2680 C ATOM 252 CG2 VAL A 52 14.076 47.697 -5.392 1.00105.73 C ANISOU 252 CG2 VAL A 52 12448 7525 20199 -1552 -1435 2823 C ATOM 253 N ASN A 53 17.295 49.121 -2.461 1.00140.80 N ANISOU 253 N ASN A 53 16885 10492 26121 -2825 -2847 2490 N ATOM 254 CA ASN A 53 17.854 49.931 -1.385 1.00121.87 C ANISOU 254 CA ASN A 53 14718 7643 23944 -3105 -3294 2246 C ATOM 255 C ASN A 53 19.374 49.822 -1.400 1.00125.61 C ANISOU 255 C ASN A 53 14656 8256 24816 -3524 -3438 2401 C ATOM 256 O ASN A 53 19.923 48.724 -1.264 1.00153.40 O ANISOU 256 O ASN A 53 17797 12122 28368 -3549 -3491 2350 O ATOM 257 CB ASN A 53 17.295 49.484 -0.034 1.00125.82 C ANISOU 257 CB ASN A 53 15609 8110 24086 -2876 -3623 1695 C ATOM 258 CG ASN A 53 17.690 50.409 1.101 1.00124.81 C ANISOU 258 CG ASN A 53 15779 7641 24001 -3048 -4023 1387 C ATOM 259 OD1 ASN A 53 18.405 51.390 0.904 1.00151.03 O ANISOU 259 OD1 ASN A 53 19034 10711 27640 -3369 -4072 1560 O ATOM 260 ND2 ASN A 53 17.223 50.094 2.304 1.00139.93 N ANISOU 260 ND2 ASN A 53 18016 9557 25594 -2832 -4306 935 N ATOM 261 N THR A 54 20.049 50.962 -1.555 1.00141.10 N ANISOU 261 N THR A 54 16588 9949 27073 -3845 -3499 2595 N ATOM 262 CA THR A 54 21.507 50.978 -1.532 1.00161.96 C ANISOU 262 CA THR A 54 18731 12726 30080 -4257 -3654 2753 C ATOM 263 C THR A 54 22.073 50.944 -0.118 1.00160.66 C ANISOU 263 C THR A 54 18682 12461 29901 -4402 -4142 2299 C ATOM 264 O THR A 54 23.260 50.645 0.050 1.00161.89 O ANISOU 264 O THR A 54 18387 12835 30290 -4685 -4300 2371 O ATOM 265 CB THR A 54 22.041 52.214 -2.261 1.00170.63 C ANISOU 265 CB THR A 54 19736 13583 31513 -4568 -3527 3159 C ATOM 266 OG1 THR A 54 21.611 53.399 -1.581 1.00166.74 O ANISOU 266 OG1 THR A 54 19825 12543 30984 -4608 -3731 2905 O ATOM 267 CG2 THR A 54 21.535 52.247 -3.697 1.00172.36 C ANISOU 267 CG2 THR A 54 19787 13963 31739 -4403 -3024 3663 C ATOM 268 N GLU A 55 21.260 51.242 0.898 1.00146.11 N ANISOU 268 N GLU A 55 17409 10337 27769 -4195 -4373 1851 N ATOM 269 CA GLU A 55 21.737 51.216 2.275 1.00138.81 C ANISOU 269 CA GLU A 55 16597 9349 26796 -4292 -4829 1417 C ATOM 270 C GLU A 55 21.812 49.807 2.848 1.00151.44 C ANISOU 270 C GLU A 55 17988 11353 28198 -4097 -4948 1200 C ATOM 271 O GLU A 55 22.588 49.575 3.782 1.00136.05 O ANISOU 271 O GLU A 55 15901 9494 26300 -4241 -5292 973 O ATOM 272 CB GLU A 55 20.849 52.095 3.158 1.00140.04 C ANISOU 272 CB GLU A 55 17425 9084 26701 -4114 -5022 1033 C ATOM 273 CG GLU A 55 20.983 53.586 2.863 1.00169.53 C ANISOU 273 CG GLU A 55 21394 12339 30682 -4367 -4998 1174 C ATOM 274 CD GLU A 55 20.104 54.445 3.752 1.00174.88 C ANISOU 274 CD GLU A 55 22740 12602 31105 -4158 -5179 781 C ATOM 275 OE1 GLU A 55 19.283 53.879 4.503 1.00187.48 O ANISOU 275 OE1 GLU A 55 24612 14325 32298 -3781 -5284 439 O ATOM 276 OE2 GLU A 55 20.237 55.686 3.704 1.00193.01 O ANISOU 276 OE2 GLU A 55 25283 14447 33604 -4365 -5211 820 O ATOM 277 N LEU A 56 21.032 48.864 2.316 1.00150.63 N ANISOU 277 N LEU A 56 17860 11493 27878 -3775 -4671 1267 N ATOM 278 CA LEU A 56 21.162 47.465 2.710 1.00140.17 C ANISOU 278 CA LEU A 56 16296 10542 26419 -3610 -4736 1117 C ATOM 279 C LEU A 56 22.454 46.830 2.222 1.00130.65 C ANISOU 279 C LEU A 56 14416 9686 25539 -3870 -4692 1404 C ATOM 280 O LEU A 56 22.707 45.663 2.541 1.00145.95 O ANISOU 280 O LEU A 56 16108 11937 27410 -3752 -4750 1301 O ATOM 281 CB LEU A 56 19.972 46.656 2.190 1.00125.47 C ANISOU 281 CB LEU A 56 14590 8821 24262 -3224 -4427 1122 C ATOM 282 CG LEU A 56 18.622 46.885 2.862 1.00133.91 C ANISOU 282 CG LEU A 56 16285 9699 24896 -2867 -4490 787 C ATOM 283 CD1 LEU A 56 17.524 46.192 2.076 1.00133.37 C ANISOU 283 CD1 LEU A 56 16298 9854 24524 -2516 -4095 886 C ATOM 284 CD2 LEU A 56 18.668 46.358 4.288 1.00130.67 C ANISOU 284 CD2 LEU A 56 16024 9360 24264 -2741 -4871 362 C ATOM 285 N LYS A 57 23.276 47.561 1.473 1.00134.50 N ANISOU 285 N LYS A 57 14594 10146 26365 -4202 -4586 1771 N ATOM 286 CA LYS A 57 24.471 47.000 0.846 1.00148.47 C ANISOU 286 CA LYS A 57 15681 12318 28411 -4415 -4479 2116 C ATOM 287 C LYS A 57 25.669 47.056 1.797 1.00148.62 C ANISOU 287 C LYS A 57 15470 12423 28576 -4689 -4877 1967 C ATOM 288 O LYS A 57 26.705 47.648 1.503 1.00157.41 O ANISOU 288 O LYS A 57 16250 13581 29978 -5043 -4912 2227 O ATOM 289 CB LYS A 57 24.764 47.736 -0.457 1.00157.70 C ANISOU 289 CB LYS A 57 16597 13482 29839 -4613 -4146 2628 C ATOM 290 CG LYS A 57 23.699 47.547 -1.525 1.00161.05 C ANISOU 290 CG LYS A 57 17127 13938 30127 -4334 -3709 2844 C ATOM 291 CD LYS A 57 24.024 48.344 -2.780 1.00178.90 C ANISOU 291 CD LYS A 57 19124 16217 32634 -4516 -3384 3382 C ATOM 292 CE LYS A 57 22.926 48.207 -3.823 1.00184.73 C ANISOU 292 CE LYS A 57 19970 17007 33212 -4218 -2943 3606 C ATOM 293 NZ LYS A 57 23.200 49.028 -5.036 1.00191.92 N ANISOU 293 NZ LYS A 57 20632 17956 34333 -4356 -2611 4160 N ATOM 294 N THR A 58 25.510 46.422 2.957 1.00128.88 N ANISOU 294 N THR A 58 17712 9192 22064 -1897 -4572 747 N ATOM 295 CA THR A 58 26.591 46.274 3.920 1.00113.59 C ANISOU 295 CA THR A 58 15568 7363 20228 -2027 -4478 595 C ATOM 296 C THR A 58 27.157 44.864 3.827 1.00126.41 C ANISOU 296 C THR A 58 16946 9353 21731 -2174 -4095 670 C ATOM 297 O THR A 58 26.431 43.909 3.539 1.00125.67 O ANISOU 297 O THR A 58 16790 9425 21535 -2014 -3948 675 O ATOM 298 CB THR A 58 26.111 46.537 5.349 1.00113.74 C ANISOU 298 CB THR A 58 15478 7329 20410 -1642 -4692 147 C ATOM 299 OG1 THR A 58 25.280 45.454 5.788 1.00106.89 O ANISOU 299 OG1 THR A 58 14437 6691 19485 -1327 -4563 -57 O ATOM 300 CG2 THR A 58 25.308 47.828 5.404 1.00120.00 C ANISOU 300 CG2 THR A 58 16502 7790 21303 -1417 -5090 38 C ATOM 301 N VAL A 59 28.463 44.741 4.093 1.00137.88 N ANISOU 301 N VAL A 59 18249 10937 23203 -2476 -3944 714 N ATOM 302 CA VAL A 59 29.161 43.467 3.901 1.00122.80 C ANISOU 302 CA VAL A 59 16102 9388 21169 -2658 -3587 812 C ATOM 303 C VAL A 59 28.441 42.333 4.620 1.00118.32 C ANISOU 303 C VAL A 59 15337 9043 20575 -2305 -3458 558 C ATOM 304 O VAL A 59 28.382 41.200 4.124 1.00114.06 O ANISOU 304 O VAL A 59 14671 8863 19801 -2293 -3145 666 O ATOM 305 CB VAL A 59 30.629 43.584 4.356 1.00129.82 C ANISOU 305 CB VAL A 59 16823 10399 22104 -2965 -3490 797 C ATOM 306 CG1 VAL A 59 31.314 42.224 4.313 1.00112.76 C ANISOU 306 CG1 VAL A 59 14380 8638 19825 -3093 -3145 836 C ATOM 307 CG2 VAL A 59 31.374 44.570 3.474 1.00134.70 C ANISOU 307 CG2 VAL A 59 17617 10881 22681 -3351 -3544 1095 C ATOM 308 N ASN A 60 27.867 42.619 5.792 1.00119.01 N ANISOU 308 N ASN A 60 15376 9058 20785 -1953 -3640 202 N ATOM 309 CA ASN A 60 27.125 41.592 6.516 1.00106.84 C ANISOU 309 CA ASN A 60 13629 7879 19086 -1566 -3457 -37 C ATOM 310 C ASN A 60 25.949 41.075 5.694 1.00106.33 C ANISOU 310 C ASN A 60 13656 7873 18872 -1405 -3390 79 C ATOM 311 O ASN A 60 25.675 39.870 5.680 1.00108.90 O ANISOU 311 O ASN A 60 13813 8570 18994 -1288 -3099 74 O ATOM 312 CB ASN A 60 26.643 42.134 7.862 1.00 98.59 C ANISOU 312 CB ASN A 60 12523 6750 18186 -1216 -3701 -433 C ATOM 313 CG ASN A 60 27.771 42.313 8.855 1.00115.51 C ANISOU 313 CG ASN A 60 14493 8972 20423 -1304 -3695 -609 C ATOM 314 OD1 ASN A 60 28.699 41.507 8.907 1.00138.80 O ANISOU 314 OD1 ASN A 60 17256 12239 23244 -1472 -3401 -532 O ATOM 315 ND2 ASN A 60 27.683 43.356 9.668 1.00144.29 N ANISOU 315 ND2 ASN A 60 18191 12342 24291 -1166 -4033 -875 N ATOM 316 N ASN A 61 25.250 41.970 4.991 1.00113.87 N ANISOU 316 N ASN A 61 14882 8455 19928 -1399 -3668 184 N ATOM 317 CA ASN A 61 24.083 41.568 4.217 1.00103.69 C ANISOU 317 CA ASN A 61 13679 7214 18502 -1225 -3637 267 C ATOM 318 C ASN A 61 24.449 40.882 2.906 1.00118.76 C ANISOU 318 C ASN A 61 15614 9284 20226 -1510 -3376 624 C ATOM 319 O ASN A 61 23.634 40.116 2.380 1.00123.17 O ANISOU 319 O ASN A 61 16143 10037 20618 -1363 -3234 660 O ATOM 320 CB ASN A 61 23.187 42.775 3.927 1.00102.04 C ANISOU 320 CB ASN A 61 13758 6557 18456 -1080 -4050 237 C ATOM 321 CG ASN A 61 22.685 43.447 5.191 1.00116.45 C ANISOU 321 CG ASN A 61 15549 8246 20450 -737 -4337 -162 C ATOM 322 OD1 ASN A 61 22.829 44.657 5.365 1.00132.29 O ANISOU 322 OD1 ASN A 61 17702 10009 22552 -739 -4611 -209 O ATOM 323 ND2 ASN A 61 22.144 42.652 6.108 1.00117.28 N ANISOU 323 ND2 ASN A 61 15400 8724 20438 -423 -4183 -443 N ATOM 324 N TYR A 62 25.641 41.147 2.361 1.00109.93 N ANISOU 324 N TYR A 62 14534 8110 19124 -1913 -3316 877 N ATOM 325 CA TYR A 62 26.080 40.438 1.161 1.00102.78 C ANISOU 325 CA TYR A 62 13607 7435 18012 -2175 -3049 1191 C ATOM 326 C TYR A 62 26.133 38.935 1.400 1.00111.09 C ANISOU 326 C TYR A 62 14383 8970 18857 -2046 -2685 1089 C ATOM 327 O TYR A 62 25.772 38.146 0.518 1.00114.87 O ANISOU 327 O TYR A 62 14844 9651 19150 -2042 -2504 1227 O ATOM 328 CB TYR A 62 27.444 40.955 0.708 1.00103.79 C ANISOU 328 CB TYR A 62 13764 7492 18178 -2634 -3031 1441 C ATOM 329 CG TYR A 62 27.423 42.339 0.096 1.00123.60 C ANISOU 329 CG TYR A 62 16564 9649 20749 -2790 -3302 1630 C ATOM 330 CD1 TYR A 62 27.151 42.522 -1.251 1.00142.32 C ANISOU 330 CD1 TYR A 62 19114 11995 22965 -2929 -3295 1946 C ATOM 331 CD2 TYR A 62 27.664 43.462 0.868 1.00137.27 C ANISOU 331 CD2 TYR A 62 18380 11126 22651 -2765 -3549 1478 C ATOM 332 CE1 TYR A 62 27.135 43.792 -1.812 1.00144.50 C ANISOU 332 CE1 TYR A 62 19653 11994 23259 -3048 -3523 2120 C ATOM 333 CE2 TYR A 62 27.643 44.729 0.323 1.00148.16 C ANISOU 333 CE2 TYR A 62 20020 12215 24059 -2882 -3782 1641 C ATOM 334 CZ TYR A 62 27.377 44.890 -1.017 1.00145.86 C ANISOU 334 CZ TYR A 62 19909 11896 23614 -3026 -3767 1969 C ATOM 335 OH TYR A 62 27.358 46.152 -1.563 1.00186.20 O ANISOU 335 OH TYR A 62 25283 16706 28758 -3146 -4007 2145 O ATOM 336 N PHE A 63 26.585 38.518 2.584 1.00105.72 N ANISOU 336 N PHE A 63 13491 8472 18205 -1934 -2586 848 N ATOM 337 CA PHE A 63 26.553 37.100 2.922 1.00100.79 C ANISOU 337 CA PHE A 63 12630 8264 17401 -1779 -2276 743 C ATOM 338 C PHE A 63 25.117 36.599 2.998 1.00109.61 C ANISOU 338 C PHE A 63 13755 9438 18455 -1443 -2281 617 C ATOM 339 O PHE A 63 24.791 35.534 2.461 1.00109.40 O ANISOU 339 O PHE A 63 13652 9656 18259 -1401 -2061 683 O ATOM 340 CB PHE A 63 27.271 36.849 4.247 1.00108.04 C ANISOU 340 CB PHE A 63 13340 9345 18364 -1703 -2205 510 C ATOM 341 CG PHE A 63 28.738 37.162 4.216 1.00103.38 C ANISOU 341 CG PHE A 63 12689 8782 17811 -2030 -2159 603 C ATOM 342 CD1 PHE A 63 29.623 36.335 3.546 1.00110.94 C ANISOU 342 CD1 PHE A 63 13524 10035 18593 -2246 -1891 770 C ATOM 343 CD2 PHE A 63 29.238 38.257 4.898 1.00100.05 C ANISOU 343 CD2 PHE A 63 12308 8113 17594 -2112 -2390 496 C ATOM 344 CE1 PHE A 63 30.976 36.619 3.526 1.00114.55 C ANISOU 344 CE1 PHE A 63 13894 10565 19066 -2549 -1844 838 C ATOM 345 CE2 PHE A 63 30.587 38.542 4.886 1.00 96.75 C ANISOU 345 CE2 PHE A 63 11811 7739 17210 -2432 -2345 571 C ATOM 346 CZ PHE A 63 31.457 37.724 4.200 1.00 96.74 C ANISOU 346 CZ PHE A 63 11676 8061 17018 -2655 -2066 745 C ATOM 347 N LEU A 64 24.246 37.362 3.664 1.00112.65 N ANISOU 347 N LEU A 64 14219 9607 18976 -1198 -2542 417 N ATOM 348 CA LEU A 64 22.829 37.016 3.724 1.00116.19 C ANISOU 348 CA LEU A 64 14666 10118 19364 -884 -2575 284 C ATOM 349 C LEU A 64 22.224 36.870 2.335 1.00106.79 C ANISOU 349 C LEU A 64 13622 8882 18072 -952 -2558 507 C ATOM 350 O LEU A 64 21.304 36.068 2.139 1.00106.52 O ANISOU 350 O LEU A 64 13516 9039 17916 -774 -2443 454 O ATOM 351 CB LEU A 64 22.071 38.074 4.529 1.00122.20 C ANISOU 351 CB LEU A 64 15507 10635 20289 -625 -2909 35 C ATOM 352 CG LEU A 64 22.002 37.918 6.049 1.00123.66 C ANISOU 352 CG LEU A 64 15486 10995 20503 -377 -2910 -287 C ATOM 353 CD1 LEU A 64 23.370 37.983 6.687 1.00120.58 C ANISOU 353 CD1 LEU A 64 14994 10643 20176 -561 -2838 -300 C ATOM 354 CD2 LEU A 64 21.120 39.015 6.621 1.00125.85 C ANISOU 354 CD2 LEU A 64 15857 11035 20925 -98 -3273 -538 C ATOM 355 N LEU A 65 22.728 37.632 1.361 1.00 99.61 N ANISOU 355 N LEU A 65 12909 7732 17205 -1216 -2672 761 N ATOM 356 CA LEU A 65 22.234 37.516 -0.006 1.00 93.29 C ANISOU 356 CA LEU A 65 12247 6912 16286 -1288 -2656 992 C ATOM 357 C LEU A 65 22.539 36.139 -0.585 1.00103.90 C ANISOU 357 C LEU A 65 13420 8639 17420 -1377 -2305 1093 C ATOM 358 O LEU A 65 21.736 35.586 -1.347 1.00102.45 O ANISOU 358 O LEU A 65 13250 8565 17110 -1281 -2237 1139 O ATOM 359 CB LEU A 65 22.847 38.616 -0.871 1.00114.44 C ANISOU 359 CB LEU A 65 15165 9277 19039 -1589 -2840 1275 C ATOM 360 CG LEU A 65 22.345 38.752 -2.305 1.00125.97 C ANISOU 360 CG LEU A 65 16812 10671 20382 -1666 -2884 1539 C ATOM 361 CD1 LEU A 65 20.869 39.091 -2.286 1.00136.72 C ANISOU 361 CD1 LEU A 65 18293 11874 21779 -1317 -3110 1380 C ATOM 362 CD2 LEU A 65 23.133 39.828 -3.039 1.00128.43 C ANISOU 362 CD2 LEU A 65 17346 10692 20760 -2016 -3049 1853 C ATOM 363 N SER A 66 23.694 35.568 -0.232 1.00 98.63 N ANISOU 363 N SER A 66 12584 8178 16711 -1544 -2093 1108 N ATOM 364 CA SER A 66 24.056 34.252 -0.751 1.00 99.19 C ANISOU 364 CA SER A 66 12495 8603 16591 -1608 -1784 1179 C ATOM 365 C SER A 66 23.226 33.152 -0.101 1.00 95.15 C ANISOU 365 C SER A 66 11826 8304 16022 -1323 -1647 962 C ATOM 366 O SER A 66 22.854 32.177 -0.765 1.00101.97 O ANISOU 366 O SER A 66 12633 9364 16747 -1288 -1483 1004 O ATOM 367 CB SER A 66 25.547 33.994 -0.540 1.00100.00 C ANISOU 367 CB SER A 66 12461 8873 16663 -1847 -1621 1236 C ATOM 368 OG SER A 66 25.855 33.893 0.838 1.00122.90 O ANISOU 368 OG SER A 66 15228 11813 19657 -1722 -1611 1009 O ATOM 369 N LEU A 67 22.940 33.281 1.200 1.00 95.14 N ANISOU 369 N LEU A 67 11748 8279 16122 -1126 -1715 731 N ATOM 370 CA LEU A 67 22.024 32.348 1.851 1.00 99.07 C ANISOU 370 CA LEU A 67 12108 8971 16564 -867 -1610 545 C ATOM 371 C LEU A 67 20.663 32.362 1.171 1.00109.98 C ANISOU 371 C LEU A 67 13577 10304 17907 -720 -1698 539 C ATOM 372 O LEU A 67 20.057 31.306 0.949 1.00107.49 O ANISOU 372 O LEU A 67 13166 10191 17485 -635 -1538 510 O ATOM 373 CB LEU A 67 21.869 32.693 3.333 1.00104.18 C ANISOU 373 CB LEU A 67 12666 9607 17312 -675 -1707 303 C ATOM 374 CG LEU A 67 22.896 32.222 4.364 1.00109.01 C ANISOU 374 CG LEU A 67 13109 10390 17920 -702 -1564 220 C ATOM 375 CD1 LEU A 67 24.204 32.975 4.225 1.00130.93 C ANISOU 375 CD1 LEU A 67 15937 13034 20775 -947 -1622 318 C ATOM 376 CD2 LEU A 67 22.332 32.392 5.766 1.00100.82 C ANISOU 376 CD2 LEU A 67 11966 9408 16933 -440 -1652 -37 C ATOM 377 N ALA A 68 20.170 33.554 0.829 1.00 88.81 N ANISOU 377 N ALA A 68 11083 7346 15316 -686 -1967 559 N ATOM 378 CA ALA A 68 18.870 33.667 0.184 1.00 92.64 C ANISOU 378 CA ALA A 68 11654 7783 15761 -522 -2081 536 C ATOM 379 C ALA A 68 18.864 33.026 -1.196 1.00103.61 C ANISOU 379 C ALA A 68 13082 9280 17006 -658 -1939 742 C ATOM 380 O ALA A 68 17.829 32.510 -1.634 1.00121.13 O ANISOU 380 O ALA A 68 15273 11607 19145 -516 -1912 686 O ATOM 381 CB ALA A 68 18.470 35.134 0.085 1.00 92.70 C ANISOU 381 CB ALA A 68 11880 7442 15900 -452 -2429 524 C ATOM 382 N CYS A 69 19.996 33.061 -1.901 1.00 97.21 N ANISOU 382 N CYS A 69 12317 8466 16152 -932 -1852 967 N ATOM 383 CA CYS A 69 20.080 32.376 -3.186 1.00 96.54 C ANISOU 383 CA CYS A 69 12233 8542 15904 -1052 -1701 1143 C ATOM 384 C CYS A 69 19.971 30.867 -3.006 1.00103.01 C ANISOU 384 C CYS A 69 12844 9671 16623 -978 -1438 1034 C ATOM 385 O CYS A 69 19.309 30.187 -3.800 1.00108.97 O ANISOU 385 O CYS A 69 13577 10553 17272 -920 -1366 1044 O ATOM 386 CB CYS A 69 21.383 32.747 -3.896 1.00 98.65 C ANISOU 386 CB CYS A 69 12561 8795 16126 -1367 -1658 1396 C ATOM 387 SG CYS A 69 21.479 34.489 -4.404 1.00116.71 S ANISOU 387 SG CYS A 69 15139 10686 18520 -1515 -1979 1603 S ATOM 388 N ALA A 70 20.608 30.325 -1.964 1.00 94.49 N ANISOU 388 N ALA A 70 11616 8706 15581 -976 -1306 926 N ATOM 389 CA ALA A 70 20.463 28.904 -1.670 1.00100.36 C ANISOU 389 CA ALA A 70 12184 9697 16249 -894 -1087 824 C ATOM 390 C ALA A 70 19.051 28.582 -1.195 1.00105.60 C ANISOU 390 C ALA A 70 12801 10389 16934 -660 -1127 649 C ATOM 391 O ALA A 70 18.470 27.569 -1.600 1.00110.83 O ANISOU 391 O ALA A 70 13389 11202 17520 -610 -1007 618 O ATOM 392 CB ALA A 70 21.495 28.478 -0.627 1.00 85.11 C ANISOU 392 CB ALA A 70 10123 7868 14346 -933 -960 762 C ATOM 393 N ASP A 71 18.480 29.440 -0.343 1.00100.86 N ANISOU 393 N ASP A 71 12231 9657 16435 -516 -1305 520 N ATOM 394 CA ASP A 71 17.117 29.222 0.131 1.00 98.28 C ANISOU 394 CA ASP A 71 11833 9401 16108 -293 -1353 339 C ATOM 395 C ASP A 71 16.112 29.297 -1.009 1.00100.79 C ANISOU 395 C ASP A 71 12235 9695 16368 -239 -1434 370 C ATOM 396 O ASP A 71 15.052 28.662 -0.948 1.00109.15 O ANISOU 396 O ASP A 71 13194 10897 17382 -109 -1391 248 O ATOM 397 CB ASP A 71 16.761 30.246 1.209 1.00 87.69 C ANISOU 397 CB ASP A 71 10502 7943 14871 -131 -1557 173 C ATOM 398 CG ASP A 71 17.554 30.047 2.479 1.00119.41 C ANISOU 398 CG ASP A 71 14398 12044 18929 -134 -1471 95 C ATOM 399 OD1 ASP A 71 17.954 28.898 2.743 1.00134.37 O ANISOU 399 OD1 ASP A 71 16166 14133 20757 -190 -1243 121 O ATOM 400 OD2 ASP A 71 17.776 31.033 3.213 1.00150.23 O ANISOU 400 OD2 ASP A 71 18336 15813 22930 -69 -1644 1 O ATOM 401 N LEU A 72 16.422 30.066 -2.051 1.00101.92 N ANISOU 401 N LEU A 72 12554 9670 16501 -344 -1553 536 N ATOM 402 CA LEU A 72 15.504 30.192 -3.176 1.00 98.31 C ANISOU 402 CA LEU A 72 12186 9195 15972 -279 -1644 574 C ATOM 403 C LEU A 72 15.490 28.920 -4.015 1.00 95.45 C ANISOU 403 C LEU A 72 11727 9054 15485 -353 -1427 626 C ATOM 404 O LEU A 72 14.438 28.515 -4.523 1.00 92.82 O ANISOU 404 O LEU A 72 11359 8814 15094 -238 -1437 546 O ATOM 405 CB LEU A 72 15.890 31.412 -4.013 1.00100.70 C ANISOU 405 CB LEU A 72 12721 9249 16291 -380 -1843 766 C ATOM 406 CG LEU A 72 14.982 31.872 -5.151 1.00115.95 C ANISOU 406 CG LEU A 72 14797 11106 18152 -292 -2005 826 C ATOM 407 CD1 LEU A 72 13.605 32.218 -4.613 1.00126.41 C ANISOU 407 CD1 LEU A 72 16103 12401 19525 0 -2184 583 C ATOM 408 CD2 LEU A 72 15.602 33.082 -5.832 1.00116.26 C ANISOU 408 CD2 LEU A 72 15080 10878 18215 -440 -2194 1066 C ATOM 409 N ILE A 73 16.646 28.267 -4.157 1.00 90.93 N ANISOU 409 N ILE A 73 11099 8579 14872 -532 -1242 737 N ATOM 410 CA ILE A 73 16.709 27.015 -4.905 1.00 95.49 C ANISOU 410 CA ILE A 73 11578 9363 15340 -583 -1052 756 C ATOM 411 C ILE A 73 15.976 25.906 -4.158 1.00 98.81 C ANISOU 411 C ILE A 73 11835 9923 15785 -465 -935 573 C ATOM 412 O ILE A 73 15.278 25.085 -4.767 1.00 96.75 O ANISOU 412 O ILE A 73 11514 9780 15468 -424 -874 518 O ATOM 413 CB ILE A 73 18.175 26.642 -5.193 1.00 86.13 C ANISOU 413 CB ILE A 73 10364 8263 14098 -780 -906 894 C ATOM 414 CG1 ILE A 73 18.805 27.671 -6.137 1.00 98.25 C ANISOU 414 CG1 ILE A 73 12050 9704 15578 -936 -1009 1107 C ATOM 415 CG2 ILE A 73 18.276 25.238 -5.773 1.00100.72 C ANISOU 415 CG2 ILE A 73 12092 10327 15850 -793 -721 860 C ATOM 416 CD1 ILE A 73 20.305 27.529 -6.292 1.00114.52 C ANISOU 416 CD1 ILE A 73 14065 11868 17581 -1147 -884 1237 C ATOM 417 N ILE A 74 16.113 25.866 -2.830 1.00 88.88 N ANISOU 417 N ILE A 74 10500 8660 14608 -418 -908 479 N ATOM 418 CA ILE A 74 15.384 24.880 -2.034 1.00 85.70 C ANISOU 418 CA ILE A 74 9946 8395 14220 -326 -804 334 C ATOM 419 C ILE A 74 13.880 25.093 -2.161 1.00 88.36 C ANISOU 419 C ILE A 74 10261 8761 14553 -177 -916 205 C ATOM 420 O ILE A 74 13.114 24.143 -2.360 1.00100.12 O ANISOU 420 O ILE A 74 11648 10382 16010 -155 -830 132 O ATOM 421 CB ILE A 74 15.843 24.931 -0.564 1.00 86.59 C ANISOU 421 CB ILE A 74 9984 8521 14397 -296 -768 274 C ATOM 422 CG1 ILE A 74 17.256 24.361 -0.427 1.00 81.52 C ANISOU 422 CG1 ILE A 74 9322 7911 13742 -429 -622 371 C ATOM 423 CG2 ILE A 74 14.848 24.217 0.347 1.00 78.62 C ANISOU 423 CG2 ILE A 74 8827 7655 13390 -188 -707 134 C ATOM 424 CD1 ILE A 74 17.864 24.557 0.943 1.00100.93 C ANISOU 424 CD1 ILE A 74 11722 10378 16252 -398 -604 321 C ATOM 425 N GLY A 75 13.434 26.346 -2.056 1.00 92.61 N ANISOU 425 N GLY A 75 10889 9174 15124 -69 -1124 163 N ATOM 426 CA GLY A 75 12.011 26.635 -2.108 1.00 85.68 C ANISOU 426 CA GLY A 75 9977 8345 14232 107 -1254 9 C ATOM 427 C GLY A 75 11.387 26.463 -3.477 1.00 96.17 C ANISOU 427 C GLY A 75 11358 9698 15484 115 -1289 39 C ATOM 428 O GLY A 75 10.165 26.303 -3.572 1.00103.01 O ANISOU 428 O GLY A 75 12143 10677 16321 244 -1340 -110 O ATOM 429 N THR A 76 12.193 26.505 -4.539 1.00 90.50 N ANISOU 429 N THR A 76 10758 8908 14719 -17 -1264 219 N ATOM 430 CA THR A 76 11.671 26.369 -5.894 1.00 95.81 C ANISOU 430 CA THR A 76 11480 9626 15297 -1 -1301 256 C ATOM 431 C THR A 76 11.697 24.928 -6.386 1.00 97.14 C ANISOU 431 C THR A 76 11519 9977 15412 -83 -1100 235 C ATOM 432 O THR A 76 10.719 24.460 -6.980 1.00110.97 O ANISOU 432 O THR A 76 13206 11840 17117 -8 -1110 130 O ATOM 433 CB THR A 76 12.461 27.257 -6.863 1.00101.13 C ANISOU 433 CB THR A 76 12351 10153 15921 -96 -1401 473 C ATOM 434 OG1 THR A 76 12.341 28.629 -6.470 1.00 97.44 O ANISOU 434 OG1 THR A 76 12031 9468 15523 -15 -1628 488 O ATOM 435 CG2 THR A 76 11.941 27.103 -8.286 1.00 86.53 C ANISOU 435 CG2 THR A 76 10547 8385 13945 -68 -1437 518 C ATOM 436 N PHE A 77 12.792 24.208 -6.148 1.00100.22 N ANISOU 436 N PHE A 77 11868 10400 15813 -224 -932 313 N ATOM 437 CA PHE A 77 12.985 22.875 -6.703 1.00 99.86 C ANISOU 437 CA PHE A 77 11726 10492 15723 -295 -770 296 C ATOM 438 C PHE A 77 13.003 21.779 -5.648 1.00101.15 C ANISOU 438 C PHE A 77 11753 10716 15962 -320 -624 207 C ATOM 439 O PHE A 77 12.280 20.786 -5.776 1.00 88.73 O ANISOU 439 O PHE A 77 10079 9236 14400 -307 -562 101 O ATOM 440 CB PHE A 77 14.293 22.829 -7.505 1.00 91.58 C ANISOU 440 CB PHE A 77 10740 9460 14595 -426 -706 458 C ATOM 441 CG PHE A 77 14.311 23.750 -8.687 1.00101.50 C ANISOU 441 CG PHE A 77 12127 10690 15746 -435 -830 585 C ATOM 442 CD1 PHE A 77 13.667 23.405 -9.864 1.00 95.95 C ANISOU 442 CD1 PHE A 77 11414 10102 14942 -381 -854 551 C ATOM 443 CD2 PHE A 77 14.979 24.961 -8.623 1.00115.43 C ANISOU 443 CD2 PHE A 77 14030 12315 17513 -503 -931 745 C ATOM 444 CE1 PHE A 77 13.686 24.254 -10.955 1.00109.16 C ANISOU 444 CE1 PHE A 77 13213 11765 16496 -385 -971 690 C ATOM 445 CE2 PHE A 77 15.003 25.816 -9.709 1.00119.28 C ANISOU 445 CE2 PHE A 77 14657 12765 17899 -532 -1053 899 C ATOM 446 CZ PHE A 77 14.355 25.462 -10.877 1.00123.81 C ANISOU 446 CZ PHE A 77 15222 13470 18351 -467 -1070 879 C ATOM 447 N SER A 78 13.816 21.937 -4.602 1.00 89.18 N ANISOU 447 N SER A 78 10236 9148 14502 -360 -576 252 N ATOM 448 CA SER A 78 14.053 20.845 -3.662 1.00 91.58 C ANISOU 448 CA SER A 78 10433 9507 14857 -394 -432 210 C ATOM 449 C SER A 78 12.784 20.475 -2.902 1.00 90.09 C ANISOU 449 C SER A 78 10131 9388 14710 -326 -431 81 C ATOM 450 O SER A 78 12.421 19.297 -2.806 1.00101.15 O ANISOU 450 O SER A 78 11444 10856 16133 -369 -331 35 O ATOM 451 CB SER A 78 15.160 21.239 -2.684 1.00 87.40 C ANISOU 451 CB SER A 78 9924 8923 14360 -429 -400 278 C ATOM 452 OG SER A 78 16.380 21.472 -3.363 1.00102.26 O ANISOU 452 OG SER A 78 11878 10780 16194 -520 -381 394 O ATOM 453 N MET A 79 12.099 21.477 -2.355 1.00 86.25 N ANISOU 453 N MET A 79 9642 8895 14235 -222 -552 15 N ATOM 454 CA MET A 79 10.998 21.225 -1.433 1.00 87.26 C ANISOU 454 CA MET A 79 9630 9145 14379 -156 -544 -113 C ATOM 455 C MET A 79 9.805 20.596 -2.147 1.00 99.30 C ANISOU 455 C MET A 79 11073 10776 15881 -150 -544 -212 C ATOM 456 O MET A 79 9.189 19.657 -1.631 1.00 84.20 O ANISOU 456 O MET A 79 9026 8980 13987 -201 -449 -269 O ATOM 457 CB MET A 79 10.607 22.541 -0.759 1.00107.68 C ANISOU 457 CB MET A 79 12229 11715 16969 -14 -702 -190 C ATOM 458 CG MET A 79 9.727 22.423 0.465 1.00118.28 C ANISOU 458 CG MET A 79 13403 13232 18304 65 -689 -323 C ATOM 459 SD MET A 79 9.352 24.066 1.111 1.00134.02 S ANISOU 459 SD MET A 79 15423 15198 20301 277 -919 -455 S ATOM 460 CE MET A 79 10.974 24.607 1.643 1.00103.82 C ANISOU 460 CE MET A 79 11724 11188 16537 219 -915 -324 C ATOM 461 N ASN A 80 9.470 21.096 -3.339 1.00 99.53 N ANISOU 461 N ASN A 80 11179 10771 15867 -97 -653 -229 N ATOM 462 CA ASN A 80 8.292 20.605 -4.050 1.00 85.80 C ANISOU 462 CA ASN A 80 9352 9149 14101 -70 -674 -351 C ATOM 463 C ASN A 80 8.508 19.194 -4.583 1.00 94.92 C ANISOU 463 C ASN A 80 10459 10327 15278 -203 -536 -334 C ATOM 464 O ASN A 80 7.625 18.336 -4.468 1.00 96.77 O ANISOU 464 O ASN A 80 10560 10668 15539 -247 -485 -436 O ATOM 465 CB ASN A 80 7.931 21.558 -5.189 1.00 98.17 C ANISOU 465 CB ASN A 80 11025 10675 15599 44 -843 -367 C ATOM 466 CG ASN A 80 7.302 22.841 -4.695 1.00103.87 C ANISOU 466 CG ASN A 80 11773 11383 16311 213 -1022 -449 C ATOM 467 OD1 ASN A 80 6.436 22.824 -3.820 1.00 97.62 O ANISOU 467 OD1 ASN A 80 10838 10725 15528 285 -1034 -594 O ATOM 468 ND2 ASN A 80 7.738 23.965 -5.250 1.00101.71 N ANISOU 468 ND2 ASN A 80 11680 10952 16013 278 -1172 -358 N ATOM 469 N LEU A 81 9.672 18.937 -5.184 1.00 90.02 N ANISOU 469 N LEU A 81 9940 9616 14648 -270 -486 -217 N ATOM 470 CA LEU A 81 9.924 17.619 -5.758 1.00 85.89 C ANISOU 470 CA LEU A 81 9381 9106 14146 -363 -386 -229 C ATOM 471 C LEU A 81 10.030 16.553 -4.675 1.00 84.00 C ANISOU 471 C LEU A 81 9064 8858 13997 -458 -263 -223 C ATOM 472 O LEU A 81 9.615 15.407 -4.884 1.00 86.86 O ANISOU 472 O LEU A 81 9357 9235 14410 -531 -212 -286 O ATOM 473 CB LEU A 81 11.187 17.651 -6.617 1.00 80.49 C ANISOU 473 CB LEU A 81 8804 8373 13407 -390 -369 -124 C ATOM 474 CG LEU A 81 11.068 18.540 -7.858 1.00 84.87 C ANISOU 474 CG LEU A 81 9438 8956 13853 -321 -483 -101 C ATOM 475 CD1 LEU A 81 12.385 18.616 -8.609 1.00100.53 C ANISOU 475 CD1 LEU A 81 11503 10939 15754 -373 -451 24 C ATOM 476 CD2 LEU A 81 9.952 18.048 -8.767 1.00 84.90 C ANISOU 476 CD2 LEU A 81 9368 9060 13830 -272 -529 -245 C ATOM 477 N TYR A 82 10.581 16.913 -3.512 1.00 81.01 N ANISOU 477 N TYR A 82 8698 8446 13636 -461 -226 -145 N ATOM 478 CA TYR A 82 10.594 16.002 -2.371 1.00 82.57 C ANISOU 478 CA TYR A 82 8824 8653 13896 -540 -119 -119 C ATOM 479 C TYR A 82 9.193 15.517 -2.020 1.00 86.77 C ANISOU 479 C TYR A 82 9214 9302 14453 -581 -109 -216 C ATOM 480 O TYR A 82 8.972 14.319 -1.804 1.00 97.39 O ANISOU 480 O TYR A 82 10507 10636 15861 -698 -32 -208 O ATOM 481 CB TYR A 82 11.239 16.685 -1.164 1.00 72.35 C ANISOU 481 CB TYR A 82 7547 7351 12590 -502 -103 -44 C ATOM 482 CG TYR A 82 10.997 15.949 0.131 1.00 84.29 C ANISOU 482 CG TYR A 82 8968 8925 14134 -561 -9 -15 C ATOM 483 CD1 TYR A 82 11.607 14.728 0.391 1.00105.10 C ANISOU 483 CD1 TYR A 82 11628 11488 16819 -654 89 64 C ATOM 484 CD2 TYR A 82 10.149 16.475 1.097 1.00 76.28 C ANISOU 484 CD2 TYR A 82 7841 8054 13087 -515 -28 -68 C ATOM 485 CE1 TYR A 82 11.371 14.049 1.576 1.00 91.16 C ANISOU 485 CE1 TYR A 82 9793 9774 15070 -719 169 124 C ATOM 486 CE2 TYR A 82 9.913 15.809 2.283 1.00 91.23 C ANISOU 486 CE2 TYR A 82 9638 10045 14980 -580 65 -21 C ATOM 487 CZ TYR A 82 10.528 14.598 2.519 1.00103.69 C ANISOU 487 CZ TYR A 82 11259 11531 16608 -692 166 92 C ATOM 488 OH TYR A 82 10.294 13.934 3.701 1.00107.68 O ANISOU 488 OH TYR A 82 11684 12127 17101 -768 253 171 O ATOM 489 N THR A 83 8.231 16.437 -1.958 1.00 90.29 N ANISOU 489 N THR A 83 9593 9865 14850 -489 -198 -312 N ATOM 490 CA THR A 83 6.890 16.075 -1.518 1.00 81.40 C ANISOU 490 CA THR A 83 8295 8909 13723 -528 -185 -418 C ATOM 491 C THR A 83 6.127 15.289 -2.579 1.00 90.07 C ANISOU 491 C THR A 83 9340 10031 14851 -595 -196 -517 C ATOM 492 O THR A 83 5.354 14.387 -2.232 1.00 85.56 O ANISOU 492 O THR A 83 8638 9546 14323 -724 -134 -556 O ATOM 493 CB THR A 83 6.130 17.334 -1.102 1.00 79.95 C ANISOU 493 CB THR A 83 8044 8868 13465 -373 -296 -524 C ATOM 494 OG1 THR A 83 6.788 17.910 0.032 1.00 93.57 O ANISOU 494 OG1 THR A 83 9792 10584 15175 -323 -282 -454 O ATOM 495 CG2 THR A 83 4.694 17.013 -0.725 1.00 90.47 C ANISOU 495 CG2 THR A 83 9165 10440 14770 -403 -287 -661 C ATOM 496 N THR A 84 6.332 15.591 -3.864 1.00 83.35 N ANISOU 496 N THR A 84 8580 9116 13974 -521 -275 -555 N ATOM 497 CA THR A 84 5.770 14.736 -4.907 1.00 96.94 C ANISOU 497 CA THR A 84 10252 10854 15726 -578 -285 -658 C ATOM 498 C THR A 84 6.330 13.324 -4.805 1.00 96.84 C ANISOU 498 C THR A 84 10257 10720 15819 -735 -185 -598 C ATOM 499 O THR A 84 5.587 12.338 -4.875 1.00103.00 O ANISOU 499 O THR A 84 10938 11525 16674 -857 -160 -674 O ATOM 500 CB THR A 84 6.056 15.311 -6.294 1.00101.13 C ANISOU 500 CB THR A 84 10885 11355 16184 -460 -384 -688 C ATOM 501 OG1 THR A 84 7.473 15.402 -6.491 1.00141.32 O ANISOU 501 OG1 THR A 84 16122 16312 21262 -459 -352 -547 O ATOM 502 CG2 THR A 84 5.449 16.677 -6.437 1.00102.78 C ANISOU 502 CG2 THR A 84 11103 11649 16299 -297 -512 -742 C ATOM 503 N TYR A 85 7.649 13.214 -4.645 1.00 92.09 N ANISOU 503 N TYR A 85 9783 9980 15228 -733 -140 -469 N ATOM 504 CA TYR A 85 8.284 11.912 -4.481 1.00 78.74 C ANISOU 504 CA TYR A 85 8130 8154 13635 -846 -69 -416 C ATOM 505 C TYR A 85 7.775 11.211 -3.228 1.00 87.94 C ANISOU 505 C TYR A 85 9214 9325 14873 -987 9 -357 C ATOM 506 O TYR A 85 7.437 10.022 -3.261 1.00 84.54 O ANISOU 506 O TYR A 85 8755 8821 14546 -1123 30 -375 O ATOM 507 CB TYR A 85 9.802 12.090 -4.440 1.00 73.09 C ANISOU 507 CB TYR A 85 7547 7334 12889 -788 -43 -302 C ATOM 508 CG TYR A 85 10.591 10.809 -4.303 1.00121.93 C ANISOU 508 CG TYR A 85 13790 13376 19163 -855 4 -264 C ATOM 509 CD1 TYR A 85 10.710 9.925 -5.367 1.00137.07 C ANISOU 509 CD1 TYR A 85 15725 15232 21125 -857 -38 -368 C ATOM 510 CD2 TYR A 85 11.242 10.499 -3.119 1.00145.07 C ANISOU 510 CD2 TYR A 85 16760 16235 22126 -893 73 -136 C ATOM 511 CE1 TYR A 85 11.439 8.755 -5.246 1.00140.91 C ANISOU 511 CE1 TYR A 85 16273 15566 21699 -890 -26 -355 C ATOM 512 CE2 TYR A 85 11.974 9.335 -2.991 1.00156.61 C ANISOU 512 CE2 TYR A 85 18291 17547 23666 -929 92 -103 C ATOM 513 CZ TYR A 85 12.071 8.467 -4.055 1.00144.88 C ANISOU 513 CZ TYR A 85 16831 15981 22237 -924 36 -217 C ATOM 514 OH TYR A 85 12.803 7.308 -3.925 1.00121.05 O ANISOU 514 OH TYR A 85 13893 12797 19305 -933 25 -207 O ATOM 515 N LEU A 86 7.704 11.940 -2.111 1.00 83.81 N ANISOU 515 N LEU A 86 8654 8896 14295 -961 42 -284 N ATOM 516 CA LEU A 86 7.150 11.375 -0.884 1.00 73.40 C ANISOU 516 CA LEU A 86 7235 7647 13005 -1094 122 -215 C ATOM 517 C LEU A 86 5.726 10.872 -1.093 1.00 91.37 C ANISOU 517 C LEU A 86 9352 10051 15314 -1218 114 -325 C ATOM 518 O LEU A 86 5.391 9.748 -0.703 1.00105.50 O ANISOU 518 O LEU A 86 11100 11796 17190 -1407 170 -269 O ATOM 519 CB LEU A 86 7.182 12.413 0.237 1.00 92.34 C ANISOU 519 CB LEU A 86 9586 10190 15307 -1006 138 -167 C ATOM 520 CG LEU A 86 6.498 11.958 1.528 1.00 94.32 C ANISOU 520 CG LEU A 86 9699 10597 15543 -1132 223 -100 C ATOM 521 CD1 LEU A 86 7.202 10.754 2.120 1.00102.60 C ANISOU 521 CD1 LEU A 86 10831 11486 16668 -1271 308 72 C ATOM 522 CD2 LEU A 86 6.409 13.092 2.540 1.00 98.27 C ANISOU 522 CD2 LEU A 86 10121 11290 15927 -1004 216 -109 C ATOM 523 N LEU A 87 4.869 11.695 -1.703 1.00103.73 N ANISOU 523 N LEU A 87 10827 11776 16811 -1119 37 -481 N ATOM 524 CA LEU A 87 3.455 11.341 -1.789 1.00 99.44 C ANISOU 524 CA LEU A 87 10094 11413 16275 -1226 31 -608 C ATOM 525 C LEU A 87 3.176 10.279 -2.846 1.00 95.77 C ANISOU 525 C LEU A 87 9633 10833 15923 -1340 3 -695 C ATOM 526 O LEU A 87 2.196 9.536 -2.719 1.00 90.99 O ANISOU 526 O LEU A 87 8882 10315 15374 -1518 26 -752 O ATOM 527 CB LEU A 87 2.607 12.585 -2.062 1.00 86.16 C ANISOU 527 CB LEU A 87 8308 9955 14475 -1050 -63 -770 C ATOM 528 CG LEU A 87 2.551 13.636 -0.948 1.00 94.43 C ANISOU 528 CG LEU A 87 9300 11166 15415 -932 -64 -747 C ATOM 529 CD1 LEU A 87 1.715 14.834 -1.384 1.00107.29 C ANISOU 529 CD1 LEU A 87 10850 12974 16939 -726 -199 -937 C ATOM 530 CD2 LEU A 87 2.028 13.051 0.360 1.00 82.72 C ANISOU 530 CD2 LEU A 87 7651 9863 13918 -1102 48 -677 C ATOM 531 N MET A 88 4.002 10.186 -3.889 1.00 87.62 N ANISOU 531 N MET A 88 8747 9625 14917 -1245 -51 -718 N ATOM 532 CA MET A 88 3.821 9.136 -4.883 1.00105.30 C ANISOU 532 CA MET A 88 10991 11754 17265 -1329 -92 -824 C ATOM 533 C MET A 88 4.528 7.838 -4.518 1.00104.64 C ANISOU 533 C MET A 88 11006 11428 17325 -1480 -47 -710 C ATOM 534 O MET A 88 4.165 6.781 -5.048 1.00 85.45 O ANISOU 534 O MET A 88 8555 8893 15021 -1602 -84 -798 O ATOM 535 CB MET A 88 4.315 9.596 -6.259 1.00 97.67 C ANISOU 535 CB MET A 88 10112 10759 16237 -1143 -182 -926 C ATOM 536 CG MET A 88 3.500 10.706 -6.887 1.00 92.72 C ANISOU 536 CG MET A 88 9406 10339 15484 -992 -263 -1059 C ATOM 537 SD MET A 88 4.048 11.041 -8.573 1.00100.31 S ANISOU 537 SD MET A 88 10469 11280 16363 -808 -365 -1151 S ATOM 538 CE MET A 88 5.629 11.827 -8.271 1.00135.35 C ANISOU 538 CE MET A 88 15098 15604 20725 -709 -331 -940 C ATOM 539 N GLY A 89 5.524 7.888 -3.639 1.00 94.98 N ANISOU 539 N GLY A 89 9894 10103 16089 -1464 16 -529 N ATOM 540 CA GLY A 89 6.262 6.697 -3.279 1.00 93.75 C ANISOU 540 CA GLY A 89 9855 9706 16060 -1571 38 -419 C ATOM 541 C GLY A 89 7.266 6.230 -4.306 1.00 96.09 C ANISOU 541 C GLY A 89 10286 9822 16400 -1458 -33 -492 C ATOM 542 O GLY A 89 7.871 5.169 -4.115 1.00 95.94 O ANISOU 542 O GLY A 89 10371 9584 16496 -1518 -47 -437 O ATOM 543 N HIS A 90 7.467 6.984 -5.384 1.00 95.13 N ANISOU 543 N HIS A 90 10166 9799 16182 -1288 -87 -613 N ATOM 544 CA HIS A 90 8.452 6.632 -6.398 1.00 96.04 C ANISOU 544 CA HIS A 90 10379 9815 16295 -1165 -149 -692 C ATOM 545 C HIS A 90 8.731 7.869 -7.242 1.00 90.41 C ANISOU 545 C HIS A 90 9665 9275 15413 -990 -174 -737 C ATOM 546 O HIS A 90 7.990 8.854 -7.197 1.00111.28 O ANISOU 546 O HIS A 90 12236 12073 17970 -962 -175 -744 O ATOM 547 CB HIS A 90 7.974 5.465 -7.269 1.00 83.31 C ANISOU 547 CB HIS A 90 8739 8098 14816 -1228 -237 -869 C ATOM 548 CG HIS A 90 6.848 5.820 -8.187 1.00 94.65 C ANISOU 548 CG HIS A 90 10042 9705 16214 -1214 -292 -1048 C ATOM 549 ND1 HIS A 90 5.544 5.937 -7.756 1.00 94.66 N ANISOU 549 ND1 HIS A 90 9907 9814 16244 -1350 -271 -1072 N ATOM 550 CD2 HIS A 90 6.830 6.080 -9.515 1.00 99.32 C ANISOU 550 CD2 HIS A 90 10606 10406 16724 -1071 -370 -1218 C ATOM 551 CE1 HIS A 90 4.772 6.257 -8.779 1.00 96.34 C ANISOU 551 CE1 HIS A 90 10018 10183 16404 -1280 -340 -1260 C ATOM 552 NE2 HIS A 90 5.528 6.350 -9.858 1.00106.56 N ANISOU 552 NE2 HIS A 90 11383 11475 17630 -1110 -402 -1344 N ATOM 553 N TRP A 91 9.813 7.804 -8.016 1.00 94.87 N ANISOU 553 N TRP A 91 10308 9818 15921 -870 -204 -766 N ATOM 554 CA TRP A 91 10.268 8.920 -8.839 1.00 90.26 C ANISOU 554 CA TRP A 91 9741 9390 15164 -729 -225 -767 C ATOM 555 C TRP A 91 9.802 8.693 -10.273 1.00106.53 C ANISOU 555 C TRP A 91 11744 11550 17184 -659 -313 -956 C ATOM 556 O TRP A 91 10.350 7.843 -10.983 1.00 90.61 O ANISOU 556 O TRP A 91 9740 9497 15190 -612 -356 -1065 O ATOM 557 CB TRP A 91 11.787 9.054 -8.780 1.00 82.68 C ANISOU 557 CB TRP A 91 8875 8407 14133 -655 -192 -671 C ATOM 558 CG TRP A 91 12.312 10.271 -9.480 1.00 85.52 C ANISOU 558 CG TRP A 91 9256 8925 14312 -557 -202 -620 C ATOM 559 CD1 TRP A 91 12.817 10.335 -10.747 1.00 89.59 C ANISOU 559 CD1 TRP A 91 9767 9568 14705 -466 -245 -693 C ATOM 560 CD2 TRP A 91 12.416 11.595 -8.940 1.00 98.98 C ANISOU 560 CD2 TRP A 91 10996 10676 15936 -550 -177 -475 C ATOM 561 NE1 TRP A 91 13.212 11.620 -11.035 1.00101.68 N ANISOU 561 NE1 TRP A 91 11335 11218 16083 -428 -242 -573 N ATOM 562 CE2 TRP A 91 12.979 12.412 -9.942 1.00109.11 C ANISOU 562 CE2 TRP A 91 12309 12087 17060 -477 -210 -445 C ATOM 563 CE3 TRP A 91 12.082 12.170 -7.711 1.00100.19 C ANISOU 563 CE3 TRP A 91 11153 10783 16133 -596 -140 -375 C ATOM 564 CZ2 TRP A 91 13.213 13.773 -9.751 1.00107.51 C ANISOU 564 CZ2 TRP A 91 12163 11919 16766 -465 -219 -306 C ATOM 565 CZ3 TRP A 91 12.316 13.521 -7.523 1.00 96.87 C ANISOU 565 CZ3 TRP A 91 10776 10409 15620 -555 -156 -272 C ATOM 566 CH2 TRP A 91 12.877 14.306 -8.538 1.00 92.84 C ANISOU 566 CH2 TRP A 91 10317 9979 14977 -498 -201 -233 C ATOM 567 N ALA A 92 8.807 9.467 -10.706 1.00104.67 N ANISOU 567 N ALA A 92 11440 11455 16876 -628 -352 -1010 N ATOM 568 CA ALA A 92 8.219 9.311 -12.029 1.00 99.72 C ANISOU 568 CA ALA A 92 10743 10950 16196 -551 -440 -1196 C ATOM 569 C ALA A 92 8.673 10.390 -13.006 1.00104.47 C ANISOU 569 C ALA A 92 11385 11721 16587 -404 -477 -1157 C ATOM 570 O ALA A 92 8.039 10.575 -14.050 1.00116.45 O ANISOU 570 O ALA A 92 12844 13382 18018 -320 -554 -1284 O ATOM 571 CB ALA A 92 6.694 9.299 -11.928 1.00120.93 C ANISOU 571 CB ALA A 92 13308 13696 18942 -613 -475 -1312 C ATOM 572 N LEU A 93 9.759 11.098 -12.698 1.00104.51 N ANISOU 572 N LEU A 93 11487 11719 16502 -381 -428 -977 N ATOM 573 CA LEU A 93 10.218 12.211 -13.521 1.00115.74 C ANISOU 573 CA LEU A 93 12963 13289 17726 -284 -460 -888 C ATOM 574 C LEU A 93 11.448 11.870 -14.355 1.00115.21 C ANISOU 574 C LEU A 93 12912 13316 17545 -232 -447 -888 C ATOM 575 O LEU A 93 12.068 12.776 -14.921 1.00119.52 O ANISOU 575 O LEU A 93 13507 13990 17915 -191 -452 -765 O ATOM 576 CB LEU A 93 10.504 13.436 -12.648 1.00125.63 C ANISOU 576 CB LEU A 93 14301 14487 18944 -307 -432 -684 C ATOM 577 CG LEU A 93 9.309 14.283 -12.198 1.00126.43 C ANISOU 577 CG LEU A 93 14389 14588 19062 -287 -487 -687 C ATOM 578 CD1 LEU A 93 8.509 13.586 -11.107 1.00137.63 C ANISOU 578 CD1 LEU A 93 15722 15925 20648 -375 -444 -762 C ATOM 579 CD2 LEU A 93 9.769 15.656 -11.732 1.00120.73 C ANISOU 579 CD2 LEU A 93 13775 13828 18270 -265 -505 -502 C ATOM 580 N GLY A 94 11.815 10.597 -14.452 1.00104.92 N ANISOU 580 N GLY A 94 11568 11965 16333 -233 -442 -1026 N ATOM 581 CA GLY A 94 12.934 10.187 -15.271 1.00103.67 C ANISOU 581 CA GLY A 94 11395 11938 16057 -155 -444 -1077 C ATOM 582 C GLY A 94 14.255 10.211 -14.524 1.00124.20 C ANISOU 582 C GLY A 94 14054 14484 18652 -188 -365 -941 C ATOM 583 O GLY A 94 14.372 10.701 -13.398 1.00118.50 O ANISOU 583 O GLY A 94 13395 13629 18000 -269 -306 -784 O ATOM 584 N THR A 95 15.280 9.671 -15.186 1.00129.39 N ANISOU 584 N THR A 95 14674 15278 19210 -108 -371 -1026 N ATOM 585 CA THR A 95 16.586 9.524 -14.555 1.00113.89 C ANISOU 585 CA THR A 95 12741 13296 17235 -116 -307 -947 C ATOM 586 C THR A 95 17.359 10.836 -14.492 1.00118.60 C ANISOU 586 C THR A 95 13372 14031 17660 -168 -240 -722 C ATOM 587 O THR A 95 18.153 11.034 -13.566 1.00119.14 O ANISOU 587 O THR A 95 13482 14024 17762 -220 -176 -607 O ATOM 588 CB THR A 95 17.410 8.460 -15.288 1.00106.67 C ANISOU 588 CB THR A 95 11756 12508 16266 11 -353 -1151 C ATOM 589 OG1 THR A 95 18.649 8.257 -14.601 1.00133.35 O ANISOU 589 OG1 THR A 95 15157 15869 19640 20 -300 -1096 O ATOM 590 CG2 THR A 95 17.695 8.875 -16.727 1.00100.56 C ANISOU 590 CG2 THR A 95 10890 12083 15234 98 -377 -1204 C ATOM 591 N LEU A 96 17.144 11.744 -15.447 1.00128.64 N ANISOU 591 N LEU A 96 14631 15496 18751 -162 -262 -652 N ATOM 592 CA LEU A 96 17.899 12.993 -15.452 1.00112.19 C ANISOU 592 CA LEU A 96 12591 13525 16512 -240 -214 -421 C ATOM 593 C LEU A 96 17.352 13.982 -14.430 1.00109.93 C ANISOU 593 C LEU A 96 12410 13022 16337 -332 -209 -249 C ATOM 594 O LEU A 96 18.124 14.695 -13.780 1.00115.87 O ANISOU 594 O LEU A 96 13212 13740 17074 -414 -161 -86 O ATOM 595 CB LEU A 96 17.891 13.611 -16.850 1.00108.31 C ANISOU 595 CB LEU A 96 12065 13313 15776 -210 -251 -378 C ATOM 596 CG LEU A 96 18.730 14.878 -17.026 1.00104.75 C ANISOU 596 CG LEU A 96 11661 12995 15145 -320 -213 -118 C ATOM 597 CD1 LEU A 96 20.203 14.584 -16.781 1.00 96.16 C ANISOU 597 CD1 LEU A 96 10505 12046 13984 -360 -129 -103 C ATOM 598 CD2 LEU A 96 18.520 15.480 -18.408 1.00111.53 C ANISOU 598 CD2 LEU A 96 12503 14114 15760 -297 -262 -48 C ATOM 599 N ALA A 97 16.026 14.040 -14.278 1.00 93.66 N ANISOU 599 N ALA A 97 10370 10833 14382 -313 -265 -303 N ATOM 600 CA ALA A 97 15.436 14.916 -13.272 1.00 94.44 C ANISOU 600 CA ALA A 97 10548 10752 14584 -369 -275 -184 C ATOM 601 C ALA A 97 15.846 14.508 -11.863 1.00103.59 C ANISOU 601 C ALA A 97 11718 11740 15900 -421 -205 -163 C ATOM 602 O ALA A 97 15.974 15.365 -10.980 1.00 99.19 O ANISOU 602 O ALA A 97 11220 11086 15379 -471 -193 -33 O ATOM 603 CB ALA A 97 13.913 14.920 -13.404 1.00 89.91 C ANISOU 603 CB ALA A 97 9956 10126 14078 -320 -350 -289 C ATOM 604 N CYS A 98 16.046 13.208 -11.630 1.00110.40 N ANISOU 604 N CYS A 98 12531 12559 16857 -401 -173 -294 N ATOM 605 CA CYS A 98 16.546 12.753 -10.337 1.00110.28 C ANISOU 605 CA CYS A 98 12537 12397 16968 -440 -110 -258 C ATOM 606 C CYS A 98 17.933 13.314 -10.055 1.00110.43 C ANISOU 606 C CYS A 98 12580 12485 16895 -465 -57 -135 C ATOM 607 O CYS A 98 18.191 13.852 -8.972 1.00108.67 O ANISOU 607 O CYS A 98 12397 12167 16726 -511 -22 -27 O ATOM 608 CB CYS A 98 16.572 11.226 -10.292 1.00 99.59 C ANISOU 608 CB CYS A 98 11148 10967 15725 -406 -114 -414 C ATOM 609 SG CYS A 98 17.282 10.563 -8.771 1.00106.78 S ANISOU 609 SG CYS A 98 12102 11702 16767 -434 -51 -355 S ATOM 610 N ASP A 99 18.843 13.192 -11.024 1.00107.44 N ANISOU 610 N ASP A 99 12159 12297 16365 -433 -51 -162 N ATOM 611 CA ASP A 99 20.213 13.647 -10.813 1.00113.53 C ANISOU 611 CA ASP A 99 12923 13177 17035 -471 5 -62 C ATOM 612 C ASP A 99 20.266 15.153 -10.588 1.00 95.49 C ANISOU 612 C ASP A 99 10701 10880 14700 -572 2 134 C ATOM 613 O ASP A 99 21.062 15.638 -9.775 1.00106.64 O ANISOU 613 O ASP A 99 12131 12260 16126 -631 43 229 O ATOM 614 CB ASP A 99 21.083 13.246 -12.004 1.00128.31 C ANISOU 614 CB ASP A 99 14707 15320 18725 -420 9 -143 C ATOM 615 CG ASP A 99 21.231 11.740 -12.136 1.00126.50 C ANISOU 615 CG ASP A 99 14423 15085 18558 -296 -13 -363 C ATOM 616 OD1 ASP A 99 21.140 11.041 -11.105 1.00118.13 O ANISOU 616 OD1 ASP A 99 13404 13812 17670 -277 -8 -403 O ATOM 617 OD2 ASP A 99 21.436 11.256 -13.270 1.00112.43 O ANISOU 617 OD2 ASP A 99 12559 13509 16650 -213 -47 -497 O ATOM 618 N LEU A 100 19.418 15.910 -11.289 1.00107.42 N ANISOU 618 N LEU A 100 12253 12404 16159 -585 -63 189 N ATOM 619 CA LEU A 100 19.416 17.360 -11.122 1.00101.90 C ANISOU 619 CA LEU A 100 11641 11651 15427 -670 -102 373 C ATOM 620 C LEU A 100 18.829 17.762 -9.774 1.00 93.44 C ANISOU 620 C LEU A 100 10624 10351 14526 -672 -122 392 C ATOM 621 O LEU A 100 19.353 18.664 -9.111 1.00 91.49 O ANISOU 621 O LEU A 100 10429 10034 14300 -739 -128 509 O ATOM 622 CB LEU A 100 18.647 18.020 -12.265 1.00 93.24 C ANISOU 622 CB LEU A 100 10586 10621 14218 -655 -189 423 C ATOM 623 CG LEU A 100 19.309 17.870 -13.634 1.00 93.60 C ANISOU 623 CG LEU A 100 10573 10945 14046 -665 -172 444 C ATOM 624 CD1 LEU A 100 18.432 18.443 -14.734 1.00 81.58 C ANISOU 624 CD1 LEU A 100 9097 9491 12409 -627 -266 489 C ATOM 625 CD2 LEU A 100 20.681 18.530 -13.629 1.00 99.70 C ANISOU 625 CD2 LEU A 100 11343 11835 14702 -801 -119 613 C ATOM 626 N TRP A 101 17.739 17.111 -9.358 1.00 78.88 N ANISOU 626 N TRP A 101 8759 8409 12802 -603 -136 270 N ATOM 627 CA TRP A 101 17.156 17.393 -8.049 1.00 87.28 C ANISOU 627 CA TRP A 101 9844 9315 14004 -597 -144 272 C ATOM 628 C TRP A 101 18.152 17.123 -6.927 1.00 93.43 C ANISOU 628 C TRP A 101 10608 10052 14838 -628 -66 304 C ATOM 629 O TRP A 101 18.283 17.926 -5.995 1.00 86.81 O ANISOU 629 O TRP A 101 9803 9136 14047 -646 -81 370 O ATOM 630 CB TRP A 101 15.889 16.561 -7.853 1.00 84.68 C ANISOU 630 CB TRP A 101 9462 8942 13772 -547 -153 137 C ATOM 631 CG TRP A 101 15.253 16.718 -6.503 1.00 84.90 C ANISOU 631 CG TRP A 101 9477 8869 13914 -543 -148 130 C ATOM 632 CD1 TRP A 101 14.706 17.853 -5.978 1.00 92.23 C ANISOU 632 CD1 TRP A 101 10436 9752 14854 -516 -220 164 C ATOM 633 CD2 TRP A 101 15.089 15.697 -5.508 1.00 87.82 C ANISOU 633 CD2 TRP A 101 9793 9188 14388 -560 -77 84 C ATOM 634 NE1 TRP A 101 14.216 17.604 -4.717 1.00 97.12 N ANISOU 634 NE1 TRP A 101 11001 10338 15563 -507 -188 127 N ATOM 635 CE2 TRP A 101 14.439 16.288 -4.406 1.00101.31 C ANISOU 635 CE2 TRP A 101 11483 10865 16147 -548 -93 97 C ATOM 636 CE3 TRP A 101 15.429 14.342 -5.443 1.00 94.64 C ANISOU 636 CE3 TRP A 101 10629 10027 15304 -579 -14 34 C ATOM 637 CZ2 TRP A 101 14.122 15.571 -3.252 1.00101.62 C ANISOU 637 CZ2 TRP A 101 11464 10881 16265 -573 -29 85 C ATOM 638 CZ3 TRP A 101 15.115 13.632 -4.295 1.00 86.80 C ANISOU 638 CZ3 TRP A 101 9608 8963 14411 -610 35 36 C ATOM 639 CH2 TRP A 101 14.468 14.247 -3.217 1.00 88.37 C ANISOU 639 CH2 TRP A 101 9777 9163 14638 -616 37 73 C ATOM 640 N LEU A 102 18.861 15.995 -6.998 1.00 88.92 N ANISOU 640 N LEU A 102 9988 9536 14262 -614 4 241 N ATOM 641 CA LEU A 102 19.851 15.672 -5.976 1.00 90.19 C ANISOU 641 CA LEU A 102 10136 9673 14460 -619 70 261 C ATOM 642 C LEU A 102 21.007 16.665 -5.995 1.00102.02 C ANISOU 642 C LEU A 102 11646 11249 15868 -684 79 367 C ATOM 643 O LEU A 102 21.478 17.104 -4.938 1.00 88.23 O ANISOU 643 O LEU A 102 9907 9448 14169 -702 97 414 O ATOM 644 CB LEU A 102 20.367 14.251 -6.189 1.00 82.46 C ANISOU 644 CB LEU A 102 9114 8731 13485 -564 111 155 C ATOM 645 CG LEU A 102 19.370 13.104 -6.029 1.00 89.23 C ANISOU 645 CG LEU A 102 9967 9475 14462 -528 98 55 C ATOM 646 CD1 LEU A 102 20.001 11.824 -6.531 1.00 87.31 C ANISOU 646 CD1 LEU A 102 9700 9261 14213 -461 97 -63 C ATOM 647 CD2 LEU A 102 18.935 12.952 -4.578 1.00 82.48 C ANISOU 647 CD2 LEU A 102 9128 8484 13725 -544 127 101 C ATOM 648 N ALA A 103 21.475 17.030 -7.188 1.00 99.98 N ANISOU 648 N ALA A 103 11378 11134 15473 -729 66 408 N ATOM 649 CA ALA A 103 22.582 17.973 -7.295 1.00 97.20 C ANISOU 649 CA ALA A 103 11028 10874 15028 -833 77 528 C ATOM 650 C ALA A 103 22.198 19.336 -6.734 1.00 99.25 C ANISOU 650 C ALA A 103 11377 10980 15354 -897 3 642 C ATOM 651 O ALA A 103 22.895 19.884 -5.872 1.00 90.80 O ANISOU 651 O ALA A 103 10309 9866 14324 -948 11 689 O ATOM 652 CB ALA A 103 23.026 18.092 -8.751 1.00 86.37 C ANISOU 652 CB ALA A 103 9622 9719 13475 -884 78 569 C ATOM 653 N LEU A 104 21.081 19.894 -7.209 1.00 94.36 N ANISOU 653 N LEU A 104 10828 10277 14748 -878 -87 669 N ATOM 654 CA LEU A 104 20.650 21.211 -6.749 1.00 81.42 C ANISOU 654 CA LEU A 104 9287 8475 13174 -907 -195 755 C ATOM 655 C LEU A 104 20.453 21.239 -5.239 1.00 84.21 C ANISOU 655 C LEU A 104 9625 8703 13667 -848 -193 687 C ATOM 656 O LEU A 104 20.787 22.230 -4.581 1.00103.74 O ANISOU 656 O LEU A 104 12145 11079 16192 -889 -254 742 O ATOM 657 CB LEU A 104 19.361 21.619 -7.462 1.00 84.53 C ANISOU 657 CB LEU A 104 9749 8810 13557 -845 -303 752 C ATOM 658 CG LEU A 104 19.462 21.912 -8.959 1.00 98.25 C ANISOU 658 CG LEU A 104 11525 10666 15138 -899 -337 852 C ATOM 659 CD1 LEU A 104 18.079 22.120 -9.557 1.00105.63 C ANISOU 659 CD1 LEU A 104 12512 11554 16067 -795 -444 807 C ATOM 660 CD2 LEU A 104 20.345 23.128 -9.207 1.00 97.08 C ANISOU 660 CD2 LEU A 104 11464 10493 14929 -1052 -390 1050 C ATOM 661 N ASP A 105 19.920 20.156 -4.670 1.00 91.48 N ANISOU 661 N ASP A 105 10481 9630 14648 -758 -130 570 N ATOM 662 CA ASP A 105 19.650 20.131 -3.236 1.00100.70 C ANISOU 662 CA ASP A 105 11621 10721 15920 -699 -121 517 C ATOM 663 C ASP A 105 20.948 20.101 -2.432 1.00111.05 C ANISOU 663 C ASP A 105 12899 12063 17233 -735 -57 541 C ATOM 664 O ASP A 105 21.111 20.859 -1.468 1.00 96.08 O ANISOU 664 O ASP A 105 11010 10103 15392 -725 -99 546 O ATOM 665 CB ASP A 105 18.770 18.926 -2.900 1.00 90.81 C ANISOU 665 CB ASP A 105 10307 9480 14715 -629 -65 419 C ATOM 666 CG ASP A 105 18.170 19.007 -1.511 1.00121.78 C ANISOU 666 CG ASP A 105 14192 13361 18718 -571 -68 377 C ATOM 667 OD1 ASP A 105 18.411 20.011 -0.811 1.00137.42 O ANISOU 667 OD1 ASP A 105 16192 15303 20720 -556 -125 395 O ATOM 668 OD2 ASP A 105 17.460 18.059 -1.114 1.00142.67 O ANISOU 668 OD2 ASP A 105 16784 16024 21401 -545 -18 323 O ATOM 669 N TYR A 106 21.889 19.236 -2.820 1.00104.27 N ANISOU 669 N TYR A 106 11992 11315 16310 -758 33 535 N ATOM 670 CA TYR A 106 23.132 19.093 -2.064 1.00100.76 C ANISOU 670 CA TYR A 106 11499 10930 15855 -769 94 533 C ATOM 671 C TYR A 106 24.066 20.280 -2.268 1.00 99.47 C ANISOU 671 C TYR A 106 11351 10796 15649 -890 56 620 C ATOM 672 O TYR A 106 24.728 20.719 -1.320 1.00 96.62 O ANISOU 672 O TYR A 106 10965 10421 15325 -901 56 615 O ATOM 673 CB TYR A 106 23.819 17.779 -2.440 1.00 93.19 C ANISOU 673 CB TYR A 106 10482 10090 14835 -729 179 473 C ATOM 674 CG TYR A 106 23.255 16.582 -1.711 1.00102.89 C ANISOU 674 CG TYR A 106 11703 11250 16140 -625 214 401 C ATOM 675 CD1 TYR A 106 23.819 16.151 -0.519 1.00109.12 C ANISOU 675 CD1 TYR A 106 12467 12033 16960 -564 257 384 C ATOM 676 CD2 TYR A 106 22.125 15.924 -2.175 1.00106.82 C ANISOU 676 CD2 TYR A 106 12220 11688 16679 -598 199 362 C ATOM 677 CE1 TYR A 106 23.307 15.068 0.165 1.00 99.96 C ANISOU 677 CE1 TYR A 106 11317 10801 15863 -490 283 356 C ATOM 678 CE2 TYR A 106 21.596 14.846 -1.492 1.00102.64 C ANISOU 678 CE2 TYR A 106 11689 11082 16228 -542 226 322 C ATOM 679 CZ TYR A 106 22.194 14.420 -0.323 1.00 98.13 C ANISOU 679 CZ TYR A 106 11108 10496 15680 -493 268 334 C ATOM 680 OH TYR A 106 21.680 13.345 0.365 1.00121.73 O ANISOU 680 OH TYR A 106 14111 13401 18740 -457 290 329 O ATOM 681 N VAL A 107 24.139 20.813 -3.490 1.00 94.60 N ANISOU 681 N VAL A 107 10770 10224 14949 -990 20 704 N ATOM 682 CA VAL A 107 24.993 21.974 -3.728 1.00 97.52 C ANISOU 682 CA VAL A 107 11163 10608 15281 -1146 -23 819 C ATOM 683 C VAL A 107 24.464 23.191 -2.979 1.00107.75 C ANISOU 683 C VAL A 107 12550 11690 16700 -1154 -150 850 C ATOM 684 O VAL A 107 25.233 23.934 -2.356 1.00111.76 O ANISOU 684 O VAL A 107 13053 12161 17250 -1233 -182 875 O ATOM 685 CB VAL A 107 25.128 22.249 -5.237 1.00 95.45 C ANISOU 685 CB VAL A 107 10926 10460 14882 -1261 -34 931 C ATOM 686 CG1 VAL A 107 25.877 23.557 -5.469 1.00 93.41 C ANISOU 686 CG1 VAL A 107 10714 10181 14596 -1461 -96 1090 C ATOM 687 CG2 VAL A 107 25.854 21.100 -5.916 1.00102.86 C ANISOU 687 CG2 VAL A 107 11745 11652 15683 -1239 81 867 C ATOM 688 N ALA A 108 23.148 23.416 -3.022 1.00 92.07 N ANISOU 688 N ALA A 108 10638 9571 14773 -1061 -237 826 N ATOM 689 CA ALA A 108 22.576 24.537 -2.282 1.00 88.63 C ANISOU 689 CA ALA A 108 10280 8943 14451 -1024 -382 815 C ATOM 690 C ALA A 108 22.739 24.344 -0.780 1.00 95.86 C ANISOU 690 C ALA A 108 11121 9851 15452 -928 -353 699 C ATOM 691 O ALA A 108 23.040 25.299 -0.055 1.00103.12 O ANISOU 691 O ALA A 108 12065 10668 16448 -944 -448 686 O ATOM 692 CB ALA A 108 21.101 24.722 -2.644 1.00 71.76 C ANISOU 692 CB ALA A 108 8213 6714 12340 -913 -481 780 C ATOM 693 N SER A 109 22.546 23.115 -0.295 1.00 87.35 N ANISOU 693 N SER A 109 9954 8877 14359 -829 -234 615 N ATOM 694 CA SER A 109 22.715 22.851 1.131 1.00 98.64 C ANISOU 694 CA SER A 109 11309 10330 15840 -735 -198 526 C ATOM 695 C SER A 109 24.169 23.024 1.554 1.00 97.30 C ANISOU 695 C SER A 109 11090 10225 15653 -808 -156 538 C ATOM 696 O SER A 109 24.447 23.508 2.658 1.00 98.87 O ANISOU 696 O SER A 109 11256 10402 15908 -761 -195 478 O ATOM 697 CB SER A 109 22.217 21.445 1.467 1.00 88.36 C ANISOU 697 CB SER A 109 9943 9112 14519 -640 -85 472 C ATOM 698 OG SER A 109 20.825 21.332 1.224 1.00 96.78 O ANISOU 698 OG SER A 109 11027 10137 15607 -582 -127 441 O ATOM 699 N GLN A 110 25.109 22.637 0.688 1.00 85.94 N ANISOU 699 N GLN A 110 9629 8895 14127 -914 -80 598 N ATOM 700 CA GLN A 110 26.521 22.816 1.009 1.00 93.22 C ANISOU 700 CA GLN A 110 10481 9919 15017 -994 -39 598 C ATOM 701 C GLN A 110 26.907 24.289 0.960 1.00 96.44 C ANISOU 701 C GLN A 110 10943 10221 15480 -1140 -159 662 C ATOM 702 O GLN A 110 27.692 24.760 1.790 1.00 95.87 O ANISOU 702 O GLN A 110 10818 10158 15449 -1167 -179 616 O ATOM 703 CB GLN A 110 27.386 21.997 0.049 1.00 88.86 C ANISOU 703 CB GLN A 110 9868 9559 14337 -1058 67 624 C ATOM 704 CG GLN A 110 28.856 21.965 0.425 1.00 74.66 C ANISOU 704 CG GLN A 110 7961 7924 12482 -1113 125 589 C ATOM 705 CD GLN A 110 29.121 21.137 1.672 1.00 91.86 C ANISOU 705 CD GLN A 110 10073 10147 14682 -942 180 472 C ATOM 706 OE1 GLN A 110 28.650 20.004 1.792 1.00108.29 O ANISOU 706 OE1 GLN A 110 12160 12234 16753 -804 231 428 O ATOM 707 NE2 GLN A 110 29.843 21.712 2.618 1.00103.47 N ANISOU 707 NE2 GLN A 110 11487 11639 16186 -952 158 425 N ATOM 708 N ALA A 111 26.363 25.034 -0.006 1.00 92.64 N ANISOU 708 N ALA A 111 10570 9627 15003 -1236 -252 769 N ATOM 709 CA ALA A 111 26.609 26.472 -0.053 1.00 90.99 C ANISOU 709 CA ALA A 111 10448 9255 14869 -1378 -399 848 C ATOM 710 C ALA A 111 26.100 27.154 1.209 1.00 93.40 C ANISOU 710 C ALA A 111 10778 9392 15318 -1251 -526 729 C ATOM 711 O ALA A 111 26.720 28.104 1.701 1.00 93.14 O ANISOU 711 O ALA A 111 10758 9263 15368 -1339 -625 722 O ATOM 712 CB ALA A 111 25.952 27.080 -1.293 1.00 88.81 C ANISOU 712 CB ALA A 111 10309 8868 14566 -1468 -495 993 C ATOM 713 N ARG A 112 24.973 26.678 1.747 1.00 84.21 N ANISOU 713 N ARG A 112 9608 8209 14181 -1047 -531 625 N ATOM 714 CA ARG A 112 24.470 27.205 3.012 1.00 74.65 C ANISOU 714 CA ARG A 112 8381 6909 13073 -895 -638 485 C ATOM 715 C ARG A 112 25.510 27.085 4.115 1.00 88.07 C ANISOU 715 C ARG A 112 9965 8712 14785 -881 -582 398 C ATOM 716 O ARG A 112 25.853 28.074 4.773 1.00102.47 O ANISOU 716 O ARG A 112 11797 10433 16703 -893 -711 333 O ATOM 717 CB ARG A 112 23.201 26.470 3.436 1.00 80.04 C ANISOU 717 CB ARG A 112 9025 7649 13739 -698 -603 392 C ATOM 718 CG ARG A 112 22.700 26.961 4.782 1.00 98.89 C ANISOU 718 CG ARG A 112 11361 10016 16196 -528 -701 234 C ATOM 719 CD ARG A 112 21.584 26.104 5.338 1.00104.52 C ANISOU 719 CD ARG A 112 11993 10858 16864 -361 -631 153 C ATOM 720 NE ARG A 112 20.379 26.169 4.528 1.00108.97 N ANISOU 720 NE ARG A 112 12620 11363 17421 -329 -692 166 N ATOM 721 CZ ARG A 112 19.484 27.145 4.613 1.00123.38 C ANISOU 721 CZ ARG A 112 14495 13083 19301 -226 -877 80 C ATOM 722 NH1 ARG A 112 19.669 28.148 5.463 1.00103.30 N ANISOU 722 NH1 ARG A 112 11952 10464 16835 -147 -1028 -30 N ATOM 723 NH2 ARG A 112 18.408 27.120 3.842 1.00138.61 N ANISOU 723 NH2 ARG A 112 16471 14986 21209 -186 -926 83 N ATOM 724 N VAL A 113 26.009 25.870 4.346 1.00 92.63 N ANISOU 724 N VAL A 113 10438 9486 15272 -841 -406 382 N ATOM 725 CA VAL A 113 26.930 25.657 5.456 1.00102.44 C ANISOU 725 CA VAL A 113 11566 10849 16509 -788 -354 288 C ATOM 726 C VAL A 113 28.267 26.331 5.174 1.00 96.76 C ANISOU 726 C VAL A 113 10823 10142 15797 -979 -375 325 C ATOM 727 O VAL A 113 28.897 26.886 6.082 1.00 94.10 O ANISOU 727 O VAL A 113 10425 9812 15516 -969 -432 229 O ATOM 728 CB VAL A 113 27.083 24.152 5.750 1.00102.02 C ANISOU 728 CB VAL A 113 11429 10978 16355 -679 -182 271 C ATOM 729 CG1 VAL A 113 25.730 23.546 6.108 1.00 94.60 C ANISOU 729 CG1 VAL A 113 10505 10024 15417 -528 -167 247 C ATOM 730 CG2 VAL A 113 27.696 23.414 4.574 1.00112.34 C ANISOU 730 CG2 VAL A 113 12737 12377 17570 -791 -76 361 C ATOM 731 N MET A 114 28.710 26.318 3.912 1.00 96.48 N ANISOU 731 N MET A 114 10824 10134 15701 -1165 -334 458 N ATOM 732 CA MET A 114 29.930 27.033 3.552 1.00 90.62 C ANISOU 732 CA MET A 114 10051 9425 14955 -1392 -354 517 C ATOM 733 C MET A 114 29.789 28.526 3.817 1.00105.69 C ANISOU 733 C MET A 114 12055 11087 17016 -1488 -556 524 C ATOM 734 O MET A 114 30.733 29.170 4.287 1.00109.01 O ANISOU 734 O MET A 114 12417 11509 17491 -1604 -605 483 O ATOM 735 CB MET A 114 30.285 26.779 2.087 1.00101.65 C ANISOU 735 CB MET A 114 11464 10927 16232 -1573 -277 674 C ATOM 736 CG MET A 114 30.785 25.373 1.795 1.00106.43 C ANISOU 736 CG MET A 114 11953 11799 16687 -1497 -98 636 C ATOM 737 SD MET A 114 32.345 25.052 2.631 1.00115.64 S ANISOU 737 SD MET A 114 12932 13208 17800 -1501 -13 512 S ATOM 738 CE MET A 114 32.605 23.322 2.251 1.00134.65 C ANISOU 738 CE MET A 114 15250 15864 20046 -1338 150 450 C ATOM 739 N ASN A 115 28.616 29.095 3.529 1.00111.93 N ANISOU 739 N ASN A 115 12991 11657 17881 -1434 -692 561 N ATOM 740 CA ASN A 115 28.387 30.498 3.855 1.00113.32 C ANISOU 740 CA ASN A 115 13277 11562 18219 -1479 -922 539 C ATOM 741 C ASN A 115 28.390 30.717 5.362 1.00116.15 C ANISOU 741 C ASN A 115 13548 11915 18668 -1292 -992 320 C ATOM 742 O ASN A 115 29.120 31.575 5.870 1.00131.87 O ANISOU 742 O ASN A 115 15524 13819 20763 -1387 -1105 260 O ATOM 743 CB ASN A 115 27.075 30.983 3.239 1.00110.34 C ANISOU 743 CB ASN A 115 13069 10969 17886 -1411 -1065 599 C ATOM 744 CG ASN A 115 27.178 31.194 1.743 1.00120.30 C ANISOU 744 CG ASN A 115 14444 12186 19078 -1630 -1061 833 C ATOM 745 OD1 ASN A 115 28.172 31.725 1.250 1.00136.25 O ANISOU 745 OD1 ASN A 115 16479 14197 21093 -1891 -1070 967 O ATOM 746 ND2 ASN A 115 26.150 30.783 1.013 1.00132.15 N ANISOU 746 ND2 ASN A 115 16015 13683 20513 -1533 -1046 883 N ATOM 747 N LEU A 116 27.593 29.932 6.096 1.00 96.05 N ANISOU 747 N LEU A 116 10936 9481 16078 -1035 -926 197 N ATOM 748 CA LEU A 116 27.542 30.063 7.550 1.00 95.43 C ANISOU 748 CA LEU A 116 10757 9455 16049 -836 -979 -9 C ATOM 749 C LEU A 116 28.925 29.981 8.180 1.00101.79 C ANISOU 749 C LEU A 116 11430 10405 16840 -907 -913 -73 C ATOM 750 O LEU A 116 29.164 30.583 9.234 1.00102.92 O ANISOU 750 O LEU A 116 11511 10530 17064 -817 -1024 -240 O ATOM 751 CB LEU A 116 26.627 28.990 8.139 1.00 84.56 C ANISOU 751 CB LEU A 116 9304 8248 14577 -598 -863 -78 C ATOM 752 CG LEU A 116 25.145 29.160 7.810 1.00 89.03 C ANISOU 752 CG LEU A 116 9958 8706 15161 -484 -953 -81 C ATOM 753 CD1 LEU A 116 24.351 27.947 8.253 1.00 78.84 C ANISOU 753 CD1 LEU A 116 8578 7617 13761 -316 -802 -110 C ATOM 754 CD2 LEU A 116 24.607 30.422 8.466 1.00 83.93 C ANISOU 754 CD2 LEU A 116 9352 7894 14642 -365 -1201 -239 C ATOM 755 N LEU A 117 29.845 29.242 7.557 1.00 88.75 N ANISOU 755 N LEU A 117 9720 8919 15081 -1051 -741 33 N ATOM 756 CA LEU A 117 31.238 29.281 7.990 1.00101.83 C ANISOU 756 CA LEU A 117 11247 10724 16721 -1148 -693 -28 C ATOM 757 C LEU A 117 31.838 30.663 7.761 1.00 98.08 C ANISOU 757 C LEU A 117 10823 10058 16384 -1386 -864 -7 C ATOM 758 O LEU A 117 32.488 31.225 8.649 1.00112.67 O ANISOU 758 O LEU A 117 12588 11911 18312 -1383 -947 -153 O ATOM 759 CB LEU A 117 32.049 28.212 7.257 1.00107.02 C ANISOU 759 CB LEU A 117 11826 11619 17220 -1239 -490 67 C ATOM 760 CG LEU A 117 31.692 26.767 7.604 1.00110.06 C ANISOU 760 CG LEU A 117 12155 12181 17481 -1011 -334 32 C ATOM 761 CD1 LEU A 117 32.443 25.787 6.717 1.00112.41 C ANISOU 761 CD1 LEU A 117 12397 12678 17636 -1092 -174 111 C ATOM 762 CD2 LEU A 117 31.983 26.508 9.067 1.00112.87 C ANISOU 762 CD2 LEU A 117 12395 12660 17829 -805 -326 -138 C ATOM 763 N LEU A 118 31.615 31.231 6.572 1.00 91.00 N ANISOU 763 N LEU A 118 10071 8987 15520 -1599 -928 180 N ATOM 764 CA LEU A 118 32.169 32.544 6.252 1.00107.73 C ANISOU 764 CA LEU A 118 12268 10891 17774 -1867 -1101 248 C ATOM 765 C LEU A 118 31.653 33.609 7.213 1.00103.25 C ANISOU 765 C LEU A 118 11769 10058 17403 -1740 -1352 78 C ATOM 766 O LEU A 118 32.428 34.425 7.725 1.00108.34 O ANISOU 766 O LEU A 118 12374 10619 18169 -1861 -1474 -9 O ATOM 767 CB LEU A 118 31.832 32.915 4.808 1.00108.18 C ANISOU 767 CB LEU A 118 12493 10801 17812 -2086 -1135 504 C ATOM 768 CG LEU A 118 32.442 32.030 3.723 1.00119.28 C ANISOU 768 CG LEU A 118 13823 12482 19017 -2244 -913 669 C ATOM 769 CD1 LEU A 118 31.897 32.416 2.360 1.00127.00 C ANISOU 769 CD1 LEU A 118 14974 13318 19963 -2409 -964 912 C ATOM 770 CD2 LEU A 118 33.960 32.120 3.745 1.00118.13 C ANISOU 770 CD2 LEU A 118 13514 12546 18824 -2487 -831 674 C ATOM 771 N ILE A 119 30.341 33.617 7.470 1.00 98.04 N ANISOU 771 N ILE A 119 11198 9277 16775 -1489 -1442 8 N ATOM 772 CA ILE A 119 29.780 34.570 8.426 1.00104.54 C ANISOU 772 CA ILE A 119 12065 9891 17765 -1312 -1691 -196 C ATOM 773 C ILE A 119 30.427 34.399 9.796 1.00114.35 C ANISOU 773 C ILE A 119 13112 11325 19010 -1166 -1665 -436 C ATOM 774 O ILE A 119 30.766 35.383 10.466 1.00134.37 O ANISOU 774 O ILE A 119 15643 13709 21704 -1174 -1867 -592 O ATOM 775 CB ILE A 119 28.245 34.432 8.506 1.00 90.33 C ANISOU 775 CB ILE A 119 10344 8027 15952 -1036 -1760 -256 C ATOM 776 CG1 ILE A 119 27.565 34.953 7.237 1.00103.35 C ANISOU 776 CG1 ILE A 119 12211 9420 17638 -1160 -1872 -59 C ATOM 777 CG2 ILE A 119 27.702 35.175 9.701 1.00 85.56 C ANISOU 777 CG2 ILE A 119 9715 7326 15468 -783 -1982 -529 C ATOM 778 CD1 ILE A 119 27.238 33.904 6.217 1.00127.68 C ANISOU 778 CD1 ILE A 119 15300 12665 20547 -1205 -1653 130 C ATOM 779 N SER A 120 30.614 33.151 10.232 1.00115.32 N ANISOU 779 N SER A 120 13078 11778 18963 -1025 -1430 -471 N ATOM 780 CA SER A 120 31.221 32.905 11.537 1.00111.46 C ANISOU 780 CA SER A 120 12403 11502 18446 -864 -1396 -685 C ATOM 781 C SER A 120 32.655 33.419 11.584 1.00102.66 C ANISOU 781 C SER A 120 11207 10405 17394 -1100 -1419 -712 C ATOM 782 O SER A 120 33.037 34.143 12.512 1.00113.35 O ANISOU 782 O SER A 120 12490 11718 18860 -1045 -1571 -917 O ATOM 783 CB SER A 120 31.168 31.414 11.869 1.00 92.19 C ANISOU 783 CB SER A 120 9840 9385 15801 -689 -1144 -671 C ATOM 784 OG SER A 120 29.829 30.981 12.032 1.00110.09 O ANISOU 784 OG SER A 120 12153 11658 18019 -472 -1133 -675 O ATOM 785 N PHE A 121 33.467 33.052 10.589 1.00 89.23 N ANISOU 785 N PHE A 121 9498 8790 15615 -1365 -1273 -522 N ATOM 786 CA PHE A 121 34.849 33.520 10.557 1.00101.04 C ANISOU 786 CA PHE A 121 10893 10346 17152 -1624 -1281 -539 C ATOM 787 C PHE A 121 34.926 35.038 10.446 1.00 97.07 C ANISOU 787 C PHE A 121 10510 9490 16882 -1836 -1551 -546 C ATOM 788 O PHE A 121 35.788 35.665 11.074 1.00108.14 O ANISOU 788 O PHE A 121 11811 10888 18387 -1930 -1650 -693 O ATOM 789 CB PHE A 121 35.614 32.857 9.409 1.00103.54 C ANISOU 789 CB PHE A 121 11168 10856 17317 -1869 -1078 -331 C ATOM 790 CG PHE A 121 36.025 31.437 9.691 1.00101.10 C ANISOU 790 CG PHE A 121 10698 10915 16801 -1687 -842 -385 C ATOM 791 CD1 PHE A 121 37.150 31.173 10.457 1.00104.78 C ANISOU 791 CD1 PHE A 121 10962 11637 17210 -1654 -780 -549 C ATOM 792 CD2 PHE A 121 35.303 30.370 9.185 1.00104.55 C ANISOU 792 CD2 PHE A 121 11188 11430 17104 -1547 -699 -278 C ATOM 793 CE1 PHE A 121 37.541 29.873 10.720 1.00103.79 C ANISOU 793 CE1 PHE A 121 10710 11828 16897 -1466 -589 -598 C ATOM 794 CE2 PHE A 121 35.687 29.065 9.445 1.00 91.09 C ANISOU 794 CE2 PHE A 121 9361 10022 15229 -1377 -512 -326 C ATOM 795 CZ PHE A 121 36.808 28.817 10.213 1.00 95.65 C ANISOU 795 CZ PHE A 121 9755 10840 15747 -1329 -461 -481 C ATOM 796 N ASP A 122 34.033 35.648 9.661 1.00103.87 N ANISOU 796 N ASP A 122 11591 10041 17834 -1909 -1689 -393 N ATOM 797 CA ASP A 122 34.071 37.099 9.494 1.00104.03 C ANISOU 797 CA ASP A 122 11766 9672 18088 -2113 -1976 -375 C ATOM 798 C ASP A 122 33.911 37.813 10.830 1.00109.01 C ANISOU 798 C ASP A 122 12352 10179 18887 -1888 -2203 -691 C ATOM 799 O ASP A 122 34.652 38.754 11.136 1.00120.99 O ANISOU 799 O ASP A 122 13859 11534 20578 -2072 -2378 -777 O ATOM 800 CB ASP A 122 32.994 37.554 8.512 1.00104.19 C ANISOU 800 CB ASP A 122 12044 9384 18160 -2149 -2102 -177 C ATOM 801 CG ASP A 122 33.055 39.044 8.237 1.00124.63 C ANISOU 801 CG ASP A 122 14830 11531 20994 -2377 -2417 -120 C ATOM 802 OD1 ASP A 122 33.969 39.482 7.506 1.00118.06 O ANISOU 802 OD1 ASP A 122 14027 10639 20191 -2774 -2412 84 O ATOM 803 OD2 ASP A 122 32.197 39.781 8.766 1.00128.51 O ANISOU 803 OD2 ASP A 122 15445 11739 21646 -2161 -2681 -282 O ATOM 804 N ARG A 123 32.944 37.378 11.643 1.00100.65 N ANISOU 804 N ARG A 123 11255 9212 17774 -1495 -2207 -875 N ATOM 805 CA ARG A 123 32.826 37.918 12.994 1.00104.20 C ANISOU 805 CA ARG A 123 11614 9641 18335 -1239 -2396 -1205 C ATOM 806 C ARG A 123 34.082 37.631 13.810 1.00109.04 C ANISOU 806 C ARG A 123 11992 10535 18903 -1269 -2293 -1362 C ATOM 807 O ARG A 123 34.536 38.481 14.585 1.00114.05 O ANISOU 807 O ARG A 123 12569 11066 19699 -1262 -2496 -1588 O ATOM 808 CB ARG A 123 31.605 37.330 13.699 1.00 92.72 C ANISOU 808 CB ARG A 123 10118 8341 16769 -823 -2367 -1351 C ATOM 809 CG ARG A 123 30.259 37.671 13.102 1.00117.28 C ANISOU 809 CG ARG A 123 13428 11208 19925 -724 -2502 -1275 C ATOM 810 CD ARG A 123 29.877 39.124 13.324 1.00135.20 C ANISOU 810 CD ARG A 123 15842 13083 22443 -684 -2886 -1437 C ATOM 811 NE ARG A 123 28.468 39.340 13.008 1.00151.87 N ANISOU 811 NE ARG A 123 18100 15040 24562 -478 -3021 -1440 N ATOM 812 CZ ARG A 123 28.005 39.608 11.793 1.00162.48 C ANISOU 812 CZ ARG A 123 19665 16128 25942 -641 -3074 -1196 C ATOM 813 NH1 ARG A 123 28.841 39.688 10.766 1.00176.09 N ANISOU 813 NH1 ARG A 123 21486 17734 27687 -1026 -2995 -912 N ATOM 814 NH2 ARG A 123 26.704 39.784 11.601 1.00152.53 N ANISOU 814 NH2 ARG A 123 18514 14764 24676 -413 -3204 -1241 N ATOM 815 N TYR A 124 34.652 36.433 13.652 1.00100.03 N ANISOU 815 N TYR A 124 10711 9749 17546 -1287 -1993 -1263 N ATOM 816 CA TYR A 124 35.832 36.063 14.425 1.00 96.25 C ANISOU 816 CA TYR A 124 10000 9574 16996 -1278 -1888 -1421 C ATOM 817 C TYR A 124 37.015 36.963 14.092 1.00 97.65 C ANISOU 817 C TYR A 124 10152 9628 17323 -1655 -1992 -1408 C ATOM 818 O TYR A 124 37.677 37.494 14.991 1.00109.08 O ANISOU 818 O TYR A 124 11467 11109 18869 -1632 -2114 -1650 O ATOM 819 CB TYR A 124 36.189 34.595 14.181 1.00 84.96 C ANISOU 819 CB TYR A 124 8457 8518 15308 -1222 -1569 -1302 C ATOM 820 CG TYR A 124 37.444 34.164 14.909 1.00 96.80 C ANISOU 820 CG TYR A 124 9720 10347 16714 -1198 -1462 -1461 C ATOM 821 CD1 TYR A 124 37.433 33.932 16.279 1.00 88.76 C ANISOU 821 CD1 TYR A 124 8557 9523 15645 -871 -1486 -1718 C ATOM 822 CD2 TYR A 124 38.647 34.011 14.229 1.00 95.81 C ANISOU 822 CD2 TYR A 124 9503 10366 16534 -1495 -1345 -1362 C ATOM 823 CE1 TYR A 124 38.578 33.549 16.947 1.00 96.76 C ANISOU 823 CE1 TYR A 124 9356 10844 16564 -828 -1402 -1871 C ATOM 824 CE2 TYR A 124 39.797 33.630 14.889 1.00102.72 C ANISOU 824 CE2 TYR A 124 10151 11561 17315 -1457 -1259 -1530 C ATOM 825 CZ TYR A 124 39.758 33.399 16.248 1.00117.88 C ANISOU 825 CZ TYR A 124 11946 13649 19196 -1117 -1292 -1784 C ATOM 826 OH TYR A 124 40.904 33.018 16.910 1.00126.55 O ANISOU 826 OH TYR A 124 12818 15076 20191 -1057 -1216 -1959 O ATOM 827 N PHE A 125 37.300 37.145 12.801 1.00105.98 N ANISOU 827 N PHE A 125 11320 10559 18388 -2016 -1944 -1125 N ATOM 828 CA PHE A 125 38.432 37.984 12.422 1.00115.90 C ANISOU 828 CA PHE A 125 12543 11721 19771 -2426 -2029 -1076 C ATOM 829 C PHE A 125 38.153 39.458 12.688 1.00112.82 C ANISOU 829 C PHE A 125 12308 10874 19684 -2521 -2384 -1171 C ATOM 830 O PHE A 125 39.085 40.222 12.965 1.00107.24 O ANISOU 830 O PHE A 125 11524 10096 19128 -2760 -2512 -1269 O ATOM 831 CB PHE A 125 38.790 37.766 10.952 1.00121.98 C ANISOU 831 CB PHE A 125 13383 12525 20441 -2792 -1876 -730 C ATOM 832 CG PHE A 125 39.321 36.393 10.652 1.00119.14 C ANISOU 832 CG PHE A 125 12845 12625 19799 -2737 -1554 -670 C ATOM 833 CD1 PHE A 125 40.615 36.045 11.001 1.00126.86 C ANISOU 833 CD1 PHE A 125 13570 13950 20681 -2829 -1429 -790 C ATOM 834 CD2 PHE A 125 38.537 35.460 9.995 1.00113.95 C ANISOU 834 CD2 PHE A 125 12271 12047 18976 -2590 -1392 -509 C ATOM 835 CE1 PHE A 125 41.108 34.784 10.723 1.00122.69 C ANISOU 835 CE1 PHE A 125 12886 13834 19895 -2748 -1161 -757 C ATOM 836 CE2 PHE A 125 39.024 34.198 9.713 1.00115.96 C ANISOU 836 CE2 PHE A 125 12378 12695 18989 -2525 -1127 -473 C ATOM 837 CZ PHE A 125 40.311 33.860 10.076 1.00123.74 C ANISOU 837 CZ PHE A 125 13121 14015 19879 -2593 -1017 -599 C ATOM 838 N SER A 126 36.885 39.873 12.620 1.00107.50 N ANISOU 838 N SER A 126 11849 9889 19108 -2332 -2562 -1160 N ATOM 839 CA SER A 126 36.550 41.264 12.906 1.00114.80 C ANISOU 839 CA SER A 126 12937 10354 20327 -2368 -2937 -1280 C ATOM 840 C SER A 126 36.801 41.614 14.366 1.00120.31 C ANISOU 840 C SER A 126 13467 11117 21129 -2112 -3094 -1686 C ATOM 841 O SER A 126 37.148 42.759 14.676 1.00138.91 O ANISOU 841 O SER A 126 15874 13164 23741 -2251 -3383 -1825 O ATOM 842 CB SER A 126 35.092 41.545 12.547 1.00108.83 C ANISOU 842 CB SER A 126 12429 9300 19622 -2159 -3094 -1215 C ATOM 843 OG SER A 126 34.865 41.379 11.159 1.00126.36 O ANISOU 843 OG SER A 126 14822 11423 21767 -2410 -2992 -844 O ATOM 844 N VAL A 127 36.636 40.652 15.268 1.00114.32 N ANISOU 844 N VAL A 127 12510 10752 20175 -1743 -2918 -1878 N ATOM 845 CA VAL A 127 36.773 40.922 16.695 1.00123.54 C ANISOU 845 CA VAL A 127 13505 12033 21401 -1448 -3060 -2271 C ATOM 846 C VAL A 127 38.194 40.662 17.185 1.00115.31 C ANISOU 846 C VAL A 127 12209 11299 20306 -1585 -2935 -2390 C ATOM 847 O VAL A 127 38.719 41.417 18.006 1.00122.00 O ANISOU 847 O VAL A 127 12955 12084 21317 -1571 -3141 -2672 O ATOM 848 CB VAL A 127 35.737 40.092 17.478 1.00126.86 C ANISOU 848 CB VAL A 127 13852 12721 21629 -961 -2961 -2410 C ATOM 849 CG1 VAL A 127 35.956 40.240 18.965 1.00145.01 C ANISOU 849 CG1 VAL A 127 15937 15231 23931 -645 -3068 -2804 C ATOM 850 CG2 VAL A 127 34.331 40.530 17.108 1.00123.72 C ANISOU 850 CG2 VAL A 127 13678 12020 21309 -811 -3137 -2362 C ATOM 851 N THR A 128 38.845 39.605 16.694 1.00110.88 N ANISOU 851 N THR A 128 11532 11080 19517 -1705 -2614 -2204 N ATOM 852 CA THR A 128 40.206 39.306 17.122 1.00112.95 C ANISOU 852 CA THR A 128 11539 11673 19705 -1816 -2491 -2328 C ATOM 853 C THR A 128 41.245 40.143 16.391 1.00116.97 C ANISOU 853 C THR A 128 12055 12009 20378 -2331 -2572 -2214 C ATOM 854 O THR A 128 42.364 40.296 16.894 1.00123.93 O ANISOU 854 O THR A 128 12723 13085 21280 -2447 -2572 -2394 O ATOM 855 CB THR A 128 40.520 37.823 16.914 1.00106.75 C ANISOU 855 CB THR A 128 10620 11335 18604 -1712 -2137 -2202 C ATOM 856 OG1 THR A 128 40.494 37.520 15.513 1.00109.28 O ANISOU 856 OG1 THR A 128 11070 11592 18858 -2006 -1991 -1852 O ATOM 857 CG2 THR A 128 39.492 36.965 17.630 1.00104.00 C ANISOU 857 CG2 THR A 128 10272 11151 18093 -1242 -2053 -2280 C ATOM 858 N ARG A 129 40.906 40.679 15.223 1.00124.14 N ANISOU 858 N ARG A 129 13197 12577 21392 -2648 -2640 -1915 N ATOM 859 CA ARG A 129 41.802 41.529 14.440 1.00125.10 C ANISOU 859 CA ARG A 129 13353 12510 21667 -3183 -2725 -1748 C ATOM 860 C ARG A 129 41.047 42.800 14.070 1.00131.39 C ANISOU 860 C ARG A 129 14455 12709 22757 -3322 -3064 -1660 C ATOM 861 O ARG A 129 40.743 43.040 12.895 1.00128.19 O ANISOU 861 O ARG A 129 14263 12076 22368 -3597 -3064 -1318 O ATOM 862 CB ARG A 129 42.299 40.784 13.200 1.00113.27 C ANISOU 862 CB ARG A 129 11826 11265 19948 -3480 -2431 -1405 C ATOM 863 CG ARG A 129 43.124 39.549 13.543 1.00125.27 C ANISOU 863 CG ARG A 129 13048 13363 21187 -3336 -2127 -1513 C ATOM 864 CD ARG A 129 43.546 38.757 12.317 1.00133.84 C ANISOU 864 CD ARG A 129 14095 14721 22036 -3573 -1850 -1211 C ATOM 865 NE ARG A 129 44.264 37.542 12.697 1.00145.07 N ANISOU 865 NE ARG A 129 15250 16675 23195 -3371 -1592 -1347 N ATOM 866 CZ ARG A 129 44.699 36.625 11.840 1.00153.03 C ANISOU 866 CZ ARG A 129 16169 18017 23958 -3464 -1339 -1174 C ATOM 867 NH1 ARG A 129 44.492 36.776 10.539 1.00162.51 N ANISOU 867 NH1 ARG A 129 17511 19107 25128 -3767 -1291 -852 N ATOM 868 NH2 ARG A 129 45.341 35.553 12.284 1.00151.42 N ANISOU 868 NH2 ARG A 129 15735 18265 23532 -3237 -1146 -1334 N ATOM 869 N PRO A 130 40.721 43.639 15.061 1.00126.58 N ANISOU 869 N PRO A 130 13878 11838 22380 -3116 -3373 -1974 N ATOM 870 CA PRO A 130 39.841 44.788 14.781 1.00141.82 C ANISOU 870 CA PRO A 130 16120 13181 24584 -3151 -3728 -1928 C ATOM 871 C PRO A 130 40.425 45.768 13.782 1.00141.15 C ANISOU 871 C PRO A 130 16232 12786 24611 -3677 -3826 -1620 C ATOM 872 O PRO A 130 39.707 46.255 12.899 1.00143.11 O ANISOU 872 O PRO A 130 16793 12736 24845 -3743 -3900 -1338 O ATOM 873 CB PRO A 130 39.663 45.434 16.164 1.00152.06 C ANISOU 873 CB PRO A 130 17340 14363 26072 -2819 -4022 -2389 C ATOM 874 CG PRO A 130 40.012 44.359 17.147 1.00144.39 C ANISOU 874 CG PRO A 130 16050 13964 24849 -2480 -3768 -2633 C ATOM 875 CD PRO A 130 41.098 43.573 16.483 1.00128.14 C ANISOU 875 CD PRO A 130 13830 12270 22588 -2807 -3430 -2400 C ATOM 876 N LEU A 131 41.715 46.073 13.898 1.00127.24 N ANISOU 876 N LEU A 131 14311 11179 22857 -4004 -3776 -1649 N ATOM 877 CA LEU A 131 42.354 47.043 13.022 1.00137.34 C ANISOU 877 CA LEU A 131 15781 12266 24138 -4482 -3808 -1351 C ATOM 878 C LEU A 131 42.842 46.412 11.723 1.00137.33 C ANISOU 878 C LEU A 131 15754 12520 23906 -4865 -3497 -948 C ATOM 879 O LEU A 131 42.779 47.054 10.668 1.00145.34 O ANISOU 879 O LEU A 131 17025 13325 24874 -5161 -3506 -605 O ATOM 880 CB LEU A 131 43.520 47.710 13.766 1.00119.14 C ANISOU 880 CB LEU A 131 13304 10019 21944 -4676 -3903 -1588 C ATOM 881 CG LEU A 131 44.113 49.048 13.303 1.00139.71 C ANISOU 881 CG LEU A 131 16114 12322 24649 -5100 -4050 -1420 C ATOM 882 CD1 LEU A 131 45.018 48.914 12.095 1.00146.77 C ANISOU 882 CD1 LEU A 131 16980 13429 25356 -5647 -3785 -1041 C ATOM 883 CD2 LEU A 131 43.003 50.053 13.032 1.00147.59 C ANISOU 883 CD2 LEU A 131 17509 12778 25791 -4950 -4336 -1314 C ATOM 884 N SER A 132 43.304 45.161 11.771 1.00134.28 N ANISOU 884 N SER A 132 15054 12597 23368 -4837 -3226 -991 N ATOM 885 CA SER A 132 43.872 44.523 10.588 1.00131.59 C ANISOU 885 CA SER A 132 14637 12569 22790 -5183 -2930 -648 C ATOM 886 C SER A 132 42.789 44.006 9.648 1.00133.52 C ANISOU 886 C SER A 132 15091 12721 22917 -5063 -2842 -361 C ATOM 887 O SER A 132 42.805 44.306 8.449 1.00148.55 O ANISOU 887 O SER A 132 17181 14570 24690 -5359 -2764 0 O ATOM 888 CB SER A 132 44.801 43.380 11.004 1.00127.98 C ANISOU 888 CB SER A 132 13751 12675 22198 -5155 -2678 -826 C ATOM 889 OG SER A 132 45.918 43.864 11.726 1.00152.94 O ANISOU 889 OG SER A 132 16695 15964 25452 -5329 -2746 -1069 O ATOM 890 N TYR A 133 41.841 43.226 10.174 1.00109.49 N ANISOU 890 N TYR A 133 12026 9710 19867 -4600 -2825 -525 N ATOM 891 CA TYR A 133 40.869 42.560 9.313 1.00109.34 C ANISOU 891 CA TYR A 133 12170 9708 19668 -4448 -2684 -280 C ATOM 892 C TYR A 133 39.900 43.555 8.686 1.00124.93 C ANISOU 892 C TYR A 133 14523 11154 21792 -4504 -2940 -76 C ATOM 893 O TYR A 133 39.644 43.504 7.477 1.00144.85 O ANISOU 893 O TYR A 133 17213 13665 24159 -4680 -2836 269 O ATOM 894 CB TYR A 133 40.111 41.491 10.098 1.00115.57 C ANISOU 894 CB TYR A 133 12867 10747 20297 -3884 -2546 -514 C ATOM 895 CG TYR A 133 39.057 40.782 9.277 1.00114.59 C ANISOU 895 CG TYR A 133 12899 10637 20004 -3714 -2411 -295 C ATOM 896 CD1 TYR A 133 39.414 39.884 8.280 1.00101.92 C ANISOU 896 CD1 TYR A 133 11218 9365 18143 -3869 -2120 -52 C ATOM 897 CD2 TYR A 133 37.706 41.005 9.505 1.00118.21 C ANISOU 897 CD2 TYR A 133 13562 10799 20552 -3388 -2584 -357 C ATOM 898 CE1 TYR A 133 38.454 39.233 7.529 1.00106.35 C ANISOU 898 CE1 TYR A 133 11912 9939 18557 -3712 -2008 127 C ATOM 899 CE2 TYR A 133 36.740 40.357 8.760 1.00118.77 C ANISOU 899 CE2 TYR A 133 13759 10898 20471 -3240 -2464 -174 C ATOM 900 CZ TYR A 133 37.120 39.473 7.774 1.00111.19 C ANISOU 900 CZ TYR A 133 12728 10247 19272 -3407 -2178 68 C ATOM 901 OH TYR A 133 36.162 38.827 7.029 1.00113.53 O ANISOU 901 OH TYR A 133 13142 10569 19424 -3259 -2070 230 O ATOM 902 N ARG A 134 39.346 44.465 9.490 1.00122.76 N ANISOU 902 N ARG A 134 14400 10520 21725 -4276 -3242 -303 N ATOM 903 CA ARG A 134 38.422 45.454 8.944 1.00138.95 C ANISOU 903 CA ARG A 134 16824 12138 23833 -4231 -3466 -140 C ATOM 904 C ARG A 134 39.094 46.403 7.962 1.00133.55 C ANISOU 904 C ARG A 134 16319 11319 23104 -4688 -3479 180 C ATOM 905 O ARG A 134 38.398 47.061 7.183 1.00145.75 O ANISOU 905 O ARG A 134 18167 12568 24644 -4707 -3603 408 O ATOM 906 CB ARG A 134 37.765 46.255 10.069 1.00152.33 C ANISOU 906 CB ARG A 134 18607 13513 25757 -3873 -3803 -486 C ATOM 907 CG ARG A 134 36.709 45.488 10.844 1.00153.33 C ANISOU 907 CG ARG A 134 18644 13702 25913 -3377 -3831 -761 C ATOM 908 CD ARG A 134 36.098 46.358 11.927 1.00173.59 C ANISOU 908 CD ARG A 134 21281 15996 28678 -3022 -4174 -1118 C ATOM 909 NE ARG A 134 35.487 47.560 11.362 1.00190.78 N ANISOU 909 NE ARG A 134 23802 17759 30928 -3041 -4433 -962 N ATOM 910 CZ ARG A 134 34.251 47.622 10.876 1.00184.34 C ANISOU 910 CZ ARG A 134 23197 16770 30073 -2811 -4527 -868 C ATOM 911 NH1 ARG A 134 33.477 46.545 10.875 1.00170.23 N ANISOU 911 NH1 ARG A 134 21320 15181 28179 -2559 -4373 -907 N ATOM 912 NH2 ARG A 134 33.790 48.764 10.384 1.00185.70 N ANISOU 912 NH2 ARG A 134 23665 16575 30318 -2833 -4781 -739 N ATOM 913 N ALA A 135 40.426 46.488 7.979 1.00131.73 N ANISOU 913 N ALA A 135 15897 11315 22839 -5053 -3354 194 N ATOM 914 CA ALA A 135 41.120 47.350 7.029 1.00140.92 C ANISOU 914 CA ALA A 135 17202 12388 23953 -5516 -3338 500 C ATOM 915 C ALA A 135 40.947 46.862 5.597 1.00137.42 C ANISOU 915 C ALA A 135 16844 12108 23263 -5702 -3114 900 C ATOM 916 O ALA A 135 41.012 47.661 4.657 1.00155.12 O ANISOU 916 O ALA A 135 19303 14166 25469 -5973 -3159 1198 O ATOM 917 CB ALA A 135 42.603 47.438 7.385 1.00131.06 C ANISOU 917 CB ALA A 135 15679 11415 22701 -5864 -3226 398 C ATOM 918 N LYS A 136 40.728 45.562 5.408 1.00140.96 N ANISOU 918 N LYS A 136 17116 12901 23541 -5553 -2881 911 N ATOM 919 CA LYS A 136 40.580 44.972 4.083 1.00159.40 C ANISOU 919 CA LYS A 136 19492 15448 25625 -5697 -2658 1256 C ATOM 920 C LYS A 136 39.221 44.303 3.909 1.00156.67 C ANISOU 920 C LYS A 136 19270 15011 25245 -5311 -2673 1269 C ATOM 921 O LYS A 136 39.076 43.384 3.103 1.00162.24 O ANISOU 921 O LYS A 136 19908 15994 25743 -5328 -2451 1449 O ATOM 922 CB LYS A 136 41.705 43.973 3.812 1.00158.69 C ANISOU 922 CB LYS A 136 19047 15924 25323 -5928 -2334 1287 C ATOM 923 N ARG A 137 38.216 44.758 4.659 1.00153.53 N ANISOU 923 N ARG A 137 19041 14246 25046 -4956 -2936 1065 N ATOM 924 CA ARG A 137 36.890 44.139 4.667 1.00135.84 C ANISOU 924 CA ARG A 137 16889 11927 22797 -4561 -2965 1016 C ATOM 925 C ARG A 137 35.985 44.941 3.732 1.00136.79 C ANISOU 925 C ARG A 137 17364 11714 22898 -4548 -3131 1263 C ATOM 926 O ARG A 137 35.153 45.748 4.153 1.00129.64 O ANISOU 926 O ARG A 137 16663 10439 22155 -4304 -3418 1136 O ATOM 927 CB ARG A 137 36.351 44.076 6.096 1.00123.68 C ANISOU 927 CB ARG A 137 15268 10261 21464 -4155 -3140 607 C ATOM 928 CG ARG A 137 35.053 43.308 6.271 1.00121.70 C ANISOU 928 CG ARG A 137 15041 9992 21206 -3742 -3141 502 C ATOM 929 CD ARG A 137 34.714 43.176 7.750 1.00115.92 C ANISOU 929 CD ARG A 137 14164 9238 20643 -3362 -3271 74 C ATOM 930 NE ARG A 137 33.511 42.382 7.985 1.00114.93 N ANISOU 930 NE ARG A 137 14034 9256 20377 -2909 -3183 -44 N ATOM 931 CZ ARG A 137 32.287 42.889 8.085 1.00116.24 C ANISOU 931 CZ ARG A 137 14398 9117 20651 -2635 -3428 -129 C ATOM 932 NH1 ARG A 137 31.251 42.090 8.301 1.00109.46 N ANISOU 932 NH1 ARG A 137 13494 8454 19642 -2255 -3316 -235 N ATOM 933 NH2 ARG A 137 32.098 44.197 7.975 1.00120.20 N ANISOU 933 NH2 ARG A 137 15137 9192 21342 -2706 -3757 -112 N ATOM 934 N THR A 138 36.163 44.706 2.429 1.00137.52 N ANISOU 934 N THR A 138 17511 11967 22776 -4803 -2953 1611 N ATOM 935 CA THR A 138 35.535 45.467 1.363 1.00151.62 C ANISOU 935 CA THR A 138 19606 13494 24509 -4871 -3081 1900 C ATOM 936 C THR A 138 34.479 44.628 0.641 1.00151.96 C ANISOU 936 C THR A 138 19709 13628 24400 -4650 -2985 2014 C ATOM 937 O THR A 138 34.575 43.398 0.605 1.00153.78 O ANISOU 937 O THR A 138 19720 14205 24505 -4596 -2739 1981 O ATOM 938 CB THR A 138 36.592 45.948 0.356 1.00161.81 C ANISOU 938 CB THR A 138 20911 14907 25662 -5357 -2965 2227 C ATOM 939 OG1 THR A 138 36.000 46.826 -0.603 1.00174.37 O ANISOU 939 OG1 THR A 138 22817 16205 27231 -5421 -3132 2505 O ATOM 940 CG2 THR A 138 37.224 44.769 -0.366 1.00151.83 C ANISOU 940 CG2 THR A 138 19398 14161 24131 -5542 -2608 2379 C ATOM 941 N PRO A 139 33.446 45.261 0.067 1.00153.48 N ANISOU 941 N PRO A 139 20193 13515 24609 -4509 -3186 2139 N ATOM 942 CA PRO A 139 32.423 44.492 -0.669 1.00134.40 C ANISOU 942 CA PRO A 139 17832 11186 22046 -4307 -3104 2244 C ATOM 943 C PRO A 139 32.959 43.739 -1.879 1.00132.14 C ANISOU 943 C PRO A 139 17445 11271 21493 -4588 -2812 2550 C ATOM 944 O PRO A 139 32.205 42.966 -2.481 1.00144.24 O ANISOU 944 O PRO A 139 18985 12923 22898 -4435 -2717 2625 O ATOM 945 CB PRO A 139 31.412 45.570 -1.091 1.00125.91 C ANISOU 945 CB PRO A 139 17097 9700 21045 -4163 -3412 2332 C ATOM 946 CG PRO A 139 31.584 46.657 -0.089 1.00143.47 C ANISOU 946 CG PRO A 139 19397 11604 23510 -4105 -3685 2117 C ATOM 947 CD PRO A 139 33.057 46.678 0.214 1.00151.54 C ANISOU 947 CD PRO A 139 20225 12815 24540 -4465 -3531 2131 C ATOM 948 N ARG A 140 34.225 43.932 -2.249 1.00135.48 N ANISOU 948 N ARG A 140 17757 11899 21821 -4985 -2671 2714 N ATOM 949 CA ARG A 140 34.826 43.210 -3.362 1.00131.44 C ANISOU 949 CA ARG A 140 17104 11805 21032 -5250 -2390 2977 C ATOM 950 C ARG A 140 35.406 41.871 -2.919 1.00134.17 C ANISOU 950 C ARG A 140 17099 12590 21292 -5220 -2116 2809 C ATOM 951 O ARG A 140 35.164 40.843 -3.559 1.00135.67 O ANISOU 951 O ARG A 140 17180 13070 21297 -5167 -1927 2893 O ATOM 952 CB ARG A 140 35.912 44.068 -4.014 1.00138.47 C ANISOU 952 CB ARG A 140 18021 12748 21843 -5692 -2369 3232 C ATOM 953 CG ARG A 140 36.630 43.406 -5.175 1.00143.97 C ANISOU 953 CG ARG A 140 18545 13929 22229 -5979 -2085 3497 C ATOM 954 CD ARG A 140 35.683 43.163 -6.334 1.00151.22 C ANISOU 954 CD ARG A 140 19629 14849 22977 -5883 -2086 3739 C ATOM 955 NE ARG A 140 36.379 42.622 -7.495 1.00162.90 N ANISOU 955 NE ARG A 140 20944 16808 24141 -6160 -1835 3998 N ATOM 956 CZ ARG A 140 36.899 43.372 -8.460 1.00171.16 C ANISOU 956 CZ ARG A 140 22080 17906 25049 -6492 -1842 4316 C ATOM 957 NH1 ARG A 140 37.520 42.803 -9.484 1.00180.48 N ANISOU 957 NH1 ARG A 140 23075 19582 25918 -6717 -1606 4524 N ATOM 958 NH2 ARG A 140 36.792 44.692 -8.403 1.00175.81 N ANISOU 958 NH2 ARG A 140 22936 18059 25803 -6594 -2094 4424 N ATOM 959 N ARG A 141 36.170 41.870 -1.823 1.00137.70 N ANISOU 959 N ARG A 141 17360 13088 21872 -5247 -2106 2565 N ATOM 960 CA ARG A 141 36.749 40.627 -1.326 1.00120.61 C ANISOU 960 CA ARG A 141 14853 11332 19640 -5203 -1870 2391 C ATOM 961 C ARG A 141 35.680 39.704 -0.757 1.00123.74 C ANISOU 961 C ARG A 141 15217 11677 20120 -4789 -1876 2192 C ATOM 962 O ARG A 141 35.838 38.479 -0.796 1.00117.73 O ANISOU 962 O ARG A 141 14240 11342 19148 -4620 -1609 2088 O ATOM 963 CB ARG A 141 37.820 40.929 -0.276 1.00119.32 C ANISOU 963 CB ARG A 141 14501 11227 19608 -5327 -1884 2173 C ATOM 964 CG ARG A 141 39.022 41.681 -0.833 1.00123.84 C ANISOU 964 CG ARG A 141 15038 11931 20083 -5768 -1829 2356 C ATOM 965 CD ARG A 141 40.089 41.910 0.225 1.00146.02 C ANISOU 965 CD ARG A 141 17632 14827 23022 -5887 -1837 2112 C ATOM 966 NE ARG A 141 41.146 42.803 -0.246 1.00155.20 N ANISOU 966 NE ARG A 141 18791 16043 24137 -6308 -1822 2275 N ATOM 967 CZ ARG A 141 42.234 42.405 -0.897 1.00148.65 C ANISOU 967 CZ ARG A 141 17717 15686 23077 -6612 -1578 2397 C ATOM 968 NH1 ARG A 141 42.421 41.118 -1.164 1.00142.95 N ANISOU 968 NH1 ARG A 141 16739 15432 22141 -6529 -1336 2368 N ATOM 969 NH2 ARG A 141 43.138 43.297 -1.282 1.00129.50 N ANISOU 969 NH2 ARG A 141 15294 13277 20635 -6989 -1582 2542 N ATOM 970 N ALA A 142 34.588 40.267 -0.234 1.00123.39 N ANISOU 970 N ALA A 142 15396 11221 20266 -4501 -2121 2065 N ATOM 971 CA ALA A 142 33.480 39.433 0.221 1.00105.09 C ANISOU 971 CA ALA A 142 13063 8941 17927 -4038 -2079 1849 C ATOM 972 C ALA A 142 32.795 38.735 -0.946 1.00115.15 C ANISOU 972 C ALA A 142 14397 10379 18977 -3969 -1937 2042 C ATOM 973 O ALA A 142 32.229 37.649 -0.772 1.00113.16 O ANISOU 973 O ALA A 142 14036 10359 18600 -3652 -1772 1886 O ATOM 974 CB ALA A 142 32.472 40.272 1.005 1.00 96.18 C ANISOU 974 CB ALA A 142 12138 7350 17055 -3772 -2400 1669 C ATOM 975 N ALA A 143 32.836 39.338 -2.137 1.00111.45 N ANISOU 975 N ALA A 143 14100 9794 18451 -4269 -2006 2385 N ATOM 976 CA ALA A 143 32.312 38.669 -3.322 1.00106.11 C ANISOU 976 CA ALA A 143 13455 9328 17535 -4228 -1860 2572 C ATOM 977 C ALA A 143 33.157 37.453 -3.679 1.00115.12 C ANISOU 977 C ALA A 143 14299 11033 18409 -4289 -1518 2557 C ATOM 978 O ALA A 143 32.618 36.394 -4.019 1.00116.98 O ANISOU 978 O ALA A 143 14457 11513 18476 -4044 -1353 2486 O ATOM 979 CB ALA A 143 32.255 39.645 -4.496 1.00101.11 C ANISOU 979 CB ALA A 143 13067 8494 16855 -4519 -2002 2939 C ATOM 980 N LEU A 144 34.484 37.590 -3.614 1.00109.61 N ANISOU 980 N LEU A 144 13426 10551 17671 -4612 -1421 2608 N ATOM 981 CA LEU A 144 35.359 36.446 -3.847 1.00120.65 C ANISOU 981 CA LEU A 144 14520 12503 18818 -4638 -1116 2543 C ATOM 982 C LEU A 144 35.116 35.350 -2.819 1.00116.33 C ANISOU 982 C LEU A 144 13811 12111 18278 -4225 -996 2186 C ATOM 983 O LEU A 144 35.135 34.160 -3.153 1.00125.87 O ANISOU 983 O LEU A 144 14866 13677 19283 -4062 -785 2114 O ATOM 984 CB LEU A 144 36.823 36.886 -3.825 1.00122.22 C ANISOU 984 CB LEU A 144 14545 12904 18990 -5051 -1059 2625 C ATOM 985 CG LEU A 144 37.440 37.404 -5.130 1.00132.94 C ANISOU 985 CG LEU A 144 15919 14417 20174 -5512 -1023 3006 C ATOM 986 CD1 LEU A 144 37.423 36.308 -6.187 1.00134.16 C ANISOU 986 CD1 LEU A 144 15930 15052 19993 -5433 -780 3074 C ATOM 987 CD2 LEU A 144 36.753 38.664 -5.640 1.00134.27 C ANISOU 987 CD2 LEU A 144 16450 14121 20447 -5609 -1266 3243 C ATOM 988 N MET A 145 34.884 35.732 -1.560 1.00111.88 N ANISOU 988 N MET A 145 13282 11282 17945 -4051 -1140 1962 N ATOM 989 CA MET A 145 34.578 34.743 -0.533 1.00119.61 C ANISOU 989 CA MET A 145 14126 12394 18926 -3661 -1040 1651 C ATOM 990 C MET A 145 33.271 34.021 -0.836 1.00121.33 C ANISOU 990 C MET A 145 14442 12576 19082 -3341 -1010 1624 C ATOM 991 O MET A 145 33.188 32.794 -0.710 1.00109.24 O ANISOU 991 O MET A 145 12768 11321 17417 -3121 -824 1492 O ATOM 992 CB MET A 145 34.517 35.414 0.840 1.00106.57 C ANISOU 992 CB MET A 145 12498 10473 17522 -3539 -1222 1428 C ATOM 993 CG MET A 145 35.844 35.982 1.322 1.00118.15 C ANISOU 993 CG MET A 145 13824 12010 19059 -3817 -1240 1387 C ATOM 994 SD MET A 145 37.115 34.722 1.546 1.00144.62 S ANISOU 994 SD MET A 145 16822 15947 22181 -3805 -933 1243 S ATOM 995 CE MET A 145 38.115 34.973 0.081 1.00150.56 C ANISOU 995 CE MET A 145 17506 16956 22743 -4294 -823 1561 C ATOM 996 N ILE A 146 32.241 34.764 -1.247 1.00110.15 N ANISOU 996 N ILE A 146 13271 10817 17764 -3313 -1204 1742 N ATOM 997 CA ILE A 146 30.975 34.133 -1.605 1.00110.17 C ANISOU 997 CA ILE A 146 13357 10800 17703 -3030 -1184 1715 C ATOM 998 C ILE A 146 31.124 33.324 -2.888 1.00110.97 C ANISOU 998 C ILE A 146 13396 11214 17555 -3119 -992 1881 C ATOM 999 O ILE A 146 30.568 32.225 -3.011 1.00110.79 O ANISOU 999 O ILE A 146 13301 11369 17424 -2882 -858 1777 O ATOM 1000 CB ILE A 146 29.861 35.190 -1.723 1.00111.87 C ANISOU 1000 CB ILE A 146 13843 10584 18079 -2961 -1461 1778 C ATOM 1001 CG1 ILE A 146 29.567 35.810 -0.355 1.00107.69 C ANISOU 1001 CG1 ILE A 146 13343 9792 17781 -2779 -1652 1538 C ATOM 1002 CG2 ILE A 146 28.604 34.582 -2.321 1.00 95.84 C ANISOU 1002 CG2 ILE A 146 11888 8576 15953 -2718 -1435 1781 C ATOM 1003 CD1 ILE A 146 28.683 37.033 -0.418 1.00110.39 C ANISOU 1003 CD1 ILE A 146 13951 9687 18303 -2733 -1972 1580 C ATOM 1004 N GLY A 147 31.883 33.842 -3.856 1.00113.53 N ANISOU 1004 N GLY A 147 13737 11621 17780 -3467 -980 2137 N ATOM 1005 CA GLY A 147 32.056 33.123 -5.107 1.00105.72 C ANISOU 1005 CA GLY A 147 12670 10971 16530 -3547 -806 2285 C ATOM 1006 C GLY A 147 32.780 31.802 -4.933 1.00111.87 C ANISOU 1006 C GLY A 147 13175 12186 17146 -3443 -557 2108 C ATOM 1007 O GLY A 147 32.384 30.785 -5.509 1.00120.95 O ANISOU 1007 O GLY A 147 14263 13551 18140 -3273 -432 2063 O ATOM 1008 N LEU A 148 33.849 31.797 -4.133 1.00105.56 N ANISOU 1008 N LEU A 148 12208 11516 16383 -3532 -500 1989 N ATOM 1009 CA LEU A 148 34.584 30.560 -3.887 1.00113.80 C ANISOU 1009 CA LEU A 148 12999 12962 17278 -3405 -290 1801 C ATOM 1010 C LEU A 148 33.764 29.563 -3.079 1.00114.92 C ANISOU 1010 C LEU A 148 13136 13047 17481 -3005 -255 1560 C ATOM 1011 O LEU A 148 33.879 28.351 -3.295 1.00112.03 O ANISOU 1011 O LEU A 148 12640 12956 16969 -2840 -102 1452 O ATOM 1012 CB LEU A 148 35.905 30.864 -3.177 1.00104.48 C ANISOU 1012 CB LEU A 148 11643 11930 16126 -3585 -256 1721 C ATOM 1013 CG LEU A 148 37.135 31.135 -4.051 1.00120.90 C ANISOU 1013 CG LEU A 148 13566 14351 18018 -3959 -161 1889 C ATOM 1014 CD1 LEU A 148 37.525 29.877 -4.810 1.00122.51 C ANISOU 1014 CD1 LEU A 148 13572 15034 17944 -3855 45 1827 C ATOM 1015 CD2 LEU A 148 36.904 32.286 -5.020 1.00136.63 C ANISOU 1015 CD2 LEU A 148 15745 16150 20017 -4290 -284 2223 C ATOM 1016 N ALA A 149 32.933 30.046 -2.152 1.00107.36 N ANISOU 1016 N ALA A 149 12315 11744 16734 -2846 -402 1471 N ATOM 1017 CA ALA A 149 32.104 29.143 -1.361 1.00103.99 C ANISOU 1017 CA ALA A 149 11877 11279 16354 -2495 -368 1268 C ATOM 1018 C ALA A 149 31.105 28.399 -2.240 1.00112.23 C ANISOU 1018 C ALA A 149 12987 12354 17299 -2354 -319 1313 C ATOM 1019 O ALA A 149 30.901 27.191 -2.076 1.00 96.53 O ANISOU 1019 O ALA A 149 10910 10523 15243 -2146 -199 1182 O ATOM 1020 CB ALA A 149 31.383 29.923 -0.262 1.00 97.07 C ANISOU 1020 CB ALA A 149 11117 10066 15698 -2367 -547 1168 C ATOM 1021 N TRP A 150 30.472 29.105 -3.179 1.00111.55 N ANISOU 1021 N TRP A 150 13062 12113 17209 -2464 -424 1496 N ATOM 1022 CA TRP A 150 29.586 28.457 -4.139 1.00105.76 C ANISOU 1022 CA TRP A 150 12378 11441 16365 -2350 -382 1540 C ATOM 1023 C TRP A 150 30.343 27.636 -5.175 1.00111.94 C ANISOU 1023 C TRP A 150 13016 12598 16916 -2441 -214 1593 C ATOM 1024 O TRP A 150 29.757 26.726 -5.771 1.00114.04 O ANISOU 1024 O TRP A 150 13264 12981 17087 -2289 -146 1545 O ATOM 1025 CB TRP A 150 28.712 29.503 -4.834 1.00 92.25 C ANISOU 1025 CB TRP A 150 10884 9463 14703 -2423 -561 1717 C ATOM 1026 CG TRP A 150 27.529 29.933 -4.024 1.00 98.77 C ANISOU 1026 CG TRP A 150 11843 9970 15716 -2210 -723 1604 C ATOM 1027 CD1 TRP A 150 27.482 30.937 -3.101 1.00115.22 C ANISOU 1027 CD1 TRP A 150 14010 11781 17987 -2214 -893 1558 C ATOM 1028 CD2 TRP A 150 26.202 29.399 -4.103 1.00103.53 C ANISOU 1028 CD2 TRP A 150 12494 10518 16326 -1961 -743 1508 C ATOM 1029 NE1 TRP A 150 26.214 31.041 -2.579 1.00118.44 N ANISOU 1029 NE1 TRP A 150 14504 11994 18502 -1962 -1013 1427 N ATOM 1030 CE2 TRP A 150 25.409 30.110 -3.181 1.00115.78 C ANISOU 1030 CE2 TRP A 150 14144 11793 18055 -1816 -918 1402 C ATOM 1031 CE3 TRP A 150 25.610 28.380 -4.857 1.00101.42 C ANISOU 1031 CE3 TRP A 150 12183 10422 15931 -1845 -636 1484 C ATOM 1032 CZ2 TRP A 150 24.056 29.836 -2.994 1.00117.98 C ANISOU 1032 CZ2 TRP A 150 14463 11993 18372 -1570 -976 1280 C ATOM 1033 CZ3 TRP A 150 24.267 28.111 -4.670 1.00109.99 C ANISOU 1033 CZ3 TRP A 150 13319 11399 17073 -1618 -696 1370 C ATOM 1034 CH2 TRP A 150 23.505 28.835 -3.746 1.00112.32 C ANISOU 1034 CH2 TRP A 150 13698 11448 17531 -1488 -858 1274 C ATOM 1035 N LEU A 151 31.625 27.927 -5.399 1.00112.95 N ANISOU 1035 N LEU A 151 13027 12939 16950 -2682 -151 1672 N ATOM 1036 CA LEU A 151 32.392 27.154 -6.369 1.00111.77 C ANISOU 1036 CA LEU A 151 12708 13203 16556 -2753 5 1694 C ATOM 1037 C LEU A 151 32.784 25.792 -5.808 1.00118.15 C ANISOU 1037 C LEU A 151 13341 14234 17316 -2518 139 1443 C ATOM 1038 O LEU A 151 32.617 24.767 -6.479 1.00113.52 O ANISOU 1038 O LEU A 151 12685 13855 16592 -2381 223 1372 O ATOM 1039 CB LEU A 151 33.632 27.935 -6.805 1.00116.93 C ANISOU 1039 CB LEU A 151 13271 14053 17103 -3105 29 1862 C ATOM 1040 CG LEU A 151 34.493 27.243 -7.862 1.00115.81 C ANISOU 1040 CG LEU A 151 12923 14407 16673 -3196 188 1886 C ATOM 1041 CD1 LEU A 151 33.691 27.000 -9.132 1.00112.14 C ANISOU 1041 CD1 LEU A 151 12536 14011 16061 -3151 186 2004 C ATOM 1042 CD2 LEU A 151 35.734 28.069 -8.158 1.00103.83 C ANISOU 1042 CD2 LEU A 151 11292 13104 15053 -3574 216 2052 C ATOM 1043 N VAL A 152 33.309 25.760 -4.581 1.00110.06 N ANISOU 1043 N VAL A 152 12249 13165 16405 -2460 144 1302 N ATOM 1044 CA VAL A 152 33.693 24.486 -3.982 1.00108.25 C ANISOU 1044 CA VAL A 152 11877 13119 16134 -2226 251 1078 C ATOM 1045 C VAL A 152 32.464 23.621 -3.727 1.00107.97 C ANISOU 1045 C VAL A 152 11941 12906 16178 -1944 238 979 C ATOM 1046 O VAL A 152 32.519 22.393 -3.861 1.00118.48 O ANISOU 1046 O VAL A 152 13192 14395 17428 -1765 319 849 O ATOM 1047 CB VAL A 152 34.510 24.714 -2.696 1.00109.81 C ANISOU 1047 CB VAL A 152 11987 13310 16426 -2221 248 959 C ATOM 1048 CG1 VAL A 152 35.798 25.451 -3.017 1.00124.81 C ANISOU 1048 CG1 VAL A 152 13754 15436 18231 -2520 274 1040 C ATOM 1049 CG2 VAL A 152 33.697 25.479 -1.663 1.00116.69 C ANISOU 1049 CG2 VAL A 152 13010 13803 17524 -2162 117 953 C ATOM 1050 N SER A 153 31.337 24.242 -3.368 1.00112.07 N ANISOU 1050 N SER A 153 12628 13099 16856 -1904 126 1030 N ATOM 1051 CA SER A 153 30.100 23.487 -3.193 1.00110.07 C ANISOU 1051 CA SER A 153 12453 12702 16668 -1674 115 949 C ATOM 1052 C SER A 153 29.696 22.796 -4.487 1.00102.81 C ANISOU 1052 C SER A 153 11531 11919 15613 -1646 160 979 C ATOM 1053 O SER A 153 29.214 21.658 -4.470 1.00 96.58 O ANISOU 1053 O SER A 153 10720 11156 14819 -1459 206 860 O ATOM 1054 CB SER A 153 28.980 24.409 -2.709 1.00104.03 C ANISOU 1054 CB SER A 153 11846 11612 16068 -1648 -25 994 C ATOM 1055 OG SER A 153 29.256 24.927 -1.419 1.00100.27 O ANISOU 1055 OG SER A 153 11359 11020 15719 -1623 -76 922 O ATOM 1056 N PHE A 154 29.897 23.468 -5.621 1.00102.81 N ANISOU 1056 N PHE A 154 11552 12011 15499 -1836 139 1140 N ATOM 1057 CA PHE A 154 29.571 22.875 -6.913 1.00104.22 C ANISOU 1057 CA PHE A 154 11711 12364 15522 -1808 177 1164 C ATOM 1058 C PHE A 154 30.526 21.736 -7.253 1.00110.51 C ANISOU 1058 C PHE A 154 12322 13507 16159 -1741 300 1029 C ATOM 1059 O PHE A 154 30.092 20.637 -7.615 1.00122.79 O ANISOU 1059 O PHE A 154 13849 15128 17678 -1560 330 901 O ATOM 1060 CB PHE A 154 29.610 23.953 -7.995 1.00105.51 C ANISOU 1060 CB PHE A 154 11945 12562 15582 -2037 121 1395 C ATOM 1061 CG PHE A 154 29.228 23.465 -9.362 1.00103.39 C ANISOU 1061 CG PHE A 154 11657 12492 15135 -2006 149 1430 C ATOM 1062 CD1 PHE A 154 27.898 23.292 -9.704 1.00 90.84 C ANISOU 1062 CD1 PHE A 154 10184 10731 13598 -1860 78 1410 C ATOM 1063 CD2 PHE A 154 30.201 23.181 -10.306 1.00115.11 C ANISOU 1063 CD2 PHE A 154 12985 14369 16382 -2114 242 1464 C ATOM 1064 CE1 PHE A 154 27.545 22.850 -10.968 1.00 97.57 C ANISOU 1064 CE1 PHE A 154 11010 11781 14282 -1819 95 1424 C ATOM 1065 CE2 PHE A 154 29.856 22.734 -11.567 1.00112.05 C ANISOU 1065 CE2 PHE A 154 12565 14197 15813 -2067 261 1478 C ATOM 1066 CZ PHE A 154 28.527 22.568 -11.898 1.00109.01 C ANISOU 1066 CZ PHE A 154 12308 13619 15494 -1917 185 1457 C ATOM 1067 N VAL A 155 31.834 21.980 -7.132 1.00 97.31 N ANISOU 1067 N VAL A 155 10517 12063 14395 -1879 358 1039 N ATOM 1068 CA VAL A 155 32.825 20.998 -7.564 1.00103.46 C ANISOU 1068 CA VAL A 155 11098 13223 14989 -1813 459 900 C ATOM 1069 C VAL A 155 32.757 19.731 -6.718 1.00106.05 C ANISOU 1069 C VAL A 155 11395 13497 15401 -1533 482 669 C ATOM 1070 O VAL A 155 33.010 18.629 -7.220 1.00118.81 O ANISOU 1070 O VAL A 155 12914 15323 16905 -1378 521 519 O ATOM 1071 CB VAL A 155 34.231 21.627 -7.539 1.00106.71 C ANISOU 1071 CB VAL A 155 11356 13906 15283 -2037 512 955 C ATOM 1072 CG1 VAL A 155 35.296 20.598 -7.895 1.00101.33 C ANISOU 1072 CG1 VAL A 155 10445 13655 14399 -1934 607 770 C ATOM 1073 CG2 VAL A 155 34.293 22.809 -8.494 1.00114.65 C ANISOU 1073 CG2 VAL A 155 12401 14971 16188 -2342 486 1218 C ATOM 1074 N LEU A 156 32.410 19.853 -5.435 1.00 99.80 N ANISOU 1074 N LEU A 156 10690 12427 14803 -1457 445 637 N ATOM 1075 CA LEU A 156 32.323 18.671 -4.582 1.00103.75 C ANISOU 1075 CA LEU A 156 11180 12861 15378 -1207 461 457 C ATOM 1076 C LEU A 156 31.204 17.739 -5.034 1.00108.55 C ANISOU 1076 C LEU A 156 11872 13345 16028 -1046 438 400 C ATOM 1077 O LEU A 156 31.428 16.543 -5.254 1.00 96.77 O ANISOU 1077 O LEU A 156 10323 11964 14484 -879 457 250 O ATOM 1078 CB LEU A 156 32.119 19.078 -3.122 1.00 95.44 C ANISOU 1078 CB LEU A 156 10196 11565 14501 -1171 428 456 C ATOM 1079 CG LEU A 156 33.283 19.736 -2.380 1.00105.70 C ANISOU 1079 CG LEU A 156 11396 12976 15789 -1271 444 444 C ATOM 1080 CD1 LEU A 156 32.845 20.182 -0.992 1.00104.53 C ANISOU 1080 CD1 LEU A 156 11327 12571 15817 -1212 392 437 C ATOM 1081 CD2 LEU A 156 34.472 18.791 -2.294 1.00105.61 C ANISOU 1081 CD2 LEU A 156 11221 13260 15647 -1154 510 282 C ATOM 1082 N TRP A 157 29.992 18.270 -5.187 1.00105.85 N ANISOU 1082 N TRP A 157 11664 12771 15785 -1089 382 504 N ATOM 1083 CA TRP A 157 28.804 17.437 -5.342 1.00109.78 C ANISOU 1083 CA TRP A 157 12240 13109 16361 -944 353 441 C ATOM 1084 C TRP A 157 28.328 17.295 -6.782 1.00100.64 C ANISOU 1084 C TRP A 157 11081 12064 15094 -964 338 457 C ATOM 1085 O TRP A 157 27.946 16.194 -7.189 1.00105.90 O ANISOU 1085 O TRP A 157 11733 12748 15756 -824 335 330 O ATOM 1086 CB TRP A 157 27.658 17.994 -4.492 1.00 99.03 C ANISOU 1086 CB TRP A 157 11005 11450 15174 -940 297 505 C ATOM 1087 CG TRP A 157 27.925 17.938 -3.022 1.00 99.41 C ANISOU 1087 CG TRP A 157 11050 11394 15326 -875 308 465 C ATOM 1088 CD1 TRP A 157 28.316 18.970 -2.221 1.00100.39 C ANISOU 1088 CD1 TRP A 157 11178 11466 15499 -957 285 521 C ATOM 1089 CD2 TRP A 157 27.841 16.784 -2.177 1.00104.22 C ANISOU 1089 CD2 TRP A 157 11655 11947 15999 -712 335 362 C ATOM 1090 NE1 TRP A 157 28.466 18.535 -0.928 1.00 99.87 N ANISOU 1090 NE1 TRP A 157 11095 11343 15507 -840 304 449 N ATOM 1091 CE2 TRP A 157 28.183 17.196 -0.874 1.00 88.39 C ANISOU 1091 CE2 TRP A 157 9643 9885 14058 -694 337 368 C ATOM 1092 CE3 TRP A 157 27.504 15.443 -2.396 1.00 91.87 C ANISOU 1092 CE3 TRP A 157 10099 10361 14446 -582 345 269 C ATOM 1093 CZ2 TRP A 157 28.200 16.317 0.206 1.00 81.60 C ANISOU 1093 CZ2 TRP A 157 8784 8969 13251 -551 359 305 C ATOM 1094 CZ3 TRP A 157 27.520 14.572 -1.321 1.00 91.69 C ANISOU 1094 CZ3 TRP A 157 10095 10246 14497 -456 357 217 C ATOM 1095 CH2 TRP A 157 27.865 15.012 -0.037 1.00100.35 C ANISOU 1095 CH2 TRP A 157 11185 11309 15635 -441 369 246 C ATOM 1096 N ALA A 158 28.335 18.378 -7.564 1.00106.99 N ANISOU 1096 N ALA A 158 11904 12937 15809 -1134 317 611 N ATOM 1097 CA ALA A 158 27.688 18.347 -8.875 1.00108.40 C ANISOU 1097 CA ALA A 158 12102 13202 15884 -1140 289 644 C ATOM 1098 C ALA A 158 28.314 17.339 -9.832 1.00112.94 C ANISOU 1098 C ALA A 158 12536 14096 16282 -1055 336 508 C ATOM 1099 O ALA A 158 27.583 16.479 -10.356 1.00117.79 O ANISOU 1099 O ALA A 158 13156 14691 16906 -915 309 389 O ATOM 1100 CB ALA A 158 27.661 19.758 -9.467 1.00109.24 C ANISOU 1100 CB ALA A 158 12273 13314 15919 -1346 246 867 C ATOM 1101 N PRO A 159 29.624 17.369 -10.112 1.00114.78 N ANISOU 1101 N PRO A 159 12624 14640 16346 -1122 398 498 N ATOM 1102 CA PRO A 159 30.160 16.373 -11.052 1.00111.90 C ANISOU 1102 CA PRO A 159 12110 14610 15799 -1002 426 330 C ATOM 1103 C PRO A 159 30.075 14.954 -10.521 1.00120.06 C ANISOU 1103 C PRO A 159 13131 15546 16941 -754 405 87 C ATOM 1104 O PRO A 159 30.010 14.011 -11.318 1.00123.75 O ANISOU 1104 O PRO A 159 13529 16164 17325 -605 380 -82 O ATOM 1105 CB PRO A 159 31.614 16.820 -11.252 1.00111.09 C ANISOU 1105 CB PRO A 159 11840 14872 15499 -1142 497 371 C ATOM 1106 CG PRO A 159 31.956 17.525 -10.007 1.00122.43 C ANISOU 1106 CG PRO A 159 13333 16104 17081 -1249 507 461 C ATOM 1107 CD PRO A 159 30.698 18.219 -9.563 1.00118.59 C ANISOU 1107 CD PRO A 159 13052 15211 16795 -1295 439 601 C ATOM 1108 N ALA A 160 30.056 14.774 -9.200 1.00117.20 N ANISOU 1108 N ALA A 160 12840 14928 16762 -703 402 67 N ATOM 1109 CA ALA A 160 29.974 13.430 -8.641 1.00 99.99 C ANISOU 1109 CA ALA A 160 10677 12623 14693 -483 370 -127 C ATOM 1110 C ALA A 160 28.567 12.858 -8.774 1.00112.38 C ANISOU 1110 C ALA A 160 12366 13921 16412 -406 309 -160 C ATOM 1111 O ALA A 160 28.396 11.718 -9.214 1.00114.97 O ANISOU 1111 O ALA A 160 12677 14257 16750 -248 260 -336 O ATOM 1112 CB ALA A 160 30.418 13.441 -7.177 1.00 98.99 C ANISOU 1112 CB ALA A 160 10586 12338 14689 -457 388 -116 C ATOM 1113 N ILE A 161 27.548 13.636 -8.405 1.00100.15 N ANISOU 1113 N ILE A 161 10933 12137 14983 -512 298 -9 N ATOM 1114 CA ILE A 161 26.177 13.135 -8.473 1.00 95.69 C ANISOU 1114 CA ILE A 161 10460 11341 14558 -455 245 -46 C ATOM 1115 C ILE A 161 25.763 12.889 -9.921 1.00 95.61 C ANISOU 1115 C ILE A 161 10404 11490 14432 -425 208 -118 C ATOM 1116 O ILE A 161 25.069 11.910 -10.224 1.00103.92 O ANISOU 1116 O ILE A 161 11471 12450 15562 -316 155 -259 O ATOM 1117 CB ILE A 161 25.217 14.107 -7.761 1.00 97.96 C ANISOU 1117 CB ILE A 161 10853 11396 14970 -559 235 110 C ATOM 1118 CG1 ILE A 161 25.529 14.164 -6.264 1.00 95.83 C ANISOU 1118 CG1 ILE A 161 10617 10978 14817 -552 262 145 C ATOM 1119 CG2 ILE A 161 23.769 13.702 -7.984 1.00 90.24 C ANISOU 1119 CG2 ILE A 161 9938 10245 14103 -520 183 68 C ATOM 1120 CD1 ILE A 161 24.775 15.251 -5.530 1.00103.96 C ANISOU 1120 CD1 ILE A 161 11723 11835 15941 -640 244 275 C ATOM 1121 N LEU A 162 26.192 13.757 -10.838 1.00 98.30 N ANISOU 1121 N LEU A 162 10685 12080 14584 -527 230 -22 N ATOM 1122 CA LEU A 162 25.784 13.623 -12.233 1.00121.15 C ANISOU 1122 CA LEU A 162 13530 15162 17339 -496 196 -74 C ATOM 1123 C LEU A 162 26.573 12.557 -12.983 1.00116.56 C ANISOU 1123 C LEU A 162 12806 14863 16617 -348 189 -291 C ATOM 1124 O LEU A 162 26.034 11.941 -13.909 1.00120.19 O ANISOU 1124 O LEU A 162 13230 15402 17034 -244 134 -430 O ATOM 1125 CB LEU A 162 25.922 14.962 -12.964 1.00117.98 C ANISOU 1125 CB LEU A 162 13128 14932 16768 -668 213 139 C ATOM 1126 CG LEU A 162 24.760 15.955 -12.880 1.00117.20 C ANISOU 1126 CG LEU A 162 13173 14597 16761 -757 162 306 C ATOM 1127 CD1 LEU A 162 24.648 16.562 -11.500 1.00113.29 C ANISOU 1127 CD1 LEU A 162 12778 13816 16452 -826 165 406 C ATOM 1128 CD2 LEU A 162 24.922 17.044 -13.930 1.00127.77 C ANISOU 1128 CD2 LEU A 162 14514 16137 17896 -895 153 498 C ATOM 1129 N PHE A 163 27.832 12.322 -12.617 1.00103.58 N ANISOU 1129 N PHE A 163 11068 13390 14897 -320 232 -349 N ATOM 1130 CA PHE A 163 28.714 11.518 -13.449 1.00110.01 C ANISOU 1130 CA PHE A 163 11716 14558 15522 -178 220 -558 C ATOM 1131 C PHE A 163 29.302 10.302 -12.746 1.00111.08 C ANISOU 1131 C PHE A 163 11833 14616 15756 21 178 -779 C ATOM 1132 O PHE A 163 30.135 9.611 -13.345 1.00117.65 O ANISOU 1132 O PHE A 163 12520 15751 16432 172 151 -986 O ATOM 1133 CB PHE A 163 29.854 12.388 -13.997 1.00123.56 C ANISOU 1133 CB PHE A 163 13284 16695 16970 -318 302 -447 C ATOM 1134 CG PHE A 163 29.382 13.535 -14.845 1.00129.09 C ANISOU 1134 CG PHE A 163 14007 17502 17540 -509 325 -218 C ATOM 1135 CD1 PHE A 163 29.019 13.340 -16.167 1.00136.08 C ANISOU 1135 CD1 PHE A 163 14819 18637 18250 -451 294 -280 C ATOM 1136 CD2 PHE A 163 29.295 14.811 -14.311 1.00124.52 C ANISOU 1136 CD2 PHE A 163 13531 16764 17016 -735 361 55 C ATOM 1137 CE1 PHE A 163 28.581 14.398 -16.942 1.00137.71 C ANISOU 1137 CE1 PHE A 163 15063 18936 18325 -617 305 -50 C ATOM 1138 CE2 PHE A 163 28.859 15.870 -15.080 1.00125.96 C ANISOU 1138 CE2 PHE A 163 13764 17007 17089 -903 357 279 C ATOM 1139 CZ PHE A 163 28.502 15.664 -16.397 1.00132.58 C ANISOU 1139 CZ PHE A 163 14538 18097 17740 -845 332 238 C ATOM 1140 N TRP A 164 28.908 10.016 -11.502 1.00112.12 N ANISOU 1140 N TRP A 164 12105 14368 16127 37 163 -744 N ATOM 1141 CA TRP A 164 29.414 8.815 -10.842 1.00108.36 C ANISOU 1141 CA TRP A 164 11641 13786 15747 235 102 -935 C ATOM 1142 C TRP A 164 28.926 7.559 -11.548 1.00117.51 C ANISOU 1142 C TRP A 164 12805 14885 16960 427 -17 -1175 C ATOM 1143 O TRP A 164 29.674 6.582 -11.678 1.00125.20 O ANISOU 1143 O TRP A 164 13715 15964 17893 633 -94 -1406 O ATOM 1144 CB TRP A 164 28.989 8.778 -9.378 1.00103.81 C ANISOU 1144 CB TRP A 164 11220 12820 15401 199 110 -817 C ATOM 1145 CG TRP A 164 29.635 7.667 -8.628 1.00117.50 C ANISOU 1145 CG TRP A 164 12980 14452 17211 392 48 -968 C ATOM 1146 CD1 TRP A 164 29.102 6.442 -8.349 1.00122.29 C ANISOU 1146 CD1 TRP A 164 13699 14770 17995 532 -59 -1087 C ATOM 1147 CD2 TRP A 164 30.942 7.678 -8.047 1.00126.14 C ANISOU 1147 CD2 TRP A 164 13996 15724 18209 465 75 -1015 C ATOM 1148 NE1 TRP A 164 30.003 5.686 -7.637 1.00115.78 N ANISOU 1148 NE1 TRP A 164 12889 13916 17188 702 -110 -1194 N ATOM 1149 CE2 TRP A 164 31.140 6.425 -7.437 1.00127.08 C ANISOU 1149 CE2 TRP A 164 14195 15644 18445 677 -27 -1163 C ATOM 1150 CE3 TRP A 164 31.967 8.628 -7.986 1.00115.58 C ANISOU 1150 CE3 TRP A 164 12526 14692 16697 366 167 -946 C ATOM 1151 CZ2 TRP A 164 32.320 6.096 -6.775 1.00116.79 C ANISOU 1151 CZ2 TRP A 164 12843 14453 17079 821 -42 -1256 C ATOM 1152 CZ3 TRP A 164 33.135 8.301 -7.327 1.00112.93 C ANISOU 1152 CZ3 TRP A 164 12121 14485 16302 491 163 -1049 C ATOM 1153 CH2 TRP A 164 33.303 7.046 -6.730 1.00117.14 C ANISOU 1153 CH2 TRP A 164 12737 14830 16944 732 58 -1208 C ATOM 1154 N GLN A 165 27.666 7.562 -11.992 1.00116.47 N ANISOU 1154 N GLN A 165 12746 14578 16927 372 -51 -1144 N ATOM 1155 CA GLN A 165 27.139 6.443 -12.763 1.00113.49 C ANISOU 1155 CA GLN A 165 12364 14153 16606 534 -174 -1383 C ATOM 1156 C GLN A 165 27.967 6.188 -14.015 1.00124.35 C ANISOU 1156 C GLN A 165 13550 15975 17724 677 -208 -1594 C ATOM 1157 O GLN A 165 28.094 5.039 -14.453 1.00132.24 O ANISOU 1157 O GLN A 165 14513 16983 18748 892 -335 -1872 O ATOM 1158 CB GLN A 165 25.678 6.712 -13.129 1.00 99.21 C ANISOU 1158 CB GLN A 165 10630 12162 14905 425 -188 -1305 C ATOM 1159 CG GLN A 165 25.479 7.944 -13.998 1.00102.40 C ANISOU 1159 CG GLN A 165 10962 12835 15109 291 -114 -1156 C ATOM 1160 CD GLN A 165 24.021 8.232 -14.282 1.00122.21 C ANISOU 1160 CD GLN A 165 13549 15163 17724 209 -140 -1090 C ATOM 1161 OE1 GLN A 165 23.138 7.473 -13.886 1.00121.46 O ANISOU 1161 OE1 GLN A 165 13537 14766 17848 237 -206 -1171 O ATOM 1162 NE2 GLN A 165 23.760 9.338 -14.968 1.00136.32 N ANISOU 1162 NE2 GLN A 165 15307 17136 19352 100 -95 -939 N ATOM 1163 N TYR A 166 28.542 7.241 -14.596 1.00129.16 N ANISOU 1163 N TYR A 166 14032 16964 18081 561 -105 -1468 N ATOM 1164 CA TYR A 166 29.419 7.087 -15.747 1.00122.62 C ANISOU 1164 CA TYR A 166 12991 16639 16961 677 -115 -1645 C ATOM 1165 C TYR A 166 30.829 6.679 -15.346 1.00119.07 C ANISOU 1165 C TYR A 166 12425 16412 16406 806 -114 -1787 C ATOM 1166 O TYR A 166 31.545 6.087 -16.161 1.00118.30 O ANISOU 1166 O TYR A 166 12149 16688 16111 996 -172 -2043 O ATOM 1167 CB TYR A 166 29.461 8.391 -16.548 1.00119.93 C ANISOU 1167 CB TYR A 166 12560 16631 16375 470 -5 -1420 C ATOM 1168 CG TYR A 166 28.123 8.794 -17.126 1.00130.97 C ANISOU 1168 CG TYR A 166 14052 17882 17830 384 -25 -1313 C ATOM 1169 CD1 TYR A 166 27.646 8.218 -18.296 1.00136.57 C ANISOU 1169 CD1 TYR A 166 14679 18768 18445 529 -110 -1514 C ATOM 1170 CD2 TYR A 166 27.336 9.752 -16.499 1.00145.69 C ANISOU 1170 CD2 TYR A 166 16075 19444 19835 180 27 -1033 C ATOM 1171 CE1 TYR A 166 26.421 8.585 -18.825 1.00148.08 C ANISOU 1171 CE1 TYR A 166 16211 20109 19944 465 -135 -1431 C ATOM 1172 CE2 TYR A 166 26.112 10.125 -17.021 1.00149.51 C ANISOU 1172 CE2 TYR A 166 16635 19810 20360 126 -4 -955 C ATOM 1173 CZ TYR A 166 25.659 9.539 -18.183 1.00152.15 C ANISOU 1173 CZ TYR A 166 16886 20327 20596 265 -82 -1150 C ATOM 1174 OH TYR A 166 24.441 9.908 -18.705 1.00159.77 O ANISOU 1174 OH TYR A 166 17918 21194 21593 225 -118 -1087 O ATOM 1175 N LEU A 167 31.239 6.980 -14.112 1.00113.11 N ANISOU 1175 N LEU A 167 11753 15459 15763 726 -56 -1645 N ATOM 1176 CA LEU A 167 32.576 6.608 -13.658 1.00124.76 C ANISOU 1176 CA LEU A 167 13117 17145 17140 860 -60 -1787 C ATOM 1177 C LEU A 167 32.667 5.111 -13.390 1.00134.89 C ANISOU 1177 C LEU A 167 14459 18225 18567 1166 -228 -2086 C ATOM 1178 O LEU A 167 33.577 4.436 -13.885 1.00147.60 O ANISOU 1178 O LEU A 167 15911 20155 20016 1395 -305 -2365 O ATOM 1179 CB LEU A 167 32.945 7.403 -12.406 1.00121.30 C ANISOU 1179 CB LEU A 167 12751 16554 16782 689 42 -1552 C ATOM 1180 CG LEU A 167 34.346 7.150 -11.844 1.00118.40 C ANISOU 1180 CG LEU A 167 12260 16419 16306 811 49 -1683 C ATOM 1181 CD1 LEU A 167 35.408 7.556 -12.852 1.00124.22 C ANISOU 1181 CD1 LEU A 167 12721 17778 16699 789 110 -1770 C ATOM 1182 CD2 LEU A 167 34.539 7.889 -10.532 1.00112.29 C ANISOU 1182 CD2 LEU A 167 11579 15438 15649 652 133 -1461 C ATOM 1183 N VAL A 168 31.733 4.572 -12.601 1.00127.99 N ANISOU 1183 N VAL A 168 13811 16824 17996 1173 -297 -2033 N ATOM 1184 CA VAL A 168 31.728 3.139 -12.314 1.00121.07 C ANISOU 1184 CA VAL A 168 13032 15679 17291 1435 -477 -2281 C ATOM 1185 C VAL A 168 31.177 2.312 -13.463 1.00123.34 C ANISOU 1185 C VAL A 168 13284 15995 17586 1591 -619 -2538 C ATOM 1186 O VAL A 168 31.297 1.080 -13.438 1.00142.61 O ANISOU 1186 O VAL A 168 15781 18259 20144 1837 -802 -2797 O ATOM 1187 CB VAL A 168 30.924 2.835 -11.036 1.00115.56 C ANISOU 1187 CB VAL A 168 12585 14416 16905 1357 -499 -2106 C ATOM 1188 CG1 VAL A 168 31.573 3.498 -9.832 1.00 97.94 C ANISOU 1188 CG1 VAL A 168 10381 12170 14663 1263 -387 -1906 C ATOM 1189 CG2 VAL A 168 29.484 3.296 -11.193 1.00125.96 C ANISOU 1189 CG2 VAL A 168 14003 15495 18362 1139 -451 -1919 C ATOM 1190 N GLY A 169 30.579 2.948 -14.467 1.00114.26 N ANISOU 1190 N GLY A 169 12047 15051 16316 1464 -557 -2481 N ATOM 1191 CA GLY A 169 30.076 2.240 -15.626 1.00107.31 C ANISOU 1191 CA GLY A 169 11105 14256 15414 1617 -688 -2740 C ATOM 1192 C GLY A 169 28.693 1.651 -15.477 1.00113.63 C ANISOU 1192 C GLY A 169 12092 14563 16517 1576 -786 -2737 C ATOM 1193 O GLY A 169 28.252 0.916 -16.368 1.00117.35 O ANISOU 1193 O GLY A 169 12524 15053 17012 1721 -925 -2990 O ATOM 1194 N GLU A 170 27.989 1.953 -14.390 1.00117.42 N ANISOU 1194 N GLU A 170 12760 14632 17222 1379 -720 -2470 N ATOM 1195 CA GLU A 170 26.675 1.374 -14.158 1.00116.08 C ANISOU 1195 CA GLU A 170 12754 14012 17340 1312 -804 -2456 C ATOM 1196 C GLU A 170 25.870 2.300 -13.258 1.00117.05 C ANISOU 1196 C GLU A 170 12993 13905 17575 1034 -658 -2106 C ATOM 1197 O GLU A 170 26.432 3.072 -12.477 1.00123.33 O ANISOU 1197 O GLU A 170 13797 14756 18305 937 -534 -1901 O ATOM 1198 CB GLU A 170 26.785 -0.019 -13.528 1.00118.82 C ANISOU 1198 CB GLU A 170 13246 13974 17927 1481 -986 -2628 C ATOM 1199 CG GLU A 170 27.417 -0.013 -12.146 1.00120.22 C ANISOU 1199 CG GLU A 170 13541 13960 18179 1463 -940 -2456 C ATOM 1200 CD GLU A 170 27.563 -1.403 -11.565 1.00134.77 C ANISOU 1200 CD GLU A 170 15545 15418 20244 1643 -1140 -2609 C ATOM 1201 OE1 GLU A 170 27.177 -2.376 -12.247 1.00142.27 O ANISOU 1201 OE1 GLU A 170 16519 16229 21308 1776 -1325 -2861 O ATOM 1202 OE2 GLU A 170 28.068 -1.523 -10.429 1.00136.93 O ANISOU 1202 OE2 GLU A 170 15928 15519 20579 1655 -1125 -2480 O ATOM 1203 N ARG A 171 24.550 2.211 -13.382 1.00111.32 N ANISOU 1203 N ARG A 171 12341 12940 17015 917 -683 -2064 N ATOM 1204 CA ARG A 171 23.615 2.963 -12.551 1.00 92.41 C ANISOU 1204 CA ARG A 171 10047 10323 14743 678 -573 -1778 C ATOM 1205 C ARG A 171 22.910 1.963 -11.641 1.00102.81 C ANISOU 1205 C ARG A 171 11527 11180 16357 642 -659 -1770 C ATOM 1206 O ARG A 171 21.996 1.256 -12.073 1.00119.24 O ANISOU 1206 O ARG A 171 13635 13082 18588 635 -764 -1898 O ATOM 1207 CB ARG A 171 22.621 3.739 -13.410 1.00 93.28 C ANISOU 1207 CB ARG A 171 10095 10567 14780 564 -529 -1728 C ATOM 1208 CG ARG A 171 21.683 4.613 -12.607 1.00 76.44 C ANISOU 1208 CG ARG A 171 8043 8255 12744 347 -427 -1461 C ATOM 1209 CD ARG A 171 20.757 5.437 -13.485 1.00 95.13 C ANISOU 1209 CD ARG A 171 10352 10773 15019 266 -401 -1421 C ATOM 1210 NE ARG A 171 19.857 6.244 -12.667 1.00104.07 N ANISOU 1210 NE ARG A 171 11558 11738 16247 91 -326 -1199 N ATOM 1211 CZ ARG A 171 20.170 7.435 -12.168 1.00 98.51 C ANISOU 1211 CZ ARG A 171 10870 11112 15448 -4 -223 -980 C ATOM 1212 NH1 ARG A 171 19.295 8.098 -11.426 1.00102.52 N ANISOU 1212 NH1 ARG A 171 11437 11469 16049 -131 -180 -820 N ATOM 1213 NH2 ARG A 171 21.359 7.964 -12.412 1.00116.84 N ANISOU 1213 NH2 ARG A 171 13138 13675 17582 29 -173 -934 N ATOM 1214 N THR A 172 23.336 1.906 -10.382 1.00103.39 N ANISOU 1214 N THR A 172 11702 11071 16509 610 -618 -1613 N ATOM 1215 CA THR A 172 22.827 0.919 -9.440 1.00108.79 C ANISOU 1215 CA THR A 172 12550 11335 17452 572 -700 -1571 C ATOM 1216 C THR A 172 21.650 1.428 -8.621 1.00 98.05 C ANISOU 1216 C THR A 172 11252 9787 16215 326 -600 -1323 C ATOM 1217 O THR A 172 21.085 0.659 -7.836 1.00 96.42 O ANISOU 1217 O THR A 172 11170 9252 16213 247 -652 -1252 O ATOM 1218 CB THR A 172 23.941 0.465 -8.492 1.00111.38 C ANISOU 1218 CB THR A 172 12958 11576 17785 697 -727 -1543 C ATOM 1219 OG1 THR A 172 24.359 1.570 -7.682 1.00116.54 O ANISOU 1219 OG1 THR A 172 13587 12372 18322 603 -561 -1315 O ATOM 1220 CG2 THR A 172 25.130 -0.046 -9.285 1.00 92.02 C ANISOU 1220 CG2 THR A 172 10421 9349 15194 965 -835 -1820 C ATOM 1221 N VAL A 173 21.270 2.698 -8.778 1.00 92.61 N ANISOU 1221 N VAL A 173 10481 9304 15401 206 -469 -1189 N ATOM 1222 CA VAL A 173 20.133 3.231 -8.040 1.00 90.76 C ANISOU 1222 CA VAL A 173 10283 8939 15264 3 -387 -989 C ATOM 1223 C VAL A 173 18.864 2.521 -8.491 1.00 89.82 C ANISOU 1223 C VAL A 173 10174 8645 15311 -79 -472 -1088 C ATOM 1224 O VAL A 173 18.669 2.247 -9.683 1.00103.15 O ANISOU 1224 O VAL A 173 11793 10431 16969 -3 -553 -1291 O ATOM 1225 CB VAL A 173 20.037 4.758 -8.219 1.00110.84 C ANISOU 1225 CB VAL A 173 12743 11734 17637 -73 -265 -859 C ATOM 1226 CG1 VAL A 173 19.800 5.117 -9.662 1.00124.72 C ANISOU 1226 CG1 VAL A 173 14400 13717 19269 -30 -295 -994 C ATOM 1227 CG2 VAL A 173 18.928 5.333 -7.354 1.00111.16 C ANISOU 1227 CG2 VAL A 173 12810 11660 17765 -246 -194 -679 C ATOM 1228 N LEU A 174 18.008 2.190 -7.526 1.00100.14 N ANISOU 1228 N LEU A 174 11553 9710 16787 -238 -456 -952 N ATOM 1229 CA LEU A 174 16.808 1.413 -7.810 1.00 88.05 C ANISOU 1229 CA LEU A 174 10028 7991 15436 -352 -538 -1035 C ATOM 1230 C LEU A 174 15.920 2.136 -8.817 1.00 91.75 C ANISOU 1230 C LEU A 174 10369 8666 15824 -390 -519 -1124 C ATOM 1231 O LEU A 174 15.788 3.363 -8.787 1.00 94.81 O ANISOU 1231 O LEU A 174 10695 9260 16066 -418 -413 -1013 O ATOM 1232 CB LEU A 174 16.056 1.132 -6.508 1.00 87.99 C ANISOU 1232 CB LEU A 174 10093 7760 15578 -552 -491 -826 C ATOM 1233 CG LEU A 174 14.797 0.266 -6.529 1.00 87.60 C ANISOU 1233 CG LEU A 174 10054 7495 15736 -732 -563 -862 C ATOM 1234 CD1 LEU A 174 15.085 -1.108 -7.117 1.00 93.48 C ANISOU 1234 CD1 LEU A 174 10883 7993 16641 -649 -750 -1062 C ATOM 1235 CD2 LEU A 174 14.265 0.131 -5.110 1.00 94.82 C ANISOU 1235 CD2 LEU A 174 11026 8264 16739 -934 -486 -606 C ATOM 1236 N ALA A 175 15.311 1.355 -9.717 1.00 92.67 N ANISOU 1236 N ALA A 175 10453 8715 16042 -379 -639 -1336 N ATOM 1237 CA ALA A 175 14.700 1.915 -10.921 1.00 89.86 C ANISOU 1237 CA ALA A 175 9971 8593 15577 -345 -652 -1478 C ATOM 1238 C ALA A 175 13.599 2.917 -10.594 1.00125.66 C ANISOU 1238 C ALA A 175 14444 13223 20077 -497 -551 -1336 C ATOM 1239 O ALA A 175 13.469 3.946 -11.268 1.00138.55 O ANISOU 1239 O ALA A 175 16001 15105 21535 -443 -512 -1339 O ATOM 1240 CB ALA A 175 14.151 0.794 -11.800 1.00108.99 C ANISOU 1240 CB ALA A 175 12368 10898 18145 -316 -812 -1745 C ATOM 1241 N GLY A 176 12.794 2.639 -9.575 1.00110.30 N ANISOU 1241 N GLY A 176 12528 11095 18285 -681 -517 -1212 N ATOM 1242 CA GLY A 176 11.704 3.538 -9.249 1.00116.93 C ANISOU 1242 CA GLY A 176 13287 12054 19086 -804 -436 -1114 C ATOM 1243 C GLY A 176 12.006 4.528 -8.142 1.00104.71 C ANISOU 1243 C GLY A 176 11768 10572 17447 -836 -312 -879 C ATOM 1244 O GLY A 176 11.087 5.136 -7.591 1.00 88.30 O ANISOU 1244 O GLY A 176 9628 8562 15361 -942 -254 -795 O ATOM 1245 N GLN A 177 13.280 4.711 -7.808 1.00 97.46 N ANISOU 1245 N GLN A 177 10925 9654 16451 -735 -278 -793 N ATOM 1246 CA GLN A 177 13.666 5.521 -6.661 1.00 90.82 C ANISOU 1246 CA GLN A 177 10115 8849 15545 -762 -174 -586 C ATOM 1247 C GLN A 177 14.682 6.574 -7.094 1.00 97.30 C ANISOU 1247 C GLN A 177 10935 9856 16179 -631 -141 -560 C ATOM 1248 O GLN A 177 15.123 6.610 -8.247 1.00 90.29 O ANISOU 1248 O GLN A 177 10022 9085 15201 -528 -189 -683 O ATOM 1249 CB GLN A 177 14.219 4.641 -5.533 1.00 97.20 C ANISOU 1249 CB GLN A 177 11022 9450 16461 -802 -162 -475 C ATOM 1250 CG GLN A 177 13.241 3.577 -5.053 1.00105.97 C ANISOU 1250 CG GLN A 177 12147 10357 17758 -972 -196 -458 C ATOM 1251 CD GLN A 177 11.992 4.158 -4.416 1.00103.80 C ANISOU 1251 CD GLN A 177 11776 10180 17482 -1132 -121 -363 C ATOM 1252 OE1 GLN A 177 12.058 5.145 -3.684 1.00106.87 O ANISOU 1252 OE1 GLN A 177 12135 10707 17763 -1121 -34 -238 O ATOM 1253 NE2 GLN A 177 10.846 3.546 -4.691 1.00101.67 N ANISOU 1253 NE2 GLN A 177 11444 9855 17331 -1277 -163 -440 N ATOM 1254 N CYS A 178 15.061 7.434 -6.148 1.00 90.88 N ANISOU 1254 N CYS A 178 10141 9086 15304 -645 -62 -397 N ATOM 1255 CA CYS A 178 15.930 8.570 -6.451 1.00 98.66 C ANISOU 1255 CA CYS A 178 11124 10237 16126 -567 -31 -345 C ATOM 1256 C CYS A 178 16.817 8.844 -5.243 1.00102.15 C ANISOU 1256 C CYS A 178 11613 10646 16555 -563 35 -205 C ATOM 1257 O CYS A 178 16.321 9.267 -4.193 1.00110.16 O ANISOU 1257 O CYS A 178 12624 11629 17603 -627 79 -98 O ATOM 1258 CB CYS A 178 15.103 9.803 -6.813 1.00 94.11 C ANISOU 1258 CB CYS A 178 10502 9785 15471 -590 -33 -318 C ATOM 1259 SG CYS A 178 16.071 11.254 -7.293 1.00105.27 S ANISOU 1259 SG CYS A 178 11933 11365 16698 -534 -20 -228 S ATOM 1260 N TYR A 179 18.121 8.615 -5.395 1.00 86.09 N ANISOU 1260 N TYR A 179 9603 8649 14458 -476 37 -224 N ATOM 1261 CA TYR A 179 19.094 8.900 -4.346 1.00 91.50 C ANISOU 1261 CA TYR A 179 10320 9334 15112 -452 93 -116 C ATOM 1262 C TYR A 179 20.492 8.886 -4.951 1.00 87.53 C ANISOU 1262 C TYR A 179 9800 8964 14491 -352 87 -179 C ATOM 1263 O TYR A 179 20.693 8.467 -6.094 1.00 89.27 O ANISOU 1263 O TYR A 179 9990 9267 14662 -292 37 -310 O ATOM 1264 CB TYR A 179 18.978 7.910 -3.179 1.00 85.56 C ANISOU 1264 CB TYR A 179 9626 8397 14485 -472 100 -60 C ATOM 1265 CG TYR A 179 19.063 6.450 -3.572 1.00 98.59 C ANISOU 1265 CG TYR A 179 11328 9895 16235 -428 22 -170 C ATOM 1266 CD1 TYR A 179 17.910 5.720 -3.836 1.00 94.19 C ANISOU 1266 CD1 TYR A 179 10777 9204 15808 -516 -27 -218 C ATOM 1267 CD2 TYR A 179 20.287 5.803 -3.680 1.00 98.80 C ANISOU 1267 CD2 TYR A 179 11393 9912 16233 -294 -19 -243 C ATOM 1268 CE1 TYR A 179 17.971 4.387 -4.191 1.00 97.42 C ANISOU 1268 CE1 TYR A 179 11246 9435 16333 -482 -124 -327 C ATOM 1269 CE2 TYR A 179 20.359 4.469 -4.038 1.00104.80 C ANISOU 1269 CE2 TYR A 179 12213 10507 17097 -230 -123 -365 C ATOM 1270 CZ TYR A 179 19.197 3.766 -4.294 1.00106.64 C ANISOU 1270 CZ TYR A 179 12469 10571 17478 -329 -180 -403 C ATOM 1271 OH TYR A 179 19.257 2.438 -4.652 1.00106.91 O ANISOU 1271 OH TYR A 179 12575 10404 17640 -270 -308 -534 O ATOM 1272 N ILE A 180 21.458 9.375 -4.173 1.00 93.66 N ANISOU 1272 N ILE A 180 10581 9796 15210 -331 136 -98 N ATOM 1273 CA ILE A 180 22.835 9.446 -4.648 1.00 92.35 C ANISOU 1273 CA ILE A 180 10372 9803 14915 -250 142 -156 C ATOM 1274 C ILE A 180 23.440 8.049 -4.680 1.00 98.10 C ANISOU 1274 C ILE A 180 11125 10464 15683 -120 85 -286 C ATOM 1275 O ILE A 180 23.423 7.321 -3.678 1.00 94.51 O ANISOU 1275 O ILE A 180 10744 9832 15335 -90 73 -251 O ATOM 1276 CB ILE A 180 23.667 10.390 -3.769 1.00 92.67 C ANISOU 1276 CB ILE A 180 10396 9923 14892 -275 203 -47 C ATOM 1277 CG1 ILE A 180 23.156 11.824 -3.889 1.00 98.34 C ANISOU 1277 CG1 ILE A 180 11101 10691 15571 -388 224 60 C ATOM 1278 CG2 ILE A 180 25.128 10.327 -4.159 1.00 89.94 C ANISOU 1278 CG2 ILE A 180 9985 9777 14412 -199 213 -121 C ATOM 1279 CD1 ILE A 180 23.818 12.765 -2.920 1.00109.18 C ANISOU 1279 CD1 ILE A 180 12465 12099 16919 -422 263 155 C ATOM 1280 N GLN A 181 24.000 7.680 -5.834 1.00100.69 N ANISOU 1280 N GLN A 181 11394 10948 15916 -31 39 -440 N ATOM 1281 CA GLN A 181 24.461 6.311 -6.041 1.00106.22 C ANISOU 1281 CA GLN A 181 12119 11576 16664 123 -53 -610 C ATOM 1282 C GLN A 181 25.674 5.984 -5.177 1.00105.89 C ANISOU 1282 C GLN A 181 12093 11550 16590 237 -50 -616 C ATOM 1283 O GLN A 181 25.777 4.872 -4.645 1.00101.67 O ANISOU 1283 O GLN A 181 11650 10813 16167 339 -129 -669 O ATOM 1284 CB GLN A 181 24.770 6.090 -7.522 1.00101.78 C ANISOU 1284 CB GLN A 181 11460 11234 15978 213 -108 -800 C ATOM 1285 CG GLN A 181 25.242 4.693 -7.877 1.00 90.78 C ANISOU 1285 CG GLN A 181 10081 9782 14629 406 -236 -1027 C ATOM 1286 CD GLN A 181 25.408 4.509 -9.373 1.00111.88 C ANISOU 1286 CD GLN A 181 12636 12706 17166 503 -295 -1235 C ATOM 1287 OE1 GLN A 181 25.136 5.421 -10.153 1.00121.53 O ANISOU 1287 OE1 GLN A 181 13774 14145 18257 411 -233 -1182 O ATOM 1288 NE2 GLN A 181 25.871 3.333 -9.780 1.00120.23 N ANISOU 1288 NE2 GLN A 181 13689 13744 18248 702 -428 -1476 N ATOM 1289 N PHE A 182 26.600 6.929 -5.017 1.00113.99 N ANISOU 1289 N PHE A 182 13036 12808 17468 219 28 -562 N ATOM 1290 CA PHE A 182 27.819 6.677 -4.258 1.00114.02 C ANISOU 1290 CA PHE A 182 13027 12878 17418 339 29 -594 C ATOM 1291 C PHE A 182 27.664 6.937 -2.762 1.00105.31 C ANISOU 1291 C PHE A 182 12004 11605 16402 289 78 -424 C ATOM 1292 O PHE A 182 28.657 6.873 -2.030 1.00 95.00 O ANISOU 1292 O PHE A 182 10683 10369 15044 384 86 -436 O ATOM 1293 CB PHE A 182 28.986 7.491 -4.832 1.00111.74 C ANISOU 1293 CB PHE A 182 12583 12957 16917 339 85 -641 C ATOM 1294 CG PHE A 182 28.754 8.974 -4.857 1.00109.18 C ANISOU 1294 CG PHE A 182 12215 12736 16534 136 182 -469 C ATOM 1295 CD1 PHE A 182 28.193 9.579 -5.970 1.00121.75 C ANISOU 1295 CD1 PHE A 182 13767 14433 18061 28 193 -442 C ATOM 1296 CD2 PHE A 182 29.117 9.766 -3.781 1.00110.40 C ANISOU 1296 CD2 PHE A 182 12373 12878 16696 66 243 -343 C ATOM 1297 CE1 PHE A 182 27.988 10.947 -6.005 1.00127.26 C ANISOU 1297 CE1 PHE A 182 14451 15190 18713 -150 254 -276 C ATOM 1298 CE2 PHE A 182 28.911 11.135 -3.809 1.00102.73 C ANISOU 1298 CE2 PHE A 182 11376 11965 15690 -113 301 -199 C ATOM 1299 CZ PHE A 182 28.344 11.725 -4.921 1.00113.68 C ANISOU 1299 CZ PHE A 182 12745 13426 17023 -222 301 -158 C ATOM 1300 N LEU A 183 26.447 7.219 -2.292 1.00 99.32 N ANISOU 1300 N LEU A 183 11315 10660 15763 155 106 -283 N ATOM 1301 CA LEU A 183 26.113 7.145 -0.874 1.00 71.32 C ANISOU 1301 CA LEU A 183 7848 6942 12307 129 134 -140 C ATOM 1302 C LEU A 183 25.238 5.938 -0.555 1.00107.96 C ANISOU 1302 C LEU A 183 12610 11302 17106 132 67 -117 C ATOM 1303 O LEU A 183 24.653 5.873 0.531 1.00114.22 O ANISOU 1303 O LEU A 183 13463 11961 17973 67 97 30 O ATOM 1304 CB LEU A 183 25.422 8.426 -0.403 1.00101.32 C ANISOU 1304 CB LEU A 183 11617 10775 16105 -23 214 4 C ATOM 1305 CG LEU A 183 26.276 9.596 0.091 1.00115.80 C ANISOU 1305 CG LEU A 183 13376 12788 17836 -41 274 50 C ATOM 1306 CD1 LEU A 183 27.045 10.255 -1.032 1.00108.13 C ANISOU 1306 CD1 LEU A 183 12309 12040 16735 -65 283 -25 C ATOM 1307 CD2 LEU A 183 25.403 10.618 0.806 1.00115.50 C ANISOU 1307 CD2 LEU A 183 13339 12706 17841 -156 315 177 C ATOM 1308 N SER A 184 25.140 4.979 -1.477 1.00112.68 N ANISOU 1308 N SER A 184 13238 11820 17756 199 -28 -260 N ATOM 1309 CA SER A 184 24.288 3.813 -1.281 1.00123.21 C ANISOU 1309 CA SER A 184 14691 12859 19262 173 -111 -244 C ATOM 1310 C SER A 184 24.993 2.763 -0.432 1.00148.33 C ANISOU 1310 C SER A 184 17993 15870 22494 313 -191 -232 C ATOM 1311 O SER A 184 25.082 1.594 -0.819 1.00173.52 O ANISOU 1311 O SER A 184 21274 18878 25779 414 -327 -349 O ATOM 1312 CB SER A 184 23.875 3.219 -2.629 1.00150.60 C ANISOU 1312 CB SER A 184 18146 16296 22781 195 -204 -426 C ATOM 1313 OG SER A 184 24.995 2.685 -3.313 1.00170.01 O ANISOU 1313 OG SER A 184 20577 18859 25161 398 -293 -630 O ATOM 1314 N GLN A 185 25.498 3.180 0.731 1.00127.15 N ANISOU 1314 N GLN A 185 15320 13241 19750 334 -123 -99 N ATOM 1315 CA GLN A 185 26.123 2.305 1.702 1.00124.66 C ANISOU 1315 CA GLN A 185 15126 12776 19463 468 -192 -49 C ATOM 1316 C GLN A 185 25.965 3.007 3.044 1.00122.00 C ANISOU 1316 C GLN A 185 14779 12494 19080 387 -79 161 C ATOM 1317 O GLN A 185 26.217 4.218 3.126 1.00102.38 O ANISOU 1317 O GLN A 185 12169 10246 16486 349 23 169 O ATOM 1318 CB GLN A 185 27.593 2.031 1.393 1.00124.20 C ANISOU 1318 CB GLN A 185 15036 12861 19293 713 -264 -239 C ATOM 1319 CG GLN A 185 28.263 1.034 2.326 1.00134.78 C ANISOU 1319 CG GLN A 185 16519 14030 20661 894 -368 -210 C ATOM 1320 CD GLN A 185 29.663 0.672 1.871 1.00142.25 C ANISOU 1320 CD GLN A 185 17417 15135 21495 1164 -465 -450 C ATOM 1321 OE1 GLN A 185 30.141 1.165 0.850 1.00145.37 O ANISOU 1321 OE1 GLN A 185 17657 15795 21782 1198 -441 -630 O ATOM 1322 NE2 GLN A 185 30.331 -0.190 2.631 1.00142.29 N ANISOU 1322 NE2 GLN A 185 17550 15002 21512 1362 -579 -452 N ATOM 1323 N PRO A 186 25.535 2.296 4.090 1.00130.05 N ANISOU 1323 N PRO A 186 15927 13307 20179 355 -102 335 N ATOM 1324 CA PRO A 186 25.185 2.988 5.345 1.00127.55 C ANISOU 1324 CA PRO A 186 15577 13080 19806 265 11 534 C ATOM 1325 C PRO A 186 26.347 3.713 6.003 1.00135.00 C ANISOU 1325 C PRO A 186 16445 14250 20599 410 59 507 C ATOM 1326 O PRO A 186 26.143 4.789 6.580 1.00138.16 O ANISOU 1326 O PRO A 186 16744 14824 20929 337 161 576 O ATOM 1327 CB PRO A 186 24.653 1.849 6.229 1.00126.22 C ANISOU 1327 CB PRO A 186 15574 12648 19735 219 -46 723 C ATOM 1328 CG PRO A 186 24.204 0.802 5.263 1.00144.23 C ANISOU 1328 CG PRO A 186 17955 14672 22172 182 -168 637 C ATOM 1329 CD PRO A 186 25.169 0.870 4.125 1.00146.65 C ANISOU 1329 CD PRO A 186 18206 15081 22432 363 -235 371 C ATOM 1330 N ILE A 187 27.560 3.159 5.944 1.00128.54 N ANISOU 1330 N ILE A 187 15667 13443 19730 623 -25 389 N ATOM 1331 CA ILE A 187 28.686 3.807 6.611 1.00107.18 C ANISOU 1331 CA ILE A 187 12875 10968 16880 758 16 350 C ATOM 1332 C ILE A 187 29.032 5.126 5.931 1.00106.88 C ANISOU 1332 C ILE A 187 12655 11201 16755 694 101 233 C ATOM 1333 O ILE A 187 29.506 6.063 6.586 1.00107.90 O ANISOU 1333 O ILE A 187 12686 11520 16792 700 170 250 O ATOM 1334 CB ILE A 187 29.901 2.860 6.668 1.00 92.85 C ANISOU 1334 CB ILE A 187 11134 9121 15022 1019 -107 226 C ATOM 1335 CG1 ILE A 187 30.949 3.388 7.649 1.00105.39 C ANISOU 1335 CG1 ILE A 187 12648 10930 16466 1161 -69 218 C ATOM 1336 CG2 ILE A 187 30.513 2.676 5.287 1.00 97.40 C ANISOU 1336 CG2 ILE A 187 11645 9784 15579 1109 -175 -22 C ATOM 1337 CD1 ILE A 187 30.491 3.387 9.092 1.00110.70 C ANISOU 1337 CD1 ILE A 187 13389 11543 17128 1130 -25 447 C ATOM 1338 N ILE A 188 28.794 5.231 4.622 1.00106.80 N ANISOU 1338 N ILE A 188 12600 11209 16772 628 88 120 N ATOM 1339 CA ILE A 188 29.118 6.460 3.906 1.00107.81 C ANISOU 1339 CA ILE A 188 12572 11580 16810 547 158 40 C ATOM 1340 C ILE A 188 28.192 7.590 4.338 1.00102.61 C ANISOU 1340 C ILE A 188 11870 10941 16174 366 247 177 C ATOM 1341 O ILE A 188 28.624 8.737 4.502 1.00105.24 O ANISOU 1341 O ILE A 188 12100 11453 16434 322 302 169 O ATOM 1342 CB ILE A 188 29.064 6.221 2.387 1.00106.56 C ANISOU 1342 CB ILE A 188 12381 11454 16653 533 115 -103 C ATOM 1343 CG1 ILE A 188 30.150 5.228 1.969 1.00104.10 C ANISOU 1343 CG1 ILE A 188 12077 11187 16289 753 13 -287 C ATOM 1344 CG2 ILE A 188 29.208 7.529 1.626 1.00 92.70 C ANISOU 1344 CG2 ILE A 188 10485 9931 14807 407 189 -130 C ATOM 1345 CD1 ILE A 188 30.029 4.759 0.539 1.00109.03 C ANISOU 1345 CD1 ILE A 188 12674 11835 16917 776 -53 -450 C ATOM 1346 N THR A 189 26.910 7.283 4.547 1.00102.33 N ANISOU 1346 N THR A 189 11908 10729 16244 259 252 292 N ATOM 1347 CA THR A 189 25.976 8.300 5.018 1.00109.25 C ANISOU 1347 CA THR A 189 12733 11643 17133 118 320 397 C ATOM 1348 C THR A 189 26.345 8.788 6.416 1.00103.62 C ANISOU 1348 C THR A 189 11989 11024 16359 171 362 473 C ATOM 1349 O THR A 189 26.101 9.953 6.750 1.00 93.30 O ANISOU 1349 O THR A 189 10599 9828 15023 108 403 490 O ATOM 1350 CB THR A 189 24.547 7.747 4.981 1.00101.09 C ANISOU 1350 CB THR A 189 11762 10439 16209 -1 315 487 C ATOM 1351 OG1 THR A 189 24.240 7.316 3.649 1.00101.16 O ANISOU 1351 OG1 THR A 189 11789 10375 16273 -37 267 388 O ATOM 1352 CG2 THR A 189 23.545 8.813 5.374 1.00 90.12 C ANISOU 1352 CG2 THR A 189 10299 9127 14818 -123 373 557 C ATOM 1353 N PHE A 190 26.941 7.921 7.239 1.00104.07 N ANISOU 1353 N PHE A 190 12113 11037 16393 303 336 511 N ATOM 1354 CA PHE A 190 27.474 8.363 8.525 1.00105.56 C ANISOU 1354 CA PHE A 190 12258 11353 16496 388 367 558 C ATOM 1355 C PHE A 190 28.618 9.352 8.338 1.00107.57 C ANISOU 1355 C PHE A 190 12393 11814 16665 440 380 423 C ATOM 1356 O PHE A 190 28.664 10.399 8.996 1.00104.03 O ANISOU 1356 O PHE A 190 11857 11493 16177 415 415 428 O ATOM 1357 CB PHE A 190 27.938 7.159 9.345 1.00120.00 C ANISOU 1357 CB PHE A 190 14199 13089 18307 536 320 627 C ATOM 1358 CG PHE A 190 28.655 7.530 10.614 1.00117.52 C ANISOU 1358 CG PHE A 190 13835 12936 17882 662 343 652 C ATOM 1359 CD1 PHE A 190 27.960 8.030 11.703 1.00113.08 C ANISOU 1359 CD1 PHE A 190 13230 12450 17284 612 399 776 C ATOM 1360 CD2 PHE A 190 30.028 7.372 10.717 1.00106.77 C ANISOU 1360 CD2 PHE A 190 12451 11679 16437 846 301 530 C ATOM 1361 CE1 PHE A 190 28.623 8.369 12.869 1.00 96.92 C ANISOU 1361 CE1 PHE A 190 11126 10574 15126 745 412 781 C ATOM 1362 CE2 PHE A 190 30.696 7.708 11.880 1.00104.93 C ANISOU 1362 CE2 PHE A 190 12161 11608 16098 973 315 535 C ATOM 1363 CZ PHE A 190 29.991 8.207 12.958 1.00106.67 C ANISOU 1363 CZ PHE A 190 12347 11895 16289 924 369 662 C ATOM 1364 N GLY A 191 29.556 9.033 7.445 1.00103.33 N ANISOU 1364 N GLY A 191 11842 11324 16096 508 343 291 N ATOM 1365 CA GLY A 191 30.701 9.906 7.246 1.00 91.71 C ANISOU 1365 CA GLY A 191 10241 10074 14532 530 359 169 C ATOM 1366 C GLY A 191 30.316 11.265 6.696 1.00 98.30 C ANISOU 1366 C GLY A 191 10991 10978 15382 349 397 172 C ATOM 1367 O GLY A 191 30.891 12.286 7.083 1.00102.88 O ANISOU 1367 O GLY A 191 11475 11698 15917 319 415 137 O ATOM 1368 N THR A 192 29.340 11.298 5.786 1.00107.33 N ANISOU 1368 N THR A 192 12175 12012 16591 227 396 208 N ATOM 1369 CA THR A 192 28.892 12.572 5.233 1.00103.91 C ANISOU 1369 CA THR A 192 11690 11616 16174 67 411 225 C ATOM 1370 C THR A 192 28.260 13.448 6.307 1.00 98.70 C ANISOU 1370 C THR A 192 11014 10938 15550 33 420 293 C ATOM 1371 O THR A 192 28.490 14.662 6.341 1.00102.19 O ANISOU 1371 O THR A 192 11394 11449 15984 -39 411 273 O ATOM 1372 CB THR A 192 27.906 12.337 4.087 1.00112.62 C ANISOU 1372 CB THR A 192 12845 12614 17333 -25 398 244 C ATOM 1373 OG1 THR A 192 26.771 11.609 4.572 1.00132.98 O ANISOU 1373 OG1 THR A 192 15503 15029 19994 -18 394 320 O ATOM 1374 CG2 THR A 192 28.568 11.557 2.957 1.00 92.33 C ANISOU 1374 CG2 THR A 192 10268 10100 14713 24 376 144 C ATOM 1375 N ALA A 193 27.457 12.853 7.192 1.00 90.73 N ANISOU 1375 N ALA A 193 10057 9841 14576 82 430 371 N ATOM 1376 CA ALA A 193 26.892 13.614 8.302 1.00 82.90 C ANISOU 1376 CA ALA A 193 9023 8886 13588 82 436 413 C ATOM 1377 C ALA A 193 27.988 14.192 9.186 1.00 97.09 C ANISOU 1377 C ALA A 193 10742 10826 15320 170 432 351 C ATOM 1378 O ALA A 193 27.907 15.350 9.612 1.00109.87 O ANISOU 1378 O ALA A 193 12295 12503 16947 141 409 315 O ATOM 1379 CB ALA A 193 25.953 12.730 9.122 1.00 70.60 C ANISOU 1379 CB ALA A 193 7515 7263 12045 113 459 521 C ATOM 1380 N MET A 194 29.027 13.402 9.469 1.00 94.79 N ANISOU 1380 N MET A 194 10456 10593 14967 291 439 319 N ATOM 1381 CA MET A 194 30.128 13.892 10.290 1.00106.11 C ANISOU 1381 CA MET A 194 11800 12186 16329 385 433 239 C ATOM 1382 C MET A 194 30.900 14.997 9.580 1.00105.35 C ANISOU 1382 C MET A 194 11615 12180 16232 279 417 140 C ATOM 1383 O MET A 194 31.219 16.027 10.185 1.00112.67 O ANISOU 1383 O MET A 194 12461 13190 17159 263 394 86 O ATOM 1384 CB MET A 194 31.066 12.739 10.655 1.00100.45 C ANISOU 1384 CB MET A 194 11112 11515 15538 557 429 215 C ATOM 1385 CG MET A 194 30.440 11.678 11.545 1.00104.50 C ANISOU 1385 CG MET A 194 11726 11935 16044 657 433 343 C ATOM 1386 SD MET A 194 29.891 12.340 13.129 1.00119.11 S ANISOU 1386 SD MET A 194 13511 13896 17847 702 453 408 S ATOM 1387 CE MET A 194 31.463 12.722 13.899 1.00113.46 C ANISOU 1387 CE MET A 194 12686 13398 17024 872 431 263 C ATOM 1388 N ALA A 195 31.199 14.806 8.293 1.00 95.58 N ANISOU 1388 N ALA A 195 10388 10936 14991 197 421 116 N ATOM 1389 CA ALA A 195 32.061 15.743 7.582 1.00 94.61 C ANISOU 1389 CA ALA A 195 10173 10933 14839 75 414 47 C ATOM 1390 C ALA A 195 31.303 16.978 7.107 1.00 99.46 C ANISOU 1390 C ALA A 195 10804 11455 15532 -104 383 102 C ATOM 1391 O ALA A 195 31.826 18.094 7.190 1.00114.19 O ANISOU 1391 O ALA A 195 12604 13376 17409 -203 353 68 O ATOM 1392 CB ALA A 195 32.732 15.045 6.399 1.00 84.37 C ANISOU 1392 CB ALA A 195 8859 9723 13473 69 431 -4 C ATOM 1393 N ALA A 196 30.082 16.806 6.602 1.00 90.01 N ANISOU 1393 N ALA A 196 9697 10109 14395 -148 377 180 N ATOM 1394 CA ALA A 196 29.342 17.925 6.031 1.00 96.66 C ANISOU 1394 CA ALA A 196 10569 10857 15301 -294 330 226 C ATOM 1395 C ALA A 196 28.512 18.688 7.052 1.00 99.00 C ANISOU 1395 C ALA A 196 10871 11078 15667 -260 278 228 C ATOM 1396 O ALA A 196 28.178 19.854 6.809 1.00 96.58 O ANISOU 1396 O ALA A 196 10579 10700 15418 -355 205 232 O ATOM 1397 CB ALA A 196 28.425 17.442 4.902 1.00101.20 C ANISOU 1397 CB ALA A 196 11219 11338 15893 -347 336 283 C ATOM 1398 N PHE A 197 28.150 18.065 8.173 1.00 94.18 N ANISOU 1398 N PHE A 197 10251 10487 15045 -121 303 225 N ATOM 1399 CA PHE A 197 27.375 18.749 9.202 1.00 90.31 C ANISOU 1399 CA PHE A 197 9736 9987 14591 -66 255 205 C ATOM 1400 C PHE A 197 28.121 18.859 10.524 1.00100.46 C ANISOU 1400 C PHE A 197 10938 11403 15829 59 255 135 C ATOM 1401 O PHE A 197 28.300 19.971 11.029 1.00102.57 O ANISOU 1401 O PHE A 197 11150 11692 16129 60 181 53 O ATOM 1402 CB PHE A 197 26.037 18.035 9.412 1.00 79.36 C ANISOU 1402 CB PHE A 197 8389 8553 13212 -26 284 272 C ATOM 1403 CG PHE A 197 25.170 18.679 10.450 1.00 81.36 C ANISOU 1403 CG PHE A 197 8588 8853 13472 44 240 237 C ATOM 1404 CD1 PHE A 197 24.466 19.836 10.161 1.00 86.92 C ANISOU 1404 CD1 PHE A 197 9293 9494 14239 2 145 185 C ATOM 1405 CD2 PHE A 197 25.067 18.135 11.720 1.00 86.32 C ANISOU 1405 CD2 PHE A 197 9162 9605 14031 166 282 252 C ATOM 1406 CE1 PHE A 197 23.664 20.430 11.112 1.00 84.36 C ANISOU 1406 CE1 PHE A 197 8902 9242 13911 97 87 117 C ATOM 1407 CE2 PHE A 197 24.265 18.728 12.677 1.00 92.56 C ANISOU 1407 CE2 PHE A 197 9874 10494 14800 243 242 203 C ATOM 1408 CZ PHE A 197 23.564 19.877 12.371 1.00 83.71 C ANISOU 1408 CZ PHE A 197 8739 9321 13744 217 141 119 C ATOM 1409 N TYR A 198 28.567 17.741 11.102 1.00 95.89 N ANISOU 1409 N TYR A 198 10353 10905 15174 175 320 158 N ATOM 1410 CA TYR A 198 29.112 17.791 12.455 1.00 86.94 C ANISOU 1410 CA TYR A 198 9141 9915 13977 321 316 100 C ATOM 1411 C TYR A 198 30.441 18.534 12.500 1.00 89.58 C ANISOU 1411 C TYR A 198 9391 10343 14302 308 281 -21 C ATOM 1412 O TYR A 198 30.715 19.259 13.461 1.00 88.61 O ANISOU 1412 O TYR A 198 9183 10313 14173 379 232 -115 O ATOM 1413 CB TYR A 198 29.249 16.381 13.030 1.00 83.17 C ANISOU 1413 CB TYR A 198 8702 9483 13416 452 380 178 C ATOM 1414 CG TYR A 198 27.916 15.774 13.405 1.00 98.67 C ANISOU 1414 CG TYR A 198 10718 11396 15379 458 411 302 C ATOM 1415 CD1 TYR A 198 27.253 16.181 14.556 1.00 90.45 C ANISOU 1415 CD1 TYR A 198 9605 10469 14292 531 402 303 C ATOM 1416 CD2 TYR A 198 27.321 14.795 12.617 1.00 95.93 C ANISOU 1416 CD2 TYR A 198 10472 10909 15068 387 444 405 C ATOM 1417 CE1 TYR A 198 26.033 15.640 14.910 1.00 96.11 C ANISOU 1417 CE1 TYR A 198 10341 11187 14988 514 440 419 C ATOM 1418 CE2 TYR A 198 26.096 14.245 12.964 1.00 95.11 C ANISOU 1418 CE2 TYR A 198 10400 10770 14966 360 474 521 C ATOM 1419 CZ TYR A 198 25.459 14.672 14.112 1.00100.07 C ANISOU 1419 CZ TYR A 198 10946 11539 15536 415 478 535 C ATOM 1420 OH TYR A 198 24.244 14.135 14.471 1.00 98.31 O ANISOU 1420 OH TYR A 198 10728 11330 15295 368 517 654 O ATOM 1421 N LEU A 199 31.274 18.380 11.469 1.00 86.01 N ANISOU 1421 N LEU A 199 8945 9891 13845 213 300 -31 N ATOM 1422 CA LEU A 199 32.518 19.148 11.437 1.00 92.82 C ANISOU 1422 CA LEU A 199 9705 10865 14696 156 270 -142 C ATOM 1423 C LEU A 199 32.261 20.641 11.260 1.00 94.02 C ANISOU 1423 C LEU A 199 9843 10927 14952 5 181 -174 C ATOM 1424 O LEU A 199 32.840 21.436 12.021 1.00102.64 O ANISOU 1424 O LEU A 199 10846 12089 16064 24 122 -284 O ATOM 1425 CB LEU A 199 33.452 18.585 10.361 1.00 92.83 C ANISOU 1425 CB LEU A 199 9691 10941 14637 89 318 -148 C ATOM 1426 CG LEU A 199 34.814 19.267 10.243 1.00106.75 C ANISOU 1426 CG LEU A 199 11323 12870 16366 3 304 -259 C ATOM 1427 CD1 LEU A 199 35.588 19.134 11.544 1.00111.64 C ANISOU 1427 CD1 LEU A 199 11843 13651 16925 183 294 -379 C ATOM 1428 CD2 LEU A 199 35.600 18.678 9.083 1.00105.28 C ANISOU 1428 CD2 LEU A 199 11104 12802 16096 -62 355 -267 C ATOM 1429 N PRO A 200 31.426 21.097 10.316 1.00 93.57 N ANISOU 1429 N PRO A 200 9874 10709 14970 -135 150 -92 N ATOM 1430 CA PRO A 200 31.154 22.543 10.242 1.00 96.57 C ANISOU 1430 CA PRO A 200 10265 10968 15458 -254 32 -122 C ATOM 1431 C PRO A 200 30.432 23.094 11.460 1.00 99.30 C ANISOU 1431 C PRO A 200 10587 11292 15851 -112 -51 -207 C ATOM 1432 O PRO A 200 30.659 24.254 11.823 1.00 99.85 O ANISOU 1432 O PRO A 200 10625 11313 16003 -151 -168 -302 O ATOM 1433 CB PRO A 200 30.299 22.676 8.974 1.00101.48 C ANISOU 1433 CB PRO A 200 11002 11433 16124 -388 19 -4 C ATOM 1434 CG PRO A 200 30.636 21.482 8.163 1.00105.00 C ANISOU 1434 CG PRO A 200 11458 11959 16477 -398 133 61 C ATOM 1435 CD PRO A 200 30.851 20.388 9.158 1.00 98.65 C ANISOU 1435 CD PRO A 200 10609 11273 15602 -201 202 17 C ATOM 1436 N VAL A 201 29.564 22.310 12.102 1.00 94.49 N ANISOU 1436 N VAL A 201 9986 10728 15189 46 -2 -181 N ATOM 1437 CA VAL A 201 28.844 22.824 13.265 1.00 96.84 C ANISOU 1437 CA VAL A 201 10232 11066 15499 191 -75 -271 C ATOM 1438 C VAL A 201 29.787 23.008 14.449 1.00 98.55 C ANISOU 1438 C VAL A 201 10327 11451 15668 316 -94 -403 C ATOM 1439 O VAL A 201 29.683 23.994 15.189 1.00 87.00 O ANISOU 1439 O VAL A 201 8801 10001 14254 381 -211 -541 O ATOM 1440 CB VAL A 201 27.653 21.912 13.612 1.00 97.57 C ANISOU 1440 CB VAL A 201 10345 11203 15526 295 -5 -189 C ATOM 1441 CG1 VAL A 201 27.086 22.272 14.973 1.00 96.65 C ANISOU 1441 CG1 VAL A 201 10130 11227 15365 470 -56 -289 C ATOM 1442 CG2 VAL A 201 26.566 22.067 12.563 1.00102.78 C ANISOU 1442 CG2 VAL A 201 11099 11701 16251 187 -29 -114 C ATOM 1443 N THR A 202 30.733 22.085 14.639 1.00 86.26 N ANISOU 1443 N THR A 202 8733 10029 14014 368 4 -383 N ATOM 1444 CA THR A 202 31.650 22.221 15.767 1.00 96.85 C ANISOU 1444 CA THR A 202 9951 11553 15293 505 -16 -517 C ATOM 1445 C THR A 202 32.550 23.439 15.607 1.00104.12 C ANISOU 1445 C THR A 202 10807 12443 16311 383 -119 -654 C ATOM 1446 O THR A 202 32.798 24.160 16.580 1.00120.66 O ANISOU 1446 O THR A 202 12803 14617 18424 479 -210 -812 O ATOM 1447 CB THR A 202 32.489 20.953 15.942 1.00105.47 C ANISOU 1447 CB THR A 202 11028 12790 16257 604 94 -472 C ATOM 1448 OG1 THR A 202 33.177 20.650 14.721 1.00122.73 O ANISOU 1448 OG1 THR A 202 13254 14922 18458 453 138 -425 O ATOM 1449 CG2 THR A 202 31.615 19.778 16.363 1.00102.81 C ANISOU 1449 CG2 THR A 202 10757 12473 15831 730 172 -334 C ATOM 1450 N VAL A 203 33.042 23.696 14.392 1.00 91.76 N ANISOU 1450 N VAL A 203 9288 10772 14805 163 -113 -596 N ATOM 1451 CA VAL A 203 33.908 24.858 14.211 1.00103.80 C ANISOU 1451 CA VAL A 203 10754 12261 16425 1 -212 -697 C ATOM 1452 C VAL A 203 33.110 26.151 14.343 1.00102.88 C ANISOU 1452 C VAL A 203 10688 11942 16459 -46 -379 -753 C ATOM 1453 O VAL A 203 33.642 27.164 14.811 1.00 99.15 O ANISOU 1453 O VAL A 203 10151 11445 16078 -86 -505 -896 O ATOM 1454 CB VAL A 203 34.664 24.788 12.869 1.00 98.55 C ANISOU 1454 CB VAL A 203 10111 11578 15756 -241 -155 -601 C ATOM 1455 CG1 VAL A 203 35.551 23.556 12.825 1.00101.64 C ANISOU 1455 CG1 VAL A 203 10430 12194 15994 -153 -20 -601 C ATOM 1456 CG2 VAL A 203 33.708 24.793 11.701 1.00119.91 C ANISOU 1456 CG2 VAL A 203 12963 14090 18506 -370 -149 -435 C ATOM 1457 N MET A 204 31.830 26.144 13.956 1.00 87.50 N ANISOU 1457 N MET A 204 8854 9846 14545 -30 -400 -661 N ATOM 1458 CA MET A 204 31.003 27.331 14.155 1.00 94.17 C ANISOU 1458 CA MET A 204 9748 10511 15522 -19 -581 -742 C ATOM 1459 C MET A 204 30.695 27.549 15.630 1.00102.71 C ANISOU 1459 C MET A 204 10719 11730 16578 233 -653 -929 C ATOM 1460 O MET A 204 30.645 28.693 16.095 1.00114.46 O ANISOU 1460 O MET A 204 12184 13126 18181 260 -836 -1091 O ATOM 1461 CB MET A 204 29.702 27.228 13.359 1.00 91.94 C ANISOU 1461 CB MET A 204 9597 10073 15262 -43 -586 -616 C ATOM 1462 CG MET A 204 29.865 27.304 11.857 1.00 93.37 C ANISOU 1462 CG MET A 204 9896 10098 15481 -288 -561 -448 C ATOM 1463 SD MET A 204 28.267 27.321 11.023 1.00112.12 S ANISOU 1463 SD MET A 204 12415 12300 17885 -281 -601 -340 S ATOM 1464 CE MET A 204 27.716 25.645 11.276 1.00 81.73 C ANISOU 1464 CE MET A 204 8521 8650 13882 -134 -398 -270 C ATOM 1465 N CYS A 205 30.475 26.466 16.379 1.00108.79 N ANISOU 1465 N CYS A 205 11420 12722 17192 422 -524 -910 N ATOM 1466 CA CYS A 205 30.228 26.604 17.811 1.00106.86 C ANISOU 1466 CA CYS A 205 11050 12671 16882 668 -576 -1075 C ATOM 1467 C CYS A 205 31.471 27.103 18.537 1.00105.34 C ANISOU 1467 C CYS A 205 10733 12587 16703 704 -640 -1254 C ATOM 1468 O CYS A 205 31.370 27.910 19.468 1.00123.71 O ANISOU 1468 O CYS A 205 12967 14970 19066 844 -783 -1460 O ATOM 1469 CB CYS A 205 29.761 25.272 18.400 1.00104.35 C ANISOU 1469 CB CYS A 205 10699 12570 16380 829 -415 -967 C ATOM 1470 SG CYS A 205 28.133 24.732 17.839 1.00112.38 S ANISOU 1470 SG CYS A 205 11816 13510 17375 811 -357 -802 S ATOM 1471 N THR A 206 32.651 26.634 18.127 1.00 85.67 N ANISOU 1471 N THR A 206 8223 10148 14179 590 -545 -1202 N ATOM 1472 CA THR A 206 33.883 27.097 18.756 1.00113.45 C ANISOU 1472 CA THR A 206 11606 13791 17710 607 -603 -1384 C ATOM 1473 C THR A 206 34.190 28.539 18.372 1.00115.22 C ANISOU 1473 C THR A 206 11846 13794 18139 412 -788 -1496 C ATOM 1474 O THR A 206 34.645 29.325 19.211 1.00117.48 O ANISOU 1474 O THR A 206 12022 14129 18486 483 -923 -1715 O ATOM 1475 CB THR A 206 35.048 26.179 18.385 1.00117.12 C ANISOU 1475 CB THR A 206 12031 14402 18068 547 -455 -1313 C ATOM 1476 OG1 THR A 206 35.200 26.145 16.960 1.00132.24 O ANISOU 1476 OG1 THR A 206 14050 16152 20044 284 -407 -1155 O ATOM 1477 CG2 THR A 206 34.804 24.772 18.908 1.00112.89 C ANISOU 1477 CG2 THR A 206 11495 14056 17342 763 -309 -1215 C ATOM 1478 N LEU A 207 33.955 28.906 17.109 1.00112.01 N ANISOU 1478 N LEU A 207 11580 13138 17842 162 -808 -1345 N ATOM 1479 CA LEU A 207 34.066 30.311 16.732 1.00108.07 C ANISOU 1479 CA LEU A 207 11136 12377 17549 -30 -1009 -1414 C ATOM 1480 C LEU A 207 33.057 31.158 17.493 1.00 96.09 C ANISOU 1480 C LEU A 207 9637 10746 16128 157 -1208 -1581 C ATOM 1481 O LEU A 207 33.381 32.260 17.949 1.00102.80 O ANISOU 1481 O LEU A 207 10450 11485 17125 140 -1409 -1772 O ATOM 1482 CB LEU A 207 33.884 30.485 15.224 1.00 97.91 C ANISOU 1482 CB LEU A 207 10012 10857 16332 -315 -991 -1188 C ATOM 1483 CG LEU A 207 35.014 29.977 14.327 1.00102.16 C ANISOU 1483 CG LEU A 207 10516 11500 16799 -550 -841 -1055 C ATOM 1484 CD1 LEU A 207 34.641 30.132 12.860 1.00 94.44 C ANISOU 1484 CD1 LEU A 207 9699 10322 15862 -797 -826 -825 C ATOM 1485 CD2 LEU A 207 36.315 30.705 14.638 1.00 80.97 C ANISOU 1485 CD2 LEU A 207 7705 8873 14187 -703 -916 -1193 C ATOM 1486 N TYR A 208 31.831 30.654 17.659 1.00119.80 N ANISOU 1486 N TYR A 208 14224 11471 19823 -4390 -1494 -2488 N ATOM 1487 CA TYR A 208 30.823 31.407 18.398 1.00119.18 C ANISOU 1487 CA TYR A 208 13780 11692 19812 -4431 -1569 -2348 C ATOM 1488 C TYR A 208 31.215 31.555 19.862 1.00116.81 C ANISOU 1488 C TYR A 208 13529 11194 19662 -4240 -1378 -2047 C ATOM 1489 O TYR A 208 30.948 32.591 20.480 1.00126.43 O ANISOU 1489 O TYR A 208 14498 12664 20874 -4049 -1457 -1863 O ATOM 1490 CB TYR A 208 29.460 30.729 18.283 1.00131.57 C ANISOU 1490 CB TYR A 208 15154 13376 21461 -4898 -1584 -2571 C ATOM 1491 CG TYR A 208 28.324 31.543 18.861 1.00127.30 C ANISOU 1491 CG TYR A 208 14173 13251 20945 -4931 -1690 -2470 C ATOM 1492 CD1 TYR A 208 27.738 32.566 18.129 1.00134.23 C ANISOU 1492 CD1 TYR A 208 14727 14620 21654 -4827 -1970 -2520 C ATOM 1493 CD2 TYR A 208 27.850 31.304 20.145 1.00132.51 C ANISOU 1493 CD2 TYR A 208 14739 13828 21780 -5035 -1507 -2313 C ATOM 1494 CE1 TYR A 208 26.700 33.315 18.648 1.00140.96 C ANISOU 1494 CE1 TYR A 208 15173 15862 22524 -4807 -2069 -2440 C ATOM 1495 CE2 TYR A 208 26.814 32.051 20.676 1.00135.70 C ANISOU 1495 CE2 TYR A 208 14722 14650 22188 -5035 -1596 -2239 C ATOM 1496 CZ TYR A 208 26.244 33.056 19.923 1.00134.93 C ANISOU 1496 CZ TYR A 208 14307 15027 21932 -4909 -1879 -2313 C ATOM 1497 OH TYR A 208 25.213 33.804 20.444 1.00130.18 O ANISOU 1497 OH TYR A 208 13283 14850 21330 -4862 -1970 -2251 O ATOM 1498 N TRP A 209 31.844 30.527 20.435 1.00133.64 N ANISOU 1498 N TRP A 209 15984 12877 21917 -4271 -1129 -1999 N ATOM 1499 CA TRP A 209 32.294 30.621 21.820 1.00136.86 C ANISOU 1499 CA TRP A 209 16450 13117 22432 -4068 -946 -1703 C ATOM 1500 C TRP A 209 33.426 31.630 21.967 1.00117.13 C ANISOU 1500 C TRP A 209 13983 10701 19821 -3620 -1007 -1508 C ATOM 1501 O TRP A 209 33.441 32.419 22.919 1.00109.21 O ANISOU 1501 O TRP A 209 12823 9832 18839 -3425 -1004 -1296 O ATOM 1502 CB TRP A 209 32.736 29.249 22.329 1.00142.22 C ANISOU 1502 CB TRP A 209 17493 13288 23254 -4182 -672 -1679 C ATOM 1503 CG TRP A 209 33.192 29.269 23.756 1.00148.85 C ANISOU 1503 CG TRP A 209 18396 13983 24178 -3971 -480 -1362 C ATOM 1504 CD1 TRP A 209 32.424 29.507 24.859 1.00149.68 C ANISOU 1504 CD1 TRP A 209 18272 14238 24362 -4056 -409 -1193 C ATOM 1505 CD2 TRP A 209 34.527 29.061 24.234 1.00154.34 C ANISOU 1505 CD2 TRP A 209 19377 14409 24855 -3624 -339 -1180 C ATOM 1506 NE1 TRP A 209 33.196 29.450 25.995 1.00150.46 N ANISOU 1506 NE1 TRP A 209 18511 14170 24486 -3790 -234 -918 N ATOM 1507 CE2 TRP A 209 34.491 29.179 25.638 1.00156.10 C ANISOU 1507 CE2 TRP A 209 19537 14630 25145 -3521 -194 -902 C ATOM 1508 CE3 TRP A 209 35.748 28.783 23.611 1.00153.52 C ANISOU 1508 CE3 TRP A 209 19556 14108 24667 -3380 -320 -1230 C ATOM 1509 CZ2 TRP A 209 35.628 29.028 26.429 1.00163.39 C ANISOU 1509 CZ2 TRP A 209 20669 15363 26050 -3186 -45 -672 C ATOM 1510 CZ3 TRP A 209 36.876 28.633 24.398 1.00158.06 C ANISOU 1510 CZ3 TRP A 209 20325 14497 25233 -3042 -167 -1002 C ATOM 1511 CH2 TRP A 209 36.808 28.756 25.792 1.00163.86 C ANISOU 1511 CH2 TRP A 209 20990 15236 26033 -2949 -37 -725 C ATOM 1512 N ARG A 210 34.384 31.619 21.036 1.00110.72 N ANISOU 1512 N ARG A 210 13364 9824 18880 -3464 -1062 -1590 N ATOM 1513 CA ARG A 210 35.506 32.549 21.122 1.00107.32 C ANISOU 1513 CA ARG A 210 12957 9481 18337 -3084 -1114 -1407 C ATOM 1514 C ARG A 210 35.056 33.988 20.912 1.00112.80 C ANISOU 1514 C ARG A 210 13346 10570 18945 -2982 -1355 -1341 C ATOM 1515 O ARG A 210 35.583 34.904 21.552 1.00142.31 O ANISOU 1515 O ARG A 210 17022 14382 22668 -2723 -1380 -1138 O ATOM 1516 CB ARG A 210 36.589 32.175 20.111 1.00112.97 C ANISOU 1516 CB ARG A 210 13921 10087 18914 -2964 -1108 -1517 C ATOM 1517 CG ARG A 210 37.278 30.854 20.403 1.00123.50 C ANISOU 1517 CG ARG A 210 15598 10997 20328 -2945 -864 -1551 C ATOM 1518 CD ARG A 210 38.015 30.933 21.727 1.00124.26 C ANISOU 1518 CD ARG A 210 15761 10952 20498 -2686 -700 -1265 C ATOM 1519 NE ARG A 210 39.051 31.960 21.711 1.00141.52 N ANISOU 1519 NE ARG A 210 17879 13349 22542 -2364 -783 -1111 N ATOM 1520 CZ ARG A 210 39.595 32.485 22.803 1.00144.83 C ANISOU 1520 CZ ARG A 210 18245 13803 22983 -2138 -724 -869 C ATOM 1521 NH1 ARG A 210 39.198 32.080 24.003 1.00152.95 N ANISOU 1521 NH1 ARG A 210 19277 14688 24150 -2172 -578 -739 N ATOM 1522 NH2 ARG A 210 40.532 33.416 22.697 1.00137.12 N ANISOU 1522 NH2 ARG A 210 17203 13020 21875 -1897 -810 -758 N ATOM 1523 N ILE A 211 34.089 34.207 20.019 1.00124.74 N ANISOU 1523 N ILE A 211 14669 12333 20393 -3174 -1540 -1514 N ATOM 1524 CA ILE A 211 33.578 35.557 19.793 1.00118.30 C ANISOU 1524 CA ILE A 211 13574 11878 19498 -3051 -1777 -1441 C ATOM 1525 C ILE A 211 33.018 36.141 21.084 1.00115.11 C ANISOU 1525 C ILE A 211 12967 11549 19222 -2965 -1745 -1281 C ATOM 1526 O ILE A 211 33.237 37.318 21.394 1.00119.67 O ANISOU 1526 O ILE A 211 13442 12257 19769 -2712 -1856 -1129 O ATOM 1527 CB ILE A 211 32.530 35.551 18.664 1.00113.97 C ANISOU 1527 CB ILE A 211 12838 11614 18851 -3275 -1975 -1661 C ATOM 1528 CG1 ILE A 211 33.201 35.257 17.320 1.00109.54 C ANISOU 1528 CG1 ILE A 211 12459 11056 18105 -3287 -2042 -1804 C ATOM 1529 CG2 ILE A 211 31.778 36.870 18.612 1.00118.15 C ANISOU 1529 CG2 ILE A 211 13055 12508 19329 -3136 -2208 -1570 C ATOM 1530 CD1 ILE A 211 32.231 34.923 16.215 1.00112.84 C ANISOU 1530 CD1 ILE A 211 12736 11726 18413 -3555 -2201 -2072 C ATOM 1531 N TYR A 212 32.308 35.326 21.869 1.00111.96 N ANISOU 1531 N TYR A 212 12518 11059 18962 -3179 -1584 -1315 N ATOM 1532 CA TYR A 212 31.752 35.811 23.130 1.00114.21 C ANISOU 1532 CA TYR A 212 12596 11456 19343 -3100 -1531 -1174 C ATOM 1533 C TYR A 212 32.845 36.325 24.062 1.00132.71 C ANISOU 1533 C TYR A 212 15071 13658 21695 -2780 -1441 -955 C ATOM 1534 O TYR A 212 32.678 37.362 24.714 1.00142.64 O ANISOU 1534 O TYR A 212 16154 15089 22955 -2574 -1519 -850 O ATOM 1535 CB TYR A 212 30.947 34.703 23.810 1.00118.06 C ANISOU 1535 CB TYR A 212 13044 11849 19962 -3416 -1333 -1220 C ATOM 1536 CG TYR A 212 30.317 35.121 25.120 1.00135.19 C ANISOU 1536 CG TYR A 212 14978 14186 22204 -3352 -1257 -1080 C ATOM 1537 CD1 TYR A 212 29.169 35.903 25.144 1.00154.15 C ANISOU 1537 CD1 TYR A 212 17000 16986 24582 -3358 -1414 -1136 C ATOM 1538 CD2 TYR A 212 30.875 34.740 26.334 1.00154.39 C ANISOU 1538 CD2 TYR A 212 17553 16407 24702 -3257 -1029 -893 C ATOM 1539 CE1 TYR A 212 28.591 36.288 26.341 1.00173.64 C ANISOU 1539 CE1 TYR A 212 19239 19641 27096 -3275 -1336 -1030 C ATOM 1540 CE2 TYR A 212 30.305 35.121 27.535 1.00172.68 C ANISOU 1540 CE2 TYR A 212 19644 18914 27050 -3191 -954 -774 C ATOM 1541 CZ TYR A 212 29.164 35.895 27.532 1.00183.26 C ANISOU 1541 CZ TYR A 212 20608 20654 28369 -3201 -1103 -854 C ATOM 1542 OH TYR A 212 28.594 36.276 28.725 1.00195.48 O ANISOU 1542 OH TYR A 212 21919 22424 29930 -3113 -1021 -757 O ATOM 1543 N ARG A 213 33.973 35.617 24.134 1.00150.12 N ANISOU 1543 N ARG A 213 17578 15563 23898 -2722 -1282 -900 N ATOM 1544 CA ARG A 213 35.050 36.029 25.027 1.00148.93 C ANISOU 1544 CA ARG A 213 17533 15315 23736 -2431 -1195 -702 C ATOM 1545 C ARG A 213 35.924 37.120 24.419 1.00145.24 C ANISOU 1545 C ARG A 213 17088 14947 23150 -2196 -1369 -654 C ATOM 1546 O ARG A 213 36.515 37.914 25.159 1.00159.95 O ANISOU 1546 O ARG A 213 18926 16845 25002 -1970 -1379 -512 O ATOM 1547 CB ARG A 213 35.911 34.821 25.402 1.00155.96 C ANISOU 1547 CB ARG A 213 18720 15874 24662 -2430 -953 -644 C ATOM 1548 N GLU A 214 36.016 37.182 23.089 1.00126.08 N ANISOU 1548 N GLU A 214 14704 12577 20623 -2262 -1506 -770 N ATOM 1549 CA GLU A 214 36.926 38.130 22.454 1.00107.10 C ANISOU 1549 CA GLU A 214 12345 10256 18092 -2073 -1647 -695 C ATOM 1550 C GLU A 214 36.323 39.522 22.302 1.00118.54 C ANISOU 1550 C GLU A 214 13580 11938 19520 -1981 -1881 -647 C ATOM 1551 O GLU A 214 37.071 40.503 22.224 1.00127.92 O ANISOU 1551 O GLU A 214 14799 13156 20649 -1805 -1977 -524 O ATOM 1552 CB GLU A 214 37.371 37.604 21.087 1.00106.75 C ANISOU 1552 CB GLU A 214 12448 10197 17914 -2160 -1681 -821 C ATOM 1553 CG GLU A 214 38.290 36.395 21.153 1.00126.60 C ANISOU 1553 CG GLU A 214 15221 12456 20426 -2153 -1461 -857 C ATOM 1554 CD GLU A 214 39.642 36.721 21.755 1.00134.39 C ANISOU 1554 CD GLU A 214 16308 13382 21372 -1896 -1372 -677 C ATOM 1555 OE1 GLU A 214 40.121 37.858 21.565 1.00151.15 O ANISOU 1555 OE1 GLU A 214 18350 15668 23410 -1769 -1509 -568 O ATOM 1556 OE2 GLU A 214 40.225 35.841 22.422 1.00148.45 O ANISOU 1556 OE2 GLU A 214 18247 14955 23203 -1826 -1168 -639 O ATOM 1557 N THR A 215 34.991 39.638 22.244 1.00128.72 N ANISOU 1557 N THR A 215 14656 13395 20858 -2096 -1978 -739 N ATOM 1558 CA THR A 215 34.383 40.961 22.113 1.00132.27 C ANISOU 1558 CA THR A 215 14909 14057 21290 -1957 -2205 -691 C ATOM 1559 C THR A 215 34.689 41.841 23.315 1.00105.63 C ANISOU 1559 C THR A 215 11500 10639 17995 -1729 -2186 -555 C ATOM 1560 O THR A 215 34.738 43.069 23.186 1.00107.56 O ANISOU 1560 O THR A 215 11700 10949 18219 -1551 -2363 -478 O ATOM 1561 CB THR A 215 32.870 40.848 21.909 1.00133.01 C ANISOU 1561 CB THR A 215 14742 14385 21411 -2099 -2301 -826 C ATOM 1562 OG1 THR A 215 32.287 40.086 22.975 1.00144.95 O ANISOU 1562 OG1 THR A 215 16164 15863 23046 -2223 -2112 -866 O ATOM 1563 CG2 THR A 215 32.552 40.206 20.567 1.00112.51 C ANISOU 1563 CG2 THR A 215 12159 11886 18702 -2316 -2380 -984 C ATOM 1564 N GLU A 216 34.891 41.238 24.488 1.00113.22 N ANISOU 1564 N GLU A 216 12493 11486 19040 -1729 -1977 -525 N ATOM 1565 CA GLU A 216 35.383 41.999 25.630 1.00115.11 C ANISOU 1565 CA GLU A 216 12725 11692 19320 -1512 -1947 -414 C ATOM 1566 C GLU A 216 36.738 42.622 25.320 1.00103.13 C ANISOU 1566 C GLU A 216 11387 10068 17731 -1380 -2000 -308 C ATOM 1567 O GLU A 216 36.983 43.792 25.639 1.00105.74 O ANISOU 1567 O GLU A 216 11689 10415 18070 -1214 -2120 -245 O ATOM 1568 CB GLU A 216 35.477 41.095 26.858 1.00128.48 C ANISOU 1568 CB GLU A 216 14441 13301 21074 -1543 -1698 -381 C ATOM 1569 CG GLU A 216 34.142 40.551 27.335 1.00147.46 C ANISOU 1569 CG GLU A 216 16644 15834 23550 -1694 -1625 -456 C ATOM 1570 CD GLU A 216 34.284 39.628 28.528 1.00161.06 C ANISOU 1570 CD GLU A 216 18416 17463 25316 -1737 -1365 -379 C ATOM 1571 OE1 GLU A 216 35.433 39.339 28.924 1.00164.29 O ANISOU 1571 OE1 GLU A 216 19025 17704 25695 -1633 -1249 -275 O ATOM 1572 OE2 GLU A 216 33.248 39.184 29.065 1.00166.79 O ANISOU 1572 OE2 GLU A 216 18971 18305 26094 -1876 -1275 -409 O ATOM 1573 N ASN A 217 37.628 41.854 24.685 1.00 93.72 N ANISOU 1573 N ASN A 217 10376 8770 16464 -1460 -1909 -299 N ATOM 1574 CA ASN A 217 38.944 42.371 24.326 1.00 99.31 C ANISOU 1574 CA ASN A 217 11223 9431 17081 -1363 -1944 -198 C ATOM 1575 C ASN A 217 38.850 43.393 23.200 1.00 92.02 C ANISOU 1575 C ASN A 217 10281 8599 16082 -1358 -2176 -169 C ATOM 1576 O ASN A 217 39.623 44.358 23.164 1.00106.42 O ANISOU 1576 O ASN A 217 12155 10408 17871 -1265 -2263 -57 O ATOM 1577 CB ASN A 217 39.865 41.220 23.924 1.00 96.15 C ANISOU 1577 CB ASN A 217 11000 8930 16603 -1420 -1775 -211 C ATOM 1578 CG ASN A 217 40.202 40.311 25.087 1.00123.82 C ANISOU 1578 CG ASN A 217 14565 12314 20168 -1370 -1546 -181 C ATOM 1579 OD1 ASN A 217 40.454 40.774 26.199 1.00146.24 O ANISOU 1579 OD1 ASN A 217 17351 15170 23044 -1241 -1511 -98 O ATOM 1580 ND2 ASN A 217 40.210 39.008 24.834 1.00138.56 N ANISOU 1580 ND2 ASN A 217 16558 14053 22037 -1468 -1391 -249 N ATOM 1581 N ARG A 218 37.917 43.191 22.268 1.00105.03 N ANISOU 1581 N ARG A 218 11858 10352 17697 -1470 -2280 -261 N ATOM 1582 CA ARG A 218 37.722 44.154 21.190 1.00106.97 C ANISOU 1582 CA ARG A 218 12079 10712 17852 -1446 -2510 -208 C ATOM 1583 C ARG A 218 37.335 45.519 21.747 1.00108.16 C ANISOU 1583 C ARG A 218 12143 10863 18090 -1274 -2667 -121 C ATOM 1584 O ARG A 218 37.805 46.554 21.261 1.00109.59 O ANISOU 1584 O ARG A 218 12396 11019 18222 -1200 -2812 8 O ATOM 1585 CB ARG A 218 36.650 43.636 20.226 1.00114.54 C ANISOU 1585 CB ARG A 218 12936 11832 18750 -1586 -2597 -343 C ATOM 1586 CG ARG A 218 36.522 44.380 18.897 1.00 97.29 C ANISOU 1586 CG ARG A 218 10747 9806 16414 -1573 -2821 -284 C ATOM 1587 CD ARG A 218 35.657 45.619 19.018 1.00110.14 C ANISOU 1587 CD ARG A 218 12233 11518 18097 -1414 -3034 -206 C ATOM 1588 NE ARG A 218 34.380 45.356 19.675 1.00103.46 N ANISOU 1588 NE ARG A 218 11170 10775 17366 -1415 -3032 -339 N ATOM 1589 CZ ARG A 218 33.291 44.912 19.058 1.00105.57 C ANISOU 1589 CZ ARG A 218 11264 11268 17579 -1524 -3114 -474 C ATOM 1590 NH1 ARG A 218 33.310 44.680 17.753 1.00117.23 N ANISOU 1590 NH1 ARG A 218 12774 12888 18882 -1629 -3215 -504 N ATOM 1591 NH2 ARG A 218 32.180 44.709 19.751 1.00111.51 N ANISOU 1591 NH2 ARG A 218 11792 12141 18435 -1536 -3096 -584 N ATOM 1592 N ASN A1001 36.469 45.539 22.764 1.00104.36 N ANISOU 1592 N ASN A1001 11514 10404 17734 -1209 -2636 -192 N ATOM 1593 CA ASN A1001 36.034 46.805 23.343 1.00104.22 C ANISOU 1593 CA ASN A1001 11415 10382 17801 -1010 -2780 -151 C ATOM 1594 C ASN A1001 37.177 47.497 24.072 1.00114.86 C ANISOU 1594 C ASN A1001 12900 11560 19183 -908 -2747 -54 C ATOM 1595 O ASN A1001 37.301 48.727 24.022 1.00103.16 O ANISOU 1595 O ASN A1001 11465 10000 17732 -782 -2909 22 O ATOM 1596 CB ASN A1001 34.863 46.568 24.294 1.00 96.58 C ANISOU 1596 CB ASN A1001 10233 9530 16934 -961 -2728 -269 C ATOM 1597 CG ASN A1001 33.640 46.032 23.585 1.00107.72 C ANISOU 1597 CG ASN A1001 11463 11153 18313 -1077 -2790 -375 C ATOM 1598 OD1 ASN A1001 33.326 46.441 22.468 1.00118.49 O ANISOU 1598 OD1 ASN A1001 12811 12614 19596 -1073 -2974 -355 O ATOM 1599 ND2 ASN A1001 32.934 45.117 24.237 1.00109.20 N ANISOU 1599 ND2 ASN A1001 11504 11435 18553 -1194 -2637 -483 N ATOM 1600 N ILE A1002 38.015 46.722 24.763 1.00114.15 N ANISOU 1600 N ILE A1002 12877 11408 19087 -961 -2541 -57 N ATOM 1601 CA ILE A1002 39.192 47.288 25.417 1.00106.91 C ANISOU 1601 CA ILE A1002 12066 10382 18173 -891 -2507 22 C ATOM 1602 C ILE A1002 40.108 47.928 24.384 1.00102.48 C ANISOU 1602 C ILE A1002 11644 9771 17523 -947 -2619 148 C ATOM 1603 O ILE A1002 40.701 48.986 24.627 1.00105.96 O ANISOU 1603 O ILE A1002 12151 10118 17991 -894 -2711 222 O ATOM 1604 CB ILE A1002 39.921 46.201 26.228 1.00102.87 C ANISOU 1604 CB ILE A1002 11587 9862 17637 -922 -2266 10 C ATOM 1605 CG1 ILE A1002 39.003 45.650 27.320 1.00 95.14 C ANISOU 1605 CG1 ILE A1002 10474 8939 16737 -878 -2149 -77 C ATOM 1606 CG2 ILE A1002 41.205 46.749 26.835 1.00 87.85 C ANISOU 1606 CG2 ILE A1002 9763 7909 15705 -860 -2241 82 C ATOM 1607 CD1 ILE A1002 39.525 44.391 27.975 1.00 98.97 C ANISOU 1607 CD1 ILE A1002 11008 9403 17192 -917 -1905 -61 C ATOM 1608 N PHE A1003 40.232 47.298 23.213 1.00102.50 N ANISOU 1608 N PHE A1003 11693 9842 17411 -1069 -2611 168 N ATOM 1609 CA PHE A1003 41.022 47.873 22.129 1.00100.69 C ANISOU 1609 CA PHE A1003 11576 9619 17063 -1134 -2711 304 C ATOM 1610 C PHE A1003 40.521 49.265 21.766 1.00112.68 C ANISOU 1610 C PHE A1003 13107 11079 18627 -1060 -2947 400 C ATOM 1611 O PHE A1003 41.294 50.228 21.738 1.00125.55 O ANISOU 1611 O PHE A1003 14839 12604 20258 -1065 -3021 531 O ATOM 1612 CB PHE A1003 40.976 46.957 20.906 1.00116.85 C ANISOU 1612 CB PHE A1003 13645 11793 18961 -1255 -2677 272 C ATOM 1613 CG PHE A1003 41.775 47.463 19.741 1.00115.34 C ANISOU 1613 CG PHE A1003 13550 11666 18606 -1326 -2761 418 C ATOM 1614 CD1 PHE A1003 43.142 47.259 19.678 1.00109.48 C ANISOU 1614 CD1 PHE A1003 12886 10948 17763 -1377 -2639 488 C ATOM 1615 CD2 PHE A1003 41.160 48.167 18.719 1.00116.68 C ANISOU 1615 CD2 PHE A1003 13718 11908 18708 -1332 -2961 502 C ATOM 1616 CE1 PHE A1003 43.877 47.728 18.605 1.00117.96 C ANISOU 1616 CE1 PHE A1003 14027 12125 18668 -1461 -2702 636 C ATOM 1617 CE2 PHE A1003 41.889 48.643 17.648 1.00113.12 C ANISOU 1617 CE2 PHE A1003 13358 11538 18086 -1407 -3029 668 C ATOM 1618 CZ PHE A1003 43.249 48.423 17.590 1.00120.62 C ANISOU 1618 CZ PHE A1003 14377 12519 18934 -1485 -2893 734 C ATOM 1619 N GLU A1004 39.223 49.387 21.481 1.00120.71 N ANISOU 1619 N GLU A1004 14021 12161 19682 -990 -3069 341 N ATOM 1620 CA GLU A1004 38.663 50.690 21.141 1.00126.98 C ANISOU 1620 CA GLU A1004 14835 12890 20522 -864 -3301 439 C ATOM 1621 C GLU A1004 38.698 51.646 22.327 1.00110.91 C ANISOU 1621 C GLU A1004 12822 10667 18652 -712 -3338 421 C ATOM 1622 O GLU A1004 38.858 52.857 22.138 1.00112.89 O ANISOU 1622 O GLU A1004 13191 10753 18948 -638 -3499 542 O ATOM 1623 CB GLU A1004 37.234 50.526 20.624 1.00131.07 C ANISOU 1623 CB GLU A1004 15196 13580 21026 -793 -3420 362 C ATOM 1624 CG GLU A1004 37.147 49.831 19.276 1.00125.58 C ANISOU 1624 CG GLU A1004 14492 13079 20144 -939 -3443 377 C ATOM 1625 CD GLU A1004 37.708 50.677 18.147 1.00136.15 C ANISOU 1625 CD GLU A1004 15977 14403 21349 -953 -3594 598 C ATOM 1626 OE1 GLU A1004 37.576 51.919 18.206 1.00134.61 O ANISOU 1626 OE1 GLU A1004 15853 14065 21227 -809 -3757 740 O ATOM 1627 OE2 GLU A1004 38.286 50.099 17.202 1.00137.41 O ANISOU 1627 OE2 GLU A1004 16193 14690 21328 -1104 -3543 634 O ATOM 1628 N MET A1005 38.540 51.127 23.547 1.00104.66 N ANISOU 1628 N MET A1005 11931 9891 17944 -663 -3193 271 N ATOM 1629 CA MET A1005 38.669 51.966 24.733 1.00 93.20 C ANISOU 1629 CA MET A1005 10498 8294 16621 -522 -3212 219 C ATOM 1630 C MET A1005 40.047 52.608 24.793 1.00110.24 C ANISOU 1630 C MET A1005 12833 10287 18767 -615 -3216 329 C ATOM 1631 O MET A1005 40.175 53.836 24.875 1.00108.89 O ANISOU 1631 O MET A1005 12775 9920 18679 -547 -3366 381 O ATOM 1632 CB MET A1005 38.424 51.134 25.990 1.00105.32 C ANISOU 1632 CB MET A1005 11893 9929 18194 -484 -3023 63 C ATOM 1633 CG MET A1005 38.387 51.942 27.271 1.00102.06 C ANISOU 1633 CG MET A1005 11463 9428 17885 -314 -3043 -35 C ATOM 1634 SD MET A1005 38.209 50.895 28.726 1.00113.24 S ANISOU 1634 SD MET A1005 12717 11014 19296 -282 -2800 -174 S ATOM 1635 CE MET A1005 38.076 52.130 30.011 1.00122.54 C ANISOU 1635 CE MET A1005 13882 12111 20567 -51 -2884 -310 C ATOM 1636 N LEU A1006 41.096 51.785 24.748 1.00112.31 N ANISOU 1636 N LEU A1006 13120 10627 18928 -774 -3051 362 N ATOM 1637 CA LEU A1006 42.457 52.296 24.818 1.00114.04 C ANISOU 1637 CA LEU A1006 13457 10762 19112 -888 -3038 459 C ATOM 1638 C LEU A1006 42.874 53.018 23.545 1.00120.43 C ANISOU 1638 C LEU A1006 14399 11504 19852 -1009 -3175 657 C ATOM 1639 O LEU A1006 43.780 53.856 23.595 1.00109.13 O ANISOU 1639 O LEU A1006 13078 9952 18434 -1108 -3223 753 O ATOM 1640 CB LEU A1006 43.424 51.152 25.117 1.00100.50 C ANISOU 1640 CB LEU A1006 11699 9199 17286 -980 -2819 440 C ATOM 1641 CG LEU A1006 43.255 50.546 26.511 1.00109.05 C ANISOU 1641 CG LEU A1006 12676 10336 18420 -868 -2674 293 C ATOM 1642 CD1 LEU A1006 44.120 49.310 26.689 1.00102.57 C ANISOU 1642 CD1 LEU A1006 11833 9656 17484 -920 -2461 302 C ATOM 1643 CD2 LEU A1006 43.584 51.585 27.567 1.00 98.48 C ANISOU 1643 CD2 LEU A1006 11354 8896 17168 -803 -2742 235 C ATOM 1644 N ARG A1007 42.237 52.719 22.409 1.00108.46 N ANISOU 1644 N ARG A1007 12874 10083 18253 -1019 -3238 722 N ATOM 1645 CA ARG A1007 42.607 53.389 21.167 1.00105.07 C ANISOU 1645 CA ARG A1007 12570 9627 17725 -1125 -3364 937 C ATOM 1646 C ARG A1007 42.346 54.886 21.245 1.00122.25 C ANISOU 1646 C ARG A1007 14879 11535 20034 -1046 -3568 1043 C ATOM 1647 O ARG A1007 43.135 55.688 20.732 1.00142.93 O ANISOU 1647 O ARG A1007 17648 14037 22622 -1184 -3635 1237 O ATOM 1648 CB ARG A1007 41.852 52.787 19.983 1.00121.01 C ANISOU 1648 CB ARG A1007 14535 11835 19610 -1124 -3409 963 C ATOM 1649 CG ARG A1007 42.261 53.397 18.654 1.00109.84 C ANISOU 1649 CG ARG A1007 13240 10449 18045 -1232 -3525 1206 C ATOM 1650 CD ARG A1007 41.560 52.743 17.482 1.00115.04 C ANISOU 1650 CD ARG A1007 13830 11348 18531 -1232 -3570 1205 C ATOM 1651 NE ARG A1007 41.964 53.354 16.220 1.00119.57 N ANISOU 1651 NE ARG A1007 14516 11986 18929 -1325 -3679 1459 N ATOM 1652 CZ ARG A1007 41.528 52.964 15.027 1.00122.92 C ANISOU 1652 CZ ARG A1007 14902 12653 19150 -1342 -3741 1500 C ATOM 1653 NH1 ARG A1007 41.954 53.578 13.932 1.00136.10 N ANISOU 1653 NH1 ARG A1007 16677 14396 20640 -1425 -3832 1760 N ATOM 1654 NH2 ARG A1007 40.668 51.960 14.927 1.00126.00 N ANISOU 1654 NH2 ARG A1007 15145 13225 19504 -1296 -3710 1281 N ATOM 1655 N ILE A1008 41.244 55.286 21.878 1.00104.78 N ANISOU 1655 N ILE A1008 12620 9220 17972 -823 -3664 920 N ATOM 1656 CA ILE A1008 40.955 56.712 21.955 1.00119.18 C ANISOU 1656 CA ILE A1008 14599 10749 19935 -702 -3862 1003 C ATOM 1657 C ILE A1008 41.691 57.353 23.131 1.00129.17 C ANISOU 1657 C ILE A1008 15948 11793 21337 -732 -3831 908 C ATOM 1658 O ILE A1008 41.975 58.556 23.104 1.00145.12 O ANISOU 1658 O ILE A1008 18164 13515 23460 -746 -3968 1007 O ATOM 1659 CB ILE A1008 39.434 56.954 22.017 1.00133.38 C ANISOU 1659 CB ILE A1008 16306 12556 21815 -409 -3998 913 C ATOM 1660 CG1 ILE A1008 38.818 56.416 23.310 1.00150.21 C ANISOU 1660 CG1 ILE A1008 18249 14783 24039 -260 -3889 637 C ATOM 1661 CG2 ILE A1008 38.746 56.309 20.824 1.00129.02 C ANISOU 1661 CG2 ILE A1008 15650 12267 21104 -412 -4041 992 C ATOM 1662 CD1 ILE A1008 38.703 57.459 24.409 1.00151.59 C ANISOU 1662 CD1 ILE A1008 18503 14699 24395 -78 -3964 517 C ATOM 1663 N ASP A1009 42.015 56.578 24.172 1.00119.94 N ANISOU 1663 N ASP A1009 14643 10760 20167 -747 -3657 717 N ATOM 1664 CA ASP A1009 42.786 57.119 25.288 1.00122.59 C ANISOU 1664 CA ASP A1009 15033 10952 20595 -790 -3626 610 C ATOM 1665 C ASP A1009 44.275 57.187 24.963 1.00116.53 C ANISOU 1665 C ASP A1009 14343 10199 19733 -1085 -3562 750 C ATOM 1666 O ASP A1009 44.925 58.207 25.212 1.00124.56 O ANISOU 1666 O ASP A1009 15504 10990 20832 -1199 -3645 783 O ATOM 1667 CB ASP A1009 42.565 56.289 26.557 1.00101.61 C ANISOU 1667 CB ASP A1009 12190 8475 17943 -674 -3468 374 C ATOM 1668 CG ASP A1009 41.206 56.525 27.183 1.00 96.64 C ANISOU 1668 CG ASP A1009 11477 7817 17425 -388 -3536 205 C ATOM 1669 OD1 ASP A1009 40.620 57.602 26.951 1.00106.52 O ANISOU 1669 OD1 ASP A1009 12844 8840 18789 -246 -3723 225 O ATOM 1670 OD2 ASP A1009 40.742 55.651 27.942 1.00107.27 O ANISOU 1670 OD2 ASP A1009 12641 9373 18743 -296 -3398 59 O ATOM 1671 N GLU A1010 44.833 56.110 24.413 1.00119.74 N ANISOU 1671 N GLU A1010 14653 10877 19967 -1215 -3412 820 N ATOM 1672 CA GLU A1010 46.267 56.031 24.166 1.00112.89 C ANISOU 1672 CA GLU A1010 13800 10112 18980 -1469 -3323 932 C ATOM 1673 C GLU A1010 46.666 56.485 22.767 1.00113.39 C ANISOU 1673 C GLU A1010 13983 10157 18942 -1654 -3401 1199 C ATOM 1674 O GLU A1010 47.862 56.660 22.511 1.00117.67 O ANISOU 1674 O GLU A1010 14543 10777 19391 -1891 -3348 1317 O ATOM 1675 CB GLU A1010 46.763 54.597 24.381 1.00110.21 C ANISOU 1675 CB GLU A1010 13293 10090 18492 -1474 -3104 856 C ATOM 1676 CG GLU A1010 46.638 54.067 25.803 1.00114.74 C ANISOU 1676 CG GLU A1010 13747 10729 19122 -1327 -2994 640 C ATOM 1677 CD GLU A1010 47.611 54.710 26.769 1.00132.94 C ANISOU 1677 CD GLU A1010 16051 13003 21457 -1415 -2995 575 C ATOM 1678 OE1 GLU A1010 48.709 55.112 26.334 1.00153.21 O ANISOU 1678 OE1 GLU A1010 18655 15607 23951 -1637 -3003 698 O ATOM 1679 OE2 GLU A1010 47.284 54.794 27.971 1.00142.20 O ANISOU 1679 OE2 GLU A1010 17170 14150 22709 -1275 -2984 394 O ATOM 1680 N GLY A1011 45.710 56.672 21.861 1.00114.12 N ANISOU 1680 N GLY A1011 14139 10191 19031 -1555 -3521 1304 N ATOM 1681 CA GLY A1011 46.016 57.024 20.492 1.00108.94 C ANISOU 1681 CA GLY A1011 13587 9565 18239 -1710 -3590 1575 C ATOM 1682 C GLY A1011 46.436 55.821 19.666 1.00114.57 C ANISOU 1682 C GLY A1011 14177 10643 18713 -1794 -3438 1608 C ATOM 1683 O GLY A1011 46.600 54.704 20.159 1.00110.98 O ANISOU 1683 O GLY A1011 13577 10381 18208 -1746 -3273 1431 O ATOM 1684 N LEU A1012 46.614 56.065 18.368 1.00111.52 N ANISOU 1684 N LEU A1012 13864 10344 18164 -1912 -3496 1844 N ATOM 1685 CA LEU A1012 47.060 55.028 17.439 1.00109.55 C ANISOU 1685 CA LEU A1012 13516 10451 17657 -1994 -3364 1875 C ATOM 1686 C LEU A1012 47.925 55.680 16.371 1.00118.64 C ANISOU 1686 C LEU A1012 14759 11685 18635 -2228 -3394 2175 C ATOM 1687 O LEU A1012 47.428 56.480 15.573 1.00138.02 O ANISOU 1687 O LEU A1012 17344 14028 21068 -2230 -3556 2391 O ATOM 1688 CB LEU A1012 45.877 54.301 16.806 1.00120.83 C ANISOU 1688 CB LEU A1012 14885 12010 19015 -1825 -3407 1787 C ATOM 1689 CG LEU A1012 46.250 53.245 15.759 1.00112.63 C ANISOU 1689 CG LEU A1012 13770 11323 17702 -1899 -3288 1784 C ATOM 1690 CD1 LEU A1012 47.086 52.132 16.367 1.00105.36 C ANISOU 1690 CD1 LEU A1012 12740 10554 16738 -1920 -3058 1600 C ATOM 1691 CD2 LEU A1012 45.012 52.676 15.083 1.00116.34 C ANISOU 1691 CD2 LEU A1012 14190 11911 18104 -1767 -3367 1689 C ATOM 1692 N ARG A1013 49.210 55.334 16.354 1.00127.81 N ANISOU 1692 N ARG A1013 15840 13064 19657 -2414 -3234 2204 N ATOM 1693 CA ARG A1013 50.138 55.817 15.340 1.00130.95 C ANISOU 1693 CA ARG A1013 16278 13626 19850 -2666 -3222 2486 C ATOM 1694 C ARG A1013 51.069 54.681 14.948 1.00136.57 C ANISOU 1694 C ARG A1013 16816 14771 20305 -2718 -3009 2413 C ATOM 1695 O ARG A1013 51.596 53.981 15.817 1.00141.20 O ANISOU 1695 O ARG A1013 17277 15447 20927 -2666 -2867 2211 O ATOM 1696 CB ARG A1013 50.944 57.023 15.842 1.00128.59 C ANISOU 1696 CB ARG A1013 16076 13099 19683 -2905 -3271 2640 C ATOM 1697 CG ARG A1013 50.112 58.286 16.030 1.00145.12 C ANISOU 1697 CG ARG A1013 18397 14728 22016 -2860 -3492 2753 C ATOM 1698 CD ARG A1013 50.952 59.458 16.510 1.00153.21 C ANISOU 1698 CD ARG A1013 19544 15489 23179 -3135 -3537 2882 C ATOM 1699 NE ARG A1013 50.138 60.652 16.714 1.00164.78 N ANISOU 1699 NE ARG A1013 21262 16457 24890 -3054 -3749 2966 N ATOM 1700 CZ ARG A1013 50.601 61.805 17.186 1.00177.18 C ANISOU 1700 CZ ARG A1013 23008 17668 26644 -3259 -3831 3049 C ATOM 1701 NH1 ARG A1013 51.881 61.927 17.507 1.00182.95 N ANISOU 1701 NH1 ARG A1013 23660 18520 27332 -3591 -3722 3060 N ATOM 1702 NH2 ARG A1013 49.782 62.837 17.336 1.00194.19 N ANISOU 1702 NH2 ARG A1013 25416 19344 29025 -3128 -4025 3109 N ATOM 1703 N LEU A1014 51.258 54.495 13.643 1.00135.32 N ANISOU 1703 N LEU A1014 16651 14893 19873 -2795 -2990 2576 N ATOM 1704 CA LEU A1014 52.126 53.446 13.127 1.00120.88 C ANISOU 1704 CA LEU A1014 14664 13495 17768 -2816 -2792 2503 C ATOM 1705 C LEU A1014 53.583 53.875 13.022 1.00124.09 C ANISOU 1705 C LEU A1014 14988 14126 18037 -3080 -2686 2681 C ATOM 1706 O LEU A1014 54.434 53.041 12.690 1.00118.10 O ANISOU 1706 O LEU A1014 14071 13755 17044 -3079 -2509 2612 O ATOM 1707 CB LEU A1014 51.634 52.980 11.752 1.00112.00 C ANISOU 1707 CB LEU A1014 13551 12626 16378 -2762 -2815 2554 C ATOM 1708 CG LEU A1014 50.272 52.285 11.695 1.00119.03 C ANISOU 1708 CG LEU A1014 14466 13423 17339 -2524 -2891 2333 C ATOM 1709 CD1 LEU A1014 49.872 52.020 10.251 1.00130.84 C ANISOU 1709 CD1 LEU A1014 15970 15206 18538 -2516 -2942 2409 C ATOM 1710 CD2 LEU A1014 50.284 50.990 12.497 1.00105.53 C ANISOU 1710 CD2 LEU A1014 12654 11737 15704 -2361 -2730 1991 C ATOM 1711 N LYS A1015 53.890 55.143 13.286 1.00120.74 N ANISOU 1711 N LYS A1015 14660 13469 17745 -3307 -2789 2898 N ATOM 1712 CA LYS A1015 55.252 55.650 13.254 1.00123.83 C ANISOU 1712 CA LYS A1015 14961 14062 18028 -3617 -2698 3071 C ATOM 1713 C LYS A1015 55.648 56.145 14.638 1.00131.57 C ANISOU 1713 C LYS A1015 15924 14794 19272 -3698 -2715 2954 C ATOM 1714 O LYS A1015 54.795 56.523 15.447 1.00131.63 O ANISOU 1714 O LYS A1015 16062 14391 19559 -3567 -2843 2837 O ATOM 1715 CB LYS A1015 55.403 56.781 12.230 1.00119.30 C ANISOU 1715 CB LYS A1015 14527 13453 17348 -3899 -2798 3468 C ATOM 1716 N ILE A1016 56.956 56.139 14.903 1.00137.94 N ANISOU 1716 N ILE A1016 16548 15893 19968 -3910 -2585 2974 N ATOM 1717 CA ILE A1016 57.457 56.528 16.215 1.00126.99 C ANISOU 1717 CA ILE A1016 15104 14362 18785 -4001 -2593 2835 C ATOM 1718 C ILE A1016 57.150 57.998 16.466 1.00125.29 C ANISOU 1718 C ILE A1016 15123 13664 18817 -4236 -2784 2993 C ATOM 1719 O ILE A1016 57.265 58.840 15.564 1.00133.79 O ANISOU 1719 O ILE A1016 16334 14668 19833 -4491 -2852 3303 O ATOM 1720 CB ILE A1016 58.966 56.248 16.319 1.00131.19 C ANISOU 1720 CB ILE A1016 15358 15382 19107 -4199 -2422 2844 C ATOM 1721 CG1 ILE A1016 59.249 54.758 16.130 1.00135.03 C ANISOU 1721 CG1 ILE A1016 15637 16304 19364 -3901 -2232 2665 C ATOM 1722 CG2 ILE A1016 59.507 56.698 17.667 1.00130.15 C ANISOU 1722 CG2 ILE A1016 15146 15143 19161 -4316 -2447 2694 C ATOM 1723 CD1 ILE A1016 60.722 54.438 15.986 1.00130.48 C ANISOU 1723 CD1 ILE A1016 14765 16289 18523 -4049 -2057 2701 C ATOM 1724 N TYR A1017 56.745 58.313 17.695 1.00127.27 N ANISOU 1724 N TYR A1017 15441 13573 19344 -4139 -2871 2781 N ATOM 1725 CA TYR A1017 56.453 59.685 18.077 1.00138.97 C ANISOU 1725 CA TYR A1017 17163 14552 21087 -4323 -3054 2867 C ATOM 1726 C TYR A1017 56.781 59.866 19.552 1.00137.21 C ANISOU 1726 C TYR A1017 16868 14215 21050 -4335 -3065 2589 C ATOM 1727 O TYR A1017 56.822 58.903 20.322 1.00134.61 O ANISOU 1727 O TYR A1017 16350 14109 20687 -4094 -2963 2331 O ATOM 1728 CB TYR A1017 54.985 60.047 17.811 1.00135.93 C ANISOU 1728 CB TYR A1017 17038 13736 20873 -4068 -3224 2901 C ATOM 1729 CG TYR A1017 54.008 59.355 18.735 1.00126.39 C ANISOU 1729 CG TYR A1017 15793 12419 19811 -3670 -3237 2576 C ATOM 1730 CD1 TYR A1017 53.527 58.085 18.449 1.00135.60 C ANISOU 1730 CD1 TYR A1017 16825 13862 20836 -3390 -3134 2456 C ATOM 1731 CD2 TYR A1017 53.554 59.982 19.889 1.00123.27 C ANISOU 1731 CD2 TYR A1017 15503 11642 19690 -3586 -3348 2384 C ATOM 1732 CE1 TYR A1017 52.633 57.452 19.295 1.00132.50 C ANISOU 1732 CE1 TYR A1017 16396 13373 20576 -3068 -3134 2183 C ATOM 1733 CE2 TYR A1017 52.662 59.360 20.738 1.00130.14 C ANISOU 1733 CE2 TYR A1017 16320 12455 20671 -3237 -3346 2105 C ATOM 1734 CZ TYR A1017 52.204 58.097 20.438 1.00124.52 C ANISOU 1734 CZ TYR A1017 15468 12024 19820 -2993 -3236 2021 C ATOM 1735 OH TYR A1017 51.315 57.481 21.286 1.00123.52 O ANISOU 1735 OH TYR A1017 15287 11842 19804 -2684 -3223 1767 O ATOM 1736 N LYS A1018 57.014 61.118 19.937 1.00145.86 N ANISOU 1736 N LYS A1018 18130 14954 22337 -4619 -3192 2645 N ATOM 1737 CA LYS A1018 57.220 61.455 21.337 1.00138.97 C ANISOU 1737 CA LYS A1018 17225 13926 21651 -4639 -3238 2361 C ATOM 1738 C LYS A1018 55.878 61.645 22.033 1.00146.75 C ANISOU 1738 C LYS A1018 18404 14468 22887 -4282 -3372 2159 C ATOM 1739 O LYS A1018 54.961 62.266 21.487 1.00159.20 O ANISOU 1739 O LYS A1018 20242 15653 24592 -4195 -3508 2300 O ATOM 1740 CB LYS A1018 58.065 62.722 21.464 1.00120.33 C ANISOU 1740 CB LYS A1018 14968 11362 19391 -5127 -3319 2470 C ATOM 1741 N ASP A1019 55.766 61.106 23.243 1.00140.75 N ANISOU 1741 N ASP A1019 17501 13800 22178 -4061 -3331 1837 N ATOM 1742 CA ASP A1019 54.512 61.143 23.984 1.00137.81 C ANISOU 1742 CA ASP A1019 17251 13106 22006 -3699 -3427 1620 C ATOM 1743 C ASP A1019 54.392 62.463 24.747 1.00149.13 C ANISOU 1743 C ASP A1019 18902 14065 23696 -3826 -3598 1499 C ATOM 1744 O ASP A1019 55.163 63.405 24.543 1.00140.81 O ANISOU 1744 O ASP A1019 17956 12855 22689 -4215 -3659 1623 O ATOM 1745 CB ASP A1019 54.408 59.932 24.909 1.00139.75 C ANISOU 1745 CB ASP A1019 17252 13679 22168 -3400 -3293 1356 C ATOM 1746 CG ASP A1019 55.516 59.885 25.950 1.00159.44 C ANISOU 1746 CG ASP A1019 19547 16431 24602 -3557 -3228 1176 C ATOM 1747 OD1 ASP A1019 56.414 60.752 25.920 1.00170.25 O ANISOU 1747 OD1 ASP A1019 20940 17759 25987 -3932 -3280 1240 O ATOM 1748 OD2 ASP A1019 55.486 58.976 26.805 1.00164.62 O ANISOU 1748 OD2 ASP A1019 20017 17342 25187 -3311 -3125 977 O ATOM 1749 N THR A1020 53.409 62.537 25.649 1.00160.71 N ANISOU 1749 N THR A1020 20437 15297 25330 -3500 -3674 1244 N ATOM 1750 CA THR A1020 53.187 63.748 26.430 1.00157.86 C ANISOU 1750 CA THR A1020 20297 14469 25215 -3552 -3838 1072 C ATOM 1751 C THR A1020 54.324 64.036 27.401 1.00159.15 C ANISOU 1751 C THR A1020 20337 14772 25362 -3842 -3816 868 C ATOM 1752 O THR A1020 54.427 65.163 27.896 1.00164.18 O ANISOU 1752 O THR A1020 21176 15016 26190 -4014 -3955 746 O ATOM 1753 CB THR A1020 51.865 63.646 27.194 1.00154.57 C ANISOU 1753 CB THR A1020 19929 13863 24937 -3096 -3902 822 C ATOM 1754 OG1 THR A1020 51.580 64.896 27.833 1.00164.61 O ANISOU 1754 OG1 THR A1020 21452 14639 26451 -3110 -4073 654 O ATOM 1755 CG2 THR A1020 51.937 62.548 28.246 1.00156.81 C ANISOU 1755 CG2 THR A1020 19916 14570 25095 -2888 -3757 557 C ATOM 1756 N GLU A1021 55.174 63.052 27.686 1.00158.70 N ANISOU 1756 N GLU A1021 19955 15263 25079 -3889 -3651 817 N ATOM 1757 CA GLU A1021 56.326 63.240 28.556 1.00143.77 C ANISOU 1757 CA GLU A1021 17891 13609 23126 -4164 -3628 635 C ATOM 1758 C GLU A1021 57.638 63.313 27.787 1.00140.03 C ANISOU 1758 C GLU A1021 17287 13427 22490 -4614 -3556 874 C ATOM 1759 O GLU A1021 58.700 63.416 28.408 1.00139.72 O ANISOU 1759 O GLU A1021 17050 13672 22363 -4877 -3528 745 O ATOM 1760 CB GLU A1021 56.397 62.115 29.594 1.00131.63 C ANISOU 1760 CB GLU A1021 16056 12524 21434 -3866 -3501 392 C ATOM 1761 N GLY A1022 57.591 63.260 26.456 1.00137.83 N ANISOU 1761 N GLY A1022 17091 13129 22147 -4708 -3523 1214 N ATOM 1762 CA GLY A1022 58.779 63.364 25.639 1.00134.05 C ANISOU 1762 CA GLY A1022 16487 12948 21498 -5135 -3445 1467 C ATOM 1763 C GLY A1022 59.450 62.053 25.293 1.00142.02 C ANISOU 1763 C GLY A1022 17143 14618 22198 -5032 -3240 1530 C ATOM 1764 O GLY A1022 60.519 62.073 24.669 1.00135.15 O ANISOU 1764 O GLY A1022 16111 14089 21150 -5370 -3157 1717 O ATOM 1765 N TYR A1023 58.867 60.918 25.670 1.00156.68 N ANISOU 1765 N TYR A1023 18881 16666 23984 -4580 -3152 1384 N ATOM 1766 CA TYR A1023 59.478 59.621 25.419 1.00160.98 C ANISOU 1766 CA TYR A1023 19122 17791 24252 -4432 -2956 1416 C ATOM 1767 C TYR A1023 58.937 59.029 24.123 1.00151.15 C ANISOU 1767 C TYR A1023 17954 16570 22908 -4281 -2890 1646 C ATOM 1768 O TYR A1023 57.763 59.208 23.787 1.00167.00 O ANISOU 1768 O TYR A1023 20197 18194 25059 -4097 -2981 1683 O ATOM 1769 CB TYR A1023 59.211 58.663 26.581 1.00149.85 C ANISOU 1769 CB TYR A1023 17553 16569 22813 -4040 -2885 1140 C ATOM 1770 CG TYR A1023 59.729 59.148 27.919 1.00135.19 C ANISOU 1770 CG TYR A1023 15591 14764 21009 -4146 -2948 886 C ATOM 1771 CD1 TYR A1023 61.085 59.120 28.218 1.00133.68 C ANISOU 1771 CD1 TYR A1023 15117 15036 20640 -4398 -2888 860 C ATOM 1772 CD2 TYR A1023 58.855 59.608 28.894 1.00127.48 C ANISOU 1772 CD2 TYR A1023 14776 13422 20240 -3977 -3068 655 C ATOM 1773 CE1 TYR A1023 61.556 59.557 29.444 1.00126.88 C ANISOU 1773 CE1 TYR A1023 14142 14263 19804 -4501 -2958 607 C ATOM 1774 CE2 TYR A1023 59.315 60.044 30.121 1.00130.54 C ANISOU 1774 CE2 TYR A1023 15066 13884 20651 -4065 -3130 395 C ATOM 1775 CZ TYR A1023 60.665 60.016 30.392 1.00132.28 C ANISOU 1775 CZ TYR A1023 15010 14562 20690 -4335 -3080 370 C ATOM 1776 OH TYR A1023 61.124 60.451 31.614 1.00142.36 O ANISOU 1776 OH TYR A1023 16173 15949 21969 -4432 -3155 92 O ATOM 1777 N TYR A1024 59.801 58.318 23.401 1.00127.38 N ANISOU 1777 N TYR A1024 14724 14042 19631 -4347 -2735 1781 N ATOM 1778 CA TYR A1024 59.416 57.747 22.116 1.00126.24 C ANISOU 1778 CA TYR A1024 14633 13984 19350 -4232 -2666 1979 C ATOM 1779 C TYR A1024 58.416 56.611 22.306 1.00143.48 C ANISOU 1779 C TYR A1024 16835 16134 21546 -3763 -2611 1823 C ATOM 1780 O TYR A1024 58.611 55.727 23.146 1.00149.15 O ANISOU 1780 O TYR A1024 17385 17071 22214 -3527 -2509 1627 O ATOM 1781 CB TYR A1024 60.652 57.260 21.361 1.00115.67 C ANISOU 1781 CB TYR A1024 13034 13211 17703 -4403 -2503 2126 C ATOM 1782 CG TYR A1024 61.519 58.385 20.835 1.00115.28 C ANISOU 1782 CG TYR A1024 12983 13201 17616 -4918 -2547 2357 C ATOM 1783 CD1 TYR A1024 61.179 59.056 19.668 1.00117.30 C ANISOU 1783 CD1 TYR A1024 13454 13244 17871 -5119 -2612 2651 C ATOM 1784 CD2 TYR A1024 62.671 58.778 21.502 1.00127.18 C ANISOU 1784 CD2 TYR A1024 14272 14971 19081 -5219 -2526 2292 C ATOM 1785 CE1 TYR A1024 61.957 60.084 19.178 1.00122.11 C ANISOU 1785 CE1 TYR A1024 14081 13866 18448 -5616 -2642 2897 C ATOM 1786 CE2 TYR A1024 63.460 59.809 21.018 1.00136.74 C ANISOU 1786 CE2 TYR A1024 15479 16212 20265 -5743 -2560 2510 C ATOM 1787 CZ TYR A1024 63.096 60.458 19.855 1.00130.48 C ANISOU 1787 CZ TYR A1024 14925 15169 19483 -5946 -2613 2823 C ATOM 1788 OH TYR A1024 63.869 61.483 19.361 1.00133.55 O ANISOU 1788 OH TYR A1024 15331 15567 19847 -6491 -2636 3074 O ATOM 1789 N THR A1025 57.345 56.639 21.514 1.00140.59 N ANISOU 1789 N THR A1025 16674 15502 21241 -3641 -2679 1923 N ATOM 1790 CA THR A1025 56.225 55.719 21.656 1.00129.07 C ANISOU 1790 CA THR A1025 15262 13947 19833 -3254 -2655 1778 C ATOM 1791 C THR A1025 55.699 55.368 20.271 1.00122.63 C ANISOU 1791 C THR A1025 14530 13172 18890 -3204 -2647 1944 C ATOM 1792 O THR A1025 55.804 56.165 19.335 1.00135.20 O ANISOU 1792 O THR A1025 16232 14698 20439 -3434 -2726 2183 O ATOM 1793 CB THR A1025 55.111 56.345 22.520 1.00122.50 C ANISOU 1793 CB THR A1025 14604 12658 19283 -3118 -2811 1637 C ATOM 1794 OG1 THR A1025 55.649 56.727 23.792 1.00118.52 O ANISOU 1794 OG1 THR A1025 14021 12144 18870 -3181 -2825 1466 O ATOM 1795 CG2 THR A1025 53.968 55.368 22.751 1.00118.72 C ANISOU 1795 CG2 THR A1025 14133 12126 18850 -2750 -2773 1483 C ATOM 1796 N ILE A1026 55.143 54.162 20.141 1.00109.60 N ANISOU 1796 N ILE A1026 12834 11639 17171 -2912 -2551 1819 N ATOM 1797 CA ILE A1026 54.523 53.725 18.894 1.00112.96 C ANISOU 1797 CA ILE A1026 13331 12116 17472 -2839 -2552 1914 C ATOM 1798 C ILE A1026 53.328 52.843 19.232 1.00114.13 C ANISOU 1798 C ILE A1026 13516 12126 17721 -2528 -2545 1713 C ATOM 1799 O ILE A1026 53.284 52.200 20.284 1.00103.24 O ANISOU 1799 O ILE A1026 12060 10743 16422 -2357 -2464 1519 O ATOM 1800 CB ILE A1026 55.532 52.983 17.982 1.00118.34 C ANISOU 1800 CB ILE A1026 13863 13258 17843 -2898 -2386 1991 C ATOM 1801 CG1 ILE A1026 54.979 52.841 16.561 1.00114.97 C ANISOU 1801 CG1 ILE A1026 13527 12898 17258 -2896 -2420 2123 C ATOM 1802 CG2 ILE A1026 55.878 51.617 18.559 1.00 99.14 C ANISOU 1802 CG2 ILE A1026 11278 11057 15334 -2646 -2203 1769 C ATOM 1803 CD1 ILE A1026 56.017 52.430 15.538 1.00120.57 C ANISOU 1803 CD1 ILE A1026 14102 14068 17640 -3005 -2279 2237 C ATOM 1804 N GLY A1027 52.343 52.829 18.336 1.00119.21 N ANISOU 1804 N GLY A1027 14270 12674 18352 -2467 -2634 1770 N ATOM 1805 CA GLY A1027 51.169 51.996 18.513 1.00122.53 C ANISOU 1805 CA GLY A1027 14708 12998 18852 -2222 -2631 1587 C ATOM 1806 C GLY A1027 50.182 52.545 19.521 1.00125.26 C ANISOU 1806 C GLY A1027 15117 13010 19466 -2107 -2754 1485 C ATOM 1807 O GLY A1027 49.967 53.759 19.590 1.00144.28 O ANISOU 1807 O GLY A1027 17636 15184 22002 -2192 -2913 1596 O ATOM 1808 N ILE A1028 49.573 51.663 20.307 1.00110.44 N ANISOU 1808 N ILE A1028 13181 11106 17675 -1909 -2676 1275 N ATOM 1809 CA ILE A1028 48.603 52.058 21.327 1.00112.34 C ANISOU 1809 CA ILE A1028 13446 11095 18143 -1773 -2766 1153 C ATOM 1810 C ILE A1028 49.373 52.145 22.642 1.00125.97 C ANISOU 1810 C ILE A1028 15102 12826 19935 -1768 -2687 1059 C ATOM 1811 O ILE A1028 49.462 51.181 23.405 1.00125.34 O ANISOU 1811 O ILE A1028 14929 12852 19843 -1639 -2542 922 O ATOM 1812 CB ILE A1028 47.421 51.092 21.407 1.00107.69 C ANISOU 1812 CB ILE A1028 12817 10502 17597 -1593 -2727 998 C ATOM 1813 CG1 ILE A1028 46.661 51.044 20.078 1.00111.48 C ANISOU 1813 CG1 ILE A1028 13344 11024 17989 -1610 -2825 1073 C ATOM 1814 CG2 ILE A1028 46.470 51.496 22.525 1.00103.32 C ANISOU 1814 CG2 ILE A1028 12252 9751 17255 -1447 -2799 871 C ATOM 1815 CD1 ILE A1028 47.109 49.928 19.155 1.00130.61 C ANISOU 1815 CD1 ILE A1028 15736 13693 20197 -1655 -2692 1057 C ATOM 1816 N GLY A1029 49.941 53.321 22.904 1.00128.42 N ANISOU 1816 N GLY A1029 15465 13020 20310 -1919 -2788 1137 N ATOM 1817 CA GLY A1029 50.597 53.589 24.175 1.00130.42 C ANISOU 1817 CA GLY A1029 15650 13277 20626 -1932 -2754 1024 C ATOM 1818 C GLY A1029 51.734 52.656 24.526 1.00118.83 C ANISOU 1818 C GLY A1029 14023 12136 18992 -1935 -2566 988 C ATOM 1819 O GLY A1029 51.948 52.373 25.710 1.00115.34 O ANISOU 1819 O GLY A1029 13489 11755 18578 -1828 -2500 849 O ATOM 1820 N HIS A1030 52.473 52.168 23.533 1.00103.59 N ANISOU 1820 N HIS A1030 12047 10441 16870 -2029 -2477 1110 N ATOM 1821 CA HIS A1030 53.606 51.273 23.768 1.00108.18 C ANISOU 1821 CA HIS A1030 12468 11361 17274 -1994 -2297 1084 C ATOM 1822 C HIS A1030 54.886 52.103 23.810 1.00125.24 C ANISOU 1822 C HIS A1030 14542 13689 19355 -2249 -2320 1178 C ATOM 1823 O HIS A1030 55.393 52.537 22.772 1.00115.11 O ANISOU 1823 O HIS A1030 13271 12502 17962 -2461 -2342 1348 O ATOM 1824 CB HIS A1030 53.685 50.196 22.692 1.00 98.09 C ANISOU 1824 CB HIS A1030 11178 10273 15819 -1919 -2173 1124 C ATOM 1825 CG HIS A1030 54.826 49.246 22.879 1.00119.66 C ANISOU 1825 CG HIS A1030 13756 13345 18364 -1826 -1987 1093 C ATOM 1826 ND1 HIS A1030 54.820 48.256 23.838 1.00126.93 N ANISOU 1826 ND1 HIS A1030 14622 14306 19299 -1581 -1861 963 N ATOM 1827 CD2 HIS A1030 56.015 49.144 22.240 1.00124.58 C ANISOU 1827 CD2 HIS A1030 14261 14300 18772 -1926 -1903 1186 C ATOM 1828 CE1 HIS A1030 55.953 47.580 23.776 1.00125.40 C ANISOU 1828 CE1 HIS A1030 14296 14437 18914 -1506 -1715 975 C ATOM 1829 NE2 HIS A1030 56.696 48.099 22.815 1.00130.63 N ANISOU 1829 NE2 HIS A1030 14902 15300 19431 -1710 -1736 1097 N ATOM 1830 N LEU A1031 55.411 52.315 25.014 1.00125.25 N ANISOU 1830 N LEU A1031 14440 13754 19395 -2244 -2312 1069 N ATOM 1831 CA LEU A1031 56.668 53.036 25.167 1.00122.28 C ANISOU 1831 CA LEU A1031 13943 13580 18937 -2508 -2330 1125 C ATOM 1832 C LEU A1031 57.822 52.186 24.648 1.00123.04 C ANISOU 1832 C LEU A1031 13842 14136 18770 -2501 -2160 1196 C ATOM 1833 O LEU A1031 57.969 51.021 25.028 1.00140.97 O ANISOU 1833 O LEU A1031 16014 16603 20945 -2226 -2016 1110 O ATOM 1834 CB LEU A1031 56.888 53.409 26.634 1.00122.92 C ANISOU 1834 CB LEU A1031 13946 13652 19105 -2484 -2372 951 C ATOM 1835 CG LEU A1031 58.045 54.347 26.996 1.00127.51 C ANISOU 1835 CG LEU A1031 14410 14391 19646 -2802 -2432 955 C ATOM 1836 CD1 LEU A1031 57.682 55.175 28.217 1.00123.63 C ANISOU 1836 CD1 LEU A1031 13980 13660 19336 -2821 -2565 765 C ATOM 1837 CD2 LEU A1031 59.331 53.573 27.257 1.00135.78 C ANISOU 1837 CD2 LEU A1031 15171 15970 20449 -2766 -2280 947 C ATOM 1838 N LEU A1032 58.642 52.773 23.777 1.00115.40 N ANISOU 1838 N LEU A1032 12822 13342 17682 -2795 -2172 1362 N ATOM 1839 CA LEU A1032 59.787 52.068 23.215 1.00119.93 C ANISOU 1839 CA LEU A1032 13182 14403 17983 -2795 -2011 1430 C ATOM 1840 C LEU A1032 61.035 52.218 24.080 1.00126.02 C ANISOU 1840 C LEU A1032 13691 15538 18651 -2892 -1969 1373 C ATOM 1841 O LEU A1032 61.701 51.224 24.387 1.00129.54 O ANISOU 1841 O LEU A1032 13942 16353 18925 -2657 -1822 1308 O ATOM 1842 CB LEU A1032 60.065 52.566 21.793 1.00118.44 C ANISOU 1842 CB LEU A1032 13031 14300 17671 -3064 -2025 1651 C ATOM 1843 CG LEU A1032 59.028 52.183 20.738 1.00111.22 C ANISOU 1843 CG LEU A1032 12312 13187 16760 -2937 -2039 1711 C ATOM 1844 CD1 LEU A1032 59.323 52.868 19.415 1.00122.94 C ANISOU 1844 CD1 LEU A1032 13837 14766 18110 -3232 -2074 1957 C ATOM 1845 CD2 LEU A1032 59.000 50.674 20.563 1.00108.32 C ANISOU 1845 CD2 LEU A1032 11876 13032 16247 -2589 -1868 1587 C ATOM 1846 N THR A1033 61.360 53.445 24.479 1.00124.62 N ANISOU 1846 N THR A1033 13512 15263 18576 -3230 -2101 1390 N ATOM 1847 CA THR A1033 62.558 53.698 25.265 1.00124.89 C ANISOU 1847 CA THR A1033 13277 15672 18504 -3385 -2084 1323 C ATOM 1848 C THR A1033 62.433 55.054 25.943 1.00121.13 C ANISOU 1848 C THR A1033 12905 14882 18238 -3705 -2269 1260 C ATOM 1849 O THR A1033 61.674 55.923 25.505 1.00117.48 O ANISOU 1849 O THR A1033 12709 13960 17966 -3874 -2398 1339 O ATOM 1850 CB THR A1033 63.822 53.648 24.398 1.00130.71 C ANISOU 1850 CB THR A1033 13768 16919 18976 -3607 -1977 1481 C ATOM 1851 OG1 THR A1033 64.981 53.788 25.228 1.00134.34 O ANISOU 1851 OG1 THR A1033 13919 17810 19314 -3727 -1958 1393 O ATOM 1852 CG2 THR A1033 63.804 54.759 23.359 1.00131.92 C ANISOU 1852 CG2 THR A1033 14064 16883 19177 -4043 -2067 1698 C ATOM 1853 N LYS A1034 63.187 55.218 27.028 1.00120.46 N ANISOU 1853 N LYS A1034 12609 15053 18107 -3767 -2284 1106 N ATOM 1854 CA LYS A1034 63.296 56.493 27.722 1.00116.18 C ANISOU 1854 CA LYS A1034 12129 14284 17731 -4108 -2454 1003 C ATOM 1855 C LYS A1034 64.573 57.239 27.370 1.00124.46 C ANISOU 1855 C LYS A1034 12978 15649 18660 -4603 -2465 1102 C ATOM 1856 O LYS A1034 64.805 58.331 27.897 1.00138.86 O ANISOU 1856 O LYS A1034 14847 17299 20616 -4956 -2604 1010 O ATOM 1857 CB LYS A1034 63.218 56.284 29.238 1.00111.34 C ANISOU 1857 CB LYS A1034 11418 13740 17144 -3884 -2487 731 C ATOM 1858 CG LYS A1034 61.838 55.873 29.728 1.00119.63 C ANISOU 1858 CG LYS A1034 12696 14395 18362 -3491 -2508 622 C ATOM 1859 CD LYS A1034 61.847 55.525 31.207 1.00121.31 C ANISOU 1859 CD LYS A1034 12775 14777 18539 -3244 -2509 383 C ATOM 1860 CE LYS A1034 62.029 56.761 32.068 1.00126.58 C ANISOU 1860 CE LYS A1034 13468 15301 19326 -3536 -2682 184 C ATOM 1861 NZ LYS A1034 61.909 56.439 33.517 1.00132.97 N ANISOU 1861 NZ LYS A1034 14162 16278 20083 -3270 -2690 -60 N ATOM 1862 N SER A1035 65.397 56.680 26.493 1.00132.66 N ANISOU 1862 N SER A1035 13798 17156 19452 -4647 -2320 1275 N ATOM 1863 CA SER A1035 66.623 57.335 26.068 1.00146.80 C ANISOU 1863 CA SER A1035 15361 19315 21101 -5135 -2308 1396 C ATOM 1864 C SER A1035 66.300 58.463 25.091 1.00158.20 C ANISOU 1864 C SER A1035 17087 20323 22697 -5565 -2404 1623 C ATOM 1865 O SER A1035 65.390 58.330 24.269 1.00171.23 O ANISOU 1865 O SER A1035 19004 21633 24423 -5408 -2405 1767 O ATOM 1866 CB SER A1035 67.560 56.328 25.410 1.00150.48 C ANISOU 1866 CB SER A1035 15491 20455 21231 -4994 -2108 1508 C ATOM 1867 OG SER A1035 67.943 55.317 26.326 1.00151.82 O ANISOU 1867 OG SER A1035 15403 21030 21253 -4588 -2023 1324 O ATOM 1868 N PRO A1036 67.026 59.581 25.159 1.00154.28 N ANISOU 1868 N PRO A1036 16544 19830 22247 -6116 -2489 1666 N ATOM 1869 CA PRO A1036 66.717 60.701 24.257 1.00160.65 C ANISOU 1869 CA PRO A1036 17658 20169 23212 -6533 -2583 1915 C ATOM 1870 C PRO A1036 66.995 60.394 22.797 1.00171.68 C ANISOU 1870 C PRO A1036 19005 21834 24393 -6615 -2449 2246 C ATOM 1871 O PRO A1036 66.378 61.010 21.920 1.00177.39 O ANISOU 1871 O PRO A1036 20043 22129 25229 -6762 -2512 2483 O ATOM 1872 CB PRO A1036 67.617 61.829 24.780 1.00154.76 C ANISOU 1872 CB PRO A1036 16818 19449 22533 -7124 -2680 1857 C ATOM 1873 CG PRO A1036 68.753 61.120 25.438 1.00169.50 C ANISOU 1873 CG PRO A1036 18189 22081 24133 -7077 -2572 1687 C ATOM 1874 CD PRO A1036 68.170 59.873 26.039 1.00162.15 C ANISOU 1874 CD PRO A1036 17202 21263 23142 -6399 -2506 1498 C ATOM 1875 N SER A1037 67.898 59.462 22.508 1.00173.84 N ANISOU 1875 N SER A1037 18890 22817 24343 -6499 -2267 2268 N ATOM 1876 CA SER A1037 68.211 59.108 21.130 1.00186.10 C ANISOU 1876 CA SER A1037 20363 24697 25649 -6549 -2124 2551 C ATOM 1877 C SER A1037 67.140 58.183 20.566 1.00183.77 C ANISOU 1877 C SER A1037 20272 24206 25345 -6022 -2077 2560 C ATOM 1878 O SER A1037 66.788 57.174 21.186 1.00174.23 O ANISOU 1878 O SER A1037 19009 23061 24130 -5536 -2029 2336 O ATOM 1879 CB SER A1037 69.584 58.440 21.052 1.00195.79 C ANISOU 1879 CB SER A1037 21083 26787 26523 -6582 -1944 2540 C ATOM 1880 OG SER A1037 69.888 58.052 19.724 1.00200.50 O ANISOU 1880 OG SER A1037 21586 27744 26851 -6594 -1794 2788 O ATOM 1881 N LEU A1038 66.619 58.532 19.389 1.00178.40 N ANISOU 1881 N LEU A1038 19831 23293 24659 -6134 -2093 2826 N ATOM 1882 CA LEU A1038 65.651 57.680 18.712 1.00167.24 C ANISOU 1882 CA LEU A1038 18588 21754 23203 -5690 -2052 2839 C ATOM 1883 C LEU A1038 66.299 56.479 18.038 1.00165.19 C ANISOU 1883 C LEU A1038 18032 22147 22585 -5442 -1838 2841 C ATOM 1884 O LEU A1038 65.579 55.568 17.612 1.00174.36 O ANISOU 1884 O LEU A1038 19298 23257 23696 -5034 -1787 2777 O ATOM 1885 CB LEU A1038 64.854 58.492 17.684 1.00175.92 C ANISOU 1885 CB LEU A1038 20037 22410 24396 -5877 -2159 3123 C ATOM 1886 CG LEU A1038 65.571 59.171 16.512 1.00190.31 C ANISOU 1886 CG LEU A1038 21812 24481 26016 -6342 -2107 3488 C ATOM 1887 CD1 LEU A1038 65.716 58.239 15.313 1.00191.09 C ANISOU 1887 CD1 LEU A1038 21771 25071 25763 -6135 -1940 3603 C ATOM 1888 CD2 LEU A1038 64.842 60.445 16.114 1.00197.77 C ANISOU 1888 CD2 LEU A1038 23160 24788 27195 -6629 -2289 3740 C ATOM 1889 N ASN A1039 67.628 56.462 17.916 1.00164.28 N ANISOU 1889 N ASN A1039 17551 22649 22218 -5681 -1714 2900 N ATOM 1890 CA ASN A1039 68.304 55.277 17.401 1.00165.01 C ANISOU 1890 CA ASN A1039 17338 23393 21965 -5382 -1505 2856 C ATOM 1891 C ASN A1039 68.074 54.082 18.315 1.00155.13 C ANISOU 1891 C ASN A1039 16020 22178 20746 -4821 -1453 2547 C ATOM 1892 O ASN A1039 67.956 52.944 17.846 1.00166.74 O ANISOU 1892 O ASN A1039 17453 23856 22045 -4407 -1321 2470 O ATOM 1893 CB ASN A1039 69.798 55.551 17.239 1.00174.53 C ANISOU 1893 CB ASN A1039 18122 25291 22902 -5743 -1390 2961 C ATOM 1894 CG ASN A1039 70.093 56.536 16.126 1.00186.95 C ANISOU 1894 CG ASN A1039 19738 26924 24371 -6281 -1390 3313 C ATOM 1895 OD1 ASN A1039 69.489 56.479 15.055 1.00193.53 O ANISOU 1895 OD1 ASN A1039 20782 27621 25130 -6224 -1376 3488 O ATOM 1896 ND2 ASN A1039 71.028 57.445 16.373 1.00194.90 N ANISOU 1896 ND2 ASN A1039 20543 28150 25362 -6821 -1407 3423 N ATOM 1897 N ALA A1040 68.007 54.324 19.626 1.00138.25 N ANISOU 1897 N ALA A1040 13878 19831 18819 -4803 -1553 2367 N ATOM 1898 CA ALA A1040 67.621 53.267 20.552 1.00130.48 C ANISOU 1898 CA ALA A1040 12892 18790 17895 -4278 -1519 2110 C ATOM 1899 C ALA A1040 66.161 52.877 20.357 1.00130.53 C ANISOU 1899 C ALA A1040 13277 18219 18099 -3974 -1577 2061 C ATOM 1900 O ALA A1040 65.804 51.701 20.492 1.00142.21 O ANISOU 1900 O ALA A1040 14778 19720 19537 -3515 -1483 1920 O ATOM 1901 CB ALA A1040 67.872 53.711 21.993 1.00118.22 C ANISOU 1901 CB ALA A1040 11244 17178 16498 -4358 -1622 1940 C ATOM 1902 N ALA A1041 65.306 53.849 20.031 1.00134.33 N ANISOU 1902 N ALA A1041 14062 18183 18796 -4227 -1732 2180 N ATOM 1903 CA ALA A1041 63.897 53.550 19.796 1.00134.14 C ANISOU 1903 CA ALA A1041 14365 17656 18946 -3962 -1800 2141 C ATOM 1904 C ALA A1041 63.718 52.654 18.577 1.00133.47 C ANISOU 1904 C ALA A1041 14297 17774 18643 -3750 -1677 2203 C ATOM 1905 O ALA A1041 62.899 51.728 18.595 1.00135.26 O ANISOU 1905 O ALA A1041 14651 17826 18916 -3376 -1645 2063 O ATOM 1906 CB ALA A1041 63.105 54.847 19.632 1.00130.87 C ANISOU 1906 CB ALA A1041 14249 16696 18780 -4265 -1997 2277 C ATOM 1907 N LYS A1042 64.477 52.912 17.508 1.00137.99 N ANISOU 1907 N LYS A1042 14739 18727 18966 -3999 -1603 2406 N ATOM 1908 CA LYS A1042 64.406 52.052 16.330 1.00143.00 C ANISOU 1908 CA LYS A1042 15363 19623 19346 -3794 -1477 2438 C ATOM 1909 C LYS A1042 64.897 50.644 16.645 1.00143.82 C ANISOU 1909 C LYS A1042 15270 20090 19287 -3359 -1298 2213 C ATOM 1910 O LYS A1042 64.313 49.658 16.180 1.00140.16 O ANISOU 1910 O LYS A1042 14921 19566 18766 -3023 -1232 2096 O ATOM 1911 CB LYS A1042 65.216 52.655 15.182 1.00136.43 C ANISOU 1911 CB LYS A1042 14396 19195 18246 -4161 -1420 2709 C ATOM 1912 CG LYS A1042 64.618 53.915 14.575 1.00129.00 C ANISOU 1912 CG LYS A1042 13712 17871 17429 -4541 -1582 2982 C ATOM 1913 CD LYS A1042 65.455 54.396 13.398 1.00138.77 C ANISOU 1913 CD LYS A1042 14806 19560 18360 -4895 -1497 3278 C ATOM 1914 CE LYS A1042 64.907 55.684 12.804 1.00141.81 C ANISOU 1914 CE LYS A1042 15470 19545 18867 -5277 -1657 3597 C ATOM 1915 NZ LYS A1042 63.597 55.473 12.131 1.00147.49 N ANISOU 1915 NZ LYS A1042 16491 19911 19637 -5028 -1753 3617 N ATOM 1916 N SER A1043 65.969 50.530 17.433 1.00144.35 N ANISOU 1916 N SER A1043 15043 20530 19272 -3355 -1223 2147 N ATOM 1917 CA SER A1043 66.487 49.210 17.782 1.00143.98 C ANISOU 1917 CA SER A1043 14814 20824 19068 -2902 -1057 1954 C ATOM 1918 C SER A1043 65.522 48.463 18.694 1.00141.57 C ANISOU 1918 C SER A1043 14724 20065 19003 -2520 -1090 1752 C ATOM 1919 O SER A1043 65.326 47.252 18.538 1.00154.18 O ANISOU 1919 O SER A1043 16370 21687 20525 -2112 -972 1613 O ATOM 1920 CB SER A1043 67.860 49.339 18.442 1.00143.45 C ANISOU 1920 CB SER A1043 14357 21302 18845 -2986 -987 1947 C ATOM 1921 OG SER A1043 67.764 49.976 19.703 1.00151.02 O ANISOU 1921 OG SER A1043 15322 22019 20039 -3122 -1119 1890 O ATOM 1922 N GLU A1044 64.915 49.164 19.654 1.00128.54 N ANISOU 1922 N GLU A1044 13208 17995 17637 -2650 -1245 1728 N ATOM 1923 CA GLU A1044 63.927 48.527 20.519 1.00132.91 C ANISOU 1923 CA GLU A1044 13960 18129 18412 -2323 -1275 1559 C ATOM 1924 C GLU A1044 62.718 48.059 19.721 1.00134.05 C ANISOU 1924 C GLU A1044 14391 17907 18635 -2185 -1291 1535 C ATOM 1925 O GLU A1044 62.142 47.004 20.014 1.00135.75 O ANISOU 1925 O GLU A1044 14719 17951 18909 -1836 -1223 1386 O ATOM 1926 CB GLU A1044 63.502 49.485 21.631 1.00129.89 C ANISOU 1926 CB GLU A1044 13652 17405 18294 -2510 -1442 1533 C ATOM 1927 CG GLU A1044 64.593 49.768 22.646 1.00136.26 C ANISOU 1927 CG GLU A1044 14175 18564 19033 -2588 -1434 1489 C ATOM 1928 CD GLU A1044 64.959 48.542 23.454 1.00148.03 C ANISOU 1928 CD GLU A1044 15526 20292 20425 -2136 -1301 1348 C ATOM 1929 OE1 GLU A1044 64.064 47.709 23.700 1.00160.46 O ANISOU 1929 OE1 GLU A1044 17302 21552 22112 -1807 -1267 1257 O ATOM 1930 OE2 GLU A1044 66.139 48.410 23.840 1.00156.44 O ANISOU 1930 OE2 GLU A1044 16279 21865 21296 -2111 -1232 1337 O ATOM 1931 N LEU A1045 62.318 48.832 18.709 1.00137.66 N ANISOU 1931 N LEU A1045 14970 18247 19087 -2468 -1382 1687 N ATOM 1932 CA LEU A1045 61.237 48.394 17.834 1.00140.53 C ANISOU 1932 CA LEU A1045 15566 18355 19474 -2350 -1403 1662 C ATOM 1933 C LEU A1045 61.647 47.181 17.008 1.00136.83 C ANISOU 1933 C LEU A1045 15027 18223 18740 -2088 -1224 1573 C ATOM 1934 O LEU A1045 60.818 46.304 16.742 1.00133.23 O ANISOU 1934 O LEU A1045 14741 17555 18325 -1847 -1196 1431 O ATOM 1935 CB LEU A1045 60.801 49.544 16.926 1.00139.53 C ANISOU 1935 CB LEU A1045 15569 18080 19367 -2697 -1548 1876 C ATOM 1936 CG LEU A1045 59.626 49.272 15.987 1.00131.65 C ANISOU 1936 CG LEU A1045 14795 16848 18380 -2611 -1609 1869 C ATOM 1937 CD1 LEU A1045 58.392 48.893 16.785 1.00131.93 C ANISOU 1937 CD1 LEU A1045 15007 16426 18694 -2394 -1684 1694 C ATOM 1938 CD2 LEU A1045 59.351 50.495 15.126 1.00123.66 C ANISOU 1938 CD2 LEU A1045 13890 15738 17355 -2944 -1754 2130 C ATOM 1939 N ASP A1046 62.918 47.110 16.607 1.00142.51 N ANISOU 1939 N ASP A1046 15491 19472 19183 -2132 -1100 1637 N ATOM 1940 CA ASP A1046 63.413 45.935 15.902 1.00151.33 C ANISOU 1940 CA ASP A1046 16524 20941 20034 -1833 -918 1520 C ATOM 1941 C ASP A1046 63.534 44.726 16.820 1.00154.10 C ANISOU 1941 C ASP A1046 16865 21246 20441 -1398 -802 1309 C ATOM 1942 O ASP A1046 63.644 43.598 16.329 1.00158.06 O ANISOU 1942 O ASP A1046 17396 21865 20793 -1079 -663 1163 O ATOM 1943 CB ASP A1046 64.769 46.238 15.264 1.00170.99 C ANISOU 1943 CB ASP A1046 18707 24065 22198 -1990 -811 1651 C ATOM 1944 CG ASP A1046 64.682 47.298 14.182 1.00176.56 C ANISOU 1944 CG ASP A1046 19439 24846 22798 -2406 -894 1891 C ATOM 1945 OD1 ASP A1046 63.608 47.431 13.561 1.00174.05 O ANISOU 1945 OD1 ASP A1046 19378 24190 22563 -2449 -994 1915 O ATOM 1946 OD2 ASP A1046 65.691 47.998 13.954 1.00180.80 O ANISOU 1946 OD2 ASP A1046 19735 25799 23161 -2696 -859 2068 O ATOM 1947 N LYS A1047 63.528 44.938 18.139 1.00157.18 N ANISOU 1947 N LYS A1047 17225 21466 21030 -1370 -855 1291 N ATOM 1948 CA LYS A1047 63.591 43.822 19.076 1.00156.61 C ANISOU 1948 CA LYS A1047 17164 21328 21013 -955 -751 1132 C ATOM 1949 C LYS A1047 62.214 43.210 19.304 1.00150.69 C ANISOU 1949 C LYS A1047 16733 20017 20505 -795 -788 1012 C ATOM 1950 O LYS A1047 62.070 41.982 19.301 1.00148.04 O ANISOU 1950 O LYS A1047 16504 19596 20148 -449 -663 871 O ATOM 1951 CB LYS A1047 64.197 44.283 20.402 1.00148.91 C ANISOU 1951 CB LYS A1047 15998 20473 20106 -985 -789 1166 C ATOM 1952 N ALA A1048 61.193 44.047 19.502 1.00136.21 N ANISOU 1952 N ALA A1048 15054 17798 18903 -1045 -956 1063 N ATOM 1953 CA ALA A1048 59.840 43.531 19.672 1.00128.90 C ANISOU 1953 CA ALA A1048 14392 16388 18195 -932 -996 953 C ATOM 1954 C ALA A1048 59.278 43.015 18.354 1.00129.65 C ANISOU 1954 C ALA A1048 14636 16430 18196 -918 -974 886 C ATOM 1955 O ALA A1048 58.584 41.992 18.324 1.00126.07 O ANISOU 1955 O ALA A1048 14355 15730 17815 -710 -913 731 O ATOM 1956 CB ALA A1048 58.934 44.613 20.259 1.00124.72 C ANISOU 1956 CB ALA A1048 13952 15515 17920 -1172 -1184 1016 C ATOM 1957 N ILE A1049 59.564 43.710 17.257 1.00134.73 N ANISOU 1957 N ILE A1049 15217 17307 18668 -1153 -1024 1001 N ATOM 1958 CA ILE A1049 59.162 43.296 15.918 1.00129.55 C ANISOU 1958 CA ILE A1049 14666 16701 17857 -1151 -1007 942 C ATOM 1959 C ILE A1049 60.416 42.825 15.195 1.00155.11 C ANISOU 1959 C ILE A1049 17723 20453 20760 -1036 -844 929 C ATOM 1960 O ILE A1049 61.307 43.629 14.896 1.00176.24 O ANISOU 1960 O ILE A1049 20198 23499 23269 -1242 -846 1102 O ATOM 1961 CB ILE A1049 58.473 44.432 15.150 1.00115.54 C ANISOU 1961 CB ILE A1049 12964 14832 16105 -1480 -1188 1103 C ATOM 1962 CG1 ILE A1049 57.348 45.044 15.988 1.00101.99 C ANISOU 1962 CG1 ILE A1049 11384 12651 14716 -1572 -1353 1123 C ATOM 1963 CG2 ILE A1049 57.946 43.930 13.816 1.00112.06 C ANISOU 1963 CG2 ILE A1049 12631 14456 15489 -1454 -1183 1019 C ATOM 1964 N GLY A1050 60.487 41.530 14.898 1.00148.10 N ANISOU 1964 N GLY A1050 16907 19594 19772 -714 -698 720 N ATOM 1965 CA GLY A1050 61.660 40.978 14.247 1.00141.07 C ANISOU 1965 CA GLY A1050 15844 19200 18556 -532 -530 669 C ATOM 1966 C GLY A1050 61.756 41.364 12.786 1.00148.47 C ANISOU 1966 C GLY A1050 16738 20456 19217 -721 -545 725 C ATOM 1967 O GLY A1050 61.655 40.511 11.899 1.00156.91 O ANISOU 1967 O GLY A1050 17893 21616 20109 -539 -459 539 O ATOM 1968 N ARG A1051 61.964 42.653 12.527 1.00152.51 N ANISOU 1968 N ARG A1051 17128 21138 19682 -1090 -652 983 N ATOM 1969 CA ARG A1051 61.968 43.185 11.173 1.00160.91 C ANISOU 1969 CA ARG A1051 18164 22486 20487 -1316 -686 1104 C ATOM 1970 C ARG A1051 62.695 44.521 11.180 1.00169.67 C ANISOU 1970 C ARG A1051 19073 23864 21528 -1690 -743 1420 C ATOM 1971 O ARG A1051 62.676 45.243 12.180 1.00167.54 O ANISOU 1971 O ARG A1051 18786 23369 21504 -1848 -836 1532 O ATOM 1972 CB ARG A1051 60.539 43.356 10.639 1.00159.93 C ANISOU 1972 CB ARG A1051 18302 21970 20493 -1430 -849 1080 C ATOM 1973 CG ARG A1051 60.447 43.822 9.193 1.00165.68 C ANISOU 1973 CG ARG A1051 19023 23001 20927 -1625 -893 1204 C ATOM 1974 CD ARG A1051 59.001 44.010 8.757 1.00162.72 C ANISOU 1974 CD ARG A1051 18884 22258 20684 -1715 -1075 1182 C ATOM 1975 NE ARG A1051 58.339 45.093 9.481 1.00154.59 N ANISOU 1975 NE ARG A1051 17936 20837 19966 -1936 -1261 1385 N ATOM 1976 CZ ARG A1051 58.420 46.376 9.143 1.00152.42 C ANISOU 1976 CZ ARG A1051 17635 20621 19657 -2244 -1379 1705 C ATOM 1977 NH1 ARG A1051 57.785 47.295 9.858 1.00150.09 N ANISOU 1977 NH1 ARG A1051 17441 19919 19666 -2396 -1546 1846 N ATOM 1978 NH2 ARG A1051 59.135 46.742 8.088 1.00155.95 N ANISOU 1978 NH2 ARG A1051 17964 21528 19762 -2396 -1325 1886 N ATOM 1979 N ASN A1052 63.340 44.840 10.058 1.00171.99 N ANISOU 1979 N ASN A1052 19218 24648 21481 -1842 -681 1555 N ATOM 1980 CA ASN A1052 63.938 46.158 9.890 1.00169.03 C ANISOU 1980 CA ASN A1052 18687 24505 21033 -2266 -738 1888 C ATOM 1981 C ASN A1052 62.835 47.184 9.670 1.00169.83 C ANISOU 1981 C ASN A1052 19030 24164 21333 -2562 -957 2085 C ATOM 1982 O ASN A1052 62.406 47.412 8.534 1.00175.22 O ANISOU 1982 O ASN A1052 19802 24941 21834 -2668 -1004 2193 O ATOM 1983 CB ASN A1052 64.927 46.162 8.723 1.00172.34 C ANISOU 1983 CB ASN A1052 18871 25608 21004 -2346 -591 1995 C ATOM 1984 N THR A1053 62.372 47.807 10.754 1.00164.85 N ANISOU 1984 N THR A1053 18502 23073 21062 -2671 -1094 2131 N ATOM 1985 CA THR A1053 61.194 48.664 10.677 1.00167.43 C ANISOU 1985 CA THR A1053 19081 22917 21618 -2855 -1308 2268 C ATOM 1986 C THR A1053 61.521 50.034 10.098 1.00169.47 C ANISOU 1986 C THR A1053 19324 23273 21794 -3284 -1395 2638 C ATOM 1987 O THR A1053 60.702 50.615 9.378 1.00173.06 O ANISOU 1987 O THR A1053 19966 23535 22253 -3406 -1533 2804 O ATOM 1988 CB THR A1053 60.569 48.820 12.063 1.00171.12 C ANISOU 1988 CB THR A1053 19663 22867 22486 -2786 -1415 2159 C ATOM 1989 OG1 THR A1053 61.510 49.450 12.942 1.00182.26 O ANISOU 1989 OG1 THR A1053 20905 24375 23972 -2967 -1396 2250 O ATOM 1990 CG2 THR A1053 60.187 47.461 12.631 1.00167.96 C ANISOU 1990 CG2 THR A1053 19306 22339 22173 -2384 -1324 1832 C ATOM 1991 N ASN A1054 62.707 50.562 10.405 1.00162.56 N ANISOU 1991 N ASN A1054 18226 22699 20840 -3520 -1318 2780 N ATOM 1992 CA ASN A1054 63.092 51.926 10.040 1.00161.79 C ANISOU 1992 CA ASN A1054 18125 22633 20714 -3985 -1396 3144 C ATOM 1993 C ASN A1054 62.083 52.943 10.575 1.00161.27 C ANISOU 1993 C ASN A1054 18347 21906 21023 -4137 -1627 3255 C ATOM 1994 O ASN A1054 61.821 53.973 9.947 1.00168.18 O ANISOU 1994 O ASN A1054 19370 22635 21896 -4426 -1741 3561 O ATOM 1995 CB ASN A1054 63.267 52.072 8.522 1.00166.87 C ANISOU 1995 CB ASN A1054 18744 23676 20984 -4124 -1343 3375 C ATOM 1996 CG ASN A1054 64.030 53.331 8.135 1.00178.74 C ANISOU 1996 CG ASN A1054 20170 25357 22385 -4629 -1353 3772 C ATOM 1997 OD1 ASN A1054 64.444 54.111 8.994 1.00176.12 O ANISOU 1997 OD1 ASN A1054 19808 24835 22276 -4896 -1407 3856 O ATOM 1998 ND2 ASN A1054 64.217 53.532 6.836 1.00184.67 N ANISOU 1998 ND2 ASN A1054 20894 26481 22792 -4779 -1301 4019 N ATOM 1999 N GLY A1055 61.498 52.651 11.736 1.00152.64 N ANISOU 1999 N GLY A1055 17341 20412 20244 -3920 -1693 3013 N ATOM 2000 CA GLY A1055 60.613 53.574 12.412 1.00151.44 C ANISOU 2000 CA GLY A1055 17428 19661 20451 -4019 -1898 3066 C ATOM 2001 C GLY A1055 59.135 53.404 12.136 1.00147.42 C ANISOU 2001 C GLY A1055 17173 18759 20079 -3792 -2036 3001 C ATOM 2002 O GLY A1055 58.324 54.097 12.765 1.00141.41 O ANISOU 2002 O GLY A1055 16601 17507 19622 -3808 -2204 3009 O ATOM 2003 N VAL A1056 58.749 52.510 11.227 1.00148.28 N ANISOU 2003 N VAL A1056 17283 19085 19970 -3580 -1975 2917 N ATOM 2004 CA VAL A1056 57.351 52.336 10.850 1.00157.35 C ANISOU 2004 CA VAL A1056 18638 19937 21211 -3395 -2112 2853 C ATOM 2005 C VAL A1056 56.963 50.872 11.005 1.00150.23 C ANISOU 2005 C VAL A1056 17693 19107 20279 -3042 -2006 2501 C ATOM 2006 O VAL A1056 57.774 49.972 10.759 1.00149.02 O ANISOU 2006 O VAL A1056 17380 19343 19899 -2935 -1823 2373 O ATOM 2007 CB VAL A1056 57.083 52.824 9.410 1.00165.07 C ANISOU 2007 CB VAL A1056 19702 21082 21937 -3532 -2183 3127 C ATOM 2008 CG1 VAL A1056 57.322 54.323 9.305 1.00164.54 C ANISOU 2008 CG1 VAL A1056 19740 20830 21948 -3882 -2304 3506 C ATOM 2009 CG2 VAL A1056 57.959 52.076 8.419 1.00173.30 C ANISOU 2009 CG2 VAL A1056 20558 22726 22562 -3521 -1995 3117 C ATOM 2010 N ILE A1057 55.717 50.639 11.418 1.00151.26 N ANISOU 2010 N ILE A1057 17970 18859 20642 -2863 -2121 2342 N ATOM 2011 CA ILE A1057 55.166 49.300 11.565 1.00146.09 C ANISOU 2011 CA ILE A1057 17318 18189 19999 -2570 -2040 2020 C ATOM 2012 C ILE A1057 53.892 49.208 10.738 1.00141.03 C ANISOU 2012 C ILE A1057 16812 17443 19331 -2508 -2178 1993 C ATOM 2013 O ILE A1057 53.323 50.216 10.311 1.00138.60 O ANISOU 2013 O ILE A1057 16604 17002 19057 -2637 -2353 2217 O ATOM 2014 CB ILE A1057 54.879 48.939 13.038 1.00142.95 C ANISOU 2014 CB ILE A1057 16928 17473 19913 -2414 -2022 1818 C ATOM 2015 CG1 ILE A1057 53.817 49.873 13.618 1.00124.66 C ANISOU 2015 CG1 ILE A1057 14749 14722 17894 -2463 -2225 1886 C ATOM 2016 CG2 ILE A1057 56.157 48.994 13.860 1.00159.32 C ANISOU 2016 CG2 ILE A1057 18844 19709 21983 -2458 -1896 1833 C ATOM 2017 CD1 ILE A1057 53.296 49.442 14.970 1.00110.49 C ANISOU 2017 CD1 ILE A1057 12966 12638 16377 -2287 -2212 1671 C ATOM 2018 N THR A1058 53.442 47.976 10.516 1.00147.47 N ANISOU 2018 N THR A1058 17632 18315 20083 -2305 -2102 1712 N ATOM 2019 CA THR A1058 52.226 47.748 9.755 1.00138.59 C ANISOU 2019 CA THR A1058 16601 17139 18917 -2251 -2228 1631 C ATOM 2020 C THR A1058 51.025 47.653 10.694 1.00130.61 C ANISOU 2020 C THR A1058 15666 15715 18245 -2146 -2332 1482 C ATOM 2021 O THR A1058 51.149 47.696 11.921 1.00130.38 O ANISOU 2021 O THR A1058 15626 15448 18465 -2101 -2293 1431 O ATOM 2022 CB THR A1058 52.341 46.483 8.905 1.00125.91 C ANISOU 2022 CB THR A1058 14968 15827 17045 -2126 -2100 1383 C ATOM 2023 OG1 THR A1058 52.466 45.340 9.759 1.00123.53 O ANISOU 2023 OG1 THR A1058 14662 15385 16887 -1941 -1948 1093 O ATOM 2024 CG2 THR A1058 53.554 46.562 7.992 1.00130.08 C ANISOU 2024 CG2 THR A1058 15394 16822 17211 -2205 -1981 1519 C ATOM 2025 N LYS A1059 49.839 47.519 10.100 1.00142.69 N ANISOU 2025 N LYS A1059 17251 17204 19760 -2109 -2467 1407 N ATOM 2026 CA LYS A1059 48.620 47.393 10.891 1.00140.07 C ANISOU 2026 CA LYS A1059 16955 16547 19717 -2017 -2563 1259 C ATOM 2027 C LYS A1059 48.610 46.094 11.690 1.00137.98 C ANISOU 2027 C LYS A1059 16676 16173 19577 -1889 -2392 952 C ATOM 2028 O LYS A1059 48.193 46.079 12.854 1.00113.51 O ANISOU 2028 O LYS A1059 13580 12797 16751 -1828 -2390 884 O ATOM 2029 CB LYS A1059 47.404 47.481 9.972 1.00136.30 C ANISOU 2029 CB LYS A1059 16500 16136 19150 -2012 -2743 1240 C ATOM 2030 CG LYS A1059 47.266 48.834 9.287 1.00133.40 C ANISOU 2030 CG LYS A1059 16176 15819 18693 -2101 -2933 1582 C ATOM 2031 CD LYS A1059 46.018 48.904 8.424 1.00128.10 C ANISOU 2031 CD LYS A1059 15504 15249 17919 -2055 -3125 1564 C ATOM 2032 CE LYS A1059 46.172 48.063 7.168 1.00139.89 C ANISOU 2032 CE LYS A1059 16960 17142 19051 -2079 -3072 1435 C ATOM 2033 NZ LYS A1059 47.221 48.606 6.261 1.00160.30 N ANISOU 2033 NZ LYS A1059 19558 20019 21330 -2188 -3033 1712 N ATOM 2034 N ASP A1060 49.068 44.997 11.081 1.00156.09 N ANISOU 2034 N ASP A1060 18965 18675 21665 -1837 -2245 767 N ATOM 2035 CA ASP A1060 49.164 43.729 11.798 1.00165.53 C ANISOU 2035 CA ASP A1060 20185 19735 22973 -1703 -2069 500 C ATOM 2036 C ASP A1060 50.127 43.834 12.975 1.00159.37 C ANISOU 2036 C ASP A1060 19365 18861 22326 -1637 -1942 577 C ATOM 2037 O ASP A1060 49.854 43.312 14.062 1.00151.01 O ANISOU 2037 O ASP A1060 18329 17559 21489 -1541 -1873 461 O ATOM 2038 CB ASP A1060 49.609 42.624 10.838 1.00184.84 C ANISOU 2038 CB ASP A1060 22658 22421 25153 -1640 -1938 294 C ATOM 2039 CG ASP A1060 49.497 41.234 11.442 1.00205.97 C ANISOU 2039 CG ASP A1060 25413 24889 27957 -1499 -1774 2 C ATOM 2040 OD1 ASP A1060 49.057 41.108 12.604 1.00212.46 O ANISOU 2040 OD1 ASP A1060 26257 25409 29061 -1462 -1757 -19 O ATOM 2041 OD2 ASP A1060 49.860 40.260 10.749 1.00216.71 O ANISOU 2041 OD2 ASP A1060 26825 26386 29130 -1419 -1657 -205 O ATOM 2042 N GLU A1061 51.258 44.515 12.777 1.00155.47 N ANISOU 2042 N GLU A1061 18798 18587 21685 -1702 -1912 778 N ATOM 2043 CA GLU A1061 52.262 44.610 13.829 1.00139.39 C ANISOU 2043 CA GLU A1061 16689 16539 19734 -1651 -1797 837 C ATOM 2044 C GLU A1061 51.774 45.450 15.003 1.00123.47 C ANISOU 2044 C GLU A1061 14679 14225 18010 -1695 -1908 926 C ATOM 2045 O GLU A1061 52.159 45.190 16.149 1.00103.01 O ANISOU 2045 O GLU A1061 12050 11536 15553 -1598 -1817 876 O ATOM 2046 CB GLU A1061 53.557 45.181 13.252 1.00138.46 C ANISOU 2046 CB GLU A1061 16461 16778 19371 -1757 -1746 1029 C ATOM 2047 CG GLU A1061 54.226 44.255 12.247 1.00145.99 C ANISOU 2047 CG GLU A1061 17378 18079 20014 -1660 -1597 910 C ATOM 2048 CD GLU A1061 55.444 44.873 11.596 1.00167.98 C ANISOU 2048 CD GLU A1061 20022 21277 22526 -1789 -1545 1118 C ATOM 2049 OE1 GLU A1061 55.695 46.075 11.820 1.00177.58 O ANISOU 2049 OE1 GLU A1061 21193 22478 23803 -1999 -1643 1371 O ATOM 2050 OE2 GLU A1061 56.152 44.158 10.856 1.00176.64 O ANISOU 2050 OE2 GLU A1061 21053 22716 23345 -1687 -1402 1022 O ATOM 2051 N ALA A1062 50.923 46.446 14.745 1.00115.57 N ANISOU 2051 N ALA A1062 13725 13089 17096 -1813 -2105 1051 N ATOM 2052 CA ALA A1062 50.379 47.251 15.834 1.00117.04 C ANISOU 2052 CA ALA A1062 13928 12984 17557 -1823 -2215 1101 C ATOM 2053 C ALA A1062 49.492 46.417 16.751 1.00120.79 C ANISOU 2053 C ALA A1062 14421 13241 18233 -1671 -2169 886 C ATOM 2054 O ALA A1062 49.571 46.537 17.980 1.00107.67 O ANISOU 2054 O ALA A1062 12732 11430 16746 -1610 -2136 860 O ATOM 2055 CB ALA A1062 49.604 48.442 15.272 1.00116.82 C ANISOU 2055 CB ALA A1062 13965 12852 17570 -1933 -2438 1275 C ATOM 2056 N GLU A1063 48.642 45.562 16.171 1.00120.64 N ANISOU 2056 N GLU A1063 14442 13218 18180 -1626 -2162 729 N ATOM 2057 CA GLU A1063 47.769 44.714 16.980 1.00127.32 C ANISOU 2057 CA GLU A1063 15303 13863 19210 -1527 -2105 537 C ATOM 2058 C GLU A1063 48.571 43.768 17.864 1.00120.43 C ANISOU 2058 C GLU A1063 14429 12964 18364 -1400 -1892 449 C ATOM 2059 O GLU A1063 48.195 43.516 19.016 1.00101.73 O ANISOU 2059 O GLU A1063 12055 10419 16180 -1323 -1844 395 O ATOM 2060 CB GLU A1063 46.822 43.915 16.085 1.00136.48 C ANISOU 2060 CB GLU A1063 16502 15052 20305 -1551 -2130 369 C ATOM 2061 CG GLU A1063 45.750 44.734 15.394 1.00145.08 C ANISOU 2061 CG GLU A1063 17569 16162 21391 -1631 -2354 433 C ATOM 2062 CD GLU A1063 44.845 43.876 14.536 1.00139.47 C ANISOU 2062 CD GLU A1063 16867 15531 20596 -1671 -2380 235 C ATOM 2063 OE1 GLU A1063 45.149 42.677 14.369 1.00145.94 O ANISOU 2063 OE1 GLU A1063 17738 16365 21348 -1653 -2221 48 O ATOM 2064 OE2 GLU A1063 43.828 44.395 14.033 1.00142.25 O ANISOU 2064 OE2 GLU A1063 17174 15929 20944 -1713 -2564 256 O ATOM 2065 N LYS A1064 49.669 43.219 17.338 1.00121.15 N ANISOU 2065 N LYS A1064 14520 13255 18255 -1356 -1761 440 N ATOM 2066 CA LYS A1064 50.482 42.296 18.123 1.00116.63 C ANISOU 2066 CA LYS A1064 13948 12680 17687 -1187 -1562 371 C ATOM 2067 C LYS A1064 51.063 42.980 19.354 1.00122.81 C ANISOU 2067 C LYS A1064 14642 13448 18573 -1156 -1560 493 C ATOM 2068 O LYS A1064 51.082 42.397 20.445 1.00127.63 O ANISOU 2068 O LYS A1064 15258 13941 19296 -1017 -1455 441 O ATOM 2069 CB LYS A1064 51.597 41.711 17.256 1.00124.20 C ANISOU 2069 CB LYS A1064 14897 13907 18386 -1117 -1435 342 C ATOM 2070 N LEU A1065 51.536 44.221 19.203 1.00102.23 N ANISOU 2070 N LEU A1065 11960 10957 15925 -1295 -1677 657 N ATOM 2071 CA LEU A1065 52.044 44.961 20.355 1.00113.83 C ANISOU 2071 CA LEU A1065 13347 12409 17495 -1301 -1699 741 C ATOM 2072 C LEU A1065 50.937 45.262 21.358 1.00114.48 C ANISOU 2072 C LEU A1065 13461 12216 17819 -1273 -1782 689 C ATOM 2073 O LEU A1065 51.170 45.232 22.572 1.00122.70 O ANISOU 2073 O LEU A1065 14452 13220 18947 -1181 -1730 668 O ATOM 2074 CB LEU A1065 52.725 46.253 19.902 1.00113.15 C ANISOU 2074 CB LEU A1065 13200 12464 17327 -1505 -1813 919 C ATOM 2075 CG LEU A1065 54.212 46.183 19.533 1.00115.00 C ANISOU 2075 CG LEU A1065 13314 13047 17334 -1538 -1704 998 C ATOM 2076 CD1 LEU A1065 54.455 45.400 18.257 1.00134.60 C ANISOU 2076 CD1 LEU A1065 15813 15740 19588 -1498 -1613 965 C ATOM 2077 CD2 LEU A1065 54.782 47.585 19.408 1.00121.04 C ANISOU 2077 CD2 LEU A1065 14021 13887 18082 -1793 -1825 1184 C ATOM 2078 N PHE A1066 49.725 45.555 20.877 1.00110.41 N ANISOU 2078 N PHE A1066 13010 11546 17395 -1337 -1913 665 N ATOM 2079 CA PHE A1066 48.630 45.827 21.803 1.00109.61 C ANISOU 2079 CA PHE A1066 12910 11229 17506 -1292 -1985 604 C ATOM 2080 C PHE A1066 48.247 44.587 22.600 1.00108.08 C ANISOU 2080 C PHE A1066 12726 10957 17384 -1152 -1824 474 C ATOM 2081 O PHE A1066 47.976 44.677 23.803 1.00106.35 O ANISOU 2081 O PHE A1066 12467 10651 17289 -1074 -1802 449 O ATOM 2082 CB PHE A1066 47.410 46.363 21.060 1.00112.06 C ANISOU 2082 CB PHE A1066 13259 11443 17878 -1365 -2160 606 C ATOM 2083 CG PHE A1066 46.229 46.597 21.956 1.00109.32 C ANISOU 2083 CG PHE A1066 12883 10924 17731 -1296 -2227 528 C ATOM 2084 CD1 PHE A1066 46.188 47.696 22.798 1.00102.10 C ANISOU 2084 CD1 PHE A1066 11945 9909 16939 -1274 -2329 570 C ATOM 2085 CD2 PHE A1066 45.173 45.700 21.979 1.00103.34 C ANISOU 2085 CD2 PHE A1066 12114 10118 17033 -1261 -2180 396 C ATOM 2086 CE1 PHE A1066 45.107 47.906 23.633 1.00107.74 C ANISOU 2086 CE1 PHE A1066 12616 10505 17817 -1182 -2380 481 C ATOM 2087 CE2 PHE A1066 44.088 45.903 22.812 1.00112.05 C ANISOU 2087 CE2 PHE A1066 13154 11118 18300 -1202 -2227 328 C ATOM 2088 CZ PHE A1066 44.055 47.006 23.642 1.00108.99 C ANISOU 2088 CZ PHE A1066 12734 10659 18018 -1144 -2325 369 C ATOM 2089 N ASN A1067 48.204 43.422 21.948 1.00 98.42 N ANISOU 2089 N ASN A1067 11565 9752 16078 -1122 -1709 389 N ATOM 2090 CA ASN A1067 47.853 42.198 22.661 1.00109.55 C ANISOU 2090 CA ASN A1067 13023 11037 17566 -1010 -1546 286 C ATOM 2091 C ASN A1067 48.905 41.849 23.706 1.00108.48 C ANISOU 2091 C ASN A1067 12858 10960 17399 -850 -1400 338 C ATOM 2092 O ASN A1067 48.571 41.367 24.794 1.00109.15 O ANISOU 2092 O ASN A1067 12947 10939 17586 -753 -1310 323 O ATOM 2093 CB ASN A1067 47.668 41.045 21.675 1.00121.62 C ANISOU 2093 CB ASN A1067 14658 12540 19014 -1023 -1459 164 C ATOM 2094 CG ASN A1067 46.404 41.182 20.849 1.00122.96 C ANISOU 2094 CG ASN A1067 14835 12658 19225 -1174 -1595 78 C ATOM 2095 OD1 ASN A1067 45.353 41.568 21.363 1.00110.44 O ANISOU 2095 OD1 ASN A1067 13193 10981 17789 -1220 -1682 66 O ATOM 2096 ND2 ASN A1067 46.497 40.860 19.564 1.00130.43 N ANISOU 2096 ND2 ASN A1067 15834 13705 20019 -1238 -1616 9 N ATOM 2097 N GLN A1068 50.180 42.092 23.397 1.00109.42 N ANISOU 2097 N GLN A1068 12930 11285 17360 -820 -1374 410 N ATOM 2098 CA GLN A1068 51.237 41.836 24.370 1.00110.93 C ANISOU 2098 CA GLN A1068 13055 11599 17494 -657 -1254 463 C ATOM 2099 C GLN A1068 51.119 42.766 25.571 1.00111.02 C ANISOU 2099 C GLN A1068 12969 11603 17609 -673 -1339 509 C ATOM 2100 O GLN A1068 51.360 42.354 26.712 1.00113.09 O ANISOU 2100 O GLN A1068 13198 11885 17887 -519 -1242 519 O ATOM 2101 CB GLN A1068 52.605 41.986 23.705 1.00111.43 C ANISOU 2101 CB GLN A1068 13043 11948 17349 -647 -1222 523 C ATOM 2102 CG GLN A1068 52.901 40.928 22.654 1.00125.22 C ANISOU 2102 CG GLN A1068 14878 13743 18958 -562 -1103 449 C ATOM 2103 CD GLN A1068 54.234 41.143 21.968 1.00130.37 C ANISOU 2103 CD GLN A1068 15418 14738 19378 -550 -1068 508 C ATOM 2104 OE1 GLN A1068 54.925 42.129 22.223 1.00147.73 O ANISOU 2104 OE1 GLN A1068 17470 17135 21527 -653 -1140 618 O ATOM 2105 NE2 GLN A1068 54.602 40.219 21.087 1.00125.90 N ANISOU 2105 NE2 GLN A1068 14916 14255 18663 -434 -953 423 N ATOM 2106 N ASP A1069 50.737 44.023 25.336 1.00110.34 N ANISOU 2106 N ASP A1069 12850 11488 17588 -843 -1523 536 N ATOM 2107 CA ASP A1069 50.665 44.991 26.425 1.00114.86 C ANISOU 2107 CA ASP A1069 13345 12041 18254 -858 -1616 545 C ATOM 2108 C ASP A1069 49.423 44.787 27.286 1.00112.41 C ANISOU 2108 C ASP A1069 13056 11552 18104 -784 -1614 469 C ATOM 2109 O ASP A1069 49.481 44.960 28.508 1.00111.77 O ANISOU 2109 O ASP A1069 12908 11501 18057 -694 -1592 450 O ATOM 2110 CB ASP A1069 50.702 46.413 25.867 1.00125.00 C ANISOU 2110 CB ASP A1069 14623 13306 19565 -1054 -1811 600 C ATOM 2111 CG ASP A1069 52.059 46.778 25.295 1.00121.85 C ANISOU 2111 CG ASP A1069 14162 13133 19002 -1162 -1805 696 C ATOM 2112 OD1 ASP A1069 53.071 46.222 25.768 1.00124.40 O ANISOU 2112 OD1 ASP A1069 14394 13667 19205 -1061 -1677 701 O ATOM 2113 OD2 ASP A1069 52.114 47.623 24.376 1.00134.00 O ANISOU 2113 OD2 ASP A1069 15734 14660 20519 -1345 -1926 781 O ATOM 2114 N VAL A1070 48.294 44.423 26.676 1.00113.96 N ANISOU 2114 N VAL A1070 13320 11599 18380 -828 -1637 419 N ATOM 2115 CA VAL A1070 47.083 44.235 27.469 1.00116.94 C ANISOU 2115 CA VAL A1070 13681 11853 18897 -780 -1627 350 C ATOM 2116 C VAL A1070 47.115 42.898 28.206 1.00107.53 C ANISOU 2116 C VAL A1070 12519 10645 17693 -652 -1416 346 C ATOM 2117 O VAL A1070 46.528 42.768 29.286 1.00115.04 O ANISOU 2117 O VAL A1070 13424 11570 18716 -582 -1365 330 O ATOM 2118 CB VAL A1070 45.828 44.372 26.587 1.00113.28 C ANISOU 2118 CB VAL A1070 13244 11281 18516 -886 -1739 296 C ATOM 2119 CG1 VAL A1070 45.738 43.232 25.585 1.00122.70 C ANISOU 2119 CG1 VAL A1070 14523 12451 19645 -936 -1645 261 C ATOM 2120 CG2 VAL A1070 44.575 44.447 27.448 1.00 96.25 C ANISOU 2120 CG2 VAL A1070 11017 9057 16497 -846 -1755 226 C ATOM 2121 N ASP A1071 47.798 41.890 27.654 1.00 99.99 N ANISOU 2121 N ASP A1071 11649 9704 16641 -607 -1284 366 N ATOM 2122 CA ASP A1071 47.983 40.647 28.396 1.00113.02 C ANISOU 2122 CA ASP A1071 13360 11304 18277 -455 -1079 392 C ATOM 2123 C ASP A1071 48.945 40.847 29.559 1.00113.76 C ANISOU 2123 C ASP A1071 13366 11569 18287 -289 -1025 474 C ATOM 2124 O ASP A1071 48.754 40.269 30.634 1.00107.34 O ANISOU 2124 O ASP A1071 12557 10736 17492 -163 -907 518 O ATOM 2125 CB ASP A1071 48.479 39.538 27.468 1.00120.23 C ANISOU 2125 CB ASP A1071 14410 12162 19111 -415 -959 371 C ATOM 2126 CG ASP A1071 47.401 39.042 26.524 1.00155.13 C ANISOU 2126 CG ASP A1071 18927 16403 23612 -574 -980 261 C ATOM 2127 OD1 ASP A1071 46.209 39.107 26.893 1.00165.23 O ANISOU 2127 OD1 ASP A1071 20177 17577 25023 -674 -1014 224 O ATOM 2128 OD2 ASP A1071 47.745 38.581 25.415 1.00169.22 O ANISOU 2128 OD2 ASP A1071 20799 18184 25312 -598 -962 199 O ATOM 2129 N ALA A1072 49.981 41.665 29.363 1.00114.28 N ANISOU 2129 N ALA A1072 13343 11828 18249 -300 -1112 500 N ATOM 2130 CA ALA A1072 50.858 42.022 30.472 1.00107.78 C ANISOU 2130 CA ALA A1072 12400 11215 17338 -178 -1097 549 C ATOM 2131 C ALA A1072 50.114 42.825 31.529 1.00112.38 C ANISOU 2131 C ALA A1072 12905 11780 18015 -203 -1185 504 C ATOM 2132 O ALA A1072 50.419 42.714 32.722 1.00112.52 O ANISOU 2132 O ALA A1072 12847 11932 17972 -60 -1124 529 O ATOM 2133 CB ALA A1072 52.063 42.810 29.959 1.00 95.42 C ANISOU 2133 CB ALA A1072 10736 9872 15648 -251 -1184 571 C ATOM 2134 N ALA A1073 49.135 43.633 31.114 1.00111.40 N ANISOU 2134 N ALA A1073 12792 11514 18022 -356 -1331 433 N ATOM 2135 CA ALA A1073 48.368 44.426 32.067 1.00105.46 C ANISOU 2135 CA ALA A1073 11967 10745 17359 -350 -1418 362 C ATOM 2136 C ALA A1073 47.475 43.541 32.928 1.00105.26 C ANISOU 2136 C ALA A1073 11943 10675 17375 -242 -1277 367 C ATOM 2137 O ALA A1073 47.479 43.649 34.159 1.00107.16 O ANISOU 2137 O ALA A1073 12101 11038 17575 -127 -1237 360 O ATOM 2138 CB ALA A1073 47.537 45.476 31.328 1.00105.80 C ANISOU 2138 CB ALA A1073 12029 10642 17528 -498 -1610 295 C ATOM 2139 N VAL A1074 46.700 42.656 32.296 1.00111.89 N ANISOU 2139 N VAL A1074 12872 11356 18284 -296 -1197 378 N ATOM 2140 CA VAL A1074 45.818 41.781 33.060 1.00117.07 C ANISOU 2140 CA VAL A1074 13535 11959 18989 -246 -1051 402 C ATOM 2141 C VAL A1074 46.629 40.781 33.873 1.00116.03 C ANISOU 2141 C VAL A1074 13447 11898 18742 -71 -858 526 C ATOM 2142 O VAL A1074 46.202 40.356 34.954 1.00119.48 O ANISOU 2142 O VAL A1074 13851 12377 19167 15 -745 583 O ATOM 2143 CB VAL A1074 44.809 41.086 32.122 1.00115.33 C ANISOU 2143 CB VAL A1074 13398 11548 18874 -395 -1023 366 C ATOM 2144 CG1 VAL A1074 45.520 40.159 31.151 1.00126.48 C ANISOU 2144 CG1 VAL A1074 14963 12860 20235 -407 -937 399 C ATOM 2145 CG2 VAL A1074 43.763 40.326 32.926 1.00120.75 C ANISOU 2145 CG2 VAL A1074 14065 12188 19626 -406 -883 389 C ATOM 2146 N ARG A1075 47.815 40.401 33.389 1.00112.69 N ANISOU 2146 N ARG A1075 13085 11515 18215 5 -816 582 N ATOM 2147 CA ARG A1075 48.682 39.526 34.170 1.00114.73 C ANISOU 2147 CA ARG A1075 13374 11871 18346 226 -650 711 C ATOM 2148 C ARG A1075 49.272 40.256 35.370 1.00109.47 C ANISOU 2148 C ARG A1075 12545 11489 17560 351 -697 726 C ATOM 2149 O ARG A1075 49.496 39.642 36.419 1.00115.50 O ANISOU 2149 O ARG A1075 13297 12359 18227 536 -567 838 O ATOM 2150 CB ARG A1075 49.787 38.958 33.278 1.00120.66 C ANISOU 2150 CB ARG A1075 14211 12628 19006 305 -599 745 C ATOM 2151 CG ARG A1075 50.706 37.960 33.955 1.00120.84 C ANISOU 2151 CG ARG A1075 14281 12740 18893 583 -427 886 C ATOM 2152 CD ARG A1075 51.665 37.339 32.951 1.00138.77 C ANISOU 2152 CD ARG A1075 16640 15002 21083 681 -370 890 C ATOM 2153 NE ARG A1075 52.526 38.335 32.319 1.00149.72 N ANISOU 2153 NE ARG A1075 17876 16634 22375 603 -514 824 N ATOM 2154 CZ ARG A1075 52.482 38.642 31.027 1.00146.02 C ANISOU 2154 CZ ARG A1075 17441 16105 21936 430 -595 735 C ATOM 2155 NH1 ARG A1075 51.620 38.026 30.229 1.00138.50 N ANISOU 2155 NH1 ARG A1075 16657 14869 21097 328 -558 674 N ATOM 2156 NH2 ARG A1075 53.299 39.561 30.531 1.00143.20 N ANISOU 2156 NH2 ARG A1075 16944 15985 21482 342 -712 711 N ATOM 2157 N GLY A1076 49.524 41.560 35.239 1.00116.48 N ANISOU 2157 N GLY A1076 13315 12497 18447 247 -883 617 N ATOM 2158 CA GLY A1076 49.915 42.345 36.397 1.00111.61 C ANISOU 2158 CA GLY A1076 12545 12129 17733 324 -949 577 C ATOM 2159 C GLY A1076 48.805 42.471 37.419 1.00115.49 C ANISOU 2159 C GLY A1076 12990 12618 18273 356 -926 539 C ATOM 2160 O GLY A1076 49.069 42.542 38.623 1.00106.01 O ANISOU 2160 O GLY A1076 11688 11646 16943 500 -890 553 O ATOM 2161 N ILE A1077 47.553 42.496 36.960 1.00128.83 N ANISOU 2161 N ILE A1077 14730 14096 20125 230 -947 486 N ATOM 2162 CA ILE A1077 46.420 42.537 37.878 1.00127.91 C ANISOU 2162 CA ILE A1077 14544 14012 20046 258 -905 453 C ATOM 2163 C ILE A1077 46.332 41.243 38.676 1.00124.00 C ANISOU 2163 C ILE A1077 14090 13557 19466 388 -675 629 C ATOM 2164 O ILE A1077 46.070 41.257 39.885 1.00112.82 O ANISOU 2164 O ILE A1077 12579 12332 17956 501 -610 655 O ATOM 2165 CB ILE A1077 45.120 42.812 37.100 1.00122.97 C ANISOU 2165 CB ILE A1077 13933 13187 19602 93 -982 361 C ATOM 2166 CG1 ILE A1077 45.157 44.208 36.475 1.00120.33 C ANISOU 2166 CG1 ILE A1077 13566 12811 19341 5 -1218 212 C ATOM 2167 CG2 ILE A1077 43.902 42.640 37.999 1.00103.52 C ANISOU 2167 CG2 ILE A1077 11376 10793 17165 121 -900 345 C ATOM 2168 CD1 ILE A1077 44.041 44.467 35.487 1.00115.71 C ANISOU 2168 CD1 ILE A1077 13004 12046 18913 -131 -1314 146 C ATOM 2169 N LEU A1078 46.568 40.105 38.019 1.00125.94 N ANISOU 2169 N LEU A1078 14494 13620 19737 381 -545 756 N ATOM 2170 CA LEU A1078 46.334 38.816 38.659 1.00126.74 C ANISOU 2170 CA LEU A1078 14690 13664 19801 475 -320 943 C ATOM 2171 C LEU A1078 47.394 38.492 39.706 1.00123.23 C ANISOU 2171 C LEU A1078 14214 13462 19145 737 -231 1089 C ATOM 2172 O LEU A1078 47.092 37.810 40.693 1.00124.72 O ANISOU 2172 O LEU A1078 14418 13712 19258 846 -73 1247 O ATOM 2173 CB LEU A1078 46.268 37.715 37.601 1.00130.13 C ANISOU 2173 CB LEU A1078 15330 13778 20336 391 -218 1003 C ATOM 2174 CG LEU A1078 45.102 37.841 36.613 1.00124.68 C ANISOU 2174 CG LEU A1078 14663 12877 19833 126 -289 870 C ATOM 2175 CD1 LEU A1078 45.186 36.779 35.527 1.00126.62 C ANISOU 2175 CD1 LEU A1078 15122 12830 20156 44 -203 888 C ATOM 2176 CD2 LEU A1078 43.759 37.782 37.330 1.00 98.87 C ANISOU 2176 CD2 LEU A1078 11303 9632 16632 20 -228 875 C ATOM 2177 N ARG A1079 48.631 38.961 39.523 1.00117.24 N ANISOU 2177 N ARG A1079 13399 12872 18274 837 -327 1052 N ATOM 2178 CA ARG A1079 49.669 38.680 40.507 1.00124.07 C ANISOU 2178 CA ARG A1079 14199 14029 18914 1100 -260 1181 C ATOM 2179 C ARG A1079 49.563 39.552 41.751 1.00123.70 C ANISOU 2179 C ARG A1079 13952 14313 18735 1157 -335 1104 C ATOM 2180 O ARG A1079 50.263 39.286 42.733 1.00120.56 O ANISOU 2180 O ARG A1079 13479 14204 18123 1381 -274 1217 O ATOM 2181 CB ARG A1079 51.068 38.851 39.901 1.00133.56 C ANISOU 2181 CB ARG A1079 15368 15363 20018 1182 -333 1160 C ATOM 2182 CG ARG A1079 51.459 40.287 39.570 1.00143.75 C ANISOU 2182 CG ARG A1079 16497 16810 21312 1020 -557 951 C ATOM 2183 CD ARG A1079 52.940 40.377 39.209 1.00145.39 C ANISOU 2183 CD ARG A1079 16623 17248 21371 1109 -600 965 C ATOM 2184 NE ARG A1079 53.274 39.672 37.975 1.00150.46 N ANISOU 2184 NE ARG A1079 17406 17691 22072 1102 -536 1018 N ATOM 2185 CZ ARG A1079 53.329 40.245 36.777 1.00147.86 C ANISOU 2185 CZ ARG A1079 17092 17249 21839 889 -646 908 C ATOM 2186 NH1 ARG A1079 53.093 41.544 36.650 1.00139.35 N ANISOU 2186 NH1 ARG A1079 15918 16201 20829 665 -829 762 N ATOM 2187 NH2 ARG A1079 53.639 39.525 35.708 1.00151.87 N ANISOU 2187 NH2 ARG A1079 17723 17615 22366 911 -573 947 N ATOM 2188 N ASN A1080 48.710 40.573 41.739 1.00127.83 N ANISOU 2188 N ASN A1080 14388 14816 19367 985 -467 908 N ATOM 2189 CA ASN A1080 48.594 41.500 42.856 1.00128.08 C ANISOU 2189 CA ASN A1080 14239 15147 19279 1042 -554 777 C ATOM 2190 C ASN A1080 47.497 41.037 43.808 1.00134.48 C ANISOU 2190 C ASN A1080 15023 16015 20057 1096 -410 861 C ATOM 2191 O ASN A1080 46.368 40.770 43.383 1.00134.78 O ANISOU 2191 O ASN A1080 15123 15824 20265 955 -358 864 O ATOM 2192 CB ASN A1080 48.299 42.912 42.350 1.00123.15 C ANISOU 2192 CB ASN A1080 13549 14454 18787 861 -780 509 C ATOM 2193 CG ASN A1080 48.424 43.961 43.437 1.00132.05 C ANISOU 2193 CG ASN A1080 14510 15878 19786 927 -895 323 C ATOM 2194 OD1 ASN A1080 48.704 43.650 44.594 1.00146.53 O ANISOU 2194 OD1 ASN A1080 16250 18017 21406 1107 -810 386 O ATOM 2195 ND2 ASN A1080 48.222 45.215 43.065 1.00141.96 N ANISOU 2195 ND2 ASN A1080 15738 17038 21161 789 -1093 88 N ATOM 2196 N ALA A1081 47.835 40.953 45.097 1.00141.02 N ANISOU 2196 N ALA A1081 15742 17192 20648 1293 -348 928 N ATOM 2197 CA ALA A1081 46.876 40.469 46.085 1.00133.50 C ANISOU 2197 CA ALA A1081 14751 16357 19618 1355 -189 1044 C ATOM 2198 C ALA A1081 45.756 41.471 46.330 1.00124.33 C ANISOU 2198 C ALA A1081 13454 15250 18534 1247 -287 798 C ATOM 2199 O ALA A1081 44.637 41.073 46.674 1.00132.63 O ANISOU 2199 O ALA A1081 14482 16295 19618 1202 -158 868 O ATOM 2200 CB ALA A1081 47.591 40.142 47.395 1.00130.15 C ANISOU 2200 CB ALA A1081 14235 16338 18879 1616 -103 1191 C ATOM 2201 N LYS A1082 46.031 42.767 46.167 1.00119.15 N ANISOU 2201 N LYS A1082 12710 14653 17911 1207 -508 513 N ATOM 2202 CA LYS A1082 44.992 43.773 46.355 1.00118.04 C ANISOU 2202 CA LYS A1082 12461 14533 17854 1150 -615 260 C ATOM 2203 C LYS A1082 44.049 43.850 45.162 1.00123.23 C ANISOU 2203 C LYS A1082 13199 14831 18793 956 -660 213 C ATOM 2204 O LYS A1082 42.866 44.164 45.333 1.00116.70 O ANISOU 2204 O LYS A1082 12284 14023 18036 930 -659 109 O ATOM 2205 CB LYS A1082 45.622 45.144 46.608 1.00126.53 C ANISOU 2205 CB LYS A1082 13452 15744 18879 1177 -841 -35 C ATOM 2206 CG LYS A1082 46.478 45.212 47.860 1.00135.90 C ANISOU 2206 CG LYS A1082 14516 17355 19763 1360 -826 -52 C ATOM 2207 CD LYS A1082 45.635 45.021 49.108 1.00143.63 C ANISOU 2207 CD LYS A1082 15364 18648 20559 1511 -696 -45 C ATOM 2208 CE LYS A1082 46.452 45.261 50.365 1.00148.27 C ANISOU 2208 CE LYS A1082 15812 19705 20820 1698 -715 -113 C ATOM 2209 NZ LYS A1082 47.478 44.204 50.583 1.00154.97 N ANISOU 2209 NZ LYS A1082 16693 20706 21482 1814 -593 197 N ATOM 2210 N LEU A1083 44.546 43.566 43.961 1.00123.70 N ANISOU 2210 N LEU A1083 13405 14604 18992 832 -701 283 N ATOM 2211 CA LEU A1083 43.740 43.643 42.751 1.00122.07 C ANISOU 2211 CA LEU A1083 13272 14085 19024 649 -762 237 C ATOM 2212 C LEU A1083 43.097 42.316 42.374 1.00128.81 C ANISOU 2212 C LEU A1083 14216 14775 19950 556 -567 445 C ATOM 2213 O LEU A1083 42.198 42.302 41.526 1.00122.89 O ANISOU 2213 O LEU A1083 13485 13831 19375 398 -601 394 O ATOM 2214 CB LEU A1083 44.597 44.134 41.583 1.00112.24 C ANISOU 2214 CB LEU A1083 12132 12637 17876 547 -923 181 C ATOM 2215 CG LEU A1083 45.171 45.544 41.713 1.00116.45 C ANISOU 2215 CG LEU A1083 12610 13243 18395 558 -1139 -35 C ATOM 2216 CD1 LEU A1083 46.108 45.817 40.552 1.00112.89 C ANISOU 2216 CD1 LEU A1083 12263 12617 18012 428 -1252 -20 C ATOM 2217 CD2 LEU A1083 44.065 46.586 41.783 1.00119.16 C ANISOU 2217 CD2 LEU A1083 12885 13533 18857 548 -1273 -250 C ATOM 2218 N LYS A1084 43.543 41.208 42.967 1.00124.65 N ANISOU 2218 N LYS A1084 13752 14316 19294 647 -370 676 N ATOM 2219 CA LYS A1084 42.954 39.906 42.659 1.00116.81 C ANISOU 2219 CA LYS A1084 12882 13117 18382 539 -174 877 C ATOM 2220 C LYS A1084 41.467 39.838 42.987 1.00127.05 C ANISOU 2220 C LYS A1084 14061 14468 19746 417 -100 851 C ATOM 2221 O LYS A1084 40.684 39.442 42.105 1.00134.94 O ANISOU 2221 O LYS A1084 15111 15238 20920 211 -84 840 O ATOM 2222 CB LYS A1084 43.746 38.808 43.379 1.00142.32 C ANISOU 2222 CB LYS A1084 16219 16409 21447 703 21 1148 C ATOM 2223 CG LYS A1084 43.218 37.397 43.180 1.00152.21 C ANISOU 2223 CG LYS A1084 17646 17402 22784 597 242 1378 C ATOM 2224 CD LYS A1084 43.472 36.884 41.775 1.00152.37 C ANISOU 2224 CD LYS A1084 17866 17046 22983 464 215 1358 C ATOM 2225 CE LYS A1084 43.063 35.425 41.655 1.00155.35 C ANISOU 2225 CE LYS A1084 18455 17130 23441 365 441 1575 C ATOM 2226 NZ LYS A1084 43.245 34.899 40.275 1.00159.56 N ANISOU 2226 NZ LYS A1084 19189 17298 24140 234 416 1512 N ATOM 2227 N PRO A1085 41.002 40.200 44.191 1.00126.33 N ANISOU 2227 N PRO A1085 13791 14699 19510 527 -52 827 N ATOM 2228 CA PRO A1085 39.560 40.065 44.459 1.00124.46 C ANISOU 2228 CA PRO A1085 13411 14552 19325 403 38 813 C ATOM 2229 C PRO A1085 38.700 41.018 43.648 1.00132.34 C ANISOU 2229 C PRO A1085 14297 15490 20497 298 -152 552 C ATOM 2230 O PRO A1085 37.612 40.630 43.204 1.00142.88 O ANISOU 2230 O PRO A1085 15576 16759 21954 111 -98 557 O ATOM 2231 CB PRO A1085 39.455 40.353 45.965 1.00115.85 C ANISOU 2231 CB PRO A1085 12143 13881 17992 595 119 826 C ATOM 2232 CG PRO A1085 40.823 40.126 46.500 1.00118.93 C ANISOU 2232 CG PRO A1085 12635 14353 18200 788 142 954 C ATOM 2233 CD PRO A1085 41.736 40.583 45.410 1.00117.72 C ANISOU 2233 CD PRO A1085 12608 13946 18173 765 -48 833 C ATOM 2234 N VAL A1086 39.152 42.257 43.443 1.00132.57 N ANISOU 2234 N VAL A1086 14292 15541 20537 410 -378 328 N ATOM 2235 CA VAL A1086 38.303 43.252 42.793 1.00138.92 C ANISOU 2235 CA VAL A1086 14993 16300 21489 368 -566 95 C ATOM 2236 C VAL A1086 38.103 42.915 41.319 1.00132.21 C ANISOU 2236 C VAL A1086 14267 15133 20836 160 -631 117 C ATOM 2237 O VAL A1086 36.998 43.062 40.783 1.00140.05 O ANISOU 2237 O VAL A1086 15155 16115 21944 56 -681 31 O ATOM 2238 CB VAL A1086 38.884 44.666 42.987 1.00138.05 C ANISOU 2238 CB VAL A1086 14859 16243 21350 536 -786 -136 C ATOM 2239 CG1 VAL A1086 38.908 45.028 44.463 1.00138.97 C ANISOU 2239 CG1 VAL A1086 14829 16715 21258 738 -729 -211 C ATOM 2240 CG2 VAL A1086 40.281 44.770 42.399 1.00136.24 C ANISOU 2240 CG2 VAL A1086 14815 15824 21128 516 -880 -94 C ATOM 2241 N TYR A1087 39.155 42.450 40.642 1.00115.37 N ANISOU 2241 N TYR A1087 12337 12777 18722 109 -634 223 N ATOM 2242 CA TYR A1087 39.035 42.103 39.230 1.00114.95 C ANISOU 2242 CA TYR A1087 12405 12449 18821 -78 -693 229 C ATOM 2243 C TYR A1087 38.069 40.940 39.035 1.00136.09 C ANISOU 2243 C TYR A1087 15078 15062 21567 -274 -521 333 C ATOM 2244 O TYR A1087 37.208 40.974 38.149 1.00134.33 O ANISOU 2244 O TYR A1087 14808 14763 21468 -436 -596 246 O ATOM 2245 CB TYR A1087 40.411 41.764 38.657 1.00119.16 C ANISOU 2245 CB TYR A1087 13142 12808 19326 -65 -700 320 C ATOM 2246 CG TYR A1087 40.417 41.438 37.179 1.00119.68 C ANISOU 2246 CG TYR A1087 13340 12620 19514 -237 -764 310 C ATOM 2247 CD1 TYR A1087 40.365 42.445 36.224 1.00119.12 C ANISOU 2247 CD1 TYR A1087 13258 12483 19519 -278 -986 174 C ATOM 2248 CD2 TYR A1087 40.476 40.121 36.739 1.00122.18 C ANISOU 2248 CD2 TYR A1087 13807 12758 19860 -351 -602 435 C ATOM 2249 CE1 TYR A1087 40.377 42.150 34.872 1.00126.22 C ANISOU 2249 CE1 TYR A1087 14267 13198 20492 -426 -1044 167 C ATOM 2250 CE2 TYR A1087 40.484 39.817 35.390 1.00115.49 C ANISOU 2250 CE2 TYR A1087 13077 11704 19099 -502 -662 392 C ATOM 2251 CZ TYR A1087 40.434 40.834 34.462 1.00129.72 C ANISOU 2251 CZ TYR A1087 14841 13499 20949 -538 -883 260 C ATOM 2252 OH TYR A1087 40.442 40.533 33.119 1.00146.47 O ANISOU 2252 OH TYR A1087 17068 15462 23122 -680 -943 220 O ATOM 2253 N ASP A1088 38.194 39.902 39.866 1.00133.29 N ANISOU 2253 N ASP A1088 14772 14745 21127 -272 -291 525 N ATOM 2254 CA ASP A1088 37.315 38.744 39.740 1.00121.40 C ANISOU 2254 CA ASP A1088 13288 13143 19696 -500 -109 641 C ATOM 2255 C ASP A1088 35.861 39.117 40.001 1.00126.92 C ANISOU 2255 C ASP A1088 13719 14074 20430 -602 -119 533 C ATOM 2256 O ASP A1088 34.949 38.580 39.360 1.00142.00 O ANISOU 2256 O ASP A1088 15592 15907 22456 -852 -86 514 O ATOM 2257 CB ASP A1088 37.762 37.641 40.700 1.00134.10 C ANISOU 2257 CB ASP A1088 15017 14740 21194 -453 142 902 C ATOM 2258 CG ASP A1088 39.092 37.028 40.306 1.00149.38 C ANISOU 2258 CG ASP A1088 17222 16427 23108 -358 176 1022 C ATOM 2259 OD1 ASP A1088 39.415 37.029 39.099 1.00155.39 O ANISOU 2259 OD1 ASP A1088 18106 16960 23977 -439 66 925 O ATOM 2260 OD2 ASP A1088 39.812 36.541 41.204 1.00145.30 O ANISOU 2260 OD2 ASP A1088 16784 15974 22450 -183 313 1214 O ATOM 2261 N SER A1089 35.623 40.041 40.934 1.00122.32 N ANISOU 2261 N SER A1089 12934 13802 19740 -406 -169 442 N ATOM 2262 CA SER A1089 34.258 40.386 41.313 1.00123.09 C ANISOU 2262 CA SER A1089 12746 14184 19840 -451 -158 339 C ATOM 2263 C SER A1089 33.561 41.255 40.271 1.00130.09 C ANISOU 2263 C SER A1089 13518 15050 20861 -484 -391 114 C ATOM 2264 O SER A1089 32.335 41.177 40.131 1.00127.87 O ANISOU 2264 O SER A1089 13022 14937 20627 -614 -375 52 O ATOM 2265 CB SER A1089 34.256 41.097 42.668 1.00124.87 C ANISOU 2265 CB SER A1089 12797 14763 19885 -193 -132 289 C ATOM 2266 OG SER A1089 34.904 42.355 42.586 1.00123.73 O ANISOU 2266 OG SER A1089 12673 14612 19728 36 -358 94 O ATOM 2267 N LEU A1090 34.307 42.079 39.539 1.00135.60 N ANISOU 2267 N LEU A1090 14343 15569 21610 -371 -606 5 N ATOM 2268 CA LEU A1090 33.699 43.017 38.608 1.00131.26 C ANISOU 2268 CA LEU A1090 13701 15005 21168 -353 -841 -181 C ATOM 2269 C LEU A1090 33.245 42.311 37.331 1.00133.82 C ANISOU 2269 C LEU A1090 14077 15158 21610 -624 -861 -159 C ATOM 2270 O LEU A1090 33.626 41.174 37.040 1.00132.72 O ANISOU 2270 O LEU A1090 14107 14833 21490 -816 -717 -24 O ATOM 2271 CB LEU A1090 34.671 44.146 38.266 1.00120.80 C ANISOU 2271 CB LEU A1090 12515 13531 19854 -167 -1057 -275 C ATOM 2272 CG LEU A1090 35.043 45.114 39.390 1.00118.04 C ANISOU 2272 CG LEU A1090 12105 13342 19403 98 -1102 -379 C ATOM 2273 CD1 LEU A1090 36.093 46.106 38.914 1.00111.04 C ANISOU 2273 CD1 LEU A1090 11391 12249 18550 196 -1308 -453 C ATOM 2274 CD2 LEU A1090 33.814 45.835 39.918 1.00124.16 C ANISOU 2274 CD2 LEU A1090 12616 14389 20171 245 -1152 -550 C ATOM 2275 N ASP A1091 32.415 43.012 36.562 1.00133.73 N ANISOU 2275 N ASP A1091 13922 15217 21671 -619 -1050 -307 N ATOM 2276 CA ASP A1091 31.930 42.515 35.286 1.00120.92 C ANISOU 2276 CA ASP A1091 12316 13490 20137 -858 -1114 -327 C ATOM 2277 C ASP A1091 32.884 42.920 34.162 1.00123.51 C ANISOU 2277 C ASP A1091 12881 13548 20498 -831 -1289 -333 C ATOM 2278 O ASP A1091 33.923 43.545 34.387 1.00137.41 O ANISOU 2278 O ASP A1091 14787 15198 22226 -657 -1349 -311 O ATOM 2279 CB ASP A1091 30.507 43.014 35.030 1.00127.83 C ANISOU 2279 CB ASP A1091 12882 14645 21043 -856 -1228 -468 C ATOM 2280 CG ASP A1091 30.404 44.530 35.031 1.00124.34 C ANISOU 2280 CG ASP A1091 12360 14283 20602 -531 -1462 -601 C ATOM 2281 OD1 ASP A1091 31.417 45.204 35.300 1.00127.21 O ANISOU 2281 OD1 ASP A1091 12904 14481 20947 -345 -1527 -592 O ATOM 2282 OD2 ASP A1091 29.301 45.051 34.764 1.00152.55 O ANISOU 2282 OD2 ASP A1091 15686 18082 24194 -461 -1583 -718 O ATOM 2283 N ALA A1092 32.515 42.568 32.928 1.00124.78 N ANISOU 2283 N ALA A1092 13064 13635 20711 -1021 -1372 -370 N ATOM 2284 CA ALA A1092 33.418 42.756 31.796 1.00121.70 C ANISOU 2284 CA ALA A1092 12899 13017 20324 -1035 -1503 -354 C ATOM 2285 C ALA A1092 33.693 44.230 31.528 1.00121.35 C ANISOU 2285 C ALA A1092 12859 12969 20280 -799 -1742 -403 C ATOM 2286 O ALA A1092 34.822 44.603 31.185 1.00125.08 O ANISOU 2286 O ALA A1092 13531 13265 20728 -741 -1804 -347 O ATOM 2287 CB ALA A1092 32.841 42.087 30.550 1.00110.36 C ANISOU 2287 CB ALA A1092 11458 11557 18916 -1285 -1549 -409 C ATOM 2288 N VAL A1093 32.679 45.084 31.673 1.00124.87 N ANISOU 2288 N VAL A1093 13089 13605 20751 -661 -1875 -503 N ATOM 2289 CA VAL A1093 32.852 46.495 31.343 1.00134.65 C ANISOU 2289 CA VAL A1093 14365 14786 22011 -434 -2113 -545 C ATOM 2290 C VAL A1093 33.723 47.192 32.383 1.00120.88 C ANISOU 2290 C VAL A1093 12717 12960 20251 -240 -2093 -543 C ATOM 2291 O VAL A1093 34.540 48.058 32.047 1.00121.94 O ANISOU 2291 O VAL A1093 13020 12914 20398 -152 -2234 -523 O ATOM 2292 CB VAL A1093 31.481 47.180 31.185 1.00147.49 C ANISOU 2292 CB VAL A1093 15736 16638 23667 -298 -2265 -658 C ATOM 2293 CG1 VAL A1093 30.690 47.115 32.483 1.00158.74 C ANISOU 2293 CG1 VAL A1093 16916 18321 25077 -192 -2135 -740 C ATOM 2294 CG2 VAL A1093 31.655 48.623 30.731 1.00138.80 C ANISOU 2294 CG2 VAL A1093 14723 15412 22601 -53 -2521 -679 C ATOM 2295 N ARG A1094 33.578 46.821 33.657 1.00115.32 N ANISOU 2295 N ARG A1094 11906 12404 19507 -190 -1917 -562 N ATOM 2296 CA ARG A1094 34.359 47.472 34.702 1.00115.55 C ANISOU 2296 CA ARG A1094 12000 12408 19495 -5 -1903 -591 C ATOM 2297 C ARG A1094 35.760 46.890 34.819 1.00118.50 C ANISOU 2297 C ARG A1094 12583 12631 19811 -100 -1789 -466 C ATOM 2298 O ARG A1094 36.689 47.607 35.206 1.00115.95 O ANISOU 2298 O ARG A1094 12366 12229 19460 9 -1853 -486 O ATOM 2299 CB ARG A1094 33.631 47.383 36.042 1.00111.55 C ANISOU 2299 CB ARG A1094 11275 12178 18931 119 -1769 -667 C ATOM 2300 CG ARG A1094 32.383 48.245 36.102 1.00113.97 C ANISOU 2300 CG ARG A1094 11357 12668 19276 308 -1902 -827 C ATOM 2301 CD ARG A1094 31.723 48.176 37.462 1.00119.69 C ANISOU 2301 CD ARG A1094 11849 13713 19913 443 -1755 -911 C ATOM 2302 NE ARG A1094 30.563 49.056 37.539 1.00126.53 N ANISOU 2302 NE ARG A1094 12489 14781 20806 674 -1886 -1085 N ATOM 2303 CZ ARG A1094 29.320 48.683 37.261 1.00120.44 C ANISOU 2303 CZ ARG A1094 11452 14270 20040 616 -1860 -1109 C ATOM 2304 NH1 ARG A1094 28.329 49.556 37.361 1.00110.05 N ANISOU 2304 NH1 ARG A1094 9919 13161 18734 882 -1988 -1275 N ATOM 2305 NH2 ARG A1094 29.071 47.436 36.886 1.00137.23 N ANISOU 2305 NH2 ARG A1094 13528 16452 22161 293 -1708 -977 N ATOM 2306 N ARG A1095 35.937 45.606 34.497 1.00112.81 N ANISOU 2306 N ARG A1095 11923 11870 19069 -298 -1625 -349 N ATOM 2307 CA ARG A1095 37.292 45.076 34.401 1.00109.60 C ANISOU 2307 CA ARG A1095 11721 11317 18606 -352 -1540 -231 C ATOM 2308 C ARG A1095 38.076 45.773 33.300 1.00118.03 C ANISOU 2308 C ARG A1095 12940 12210 19695 -374 -1722 -225 C ATOM 2309 O ARG A1095 39.295 45.935 33.414 1.00119.55 O ANISOU 2309 O ARG A1095 13256 12337 19831 -345 -1717 -171 O ATOM 2310 CB ARG A1095 37.271 43.565 34.162 1.00112.18 C ANISOU 2310 CB ARG A1095 12113 11587 18921 -538 -1338 -121 C ATOM 2311 CG ARG A1095 36.822 42.748 35.361 1.00118.95 C ANISOU 2311 CG ARG A1095 12877 12585 19736 -538 -1114 -58 C ATOM 2312 CD ARG A1095 36.912 41.254 35.084 1.00118.01 C ANISOU 2312 CD ARG A1095 12886 12324 19627 -729 -916 66 C ATOM 2313 NE ARG A1095 35.938 40.797 34.101 1.00141.26 N ANISOU 2313 NE ARG A1095 15788 15220 22664 -955 -947 2 N ATOM 2314 CZ ARG A1095 35.912 39.566 33.601 1.00156.41 C ANISOU 2314 CZ ARG A1095 17841 16968 24620 -1162 -812 57 C ATOM 2315 NH1 ARG A1095 36.810 38.672 33.994 1.00144.33 N ANISOU 2315 NH1 ARG A1095 16510 15279 23049 -1136 -634 197 N ATOM 2316 NH2 ARG A1095 34.991 39.228 32.709 1.00163.67 N ANISOU 2316 NH2 ARG A1095 18698 17877 25612 -1385 -862 -38 N ATOM 2317 N ALA A1096 37.395 46.202 32.235 1.00113.58 N ANISOU 2317 N ALA A1096 12354 11604 19196 -425 -1884 -268 N ATOM 2318 CA ALA A1096 38.070 46.944 31.176 1.00108.94 C ANISOU 2318 CA ALA A1096 11908 10869 18614 -448 -2061 -234 C ATOM 2319 C ALA A1096 38.551 48.303 31.669 1.00106.19 C ANISOU 2319 C ALA A1096 11597 10463 18289 -294 -2204 -279 C ATOM 2320 O ALA A1096 39.635 48.760 31.287 1.00117.19 O ANISOU 2320 O ALA A1096 13132 11739 19655 -335 -2269 -217 O ATOM 2321 CB ALA A1096 37.140 47.106 29.977 1.00 96.12 C ANISOU 2321 CB ALA A1096 10240 9250 17033 -515 -2207 -258 C ATOM 2322 N ALA A1097 37.759 48.966 32.514 1.00 99.93 N ANISOU 2322 N ALA A1097 10675 9754 17540 -125 -2253 -398 N ATOM 2323 CA ALA A1097 38.190 50.243 33.072 1.00109.87 C ANISOU 2323 CA ALA A1097 11990 10927 18829 24 -2386 -480 C ATOM 2324 C ALA A1097 39.357 50.053 34.029 1.00117.48 C ANISOU 2324 C ALA A1097 13003 11929 19706 19 -2268 -473 C ATOM 2325 O ALA A1097 40.260 50.896 34.094 1.00110.03 O ANISOU 2325 O ALA A1097 12171 10870 18765 20 -2370 -492 O ATOM 2326 CB ALA A1097 37.022 50.935 33.773 1.00100.97 C ANISOU 2326 CB ALA A1097 10707 9901 17756 241 -2456 -642 C ATOM 2327 N LEU A1098 39.355 48.950 34.780 1.00116.15 N ANISOU 2327 N LEU A1098 12748 11929 19453 8 -2054 -437 N ATOM 2328 CA LEU A1098 40.492 48.638 35.638 1.00103.84 C ANISOU 2328 CA LEU A1098 11224 10448 17781 22 -1937 -400 C ATOM 2329 C LEU A1098 41.728 48.320 34.808 1.00106.16 C ANISOU 2329 C LEU A1098 11665 10637 18035 -119 -1932 -269 C ATOM 2330 O LEU A1098 42.835 48.760 35.139 1.00110.14 O ANISOU 2330 O LEU A1098 12216 11155 18476 -116 -1962 -273 O ATOM 2331 CB LEU A1098 40.142 47.472 36.563 1.00106.32 C ANISOU 2331 CB LEU A1098 11431 10957 18009 54 -1704 -347 C ATOM 2332 CG LEU A1098 41.172 47.097 37.628 1.00112.99 C ANISOU 2332 CG LEU A1098 12280 11945 18706 126 -1574 -297 C ATOM 2333 CD1 LEU A1098 41.371 48.253 38.595 1.00100.56 C ANISOU 2333 CD1 LEU A1098 10644 10474 17089 273 -1684 -471 C ATOM 2334 CD2 LEU A1098 40.739 45.841 38.369 1.00118.92 C ANISOU 2334 CD2 LEU A1098 12958 12847 19377 142 -1336 -185 C ATOM 2335 N ILE A1099 41.556 47.562 33.721 1.00103.97 N ANISOU 2335 N ILE A1099 11444 10280 17778 -246 -1894 -171 N ATOM 2336 CA ILE A1099 42.663 47.301 32.804 1.00100.65 C ANISOU 2336 CA ILE A1099 11151 9784 17306 -364 -1894 -63 C ATOM 2337 C ILE A1099 43.182 48.605 32.211 1.00102.26 C ANISOU 2337 C ILE A1099 11431 9878 17547 -411 -2100 -77 C ATOM 2338 O ILE A1099 44.388 48.765 31.989 1.00110.60 O ANISOU 2338 O ILE A1099 12550 10942 18531 -481 -2106 -14 O ATOM 2339 CB ILE A1099 42.226 46.307 31.709 1.00 97.10 C ANISOU 2339 CB ILE A1099 10750 9275 16869 -483 -1830 1 C ATOM 2340 CG1 ILE A1099 41.966 44.926 32.314 1.00104.53 C ANISOU 2340 CG1 ILE A1099 11667 10273 17778 -474 -1603 41 C ATOM 2341 CG2 ILE A1099 43.270 46.215 30.604 1.00 91.55 C ANISOU 2341 CG2 ILE A1099 10169 8516 16101 -588 -1858 88 C ATOM 2342 CD1 ILE A1099 41.262 43.970 31.372 1.00 99.26 C ANISOU 2342 CD1 ILE A1099 11038 9527 17150 -612 -1547 50 C ATOM 2343 N ASN A1100 42.284 49.560 31.955 1.00105.04 N ANISOU 2343 N ASN A1100 11774 10129 18006 -370 -2270 -151 N ATOM 2344 CA ASN A1100 42.707 50.858 31.435 1.00108.29 C ANISOU 2344 CA ASN A1100 12292 10381 18472 -413 -2470 -145 C ATOM 2345 C ASN A1100 43.648 51.559 32.410 1.00111.18 C ANISOU 2345 C ASN A1100 12672 10758 18812 -393 -2491 -218 C ATOM 2346 O ASN A1100 44.724 52.028 32.022 1.00107.44 O ANISOU 2346 O ASN A1100 12284 10231 18307 -528 -2548 -153 O ATOM 2347 CB ASN A1100 41.481 51.726 31.138 1.00116.80 C ANISOU 2347 CB ASN A1100 13362 11342 19673 -308 -2643 -214 C ATOM 2348 CG ASN A1100 41.831 53.012 30.399 1.00114.28 C ANISOU 2348 CG ASN A1100 13201 10798 19423 -358 -2853 -161 C ATOM 2349 OD1 ASN A1100 42.998 53.306 30.148 1.00130.59 O ANISOU 2349 OD1 ASN A1100 15367 12805 21445 -506 -2867 -79 O ATOM 2350 ND2 ASN A1100 40.812 53.778 30.038 1.00121.85 N ANISOU 2350 ND2 ASN A1100 14177 11638 20484 -234 -3016 -193 N ATOM 2351 N MET A1101 43.255 51.639 33.684 1.00109.25 N ANISOU 2351 N MET A1101 12329 10615 18566 -238 -2446 -362 N ATOM 2352 CA MET A1101 44.101 52.296 34.676 1.00109.39 C ANISOU 2352 CA MET A1101 12344 10678 18540 -218 -2475 -470 C ATOM 2353 C MET A1101 45.444 51.592 34.810 1.00114.02 C ANISOU 2353 C MET A1101 12911 11432 18977 -320 -2349 -369 C ATOM 2354 O MET A1101 46.492 52.245 34.878 1.00118.31 O ANISOU 2354 O MET A1101 13493 11971 19488 -430 -2422 -387 O ATOM 2355 CB MET A1101 43.394 52.340 36.029 1.00110.99 C ANISOU 2355 CB MET A1101 12422 11028 18723 -14 -2424 -645 C ATOM 2356 CG MET A1101 42.141 53.184 36.069 1.00112.53 C ANISOU 2356 CG MET A1101 12609 11098 19048 138 -2557 -787 C ATOM 2357 SD MET A1101 41.401 53.144 37.711 1.00109.31 S ANISOU 2357 SD MET A1101 12020 10946 18566 385 -2464 -999 S ATOM 2358 CE MET A1101 42.561 54.159 38.622 1.00 99.20 C ANISOU 2358 CE MET A1101 10808 9650 17234 378 -2561 -1182 C ATOM 2359 N VAL A1102 45.431 50.257 34.855 1.00113.48 N ANISOU 2359 N VAL A1102 12783 11516 18819 -285 -2158 -265 N ATOM 2360 CA VAL A1102 46.678 49.499 34.927 1.00115.94 C ANISOU 2360 CA VAL A1102 13077 11992 18982 -327 -2032 -157 C ATOM 2361 C VAL A1102 47.512 49.738 33.677 1.00109.10 C ANISOU 2361 C VAL A1102 12299 11044 18111 -510 -2102 -49 C ATOM 2362 O VAL A1102 48.738 49.894 33.748 1.00107.47 O ANISOU 2362 O VAL A1102 12066 10964 17802 -586 -2099 -17 O ATOM 2363 CB VAL A1102 46.381 48.002 35.132 1.00115.71 C ANISOU 2363 CB VAL A1102 13013 12068 18883 -235 -1816 -56 C ATOM 2364 CG1 VAL A1102 47.670 47.193 35.120 1.00109.46 C ANISOU 2364 CG1 VAL A1102 12219 11431 17940 -227 -1690 65 C ATOM 2365 CG2 VAL A1102 45.620 47.787 36.428 1.00113.95 C ANISOU 2365 CG2 VAL A1102 12688 11969 18637 -75 -1733 -133 C ATOM 2366 N PHE A1103 46.857 49.776 32.514 1.00101.53 N ANISOU 2366 N PHE A1103 11425 9912 17240 -585 -2165 11 N ATOM 2367 CA PHE A1103 47.555 50.064 31.265 1.00 99.17 C ANISOU 2367 CA PHE A1103 11209 9555 16918 -760 -2234 125 C ATOM 2368 C PHE A1103 48.234 51.426 31.331 1.00123.88 C ANISOU 2368 C PHE A1103 14378 12609 20081 -889 -2396 96 C ATOM 2369 O PHE A1103 49.354 51.600 30.836 1.00127.89 O ANISOU 2369 O PHE A1103 14892 13197 20504 -1047 -2400 186 O ATOM 2370 CB PHE A1103 46.558 50.025 30.106 1.00107.22 C ANISOU 2370 CB PHE A1103 12304 10419 18018 -798 -2303 174 C ATOM 2371 CG PHE A1103 47.192 49.932 28.750 1.00104.36 C ANISOU 2371 CG PHE A1103 12012 10061 17578 -953 -2321 311 C ATOM 2372 CD1 PHE A1103 47.538 48.697 28.224 1.00 99.85 C ANISOU 2372 CD1 PHE A1103 11434 9612 16894 -952 -2165 368 C ATOM 2373 CD2 PHE A1103 47.456 51.070 28.007 1.00 99.37 C ANISOU 2373 CD2 PHE A1103 11466 9312 16979 -1095 -2488 386 C ATOM 2374 CE1 PHE A1103 48.117 48.597 26.975 1.00102.87 C ANISOU 2374 CE1 PHE A1103 11868 10040 17177 -1077 -2174 474 C ATOM 2375 CE2 PHE A1103 48.043 50.977 26.758 1.00101.47 C ANISOU 2375 CE2 PHE A1103 11784 9629 17142 -1242 -2492 528 C ATOM 2376 CZ PHE A1103 48.374 49.741 26.242 1.00111.01 C ANISOU 2376 CZ PHE A1103 12959 11003 18218 -1226 -2335 561 C ATOM 2377 N GLN A1104 47.570 52.400 31.955 1.00118.70 N ANISOU 2377 N GLN A1104 13750 11803 19549 -828 -2526 -37 N ATOM 2378 CA GLN A1104 48.081 53.763 32.032 1.00119.15 C ANISOU 2378 CA GLN A1104 13888 11707 19675 -960 -2694 -88 C ATOM 2379 C GLN A1104 49.207 53.886 33.053 1.00125.05 C ANISOU 2379 C GLN A1104 14540 12655 20319 -1011 -2654 -182 C ATOM 2380 O GLN A1104 50.311 54.336 32.726 1.00118.04 O ANISOU 2380 O GLN A1104 13662 11808 19381 -1225 -2695 -123 O ATOM 2381 CB GLN A1104 46.941 54.723 32.382 1.00113.43 C ANISOU 2381 CB GLN A1104 13241 10737 19122 -831 -2845 -229 C ATOM 2382 CG GLN A1104 47.349 56.182 32.465 1.00112.34 C ANISOU 2382 CG GLN A1104 13241 10352 19091 -956 -3030 -300 C ATOM 2383 CD GLN A1104 46.182 57.094 32.801 1.00116.77 C ANISOU 2383 CD GLN A1104 13894 10651 19822 -767 -3176 -453 C ATOM 2384 OE1 GLN A1104 45.056 56.635 32.997 1.00129.47 O ANISOU 2384 OE1 GLN A1104 15424 12316 21452 -543 -3136 -508 O ATOM 2385 NE2 GLN A1104 46.448 58.392 32.877 1.00107.66 N ANISOU 2385 NE2 GLN A1104 12905 9212 18790 -856 -3345 -529 N ATOM 2386 N MET A1105 48.939 53.502 34.301 1.00122.60 N ANISOU 2386 N MET A1105 14119 12505 19959 -824 -2575 -325 N ATOM 2387 CA MET A1105 49.870 53.725 35.402 1.00111.63 C ANISOU 2387 CA MET A1105 12625 11332 18458 -841 -2564 -450 C ATOM 2388 C MET A1105 50.737 52.509 35.703 1.00113.10 C ANISOU 2388 C MET A1105 12662 11873 18439 -783 -2379 -347 C ATOM 2389 O MET A1105 51.963 52.622 35.763 1.00119.13 O ANISOU 2389 O MET A1105 13347 12834 19085 -915 -2379 -326 O ATOM 2390 CB MET A1105 49.102 54.133 36.668 1.00 95.41 C ANISOU 2390 CB MET A1105 10533 9280 16438 -648 -2600 -681 C ATOM 2391 CG MET A1105 48.339 55.435 36.534 1.00120.62 C ANISOU 2391 CG MET A1105 13876 12125 19829 -656 -2794 -824 C ATOM 2392 SD MET A1105 47.624 56.009 38.088 1.00154.02 S ANISOU 2392 SD MET A1105 18048 16408 24065 -418 -2838 -1148 S ATOM 2393 CE MET A1105 46.290 54.850 38.333 1.00122.61 C ANISOU 2393 CE MET A1105 13950 12584 20051 -143 -2668 -1087 C ATOM 2394 N GLY A1106 50.120 51.352 35.903 1.00101.31 N ANISOU 2394 N GLY A1106 11127 10466 16899 -588 -2221 -280 N ATOM 2395 CA GLY A1106 50.814 50.152 36.315 1.00 95.60 C ANISOU 2395 CA GLY A1106 10294 10037 15992 -472 -2039 -178 C ATOM 2396 C GLY A1106 50.096 49.464 37.461 1.00 99.66 C ANISOU 2396 C GLY A1106 10741 10672 16452 -236 -1917 -220 C ATOM 2397 O GLY A1106 49.200 50.017 38.096 1.00121.92 O ANISOU 2397 O GLY A1106 13558 13420 19347 -167 -1979 -364 O ATOM 2398 N GLU A1107 50.513 48.227 37.704 1.00109.32 N ANISOU 2398 N GLU A1107 11915 12087 17535 -103 -1736 -80 N ATOM 2399 CA GLU A1107 49.876 47.426 38.747 1.00120.41 C ANISOU 2399 CA GLU A1107 13270 13609 18870 107 -1591 -58 C ATOM 2400 C GLU A1107 50.023 48.082 40.116 1.00119.46 C ANISOU 2400 C GLU A1107 13025 13724 18639 199 -1646 -220 C ATOM 2401 O GLU A1107 49.045 48.217 40.859 1.00 99.63 O ANISOU 2401 O GLU A1107 10487 11216 16153 301 -1632 -312 O ATOM 2402 CB GLU A1107 50.454 46.003 38.751 1.00120.83 C ANISOU 2402 CB GLU A1107 13325 13795 18788 244 -1391 145 C ATOM 2403 CG GLU A1107 51.962 45.904 39.011 1.00144.58 C ANISOU 2403 CG GLU A1107 16227 17107 21599 294 -1380 192 C ATOM 2404 CD GLU A1107 52.468 44.473 38.995 1.00155.35 C ANISOU 2404 CD GLU A1107 17616 18571 22839 488 -1181 397 C ATOM 2405 OE1 GLU A1107 51.644 43.560 38.782 1.00161.50 O ANISOU 2405 OE1 GLU A1107 18521 19143 23700 550 -1050 498 O ATOM 2406 OE2 GLU A1107 53.683 44.258 39.195 1.00161.21 O ANISOU 2406 OE2 GLU A1107 18255 19596 23402 581 -1157 453 O ATOM 2407 N THR A1108 51.237 48.514 40.463 1.00127.21 N ANISOU 2407 N THR A1108 13912 14937 19484 158 -1713 -273 N ATOM 2408 CA THR A1108 51.462 49.090 41.783 1.00129.79 C ANISOU 2408 CA THR A1108 14110 15532 19673 240 -1769 -451 C ATOM 2409 C THR A1108 50.860 50.484 41.918 1.00117.67 C ANISOU 2409 C THR A1108 12621 13801 18287 130 -1960 -713 C ATOM 2410 O THR A1108 50.614 50.932 43.043 1.00122.39 O ANISOU 2410 O THR A1108 13138 14565 18799 236 -1996 -902 O ATOM 2411 CB THR A1108 52.961 49.126 42.095 1.00131.96 C ANISOU 2411 CB THR A1108 14244 16151 19744 211 -1794 -447 C ATOM 2412 OG1 THR A1108 53.157 49.564 43.446 1.00128.28 O ANISOU 2412 OG1 THR A1108 13638 15996 19108 308 -1842 -628 O ATOM 2413 CG2 THR A1108 53.690 50.068 41.147 1.00149.15 C ANISOU 2413 CG2 THR A1108 16453 18195 22022 -81 -1953 -511 C ATOM 2414 N GLY A1109 50.612 51.175 40.806 1.00112.14 N ANISOU 2414 N GLY A1109 12057 12754 17796 -60 -2082 -728 N ATOM 2415 CA GLY A1109 49.987 52.485 40.891 1.00118.71 C ANISOU 2415 CA GLY A1109 12971 13344 18790 -128 -2263 -959 C ATOM 2416 C GLY A1109 48.520 52.405 41.274 1.00126.96 C ANISOU 2416 C GLY A1109 14032 14289 19918 64 -2226 -1030 C ATOM 2417 O GLY A1109 48.048 53.151 42.137 1.00140.75 O ANISOU 2417 O GLY A1109 15752 16062 21666 163 -2304 -1268 O ATOM 2418 N VAL A1110 47.778 51.495 40.638 1.00113.93 N ANISOU 2418 N VAL A1110 12414 12545 18329 115 -2105 -842 N ATOM 2419 CA VAL A1110 46.348 51.375 40.910 1.00117.49 C ANISOU 2419 CA VAL A1110 12847 12938 18856 266 -2063 -895 C ATOM 2420 C VAL A1110 46.062 50.689 42.239 1.00111.56 C ANISOU 2420 C VAL A1110 11947 12521 17918 466 -1903 -912 C ATOM 2421 O VAL A1110 44.957 50.836 42.776 1.00113.67 O ANISOU 2421 O VAL A1110 12154 12827 18209 600 -1882 -1019 O ATOM 2422 CB VAL A1110 45.635 50.611 39.782 1.00123.44 C ANISOU 2422 CB VAL A1110 13667 13506 19730 214 -1991 -703 C ATOM 2423 CG1 VAL A1110 45.775 51.347 38.467 1.00122.76 C ANISOU 2423 CG1 VAL A1110 13723 13114 19806 39 -2156 -680 C ATOM 2424 CG2 VAL A1110 46.200 49.218 39.661 1.00139.25 C ANISOU 2424 CG2 VAL A1110 15651 15647 21609 210 -1796 -476 C ATOM 2425 N ALA A1111 47.019 49.935 42.785 1.00114.81 N ANISOU 2425 N ALA A1111 12288 13204 18130 503 -1785 -794 N ATOM 2426 CA ALA A1111 46.784 49.227 44.038 1.00108.32 C ANISOU 2426 CA ALA A1111 11336 12715 17105 700 -1624 -759 C ATOM 2427 C ALA A1111 46.727 50.161 45.239 1.00123.64 C ANISOU 2427 C ALA A1111 13171 14878 18928 812 -1716 -1041 C ATOM 2428 O ALA A1111 46.224 49.760 46.294 1.00121.49 O ANISOU 2428 O ALA A1111 12783 14884 18493 988 -1595 -1049 O ATOM 2429 CB ALA A1111 47.869 48.176 44.259 1.00103.71 C ANISOU 2429 CB ALA A1111 10718 12358 16328 746 -1484 -536 C ATOM 2430 N GLY A1112 47.228 51.391 45.107 1.00131.82 N ANISOU 2430 N GLY A1112 14253 15797 20035 704 -1924 -1274 N ATOM 2431 CA GLY A1112 47.244 52.313 46.228 1.00132.54 C ANISOU 2431 CA GLY A1112 14266 16078 20016 798 -2026 -1588 C ATOM 2432 C GLY A1112 45.881 52.846 46.620 1.00139.56 C ANISOU 2432 C GLY A1112 15143 16896 20988 954 -2049 -1787 C ATOM 2433 O GLY A1112 45.718 53.322 47.748 1.00153.35 O ANISOU 2433 O GLY A1112 16792 18891 22585 1104 -2073 -2034 O ATOM 2434 N PHE A1113 44.898 52.773 45.720 1.00136.04 N ANISOU 2434 N PHE A1113 14775 16155 20757 937 -2045 -1697 N ATOM 2435 CA PHE A1113 43.563 53.316 45.979 1.00130.06 C ANISOU 2435 CA PHE A1113 13986 15344 20089 1103 -2078 -1885 C ATOM 2436 C PHE A1113 42.769 52.310 46.814 1.00130.92 C ANISOU 2436 C PHE A1113 13913 15811 20019 1272 -1852 -1774 C ATOM 2437 O PHE A1113 41.799 51.696 46.365 1.00134.95 O ANISOU 2437 O PHE A1113 14390 16270 20617 1280 -1747 -1621 O ATOM 2438 CB PHE A1113 42.849 53.637 44.673 1.00117.73 C ANISOU 2438 CB PHE A1113 12553 13376 18803 1023 -2174 -1823 C ATOM 2439 CG PHE A1113 43.589 54.605 43.798 1.00118.92 C ANISOU 2439 CG PHE A1113 12897 13161 19125 841 -2383 -1880 C ATOM 2440 CD1 PHE A1113 43.645 55.950 44.118 1.00126.89 C ANISOU 2440 CD1 PHE A1113 13998 14001 20213 880 -2575 -2186 C ATOM 2441 CD2 PHE A1113 44.206 54.170 42.635 1.00109.14 C ANISOU 2441 CD2 PHE A1113 11760 11739 17968 625 -2381 -1628 C ATOM 2442 CE1 PHE A1113 44.327 56.838 43.309 1.00125.18 C ANISOU 2442 CE1 PHE A1113 13979 13423 20162 677 -2758 -2209 C ATOM 2443 CE2 PHE A1113 44.884 55.057 41.818 1.00108.68 C ANISOU 2443 CE2 PHE A1113 11871 11372 18051 434 -2559 -1650 C ATOM 2444 CZ PHE A1113 44.944 56.393 42.156 1.00116.78 C ANISOU 2444 CZ PHE A1113 12995 12212 19163 446 -2746 -1926 C ATOM 2445 N THR A1114 43.200 52.156 48.069 1.00127.33 N ANISOU 2445 N THR A1114 13333 15750 19297 1394 -1778 -1852 N ATOM 2446 CA THR A1114 42.658 51.096 48.914 1.00131.36 C ANISOU 2446 CA THR A1114 13681 16633 19596 1528 -1540 -1681 C ATOM 2447 C THR A1114 41.174 51.307 49.192 1.00139.09 C ANISOU 2447 C THR A1114 14546 17686 20616 1675 -1493 -1804 C ATOM 2448 O THR A1114 40.377 50.368 49.099 1.00137.48 O ANISOU 2448 O THR A1114 14263 17564 20408 1665 -1310 -1577 O ATOM 2449 CB THR A1114 43.449 51.006 50.219 1.00134.21 C ANISOU 2449 CB THR A1114 13926 17436 19631 1649 -1493 -1749 C ATOM 2450 OG1 THR A1114 43.330 52.237 50.941 1.00151.34 O ANISOU 2450 OG1 THR A1114 16051 19707 21744 1769 -1649 -2162 O ATOM 2451 CG2 THR A1114 44.917 50.732 49.927 1.00133.46 C ANISOU 2451 CG2 THR A1114 13903 17327 19480 1517 -1534 -1613 C ATOM 2452 N ASN A1115 40.781 52.538 49.536 1.00141.04 N ANISOU 2452 N ASN A1115 14780 17908 20903 1811 -1654 -2171 N ATOM 2453 CA ASN A1115 39.366 52.808 49.776 1.00143.33 C ANISOU 2453 CA ASN A1115 14936 18297 21224 1991 -1619 -2312 C ATOM 2454 C ASN A1115 38.540 52.611 48.511 1.00141.85 C ANISOU 2454 C ASN A1115 14801 17785 21308 1888 -1637 -2159 C ATOM 2455 O ASN A1115 37.449 52.031 48.559 1.00142.34 O ANISOU 2455 O ASN A1115 14705 18020 21357 1934 -1493 -2057 O ATOM 2456 CB ASN A1115 39.173 54.221 50.329 1.00136.43 C ANISOU 2456 CB ASN A1115 14071 17411 20354 2190 -1806 -2763 C ATOM 2457 CG ASN A1115 39.555 54.332 51.792 1.00156.67 C ANISOU 2457 CG ASN A1115 16500 20439 22588 2351 -1748 -2962 C ATOM 2458 OD1 ASN A1115 39.281 53.432 52.586 1.00160.40 O ANISOU 2458 OD1 ASN A1115 16787 21348 22809 2425 -1531 -2796 O ATOM 2459 ND2 ASN A1115 40.170 55.449 52.161 1.00173.70 N ANISOU 2459 ND2 ASN A1115 18753 22509 24737 2398 -1944 -3322 N ATOM 2460 N SER A1116 39.042 53.082 47.367 1.00125.66 N ANISOU 2460 N SER A1116 12957 15296 19490 1733 -1812 -2137 N ATOM 2461 CA SER A1116 38.301 52.920 46.119 1.00117.62 C ANISOU 2461 CA SER A1116 11989 13996 18705 1639 -1847 -1996 C ATOM 2462 C SER A1116 38.176 51.450 45.732 1.00123.78 C ANISOU 2462 C SER A1116 12717 14859 19453 1468 -1635 -1641 C ATOM 2463 O SER A1116 37.101 51.003 45.315 1.00120.12 O ANISOU 2463 O SER A1116 12152 14423 19066 1451 -1563 -1555 O ATOM 2464 CB SER A1116 38.974 53.715 45.001 1.00116.23 C ANISOU 2464 CB SER A1116 12053 13360 18747 1501 -2070 -2018 C ATOM 2465 OG SER A1116 38.927 55.106 45.267 1.00126.50 O ANISOU 2465 OG SER A1116 13436 14505 20122 1651 -2272 -2344 O ATOM 2466 N LEU A1117 39.264 50.684 45.858 1.00125.59 N ANISOU 2466 N LEU A1117 13017 15130 19571 1343 -1537 -1443 N ATOM 2467 CA LEU A1117 39.196 49.252 45.583 1.00130.24 C ANISOU 2467 CA LEU A1117 13593 15765 20127 1204 -1326 -1116 C ATOM 2468 C LEU A1117 38.256 48.551 46.556 1.00138.41 C ANISOU 2468 C LEU A1117 14423 17166 21002 1297 -1110 -1051 C ATOM 2469 O LEU A1117 37.439 47.716 46.152 1.00129.16 O ANISOU 2469 O LEU A1117 13195 15983 19895 1184 -977 -878 O ATOM 2470 CB LEU A1117 40.594 48.637 45.651 1.00128.34 C ANISOU 2470 CB LEU A1117 13465 15523 19776 1122 -1268 -936 C ATOM 2471 CG LEU A1117 41.590 49.071 44.575 1.00128.24 C ANISOU 2471 CG LEU A1117 13637 15185 19903 976 -1435 -929 C ATOM 2472 CD1 LEU A1117 42.976 48.520 44.874 1.00141.36 C ANISOU 2472 CD1 LEU A1117 15346 16962 21404 949 -1371 -786 C ATOM 2473 CD2 LEU A1117 41.119 48.625 43.201 1.00118.71 C ANISOU 2473 CD2 LEU A1117 12526 13681 18900 811 -1441 -781 C ATOM 2474 N ARG A1118 38.359 48.885 47.845 1.00147.92 N ANISOU 2474 N ARG A1118 15504 18715 21983 1485 -1070 -1193 N ATOM 2475 CA ARG A1118 37.474 48.320 48.858 1.00151.11 C ANISOU 2475 CA ARG A1118 15693 19525 22197 1585 -860 -1135 C ATOM 2476 C ARG A1118 36.009 48.633 48.582 1.00152.99 C ANISOU 2476 C ARG A1118 15768 19807 22552 1624 -869 -1258 C ATOM 2477 O ARG A1118 35.131 47.896 49.044 1.00157.31 O ANISOU 2477 O ARG A1118 16135 20636 23001 1604 -666 -1125 O ATOM 2478 CB ARG A1118 37.908 48.834 50.237 1.00160.22 C ANISOU 2478 CB ARG A1118 16746 21058 23072 1804 -858 -1324 C ATOM 2479 CG ARG A1118 37.094 48.367 51.435 1.00165.30 C ANISOU 2479 CG ARG A1118 17151 22199 23456 1937 -641 -1281 C ATOM 2480 CD ARG A1118 36.120 49.446 51.887 1.00169.19 C ANISOU 2480 CD ARG A1118 17467 22889 23928 2154 -731 -1652 C ATOM 2481 NE ARG A1118 35.442 49.092 53.131 1.00175.22 N ANISOU 2481 NE ARG A1118 17979 24203 24393 2302 -523 -1638 N ATOM 2482 CZ ARG A1118 35.939 49.324 54.342 1.00177.97 C ANISOU 2482 CZ ARG A1118 18251 24938 24432 2484 -491 -1762 C ATOM 2483 NH1 ARG A1118 37.123 49.907 54.476 1.00177.07 N ANISOU 2483 NH1 ARG A1118 18285 24713 24278 2524 -661 -1922 N ATOM 2484 NH2 ARG A1118 35.254 48.971 55.422 1.00179.88 N ANISOU 2484 NH2 ARG A1118 18253 25708 24387 2612 -289 -1726 N ATOM 2485 N MET A1119 35.726 49.694 47.826 1.00153.72 N ANISOU 2485 N MET A1119 15917 19639 22850 1677 -1097 -1490 N ATOM 2486 CA MET A1119 34.358 50.032 47.453 1.00163.40 C ANISOU 2486 CA MET A1119 16981 20910 24193 1747 -1132 -1606 C ATOM 2487 C MET A1119 33.917 49.344 46.166 1.00162.97 C ANISOU 2487 C MET A1119 16973 20606 24342 1505 -1121 -1391 C ATOM 2488 O MET A1119 32.748 48.959 46.042 1.00160.50 O ANISOU 2488 O MET A1119 16458 20473 24051 1470 -1030 -1354 O ATOM 2489 CB MET A1119 34.214 51.548 47.306 1.00159.77 C ANISOU 2489 CB MET A1119 16570 20291 23846 1973 -1390 -1961 C ATOM 2490 CG MET A1119 34.338 52.307 48.613 1.00167.48 C ANISOU 2490 CG MET A1119 17461 21555 24619 2242 -1405 -2255 C ATOM 2491 SD MET A1119 34.236 54.089 48.385 1.00175.16 S ANISOU 2491 SD MET A1119 18562 22229 25761 2499 -1718 -2683 S ATOM 2492 CE MET A1119 34.535 54.663 50.055 1.00186.96 C ANISOU 2492 CE MET A1119 19956 24120 26960 2762 -1685 -3016 C ATOM 2493 N LEU A1120 34.824 49.187 45.197 1.00148.68 N ANISOU 2493 N LEU A1120 15407 18418 22668 1329 -1213 -1263 N ATOM 2494 CA LEU A1120 34.465 48.499 43.961 1.00131.48 C ANISOU 2494 CA LEU A1120 13281 16016 20657 1096 -1204 -1080 C ATOM 2495 C LEU A1120 34.181 47.024 44.215 1.00140.40 C ANISOU 2495 C LEU A1120 14339 17302 21704 903 -934 -813 C ATOM 2496 O LEU A1120 33.244 46.458 43.639 1.00140.11 O ANISOU 2496 O LEU A1120 14200 17281 21757 747 -873 -736 O ATOM 2497 CB LEU A1120 35.574 48.662 42.920 1.00118.18 C ANISOU 2497 CB LEU A1120 11870 13933 19100 967 -1349 -1010 C ATOM 2498 CG LEU A1120 35.812 50.077 42.390 1.00108.27 C ANISOU 2498 CG LEU A1120 10730 12434 17973 1084 -1623 -1221 C ATOM 2499 CD1 LEU A1120 37.000 50.105 41.439 1.00 96.54 C ANISOU 2499 CD1 LEU A1120 9494 10614 16572 915 -1724 -1106 C ATOM 2500 CD2 LEU A1120 34.563 50.614 41.712 1.00115.91 C ANISOU 2500 CD2 LEU A1120 11590 13370 19079 1162 -1747 -1327 C ATOM 2501 N GLN A1121 34.982 46.384 45.070 1.00144.41 N ANISOU 2501 N GLN A1121 14903 17924 22040 905 -774 -665 N ATOM 2502 CA GLN A1121 34.687 45.012 45.468 1.00146.08 C ANISOU 2502 CA GLN A1121 15066 18273 22163 746 -503 -393 C ATOM 2503 C GLN A1121 33.390 44.936 46.263 1.00154.24 C ANISOU 2503 C GLN A1121 15804 19708 23094 793 -366 -437 C ATOM 2504 O GLN A1121 32.705 43.906 46.242 1.00157.60 O ANISOU 2504 O GLN A1121 16148 20209 23522 586 -172 -239 O ATOM 2505 CB GLN A1121 35.852 44.444 46.280 1.00130.78 C ANISOU 2505 CB GLN A1121 13254 16397 20040 800 -376 -217 C ATOM 2506 CG GLN A1121 35.700 42.985 46.675 1.00136.54 C ANISOU 2506 CG GLN A1121 14002 17192 20684 650 -95 112 C ATOM 2507 CD GLN A1121 36.914 42.451 47.411 1.00157.25 C ANISOU 2507 CD GLN A1121 16763 19868 23118 753 9 304 C ATOM 2508 OE1 GLN A1121 37.882 43.175 47.644 1.00159.45 O ANISOU 2508 OE1 GLN A1121 17092 20176 23317 919 -133 174 O ATOM 2509 NE2 GLN A1121 36.865 41.178 47.786 1.00173.58 N ANISOU 2509 NE2 GLN A1121 18891 21952 25110 652 255 621 N ATOM 2510 N GLN A1122 33.031 46.015 46.952 1.00153.01 N ANISOU 2510 N GLN A1122 15480 19811 22844 1054 -461 -702 N ATOM 2511 CA GLN A1122 31.821 46.080 47.757 1.00161.91 C ANISOU 2511 CA GLN A1122 16291 21385 23842 1149 -339 -784 C ATOM 2512 C GLN A1122 30.615 46.558 46.950 1.00162.07 C ANISOU 2512 C GLN A1122 16135 21411 24033 1141 -457 -944 C ATOM 2513 O GLN A1122 29.526 46.714 47.514 1.00159.64 O ANISOU 2513 O GLN A1122 15525 21504 23627 1241 -376 -1045 O ATOM 2514 CB GLN A1122 32.074 46.991 48.969 1.00172.87 C ANISOU 2514 CB GLN A1122 17585 23085 25013 1474 -377 -1020 C ATOM 2515 CG GLN A1122 31.039 46.943 50.083 1.00183.59 C ANISOU 2515 CG GLN A1122 18611 24998 26146 1606 -200 -1078 C ATOM 2516 CD GLN A1122 31.445 47.783 51.280 1.00183.64 C ANISOU 2516 CD GLN A1122 18558 25305 25910 1927 -239 -1326 C ATOM 2517 OE1 GLN A1122 32.495 48.428 51.273 1.00170.57 O ANISOU 2517 OE1 GLN A1122 17110 23428 24271 2030 -409 -1465 O ATOM 2518 NE2 GLN A1122 30.615 47.780 52.316 1.00191.28 N ANISOU 2518 NE2 GLN A1122 19231 26806 26641 2072 -79 -1393 N ATOM 2519 N LYS A1123 30.788 46.781 45.644 1.00151.22 N ANISOU 2519 N LYS A1123 14927 19641 22890 1036 -644 -963 N ATOM 2520 CA LYS A1123 29.698 47.153 44.736 1.00137.15 C ANISOU 2520 CA LYS A1123 12991 17856 21264 1020 -773 -1080 C ATOM 2521 C LYS A1123 29.049 48.472 45.155 1.00150.02 C ANISOU 2521 C LYS A1123 14436 19702 22862 1387 -925 -1400 C ATOM 2522 O LYS A1123 27.828 48.582 45.281 1.00162.62 O ANISOU 2522 O LYS A1123 15724 21635 24429 1465 -892 -1495 O ATOM 2523 CB LYS A1123 28.658 46.033 44.635 1.00124.99 C ANISOU 2523 CB LYS A1123 11227 16548 19715 743 -567 -907 C ATOM 2524 N ARG A1124 29.890 49.488 45.365 1.00157.00 N ANISOU 2524 N ARG A1124 15511 20389 23751 1615 -1096 -1578 N ATOM 2525 CA ARG A1124 29.457 50.830 45.759 1.00154.13 C ANISOU 2525 CA ARG A1124 15056 20127 23377 1990 -1264 -1912 C ATOM 2526 C ARG A1124 30.060 51.790 44.735 1.00152.21 C ANISOU 2526 C ARG A1124 15100 19383 23349 2047 -1551 -2006 C ATOM 2527 O ARG A1124 31.128 52.367 44.953 1.00153.63 O ANISOU 2527 O ARG A1124 15518 19322 23532 2103 -1652 -2087 O ATOM 2528 CB ARG A1124 29.901 51.135 47.191 1.00160.96 C ANISOU 2528 CB ARG A1124 15885 21261 24014 2196 -1174 -2057 C ATOM 2529 CG ARG A1124 29.280 50.184 48.207 1.00170.32 C ANISOU 2529 CG ARG A1124 16782 22971 24961 2137 -878 -1926 C ATOM 2530 CD ARG A1124 29.870 50.319 49.604 1.00177.96 C ANISOU 2530 CD ARG A1124 17732 24227 25659 2307 -774 -2016 C ATOM 2531 NE ARG A1124 29.515 51.560 50.282 1.00188.56 N ANISOU 2531 NE ARG A1124 18966 25761 26916 2697 -897 -2413 N ATOM 2532 CZ ARG A1124 30.022 51.932 51.454 1.00188.20 C ANISOU 2532 CZ ARG A1124 18913 25958 26635 2891 -861 -2587 C ATOM 2533 NH1 ARG A1124 30.905 51.159 52.071 1.00179.41 N ANISOU 2533 NH1 ARG A1124 17879 24948 25342 2740 -711 -2371 N ATOM 2534 NH2 ARG A1124 29.647 53.076 52.010 1.00195.11 N ANISOU 2534 NH2 ARG A1124 19705 26981 27448 3254 -981 -2986 N ATOM 2535 N TRP A1125 29.359 51.966 43.613 1.00163.08 N ANISOU 2535 N TRP A1125 16443 20626 24894 2022 -1684 -1988 N ATOM 2536 CA TRP A1125 29.975 52.578 42.440 1.00169.45 C ANISOU 2536 CA TRP A1125 17541 20946 25897 1980 -1921 -1965 C ATOM 2537 C TRP A1125 29.972 54.099 42.527 1.00177.34 C ANISOU 2537 C TRP A1125 18651 21755 26977 2330 -2159 -2242 C ATOM 2538 O TRP A1125 30.982 54.746 42.233 1.00171.43 O ANISOU 2538 O TRP A1125 18204 20615 26318 2311 -2308 -2266 O ATOM 2539 CB TRP A1125 29.256 52.114 41.173 1.00168.57 C ANISOU 2539 CB TRP A1125 17356 20787 25907 1808 -1972 -1819 C ATOM 2540 CG TRP A1125 29.295 50.632 40.984 1.00173.07 C ANISOU 2540 CG TRP A1125 17870 21459 26429 1438 -1754 -1568 C ATOM 2541 CD1 TRP A1125 30.302 49.901 40.427 1.00177.84 C ANISOU 2541 CD1 TRP A1125 18719 21782 27071 1154 -1708 -1363 C ATOM 2542 CD2 TRP A1125 28.268 49.699 41.336 1.00176.05 C ANISOU 2542 CD2 TRP A1125 17934 22236 26719 1308 -1550 -1501 C ATOM 2543 NE1 TRP A1125 29.970 48.566 40.422 1.00176.50 N ANISOU 2543 NE1 TRP A1125 18440 21767 26855 873 -1491 -1181 N ATOM 2544 CE2 TRP A1125 28.725 48.418 40.973 1.00180.06 C ANISOU 2544 CE2 TRP A1125 18553 22629 27235 935 -1390 -1253 C ATOM 2545 CE3 TRP A1125 27.007 49.824 41.927 1.00193.00 C ANISOU 2545 CE3 TRP A1125 19713 24838 28779 1467 -1482 -1629 C ATOM 2546 CZ2 TRP A1125 27.967 47.269 41.182 1.00199.04 C ANISOU 2546 CZ2 TRP A1125 20740 25306 29579 686 -1168 -1123 C ATOM 2547 CZ3 TRP A1125 26.256 48.683 42.134 1.00206.65 C ANISOU 2547 CZ3 TRP A1125 21190 26894 30433 1205 -1255 -1491 C ATOM 2548 CH2 TRP A1125 26.737 47.422 41.762 1.00210.62 C ANISOU 2548 CH2 TRP A1125 21839 27224 30963 803 -1102 -1237 C ATOM 2549 N ASP A1126 28.839 54.688 42.915 1.00192.34 N ANISOU 2549 N ASP A1126 20311 23922 28848 2650 -2196 -2455 N ATOM 2550 CA ASP A1126 28.768 56.140 43.033 1.00199.28 C ANISOU 2550 CA ASP A1126 21315 24589 29812 3025 -2420 -2738 C ATOM 2551 C ASP A1126 29.689 56.658 44.130 1.00199.23 C ANISOU 2551 C ASP A1126 21465 24520 29712 3121 -2408 -2934 C ATOM 2552 O ASP A1126 30.251 57.752 44.002 1.00209.60 O ANISOU 2552 O ASP A1126 23053 25442 31145 3257 -2610 -3099 O ATOM 2553 CB ASP A1126 27.328 56.577 43.297 1.00198.20 C ANISOU 2553 CB ASP A1126 20856 24815 29638 3389 -2440 -2937 C ATOM 2554 CG ASP A1126 26.429 56.374 42.092 1.00193.12 C ANISOU 2554 CG ASP A1126 20077 24194 29106 3350 -2531 -2793 C ATOM 2555 OD1 ASP A1126 26.935 56.443 40.952 1.00186.45 O ANISOU 2555 OD1 ASP A1126 19482 22946 28414 3174 -2677 -2621 O ATOM 2556 OD2 ASP A1126 25.217 56.144 42.286 1.00199.25 O ANISOU 2556 OD2 ASP A1126 20477 25431 29799 3492 -2455 -2855 O ATOM 2557 N GLU A1127 29.860 55.890 45.207 1.00184.24 N ANISOU 2557 N GLU A1127 19402 23006 27594 3041 -2175 -2915 N ATOM 2558 CA GLU A1127 30.732 56.318 46.293 1.00174.00 C ANISOU 2558 CA GLU A1127 18221 21727 26166 3128 -2161 -3109 C ATOM 2559 C GLU A1127 32.206 56.162 45.938 1.00170.10 C ANISOU 2559 C GLU A1127 18038 20865 25729 2832 -2211 -2953 C ATOM 2560 O GLU A1127 33.032 56.967 46.380 1.00176.38 O ANISOU 2560 O GLU A1127 19025 21471 26520 2900 -2327 -3156 O ATOM 2561 CB GLU A1127 30.400 55.538 47.566 1.00178.74 C ANISOU 2561 CB GLU A1127 18526 22910 26478 3160 -1895 -3113 C ATOM 2562 CG GLU A1127 31.207 55.951 48.784 1.00195.47 C ANISOU 2562 CG GLU A1127 20712 25150 28405 3279 -1875 -3335 C ATOM 2563 CD GLU A1127 30.755 55.237 50.038 1.00205.34 C ANISOU 2563 CD GLU A1127 21651 27027 29341 3349 -1612 -3330 C ATOM 2564 OE1 GLU A1127 29.793 54.446 49.948 1.00206.87 O ANISOU 2564 OE1 GLU A1127 21579 27536 29486 3287 -1442 -3150 O ATOM 2565 OE2 GLU A1127 31.359 55.460 51.109 1.00206.76 O ANISOU 2565 OE2 GLU A1127 21844 27403 29312 3450 -1574 -3499 O ATOM 2566 N ALA A1128 32.555 55.146 45.147 1.00160.76 N ANISOU 2566 N ALA A1128 16899 19591 24592 2502 -2126 -2615 N ATOM 2567 CA ALA A1128 33.929 54.992 44.688 1.00146.07 C ANISOU 2567 CA ALA A1128 15310 17405 22784 2238 -2175 -2460 C ATOM 2568 C ALA A1128 34.288 55.977 43.585 1.00140.79 C ANISOU 2568 C ALA A1128 14914 16229 22353 2218 -2435 -2492 C ATOM 2569 O ALA A1128 35.477 56.237 43.366 1.00139.99 O ANISOU 2569 O ALA A1128 15043 15857 22290 2050 -2515 -2455 O ATOM 2570 CB ALA A1128 34.167 53.563 44.195 1.00135.01 C ANISOU 2570 CB ALA A1128 13877 16070 21350 1926 -1992 -2105 C ATOM 2571 N ALA A1129 33.291 56.528 42.891 1.00152.07 N ANISOU 2571 N ALA A1129 16310 17544 23925 2384 -2565 -2546 N ATOM 2572 CA ALA A1129 33.568 57.469 41.812 1.00157.66 C ANISOU 2572 CA ALA A1129 17289 17765 24850 2380 -2811 -2535 C ATOM 2573 C ALA A1129 34.101 58.792 42.350 1.00156.18 C ANISOU 2573 C ALA A1129 17317 17303 24721 2554 -2982 -2823 C ATOM 2574 O ALA A1129 34.964 59.419 41.724 1.00153.75 O ANISOU 2574 O ALA A1129 17299 16571 24549 2407 -3138 -2777 O ATOM 2575 CB ALA A1129 32.305 57.694 40.983 1.00161.58 C ANISOU 2575 CB ALA A1129 17675 18260 25458 2556 -2909 -2509 C ATOM 2576 N VAL A1130 33.598 59.236 43.504 1.00157.90 N ANISOU 2576 N VAL A1130 17400 17761 24835 2853 -2952 -3130 N ATOM 2577 CA VAL A1130 34.045 60.509 44.059 1.00161.89 C ANISOU 2577 CA VAL A1130 18120 17994 25398 3027 -3118 -3456 C ATOM 2578 C VAL A1130 35.416 60.399 44.716 1.00158.87 C ANISOU 2578 C VAL A1130 17852 17608 24903 2784 -3075 -3499 C ATOM 2579 O VAL A1130 36.112 61.413 44.849 1.00165.11 O ANISOU 2579 O VAL A1130 18894 18055 25787 2774 -3241 -3702 O ATOM 2580 CB VAL A1130 33.017 61.060 45.062 1.00161.21 C ANISOU 2580 CB VAL A1130 17847 18184 25222 3465 -3108 -3813 C ATOM 2581 CG1 VAL A1130 31.677 61.287 44.376 1.00164.39 C ANISOU 2581 CG1 VAL A1130 18124 18599 25737 3740 -3178 -3788 C ATOM 2582 CG2 VAL A1130 32.864 60.125 46.250 1.00159.40 C ANISOU 2582 CG2 VAL A1130 17301 18564 24700 3472 -2852 -3849 C ATOM 2583 N ASN A1131 35.827 59.198 45.130 1.00152.78 N ANISOU 2583 N ASN A1131 16906 17210 23935 2585 -2861 -3310 N ATOM 2584 CA ASN A1131 37.146 59.039 45.737 1.00150.02 C ANISOU 2584 CA ASN A1131 16632 16914 23454 2376 -2823 -3329 C ATOM 2585 C ASN A1131 38.249 59.124 44.690 1.00149.21 C ANISOU 2585 C ASN A1131 16780 16412 23501 2042 -2930 -3114 C ATOM 2586 O ASN A1131 39.264 59.799 44.899 1.00175.39 O ANISOU 2586 O ASN A1131 20270 19534 26835 1916 -3044 -3251 O ATOM 2587 CB ASN A1131 37.227 57.715 46.498 1.00141.51 C ANISOU 2587 CB ASN A1131 15301 16354 22111 2310 -2560 -3163 C ATOM 2588 CG ASN A1131 36.375 57.712 47.749 1.00159.35 C ANISOU 2588 CG ASN A1131 17311 19068 24164 2612 -2444 -3398 C ATOM 2589 OD1 ASN A1131 35.397 56.973 47.846 1.00169.66 O ANISOU 2589 OD1 ASN A1131 18384 20683 25395 2693 -2282 -3274 O ATOM 2590 ND2 ASN A1131 36.749 58.535 48.721 1.00168.35 N ANISOU 2590 ND2 ASN A1131 18491 20275 25200 2764 -2523 -3750 N ATOM 2591 N LEU A1132 38.075 58.441 43.558 1.00122.56 N ANISOU 2591 N LEU A1132 13412 12937 20219 1881 -2892 -2786 N ATOM 2592 CA LEU A1132 39.085 58.496 42.509 1.00121.10 C ANISOU 2592 CA LEU A1132 13444 12417 20152 1574 -2980 -2571 C ATOM 2593 C LEU A1132 39.205 59.883 41.892 1.00129.97 C ANISOU 2593 C LEU A1132 14846 13039 21500 1588 -3232 -2693 C ATOM 2594 O LEU A1132 40.231 60.185 41.273 1.00134.17 O ANISOU 2594 O LEU A1132 15573 13299 22107 1318 -3320 -2579 O ATOM 2595 CB LEU A1132 38.781 57.463 41.425 1.00115.11 C ANISOU 2595 CB LEU A1132 12629 11683 19426 1425 -2885 -2226 C ATOM 2596 CG LEU A1132 38.915 55.993 41.825 1.00118.24 C ANISOU 2596 CG LEU A1132 12829 12465 19633 1326 -2634 -2038 C ATOM 2597 CD1 LEU A1132 38.461 55.086 40.695 1.00110.14 C ANISOU 2597 CD1 LEU A1132 11773 11404 18670 1190 -2565 -1756 C ATOM 2598 CD2 LEU A1132 40.350 55.686 42.217 1.00126.64 C ANISOU 2598 CD2 LEU A1132 13948 13600 20570 1135 -2579 -1981 C ATOM 2599 N ALA A1133 38.186 60.732 42.044 1.00138.29 N ANISOU 2599 N ALA A1133 15923 13965 22657 1901 -3346 -2911 N ATOM 2600 CA ALA A1133 38.327 62.125 41.637 1.00130.52 C ANISOU 2600 CA ALA A1133 15241 12462 21886 1950 -3586 -3054 C ATOM 2601 C ALA A1133 39.281 62.874 42.558 1.00135.49 C ANISOU 2601 C ALA A1133 16006 12990 22484 1872 -3656 -3348 C ATOM 2602 O ALA A1133 39.925 63.840 42.133 1.00151.38 O ANISOU 2602 O ALA A1133 18310 14544 24665 1720 -3831 -3391 O ATOM 2603 CB ALA A1133 36.961 62.808 41.609 1.00127.88 C ANISOU 2603 CB ALA A1133 14893 12035 21662 2365 -3687 -3222 C ATOM 2604 N LYS A1134 39.389 62.443 43.816 1.00137.06 N ANISOU 2604 N LYS A1134 15996 13623 22459 1957 -3522 -3550 N ATOM 2605 CA LYS A1134 40.324 63.046 44.757 1.00151.98 C ANISOU 2605 CA LYS A1134 17969 15507 24271 1867 -3582 -3849 C ATOM 2606 C LYS A1134 41.775 62.718 44.433 1.00156.94 C ANISOU 2606 C LYS A1134 18661 16112 24856 1437 -3570 -3656 C ATOM 2607 O LYS A1134 42.676 63.312 45.035 1.00173.11 O ANISOU 2607 O LYS A1134 20798 18112 26864 1292 -3653 -3888 O ATOM 2608 CB LYS A1134 40.007 62.574 46.176 1.00160.69 C ANISOU 2608 CB LYS A1134 18794 17162 25097 2092 -3429 -4086 C ATOM 2609 CG LYS A1134 38.639 62.985 46.687 1.00169.62 C ANISOU 2609 CG LYS A1134 19826 18393 26229 2536 -3433 -4345 C ATOM 2610 CD LYS A1134 38.392 62.417 48.075 1.00178.84 C ANISOU 2610 CD LYS A1134 20695 20174 27079 2722 -3254 -4533 C ATOM 2611 CE LYS A1134 36.998 62.756 48.574 1.00187.14 C ANISOU 2611 CE LYS A1134 21599 21403 28102 3169 -3234 -4780 C ATOM 2612 NZ LYS A1134 36.733 62.168 49.917 1.00189.59 N ANISOU 2612 NZ LYS A1134 21601 22360 28074 3340 -3040 -4934 N ATOM 2613 N SER A1135 42.019 61.798 43.505 1.00146.87 N ANISOU 2613 N SER A1135 17334 14893 23579 1235 -3473 -3259 N ATOM 2614 CA SER A1135 43.358 61.296 43.252 1.00140.39 C ANISOU 2614 CA SER A1135 16509 14162 22670 875 -3425 -3063 C ATOM 2615 C SER A1135 44.194 62.309 42.476 1.00131.45 C ANISOU 2615 C SER A1135 15661 12550 21732 585 -3616 -3046 C ATOM 2616 O SER A1135 43.678 63.196 41.790 1.00121.83 O ANISOU 2616 O SER A1135 14671 10875 20743 640 -3770 -3057 O ATOM 2617 CB SER A1135 43.298 59.980 42.476 1.00126.97 C ANISOU 2617 CB SER A1135 14676 12658 20907 783 -3256 -2666 C ATOM 2618 OG SER A1135 42.798 60.179 41.165 1.00133.03 O ANISOU 2618 OG SER A1135 15589 13080 21876 745 -3337 -2456 O ATOM 2619 N ARG A1136 45.514 62.162 42.602 1.00139.13 N ANISOU 2619 N ARG A1136 16610 13651 22601 271 -3601 -3006 N ATOM 2620 CA ARG A1136 46.433 62.913 41.757 1.00136.93 C ANISOU 2620 CA ARG A1136 16558 12992 22478 -86 -3743 -2910 C ATOM 2621 C ARG A1136 46.321 62.467 40.303 1.00122.52 C ANISOU 2621 C ARG A1136 14800 11001 20752 -208 -3714 -2499 C ATOM 2622 O ARG A1136 46.546 63.267 39.387 1.00115.64 O ANISOU 2622 O ARG A1136 14170 9700 20068 -400 -3853 -2389 O ATOM 2623 CB ARG A1136 47.860 62.741 42.284 1.00141.88 C ANISOU 2623 CB ARG A1136 17071 13911 22928 -387 -3715 -2964 C ATOM 2624 CG ARG A1136 48.910 63.635 41.647 1.00160.31 C ANISOU 2624 CG ARG A1136 19606 15906 25397 -804 -3862 -2931 C ATOM 2625 CD ARG A1136 50.278 63.393 42.280 1.00164.36 C ANISOU 2625 CD ARG A1136 19934 16818 25698 -1077 -3828 -3013 C ATOM 2626 NE ARG A1136 50.328 63.800 43.684 1.00156.75 N ANISOU 2626 NE ARG A1136 18892 16052 24613 -959 -3876 -3440 N ATOM 2627 CZ ARG A1136 50.633 65.025 44.097 1.00163.52 C ANISOU 2627 CZ ARG A1136 19934 16611 25587 -1121 -4058 -3781 C ATOM 2628 NH1 ARG A1136 50.927 65.969 43.214 1.00171.28 N ANISOU 2628 NH1 ARG A1136 21201 17054 26824 -1421 -4203 -3711 N ATOM 2629 NH2 ARG A1136 50.654 65.306 45.393 1.00174.52 N ANISOU 2629 NH2 ARG A1136 21235 18242 26834 -991 -4093 -4190 N ATOM 2630 N TRP A1137 45.962 61.199 40.081 1.00118.53 N ANISOU 2630 N TRP A1137 14092 10826 20116 -102 -3535 -2273 N ATOM 2631 CA TRP A1137 45.668 60.709 38.737 1.00117.53 C ANISOU 2631 CA TRP A1137 14013 10578 20066 -168 -3505 -1929 C ATOM 2632 C TRP A1137 44.534 61.489 38.086 1.00129.72 C ANISOU 2632 C TRP A1137 15739 11725 21824 16 -3647 -1930 C ATOM 2633 O TRP A1137 44.589 61.795 36.889 1.00126.72 O ANISOU 2633 O TRP A1137 15524 11059 21564 -126 -3731 -1698 O ATOM 2634 CB TRP A1137 45.323 59.223 38.802 1.00116.17 C ANISOU 2634 CB TRP A1137 13601 10813 19725 -51 -3289 -1760 C ATOM 2635 CG TRP A1137 44.702 58.684 37.558 1.00126.99 C ANISOU 2635 CG TRP A1137 14999 12086 21166 -51 -3259 -1483 C ATOM 2636 CD1 TRP A1137 45.266 58.598 36.319 1.00135.90 C ANISOU 2636 CD1 TRP A1137 16231 13073 22331 -290 -3285 -1224 C ATOM 2637 CD2 TRP A1137 43.380 58.148 37.436 1.00127.86 C ANISOU 2637 CD2 TRP A1137 15011 12274 21296 192 -3198 -1453 C ATOM 2638 NE1 TRP A1137 44.374 58.040 35.431 1.00118.82 N ANISOU 2638 NE1 TRP A1137 14051 10891 20205 -200 -3253 -1048 N ATOM 2639 CE2 TRP A1137 43.208 57.755 36.094 1.00120.09 C ANISOU 2639 CE2 TRP A1137 14083 11182 20363 82 -3202 -1187 C ATOM 2640 CE3 TRP A1137 42.324 57.962 38.334 1.00127.43 C ANISOU 2640 CE3 TRP A1137 14806 12406 21205 480 -3137 -1631 C ATOM 2641 CZ2 TRP A1137 42.023 57.187 35.629 1.00124.11 C ANISOU 2641 CZ2 TRP A1137 14502 11758 20896 236 -3160 -1108 C ATOM 2642 CZ3 TRP A1137 41.149 57.398 37.871 1.00121.89 C ANISOU 2642 CZ3 TRP A1137 14004 11775 20532 624 -3084 -1535 C ATOM 2643 CH2 TRP A1137 41.008 57.017 36.532 1.00117.74 C ANISOU 2643 CH2 TRP A1137 13536 11132 20065 495 -3102 -1283 C ATOM 2644 N TYR A1138 43.487 61.801 38.853 1.00132.44 N ANISOU 2644 N TYR A1138 16041 12080 22199 353 -3672 -2179 N ATOM 2645 CA TYR A1138 42.364 62.553 38.303 1.00118.35 C ANISOU 2645 CA TYR A1138 14406 9956 20605 592 -3813 -2197 C ATOM 2646 C TYR A1138 42.796 63.942 37.851 1.00136.00 C ANISOU 2646 C TYR A1138 16981 11643 23049 460 -4029 -2240 C ATOM 2647 O TYR A1138 42.382 64.415 36.787 1.00142.43 O ANISOU 2647 O TYR A1138 17979 12121 24016 479 -4146 -2045 O ATOM 2648 CB TYR A1138 41.247 62.656 39.341 1.00117.96 C ANISOU 2648 CB TYR A1138 14218 10079 20524 994 -3789 -2495 C ATOM 2649 CG TYR A1138 40.033 63.423 38.870 1.00138.03 C ANISOU 2649 CG TYR A1138 16874 12328 23243 1309 -3933 -2541 C ATOM 2650 CD1 TYR A1138 39.091 62.831 38.039 1.00140.51 C ANISOU 2650 CD1 TYR A1138 17071 12751 23567 1433 -3897 -2315 C ATOM 2651 CD2 TYR A1138 39.833 64.745 39.250 1.00156.22 C ANISOU 2651 CD2 TYR A1138 19407 14247 25703 1491 -4113 -2820 C ATOM 2652 CE1 TYR A1138 37.979 63.532 37.607 1.00144.20 C ANISOU 2652 CE1 TYR A1138 17614 13000 24175 1750 -4039 -2352 C ATOM 2653 CE2 TYR A1138 38.726 65.453 38.824 1.00144.81 C ANISOU 2653 CE2 TYR A1138 18070 12535 24415 1831 -4249 -2855 C ATOM 2654 CZ TYR A1138 37.803 64.843 38.003 1.00153.57 C ANISOU 2654 CZ TYR A1138 19030 13806 25514 1968 -4213 -2612 C ATOM 2655 OH TYR A1138 36.700 65.545 37.576 1.00172.42 O ANISOU 2655 OH TYR A1138 21497 15976 28038 2333 -4358 -2640 O ATOM 2656 N ASN A1139 43.634 64.606 38.647 1.00131.66 N ANISOU 2656 N ASN A1139 16525 10999 22502 312 -4089 -2489 N ATOM 2657 CA ASN A1139 44.022 65.981 38.367 1.00141.81 C ANISOU 2657 CA ASN A1139 18157 11721 24002 170 -4294 -2575 C ATOM 2658 C ASN A1139 45.035 66.098 37.235 1.00138.52 C ANISOU 2658 C ASN A1139 17893 11100 23639 -269 -4330 -2238 C ATOM 2659 O ASN A1139 45.186 67.187 36.670 1.00141.69 O ANISOU 2659 O ASN A1139 18614 10977 24243 -395 -4497 -2189 O ATOM 2660 CB ASN A1139 44.590 66.628 39.632 1.00167.09 C ANISOU 2660 CB ASN A1139 21396 14913 27178 123 -4346 -2992 C ATOM 2661 CG ASN A1139 43.542 66.811 40.713 1.00178.24 C ANISOU 2661 CG ASN A1139 22719 16445 28558 582 -4345 -3364 C ATOM 2662 OD1 ASN A1139 42.407 67.201 40.436 1.00175.11 O ANISOU 2662 OD1 ASN A1139 22410 15833 28292 930 -4415 -3387 O ATOM 2663 ND2 ASN A1139 43.917 66.527 41.955 1.00185.18 N ANISOU 2663 ND2 ASN A1139 23406 17714 29242 601 -4264 -3655 N ATOM 2664 N GLN A1140 45.732 65.014 36.889 1.00137.92 N ANISOU 2664 N GLN A1140 17603 11419 23382 -496 -4173 -1999 N ATOM 2665 CA GLN A1140 46.780 65.097 35.879 1.00142.19 C ANISOU 2665 CA GLN A1140 18247 11846 23934 -917 -4189 -1700 C ATOM 2666 C GLN A1140 46.272 64.807 34.471 1.00147.43 C ANISOU 2666 C GLN A1140 18976 12401 24640 -895 -4191 -1323 C ATOM 2667 O GLN A1140 46.629 65.523 33.529 1.00128.97 O ANISOU 2667 O GLN A1140 16877 9707 22420 -1122 -4301 -1108 O ATOM 2668 CB GLN A1140 47.930 64.151 36.232 1.00128.09 C ANISOU 2668 CB GLN A1140 16197 10555 21916 -1168 -4027 -1658 C ATOM 2669 CG GLN A1140 48.722 64.595 37.455 1.00155.83 C ANISOU 2669 CG GLN A1140 19664 14174 25371 -1298 -4058 -1996 C ATOM 2670 CD GLN A1140 49.866 63.660 37.787 1.00169.89 C ANISOU 2670 CD GLN A1140 21163 16483 26902 -1509 -3908 -1936 C ATOM 2671 OE1 GLN A1140 50.043 62.624 37.147 1.00178.34 O ANISOU 2671 OE1 GLN A1140 22083 17830 27849 -1528 -3768 -1654 O ATOM 2672 NE2 GLN A1140 50.656 64.025 38.791 1.00170.63 N ANISOU 2672 NE2 GLN A1140 21186 16730 26914 -1654 -3944 -2215 N ATOM 2673 N THR A1141 45.447 63.769 34.299 1.00170.20 N ANISOU 2673 N THR A1141 21653 15595 27421 -643 -4073 -1234 N ATOM 2674 CA THR A1141 44.881 63.559 32.971 1.00180.15 C ANISOU 2674 CA THR A1141 22974 16761 28714 -608 -4099 -916 C ATOM 2675 C THR A1141 43.513 64.221 32.877 1.00195.03 C ANISOU 2675 C THR A1141 24980 18367 30756 -230 -4237 -993 C ATOM 2676 O THR A1141 42.682 64.055 33.783 1.00196.84 O ANISOU 2676 O THR A1141 25069 18745 30974 92 -4206 -1248 O ATOM 2677 CB THR A1141 44.785 62.066 32.648 1.00172.66 C ANISOU 2677 CB THR A1141 21753 16278 27572 -594 -3906 -760 C ATOM 2678 OG1 THR A1141 44.235 61.886 31.337 1.00180.49 O ANISOU 2678 OG1 THR A1141 22802 17198 28579 -572 -3945 -483 O ATOM 2679 CG2 THR A1141 43.960 61.308 33.684 1.00178.71 C ANISOU 2679 CG2 THR A1141 22281 17360 28260 -287 -3789 -980 C ATOM 2680 N PRO A1142 43.257 65.008 31.823 1.00204.43 N ANISOU 2680 N PRO A1142 26423 19169 32081 -241 -4392 -775 N ATOM 2681 CA PRO A1142 42.072 65.879 31.817 1.00214.17 C ANISOU 2681 CA PRO A1142 27816 20073 33485 145 -4557 -870 C ATOM 2682 C PRO A1142 40.744 65.139 31.768 1.00203.64 C ANISOU 2682 C PRO A1142 26235 19057 32081 522 -4507 -893 C ATOM 2683 O PRO A1142 39.888 65.327 32.638 1.00229.03 O ANISOU 2683 O PRO A1142 29365 22320 35336 871 -4523 -1173 O ATOM 2684 CB PRO A1142 42.277 66.730 30.557 1.00224.41 C ANISOU 2684 CB PRO A1142 29432 20932 34900 -6 -4714 -543 C ATOM 2685 CG PRO A1142 43.118 65.877 29.661 1.00216.88 C ANISOU 2685 CG PRO A1142 28366 20262 33775 -373 -4593 -233 C ATOM 2686 CD PRO A1142 44.027 65.101 30.570 1.00207.94 C ANISOU 2686 CD PRO A1142 27007 19496 32505 -585 -4417 -413 C ATOM 2687 N ASN A1143 40.568 64.282 30.762 1.00153.24 N ANISOU 2687 N ASN A1143 19722 12921 25581 441 -4441 -615 N ATOM 2688 CA ASN A1143 39.285 63.651 30.501 1.00144.49 C ANISOU 2688 CA ASN A1143 18395 12088 24416 746 -4420 -603 C ATOM 2689 C ASN A1143 39.325 62.134 30.525 1.00134.68 C ANISOU 2689 C ASN A1143 16841 11350 22982 623 -4206 -564 C ATOM 2690 O ASN A1143 38.263 61.512 30.641 1.00145.45 O ANISOU 2690 O ASN A1143 17976 12994 24295 849 -4154 -632 O ATOM 2691 CB ASN A1143 38.732 64.102 29.139 1.00168.13 C ANISOU 2691 CB ASN A1143 21537 14888 27457 830 -4581 -314 C ATOM 2692 N ARG A1144 40.504 61.522 30.403 1.00128.13 N ANISOU 2692 N ARG A1144 15995 10642 22045 273 -4079 -456 N ATOM 2693 CA ARG A1144 40.591 60.069 30.494 1.00105.42 C ANISOU 2693 CA ARG A1144 12859 8196 18999 179 -3870 -431 C ATOM 2694 C ARG A1144 40.107 59.578 31.850 1.00121.54 C ANISOU 2694 C ARG A1144 14685 10492 21002 374 -3746 -701 C ATOM 2695 O ARG A1144 39.373 58.586 31.934 1.00129.08 O ANISOU 2695 O ARG A1144 15419 11752 21876 466 -3625 -712 O ATOM 2696 CB ARG A1144 42.025 59.613 30.239 1.00108.16 C ANISOU 2696 CB ARG A1144 13237 8618 19239 -180 -3764 -294 C ATOM 2697 CG ARG A1144 42.194 58.107 30.251 1.00115.30 C ANISOU 2697 CG ARG A1144 13920 9912 19976 -261 -3550 -250 C ATOM 2698 CD ARG A1144 43.610 57.712 29.899 1.00104.82 C ANISOU 2698 CD ARG A1144 12622 8669 18536 -568 -3457 -108 C ATOM 2699 NE ARG A1144 43.791 56.265 29.910 1.00111.15 N ANISOU 2699 NE ARG A1144 13244 9802 19186 -607 -3253 -71 N ATOM 2700 CZ ARG A1144 44.929 55.659 29.597 1.00111.57 C ANISOU 2700 CZ ARG A1144 13276 10003 19111 -814 -3140 43 C ATOM 2701 NH1 ARG A1144 45.014 54.337 29.629 1.00134.33 N ANISOU 2701 NH1 ARG A1144 16026 13142 21873 -804 -2958 65 N ATOM 2702 NH2 ARG A1144 45.984 56.379 29.244 1.00113.81 N ANISOU 2702 NH2 ARG A1144 13676 10179 19389 -1030 -3207 137 N ATOM 2703 N ALA A1145 40.504 60.265 32.924 1.00122.11 N ANISOU 2703 N ALA A1145 14821 10452 21125 422 -3773 -924 N ATOM 2704 CA ALA A1145 40.058 59.880 34.259 1.00122.54 C ANISOU 2704 CA ALA A1145 14672 10773 21113 621 -3658 -1183 C ATOM 2705 C ALA A1145 38.540 59.932 34.371 1.00120.88 C ANISOU 2705 C ALA A1145 14327 10657 20947 968 -3694 -1286 C ATOM 2706 O ALA A1145 37.921 59.009 34.912 1.00113.24 O ANISOU 2706 O ALA A1145 13104 10049 19874 1065 -3539 -1346 O ATOM 2707 CB ALA A1145 40.703 60.784 35.310 1.00119.74 C ANISOU 2707 CB ALA A1145 14431 10264 20802 628 -3718 -1433 C ATOM 2708 N LYS A1146 37.922 60.993 33.846 1.00126.24 N ANISOU 2708 N LYS A1146 15167 11026 21774 1160 -3895 -1292 N ATOM 2709 CA LYS A1146 36.475 61.137 33.968 1.00127.17 C ANISOU 2709 CA LYS A1146 15133 11261 21924 1532 -3945 -1406 C ATOM 2710 C LYS A1146 35.740 60.078 33.154 1.00130.24 C ANISOU 2710 C LYS A1146 15303 11957 22226 1496 -3867 -1219 C ATOM 2711 O LYS A1146 34.679 59.596 33.569 1.00138.61 O ANISOU 2711 O LYS A1146 16097 13336 23233 1696 -3794 -1328 O ATOM 2712 CB LYS A1146 36.049 62.540 33.539 1.00129.66 C ANISOU 2712 CB LYS A1146 15698 11148 22418 1774 -4190 -1434 C ATOM 2713 CG LYS A1146 34.583 62.836 33.789 1.00154.41 C ANISOU 2713 CG LYS A1146 18667 14415 25584 2225 -4257 -1595 C ATOM 2714 CD LYS A1146 34.227 64.259 33.392 1.00169.49 C ANISOU 2714 CD LYS A1146 20865 15856 27679 2508 -4505 -1618 C ATOM 2715 CE LYS A1146 32.792 64.587 33.767 1.00160.35 C ANISOU 2715 CE LYS A1146 19517 14870 26539 3015 -4567 -1818 C ATOM 2716 NZ LYS A1146 31.817 63.777 32.986 1.00154.90 N ANISOU 2716 NZ LYS A1146 18533 14571 25750 3078 -4540 -1643 N ATOM 2717 N ARG A1147 36.284 59.701 31.993 1.00120.07 N ANISOU 2717 N ARG A1147 14111 10599 20911 1227 -3879 -948 N ATOM 2718 CA ARG A1147 35.684 58.614 31.223 1.00120.07 C ANISOU 2718 CA ARG A1147 13912 10896 20814 1149 -3799 -802 C ATOM 2719 C ARG A1147 35.776 57.293 31.975 1.00125.39 C ANISOU 2719 C ARG A1147 14354 11927 21361 1019 -3550 -865 C ATOM 2720 O ARG A1147 34.819 56.509 31.991 1.00125.30 O ANISOU 2720 O ARG A1147 14100 12215 21295 1077 -3464 -890 O ATOM 2721 CB ARG A1147 36.357 58.493 29.854 1.00116.46 C ANISOU 2721 CB ARG A1147 13621 10302 20329 888 -3857 -522 C ATOM 2722 CG ARG A1147 36.051 59.632 28.900 1.00113.20 C ANISOU 2722 CG ARG A1147 13413 9585 20011 1020 -4099 -386 C ATOM 2723 CD ARG A1147 36.503 59.301 27.484 1.00114.65 C ANISOU 2723 CD ARG A1147 13690 9762 20110 774 -4131 -98 C ATOM 2724 NE ARG A1147 37.953 59.194 27.365 1.00125.89 N ANISOU 2724 NE ARG A1147 15274 11066 21494 442 -4051 14 N ATOM 2725 CZ ARG A1147 38.754 60.212 27.066 1.00126.04 C ANISOU 2725 CZ ARG A1147 15565 10737 21588 335 -4167 133 C ATOM 2726 NH1 ARG A1147 40.064 60.025 26.979 1.00133.00 N ANISOU 2726 NH1 ARG A1147 16534 11591 22410 15 -4077 226 N ATOM 2727 NH2 ARG A1147 38.245 61.416 26.848 1.00127.89 N ANISOU 2727 NH2 ARG A1147 15983 10653 21955 548 -4371 166 N ATOM 2728 N VAL A1148 36.923 57.030 32.605 1.00118.05 N ANISOU 2728 N VAL A1148 13494 10978 20382 837 -3432 -882 N ATOM 2729 CA VAL A1148 37.089 55.807 33.385 1.00114.22 C ANISOU 2729 CA VAL A1148 12823 10805 19772 742 -3194 -916 C ATOM 2730 C VAL A1148 36.163 55.815 34.597 1.00122.24 C ANISOU 2730 C VAL A1148 13628 12049 20766 995 -3125 -1136 C ATOM 2731 O VAL A1148 35.614 54.775 34.981 1.00114.43 O ANISOU 2731 O VAL A1148 12423 11366 19691 975 -2951 -1133 O ATOM 2732 CB VAL A1148 38.566 55.637 33.787 1.00117.31 C ANISOU 2732 CB VAL A1148 13330 11142 20098 534 -3108 -879 C ATOM 2733 CG1 VAL A1148 38.743 54.466 34.733 1.00 95.11 C ANISOU 2733 CG1 VAL A1148 10346 8639 17154 496 -2872 -907 C ATOM 2734 CG2 VAL A1148 39.427 55.443 32.548 1.00 95.48 C ANISOU 2734 CG2 VAL A1148 10719 8240 17320 277 -3140 -651 C ATOM 2735 N ILE A1149 35.963 56.986 35.209 1.00118.39 N ANISOU 2735 N ILE A1149 13207 11419 20355 1233 -3256 -1332 N ATOM 2736 CA ILE A1149 35.045 57.091 36.343 1.00115.27 C ANISOU 2736 CA ILE A1149 12603 11273 19921 1512 -3198 -1565 C ATOM 2737 C ILE A1149 33.627 56.729 35.920 1.00127.66 C ANISOU 2737 C ILE A1149 13937 13075 21492 1658 -3197 -1548 C ATOM 2738 O ILE A1149 32.979 55.868 36.529 1.00127.59 O ANISOU 2738 O ILE A1149 13664 13434 21382 1671 -3021 -1587 O ATOM 2739 CB ILE A1149 35.104 58.498 36.961 1.00127.86 C ANISOU 2739 CB ILE A1149 14348 12626 21607 1761 -3361 -1808 C ATOM 2740 CG1 ILE A1149 36.473 58.740 37.584 1.00133.76 C ANISOU 2740 CG1 ILE A1149 15264 13238 22320 1584 -3338 -1869 C ATOM 2741 CG2 ILE A1149 34.012 58.667 37.996 1.00143.49 C ANISOU 2741 CG2 ILE A1149 16094 14890 23535 2101 -3315 -2063 C ATOM 2742 CD1 ILE A1149 36.799 57.749 38.652 1.00141.77 C ANISOU 2742 CD1 ILE A1149 16085 14633 23151 1513 -3110 -1911 C ATOM 2743 N THR A1150 33.118 57.387 34.875 1.00132.35 N ANISOU 2743 N THR A1150 14616 13480 22193 1763 -3394 -1480 N ATOM 2744 CA THR A1150 31.769 57.094 34.405 1.00143.68 C ANISOU 2744 CA THR A1150 15801 15176 23617 1906 -3419 -1469 C ATOM 2745 C THR A1150 31.618 55.649 33.951 1.00140.75 C ANISOU 2745 C THR A1150 15255 15076 23149 1606 -3247 -1310 C ATOM 2746 O THR A1150 30.499 55.126 33.948 1.00140.49 O ANISOU 2746 O THR A1150 14935 15373 23070 1663 -3192 -1346 O ATOM 2747 CB THR A1150 31.384 58.040 33.264 1.00139.51 C ANISOU 2747 CB THR A1150 15419 14391 23198 2066 -3675 -1383 C ATOM 2748 OG1 THR A1150 32.302 57.877 32.176 1.00146.85 O ANISOU 2748 OG1 THR A1150 16579 15076 24140 1769 -3724 -1141 O ATOM 2749 CG2 THR A1150 31.413 59.486 33.736 1.00128.02 C ANISOU 2749 CG2 THR A1150 14160 12621 21861 2391 -3847 -1554 C ATOM 2750 N THR A1151 32.717 54.989 33.577 1.00132.21 N ANISOU 2750 N THR A1151 14334 13866 22035 1288 -3159 -1148 N ATOM 2751 CA THR A1151 32.632 53.585 33.189 1.00130.37 C ANISOU 2751 CA THR A1151 13975 13838 21720 1011 -2988 -1021 C ATOM 2752 C THR A1151 32.377 52.694 34.400 1.00134.64 C ANISOU 2752 C THR A1151 14308 14678 22171 981 -2745 -1097 C ATOM 2753 O THR A1151 31.642 51.703 34.303 1.00138.48 O ANISOU 2753 O THR A1151 14589 15415 22610 854 -2618 -1061 O ATOM 2754 CB THR A1151 33.909 53.164 32.460 1.00115.51 C ANISOU 2754 CB THR A1151 12331 11737 19819 728 -2961 -841 C ATOM 2755 OG1 THR A1151 34.109 54.008 31.319 1.00101.16 O ANISOU 2755 OG1 THR A1151 10699 9672 18066 744 -3178 -744 O ATOM 2756 CG2 THR A1151 33.804 51.720 31.991 1.00100.54 C ANISOU 2756 CG2 THR A1151 10341 10007 17851 465 -2794 -734 C ATOM 2757 N PHE A1152 32.965 53.031 35.552 1.00124.66 N ANISOU 2757 N PHE A1152 13091 13401 20871 1083 -2679 -1201 N ATOM 2758 CA PHE A1152 32.717 52.247 36.760 1.00123.45 C ANISOU 2758 CA PHE A1152 12742 13560 20604 1080 -2449 -1253 C ATOM 2759 C PHE A1152 31.299 52.456 37.280 1.00133.26 C ANISOU 2759 C PHE A1152 13683 15123 21825 1307 -2439 -1407 C ATOM 2760 O PHE A1152 30.604 51.489 37.613 1.00153.76 O ANISOU 2760 O PHE A1152 16045 18029 24346 1200 -2258 -1367 O ATOM 2761 CB PHE A1152 33.733 52.591 37.852 1.00132.41 C ANISOU 2761 CB PHE A1152 13991 14647 21673 1145 -2396 -1333 C ATOM 2762 CG PHE A1152 35.104 52.017 37.624 1.00136.52 C ANISOU 2762 CG PHE A1152 14712 15003 22157 903 -2324 -1169 C ATOM 2763 CD1 PHE A1152 35.342 50.666 37.829 1.00140.89 C ANISOU 2763 CD1 PHE A1152 15212 15703 22616 715 -2099 -1015 C ATOM 2764 CD2 PHE A1152 36.164 52.828 37.258 1.00135.53 C ANISOU 2764 CD2 PHE A1152 14824 14586 22086 872 -2472 -1170 C ATOM 2765 CE1 PHE A1152 36.602 50.128 37.636 1.00129.30 C ANISOU 2765 CE1 PHE A1152 13916 14107 21104 544 -2032 -872 C ATOM 2766 CE2 PHE A1152 37.429 52.297 37.068 1.00135.30 C ANISOU 2766 CE2 PHE A1152 14936 14469 22003 665 -2400 -1027 C ATOM 2767 CZ PHE A1152 37.647 50.946 37.257 1.00129.52 C ANISOU 2767 CZ PHE A1152 14140 13902 21170 526 -2182 -883 C ATOM 2768 N ARG A1153 30.850 53.711 37.362 1.00135.06 N ANISOU 2768 N ARG A1153 13913 15285 22118 1623 -2628 -1582 N ATOM 2769 CA ARG A1153 29.577 53.983 38.024 1.00140.86 C ANISOU 2769 CA ARG A1153 14343 16370 22808 1898 -2608 -1763 C ATOM 2770 C ARG A1153 28.389 53.582 37.155 1.00141.09 C ANISOU 2770 C ARG A1153 14132 16617 22858 1863 -2645 -1702 C ATOM 2771 O ARG A1153 27.381 53.085 37.671 1.00147.58 O ANISOU 2771 O ARG A1153 14621 17858 23596 1896 -2513 -1762 O ATOM 2772 CB ARG A1153 29.486 55.458 38.422 1.00138.73 C ANISOU 2772 CB ARG A1153 14167 15942 22601 2289 -2799 -1996 C ATOM 2773 CG ARG A1153 29.466 56.447 37.268 1.00128.57 C ANISOU 2773 CG ARG A1153 13092 14286 21472 2413 -3073 -1963 C ATOM 2774 CD ARG A1153 29.281 57.868 37.778 1.00136.09 C ANISOU 2774 CD ARG A1153 14149 15062 22498 2824 -3244 -2211 C ATOM 2775 NE ARG A1153 29.330 58.853 36.702 1.00149.79 N ANISOU 2775 NE ARG A1153 16136 16386 24391 2946 -3506 -2144 N ATOM 2776 CZ ARG A1153 28.281 59.212 35.969 1.00155.00 C ANISOU 2776 CZ ARG A1153 16674 17121 25098 3182 -3651 -2125 C ATOM 2777 NH1 ARG A1153 27.094 58.662 36.190 1.00154.39 N ANISOU 2777 NH1 ARG A1153 16200 17538 24925 3299 -3560 -2188 N ATOM 2778 NH2 ARG A1153 28.419 60.119 35.012 1.00157.91 N ANISOU 2778 NH2 ARG A1153 17308 17091 25598 3296 -3888 -2028 N ATOM 2779 N THR A1154 28.481 53.782 35.840 1.00142.70 N ANISOU 2779 N THR A1154 14482 16582 23156 1783 -2820 -1583 N ATOM 2780 CA THR A1154 27.373 53.438 34.956 1.00139.95 C ANISOU 2780 CA THR A1154 13898 16468 22810 1749 -2882 -1539 C ATOM 2781 C THR A1154 27.391 51.977 34.533 1.00132.56 C ANISOU 2781 C THR A1154 12880 15666 21822 1323 -2704 -1384 C ATOM 2782 O THR A1154 26.330 51.412 34.241 1.00137.30 O ANISOU 2782 O THR A1154 13184 16597 22385 1238 -2669 -1395 O ATOM 2783 CB THR A1154 27.387 54.321 33.703 1.00131.74 C ANISOU 2783 CB THR A1154 13039 15152 21865 1876 -3161 -1475 C ATOM 2784 OG1 THR A1154 28.594 54.092 32.966 1.00122.85 O ANISOU 2784 OG1 THR A1154 12238 13668 20772 1601 -3181 -1297 O ATOM 2785 CG2 THR A1154 27.299 55.791 34.083 1.00141.01 C ANISOU 2785 CG2 THR A1154 14326 16136 23115 2312 -3345 -1628 C ATOM 2786 N GLY A1155 28.565 51.350 34.495 1.00127.20 N ANISOU 2786 N GLY A1155 12452 14740 21139 1056 -2593 -1252 N ATOM 2787 CA GLY A1155 28.646 49.984 34.022 1.00124.57 C ANISOU 2787 CA GLY A1155 12099 14460 20774 674 -2436 -1116 C ATOM 2788 C GLY A1155 28.338 49.815 32.554 1.00123.24 C ANISOU 2788 C GLY A1155 11946 14243 20637 530 -2585 -1047 C ATOM 2789 O GLY A1155 28.001 48.710 32.124 1.00135.64 O ANISOU 2789 O GLY A1155 13419 15937 22180 233 -2475 -996 O ATOM 2790 N THR A1156 28.425 50.888 31.772 1.00115.86 N ANISOU 2790 N THR A1156 11139 13131 19752 730 -2834 -1044 N ATOM 2791 CA THR A1156 28.186 50.851 30.338 1.00127.21 C ANISOU 2791 CA THR A1156 12604 14541 21188 629 -3000 -965 C ATOM 2792 C THR A1156 29.394 51.442 29.623 1.00124.34 C ANISOU 2792 C THR A1156 12607 13779 20857 619 -3126 -838 C ATOM 2793 O THR A1156 30.332 51.945 30.248 1.00132.39 O ANISOU 2793 O THR A1156 13833 14558 21913 693 -3101 -830 O ATOM 2794 CB THR A1156 26.910 51.616 29.958 1.00132.71 C ANISOU 2794 CB THR A1156 13050 15487 21886 910 -3201 -1052 C ATOM 2795 OG1 THR A1156 27.070 53.005 30.268 1.00126.81 O ANISOU 2795 OG1 THR A1156 12438 14539 21205 1294 -3367 -1096 O ATOM 2796 CG2 THR A1156 25.713 51.074 30.724 1.00141.44 C ANISOU 2796 CG2 THR A1156 13751 17045 22946 916 -3065 -1184 C ATOM 2797 N TRP A1157 29.364 51.380 28.293 1.00121.82 N ANISOU 2797 N TRP A1157 12351 13426 20507 511 -3264 -740 N ATOM 2798 CA TRP A1157 30.403 51.954 27.450 1.00107.65 C ANISOU 2798 CA TRP A1157 10874 11309 18718 484 -3392 -594 C ATOM 2799 C TRP A1157 30.029 53.336 26.928 1.00108.34 C ANISOU 2799 C TRP A1157 11026 11290 18848 794 -3662 -555 C ATOM 2800 O TRP A1157 30.680 53.838 26.006 1.00115.32 O ANISOU 2800 O TRP A1157 12146 11950 19720 761 -3795 -399 O ATOM 2801 CB TRP A1157 30.707 51.015 26.282 1.00103.30 C ANISOU 2801 CB TRP A1157 10382 10789 18079 175 -3366 -498 C ATOM 2802 CG TRP A1157 31.401 49.759 26.690 1.00109.54 C ANISOU 2802 CG TRP A1157 11226 11552 18843 -109 -3112 -501 C ATOM 2803 CD1 TRP A1157 30.830 48.544 26.929 1.00114.97 C ANISOU 2803 CD1 TRP A1157 11736 12441 19508 -313 -2940 -578 C ATOM 2804 CD2 TRP A1157 32.805 49.593 26.909 1.00115.13 C ANISOU 2804 CD2 TRP A1157 12188 12011 19546 -213 -3002 -415 C ATOM 2805 NE1 TRP A1157 31.793 47.630 27.283 1.00122.53 N ANISOU 2805 NE1 TRP A1157 12851 13252 20453 -509 -2730 -534 N ATOM 2806 CE2 TRP A1157 33.015 48.251 27.278 1.00115.74 C ANISOU 2806 CE2 TRP A1157 12239 12143 19594 -436 -2766 -439 C ATOM 2807 CE3 TRP A1157 33.906 50.452 26.828 1.00119.73 C ANISOU 2807 CE3 TRP A1157 13011 12337 20143 -147 -3080 -317 C ATOM 2808 CZ2 TRP A1157 34.281 47.746 27.567 1.00117.33 C ANISOU 2808 CZ2 TRP A1157 12637 12174 19770 -544 -2614 -367 C ATOM 2809 CZ3 TRP A1157 35.162 49.949 27.114 1.00124.58 C ANISOU 2809 CZ3 TRP A1157 13788 12820 20726 -292 -2926 -258 C ATOM 2810 CH2 TRP A1157 35.339 48.609 27.477 1.00126.58 C ANISOU 2810 CH2 TRP A1157 14000 13154 20939 -463 -2699 -284 C ATOM 2811 N ASP A1158 29.009 53.967 27.520 1.00116.51 N ANISOU 2811 N ASP A1158 11862 12479 19927 1109 -3738 -684 N ATOM 2812 CA ASP A1158 28.440 55.187 26.951 1.00130.00 C ANISOU 2812 CA ASP A1158 13603 14119 21672 1448 -4003 -647 C ATOM 2813 C ASP A1158 29.466 56.308 26.840 1.00125.67 C ANISOU 2813 C ASP A1158 13440 13098 21211 1548 -4124 -533 C ATOM 2814 O ASP A1158 29.374 57.143 25.934 1.00128.66 O ANISOU 2814 O ASP A1158 13964 13320 21600 1699 -4341 -393 O ATOM 2815 CB ASP A1158 27.247 55.643 27.792 1.00141.98 C ANISOU 2815 CB ASP A1158 14836 15889 23222 1806 -4033 -837 C ATOM 2816 CG ASP A1158 26.079 54.680 27.714 1.00144.85 C ANISOU 2816 CG ASP A1158 14783 16764 23491 1707 -3956 -928 C ATOM 2817 OD1 ASP A1158 25.942 53.996 26.678 1.00150.99 O ANISOU 2817 OD1 ASP A1158 15504 17681 24186 1462 -3986 -838 O ATOM 2818 OD2 ASP A1158 25.300 54.606 28.687 1.00147.98 O ANISOU 2818 OD2 ASP A1158 14899 17441 23886 1861 -3862 -1098 O ATOM 2819 N ALA A1159 30.448 56.347 27.741 1.00126.57 N ANISOU 2819 N ALA A1159 13721 12989 21380 1453 -3991 -582 N ATOM 2820 CA ALA A1159 31.478 57.375 27.679 1.00113.57 C ANISOU 2820 CA ALA A1159 12430 10901 19819 1482 -4094 -491 C ATOM 2821 C ALA A1159 32.437 57.184 26.512 1.00122.48 C ANISOU 2821 C ALA A1159 13780 11868 20888 1189 -4125 -249 C ATOM 2822 O ALA A1159 33.195 58.108 26.199 1.00119.70 O ANISOU 2822 O ALA A1159 13718 11165 20599 1189 -4241 -123 O ATOM 2823 CB ALA A1159 32.266 57.413 28.988 1.00108.82 C ANISOU 2823 CB ALA A1159 11904 10175 19267 1439 -3944 -634 C ATOM 2824 N TYR A1160 32.429 56.018 25.870 1.00124.90 N ANISOU 2824 N TYR A1160 13962 12422 21073 930 -4020 -188 N ATOM 2825 CA TYR A1160 33.335 55.715 24.770 1.00120.18 C ANISOU 2825 CA TYR A1160 13543 11736 20385 657 -4025 14 C ATOM 2826 C TYR A1160 32.616 55.503 23.445 1.00120.45 C ANISOU 2826 C TYR A1160 13486 11975 20304 651 -4159 124 C ATOM 2827 O TYR A1160 33.041 56.046 22.419 1.00106.26 O ANISOU 2827 O TYR A1160 11880 10041 18453 618 -4296 329 O ATOM 2828 CB TYR A1160 34.175 54.477 25.122 1.00126.91 C ANISOU 2828 CB TYR A1160 14375 12673 21171 351 -3776 -22 C ATOM 2829 CG TYR A1160 35.205 54.717 26.207 1.00128.09 C ANISOU 2829 CG TYR A1160 14655 12625 21388 315 -3662 -73 C ATOM 2830 CD1 TYR A1160 36.446 55.257 25.902 1.00113.86 C ANISOU 2830 CD1 TYR A1160 13103 10572 19587 181 -3695 64 C ATOM 2831 CD2 TYR A1160 34.933 54.414 27.536 1.00127.96 C ANISOU 2831 CD2 TYR A1160 14494 12711 21414 404 -3525 -258 C ATOM 2832 CE1 TYR A1160 37.393 55.482 26.886 1.00110.37 C ANISOU 2832 CE1 TYR A1160 12753 9993 19191 132 -3604 0 C ATOM 2833 CE2 TYR A1160 35.876 54.637 28.529 1.00114.76 C ANISOU 2833 CE2 TYR A1160 12926 10902 19775 378 -3434 -315 C ATOM 2834 CZ TYR A1160 37.104 55.173 28.195 1.00117.51 C ANISOU 2834 CZ TYR A1160 13513 11009 20128 240 -3480 -195 C ATOM 2835 OH TYR A1160 38.049 55.403 29.169 1.00116.28 O ANISOU 2835 OH TYR A1160 13434 10757 19990 197 -3403 -268 O ATOM 2836 N PHE A 355 31.531 54.732 23.441 1.00111.24 N ANISOU 2836 N PHE A 355 12021 11159 19084 667 -4123 -6 N ATOM 2837 CA PHE A 355 30.789 54.392 22.230 1.00107.38 C ANISOU 2837 CA PHE A 355 11396 10942 18463 633 -4244 53 C ATOM 2838 C PHE A 355 29.462 53.749 22.624 1.00108.54 C ANISOU 2838 C PHE A 355 11168 11475 18597 692 -4205 -144 C ATOM 2839 O PHE A 355 29.231 53.419 23.789 1.00117.93 O ANISOU 2839 O PHE A 355 12222 12721 19865 712 -4050 -302 O ATOM 2840 CB PHE A 355 31.620 53.494 21.300 1.00108.13 C ANISOU 2840 CB PHE A 355 11599 11067 18419 285 -4156 147 C ATOM 2841 CG PHE A 355 32.431 52.450 22.019 1.00102.65 C ANISOU 2841 CG PHE A 355 10937 10322 17745 29 -3889 55 C ATOM 2842 CD1 PHE A 355 33.778 52.667 22.265 1.00108.67 C ANISOU 2842 CD1 PHE A 355 11948 10809 18532 -70 -3805 151 C ATOM 2843 CD2 PHE A 355 31.855 51.278 22.475 1.00111.91 C ANISOU 2843 CD2 PHE A 355 11889 11722 18911 -110 -3724 -117 C ATOM 2844 CE1 PHE A 355 34.543 51.729 22.930 1.00 98.37 C ANISOU 2844 CE1 PHE A 355 10667 9477 17231 -259 -3570 82 C ATOM 2845 CE2 PHE A 355 32.616 50.333 23.147 1.00122.22 C ANISOU 2845 CE2 PHE A 355 13254 12950 20235 -312 -3481 -171 C ATOM 2846 CZ PHE A 355 33.962 50.560 23.374 1.00104.14 C ANISOU 2846 CZ PHE A 355 11208 10404 17957 -363 -3408 -71 C ATOM 2847 N SER A 356 28.580 53.589 21.635 1.00117.53 N ANISOU 2847 N SER A 356 12124 12913 19617 714 -4350 -128 N ATOM 2848 CA SER A 356 27.206 53.194 21.929 1.00156.42 C ANISOU 2848 CA SER A 356 16659 18249 24525 800 -4358 -306 C ATOM 2849 C SER A 356 27.001 51.683 21.922 1.00149.33 C ANISOU 2849 C SER A 356 15571 17605 23561 413 -4162 -443 C ATOM 2850 O SER A 356 26.291 51.158 22.788 1.00161.50 O ANISOU 2850 O SER A 356 16851 19362 25149 381 -4031 -605 O ATOM 2851 CB SER A 356 26.240 53.844 20.933 1.00165.85 C ANISOU 2851 CB SER A 356 17705 19693 25617 1052 -4634 -237 C ATOM 2852 OG SER A 356 26.398 53.300 19.634 1.00162.30 O ANISOU 2852 OG SER A 356 17284 19387 24997 815 -4702 -151 O ATOM 2853 N LEU A 357 27.597 50.975 20.962 1.00110.54 N ANISOU 2853 N LEU A 357 10792 12670 18540 119 -4136 -385 N ATOM 2854 CA LEU A 357 27.407 49.529 20.805 1.00116.24 C ANISOU 2854 CA LEU A 357 11379 13584 19202 -257 -3969 -526 C ATOM 2855 C LEU A 357 25.929 49.155 20.703 1.00129.69 C ANISOU 2855 C LEU A 357 12671 15748 20856 -275 -4034 -687 C ATOM 2856 O LEU A 357 25.461 48.203 21.330 1.00143.23 O ANISOU 2856 O LEU A 357 14194 17614 22613 -498 -3853 -839 O ATOM 2857 CB LEU A 357 28.073 48.750 21.941 1.00118.24 C ANISOU 2857 CB LEU A 357 11726 13632 19567 -439 -3681 -587 C ATOM 2858 CG LEU A 357 29.595 48.661 21.985 1.00118.11 C ANISOU 2858 CG LEU A 357 12068 13242 19566 -535 -3565 -468 C ATOM 2859 CD1 LEU A 357 30.032 47.963 23.259 1.00122.45 C ANISOU 2859 CD1 LEU A 357 12647 13661 20217 -640 -3299 -529 C ATOM 2860 CD2 LEU A 357 30.102 47.916 20.767 1.00124.98 C ANISOU 2860 CD2 LEU A 357 13066 14123 20300 -793 -3564 -446 C ATOM 2861 N VAL A 358 25.184 49.910 19.897 1.00121.66 N ANISOU 2861 N VAL A 358 11511 14973 19740 -42 -4295 -642 N ATOM 2862 CA VAL A 358 23.791 49.565 19.633 1.00128.61 C ANISOU 2862 CA VAL A 358 11966 16363 20537 -66 -4387 -796 C ATOM 2863 C VAL A 358 23.692 48.951 18.243 1.00126.31 C ANISOU 2863 C VAL A 358 11647 16293 20053 -319 -4497 -820 C ATOM 2864 O VAL A 358 22.822 48.112 17.982 1.00122.58 O ANISOU 2864 O VAL A 358 10868 16201 19505 -564 -4488 -1003 O ATOM 2865 CB VAL A 358 22.859 50.783 19.781 1.00144.12 C ANISOU 2865 CB VAL A 358 13717 18537 22505 414 -4607 -760 C ATOM 2866 CG1 VAL A 358 22.858 51.275 21.220 1.00148.28 C ANISOU 2866 CG1 VAL A 358 14236 18898 23207 648 -4480 -801 C ATOM 2867 CG2 VAL A 358 23.278 51.899 18.836 1.00167.90 C ANISOU 2867 CG2 VAL A 358 16979 21372 25441 707 -4857 -533 C ATOM 2868 N LYS A 359 24.592 49.356 17.345 1.00125.92 N ANISOU 2868 N LYS A 359 11911 16023 19911 -282 -4598 -645 N ATOM 2869 CA LYS A 359 24.630 48.759 16.015 1.00121.70 C ANISOU 2869 CA LYS A 359 11381 15696 19165 -520 -4690 -675 C ATOM 2870 C LYS A 359 25.233 47.362 16.046 1.00127.09 C ANISOU 2870 C LYS A 359 12180 16248 19860 -973 -4445 -832 C ATOM 2871 O LYS A 359 24.816 46.489 15.276 1.00135.48 O ANISOU 2871 O LYS A 359 13108 17582 20785 -1255 -4468 -1000 O ATOM 2872 CB LYS A 359 25.423 49.654 15.062 1.00127.27 C ANISOU 2872 CB LYS A 359 12382 16230 19746 -333 -4860 -416 C ATOM 2873 CG LYS A 359 25.467 49.157 13.626 1.00132.39 C ANISOU 2873 CG LYS A 359 13031 17142 20128 -531 -4974 -434 C ATOM 2874 CD LYS A 359 26.221 50.121 12.726 1.00134.37 C ANISOU 2874 CD LYS A 359 13564 17252 20240 -332 -5136 -134 C ATOM 2875 CE LYS A 359 26.282 49.611 11.295 1.00148.46 C ANISOU 2875 CE LYS A 359 15339 19347 21721 -522 -5242 -158 C ATOM 2876 NZ LYS A 359 27.017 50.547 10.399 1.00157.73 N ANISOU 2876 NZ LYS A 359 16781 20417 22732 -344 -5387 169 N ATOM 2877 N GLU A 360 26.195 47.128 16.936 1.00115.56 N ANISOU 2877 N GLU A 360 10968 14379 18559 -1037 -4215 -791 N ATOM 2878 CA GLU A 360 26.940 45.877 16.960 1.00113.74 C ANISOU 2878 CA GLU A 360 10916 13956 18344 -1400 -3982 -899 C ATOM 2879 C GLU A 360 26.243 44.790 17.764 1.00132.90 C ANISOU 2879 C GLU A 360 13135 16476 20884 -1670 -3789 -1109 C ATOM 2880 O GLU A 360 26.365 43.608 17.425 1.00119.73 O ANISOU 2880 O GLU A 360 11520 14786 19186 -2017 -3664 -1262 O ATOM 2881 CB GLU A 360 28.345 46.126 17.512 1.00110.27 C ANISOU 2881 CB GLU A 360 10830 13067 18001 -1327 -3831 -739 C ATOM 2882 CG GLU A 360 29.159 47.041 16.618 1.00163.73 C ANISOU 2882 CG GLU A 360 17830 19732 24647 -1159 -3990 -525 C ATOM 2883 CD GLU A 360 28.831 48.511 16.835 1.00174.24 C ANISOU 2883 CD GLU A 360 19130 21047 26028 -782 -4186 -349 C ATOM 2884 OE1 GLU A 360 28.068 48.819 17.773 1.00174.13 O ANISOU 2884 OE1 GLU A 360 18924 21090 26149 -625 -4182 -412 O ATOM 2885 OE2 GLU A 360 29.310 49.358 16.052 1.00179.32 O ANISOU 2885 OE2 GLU A 360 19942 21624 26567 -640 -4344 -146 O ATOM 2886 N LYS A 361 25.523 45.158 18.827 1.00129.00 N ANISOU 2886 N LYS A 361 12418 16080 20518 -1521 -3755 -1119 N ATOM 2887 CA LYS A 361 24.649 44.190 19.478 1.00116.27 C ANISOU 2887 CA LYS A 361 10541 14657 18980 -1795 -3597 -1302 C ATOM 2888 C LYS A 361 23.546 43.734 18.536 1.00147.93 C ANISOU 2888 C LYS A 361 14239 19118 22850 -2007 -3747 -1482 C ATOM 2889 O LYS A 361 23.110 42.579 18.600 1.00157.67 O ANISOU 2889 O LYS A 361 15360 20440 24107 -2401 -3610 -1663 O ATOM 2890 CB LYS A 361 24.051 44.782 20.754 1.00116.44 C ANISOU 2890 CB LYS A 361 10346 14772 19125 -1558 -3545 -1274 C ATOM 2891 CG LYS A 361 25.053 44.985 21.876 1.00122.66 C ANISOU 2891 CG LYS A 361 11401 15156 20048 -1429 -3355 -1151 C ATOM 2892 CD LYS A 361 24.372 45.495 23.135 1.00124.34 C ANISOU 2892 CD LYS A 361 11371 15520 20352 -1208 -3297 -1164 C ATOM 2893 CE LYS A 361 25.373 45.698 24.260 1.00132.99 C ANISOU 2893 CE LYS A 361 12721 16253 21557 -1083 -3119 -1061 C ATOM 2894 NZ LYS A 361 24.719 46.191 25.502 1.00135.97 N ANISOU 2894 NZ LYS A 361 12861 16804 21995 -857 -3057 -1097 N ATOM 2895 N LYS A 362 23.089 44.624 17.653 1.00112.76 N ANISOU 2895 N LYS A 362 15391 11507 15946 -1184 -997 -1591 N ATOM 2896 CA LYS A 362 22.074 44.258 16.671 1.00108.97 C ANISOU 2896 CA LYS A 362 15181 10882 15342 -873 -1218 -1398 C ATOM 2897 C LYS A 362 22.614 43.225 15.687 1.00117.08 C ANISOU 2897 C LYS A 362 16522 12057 15906 -852 -1099 -895 C ATOM 2898 O LYS A 362 21.960 42.213 15.411 1.00117.72 O ANISOU 2898 O LYS A 362 16667 12396 15664 -716 -1170 -852 O ATOM 2899 CB LYS A 362 21.588 45.520 15.951 1.00128.49 C ANISOU 2899 CB LYS A 362 17847 12716 18256 -696 -1421 -1313 C ATOM 2900 CG LYS A 362 20.500 45.328 14.898 1.00153.71 C ANISOU 2900 CG LYS A 362 21307 15726 21371 -387 -1698 -1083 C ATOM 2901 CD LYS A 362 21.082 45.053 13.516 1.00159.97 C ANISOU 2901 CD LYS A 362 22550 16375 21855 -383 -1652 -457 C ATOM 2902 CE LYS A 362 21.974 46.201 13.062 1.00157.27 C ANISOU 2902 CE LYS A 362 22388 15549 21817 -512 -1584 -184 C ATOM 2903 NZ LYS A 362 21.219 47.474 12.905 1.00149.23 N ANISOU 2903 NZ LYS A 362 21371 13969 21361 -343 -1864 -254 N ATOM 2904 N ALA A 363 23.811 43.466 15.146 1.00120.83 N ANISOU 2904 N ALA A 363 17185 12373 16351 -1002 -898 -537 N ATOM 2905 CA ALA A 363 24.402 42.524 14.201 1.00102.08 C ANISOU 2905 CA ALA A 363 15087 10130 13569 -1011 -737 -103 C ATOM 2906 C ALA A 363 24.762 41.206 14.872 1.00110.99 C ANISOU 2906 C ALA A 363 15988 11797 14388 -1104 -560 -179 C ATOM 2907 O ALA A 363 24.678 40.145 14.239 1.00 99.80 O ANISOU 2907 O ALA A 363 14736 10551 12633 -1026 -496 31 O ATOM 2908 CB ALA A 363 25.637 43.137 13.543 1.00100.43 C ANISOU 2908 CB ALA A 363 15091 9646 13423 -1184 -541 251 C ATOM 2909 N ALA A 364 25.171 41.249 16.141 1.00 96.01 N ANISOU 2909 N ALA A 364 13706 10169 12604 -1291 -481 -467 N ATOM 2910 CA ALA A 364 25.462 40.014 16.861 1.00 93.99 C ANISOU 2910 CA ALA A 364 13201 10426 12085 -1390 -361 -508 C ATOM 2911 C ALA A 364 24.198 39.190 17.074 1.00 90.70 C ANISOU 2911 C ALA A 364 12729 10254 11478 -1223 -546 -714 C ATOM 2912 O ALA A 364 24.241 37.956 17.023 1.00109.51 O ANISOU 2912 O ALA A 364 15105 12934 13571 -1205 -467 -586 O ATOM 2913 CB ALA A 364 26.129 40.328 18.198 1.00 82.56 C ANISOU 2913 CB ALA A 364 11341 9245 10785 -1672 -274 -755 C ATOM 2914 N ARG A 365 23.066 39.855 17.314 1.00 96.67 N ANISOU 2914 N ARG A 365 13432 10877 12419 -1102 -787 -1044 N ATOM 2915 CA ARG A 365 21.799 39.141 17.437 1.00 97.04 C ANISOU 2915 CA ARG A 365 13438 11144 12288 -940 -973 -1252 C ATOM 2916 C ARG A 365 21.364 38.558 16.100 1.00100.00 C ANISOU 2916 C ARG A 365 14205 11373 12416 -719 -1019 -923 C ATOM 2917 O ARG A 365 20.776 37.472 16.053 1.00 97.26 O ANISOU 2917 O ARG A 365 13869 11309 11776 -647 -1049 -943 O ATOM 2918 CB ARG A 365 20.722 40.070 17.996 1.00 96.16 C ANISOU 2918 CB ARG A 365 13144 10905 12487 -863 -1204 -1709 C ATOM 2919 CG ARG A 365 20.939 40.472 19.443 1.00110.28 C ANISOU 2919 CG ARG A 365 14499 12953 14451 -1125 -1153 -2144 C ATOM 2920 CD ARG A 365 19.874 41.446 19.906 1.00141.46 C ANISOU 2920 CD ARG A 365 18264 16721 18762 -1043 -1345 -2640 C ATOM 2921 NE ARG A 365 18.546 40.843 19.876 1.00166.68 N ANISOU 2921 NE ARG A 365 21429 20094 21808 -851 -1544 -2844 N ATOM 2922 CZ ARG A 365 18.025 40.133 20.870 1.00176.87 C ANISOU 2922 CZ ARG A 365 22418 21893 22892 -989 -1565 -3192 C ATOM 2923 NH1 ARG A 365 18.723 39.931 21.980 1.00178.14 N ANISOU 2923 NH1 ARG A 365 22276 22447 22962 -1330 -1415 -3351 N ATOM 2924 NH2 ARG A 365 16.807 39.621 20.755 1.00176.38 N ANISOU 2924 NH2 ARG A 365 22350 21970 22696 -813 -1745 -3367 N ATOM 2925 N THR A 366 21.638 39.268 15.002 1.00104.46 N ANISOU 2925 N THR A 366 15096 11515 13079 -643 -1025 -620 N ATOM 2926 CA THR A 366 21.354 38.720 13.679 1.00 99.08 C ANISOU 2926 CA THR A 366 14796 10739 12112 -506 -1041 -281 C ATOM 2927 C THR A 366 22.156 37.447 13.433 1.00101.82 C ANISOU 2927 C THR A 366 15204 11365 12118 -608 -757 -55 C ATOM 2928 O THR A 366 21.632 36.468 12.887 1.00108.55 O ANISOU 2928 O THR A 366 16204 12375 12664 -519 -755 17 O ATOM 2929 CB THR A 366 21.656 39.764 12.602 1.00101.96 C ANISOU 2929 CB THR A 366 15483 10627 12629 -481 -1087 40 C ATOM 2930 OG1 THR A 366 20.843 40.925 12.817 1.00122.97 O ANISOU 2930 OG1 THR A 366 18070 12977 15677 -354 -1369 -161 O ATOM 2931 CG2 THR A 366 21.376 39.201 11.217 1.00 90.83 C ANISOU 2931 CG2 THR A 366 14465 9177 10870 -401 -1100 393 C ATOM 2932 N LEU A 367 23.430 37.443 13.836 1.00112.97 N ANISOU 2932 N LEU A 367 16484 12835 13606 -798 -508 46 N ATOM 2933 CA LEU A 367 24.249 36.238 13.738 1.00103.30 C ANISOU 2933 CA LEU A 367 15238 11860 12152 -886 -231 236 C ATOM 2934 C LEU A 367 23.674 35.105 14.576 1.00105.29 C ANISOU 2934 C LEU A 367 15241 12514 12250 -864 -275 26 C ATOM 2935 O LEU A 367 23.520 33.976 14.094 1.00103.22 O ANISOU 2935 O LEU A 367 15096 12386 11737 -806 -175 139 O ATOM 2936 CB LEU A 367 25.680 36.542 14.179 1.00116.07 C ANISOU 2936 CB LEU A 367 16681 13482 13938 -1094 5 354 C ATOM 2937 CG LEU A 367 26.571 35.305 14.316 1.00113.26 C ANISOU 2937 CG LEU A 367 16192 13396 13445 -1179 278 522 C ATOM 2938 CD1 LEU A 367 26.740 34.590 12.990 1.00110.78 C ANISOU 2938 CD1 LEU A 367 16216 12972 12902 -1108 469 786 C ATOM 2939 CD2 LEU A 367 27.917 35.667 14.919 1.00118.36 C ANISOU 2939 CD2 LEU A 367 16590 14093 14289 -1388 465 611 C ATOM 2940 N SER A 368 23.366 35.386 15.844 1.00100.27 N ANISOU 2940 N SER A 368 14256 12082 11758 -941 -412 -290 N ATOM 2941 CA SER A 368 22.887 34.338 16.738 1.00101.14 C ANISOU 2941 CA SER A 368 14108 12610 11711 -979 -460 -471 C ATOM 2942 C SER A 368 21.587 33.721 16.237 1.00 97.69 C ANISOU 2942 C SER A 368 13848 12223 11048 -790 -620 -571 C ATOM 2943 O SER A 368 21.336 32.532 16.465 1.00 97.80 O ANISOU 2943 O SER A 368 13794 12516 10849 -797 -580 -573 O ATOM 2944 CB SER A 368 22.706 34.900 18.149 1.00107.38 C ANISOU 2944 CB SER A 368 14503 13628 12669 -1144 -590 -828 C ATOM 2945 OG SER A 368 22.231 33.904 19.036 1.00131.30 O ANISOU 2945 OG SER A 368 17280 17091 15516 -1225 -653 -986 O ATOM 2946 N ALA A 369 20.763 34.502 15.535 1.00105.05 N ANISOU 2946 N ALA A 369 15001 12882 12032 -626 -806 -635 N ATOM 2947 CA ALA A 369 19.480 33.990 15.065 1.00103.15 C ANISOU 2947 CA ALA A 369 14905 12710 11576 -456 -984 -739 C ATOM 2948 C ALA A 369 19.652 33.021 13.900 1.00 99.48 C ANISOU 2948 C ALA A 369 14766 12222 10808 -405 -816 -430 C ATOM 2949 O ALA A 369 19.013 31.962 13.872 1.00109.52 O ANISOU 2949 O ALA A 369 16053 13729 11830 -367 -824 -500 O ATOM 2950 CB ALA A 369 18.568 35.150 14.667 1.00 96.99 C ANISOU 2950 CB ALA A 369 14227 11637 10986 -294 -1256 -867 C ATOM 2951 N ILE A 370 20.502 33.361 12.926 1.00 84.84 N ANISOU 2951 N ILE A 370 13174 10097 8965 -431 -647 -109 N ATOM 2952 CA ILE A 370 20.629 32.509 11.746 1.00 96.21 C ANISOU 2952 CA ILE A 370 14930 11520 10107 -418 -466 137 C ATOM 2953 C ILE A 370 21.349 31.207 12.083 1.00108.85 C ANISOU 2953 C ILE A 370 16397 13350 11610 -512 -175 193 C ATOM 2954 O ILE A 370 21.072 30.166 11.473 1.00120.25 O ANISOU 2954 O ILE A 370 18000 14888 12802 -489 -55 240 O ATOM 2955 CB ILE A 370 21.330 33.257 10.595 1.00 75.93 C ANISOU 2955 CB ILE A 370 12673 8625 7552 -465 -359 452 C ATOM 2956 CG1 ILE A 370 22.761 33.638 10.977 1.00114.74 C ANISOU 2956 CG1 ILE A 370 17451 13451 12695 -615 -121 580 C ATOM 2957 CG2 ILE A 370 20.532 34.487 10.199 1.00 94.43 C ANISOU 2957 CG2 ILE A 370 15156 10708 10015 -358 -683 451 C ATOM 2958 CD1 ILE A 370 23.592 34.129 9.807 1.00128.38 C ANISOU 2958 CD1 ILE A 370 19487 14914 14377 -713 59 902 C ATOM 2959 N LEU A 371 22.271 31.230 13.048 1.00 93.49 N ANISOU 2959 N LEU A 371 14149 11495 9879 -626 -62 192 N ATOM 2960 CA LEU A 371 22.924 29.993 13.467 1.00104.29 C ANISOU 2960 CA LEU A 371 15336 13071 11220 -702 170 273 C ATOM 2961 C LEU A 371 21.961 29.108 14.248 1.00103.67 C ANISOU 2961 C LEU A 371 15079 13299 11014 -675 15 55 C ATOM 2962 O LEU A 371 21.894 27.895 14.021 1.00104.32 O ANISOU 2962 O LEU A 371 15201 13482 10952 -663 159 114 O ATOM 2963 CB LEU A 371 24.166 30.301 14.307 1.00 94.28 C ANISOU 2963 CB LEU A 371 13764 11844 10215 -849 295 368 C ATOM 2964 CG LEU A 371 25.349 30.982 13.619 1.00 92.49 C ANISOU 2964 CG LEU A 371 13666 11353 10121 -917 514 606 C ATOM 2965 CD1 LEU A 371 26.435 31.310 14.632 1.00 90.83 C ANISOU 2965 CD1 LEU A 371 13098 11248 10164 -1077 587 654 C ATOM 2966 CD2 LEU A 371 25.899 30.114 12.501 1.00 93.20 C ANISOU 2966 CD2 LEU A 371 13984 11342 10085 -903 832 823 C ATOM 2967 N LEU A 372 21.204 29.701 15.175 1.00 96.95 N ANISOU 2967 N LEU A 372 14022 12592 10221 -684 -263 -219 N ATOM 2968 CA LEU A 372 20.295 28.916 16.003 1.00 99.49 C ANISOU 2968 CA LEU A 372 14150 13246 10406 -704 -415 -446 C ATOM 2969 C LEU A 372 19.145 28.344 15.178 1.00109.40 C ANISOU 2969 C LEU A 372 15675 14503 11389 -563 -494 -528 C ATOM 2970 O LEU A 372 18.681 27.227 15.439 1.00100.21 O ANISOU 2970 O LEU A 372 14457 13564 10054 -585 -481 -587 O ATOM 2971 CB LEU A 372 19.772 29.774 17.154 1.00 87.82 C ANISOU 2971 CB LEU A 372 12377 11936 9056 -781 -667 -769 C ATOM 2972 CG LEU A 372 18.885 29.072 18.182 1.00 97.70 C ANISOU 2972 CG LEU A 372 13374 13587 10160 -869 -828 -1037 C ATOM 2973 CD1 LEU A 372 19.652 27.944 18.847 1.00109.87 C ANISOU 2973 CD1 LEU A 372 14704 15374 11666 -1036 -680 -834 C ATOM 2974 CD2 LEU A 372 18.391 30.066 19.219 1.00 98.53 C ANISOU 2974 CD2 LEU A 372 13194 13840 10402 -971 -1041 -1410 C ATOM 2975 N ALA A 373 18.675 29.090 14.176 1.00 95.38 N ANISOU 2975 N ALA A 373 14188 12485 9567 -436 -587 -513 N ATOM 2976 CA ALA A 373 17.660 28.551 13.277 1.00 95.60 C ANISOU 2976 CA ALA A 373 14485 12532 9308 -330 -653 -548 C ATOM 2977 C ALA A 373 18.213 27.406 12.438 1.00102.27 C ANISOU 2977 C ALA A 373 15539 13350 9968 -370 -336 -327 C ATOM 2978 O ALA A 373 17.466 26.500 12.052 1.00119.84 O ANISOU 2978 O ALA A 373 17890 15706 11937 -347 -326 -402 O ATOM 2979 CB ALA A 373 17.116 29.658 12.374 1.00 81.05 C ANISOU 2979 CB ALA A 373 12885 10437 7472 -209 -845 -515 C ATOM 2980 N PHE A 374 19.514 27.437 12.144 1.00 88.06 N ANISOU 2980 N PHE A 374 13769 11383 8309 -442 -59 -81 N ATOM 2981 CA PHE A 374 20.150 26.335 11.430 1.00 91.66 C ANISOU 2981 CA PHE A 374 14366 11798 8663 -491 290 87 C ATOM 2982 C PHE A 374 20.272 25.099 12.313 1.00 97.76 C ANISOU 2982 C PHE A 374 14876 12778 9489 -537 389 41 C ATOM 2983 O PHE A 374 20.079 23.971 11.844 1.00 86.52 O ANISOU 2983 O PHE A 374 13568 11387 7920 -542 567 41 O ATOM 2984 CB PHE A 374 21.523 26.777 10.928 1.00 91.28 C ANISOU 2984 CB PHE A 374 14375 11519 8786 -561 559 336 C ATOM 2985 CG PHE A 374 22.313 25.687 10.269 1.00 94.19 C ANISOU 2985 CG PHE A 374 14828 11831 9130 -620 961 472 C ATOM 2986 CD1 PHE A 374 22.029 25.291 8.974 1.00 91.31 C ANISOU 2986 CD1 PHE A 374 14809 11394 8490 -645 1128 489 C ATOM 2987 CD2 PHE A 374 23.348 25.060 10.948 1.00 95.83 C ANISOU 2987 CD2 PHE A 374 14745 12061 9606 -667 1177 575 C ATOM 2988 CE1 PHE A 374 22.764 24.287 8.366 1.00 99.05 C ANISOU 2988 CE1 PHE A 374 15845 12309 9479 -717 1540 556 C ATOM 2989 CE2 PHE A 374 24.084 24.057 10.348 1.00 97.58 C ANISOU 2989 CE2 PHE A 374 15006 12189 9880 -703 1564 676 C ATOM 2990 CZ PHE A 374 23.791 23.670 9.055 1.00 97.19 C ANISOU 2990 CZ PHE A 374 15304 12052 9571 -729 1764 640 C ATOM 2991 N ILE A 375 20.592 25.291 13.593 1.00 87.46 N ANISOU 2991 N ILE A 375 13216 11621 8395 -596 273 9 N ATOM 2992 CA ILE A 375 20.781 24.157 14.489 1.00 91.73 C ANISOU 2992 CA ILE A 375 13485 12366 9004 -670 334 35 C ATOM 2993 C ILE A 375 19.458 23.452 14.757 1.00 94.30 C ANISOU 2993 C ILE A 375 13827 12919 9085 -656 151 -191 C ATOM 2994 O ILE A 375 19.382 22.218 14.734 1.00121.83 O ANISOU 2994 O ILE A 375 17311 16462 12517 -679 289 -148 O ATOM 2995 CB ILE A 375 21.455 24.618 15.795 1.00 93.96 C ANISOU 2995 CB ILE A 375 13374 12800 9527 -791 230 78 C ATOM 2996 CG1 ILE A 375 22.836 25.205 15.502 1.00100.25 C ANISOU 2996 CG1 ILE A 375 14144 13381 10566 -820 443 314 C ATOM 2997 CG2 ILE A 375 21.550 23.473 16.790 1.00 97.22 C ANISOU 2997 CG2 ILE A 375 13488 13462 9989 -897 225 144 C ATOM 2998 CD1 ILE A 375 23.786 24.230 14.840 1.00109.61 C ANISOU 2998 CD1 ILE A 375 15381 14402 11862 -803 805 562 C ATOM 2999 N LEU A 376 18.393 24.216 15.004 1.00103.66 N ANISOU 2999 N LEU A 376 15020 14224 10143 -619 -154 -446 N ATOM 3000 CA LEU A 376 17.126 23.623 15.417 1.00104.46 C ANISOU 3000 CA LEU A 376 15013 14561 10116 -581 -343 -677 C ATOM 3001 C LEU A 376 16.410 22.880 14.294 1.00 98.81 C ANISOU 3001 C LEU A 376 14428 13761 9354 -418 -244 -674 C ATOM 3002 O LEU A 376 15.490 22.108 14.584 1.00105.51 O ANISOU 3002 O LEU A 376 15080 14733 10275 -304 -323 -784 O ATOM 3003 CB LEU A 376 16.205 24.703 15.989 1.00 92.76 C ANISOU 3003 CB LEU A 376 13343 13152 8749 -481 -654 -940 C ATOM 3004 CG LEU A 376 16.691 25.387 17.269 1.00 92.83 C ANISOU 3004 CG LEU A 376 13072 13310 8891 -665 -771 -1025 C ATOM 3005 CD1 LEU A 376 15.735 26.496 17.694 1.00 96.17 C ANISOU 3005 CD1 LEU A 376 13388 13674 9476 -561 -1030 -1297 C ATOM 3006 CD2 LEU A 376 16.890 24.376 18.388 1.00 88.08 C ANISOU 3006 CD2 LEU A 376 12163 12904 8401 -796 -731 -946 C ATOM 3007 N THR A 377 16.803 23.075 13.036 1.00 84.77 N ANISOU 3007 N THR A 377 12977 11761 7469 -412 -70 -541 N ATOM 3008 CA THR A 377 16.128 22.440 11.911 1.00 88.08 C ANISOU 3008 CA THR A 377 13465 12157 7845 -338 11 -551 C ATOM 3009 C THR A 377 16.991 21.419 11.179 1.00 96.07 C ANISOU 3009 C THR A 377 14662 13009 8832 -412 374 -396 C ATOM 3010 O THR A 377 16.507 20.782 10.235 1.00 96.54 O ANISOU 3010 O THR A 377 14769 13058 8853 -394 460 -427 O ATOM 3011 CB THR A 377 15.643 23.503 10.919 1.00 92.40 C ANISOU 3011 CB THR A 377 14216 12599 8292 -286 -116 -547 C ATOM 3012 OG1 THR A 377 16.769 24.222 10.402 1.00 98.12 O ANISOU 3012 OG1 THR A 377 15288 13064 8931 -347 29 -354 O ATOM 3013 CG2 THR A 377 14.692 24.473 11.605 1.00 95.81 C ANISOU 3013 CG2 THR A 377 14448 13166 8790 -215 -450 -735 C ATOM 3014 N TRP A 378 18.245 21.242 11.588 1.00 83.14 N ANISOU 3014 N TRP A 378 13099 11260 7231 -509 612 -239 N ATOM 3015 CA TRP A 378 19.190 20.349 10.929 1.00 82.34 C ANISOU 3015 CA TRP A 378 13134 10972 7181 -568 1029 -99 C ATOM 3016 C TRP A 378 19.742 19.257 11.832 1.00 85.86 C ANISOU 3016 C TRP A 378 13414 11452 7757 -636 1210 -13 C ATOM 3017 O TRP A 378 20.059 18.173 11.335 1.00 91.10 O ANISOU 3017 O TRP A 378 14128 11985 8500 -655 1522 18 O ATOM 3018 CB TRP A 378 20.350 21.171 10.348 1.00 84.85 C ANISOU 3018 CB TRP A 378 13652 11069 7519 -608 1263 88 C ATOM 3019 CG TRP A 378 20.035 21.811 9.036 1.00 72.57 C ANISOU 3019 CG TRP A 378 12332 9415 5825 -595 1234 72 C ATOM 3020 CD1 TRP A 378 19.166 22.837 8.816 1.00 89.35 C ANISOU 3020 CD1 TRP A 378 14538 11595 7817 -541 898 11 C ATOM 3021 CD2 TRP A 378 20.699 21.578 7.787 1.00 70.66 C ANISOU 3021 CD2 TRP A 378 12261 9003 5584 -667 1557 149 C ATOM 3022 NE1 TRP A 378 19.177 23.193 7.489 1.00 89.54 N ANISOU 3022 NE1 TRP A 378 14791 11508 7722 -584 975 81 N ATOM 3023 CE2 TRP A 378 20.121 22.444 6.838 1.00 58.18 C ANISOU 3023 CE2 TRP A 378 10872 7417 3816 -677 1372 150 C ATOM 3024 CE3 TRP A 378 21.703 20.699 7.373 1.00 75.37 C ANISOU 3024 CE3 TRP A 378 12842 9456 6340 -735 1986 202 C ATOM 3025 CZ2 TRP A 378 20.512 22.458 5.501 1.00 66.68 C ANISOU 3025 CZ2 TRP A 378 12132 8394 4808 -786 1584 208 C ATOM 3026 CZ3 TRP A 378 22.091 20.714 6.044 1.00 87.10 C ANISOU 3026 CZ3 TRP A 378 14493 10829 7771 -827 2204 206 C ATOM 3027 CH2 TRP A 378 21.496 21.587 5.124 1.00 78.65 C ANISOU 3027 CH2 TRP A 378 13620 9801 6463 -869 1996 213 C ATOM 3028 N THR A 379 19.855 19.501 13.137 1.00 72.96 N ANISOU 3028 N THR A 379 11445 9983 6293 -661 975 33 N ATOM 3029 CA THR A 379 20.342 18.473 14.050 1.00 98.29 C ANISOU 3029 CA THR A 379 14348 13244 9755 -720 1045 180 C ATOM 3030 C THR A 379 19.360 17.310 14.215 1.00107.75 C ANISOU 3030 C THR A 379 15585 14572 10783 -758 1006 45 C ATOM 3031 O THR A 379 19.816 16.170 14.370 1.00119.17 O ANISOU 3031 O THR A 379 16917 15914 12449 -784 1210 186 O ATOM 3032 CB THR A 379 20.692 19.070 15.422 1.00102.93 C ANISOU 3032 CB THR A 379 14560 14038 10509 -798 782 272 C ATOM 3033 OG1 THR A 379 19.521 19.610 16.046 1.00123.98 O ANISOU 3033 OG1 THR A 379 17196 16991 12919 -840 422 19 O ATOM 3034 CG2 THR A 379 21.734 20.172 15.274 1.00100.79 C ANISOU 3034 CG2 THR A 379 14240 13627 10428 -781 849 406 C ATOM 3035 N PRO A 380 18.009 17.523 14.199 1.00109.99 N ANISOU 3035 N PRO A 380 15925 15046 10822 -717 720 -214 N ATOM 3036 CA PRO A 380 17.103 16.363 14.263 1.00104.76 C ANISOU 3036 CA PRO A 380 15180 14447 10177 -687 672 -320 C ATOM 3037 C PRO A 380 17.398 15.295 13.220 1.00 89.87 C ANISOU 3037 C PRO A 380 13502 12330 8317 -699 1040 -294 C ATOM 3038 O PRO A 380 17.595 14.131 13.573 1.00 80.13 O ANISOU 3038 O PRO A 380 12260 11052 7132 -799 1225 -223 O ATOM 3039 CB PRO A 380 15.718 16.987 14.044 1.00100.91 C ANISOU 3039 CB PRO A 380 14583 14065 9692 -483 351 -537 C ATOM 3040 CG PRO A 380 15.854 18.349 14.571 1.00 94.31 C ANISOU 3040 CG PRO A 380 13673 13293 8868 -458 150 -561 C ATOM 3041 CD PRO A 380 17.241 18.787 14.220 1.00100.14 C ANISOU 3041 CD PRO A 380 14604 13894 9550 -593 393 -379 C ATOM 3042 N TYR A 381 17.428 15.668 11.939 1.00 84.56 N ANISOU 3042 N TYR A 381 13002 11505 7623 -627 1158 -351 N ATOM 3043 CA TYR A 381 17.795 14.705 10.905 1.00 72.09 C ANISOU 3043 CA TYR A 381 11592 9695 6102 -665 1529 -364 C ATOM 3044 C TYR A 381 19.180 14.122 11.155 1.00 92.86 C ANISOU 3044 C TYR A 381 14272 12087 8923 -734 1982 -169 C ATOM 3045 O TYR A 381 19.417 12.935 10.909 1.00104.22 O ANISOU 3045 O TYR A 381 15744 13346 10509 -772 2307 -176 O ATOM 3046 CB TYR A 381 17.735 15.364 9.529 1.00 75.09 C ANISOU 3046 CB TYR A 381 12127 9995 6407 -634 1562 -421 C ATOM 3047 CG TYR A 381 18.205 14.481 8.391 1.00 87.79 C ANISOU 3047 CG TYR A 381 13896 11382 8079 -707 1951 -466 C ATOM 3048 CD1 TYR A 381 17.415 13.444 7.909 1.00 87.73 C ANISOU 3048 CD1 TYR A 381 13884 11399 8050 -742 1968 -613 C ATOM 3049 CD2 TYR A 381 19.439 14.695 7.791 1.00 84.19 C ANISOU 3049 CD2 TYR A 381 13569 10696 7724 -750 2311 -376 C ATOM 3050 CE1 TYR A 381 17.847 12.642 6.863 1.00 73.51 C ANISOU 3050 CE1 TYR A 381 12222 9394 6314 -836 2332 -691 C ATOM 3051 CE2 TYR A 381 19.877 13.902 6.749 1.00 91.99 C ANISOU 3051 CE2 TYR A 381 14664 11487 8802 -832 2678 -463 C ATOM 3052 CZ TYR A 381 19.079 12.876 6.287 1.00 91.77 C ANISOU 3052 CZ TYR A 381 14648 11482 8737 -883 2687 -631 C ATOM 3053 OH TYR A 381 19.516 12.088 5.246 1.00 86.04 O ANISOU 3053 OH TYR A 381 14026 10562 8104 -992 3061 -749 O ATOM 3054 N ASN A 382 20.105 14.942 11.650 1.00105.45 N ANISOU 3054 N ASN A 382 15781 13655 10631 -726 2006 31 N ATOM 3055 CA ASN A 382 21.480 14.494 11.833 1.00 95.64 C ANISOU 3055 CA ASN A 382 14292 12167 9882 -698 2291 279 C ATOM 3056 C ASN A 382 21.660 13.632 13.077 1.00 96.89 C ANISOU 3056 C ASN A 382 14084 12372 10357 -717 2173 474 C ATOM 3057 O ASN A 382 22.523 12.747 13.083 1.00 86.01 O ANISOU 3057 O ASN A 382 12530 10743 9407 -689 2456 648 O ATOM 3058 CB ASN A 382 22.406 15.707 11.857 1.00 82.80 C ANISOU 3058 CB ASN A 382 12578 10504 8378 -667 2259 431 C ATOM 3059 CG ASN A 382 22.668 16.250 10.467 1.00 95.71 C ANISOU 3059 CG ASN A 382 14544 11983 9840 -674 2523 334 C ATOM 3060 OD1 ASN A 382 23.090 15.514 9.575 1.00 86.85 O ANISOU 3060 OD1 ASN A 382 13540 10649 8809 -698 2933 280 O ATOM 3061 ND2 ASN A 382 22.346 17.519 10.255 1.00115.31 N ANISOU 3061 ND2 ASN A 382 17181 14572 12060 -675 2288 294 N ATOM 3062 N ILE A 383 20.881 13.863 14.138 1.00 75.02 N ANISOU 3062 N ILE A 383 11178 9919 7408 -780 1762 458 N ATOM 3063 CA ILE A 383 20.918 12.921 15.251 1.00 92.23 C ANISOU 3063 CA ILE A 383 13047 12177 9820 -852 1641 651 C ATOM 3064 C ILE A 383 20.194 11.629 14.893 1.00 97.55 C ANISOU 3064 C ILE A 383 13877 12754 10436 -882 1793 522 C ATOM 3065 O ILE A 383 20.402 10.605 15.552 1.00103.57 O ANISOU 3065 O ILE A 383 14415 13446 11492 -929 1805 725 O ATOM 3066 CB ILE A 383 20.336 13.537 16.539 1.00 88.73 C ANISOU 3066 CB ILE A 383 12388 12147 9180 -971 1174 655 C ATOM 3067 CG1 ILE A 383 18.849 13.850 16.379 1.00127.40 C ANISOU 3067 CG1 ILE A 383 17532 17300 13576 -1009 948 294 C ATOM 3068 CG2 ILE A 383 21.104 14.790 16.919 1.00 76.84 C ANISOU 3068 CG2 ILE A 383 10712 10718 7765 -966 1054 764 C ATOM 3069 CD1 ILE A 383 18.167 14.248 17.671 1.00140.76 C ANISOU 3069 CD1 ILE A 383 18990 19411 15081 -1159 529 232 C ATOM 3070 N MET A 384 19.351 11.650 13.857 1.00 94.62 N ANISOU 3070 N MET A 384 13881 12376 9696 -873 1903 204 N ATOM 3071 CA MET A 384 18.701 10.428 13.394 1.00 99.94 C ANISOU 3071 CA MET A 384 14726 12944 10303 -923 2100 43 C ATOM 3072 C MET A 384 19.644 9.593 12.540 1.00104.68 C ANISOU 3072 C MET A 384 15361 13112 11302 -869 2613 94 C ATOM 3073 O MET A 384 19.748 8.377 12.727 1.00107.77 O ANISOU 3073 O MET A 384 15649 13299 11998 -892 2788 163 O ATOM 3074 CB MET A 384 17.435 10.761 12.606 1.00 93.01 C ANISOU 3074 CB MET A 384 14128 12250 8961 -928 1949 -307 C ATOM 3075 CG MET A 384 16.326 11.360 13.437 1.00 97.11 C ANISOU 3075 CG MET A 384 14447 13137 9315 -902 1397 -391 C ATOM 3076 SD MET A 384 14.897 11.777 12.426 1.00100.84 S ANISOU 3076 SD MET A 384 14874 13720 9722 -714 1106 -640 S ATOM 3077 CE MET A 384 13.901 12.652 13.630 1.00104.61 C ANISOU 3077 CE MET A 384 15066 14485 10196 -578 616 -680 C ATOM 3078 N VAL A 385 20.337 10.230 11.593 1.00 85.77 N ANISOU 3078 N VAL A 385 13103 10563 8925 -810 2868 48 N ATOM 3079 CA VAL A 385 21.307 9.495 10.788 1.00 94.57 C ANISOU 3079 CA VAL A 385 14212 11279 10440 -775 3389 56 C ATOM 3080 C VAL A 385 22.441 8.984 11.668 1.00116.09 C ANISOU 3080 C VAL A 385 16503 13787 13819 -694 3440 418 C ATOM 3081 O VAL A 385 23.077 7.971 11.351 1.00128.98 O ANISOU 3081 O VAL A 385 18030 15060 15917 -656 3824 451 O ATOM 3082 CB VAL A 385 21.825 10.371 9.631 1.00 72.35 C ANISOU 3082 CB VAL A 385 11624 8401 7466 -773 3632 -62 C ATOM 3083 CG1 VAL A 385 22.616 11.547 10.159 1.00115.70 C ANISOU 3083 CG1 VAL A 385 16917 13971 13073 -704 3421 185 C ATOM 3084 CG2 VAL A 385 22.676 9.552 8.688 1.00 92.72 C ANISOU 3084 CG2 VAL A 385 14226 10607 10396 -783 4217 -156 C ATOM 3085 N LEU A 386 22.698 9.656 12.791 1.00104.48 N ANISOU 3085 N LEU A 386 14756 12534 12410 -679 3054 691 N ATOM 3086 CA LEU A 386 23.686 9.165 13.743 1.00110.20 C ANISOU 3086 CA LEU A 386 15036 13122 13714 -635 3024 1085 C ATOM 3087 C LEU A 386 23.222 7.863 14.387 1.00108.80 C ANISOU 3087 C LEU A 386 14725 12872 13744 -684 2959 1197 C ATOM 3088 O LEU A 386 23.904 6.835 14.303 1.00111.17 O ANISOU 3088 O LEU A 386 14842 12798 14599 -619 3248 1353 O ATOM 3089 CB LEU A 386 23.959 10.233 14.804 1.00103.56 C ANISOU 3089 CB LEU A 386 13946 12603 12798 -669 2605 1318 C ATOM 3090 CG LEU A 386 25.019 9.908 15.857 1.00118.82 C ANISOU 3090 CG LEU A 386 15389 14485 15271 -660 2509 1772 C ATOM 3091 CD1 LEU A 386 26.367 9.689 15.197 1.00122.26 C ANISOU 3091 CD1 LEU A 386 15684 14527 16243 -526 2938 1897 C ATOM 3092 CD2 LEU A 386 25.103 11.020 16.891 1.00122.14 C ANISOU 3092 CD2 LEU A 386 15605 15304 15499 -758 2085 1923 C ATOM 3093 N VAL A 387 22.049 7.886 15.025 1.00 97.21 N ANISOU 3093 N VAL A 387 13337 11745 11851 -806 2587 1113 N ATOM 3094 CA VAL A 387 21.561 6.693 15.711 1.00107.15 C ANISOU 3094 CA VAL A 387 14475 12974 13264 -894 2485 1242 C ATOM 3095 C VAL A 387 21.176 5.609 14.713 1.00109.17 C ANISOU 3095 C VAL A 387 14992 12895 13594 -880 2894 975 C ATOM 3096 O VAL A 387 21.215 4.418 15.039 1.00112.46 O ANISOU 3096 O VAL A 387 15271 13069 14390 -903 2983 1128 O ATOM 3097 CB VAL A 387 20.384 7.047 16.639 1.00104.78 C ANISOU 3097 CB VAL A 387 14192 13171 12451 -1064 1995 1177 C ATOM 3098 CG1 VAL A 387 20.818 8.071 17.680 1.00102.44 C ANISOU 3098 CG1 VAL A 387 13601 13204 12116 -1117 1625 1415 C ATOM 3099 CG2 VAL A 387 19.198 7.556 15.838 1.00115.94 C ANISOU 3099 CG2 VAL A 387 16019 14784 13248 -1090 1980 709 C ATOM 3100 N SER A 388 20.807 5.989 13.486 1.00112.61 N ANISOU 3100 N SER A 388 15800 13309 13676 -864 3148 581 N ATOM 3101 CA SER A 388 20.501 4.986 12.471 1.00106.48 C ANISOU 3101 CA SER A 388 15271 12236 12950 -892 3582 287 C ATOM 3102 C SER A 388 21.732 4.177 12.089 1.00116.43 C ANISOU 3102 C SER A 388 16329 12971 14940 -782 4054 415 C ATOM 3103 O SER A 388 21.608 3.016 11.684 1.00123.45 O ANISOU 3103 O SER A 388 17270 13535 16099 -809 4383 278 O ATOM 3104 CB SER A 388 19.912 5.650 11.228 1.00 98.06 C ANISOU 3104 CB SER A 388 14627 11313 11317 -940 3736 -131 C ATOM 3105 OG SER A 388 19.678 4.699 10.204 1.00111.44 O ANISOU 3105 OG SER A 388 16553 12750 13037 -1011 4190 -442 O ATOM 3106 N THR A 389 22.920 4.772 12.200 1.00116.84 N ANISOU 3106 N THR A 389 16135 12922 15337 -662 4108 653 N ATOM 3107 CA THR A 389 24.140 4.060 11.837 1.00113.30 C ANISOU 3107 CA THR A 389 15447 11977 15624 -542 4562 762 C ATOM 3108 C THR A 389 24.475 2.983 12.863 1.00126.80 C ANISOU 3108 C THR A 389 16767 13440 17970 -493 4453 1161 C ATOM 3109 O THR A 389 24.953 1.901 12.503 1.00107.66 O ANISOU 3109 O THR A 389 14225 10536 16146 -425 4852 1145 O ATOM 3110 CB THR A 389 25.296 5.051 11.696 1.00115.29 C ANISOU 3110 CB THR A 389 15532 12232 16038 -444 4626 909 C ATOM 3111 OG1 THR A 389 24.963 6.036 10.708 1.00107.23 O ANISOU 3111 OG1 THR A 389 14892 11422 14430 -511 4717 571 O ATOM 3112 CG2 THR A 389 26.568 4.331 11.274 1.00107.45 C ANISOU 3112 CG2 THR A 389 14266 10733 15827 -316 5122 983 C ATOM 3113 N PHE A 390 24.219 3.256 14.142 1.00135.22 N ANISOU 3113 N PHE A 390 17623 14828 18927 -547 3916 1519 N ATOM 3114 CA PHE A 390 24.534 2.313 15.211 1.00129.50 C ANISOU 3114 CA PHE A 390 16510 13932 18762 -542 3733 1981 C ATOM 3115 C PHE A 390 23.341 1.410 15.519 1.00123.51 C ANISOU 3115 C PHE A 390 15918 13221 17791 -693 3592 1894 C ATOM 3116 O PHE A 390 23.433 0.185 15.402 1.00130.08 O ANISOU 3116 O PHE A 390 16675 13618 19130 -667 3840 1948 O ATOM 3117 CB PHE A 390 24.975 3.077 16.465 1.00134.09 C ANISOU 3117 CB PHE A 390 16744 14879 19326 -580 3231 2440 C ATOM 3118 CG PHE A 390 26.270 3.825 16.299 1.00149.56 C ANISOU 3118 CG PHE A 390 18468 16758 21602 -442 3363 2598 C ATOM 3119 CD1 PHE A 390 27.136 3.524 15.259 1.00151.35 C ANISOU 3119 CD1 PHE A 390 18686 16524 22294 -278 3906 2443 C ATOM 3120 CD2 PHE A 390 26.611 4.842 17.175 1.00154.52 C ANISOU 3120 CD2 PHE A 390 18878 17789 22045 -503 2964 2867 C ATOM 3121 CE1 PHE A 390 28.324 4.215 15.104 1.00154.13 C ANISOU 3121 CE1 PHE A 390 18816 16824 22924 -170 4034 2576 C ATOM 3122 CE2 PHE A 390 27.796 5.538 17.025 1.00158.70 C ANISOU 3122 CE2 PHE A 390 19192 18257 22849 -397 3087 3005 C ATOM 3123 CZ PHE A 390 28.653 5.225 15.988 1.00158.57 C ANISOU 3123 CZ PHE A 390 19169 17785 23295 -226 3616 2869 C ATOM 3124 N CYS A 391 22.219 2.006 15.910 1.00170.46 N ANISOU 3124 N CYS A 391 16329 16518 31919 1581 -593 4961 N ATOM 3125 CA CYS A 391 21.002 1.241 16.142 1.00160.70 C ANISOU 3125 CA CYS A 391 15735 15268 30054 1207 -901 4940 C ATOM 3126 C CYS A 391 20.455 0.716 14.820 1.00163.85 C ANISOU 3126 C CYS A 391 16854 15102 30300 1393 -163 4269 C ATOM 3127 O CYS A 391 20.397 1.440 13.823 1.00164.80 O ANISOU 3127 O CYS A 391 17203 15338 30074 1514 468 3659 O ATOM 3128 CB CYS A 391 19.962 2.113 16.844 1.00174.25 C ANISOU 3128 CB CYS A 391 17660 17975 30572 600 -1385 4882 C ATOM 3129 SG CYS A 391 18.405 1.296 17.233 1.00194.40 S ANISOU 3129 SG CYS A 391 20885 20691 32287 56 -1793 4937 S ATOM 3130 N LYS A 392 20.057 -0.556 14.813 1.00185.12 N ANISOU 3130 N LYS A 392 19939 17162 33235 1369 -277 4401 N ATOM 3131 CA LYS A 392 19.611 -1.207 13.586 1.00193.61 C ANISOU 3131 CA LYS A 392 21760 17575 34227 1512 380 3784 C ATOM 3132 C LYS A 392 18.378 -0.524 13.005 1.00182.79 C ANISOU 3132 C LYS A 392 21026 16808 31616 1068 511 3222 C ATOM 3133 O LYS A 392 18.432 0.051 11.912 1.00167.60 O ANISOU 3133 O LYS A 392 19368 14879 29435 1222 1180 2620 O ATOM 3134 CB LYS A 392 19.319 -2.685 13.850 1.00195.93 C ANISOU 3134 CB LYS A 392 22387 17096 34959 1462 79 4095 C ATOM 3135 N ASP A 393 17.262 -0.575 13.735 1.00183.77 N ANISOU 3135 N ASP A 393 21365 17477 30983 503 -127 3458 N ATOM 3136 CA ASP A 393 16.020 0.055 13.284 1.00167.81 C ANISOU 3136 CA ASP A 393 19844 16060 27855 71 -82 3030 C ATOM 3137 C ASP A 393 15.222 0.440 14.531 1.00171.08 C ANISOU 3137 C ASP A 393 20032 17351 27621 -437 -819 3465 C ATOM 3138 O ASP A 393 14.426 -0.349 15.042 1.00183.75 O ANISOU 3138 O ASP A 393 21881 18961 28976 -826 -1266 3772 O ATOM 3139 CB ASP A 393 15.229 -0.872 12.372 1.00167.20 C ANISOU 3139 CB ASP A 393 20588 15407 27531 -102 153 2675 C ATOM 3140 N CYS A 394 15.449 1.663 15.008 1.00164.09 N ANISOU 3140 N CYS A 394 18697 17193 26456 -447 -914 3474 N ATOM 3141 CA CYS A 394 14.696 2.192 16.135 1.00166.91 C ANISOU 3141 CA CYS A 394 18878 18430 26109 -909 -1481 3758 C ATOM 3142 C CYS A 394 14.307 3.653 15.967 1.00146.23 C ANISOU 3142 C CYS A 394 16189 16548 22825 -976 -1302 3353 C ATOM 3143 O CYS A 394 13.720 4.225 16.891 1.00158.68 O ANISOU 3143 O CYS A 394 17612 18864 23816 -1309 -1676 3502 O ATOM 3144 CB CYS A 394 15.487 2.014 17.440 1.00190.95 C ANISOU 3144 CB CYS A 394 21369 21596 29589 -944 -2044 4417 C ATOM 3145 SG CYS A 394 17.092 2.830 17.458 1.00202.06 S ANISOU 3145 SG CYS A 394 22120 22901 31752 -475 -1872 4467 S ATOM 3146 N VAL A 395 14.615 4.271 14.834 1.00106.86 N ANISOU 3146 N VAL A 395 11322 11368 17913 -680 -733 2854 N ATOM 3147 CA VAL A 395 14.093 5.587 14.476 1.00113.86 C ANISOU 3147 CA VAL A 395 12244 12840 18178 -757 -550 2456 C ATOM 3148 C VAL A 395 12.985 5.389 13.447 1.00106.36 C ANISOU 3148 C VAL A 395 11879 11822 16711 -940 -302 2095 C ATOM 3149 O VAL A 395 13.250 4.845 12.364 1.00114.17 O ANISOU 3149 O VAL A 395 13235 12189 17956 -769 119 1839 O ATOM 3150 CB VAL A 395 15.201 6.516 13.955 1.00119.41 C ANISOU 3150 CB VAL A 395 12650 13437 19283 -382 -159 2231 C ATOM 3151 CG1 VAL A 395 16.054 5.819 12.908 1.00132.61 C ANISOU 3151 CG1 VAL A 395 14456 14301 21629 1 383 2076 C ATOM 3152 CG2 VAL A 395 14.585 7.783 13.371 1.00 93.08 C ANISOU 3152 CG2 VAL A 395 9457 10564 15344 -462 57 1806 C ATOM 3153 N PRO A 396 11.745 5.774 13.746 1.00 99.28 N ANISOU 3153 N PRO A 396 11086 11537 15100 -1304 -546 2080 N ATOM 3154 CA PRO A 396 10.633 5.465 12.842 1.00 81.23 C ANISOU 3154 CA PRO A 396 9315 9196 12352 -1559 -434 1860 C ATOM 3155 C PRO A 396 10.775 6.156 11.494 1.00 90.56 C ANISOU 3155 C PRO A 396 10759 10200 13449 -1388 58 1391 C ATOM 3156 O PRO A 396 11.535 7.113 11.325 1.00117.32 O ANISOU 3156 O PRO A 396 13883 13671 17022 -1107 299 1225 O ATOM 3157 CB PRO A 396 9.405 5.982 13.601 1.00 88.60 C ANISOU 3157 CB PRO A 396 10090 10939 12635 -1919 -784 1999 C ATOM 3158 CG PRO A 396 9.831 6.005 15.038 1.00 91.11 C ANISOU 3158 CG PRO A 396 9963 11590 13065 -1943 -1136 2366 C ATOM 3159 CD PRO A 396 11.281 6.378 15.006 1.00104.51 C ANISOU 3159 CD PRO A 396 11396 12954 15359 -1535 -957 2311 C ATOM 3160 N GLU A 397 10.022 5.644 10.517 1.00 94.84 N ANISOU 3160 N GLU A 397 11859 10498 13679 -1624 172 1207 N ATOM 3161 CA GLU A 397 10.011 6.256 9.193 1.00112.76 C ANISOU 3161 CA GLU A 397 14466 12648 15730 -1582 584 801 C ATOM 3162 C GLU A 397 9.382 7.644 9.219 1.00115.04 C ANISOU 3162 C GLU A 397 14495 13624 15589 -1655 485 741 C ATOM 3163 O GLU A 397 9.809 8.530 8.470 1.00113.66 O ANISOU 3163 O GLU A 397 14336 13438 15413 -1488 803 491 O ATOM 3164 CB GLU A 397 9.268 5.357 8.205 1.00109.14 C ANISOU 3164 CB GLU A 397 14721 11801 14946 -1926 633 652 C ATOM 3165 CG GLU A 397 9.231 5.897 6.786 1.00129.32 C ANISOU 3165 CG GLU A 397 17726 14231 17181 -1980 1029 259 C ATOM 3166 CD GLU A 397 8.502 4.977 5.830 1.00153.54 C ANISOU 3166 CD GLU A 397 21576 16907 19855 -2407 1024 107 C ATOM 3167 OE1 GLU A 397 8.022 3.912 6.273 1.00161.80 O ANISOU 3167 OE1 GLU A 397 22803 17746 20928 -2648 709 307 O ATOM 3168 OE2 GLU A 397 8.404 5.326 4.635 1.00157.94 O ANISOU 3168 OE2 GLU A 397 22598 17364 20046 -2554 1304 -195 O ATOM 3169 N THR A 398 8.372 7.851 10.069 1.00105.36 N ANISOU 3169 N THR A 398 13022 12983 14027 -1897 72 977 N ATOM 3170 CA THR A 398 7.724 9.156 10.148 1.00102.41 C ANISOU 3170 CA THR A 398 12374 13210 13325 -1914 3 912 C ATOM 3171 C THR A 398 8.690 10.235 10.619 1.00110.34 C ANISOU 3171 C THR A 398 12956 14352 14616 -1556 136 809 C ATOM 3172 O THR A 398 8.587 11.391 10.190 1.00105.50 O ANISOU 3172 O THR A 398 12256 13939 13891 -1464 252 632 O ATOM 3173 CB THR A 398 6.514 9.088 11.081 1.00100.35 C ANISOU 3173 CB THR A 398 11872 13543 12713 -2200 -384 1181 C ATOM 3174 OG1 THR A 398 6.946 8.750 12.405 1.00109.56 O ANISOU 3174 OG1 THR A 398 12714 14865 14051 -2149 -573 1410 O ATOM 3175 CG2 THR A 398 5.525 8.038 10.595 1.00 86.04 C ANISOU 3175 CG2 THR A 398 10454 11609 10628 -2624 -572 1336 C ATOM 3176 N LEU A 399 9.638 9.882 11.490 1.00 89.74 N ANISOU 3176 N LEU A 399 10084 11616 12398 -1384 76 958 N ATOM 3177 CA LEU A 399 10.585 10.874 11.988 1.00 76.51 C ANISOU 3177 CA LEU A 399 8009 10068 10993 -1118 129 902 C ATOM 3178 C LEU A 399 11.628 11.231 10.936 1.00 90.50 C ANISOU 3178 C LEU A 399 9864 11395 13126 -854 556 683 C ATOM 3179 O LEU A 399 12.041 12.394 10.840 1.00 96.65 O ANISOU 3179 O LEU A 399 10435 12325 13964 -717 654 550 O ATOM 3180 CB LEU A 399 11.251 10.374 13.270 1.00 92.04 C ANISOU 3180 CB LEU A 399 9651 12076 13245 -1095 -154 1208 C ATOM 3181 CG LEU A 399 10.489 10.592 14.582 1.00101.29 C ANISOU 3181 CG LEU A 399 10599 13879 14006 -1336 -542 1386 C ATOM 3182 CD1 LEU A 399 9.290 9.666 14.701 1.00119.13 C ANISOU 3182 CD1 LEU A 399 13074 16293 15898 -1660 -722 1568 C ATOM 3183 CD2 LEU A 399 11.419 10.424 15.776 1.00111.45 C ANISOU 3183 CD2 LEU A 399 11559 15222 15563 -1324 -827 1672 C ATOM 3184 N TRP A 400 12.078 10.250 10.148 1.00 89.70 N ANISOU 3184 N TRP A 400 10077 10730 13274 -788 842 636 N ATOM 3185 CA TRP A 400 12.969 10.551 9.029 1.00103.34 C ANISOU 3185 CA TRP A 400 11932 12069 15262 -569 1354 396 C ATOM 3186 C TRP A 400 12.348 11.573 8.089 1.00107.72 C ANISOU 3186 C TRP A 400 12719 12853 15358 -705 1484 166 C ATOM 3187 O TRP A 400 13.009 12.529 7.669 1.00115.35 O ANISOU 3187 O TRP A 400 13532 13831 16465 -556 1720 55 O ATOM 3188 CB TRP A 400 13.318 9.276 8.262 1.00 75.27 C ANISOU 3188 CB TRP A 400 8798 7866 11935 -512 1703 299 C ATOM 3189 CG TRP A 400 14.441 8.488 8.836 1.00112.78 C ANISOU 3189 CG TRP A 400 13238 12200 17414 -211 1775 498 C ATOM 3190 CD1 TRP A 400 14.359 7.459 9.727 1.00136.63 C ANISOU 3190 CD1 TRP A 400 16171 15072 20672 -248 1427 804 C ATOM 3191 CD2 TRP A 400 15.829 8.630 8.514 1.00115.69 C ANISOU 3191 CD2 TRP A 400 13307 12221 18429 170 2223 460 C ATOM 3192 NE1 TRP A 400 15.613 6.968 9.997 1.00133.89 N ANISOU 3192 NE1 TRP A 400 15473 14283 21118 107 1590 979 N ATOM 3193 CE2 TRP A 400 16.533 7.671 9.264 1.00135.84 C ANISOU 3193 CE2 TRP A 400 15555 14411 21647 381 2098 768 C ATOM 3194 CE3 TRP A 400 16.544 9.483 7.670 1.00104.04 C ANISOU 3194 CE3 TRP A 400 11754 10719 17058 334 2709 243 C ATOM 3195 CZ2 TRP A 400 17.918 7.542 9.198 1.00133.62 C ANISOU 3195 CZ2 TRP A 400 14841 13743 22185 788 2449 869 C ATOM 3196 CZ3 TRP A 400 17.918 9.353 7.605 1.00113.13 C ANISOU 3196 CZ3 TRP A 400 12491 11520 18972 711 3094 324 C ATOM 3197 CH2 TRP A 400 18.591 8.391 8.365 1.00114.37 C ANISOU 3197 CH2 TRP A 400 12297 11320 19838 952 2967 636 C ATOM 3198 N GLU A 401 11.073 11.385 7.744 1.00 98.25 N ANISOU 3198 N GLU A 401 11864 11832 13632 -1018 1293 148 N ATOM 3199 CA GLU A 401 10.425 12.304 6.816 1.00 91.21 C ANISOU 3199 CA GLU A 401 11182 11137 12336 -1177 1344 14 C ATOM 3200 C GLU A 401 10.283 13.693 7.424 1.00 90.04 C ANISOU 3200 C GLU A 401 10576 11441 12192 -1069 1142 53 C ATOM 3201 O GLU A 401 10.438 14.697 6.723 1.00 98.15 O ANISOU 3201 O GLU A 401 11626 12491 13176 -1037 1286 -49 O ATOM 3202 CB GLU A 401 9.065 11.757 6.394 1.00 87.86 C ANISOU 3202 CB GLU A 401 11153 10825 11405 -1570 1098 72 C ATOM 3203 CG GLU A 401 9.145 10.472 5.589 1.00 98.56 C ANISOU 3203 CG GLU A 401 13115 11660 12675 -1749 1308 -41 C ATOM 3204 CD GLU A 401 9.870 10.654 4.267 1.00111.04 C ANISOU 3204 CD GLU A 401 15113 12864 14212 -1714 1826 -328 C ATOM 3205 OE1 GLU A 401 9.830 11.768 3.706 1.00127.34 O ANISOU 3205 OE1 GLU A 401 17130 15154 16100 -1739 1887 -369 O ATOM 3206 OE2 GLU A 401 10.470 9.675 3.780 1.00116.88 O ANISOU 3206 OE2 GLU A 401 16247 13068 15093 -1669 2192 -512 O ATOM 3207 N LEU A 402 10.000 13.770 8.725 1.00 81.84 N ANISOU 3207 N LEU A 402 9159 10745 11193 -1032 818 194 N ATOM 3208 CA LEU A 402 9.946 15.064 9.398 1.00 80.00 C ANISOU 3208 CA LEU A 402 8540 10876 10980 -911 668 160 C ATOM 3209 C LEU A 402 11.324 15.714 9.464 1.00 89.66 C ANISOU 3209 C LEU A 402 9534 11902 12629 -673 850 91 C ATOM 3210 O LEU A 402 11.482 16.889 9.114 1.00104.40 O ANISOU 3210 O LEU A 402 11320 13815 14531 -605 910 -15 O ATOM 3211 CB LEU A 402 9.356 14.900 10.797 1.00 72.01 C ANISOU 3211 CB LEU A 402 7246 10281 9832 -973 340 290 C ATOM 3212 CG LEU A 402 7.859 14.604 10.830 1.00 87.23 C ANISOU 3212 CG LEU A 402 9255 12543 11346 -1212 150 387 C ATOM 3213 CD1 LEU A 402 7.425 14.218 12.230 1.00 96.55 C ANISOU 3213 CD1 LEU A 402 10177 14127 12382 -1306 -95 542 C ATOM 3214 CD2 LEU A 402 7.090 15.824 10.348 1.00 83.92 C ANISOU 3214 CD2 LEU A 402 8760 12343 10782 -1176 148 281 C ATOM 3215 N GLY A 403 12.335 14.965 9.912 1.00 83.16 N ANISOU 3215 N GLY A 403 8573 10843 12183 -559 910 199 N ATOM 3216 CA GLY A 403 13.667 15.536 10.034 1.00 86.89 C ANISOU 3216 CA GLY A 403 8738 11157 13121 -363 1041 209 C ATOM 3217 C GLY A 403 14.239 15.983 8.702 1.00 97.36 C ANISOU 3217 C GLY A 403 10230 12193 14570 -289 1477 71 C ATOM 3218 O GLY A 403 14.811 17.070 8.594 1.00107.00 O ANISOU 3218 O GLY A 403 11247 13452 15957 -228 1524 37 O ATOM 3219 N TYR A 404 14.099 15.143 7.673 1.00 99.56 N ANISOU 3219 N TYR A 404 10917 12175 14738 -337 1804 -12 N ATOM 3220 CA TYR A 404 14.509 15.526 6.326 1.00101.22 C ANISOU 3220 CA TYR A 404 11386 12162 14912 -345 2259 -162 C ATOM 3221 C TYR A 404 13.767 16.778 5.876 1.00106.00 C ANISOU 3221 C TYR A 404 12087 13043 15146 -509 2100 -211 C ATOM 3222 O TYR A 404 14.357 17.687 5.280 1.00108.00 O ANISOU 3222 O TYR A 404 12281 13248 15507 -489 2301 -235 O ATOM 3223 CB TYR A 404 14.227 14.371 5.366 1.00 82.55 C ANISOU 3223 CB TYR A 404 9577 9467 12323 -456 2582 -295 C ATOM 3224 CG TYR A 404 14.842 14.482 3.991 1.00 77.67 C ANISOU 3224 CG TYR A 404 9289 8569 11655 -473 3173 -480 C ATOM 3225 CD1 TYR A 404 16.111 13.981 3.736 1.00 70.33 C ANISOU 3225 CD1 TYR A 404 8226 7265 11232 -209 3708 -536 C ATOM 3226 CD2 TYR A 404 14.165 15.107 2.954 1.00 88.64 C ANISOU 3226 CD2 TYR A 404 11094 10084 12500 -765 3207 -566 C ATOM 3227 CE1 TYR A 404 16.673 14.069 2.478 1.00 84.93 C ANISOU 3227 CE1 TYR A 404 10386 8894 12988 -238 4339 -730 C ATOM 3228 CE2 TYR A 404 14.724 15.210 1.694 1.00 86.77 C ANISOU 3228 CE2 TYR A 404 11210 9637 12121 -850 3761 -724 C ATOM 3229 CZ TYR A 404 15.978 14.692 1.463 1.00 87.86 C ANISOU 3229 CZ TYR A 404 11239 9429 12713 -585 4364 -832 C ATOM 3230 OH TYR A 404 16.539 14.793 0.211 1.00106.16 O ANISOU 3230 OH TYR A 404 13913 11575 14847 -679 5002 -1013 O ATOM 3231 N TRP A 405 12.466 16.836 6.166 1.00 96.00 N ANISOU 3231 N TRP A 405 10932 12059 13487 -673 1730 -185 N ATOM 3232 CA TRP A 405 11.638 17.985 5.813 1.00 88.29 C ANISOU 3232 CA TRP A 405 9986 11317 12243 -789 1530 -181 C ATOM 3233 C TRP A 405 12.023 19.221 6.615 1.00 95.00 C ANISOU 3233 C TRP A 405 10404 12320 13370 -620 1350 -183 C ATOM 3234 O TRP A 405 12.050 20.333 6.075 1.00 90.99 O ANISOU 3234 O TRP A 405 9896 11797 12880 -639 1353 -189 O ATOM 3235 CB TRP A 405 10.175 17.627 6.056 1.00 63.16 C ANISOU 3235 CB TRP A 405 6913 8405 8680 -967 1194 -110 C ATOM 3236 CG TRP A 405 9.167 18.692 5.815 1.00 80.55 C ANISOU 3236 CG TRP A 405 9058 10852 10695 -1044 945 -49 C ATOM 3237 CD1 TRP A 405 8.724 19.160 4.611 1.00 80.38 C ANISOU 3237 CD1 TRP A 405 9323 10773 10446 -1244 948 21 C ATOM 3238 CD2 TRP A 405 8.469 19.432 6.818 1.00 84.83 C ANISOU 3238 CD2 TRP A 405 9222 11719 11292 -916 657 -36 C ATOM 3239 NE1 TRP A 405 7.774 20.136 4.808 1.00 86.95 N ANISOU 3239 NE1 TRP A 405 9922 11846 11270 -1218 640 125 N ATOM 3240 CE2 TRP A 405 7.603 20.322 6.155 1.00 91.79 C ANISOU 3240 CE2 TRP A 405 10127 12684 12066 -989 504 54 C ATOM 3241 CE3 TRP A 405 8.481 19.418 8.216 1.00 90.78 C ANISOU 3241 CE3 TRP A 405 9637 12700 12156 -763 526 -91 C ATOM 3242 CZ2 TRP A 405 6.765 21.195 6.844 1.00 87.60 C ANISOU 3242 CZ2 TRP A 405 9253 12409 11620 -840 283 59 C ATOM 3243 CZ3 TRP A 405 7.651 20.285 8.897 1.00100.66 C ANISOU 3243 CZ3 TRP A 405 10616 14245 13385 -661 339 -133 C ATOM 3244 CH2 TRP A 405 6.806 21.163 8.211 1.00 97.97 C ANISOU 3244 CH2 TRP A 405 10267 13935 13021 -663 247 -74 C ATOM 3245 N LEU A 406 12.322 19.048 7.907 1.00 96.46 N ANISOU 3245 N LEU A 406 10260 12636 13755 -495 1161 -167 N ATOM 3246 CA LEU A 406 12.588 20.196 8.768 1.00 82.78 C ANISOU 3246 CA LEU A 406 8201 11051 12200 -397 946 -217 C ATOM 3247 C LEU A 406 13.804 20.983 8.295 1.00 85.94 C ANISOU 3247 C LEU A 406 8480 11210 12962 -341 1129 -207 C ATOM 3248 O LEU A 406 13.877 22.200 8.506 1.00 93.18 O ANISOU 3248 O LEU A 406 9270 12156 13977 -325 977 -265 O ATOM 3249 CB LEU A 406 12.778 19.733 10.214 1.00 76.04 C ANISOU 3249 CB LEU A 406 7090 10390 11412 -362 706 -179 C ATOM 3250 CG LEU A 406 12.877 20.843 11.260 1.00 93.14 C ANISOU 3250 CG LEU A 406 9019 12747 13624 -329 447 -292 C ATOM 3251 CD1 LEU A 406 11.567 21.617 11.322 1.00 90.65 C ANISOU 3251 CD1 LEU A 406 8776 12656 13011 -317 343 -450 C ATOM 3252 CD2 LEU A 406 13.244 20.282 12.624 1.00 94.41 C ANISOU 3252 CD2 LEU A 406 8982 13098 13793 -382 207 -210 C ATOM 3253 N CYS A 407 14.761 20.312 7.647 1.00 80.76 N ANISOU 3253 N CYS A 407 7856 10297 12531 -313 1478 -134 N ATOM 3254 CA CYS A 407 15.889 21.019 7.050 1.00 90.44 C ANISOU 3254 CA CYS A 407 8943 11327 14094 -292 1725 -83 C ATOM 3255 C CYS A 407 15.422 22.033 6.012 1.00102.21 C ANISOU 3255 C CYS A 407 10681 12795 15358 -427 1780 -112 C ATOM 3256 O CYS A 407 16.029 23.101 5.868 1.00110.26 O ANISOU 3256 O CYS A 407 11541 13744 16608 -455 1763 -59 O ATOM 3257 CB CYS A 407 16.854 20.016 6.417 1.00 91.03 C ANISOU 3257 CB CYS A 407 9022 11136 14429 -210 2206 -24 C ATOM 3258 SG CYS A 407 17.621 18.873 7.590 1.00 97.19 S ANISOU 3258 SG CYS A 407 9415 11847 15665 -25 2108 126 S ATOM 3259 N TYR A 408 14.347 21.716 5.284 1.00 82.05 N ANISOU 3259 N TYR A 408 8515 10292 12368 -552 1795 -147 N ATOM 3260 CA TYR A 408 13.796 22.647 4.306 1.00 98.25 C ANISOU 3260 CA TYR A 408 10802 12334 14193 -720 1755 -94 C ATOM 3261 C TYR A 408 13.156 23.858 4.975 1.00102.12 C ANISOU 3261 C TYR A 408 11090 12944 14768 -654 1329 -100 C ATOM 3262 O TYR A 408 13.166 24.955 4.406 1.00 95.96 O ANISOU 3262 O TYR A 408 10343 12061 14055 -731 1260 -14 O ATOM 3263 CB TYR A 408 12.771 21.925 3.428 1.00 92.12 C ANISOU 3263 CB TYR A 408 10479 11600 12921 -924 1791 -79 C ATOM 3264 CG TYR A 408 13.361 20.937 2.443 1.00 85.22 C ANISOU 3264 CG TYR A 408 9968 10526 11884 -1046 2283 -133 C ATOM 3265 CD1 TYR A 408 14.671 21.058 2.000 1.00 80.08 C ANISOU 3265 CD1 TYR A 408 9232 9687 11507 -991 2735 -143 C ATOM 3266 CD2 TYR A 408 12.613 19.861 1.984 1.00 83.81 C ANISOU 3266 CD2 TYR A 408 10217 10334 11294 -1222 2322 -189 C ATOM 3267 CE1 TYR A 408 15.209 20.152 1.100 1.00 79.74 C ANISOU 3267 CE1 TYR A 408 9530 9444 11326 -1063 3287 -251 C ATOM 3268 CE2 TYR A 408 13.142 18.948 1.093 1.00 75.88 C ANISOU 3268 CE2 TYR A 408 9623 9088 10121 -1330 2817 -316 C ATOM 3269 CZ TYR A 408 14.439 19.096 0.653 1.00 96.29 C ANISOU 3269 CZ TYR A 408 12122 11483 12980 -1225 3337 -370 C ATOM 3270 OH TYR A 408 14.963 18.183 -0.236 1.00 97.38 O ANISOU 3270 OH TYR A 408 12677 11363 12958 -1294 3927 -552 O ATOM 3271 N VAL A 409 12.600 23.681 6.178 1.00 84.25 N ANISOU 3271 N VAL A 409 8632 10876 12505 -518 1064 -204 N ATOM 3272 CA VAL A 409 11.946 24.773 6.892 1.00 87.11 C ANISOU 3272 CA VAL A 409 8825 11331 12940 -414 744 -291 C ATOM 3273 C VAL A 409 12.934 25.877 7.259 1.00 94.43 C ANISOU 3273 C VAL A 409 9562 12075 14242 -370 679 -339 C ATOM 3274 O VAL A 409 12.536 27.034 7.434 1.00 96.82 O ANISOU 3274 O VAL A 409 9825 12298 14663 -312 471 -408 O ATOM 3275 CB VAL A 409 11.219 24.213 8.136 1.00 92.00 C ANISOU 3275 CB VAL A 409 9302 12245 13410 -313 571 -415 C ATOM 3276 CG1 VAL A 409 10.604 25.326 8.977 1.00 77.58 C ANISOU 3276 CG1 VAL A 409 7309 10507 11661 -168 343 -590 C ATOM 3277 CG2 VAL A 409 10.142 23.220 7.713 1.00107.67 C ANISOU 3277 CG2 VAL A 409 11463 14403 15043 -413 580 -316 C ATOM 3278 N ASN A 410 14.225 25.550 7.364 1.00100.19 N ANISOU 3278 N ASN A 410 10156 12703 15208 -401 842 -285 N ATOM 3279 CA ASN A 410 15.230 26.576 7.623 1.00 95.80 C ANISOU 3279 CA ASN A 410 9406 11971 15024 -437 749 -267 C ATOM 3280 C ASN A 410 15.190 27.661 6.553 1.00101.95 C ANISOU 3280 C ASN A 410 10328 12533 15877 -547 771 -151 C ATOM 3281 O ASN A 410 15.242 28.856 6.867 1.00 95.45 O ANISOU 3281 O ASN A 410 9448 11551 15266 -554 523 -202 O ATOM 3282 CB ASN A 410 16.621 25.944 7.693 1.00 87.98 C ANISOU 3282 CB ASN A 410 8180 10920 14329 -470 958 -126 C ATOM 3283 CG ASN A 410 17.662 26.875 8.298 1.00 94.25 C ANISOU 3283 CG ASN A 410 8694 11597 15520 -553 747 -77 C ATOM 3284 OD1 ASN A 410 17.348 27.987 8.723 1.00120.07 O ANISOU 3284 OD1 ASN A 410 12013 14796 18813 -591 445 -208 O ATOM 3285 ND2 ASN A 410 18.910 26.425 8.326 1.00 87.92 N ANISOU 3285 ND2 ASN A 410 7589 10746 15070 -588 905 121 N ATOM 3286 N SER A 411 15.079 27.261 5.282 1.00 93.04 N ANISOU 3286 N SER A 411 9430 11373 14550 -666 1052 8 N ATOM 3287 CA SER A 411 15.034 28.230 4.191 1.00 94.14 C ANISOU 3287 CA SER A 411 9737 11335 14696 -841 1053 195 C ATOM 3288 C SER A 411 13.822 29.147 4.295 1.00 98.63 C ANISOU 3288 C SER A 411 10385 11857 15232 -776 671 175 C ATOM 3289 O SER A 411 13.856 30.282 3.804 1.00 94.55 O ANISOU 3289 O SER A 411 9911 11114 14899 -872 514 325 O ATOM 3290 CB SER A 411 15.023 27.505 2.845 1.00 76.84 C ANISOU 3290 CB SER A 411 7863 9175 12158 -1037 1425 344 C ATOM 3291 OG SER A 411 16.231 26.801 2.629 1.00 81.97 O ANISOU 3291 OG SER A 411 8413 9798 12932 -1057 1872 358 O ATOM 3292 N THR A 412 12.745 28.679 4.925 1.00 88.54 N ANISOU 3292 N THR A 412 9095 10774 13770 -609 525 22 N ATOM 3293 CA THR A 412 11.531 29.480 5.013 1.00 96.52 C ANISOU 3293 CA THR A 412 10103 11750 14819 -491 223 20 C ATOM 3294 C THR A 412 11.645 30.578 6.062 1.00 85.30 C ANISOU 3294 C THR A 412 8497 10150 13762 -297 5 -212 C ATOM 3295 O THR A 412 11.057 31.653 5.895 1.00103.69 O ANISOU 3295 O THR A 412 10829 12250 16319 -208 -210 -174 O ATOM 3296 CB THR A 412 10.336 28.575 5.323 1.00 86.76 C ANISOU 3296 CB THR A 412 8863 10823 13278 -397 185 -36 C ATOM 3297 OG1 THR A 412 10.256 27.541 4.335 1.00100.63 O ANISOU 3297 OG1 THR A 412 10875 12690 14671 -630 363 147 O ATOM 3298 CG2 THR A 412 9.041 29.370 5.309 1.00 71.61 C ANISOU 3298 CG2 THR A 412 6855 8882 11472 -252 -87 26 C ATOM 3299 N ILE A 413 12.404 30.341 7.136 1.00 82.66 N ANISOU 3299 N ILE A 413 8026 9884 13498 -249 35 -444 N ATOM 3300 CA ILE A 413 12.434 31.262 8.269 1.00104.44 C ANISOU 3300 CA ILE A 413 10695 12506 16481 -113 -174 -744 C ATOM 3301 C ILE A 413 13.634 32.202 8.259 1.00109.38 C ANISOU 3301 C ILE A 413 11309 12794 17458 -277 -285 -707 C ATOM 3302 O ILE A 413 13.677 33.133 9.082 1.00109.70 O ANISOU 3302 O ILE A 413 11362 12624 17696 -217 -495 -969 O ATOM 3303 CB ILE A 413 12.384 30.496 9.609 1.00105.30 C ANISOU 3303 CB ILE A 413 10702 12937 16370 -31 -165 -1018 C ATOM 3304 CG1 ILE A 413 13.592 29.569 9.750 1.00104.40 C ANISOU 3304 CG1 ILE A 413 10494 12941 16233 -205 -60 -888 C ATOM 3305 CG2 ILE A 413 11.083 29.714 9.729 1.00 99.62 C ANISOU 3305 CG2 ILE A 413 9967 12550 15333 114 -88 -1049 C ATOM 3306 CD1 ILE A 413 13.709 28.932 11.116 1.00115.70 C ANISOU 3306 CD1 ILE A 413 11825 14650 17485 -197 -149 -1079 C ATOM 3307 N ASN A 414 14.611 31.993 7.371 1.00 91.23 N ANISOU 3307 N ASN A 414 8993 10433 15238 -501 -131 -404 N ATOM 3308 CA ASN A 414 15.704 32.958 7.256 1.00108.17 C ANISOU 3308 CA ASN A 414 11084 12265 17750 -704 -250 -290 C ATOM 3309 C ASN A 414 15.211 34.363 6.926 1.00104.16 C ANISOU 3309 C ASN A 414 10724 11353 17501 -692 -508 -274 C ATOM 3310 O ASN A 414 15.655 35.314 7.591 1.00103.50 O ANISOU 3310 O ASN A 414 10642 10972 17710 -745 -758 -434 O ATOM 3311 CB ASN A 414 16.741 32.479 6.233 1.00108.07 C ANISOU 3311 CB ASN A 414 10993 12296 17773 -936 53 65 C ATOM 3312 CG ASN A 414 17.562 31.310 6.733 1.00121.65 C ANISOU 3312 CG ASN A 414 12484 14274 19465 -930 266 58 C ATOM 3313 OD1 ASN A 414 17.519 30.218 6.168 1.00157.32 O ANISOU 3313 OD1 ASN A 414 17030 18980 23766 -893 603 145 O ATOM 3314 ND2 ASN A 414 18.322 31.537 7.798 1.00119.89 N ANISOU 3314 ND2 ASN A 414 12048 14026 19478 -984 40 -33 N ATOM 3315 N PRO A 415 14.324 34.577 5.943 1.00 88.88 N ANISOU 3315 N PRO A 415 8924 9346 15501 -651 -506 -65 N ATOM 3316 CA PRO A 415 13.790 35.937 5.756 1.00 98.78 C ANISOU 3316 CA PRO A 415 10279 10153 17101 -587 -806 -30 C ATOM 3317 C PRO A 415 13.060 36.460 6.979 1.00104.83 C ANISOU 3317 C PRO A 415 11035 10779 18018 -258 -974 -495 C ATOM 3318 O PRO A 415 13.129 37.661 7.271 1.00116.19 O ANISOU 3318 O PRO A 415 12557 11744 19845 -222 -1212 -622 O ATOM 3319 CB PRO A 415 12.848 35.781 4.553 1.00 95.47 C ANISOU 3319 CB PRO A 415 9962 9795 16518 -602 -795 325 C ATOM 3320 CG PRO A 415 13.367 34.604 3.820 1.00103.76 C ANISOU 3320 CG PRO A 415 11055 11213 17157 -836 -461 528 C ATOM 3321 CD PRO A 415 13.854 33.666 4.883 1.00 89.16 C ANISOU 3321 CD PRO A 415 9053 9646 15177 -720 -275 197 C ATOM 3322 N MET A 416 12.364 35.583 7.708 1.00102.57 N ANISOU 3322 N MET A 416 10670 10880 17423 -34 -831 -764 N ATOM 3323 CA MET A 416 11.678 36.009 8.923 1.00 96.69 C ANISOU 3323 CA MET A 416 9923 10074 16741 265 -891 -1247 C ATOM 3324 C MET A 416 12.668 36.506 9.968 1.00103.36 C ANISOU 3324 C MET A 416 10854 10739 17678 125 -1016 -1582 C ATOM 3325 O MET A 416 12.417 37.511 10.642 1.00121.81 O ANISOU 3325 O MET A 416 13327 12709 20248 264 -1150 -1944 O ATOM 3326 CB MET A 416 10.834 34.862 9.477 1.00107.11 C ANISOU 3326 CB MET A 416 11123 11925 17648 446 -687 -1403 C ATOM 3327 CG MET A 416 9.662 34.479 8.589 1.00115.65 C ANISOU 3327 CG MET A 416 12117 13165 18660 575 -638 -1104 C ATOM 3328 SD MET A 416 8.766 33.035 9.189 1.00132.68 S ANISOU 3328 SD MET A 416 14124 15962 20328 686 -428 -1208 S ATOM 3329 CE MET A 416 7.999 33.699 10.665 1.00147.58 C ANISOU 3329 CE MET A 416 15919 17841 22311 1050 -366 -1769 C ATOM 3330 N CYS A 417 13.804 35.820 10.114 1.00104.60 N ANISOU 3330 N CYS A 417 10939 11126 17679 -162 -985 -1460 N ATOM 3331 CA CYS A 417 14.837 36.301 11.027 1.00119.29 C ANISOU 3331 CA CYS A 417 12854 12823 19646 -391 -1195 -1670 C ATOM 3332 C CYS A 417 15.396 37.643 10.573 1.00115.23 C ANISOU 3332 C CYS A 417 12465 11721 19595 -571 -1446 -1560 C ATOM 3333 O CYS A 417 15.688 38.513 11.401 1.00114.04 O ANISOU 3333 O CYS A 417 12495 11236 19597 -659 -1689 -1891 O ATOM 3334 CB CYS A 417 15.960 35.272 11.149 1.00120.47 C ANISOU 3334 CB CYS A 417 12798 13326 19650 -655 -1137 -1434 C ATOM 3335 SG CYS A 417 15.488 33.749 11.990 1.00131.47 S ANISOU 3335 SG CYS A 417 14082 15330 20540 -518 -955 -1578 S ATOM 3336 N TYR A 418 15.544 37.832 9.260 1.00106.32 N ANISOU 3336 N TYR A 418 11285 10450 18664 -671 -1403 -1093 N ATOM 3337 CA TYR A 418 16.100 39.079 8.744 1.00106.56 C ANISOU 3337 CA TYR A 418 11421 9927 19139 -899 -1659 -892 C ATOM 3338 C TYR A 418 15.206 40.260 9.100 1.00112.52 C ANISOU 3338 C TYR A 418 12414 10143 20195 -638 -1868 -1222 C ATOM 3339 O TYR A 418 15.679 41.284 9.606 1.00117.80 O ANISOU 3339 O TYR A 418 13268 10320 21169 -783 -2147 -1425 O ATOM 3340 CB TYR A 418 16.275 38.986 7.227 1.00114.20 C ANISOU 3340 CB TYR A 418 12318 10913 20159 -1071 -1534 -305 C ATOM 3341 CG TYR A 418 17.229 37.909 6.759 1.00115.87 C ANISOU 3341 CG TYR A 418 12310 11571 20146 -1308 -1239 1 C ATOM 3342 CD1 TYR A 418 18.110 37.293 7.639 1.00113.91 C ANISOU 3342 CD1 TYR A 418 11872 11573 19836 -1409 -1206 -137 C ATOM 3343 CD2 TYR A 418 17.240 37.502 5.432 1.00127.37 C ANISOU 3343 CD2 TYR A 418 13755 13182 21456 -1434 -984 434 C ATOM 3344 CE1 TYR A 418 18.973 36.303 7.208 1.00128.53 C ANISOU 3344 CE1 TYR A 418 13468 13775 21591 -1556 -900 152 C ATOM 3345 CE2 TYR A 418 18.100 36.517 4.992 1.00127.69 C ANISOU 3345 CE2 TYR A 418 13613 13583 21319 -1601 -622 652 C ATOM 3346 CZ TYR A 418 18.965 35.921 5.883 1.00132.06 C ANISOU 3346 CZ TYR A 418 13918 14337 21920 -1625 -567 511 C ATOM 3347 OH TYR A 418 19.823 34.938 5.444 1.00133.37 O ANISOU 3347 OH TYR A 418 13850 14807 22018 -1727 -174 738 O ATOM 3348 N ALA A 419 13.901 40.129 8.841 1.00109.29 N ANISOU 3348 N ALA A 419 11991 9790 19742 -250 -1739 -1272 N ATOM 3349 CA ALA A 419 12.965 41.202 9.155 1.00112.41 C ANISOU 3349 CA ALA A 419 12537 9657 20517 93 -1871 -1573 C ATOM 3350 C ALA A 419 12.805 41.387 10.658 1.00122.59 C ANISOU 3350 C ALA A 419 13985 10902 21690 270 -1828 -2290 C ATOM 3351 O ALA A 419 12.564 42.507 11.121 1.00124.25 O ANISOU 3351 O ALA A 419 14429 10511 22271 420 -1967 -2652 O ATOM 3352 CB ALA A 419 11.609 40.924 8.506 1.00 98.01 C ANISOU 3352 CB ALA A 419 10556 7973 18710 458 -1745 -1374 C ATOM 3353 N LEU A 420 12.933 40.308 11.433 1.00119.45 N ANISOU 3353 N LEU A 420 13504 11110 20771 233 -1634 -2506 N ATOM 3354 CA LEU A 420 12.858 40.424 12.886 1.00129.93 C ANISOU 3354 CA LEU A 420 15034 12475 21861 296 -1598 -3163 C ATOM 3355 C LEU A 420 14.142 41.001 13.474 1.00132.12 C ANISOU 3355 C LEU A 420 15547 12462 22192 -158 -1919 -3306 C ATOM 3356 O LEU A 420 14.089 41.794 14.422 1.00120.23 O ANISOU 3356 O LEU A 420 14380 10591 20712 -151 -2020 -3865 O ATOM 3357 CB LEU A 420 12.547 39.061 13.509 1.00133.45 C ANISOU 3357 CB LEU A 420 15312 13679 21712 350 -1338 -3263 C ATOM 3358 CG LEU A 420 11.079 38.679 13.737 1.00143.87 C ANISOU 3358 CG LEU A 420 16505 15283 22876 816 -1013 -3477 C ATOM 3359 CD1 LEU A 420 10.466 39.557 14.815 1.00153.60 C ANISOU 3359 CD1 LEU A 420 17988 16209 24164 1084 -903 -4171 C ATOM 3360 CD2 LEU A 420 10.249 38.766 12.463 1.00145.04 C ANISOU 3360 CD2 LEU A 420 16432 15311 23364 1069 -970 -3027 C ATOM 3361 N CYS A 421 15.300 40.621 12.932 1.00130.09 N ANISOU 3361 N CYS A 421 15118 12356 21957 -571 -2071 -2812 N ATOM 3362 CA CYS A 421 16.566 41.119 13.462 1.00131.11 C ANISOU 3362 CA CYS A 421 15382 12257 22176 -1058 -2425 -2844 C ATOM 3363 C CYS A 421 16.911 42.490 12.890 1.00138.61 C ANISOU 3363 C CYS A 421 16524 12446 23695 -1221 -2721 -2718 C ATOM 3364 O CYS A 421 17.045 43.469 13.632 1.00141.76 O ANISOU 3364 O CYS A 421 17296 12327 24240 -1339 -2977 -3155 O ATOM 3365 CB CYS A 421 17.691 40.123 13.175 1.00130.11 C ANISOU 3365 CB CYS A 421 14897 12619 21919 -1410 -2437 -2336 C ATOM 3366 SG CYS A 421 17.528 38.561 14.051 1.00145.63 S ANISOU 3366 SG CYS A 421 16679 15375 23278 -1327 -2223 -2461 S ATOM 3367 N ASN A 422 17.067 42.577 11.571 1.00136.86 N ANISOU 3367 N ASN A 422 16096 12132 23772 -1271 -2697 -2122 N ATOM 3368 CA ASN A 422 17.449 43.822 10.919 1.00138.24 C ANISOU 3368 CA ASN A 422 16422 11612 24491 -1490 -3003 -1870 C ATOM 3369 C ASN A 422 16.197 44.643 10.637 1.00138.99 C ANISOU 3369 C ASN A 422 16719 11175 24917 -1029 -2983 -2063 C ATOM 3370 O ASN A 422 15.328 44.223 9.863 1.00133.58 O ANISOU 3370 O ASN A 422 15848 10702 24205 -708 -2759 -1803 O ATOM 3371 CB ASN A 422 18.218 43.548 9.628 1.00139.80 C ANISOU 3371 CB ASN A 422 16314 11992 24813 -1810 -2966 -1105 C ATOM 3372 CG ASN A 422 18.845 44.803 9.043 1.00154.53 C ANISOU 3372 CG ASN A 422 18313 13197 27206 -2181 -3329 -770 C ATOM 3373 OD1 ASN A 422 18.695 45.899 9.586 1.00188.99 O ANISOU 3373 OD1 ASN A 422 23023 16893 31890 -2187 -3645 -1117 O ATOM 3374 ND2 ASN A 422 19.554 44.648 7.932 1.00142.15 N ANISOU 3374 ND2 ASN A 422 16493 11796 25722 -2511 -3264 -101 N ATOM 3375 N LYS A 423 16.109 45.815 11.259 1.00138.96 N ANISOU 3375 N LYS A 423 17093 10449 25256 -1008 -3236 -2501 N ATOM 3376 CA LYS A 423 14.956 46.684 11.089 1.00155.03 C ANISOU 3376 CA LYS A 423 19299 11866 27739 -518 -3218 -2716 C ATOM 3377 C LYS A 423 15.011 47.493 9.800 1.00144.65 C ANISOU 3377 C LYS A 423 17943 10017 27002 -633 -3484 -2061 C ATOM 3378 O LYS A 423 14.109 48.300 9.556 1.00130.67 O ANISOU 3378 O LYS A 423 16276 7641 25733 -244 -3548 -2120 O ATOM 3379 CB LYS A 423 14.831 47.609 12.301 1.00176.40 C ANISOU 3379 CB LYS A 423 22485 13949 30592 -424 -3328 -3519 C ATOM 3380 CG LYS A 423 14.543 46.849 13.588 1.00187.40 C ANISOU 3380 CG LYS A 423 23965 15889 31351 -275 -3025 -4190 C ATOM 3381 CD LYS A 423 14.446 47.767 14.792 1.00201.92 C ANISOU 3381 CD LYS A 423 26370 17122 33228 -242 -3090 -5045 C ATOM 3382 CE LYS A 423 14.072 46.981 16.041 1.00195.09 C ANISOU 3382 CE LYS A 423 25608 16875 31643 -120 -2746 -5683 C ATOM 3383 NZ LYS A 423 15.143 46.024 16.440 1.00177.20 N ANISOU 3383 NZ LYS A 423 23220 15323 28785 -693 -2918 -5453 N ATOM 3384 N ALA A 424 16.037 47.292 8.972 1.00148.64 N ANISOU 3384 N ALA A 424 18278 10734 27466 -1158 -3625 -1414 N ATOM 3385 CA ALA A 424 16.081 47.898 7.647 1.00139.07 C ANISOU 3385 CA ALA A 424 17006 9169 26665 -1336 -3834 -696 C ATOM 3386 C ALA A 424 15.464 46.988 6.590 1.00132.82 C ANISOU 3386 C ALA A 424 15906 8977 25583 -1179 -3555 -192 C ATOM 3387 O ALA A 424 14.810 47.479 5.664 1.00135.84 O ANISOU 3387 O ALA A 424 16281 9045 26285 -1069 -3697 244 O ATOM 3388 CB ALA A 424 17.523 48.250 7.270 1.00124.79 C ANISOU 3388 CB ALA A 424 15187 7264 24964 -2038 -4101 -241 C ATOM 3389 N PHE A 425 15.661 45.669 6.704 1.00117.49 N ANISOU 3389 N PHE A 425 13732 7865 23042 -1198 -3199 -220 N ATOM 3390 CA PHE A 425 14.878 44.741 5.892 1.00118.38 C ANISOU 3390 CA PHE A 425 13637 8519 22823 -995 -2922 95 C ATOM 3391 C PHE A 425 13.396 44.852 6.219 1.00126.93 C ANISOU 3391 C PHE A 425 14719 9460 24049 -394 -2873 -219 C ATOM 3392 O PHE A 425 12.550 44.842 5.317 1.00138.38 O ANISOU 3392 O PHE A 425 16070 10914 25594 -247 -2911 197 O ATOM 3393 CB PHE A 425 15.340 43.295 6.101 1.00123.89 C ANISOU 3393 CB PHE A 425 14127 10042 22902 -1087 -2547 34 C ATOM 3394 CG PHE A 425 16.656 42.960 5.453 1.00117.63 C ANISOU 3394 CG PHE A 425 13207 9509 21978 -1610 -2467 491 C ATOM 3395 CD1 PHE A 425 16.744 42.813 4.078 1.00111.21 C ANISOU 3395 CD1 PHE A 425 12350 8840 21066 -1855 -2366 1108 C ATOM 3396 CD2 PHE A 425 17.783 42.717 6.220 1.00113.59 C ANISOU 3396 CD2 PHE A 425 12595 9152 21413 -1865 -2461 318 C ATOM 3397 CE1 PHE A 425 17.945 42.484 3.475 1.00113.01 C ANISOU 3397 CE1 PHE A 425 12434 9337 21169 -2309 -2183 1501 C ATOM 3398 CE2 PHE A 425 18.989 42.383 5.624 1.00106.69 C ANISOU 3398 CE2 PHE A 425 11505 8537 20498 -2301 -2332 767 C ATOM 3399 CZ PHE A 425 19.070 42.266 4.250 1.00107.21 C ANISOU 3399 CZ PHE A 425 11521 8732 20481 -2501 -2145 1335 C ATOM 3400 N ARG A 426 13.068 44.948 7.511 1.00131.23 N ANISOU 3400 N ARG A 426 15357 9905 24598 -69 -2782 -932 N ATOM 3401 CA ARG A 426 11.677 45.032 7.949 1.00122.16 C ANISOU 3401 CA ARG A 426 14149 8665 23603 537 -2637 -1289 C ATOM 3402 C ARG A 426 10.948 46.175 7.256 1.00139.52 C ANISOU 3402 C ARG A 426 16371 10118 26521 773 -2916 -987 C ATOM 3403 O ARG A 426 9.833 46.005 6.749 1.00145.08 O ANISOU 3403 O ARG A 426 16840 10918 27365 1119 -2871 -732 O ATOM 3404 CB ARG A 426 11.631 45.219 9.466 1.00138.73 C ANISOU 3404 CB ARG A 426 16445 10648 25618 759 -2495 -2140 C ATOM 3405 CG ARG A 426 10.241 45.194 10.075 1.00143.27 C ANISOU 3405 CG ARG A 426 16916 11236 26285 1398 -2208 -2593 C ATOM 3406 CD ARG A 426 10.314 45.504 11.563 1.00164.28 C ANISOU 3406 CD ARG A 426 19880 13736 28804 1530 -2045 -3471 C ATOM 3407 NE ARG A 426 11.035 44.482 12.315 1.00166.67 N ANISOU 3407 NE ARG A 426 20214 14743 28371 1194 -1915 -3685 N ATOM 3408 CZ ARG A 426 11.437 44.630 13.573 1.00168.92 C ANISOU 3408 CZ ARG A 426 20822 14997 28362 1072 -1875 -4343 C ATOM 3409 NH1 ARG A 426 12.089 43.650 14.185 1.00174.56 N ANISOU 3409 NH1 ARG A 426 21515 16373 28437 738 -1826 -4409 N ATOM 3410 NH2 ARG A 426 11.196 45.764 14.217 1.00161.85 N ANISOU 3410 NH2 ARG A 426 20301 13379 27815 1264 -1902 -4928 N ATOM 3411 N ASP A 427 11.569 47.354 7.224 1.00140.08 N ANISOU 3411 N ASP A 427 16710 9420 27095 564 -3254 -964 N ATOM 3412 CA ASP A 427 10.932 48.511 6.611 1.00133.63 C ANISOU 3412 CA ASP A 427 15935 7784 27054 785 -3573 -652 C ATOM 3413 C ASP A 427 10.976 48.448 5.090 1.00137.64 C ANISOU 3413 C ASP A 427 16294 8411 27593 443 -3823 309 C ATOM 3414 O ASP A 427 10.031 48.895 4.430 1.00131.16 O ANISOU 3414 O ASP A 427 15336 7274 27226 712 -4019 715 O ATOM 3415 CB ASP A 427 11.595 49.798 7.104 1.00140.97 C ANISOU 3415 CB ASP A 427 17238 8005 28318 618 -3820 -933 C ATOM 3416 CG ASP A 427 11.356 50.047 8.581 1.00153.94 C ANISOU 3416 CG ASP A 427 19121 9488 29880 970 -3564 -1895 C ATOM 3417 OD1 ASP A 427 10.328 49.571 9.107 1.00161.21 O ANISOU 3417 OD1 ASP A 427 19872 10644 30738 1512 -3211 -2298 O ATOM 3418 OD2 ASP A 427 12.193 50.725 9.214 1.00164.52 O ANISOU 3418 OD2 ASP A 427 20831 10506 31174 670 -3705 -2227 O ATOM 3419 N THR A 428 12.052 47.904 4.517 1.00139.67 N ANISOU 3419 N THR A 428 16566 9138 27364 -159 -3809 698 N ATOM 3420 CA THR A 428 12.133 47.818 3.064 1.00144.54 C ANISOU 3420 CA THR A 428 17110 9920 27887 -550 -3983 1576 C ATOM 3421 C THR A 428 11.169 46.771 2.519 1.00144.40 C ANISOU 3421 C THR A 428 16855 10574 27438 -355 -3773 1811 C ATOM 3422 O THR A 428 10.671 46.910 1.396 1.00146.09 O ANISOU 3422 O THR A 428 17023 10761 27722 -498 -4010 2494 O ATOM 3423 CB THR A 428 13.568 47.515 2.631 1.00134.73 C ANISOU 3423 CB THR A 428 15931 9012 26248 -1226 -3919 1876 C ATOM 3424 OG1 THR A 428 14.450 48.491 3.200 1.00151.66 O ANISOU 3424 OG1 THR A 428 18276 10536 28813 -1453 -4170 1674 O ATOM 3425 CG2 THR A 428 13.692 47.590 1.120 1.00122.28 C ANISOU 3425 CG2 THR A 428 14360 7541 24561 -1687 -4078 2766 C ATOM 3426 N PHE A 429 10.877 45.731 3.305 1.00133.19 N ANISOU 3426 N PHE A 429 15299 9746 25559 -76 -3377 1286 N ATOM 3427 CA PHE A 429 9.870 44.762 2.892 1.00131.69 C ANISOU 3427 CA PHE A 429 14891 10140 25006 115 -3215 1472 C ATOM 3428 C PHE A 429 8.478 45.377 2.882 1.00130.41 C ANISOU 3428 C PHE A 429 14539 9569 25443 637 -3426 1557 C ATOM 3429 O PHE A 429 7.640 44.996 2.057 1.00140.61 O ANISOU 3429 O PHE A 429 15657 11127 26644 637 -3545 2070 O ATOM 3430 CB PHE A 429 9.888 43.542 3.813 1.00132.91 C ANISOU 3430 CB PHE A 429 14943 10973 24582 279 -2770 904 C ATOM 3431 CG PHE A 429 11.121 42.701 3.686 1.00123.54 C ANISOU 3431 CG PHE A 429 13839 10278 22822 -186 -2538 931 C ATOM 3432 CD1 PHE A 429 11.997 42.882 2.628 1.00129.81 C ANISOU 3432 CD1 PHE A 429 14750 11039 23532 -712 -2636 1483 C ATOM 3433 CD2 PHE A 429 11.402 41.720 4.624 1.00114.77 C ANISOU 3433 CD2 PHE A 429 12661 9666 21279 -95 -2205 437 C ATOM 3434 CE1 PHE A 429 13.133 42.107 2.512 1.00130.03 C ANISOU 3434 CE1 PHE A 429 14784 11508 23112 -1082 -2350 1506 C ATOM 3435 CE2 PHE A 429 12.535 40.939 4.512 1.00110.67 C ANISOU 3435 CE2 PHE A 429 12152 9552 20344 -470 -1992 500 C ATOM 3436 CZ PHE A 429 13.400 41.134 3.455 1.00112.50 C ANISOU 3436 CZ PHE A 429 12458 9733 20555 -935 -2037 1018 C ATOM 3437 N ARG A 430 8.215 46.323 3.785 1.00139.43 N ANISOU 3437 N ARG A 430 15710 10051 27216 1074 -3472 1064 N ATOM 3438 CA ARG A 430 6.879 46.900 3.883 1.00142.56 C ANISOU 3438 CA ARG A 430 15852 10028 28286 1673 -3583 1084 C ATOM 3439 C ARG A 430 6.555 47.767 2.672 1.00161.76 C ANISOU 3439 C ARG A 430 18247 11911 31301 1532 -4120 1935 C ATOM 3440 O ARG A 430 5.412 47.778 2.202 1.00177.97 O ANISOU 3440 O ARG A 430 19980 14051 33591 1791 -4255 2328 O ATOM 3441 CB ARG A 430 6.752 47.705 5.177 1.00140.23 C ANISOU 3441 CB ARG A 430 15662 9116 28502 2180 -3415 258 C ATOM 3442 CG ARG A 430 5.351 48.226 5.459 1.00171.37 C ANISOU 3442 CG ARG A 430 19304 12904 32904 2813 -3296 132 C ATOM 3443 CD ARG A 430 5.279 48.905 6.818 1.00192.33 C ANISOU 3443 CD ARG A 430 22166 15223 35689 3210 -2945 -789 C ATOM 3444 NE ARG A 430 3.962 49.478 7.082 1.00204.63 N ANISOU 3444 NE ARG A 430 23448 16617 37685 3810 -2751 -897 N ATOM 3445 CZ ARG A 430 2.949 48.807 7.621 1.00206.41 C ANISOU 3445 CZ ARG A 430 23318 17345 37763 4246 -2334 -1152 C ATOM 3446 NH1 ARG A 430 3.098 47.532 7.956 1.00203.38 N ANISOU 3446 NH1 ARG A 430 22826 17660 36790 4146 -2094 -1339 N ATOM 3447 NH2 ARG A 430 1.786 49.409 7.825 1.00211.63 N ANISOU 3447 NH2 ARG A 430 23714 17820 38877 4775 -2149 -1195 N ATOM 3448 N LEU A 431 7.544 48.495 2.145 1.00169.87 N ANISOU 3448 N LEU A 431 19578 12564 32402 1035 -4405 2246 N ATOM 3449 CA LEU A 431 7.300 49.339 0.981 1.00184.68 C ANISOU 3449 CA LEU A 431 21442 14190 34540 772 -4862 3031 C ATOM 3450 C LEU A 431 7.257 48.546 -0.319 1.00167.56 C ANISOU 3450 C LEU A 431 19241 12537 31887 261 -5052 3876 C ATOM 3451 O LEU A 431 6.647 49.009 -1.289 1.00174.72 O ANISOU 3451 O LEU A 431 20042 13400 32943 119 -5433 4549 O ATOM 3452 CB LEU A 431 8.357 50.448 0.891 1.00192.40 C ANISOU 3452 CB LEU A 431 22741 14671 35692 397 -5080 3060 C ATOM 3453 CG LEU A 431 9.845 50.124 0.720 1.00200.65 C ANISOU 3453 CG LEU A 431 24060 15927 36251 -254 -5015 3129 C ATOM 3454 CD1 LEU A 431 10.220 49.941 -0.746 1.00208.04 C ANISOU 3454 CD1 LEU A 431 25046 17208 36791 -908 -5236 4038 C ATOM 3455 CD2 LEU A 431 10.694 51.217 1.351 1.00195.54 C ANISOU 3455 CD2 LEU A 431 23669 14743 35884 -346 -5109 2746 C ATOM 3456 N LEU A 432 7.886 47.371 -0.365 1.00150.15 N ANISOU 3456 N LEU A 432 17138 10998 28916 -73 -4724 3779 N ATOM 3457 CA LEU A 432 7.793 46.534 -1.556 1.00145.94 C ANISOU 3457 CA LEU A 432 16640 11125 27686 -579 -4769 4429 C ATOM 3458 C LEU A 432 6.460 45.802 -1.619 1.00150.98 C ANISOU 3458 C LEU A 432 16970 12186 28212 -247 -4764 4519 C ATOM 3459 O LEU A 432 5.838 45.730 -2.685 1.00153.97 O ANISOU 3459 O LEU A 432 17312 12698 28493 -523 -5130 5267 O ATOM 3460 CB LEU A 432 8.945 45.530 -1.592 1.00119.72 C ANISOU 3460 CB LEU A 432 13522 8477 23490 -1037 -4305 4190 C ATOM 3461 CG LEU A 432 10.349 46.090 -1.815 1.00131.44 C ANISOU 3461 CG LEU A 432 15256 9719 24968 -1537 -4309 4307 C ATOM 3462 CD1 LEU A 432 11.382 44.985 -1.684 1.00124.19 C ANISOU 3462 CD1 LEU A 432 14405 9492 23290 -1837 -3770 4001 C ATOM 3463 CD2 LEU A 432 10.443 46.761 -3.177 1.00137.30 C ANISOU 3463 CD2 LEU A 432 16170 10227 25768 -2090 -4742 5227 C ATOM 3464 N LEU A 433 6.007 45.254 -0.489 1.00149.74 N ANISOU 3464 N LEU A 433 16589 12265 28042 290 -4380 3803 N ATOM 3465 CA LEU A 433 4.750 44.515 -0.478 1.00154.22 C ANISOU 3465 CA LEU A 433 16811 13278 28508 584 -4349 3889 C ATOM 3466 C LEU A 433 3.553 45.440 -0.650 1.00161.49 C ANISOU 3466 C LEU A 433 17368 13628 30364 1028 -4784 4305 C ATOM 3467 O LEU A 433 2.558 45.054 -1.274 1.00169.42 O ANISOU 3467 O LEU A 433 18100 14928 31344 1001 -5041 4856 O ATOM 3468 CB LEU A 433 4.628 43.713 0.817 1.00141.28 C ANISOU 3468 CB LEU A 433 15024 12051 26603 1005 -3802 3036 C ATOM 3469 CG LEU A 433 5.673 42.611 1.003 1.00138.83 C ANISOU 3469 CG LEU A 433 14983 12363 25404 613 -3391 2688 C ATOM 3470 CD1 LEU A 433 5.553 41.979 2.381 1.00136.24 C ANISOU 3470 CD1 LEU A 433 14514 12347 24905 1028 -2932 1885 C ATOM 3471 CD2 LEU A 433 5.551 41.558 -0.090 1.00132.93 C ANISOU 3471 CD2 LEU A 433 14339 12242 23925 107 -3426 3208 C ATOM 3472 N LEU A 434 3.626 46.655 -0.111 1.00150.85 N ANISOU 3472 N LEU A 434 16008 11492 29816 1407 -4861 4039 N ATOM 3473 CA LEU A 434 2.575 47.648 -0.280 1.00166.56 C ANISOU 3473 CA LEU A 434 17695 13139 32450 1724 -5089 4256 C ATOM 3474 C LEU A 434 2.764 48.494 -1.533 1.00165.51 C ANISOU 3474 C LEU A 434 17711 12713 32463 1205 -5653 5069 C ATOM 3475 O LEU A 434 1.993 49.434 -1.751 1.00165.33 O ANISOU 3475 O LEU A 434 17451 12314 33054 1425 -5905 5313 O ATOM 3476 CB LEU A 434 2.501 48.556 0.951 1.00172.73 C ANISOU 3476 CB LEU A 434 18462 13380 33789 2329 -4760 3429 C ATOM 3477 CG LEU A 434 2.100 47.894 2.272 1.00173.79 C ANISOU 3477 CG LEU A 434 18418 13825 33790 2882 -4166 2582 C ATOM 3478 CD1 LEU A 434 2.158 48.895 3.418 1.00181.87 C ANISOU 3478 CD1 LEU A 434 19582 14279 35240 3356 -3853 1777 C ATOM 3479 CD2 LEU A 434 0.721 47.260 2.171 1.00180.21 C ANISOU 3479 CD2 LEU A 434 18709 15150 34612 3171 -4085 2831 C ATOM 3480 N CYS A 435 3.771 48.180 -2.353 1.00172.74 N ANISOU 3480 N CYS A 435 19008 13816 32809 511 -5821 5489 N ATOM 3481 CA CYS A 435 4.056 48.898 -3.596 1.00182.89 C ANISOU 3481 CA CYS A 435 20474 14965 34050 -87 -6315 6260 C ATOM 3482 C CYS A 435 4.276 50.390 -3.332 1.00179.98 C ANISOU 3482 C CYS A 435 20137 13836 34409 111 -6485 6109 C ATOM 3483 O CYS A 435 3.558 51.256 -3.836 1.00188.20 O ANISOU 3483 O CYS A 435 20972 14563 35972 176 -6875 6544 O ATOM 3484 CB CYS A 435 2.944 48.672 -4.627 1.00185.09 C ANISOU 3484 CB CYS A 435 20495 15593 34237 -304 -6731 7029 C ATOM 3485 SG CYS A 435 2.796 46.961 -5.202 1.00180.21 S ANISOU 3485 SG CYS A 435 19992 15891 32590 -760 -6636 7335 S ATOM 3486 N ARG A 436 5.298 50.675 -2.522 1.00179.84 N ANISOU 3486 N ARG A 436 20393 13516 34422 175 -6205 5492 N ATOM 3487 CA ARG A 436 5.648 52.044 -2.158 1.00193.43 C ANISOU 3487 CA ARG A 436 22238 14508 36749 320 -6339 5263 C ATOM 3488 C ARG A 436 7.094 52.380 -2.508 1.00202.12 C ANISOU 3488 C ARG A 436 23742 15535 37518 -304 -6427 5397 C ATOM 3489 O ARG A 436 7.658 53.330 -1.955 1.00199.53 O ANISOU 3489 O ARG A 436 23595 14653 37563 -224 -6449 5040 O ATOM 3490 CB ARG A 436 5.398 52.282 -0.667 1.00193.11 C ANISOU 3490 CB ARG A 436 22147 14105 37120 1034 -5918 4289 C ATOM 3491 CG ARG A 436 3.932 52.242 -0.262 1.00198.10 C ANISOU 3491 CG ARG A 436 22342 14735 38191 1708 -5777 4132 C ATOM 3492 CD ARG A 436 3.764 52.497 1.228 1.00203.78 C ANISOU 3492 CD ARG A 436 23093 15154 39179 2362 -5273 3117 C ATOM 3493 NE ARG A 436 2.365 52.428 1.643 1.00209.79 N ANISOU 3493 NE ARG A 436 23411 15989 40309 3009 -5038 2957 N ATOM 3494 CZ ARG A 436 1.950 52.566 2.899 1.00205.83 C ANISOU 3494 CZ ARG A 436 22880 15346 39982 3624 -4526 2116 C ATOM 3495 NH1 ARG A 436 2.827 52.784 3.869 1.00210.72 N ANISOU 3495 NH1 ARG A 436 23922 15719 40420 3647 -4245 1346 N ATOM 3496 NH2 ARG A 436 0.657 52.488 3.184 1.00193.04 N ANISOU 3496 NH2 ARG A 436 20815 13856 38675 4178 -4289 2061 N ATOM 3497 N TRP A 437 7.706 51.624 -3.415 1.00203.67 N ANISOU 3497 N TRP A 437 24092 16306 36988 -944 -6445 5900 N ATOM 3498 CA TRP A 437 9.087 51.875 -3.813 1.00189.18 C ANISOU 3498 CA TRP A 437 22580 14527 34774 -1564 -6442 6066 C ATOM 3499 C TRP A 437 9.162 52.984 -4.857 1.00194.92 C ANISOU 3499 C TRP A 437 23371 14993 35696 -1955 -6954 6771 C ATOM 3500 O TRP A 437 10.249 53.418 -5.239 1.00193.65 O ANISOU 3500 O TRP A 437 23442 14826 35311 -2455 -7002 6969 O ATOM 3501 CB TRP A 437 9.731 50.597 -4.356 1.00160.31 C ANISOU 3501 CB TRP A 437 19068 11635 30208 -2081 -6127 6262 C TER 3502 TRP A 437 ATOM 3503 N GLY C -3 26.178 -21.398 -16.098 1.00119.98 N ANISOU 3503 N GLY C -3 16824 9268 19495 2602 -3088 -1998 N ATOM 3504 CA GLY C -3 26.835 -22.279 -17.047 1.00104.30 C ANISOU 3504 CA GLY C -3 14485 7393 17751 3329 -3079 -2226 C ATOM 3505 C GLY C -3 26.734 -23.743 -16.668 1.00133.62 C ANISOU 3505 C GLY C -3 19044 10472 21254 3768 -3701 -2295 C ATOM 3506 O GLY C -3 26.304 -24.075 -15.563 1.00145.54 O ANISOU 3506 O GLY C -3 21447 11477 22376 3462 -4245 -2096 O ATOM 3507 N PRO C -2 27.134 -24.627 -17.580 1.00126.23 N ANISOU 3507 N PRO C -2 17827 9565 20569 4420 -3654 -2605 N ATOM 3508 CA PRO C -2 27.059 -26.064 -17.288 1.00142.31 C ANISOU 3508 CA PRO C -2 20495 11283 22293 4635 -4140 -2558 C ATOM 3509 C PRO C -2 28.107 -26.487 -16.274 1.00154.28 C ANISOU 3509 C PRO C -2 21996 12480 24144 4947 -5192 -2585 C ATOM 3510 O PRO C -2 29.284 -26.612 -16.615 1.00144.23 O ANISOU 3510 O PRO C -2 19861 11397 23545 5534 -5432 -2972 O ATOM 3511 CB PRO C -2 27.307 -26.709 -18.657 1.00125.48 C ANISOU 3511 CB PRO C -2 17794 9480 20403 5130 -3656 -2950 C ATOM 3512 CG PRO C -2 28.118 -25.701 -19.402 1.00123.28 C ANISOU 3512 CG PRO C -2 16367 9727 20746 5361 -3246 -3330 C ATOM 3513 CD PRO C -2 27.640 -24.356 -18.938 1.00122.30 C ANISOU 3513 CD PRO C -2 16298 9753 20418 4667 -2971 -2929 C ATOM 3514 N GLY C -1 27.694 -26.733 -15.034 1.00156.05 N ANISOU 3514 N GLY C -1 23151 12254 23888 4495 -5840 -2214 N ATOM 3515 CA GLY C -1 28.636 -27.064 -13.981 1.00149.24 C ANISOU 3515 CA GLY C -1 22389 11014 23300 4665 -6962 -2158 C ATOM 3516 C GLY C -1 29.130 -25.856 -13.210 1.00175.64 C ANISOU 3516 C GLY C -1 25462 14369 26905 4444 -7197 -2065 C ATOM 3517 O GLY C -1 28.904 -25.747 -12.001 1.00180.73 O ANISOU 3517 O GLY C -1 26885 14632 27154 3899 -7821 -1739 O ATOM 3518 N SER C 0 29.812 -24.943 -13.894 1.00184.00 N ANISOU 3518 N SER C 0 25406 15893 28611 4796 -6714 -2361 N ATOM 3519 CA SER C 0 30.332 -23.738 -13.265 1.00173.86 C ANISOU 3519 CA SER C 0 23612 14949 27497 4456 -6722 -2252 C ATOM 3520 C SER C 0 29.340 -22.591 -13.419 1.00163.27 C ANISOU 3520 C SER C 0 22274 14054 25706 3661 -5765 -2071 C ATOM 3521 O SER C 0 28.538 -22.558 -14.356 1.00155.34 O ANISOU 3521 O SER C 0 21278 13235 24510 3561 -4995 -2119 O ATOM 3522 CB SER C 0 31.683 -23.350 -13.870 1.00177.36 C ANISOU 3522 CB SER C 0 22711 15902 28775 5075 -6657 -2655 C ATOM 3523 OG SER C 0 32.193 -22.172 -13.271 1.00186.13 O ANISOU 3523 OG SER C 0 23311 17398 30014 4704 -6635 -2521 O ATOM 3524 N LEU C 1 29.402 -21.645 -12.485 1.00150.53 N ANISOU 3524 N LEU C 1 20628 12577 23989 3086 -5875 -1897 N ATOM 3525 CA LEU C 1 28.472 -20.520 -12.481 1.00124.97 C ANISOU 3525 CA LEU C 1 17348 9657 20477 2320 -5121 -1814 C ATOM 3526 C LEU C 1 29.168 -19.329 -11.842 1.00125.28 C ANISOU 3526 C LEU C 1 16712 10051 20837 2034 -5214 -1790 C ATOM 3527 O LEU C 1 29.564 -19.394 -10.675 1.00130.83 O ANISOU 3527 O LEU C 1 17759 10539 21410 1832 -5905 -1695 O ATOM 3528 CB LEU C 1 27.185 -20.888 -11.733 1.00126.78 C ANISOU 3528 CB LEU C 1 18750 9473 19946 1621 -5159 -1701 C ATOM 3529 CG LEU C 1 25.917 -20.027 -11.834 1.00117.33 C ANISOU 3529 CG LEU C 1 17642 8449 18488 864 -4378 -1779 C ATOM 3530 CD1 LEU C 1 25.975 -18.824 -10.938 1.00102.06 C ANISOU 3530 CD1 LEU C 1 15368 6758 16652 218 -4361 -1848 C ATOM 3531 CD2 LEU C 1 25.662 -19.591 -13.265 1.00123.56 C ANISOU 3531 CD2 LEU C 1 17745 9556 19646 1117 -3608 -1835 C ATOM 3532 N THR C 2 29.322 -18.251 -12.606 1.00123.73 N ANISOU 3532 N THR C 2 15589 10385 21037 1963 -4573 -1847 N ATOM 3533 CA THR C 2 30.017 -17.052 -12.157 1.00142.30 C ANISOU 3533 CA THR C 2 17189 13108 23772 1723 -4612 -1832 C ATOM 3534 C THR C 2 29.023 -15.905 -12.038 1.00149.34 C ANISOU 3534 C THR C 2 18033 14107 24601 942 -4089 -1810 C ATOM 3535 O THR C 2 28.312 -15.593 -12.999 1.00147.85 O ANISOU 3535 O THR C 2 17680 14023 24475 801 -3499 -1800 O ATOM 3536 CB THR C 2 31.140 -16.672 -13.125 1.00135.58 C ANISOU 3536 CB THR C 2 15210 12795 23511 2217 -4401 -1941 C ATOM 3537 OG1 THR C 2 30.576 -16.283 -14.383 1.00158.98 O ANISOU 3537 OG1 THR C 2 17835 16067 26502 2058 -3644 -1923 O ATOM 3538 CG2 THR C 2 32.056 -17.858 -13.359 1.00139.37 C ANISOU 3538 CG2 THR C 2 15611 13148 24196 3036 -4879 -2154 C ATOM 3539 N CYS C 3 28.975 -15.282 -10.864 1.00139.20 N ANISOU 3539 N CYS C 3 16864 12778 23246 414 -4350 -1844 N ATOM 3540 CA CYS C 3 28.087 -14.160 -10.607 1.00112.68 C ANISOU 3540 CA CYS C 3 13352 9483 19979 -328 -3944 -1980 C ATOM 3541 C CYS C 3 28.884 -12.868 -10.479 1.00115.13 C ANISOU 3541 C CYS C 3 12684 10169 20893 -443 -3958 -1974 C ATOM 3542 O CYS C 3 30.072 -12.872 -10.146 1.00125.36 O ANISOU 3542 O CYS C 3 13609 11652 22368 -100 -4366 -1892 O ATOM 3543 CB CYS C 3 27.267 -14.378 -9.329 1.00118.05 C ANISOU 3543 CB CYS C 3 14887 9882 20085 -1020 -4137 -2180 C ATOM 3544 SG CYS C 3 26.090 -15.748 -9.375 1.00130.22 S ANISOU 3544 SG CYS C 3 17659 10982 20837 -1142 -4074 -2215 S ATOM 3545 N VAL C 4 28.206 -11.752 -10.749 1.00114.72 N ANISOU 3545 N VAL C 4 13777 11942 17869 2931 -1493 -2562 N ATOM 3546 CA VAL C 4 28.776 -10.446 -10.448 1.00102.41 C ANISOU 3546 CA VAL C 4 12304 10946 15662 2539 -1552 -2363 C ATOM 3547 C VAL C 4 28.806 -10.264 -8.938 1.00103.43 C ANISOU 3547 C VAL C 4 12748 10930 15623 2445 -1706 -1819 C ATOM 3548 O VAL C 4 27.838 -10.586 -8.236 1.00 95.50 O ANISOU 3548 O VAL C 4 12142 9348 14795 2463 -1645 -1549 O ATOM 3549 CB VAL C 4 27.965 -9.330 -11.128 1.00109.97 C ANISOU 3549 CB VAL C 4 13522 12035 16228 2162 -1319 -2522 C ATOM 3550 CG1 VAL C 4 28.525 -7.955 -10.766 1.00108.93 C ANISOU 3550 CG1 VAL C 4 13494 12386 15510 1721 -1286 -2312 C ATOM 3551 CG2 VAL C 4 27.935 -9.529 -12.637 1.00 98.47 C ANISOU 3551 CG2 VAL C 4 11753 10805 14856 2365 -1172 -3065 C ATOM 3552 N LYS C 5 29.925 -9.756 -8.426 1.00111.33 N ANISOU 3552 N LYS C 5 13543 12477 16282 2367 -1896 -1694 N ATOM 3553 CA LYS C 5 30.131 -9.585 -6.994 1.00117.10 C ANISOU 3553 CA LYS C 5 14477 13238 16777 2366 -2099 -1245 C ATOM 3554 C LYS C 5 30.232 -8.100 -6.677 1.00118.30 C ANISOU 3554 C LYS C 5 14754 13823 16373 1804 -2065 -1215 C ATOM 3555 O LYS C 5 31.008 -7.377 -7.310 1.00118.13 O ANISOU 3555 O LYS C 5 14404 14328 16152 1564 -1998 -1518 O ATOM 3556 CB LYS C 5 31.390 -10.324 -6.530 1.00117.65 C ANISOU 3556 CB LYS C 5 14134 13636 16932 2835 -2389 -1191 C ATOM 3557 CG LYS C 5 31.604 -10.313 -5.024 1.00127.52 C ANISOU 3557 CG LYS C 5 15576 14971 17905 3009 -2631 -733 C ATOM 3558 CD LYS C 5 30.537 -11.134 -4.318 1.00131.13 C ANISOU 3558 CD LYS C 5 16540 14641 18644 3298 -2516 -282 C ATOM 3559 CE LYS C 5 30.733 -11.137 -2.809 1.00139.26 C ANISOU 3559 CE LYS C 5 17800 15789 19325 3562 -2733 224 C ATOM 3560 NZ LYS C 5 31.977 -11.846 -2.400 1.00154.03 N ANISOU 3560 NZ LYS C 5 19274 18091 21161 4186 -3030 284 N ATOM 3561 N SER C 6 29.450 -7.650 -5.697 1.00111.72 N ANISOU 3561 N SER C 6 14388 12736 15325 1591 -2064 -860 N ATOM 3562 CA SER C 6 29.381 -6.228 -5.371 1.00101.00 C ANISOU 3562 CA SER C 6 13190 11692 13493 1027 -1982 -841 C ATOM 3563 C SER C 6 28.908 -6.068 -3.936 1.00100.18 C ANISOU 3563 C SER C 6 13472 11421 13169 988 -2129 -410 C ATOM 3564 O SER C 6 27.824 -6.545 -3.585 1.00107.28 O ANISOU 3564 O SER C 6 14808 11714 14240 1093 -2049 -131 O ATOM 3565 CB SER C 6 28.441 -5.495 -6.331 1.00116.14 C ANISOU 3565 CB SER C 6 15375 13407 15348 654 -1632 -1004 C ATOM 3566 OG SER C 6 28.301 -4.132 -5.970 1.00142.23 O ANISOU 3566 OG SER C 6 18885 16920 18237 120 -1494 -941 O ATOM 3567 N ASN C 7 29.716 -5.401 -3.111 1.00106.84 N ANISOU 3567 N ASN C 7 14130 12817 13649 846 -2326 -399 N ATOM 3568 CA ASN C 7 29.324 -5.047 -1.754 1.00110.98 C ANISOU 3568 CA ASN C 7 14989 13321 13858 775 -2468 -46 C ATOM 3569 C ASN C 7 29.616 -3.585 -1.439 1.00127.92 C ANISOU 3569 C ASN C 7 17052 15951 15601 179 -2418 -243 C ATOM 3570 O ASN C 7 29.414 -3.157 -0.297 1.00130.70 O ANISOU 3570 O ASN C 7 17603 16414 15643 85 -2560 -37 O ATOM 3571 CB ASN C 7 30.022 -5.953 -0.734 1.00128.43 C ANISOU 3571 CB ASN C 7 17039 15745 16015 1407 -2831 197 C ATOM 3572 CG ASN C 7 29.593 -7.402 -0.851 1.00159.02 C ANISOU 3572 CG ASN C 7 21093 18994 20334 2001 -2788 485 C ATOM 3573 OD1 ASN C 7 30.392 -8.272 -1.197 1.00174.98 O ANISOU 3573 OD1 ASN C 7 22743 21147 22595 2470 -2911 379 O ATOM 3574 ND2 ASN C 7 28.325 -7.669 -0.561 1.00158.78 N ANISOU 3574 ND2 ASN C 7 21617 18252 20461 1975 -2578 822 N ATOM 3575 N SER C 8 30.079 -2.811 -2.417 1.00131.39 N ANISOU 3575 N SER C 8 17206 16661 16055 -212 -2176 -642 N ATOM 3576 CA SER C 8 30.422 -1.411 -2.213 1.00138.36 C ANISOU 3576 CA SER C 8 17966 17942 16663 -805 -2015 -882 C ATOM 3577 C SER C 8 29.909 -0.610 -3.405 1.00139.47 C ANISOU 3577 C SER C 8 18287 17848 16857 -1236 -1518 -1021 C ATOM 3578 O SER C 8 29.196 -1.129 -4.271 1.00136.39 O ANISOU 3578 O SER C 8 18134 17040 16645 -1053 -1371 -937 O ATOM 3579 CB SER C 8 31.935 -1.244 -2.014 1.00161.80 C ANISOU 3579 CB SER C 8 20237 21653 19588 -767 -2203 -1297 C ATOM 3580 OG SER C 8 32.277 0.121 -1.856 1.00177.56 O ANISOU 3580 OG SER C 8 22061 23984 21422 -1386 -1965 -1613 O ATOM 3581 N ILE C 9 30.283 0.669 -3.447 1.00134.32 N ANISOU 3581 N ILE C 9 17504 17481 16049 -1780 -1231 -1261 N ATOM 3582 CA ILE C 9 29.854 1.581 -4.500 1.00120.36 C ANISOU 3582 CA ILE C 9 15943 15522 14267 -2163 -683 -1340 C ATOM 3583 C ILE C 9 30.889 1.692 -5.616 1.00124.12 C ANISOU 3583 C ILE C 9 15939 16318 14903 -2161 -403 -1710 C ATOM 3584 O ILE C 9 30.746 2.537 -6.506 1.00118.70 O ANISOU 3584 O ILE C 9 15373 15553 14175 -2445 128 -1784 O ATOM 3585 CB ILE C 9 29.512 2.964 -3.918 1.00114.83 C ANISOU 3585 CB ILE C 9 15472 14811 13348 -2769 -402 -1327 C ATOM 3586 CG1 ILE C 9 30.673 3.517 -3.080 1.00123.94 C ANISOU 3586 CG1 ILE C 9 16086 16531 14474 -3035 -515 -1683 C ATOM 3587 CG2 ILE C 9 28.252 2.888 -3.072 1.00115.88 C ANISOU 3587 CG2 ILE C 9 16183 14529 13316 -2774 -581 -929 C ATOM 3588 CD1 ILE C 9 31.688 4.337 -3.852 1.00118.76 C ANISOU 3588 CD1 ILE C 9 14965 16181 13977 -3391 -37 -2132 C ATOM 3589 N TRP C 10 31.925 0.862 -5.591 1.00125.61 N ANISOU 3589 N TRP C 10 15603 16864 15261 -1812 -719 -1924 N ATOM 3590 CA TRP C 10 33.017 0.937 -6.545 1.00137.68 C ANISOU 3590 CA TRP C 10 16612 18741 16959 -1814 -477 -2312 C ATOM 3591 C TRP C 10 32.765 -0.065 -7.675 1.00132.71 C ANISOU 3591 C TRP C 10 16028 17900 16496 -1333 -478 -2264 C ATOM 3592 O TRP C 10 31.678 -0.639 -7.791 1.00140.85 O ANISOU 3592 O TRP C 10 17496 18493 17528 -1085 -580 -1984 O ATOM 3593 CB TRP C 10 34.343 0.708 -5.810 1.00151.38 C ANISOU 3593 CB TRP C 10 17685 21062 18771 -1734 -829 -2657 C ATOM 3594 CG TRP C 10 35.571 1.056 -6.602 1.00166.79 C ANISOU 3594 CG TRP C 10 19034 23423 20914 -1889 -518 -3146 C ATOM 3595 CD1 TRP C 10 36.458 0.188 -7.171 1.00181.15 C ANISOU 3595 CD1 TRP C 10 20374 25514 22941 -1491 -688 -3384 C ATOM 3596 CD2 TRP C 10 36.039 2.372 -6.917 1.00170.49 C ANISOU 3596 CD2 TRP C 10 19318 24033 21428 -2495 80 -3465 C ATOM 3597 NE1 TRP C 10 37.453 0.884 -7.815 1.00187.93 N ANISOU 3597 NE1 TRP C 10 20753 26697 23954 -1818 -247 -3839 N ATOM 3598 CE2 TRP C 10 37.217 2.227 -7.675 1.00183.69 C ANISOU 3598 CE2 TRP C 10 20389 26062 23343 -2439 262 -3893 C ATOM 3599 CE3 TRP C 10 35.577 3.660 -6.629 1.00161.60 C ANISOU 3599 CE3 TRP C 10 18473 22729 20199 -3082 528 -3435 C ATOM 3600 CZ2 TRP C 10 37.940 3.321 -8.150 1.00182.48 C ANISOU 3600 CZ2 TRP C 10 19915 26063 23355 -2958 918 -4287 C ATOM 3601 CZ3 TRP C 10 36.295 4.744 -7.100 1.00157.81 C ANISOU 3601 CZ3 TRP C 10 17679 22385 19896 -3589 1186 -3818 C ATOM 3602 CH2 TRP C 10 37.463 4.568 -7.852 1.00167.48 C ANISOU 3602 CH2 TRP C 10 18310 23938 21385 -3528 1397 -4238 C ATOM 3603 N PHE C 11 33.766 -0.263 -8.529 1.00135.19 N ANISOU 3603 N PHE C 11 15855 18535 16975 -1212 -342 -2594 N ATOM 3604 CA PHE C 11 33.629 -1.179 -9.653 1.00132.89 C ANISOU 3604 CA PHE C 11 15529 18120 16842 -756 -331 -2632 C ATOM 3605 C PHE C 11 33.303 -2.586 -9.158 1.00129.21 C ANISOU 3605 C PHE C 11 15095 17434 16564 -224 -872 -2462 C ATOM 3606 O PHE C 11 33.852 -3.034 -8.143 1.00123.36 O ANISOU 3606 O PHE C 11 14128 16876 15868 -74 -1277 -2430 O ATOM 3607 CB PHE C 11 34.914 -1.209 -10.482 1.00138.05 C ANISOU 3607 CB PHE C 11 15586 19213 17655 -703 -143 -3035 C ATOM 3608 CG PHE C 11 35.187 0.062 -11.233 1.00148.29 C ANISOU 3608 CG PHE C 11 16885 20623 18838 -1145 544 -3180 C ATOM 3609 CD1 PHE C 11 34.572 0.308 -12.449 1.00149.88 C ANISOU 3609 CD1 PHE C 11 17406 20636 18904 -1038 999 -3089 C ATOM 3610 CD2 PHE C 11 36.063 1.008 -10.727 1.00161.04 C ANISOU 3610 CD2 PHE C 11 18166 22535 20488 -1631 775 -3431 C ATOM 3611 CE1 PHE C 11 34.824 1.474 -13.146 1.00162.41 C ANISOU 3611 CE1 PHE C 11 19050 22289 20369 -1372 1715 -3148 C ATOM 3612 CE2 PHE C 11 36.318 2.177 -11.418 1.00168.42 C ANISOU 3612 CE2 PHE C 11 19116 23482 21393 -2044 1521 -3549 C ATOM 3613 CZ PHE C 11 35.698 2.410 -12.629 1.00170.98 C ANISOU 3613 CZ PHE C 11 19830 23575 21559 -1896 2015 -3358 C ATOM 3614 N PRO C 12 32.421 -3.307 -9.840 1.00126.25 N ANISOU 3614 N PRO C 12 14984 16675 16310 99 -860 -2372 N ATOM 3615 CA PRO C 12 32.106 -4.678 -9.433 1.00127.61 C ANISOU 3615 CA PRO C 12 15174 16543 16769 595 -1258 -2237 C ATOM 3616 C PRO C 12 33.151 -5.669 -9.922 1.00126.50 C ANISOU 3616 C PRO C 12 14476 16663 16926 1027 -1444 -2505 C ATOM 3617 O PRO C 12 33.885 -5.429 -10.882 1.00117.76 O ANISOU 3617 O PRO C 12 13012 15904 15826 995 -1233 -2826 O ATOM 3618 CB PRO C 12 30.752 -4.940 -10.100 1.00120.70 C ANISOU 3618 CB PRO C 12 14723 15176 15962 706 -1089 -2177 C ATOM 3619 CG PRO C 12 30.775 -4.072 -11.313 1.00128.19 C ANISOU 3619 CG PRO C 12 15660 16359 16688 518 -658 -2401 C ATOM 3620 CD PRO C 12 31.544 -2.835 -10.927 1.00128.89 C ANISOU 3620 CD PRO C 12 15652 16810 16509 31 -450 -2390 C ATOM 3621 N THR C 13 33.199 -6.804 -9.235 1.00131.05 N ANISOU 3621 N THR C 13 14999 17040 17752 1461 -1806 -2345 N ATOM 3622 CA THR C 13 34.051 -7.927 -9.595 1.00131.22 C ANISOU 3622 CA THR C 13 14545 17202 18110 1958 -2009 -2544 C ATOM 3623 C THR C 13 33.170 -9.136 -9.915 1.00132.46 C ANISOU 3623 C THR C 13 14893 16753 18682 2379 -2028 -2473 C ATOM 3624 O THR C 13 31.940 -9.039 -9.967 1.00126.74 O ANISOU 3624 O THR C 13 14618 15563 17977 2258 -1869 -2344 O ATOM 3625 CB THR C 13 35.051 -8.225 -8.474 1.00128.29 C ANISOU 3625 CB THR C 13 13876 17178 17688 2181 -2389 -2447 C ATOM 3626 OG1 THR C 13 34.343 -8.553 -7.272 1.00130.86 O ANISOU 3626 OG1 THR C 13 14629 17129 17961 2339 -2577 -1990 O ATOM 3627 CG2 THR C 13 35.941 -7.016 -8.219 1.00124.20 C ANISOU 3627 CG2 THR C 13 13065 17288 16837 1728 -2340 -2674 C ATOM 3628 N SER C 14 33.809 -10.281 -10.137 1.00131.47 N ANISOU 3628 N SER C 14 14390 16630 18932 2872 -2199 -2606 N ATOM 3629 CA SER C 14 33.115 -11.524 -10.444 1.00119.03 C ANISOU 3629 CA SER C 14 12894 14460 17870 3289 -2173 -2619 C ATOM 3630 C SER C 14 33.533 -12.604 -9.456 1.00127.52 C ANISOU 3630 C SER C 14 13911 15318 19224 3797 -2426 -2313 C ATOM 3631 O SER C 14 34.714 -12.721 -9.112 1.00147.26 O ANISOU 3631 O SER C 14 16037 18295 21619 4008 -2667 -2327 O ATOM 3632 CB SER C 14 33.406 -11.982 -11.878 1.00110.53 C ANISOU 3632 CB SER C 14 11409 13528 17061 3471 -2045 -3128 C ATOM 3633 OG SER C 14 34.771 -12.324 -12.037 1.00145.05 O ANISOU 3633 OG SER C 14 15240 18374 21496 3709 -2220 -3310 O ATOM 3634 N GLU C 15 32.559 -13.387 -9.001 1.00120.77 N ANISOU 3634 N GLU C 15 13422 13738 18727 4022 -2337 -2044 N ATOM 3635 CA GLU C 15 32.786 -14.468 -8.051 1.00126.83 C ANISOU 3635 CA GLU C 15 14245 14159 19785 4576 -2461 -1659 C ATOM 3636 C GLU C 15 32.422 -15.797 -8.694 1.00139.37 C ANISOU 3636 C GLU C 15 15706 15126 22121 4983 -2265 -1854 C ATOM 3637 O GLU C 15 31.377 -15.911 -9.343 1.00133.96 O ANISOU 3637 O GLU C 15 15167 13984 21746 4802 -2002 -2105 O ATOM 3638 CB GLU C 15 31.958 -14.274 -6.778 1.00129.26 C ANISOU 3638 CB GLU C 15 15139 14058 19914 4521 -2429 -1097 C ATOM 3639 CG GLU C 15 32.195 -15.350 -5.728 1.00141.12 C ANISOU 3639 CG GLU C 15 16769 15212 21640 5177 -2497 -604 C ATOM 3640 CD GLU C 15 31.303 -15.197 -4.514 1.00147.13 C ANISOU 3640 CD GLU C 15 18145 15528 22229 5158 -2399 -30 C ATOM 3641 OE1 GLU C 15 30.452 -14.284 -4.509 1.00153.53 O ANISOU 3641 OE1 GLU C 15 19269 16270 22796 4601 -2293 -53 O ATOM 3642 OE2 GLU C 15 31.449 -15.994 -3.564 1.00152.71 O ANISOU 3642 OE2 GLU C 15 19038 15955 23030 5737 -2404 463 O ATOM 3643 N ASP C 16 33.280 -16.798 -8.511 1.00137.74 N ANISOU 3643 N ASP C 16 15200 14917 22216 5550 -2386 -1784 N ATOM 3644 CA ASP C 16 32.944 -18.163 -8.891 1.00130.82 C ANISOU 3644 CA ASP C 16 14236 13337 22134 5990 -2151 -1896 C ATOM 3645 C ASP C 16 32.110 -18.784 -7.778 1.00133.12 C ANISOU 3645 C ASP C 16 15061 12806 22712 6249 -1929 -1319 C ATOM 3646 O ASP C 16 32.544 -18.826 -6.622 1.00149.82 O ANISOU 3646 O ASP C 16 17385 15022 24518 6567 -2083 -756 O ATOM 3647 CB ASP C 16 34.207 -18.984 -9.142 1.00151.58 C ANISOU 3647 CB ASP C 16 16346 16262 24987 6521 -2329 -2029 C ATOM 3648 CG ASP C 16 34.988 -18.503 -10.349 1.00155.47 C ANISOU 3648 CG ASP C 16 16290 17478 25303 6290 -2465 -2641 C ATOM 3649 OD1 ASP C 16 34.372 -17.926 -11.267 1.00144.02 O ANISOU 3649 OD1 ASP C 16 14839 16085 23796 5856 -2310 -3038 O ATOM 3650 OD2 ASP C 16 36.220 -18.708 -10.381 1.00155.58 O ANISOU 3650 OD2 ASP C 16 15873 18018 25223 6581 -2709 -2725 O ATOM 3651 N CYS C 17 30.917 -19.251 -8.117 1.00129.90 N ANISOU 3651 N CYS C 17 14859 11616 22883 6138 -1549 -1484 N ATOM 3652 CA CYS C 17 30.019 -19.791 -7.102 1.00136.68 C ANISOU 3652 CA CYS C 17 16248 11613 24072 6318 -1232 -959 C ATOM 3653 C CYS C 17 30.549 -21.110 -6.557 1.00151.78 C ANISOU 3653 C CYS C 17 18126 13042 26500 7065 -1081 -585 C ATOM 3654 O CYS C 17 30.957 -21.980 -7.335 1.00142.30 O ANISOU 3654 O CYS C 17 16554 11818 25696 7249 -944 -939 O ATOM 3655 CB CYS C 17 28.617 -19.993 -7.665 1.00161.68 C ANISOU 3655 CB CYS C 17 19566 14074 27791 5984 -817 -1343 C ATOM 3656 SG CYS C 17 27.702 -18.471 -7.892 1.00177.18 S ANISOU 3656 SG CYS C 17 21799 16386 29136 5232 -912 -1538 S ATOM 3657 N PRO C 18 30.559 -21.298 -5.241 1.00141.38 N ANISOU 3657 N PRO C 18 20763 12515 20440 5504 -3477 -45 N ATOM 3658 CA PRO C 18 30.902 -22.606 -4.681 1.00136.74 C ANISOU 3658 CA PRO C 18 20796 11395 19765 5899 -3299 60 C ATOM 3659 C PRO C 18 29.770 -23.595 -4.906 1.00140.24 C ANISOU 3659 C PRO C 18 21327 10962 20995 5729 -2828 -214 C ATOM 3660 O PRO C 18 28.647 -23.232 -5.264 1.00137.67 O ANISOU 3660 O PRO C 18 20669 10400 21238 5278 -2590 -465 O ATOM 3661 CB PRO C 18 31.105 -22.313 -3.193 1.00139.37 C ANISOU 3661 CB PRO C 18 21805 11512 19636 5959 -3047 497 C ATOM 3662 CG PRO C 18 30.232 -21.130 -2.934 1.00140.78 C ANISOU 3662 CG PRO C 18 21797 11682 20009 5428 -2850 500 C ATOM 3663 CD PRO C 18 30.270 -20.303 -4.193 1.00138.94 C ANISOU 3663 CD PRO C 18 20723 12119 19949 5203 -3264 228 C ATOM 3664 N ASP C 19 30.084 -24.870 -4.690 1.00135.29 N ANISOU 3664 N ASP C 19 21132 9829 20444 6108 -2690 -178 N ATOM 3665 CA ASP C 19 29.083 -25.917 -4.839 1.00139.76 C ANISOU 3665 CA ASP C 19 21782 9435 21884 5960 -2218 -441 C ATOM 3666 C ASP C 19 27.943 -25.705 -3.852 1.00151.78 C ANISOU 3666 C ASP C 19 23662 10198 23811 5528 -1500 -181 C ATOM 3667 O ASP C 19 28.169 -25.424 -2.671 1.00152.80 O ANISOU 3667 O ASP C 19 24368 10244 23443 5638 -1231 343 O ATOM 3668 CB ASP C 19 29.717 -27.292 -4.629 1.00147.71 C ANISOU 3668 CB ASP C 19 23265 9967 22890 6482 -2148 -348 C ATOM 3669 CG ASP C 19 30.641 -27.687 -5.763 1.00150.24 C ANISOU 3669 CG ASP C 19 23168 10933 22983 6912 -2817 -720 C ATOM 3670 OD1 ASP C 19 30.416 -27.228 -6.903 1.00141.91 O ANISOU 3670 OD1 ASP C 19 21390 10424 22106 6770 -3200 -1190 O ATOM 3671 OD2 ASP C 19 31.588 -28.464 -5.518 1.00163.51 O ANISOU 3671 OD2 ASP C 19 25244 12608 24275 7451 -2946 -530 O ATOM 3672 N GLY C 20 26.713 -25.834 -4.345 1.00165.33 N ANISOU 3672 N GLY C 20 25001 11405 26410 5082 -1203 -575 N ATOM 3673 CA GLY C 20 25.525 -25.643 -3.548 1.00171.29 C ANISOU 3673 CA GLY C 20 25980 11448 27656 4643 -501 -372 C ATOM 3674 C GLY C 20 24.841 -24.307 -3.743 1.00166.10 C ANISOU 3674 C GLY C 20 24886 11259 26966 4174 -567 -493 C ATOM 3675 O GLY C 20 23.681 -24.157 -3.342 1.00172.06 O ANISOU 3675 O GLY C 20 25657 11451 28269 3760 -18 -470 O ATOM 3676 N GLN C 21 25.525 -23.336 -4.343 1.00150.27 N ANISOU 3676 N GLN C 21 22478 10247 24371 4241 -1189 -590 N ATOM 3677 CA GLN C 21 24.971 -22.011 -4.612 1.00137.35 C ANISOU 3677 CA GLN C 21 20397 9097 22694 3846 -1283 -683 C ATOM 3678 C GLN C 21 24.819 -21.872 -6.124 1.00140.38 C ANISOU 3678 C GLN C 21 19956 10019 23363 3826 -1730 -1260 C ATOM 3679 O GLN C 21 25.803 -21.659 -6.838 1.00147.64 O ANISOU 3679 O GLN C 21 20570 11711 23815 4158 -2293 -1311 O ATOM 3680 CB GLN C 21 25.867 -20.920 -4.035 1.00137.22 C ANISOU 3680 CB GLN C 21 20552 9753 21832 3959 -1585 -284 C ATOM 3681 CG GLN C 21 25.944 -20.914 -2.519 1.00152.38 C ANISOU 3681 CG GLN C 21 23250 11270 23379 4052 -1183 220 C ATOM 3682 CD GLN C 21 26.857 -19.825 -1.992 1.00165.28 C ANISOU 3682 CD GLN C 21 24969 13593 24235 4187 -1577 468 C ATOM 3683 OE1 GLN C 21 27.491 -19.104 -2.763 1.00170.92 O ANISOU 3683 OE1 GLN C 21 25157 15037 24750 4182 -2118 325 O ATOM 3684 NE2 GLN C 21 26.930 -19.701 -0.672 1.00175.41 N ANISOU 3684 NE2 GLN C 21 26889 14654 25104 4342 -1299 834 N ATOM 3685 N ASN C 22 23.583 -21.982 -6.608 1.00142.26 N ANISOU 3685 N ASN C 22 19808 9893 24353 3483 -1471 -1693 N ATOM 3686 CA ASN C 22 23.303 -22.025 -8.038 1.00140.47 C ANISOU 3686 CA ASN C 22 18800 10131 24441 3559 -1862 -2335 C ATOM 3687 C ASN C 22 22.478 -20.826 -8.494 1.00136.03 C ANISOU 3687 C ASN C 22 17707 10022 23957 3231 -1859 -2484 C ATOM 3688 O ASN C 22 21.684 -20.935 -9.430 1.00149.47 O ANISOU 3688 O ASN C 22 18813 11821 26158 3174 -1935 -3074 O ATOM 3689 CB ASN C 22 22.591 -23.327 -8.403 1.00135.90 C ANISOU 3689 CB ASN C 22 18100 8779 24758 3538 -1662 -2895 C ATOM 3690 CG ASN C 22 23.488 -24.542 -8.269 1.00142.48 C ANISOU 3690 CG ASN C 22 19327 9274 25534 3966 -1772 -2844 C ATOM 3691 OD1 ASN C 22 24.651 -24.519 -8.674 1.00151.78 O ANISOU 3691 OD1 ASN C 22 20477 11143 26049 4419 -2283 -2751 O ATOM 3692 ND2 ASN C 22 22.953 -25.611 -7.692 1.00157.07 N ANISOU 3692 ND2 ASN C 22 21533 10136 28009 3802 -1233 -2837 N ATOM 3693 N LEU C 23 22.652 -19.675 -7.844 1.00121.17 N ANISOU 3693 N LEU C 23 16019 8427 21594 3051 -1789 -1994 N ATOM 3694 CA LEU C 23 21.893 -18.481 -8.186 1.00120.89 C ANISOU 3694 CA LEU C 23 15538 8776 21620 2753 -1746 -2064 C ATOM 3695 C LEU C 23 22.768 -17.242 -8.078 1.00119.95 C ANISOU 3695 C LEU C 23 15381 9378 20817 2831 -2043 -1616 C ATOM 3696 O LEU C 23 23.701 -17.183 -7.272 1.00110.60 O ANISOU 3696 O LEU C 23 14673 8187 19164 2954 -2123 -1197 O ATOM 3697 CB LEU C 23 20.659 -18.303 -7.287 1.00116.54 C ANISOU 3697 CB LEU C 23 15267 7496 21518 2265 -1122 -1990 C ATOM 3698 CG LEU C 23 19.498 -19.283 -7.443 1.00134.01 C ANISOU 3698 CG LEU C 23 17339 8957 24623 2048 -735 -2467 C ATOM 3699 CD1 LEU C 23 18.434 -19.015 -6.389 1.00141.14 C ANISOU 3699 CD1 LEU C 23 18579 9185 25865 1599 -69 -2222 C ATOM 3700 CD2 LEU C 23 18.905 -19.194 -8.842 1.00139.48 C ANISOU 3700 CD2 LEU C 23 17185 10131 25679 2102 -1042 -3161 C ATOM 3701 N CYS C 24 22.453 -16.258 -8.915 1.00116.48 N ANISOU 3701 N CYS C 24 14334 9558 20367 2786 -2202 -1725 N ATOM 3702 CA CYS C 24 22.980 -14.905 -8.811 1.00107.56 C ANISOU 3702 CA CYS C 24 13076 8973 18819 2737 -2360 -1312 C ATOM 3703 C CYS C 24 21.862 -14.010 -8.298 1.00112.56 C ANISOU 3703 C CYS C 24 13749 9321 19698 2284 -1965 -1267 C ATOM 3704 O CYS C 24 20.746 -14.051 -8.826 1.00112.40 O ANISOU 3704 O CYS C 24 13385 9217 20104 2139 -1767 -1635 O ATOM 3705 CB CYS C 24 23.476 -14.395 -10.168 1.00105.40 C ANISOU 3705 CB CYS C 24 12065 9623 18358 3089 -2767 -1366 C ATOM 3706 SG CYS C 24 24.841 -15.322 -10.919 1.00113.24 S ANISOU 3706 SG CYS C 24 12907 11129 18990 3710 -3271 -1404 S ATOM 3707 N PHE C 25 22.147 -13.218 -7.268 1.00114.81 N ANISOU 3707 N PHE C 25 14433 9472 19717 2093 -1871 -869 N ATOM 3708 CA PHE C 25 21.154 -12.307 -6.719 1.00100.55 C ANISOU 3708 CA PHE C 25 12699 7419 18087 1706 -1518 -810 C ATOM 3709 C PHE C 25 21.603 -10.866 -6.909 1.00101.69 C ANISOU 3709 C PHE C 25 12528 8094 18017 1668 -1740 -546 C ATOM 3710 O PHE C 25 22.800 -10.563 -6.907 1.00 96.94 O ANISOU 3710 O PHE C 25 11892 7849 17094 1861 -2096 -299 O ATOM 3711 CB PHE C 25 20.882 -12.576 -5.225 1.00104.96 C ANISOU 3711 CB PHE C 25 14023 7277 18581 1527 -1138 -612 C ATOM 3712 CG PHE C 25 22.034 -12.240 -4.318 1.00116.50 C ANISOU 3712 CG PHE C 25 15922 8834 19507 1690 -1374 -264 C ATOM 3713 CD1 PHE C 25 23.001 -13.188 -4.021 1.00114.19 C ANISOU 3713 CD1 PHE C 25 15981 8483 18924 2018 -1552 -165 C ATOM 3714 CD2 PHE C 25 22.138 -10.980 -3.745 1.00108.80 C ANISOU 3714 CD2 PHE C 25 14996 8003 18341 1540 -1434 -84 C ATOM 3715 CE1 PHE C 25 24.057 -12.881 -3.181 1.00110.47 C ANISOU 3715 CE1 PHE C 25 15873 8157 17943 2213 -1804 92 C ATOM 3716 CE2 PHE C 25 23.192 -10.666 -2.908 1.00120.28 C ANISOU 3716 CE2 PHE C 25 16792 9563 19347 1711 -1708 125 C ATOM 3717 CZ PHE C 25 24.153 -11.619 -2.625 1.00121.19 C ANISOU 3717 CZ PHE C 25 17231 9678 19138 2057 -1900 206 C ATOM 3718 N LYS C 26 20.620 -9.985 -7.080 1.00104.32 N ANISOU 3718 N LYS C 26 12602 8447 18587 1416 -1508 -604 N ATOM 3719 CA LYS C 26 20.827 -8.542 -7.150 1.00 94.04 C ANISOU 3719 CA LYS C 26 11033 7485 17213 1321 -1605 -344 C ATOM 3720 C LYS C 26 19.853 -7.924 -6.156 1.00104.66 C ANISOU 3720 C LYS C 26 12740 8345 18679 961 -1224 -333 C ATOM 3721 O LYS C 26 18.636 -7.977 -6.363 1.00109.11 O ANISOU 3721 O LYS C 26 13181 8739 19536 795 -894 -558 O ATOM 3722 CB LYS C 26 20.600 -8.022 -8.571 1.00106.52 C ANISOU 3722 CB LYS C 26 11841 9700 18931 1501 -1701 -399 C ATOM 3723 CG LYS C 26 20.986 -6.571 -8.798 1.00103.29 C ANISOU 3723 CG LYS C 26 11081 9652 18514 1473 -1787 -39 C ATOM 3724 CD LYS C 26 20.853 -6.210 -10.272 1.00104.96 C ANISOU 3724 CD LYS C 26 10531 10560 18788 1800 -1845 -13 C ATOM 3725 CE LYS C 26 21.252 -4.769 -10.542 1.00115.63 C ANISOU 3725 CE LYS C 26 11499 12216 20219 1798 -1851 438 C ATOM 3726 NZ LYS C 26 21.124 -4.418 -11.983 1.00113.92 N ANISOU 3726 NZ LYS C 26 10548 12731 20004 2226 -1841 556 N ATOM 3727 N ARG C 27 20.382 -7.357 -5.073 1.00103.11 N ANISOU 3727 N ARG C 27 12971 7953 18254 876 -1288 -115 N ATOM 3728 CA ARG C 27 19.607 -7.125 -3.858 1.00101.68 C ANISOU 3728 CA ARG C 27 13328 7254 18053 653 -937 -116 C ATOM 3729 C ARG C 27 19.711 -5.666 -3.432 1.00119.44 C ANISOU 3729 C ARG C 27 15524 9583 20275 509 -1032 11 C ATOM 3730 O ARG C 27 20.810 -5.172 -3.159 1.00135.99 O ANISOU 3730 O ARG C 27 17623 11850 22196 606 -1403 140 O ATOM 3731 CB ARG C 27 20.097 -8.069 -2.751 1.00 98.30 C ANISOU 3731 CB ARG C 27 13592 6451 17305 811 -897 -40 C ATOM 3732 CG ARG C 27 19.311 -8.076 -1.449 1.00113.49 C ANISOU 3732 CG ARG C 27 16131 7859 19132 712 -467 12 C ATOM 3733 CD ARG C 27 19.990 -7.248 -0.373 1.00148.50 C ANISOU 3733 CD ARG C 27 20930 12335 23158 819 -697 127 C ATOM 3734 NE ARG C 27 19.348 -7.421 0.928 1.00155.19 N ANISOU 3734 NE ARG C 27 22426 12759 23780 880 -290 202 N ATOM 3735 CZ ARG C 27 19.668 -8.378 1.793 1.00120.36 C ANISOU 3735 CZ ARG C 27 18602 8108 19022 1186 -143 351 C ATOM 3736 NH1 ARG C 27 19.036 -8.466 2.954 1.00121.00 N ANISOU 3736 NH1 ARG C 27 19245 7856 18874 1308 284 482 N ATOM 3737 NH2 ARG C 27 20.625 -9.244 1.496 1.00143.48 N ANISOU 3737 NH2 ARG C 27 21558 11152 21805 1425 -401 401 N ATOM 3738 N TRP C 28 18.564 -4.982 -3.379 1.00103.12 N ANISOU 3738 N TRP C 28 13378 7373 18431 282 -706 -59 N ATOM 3739 CA TRP C 28 18.448 -3.645 -2.800 1.00 93.91 C ANISOU 3739 CA TRP C 28 12258 6142 17281 135 -721 9 C ATOM 3740 C TRP C 28 17.792 -3.781 -1.430 1.00100.36 C ANISOU 3740 C TRP C 28 13748 6486 17897 77 -411 -47 C ATOM 3741 O TRP C 28 16.611 -4.130 -1.334 1.00119.98 O ANISOU 3741 O TRP C 28 16337 8728 20522 -46 39 -128 O ATOM 3742 CB TRP C 28 17.618 -2.719 -3.688 1.00 92.01 C ANISOU 3742 CB TRP C 28 11469 6107 17383 -6 -556 1 C ATOM 3743 CG TRP C 28 18.260 -2.278 -4.968 1.00 93.33 C ANISOU 3743 CG TRP C 28 10954 6793 17715 131 -813 156 C ATOM 3744 CD1 TRP C 28 19.025 -1.164 -5.159 1.00 90.49 C ANISOU 3744 CD1 TRP C 28 10278 6610 17493 133 -1050 384 C ATOM 3745 CD2 TRP C 28 18.162 -2.922 -6.245 1.00110.27 C ANISOU 3745 CD2 TRP C 28 12612 9355 19930 333 -825 106 C ATOM 3746 NE1 TRP C 28 19.418 -1.078 -6.474 1.00 89.64 N ANISOU 3746 NE1 TRP C 28 9530 7016 17513 342 -1152 571 N ATOM 3747 CE2 TRP C 28 18.904 -2.147 -7.160 1.00108.87 C ANISOU 3747 CE2 TRP C 28 11861 9652 19852 504 -1044 381 C ATOM 3748 CE3 TRP C 28 17.528 -4.082 -6.701 1.00111.30 C ANISOU 3748 CE3 TRP C 28 12707 9494 20086 414 -677 -170 C ATOM 3749 CZ2 TRP C 28 19.028 -2.494 -8.503 1.00111.87 C ANISOU 3749 CZ2 TRP C 28 11670 10598 20236 826 -1117 415 C ATOM 3750 CZ3 TRP C 28 17.653 -4.425 -8.037 1.00102.18 C ANISOU 3750 CZ3 TRP C 28 10971 8878 18977 705 -816 -239 C ATOM 3751 CH2 TRP C 28 18.396 -3.634 -8.921 1.00105.97 C ANISOU 3751 CH2 TRP C 28 10919 9909 19436 945 -1033 64 C ATOM 3752 N GLN C 29 18.547 -3.497 -0.374 1.00110.38 N ANISOU 3752 N GLN C 29 11462 9624 20852 2363 -275 -2015 N ATOM 3753 CA GLN C 29 18.057 -3.635 0.991 1.00116.19 C ANISOU 3753 CA GLN C 29 12964 9869 21312 2454 -201 -1922 C ATOM 3754 C GLN C 29 17.623 -2.276 1.524 1.00114.75 C ANISOU 3754 C GLN C 29 13189 9514 20899 2160 -183 -1890 C ATOM 3755 O GLN C 29 18.396 -1.313 1.482 1.00116.64 O ANISOU 3755 O GLN C 29 13304 9981 21034 1913 -487 -1882 O ATOM 3756 CB GLN C 29 19.129 -4.234 1.899 1.00122.06 C ANISOU 3756 CB GLN C 29 13926 10638 21812 2704 -645 -1828 C ATOM 3757 CG GLN C 29 18.650 -4.498 3.313 1.00132.06 C ANISOU 3757 CG GLN C 29 16075 11391 22710 2869 -547 -1692 C ATOM 3758 CD GLN C 29 19.730 -5.095 4.187 1.00141.93 C ANISOU 3758 CD GLN C 29 17585 12720 23623 3261 -1047 -1594 C ATOM 3759 OE1 GLN C 29 20.871 -5.260 3.757 1.00146.23 O ANISOU 3759 OE1 GLN C 29 17572 13750 24240 3394 -1508 -1692 O ATOM 3760 NE2 GLN C 29 19.375 -5.427 5.422 1.00157.76 N ANISOU 3760 NE2 GLN C 29 20445 14273 25221 3485 -960 -1433 N ATOM 3761 N TYR C 30 16.395 -2.206 2.032 1.00118.46 N ANISOU 3761 N TYR C 30 14135 9567 21308 2159 217 -1930 N ATOM 3762 CA TYR C 30 15.849 -0.962 2.562 1.00108.48 C ANISOU 3762 CA TYR C 30 13280 8092 19847 1923 275 -1938 C ATOM 3763 C TYR C 30 16.318 -0.735 3.995 1.00109.72 C ANISOU 3763 C TYR C 30 14030 8042 19615 1870 8 -1839 C ATOM 3764 O TYR C 30 16.269 -1.647 4.827 1.00143.13 O ANISOU 3764 O TYR C 30 18672 12040 23670 2087 52 -1772 O ATOM 3765 CB TYR C 30 14.322 -0.996 2.510 1.00 97.79 C ANISOU 3765 CB TYR C 30 12125 6588 18443 1922 785 -2078 C ATOM 3766 CG TYR C 30 13.641 0.237 3.067 1.00 88.92 C ANISOU 3766 CG TYR C 30 11429 5269 17087 1735 858 -2115 C ATOM 3767 CD1 TYR C 30 13.561 1.409 2.326 1.00 88.00 C ANISOU 3767 CD1 TYR C 30 11133 5244 17059 1660 810 -2134 C ATOM 3768 CD2 TYR C 30 13.077 0.224 4.335 1.00 97.79 C ANISOU 3768 CD2 TYR C 30 13189 6088 17880 1658 1000 -2128 C ATOM 3769 CE1 TYR C 30 12.932 2.533 2.836 1.00 88.72 C ANISOU 3769 CE1 TYR C 30 11653 5140 16918 1530 881 -2165 C ATOM 3770 CE2 TYR C 30 12.453 1.341 4.853 1.00104.69 C ANISOU 3770 CE2 TYR C 30 14420 6822 18534 1491 1054 -2192 C ATOM 3771 CZ TYR C 30 12.383 2.493 4.101 1.00 92.59 C ANISOU 3771 CZ TYR C 30 12684 5397 17100 1437 985 -2210 C ATOM 3772 OH TYR C 30 11.758 3.603 4.620 1.00112.41 O ANISOU 3772 OH TYR C 30 15583 7746 19382 1315 1038 -2272 O ATOM 3773 N ILE C 31 16.769 0.487 4.280 1.00117.42 N ANISOU 3773 N ILE C 31 15092 9092 20432 1591 -235 -1845 N ATOM 3774 CA ILE C 31 17.138 0.888 5.634 1.00117.14 C ANISOU 3774 CA ILE C 31 15577 8925 20005 1510 -487 -1839 C ATOM 3775 C ILE C 31 16.259 2.060 6.052 1.00128.50 C ANISOU 3775 C ILE C 31 17421 10043 21359 1242 -243 -1915 C ATOM 3776 O ILE C 31 15.495 1.970 7.019 1.00143.55 O ANISOU 3776 O ILE C 31 19890 11604 23051 1277 -42 -1937 O ATOM 3777 CB ILE C 31 18.628 1.266 5.737 1.00121.12 C ANISOU 3777 CB ILE C 31 15755 9870 20395 1389 -1026 -1918 C ATOM 3778 CG1 ILE C 31 19.525 0.070 5.414 1.00140.91 C ANISOU 3778 CG1 ILE C 31 17858 12722 22962 1736 -1324 -1895 C ATOM 3779 CG2 ILE C 31 18.945 1.809 7.123 1.00128.86 C ANISOU 3779 CG2 ILE C 31 17222 10792 20948 1303 -1292 -2006 C ATOM 3780 CD1 ILE C 31 19.946 -0.010 3.964 1.00147.21 C ANISOU 3780 CD1 ILE C 31 17906 13868 24158 1641 -1294 -1946 C ATOM 3781 N SER C 32 16.367 3.158 5.321 1.00125.78 N ANISOU 3781 N SER C 32 16838 9782 21171 982 -224 -1961 N ATOM 3782 CA SER C 32 15.609 4.383 5.546 1.00117.99 C ANISOU 3782 CA SER C 32 16212 8477 20140 770 -3 -2035 C ATOM 3783 C SER C 32 15.032 4.814 4.208 1.00114.68 C ANISOU 3783 C SER C 32 15512 8071 19989 838 259 -2012 C ATOM 3784 O SER C 32 15.439 4.304 3.159 1.00107.01 O ANISOU 3784 O SER C 32 14043 7408 19207 949 223 -1946 O ATOM 3785 CB SER C 32 16.518 5.464 6.162 1.00119.88 C ANISOU 3785 CB SER C 32 16592 8753 20205 391 -265 -2124 C ATOM 3786 OG SER C 32 17.502 5.912 5.254 1.00141.05 O ANISOU 3786 OG SER C 32 18822 11718 23053 164 -383 -2137 O ATOM 3787 N PRO C 33 14.052 5.769 4.203 1.00 97.81 N ANISOU 3787 N PRO C 33 13703 5621 17841 833 517 -2086 N ATOM 3788 CA PRO C 33 13.257 6.025 2.986 1.00115.51 C ANISOU 3788 CA PRO C 33 15743 7899 20247 1099 759 -2095 C ATOM 3789 C PRO C 33 14.000 6.045 1.655 1.00122.19 C ANISOU 3789 C PRO C 33 16135 9066 21226 1119 690 -1939 C ATOM 3790 O PRO C 33 13.668 5.262 0.759 1.00143.50 O ANISOU 3790 O PRO C 33 18410 12043 24072 1417 773 -1969 O ATOM 3791 CB PRO C 33 12.635 7.396 3.280 1.00111.14 C ANISOU 3791 CB PRO C 33 15681 7100 19445 1019 874 -2106 C ATOM 3792 CG PRO C 33 12.443 7.381 4.747 1.00101.75 C ANISOU 3792 CG PRO C 33 14896 5742 18023 828 830 -2212 C ATOM 3793 CD PRO C 33 13.619 6.637 5.314 1.00 96.30 C ANISOU 3793 CD PRO C 33 14072 5062 17455 647 575 -2198 C ATOM 3794 N ARG C 34 14.997 6.913 1.500 1.00100.45 N ANISOU 3794 N ARG C 34 13450 6293 18422 768 588 -1826 N ATOM 3795 CA ARG C 34 15.757 6.998 0.259 1.00116.41 C ANISOU 3795 CA ARG C 34 15098 8596 20536 704 595 -1696 C ATOM 3796 C ARG C 34 17.035 6.165 0.281 1.00121.59 C ANISOU 3796 C ARG C 34 15253 9666 21281 493 314 -1736 C ATOM 3797 O ARG C 34 17.909 6.366 -0.569 1.00121.81 O ANISOU 3797 O ARG C 34 14973 9933 21377 282 317 -1698 O ATOM 3798 CB ARG C 34 16.082 8.459 -0.060 1.00137.69 C ANISOU 3798 CB ARG C 34 18194 10983 23140 405 779 -1595 C ATOM 3799 CG ARG C 34 15.030 9.161 -0.907 1.00150.74 C ANISOU 3799 CG ARG C 34 20173 12395 24706 812 1058 -1467 C ATOM 3800 CD ARG C 34 13.797 9.564 -0.115 1.00133.83 C ANISOU 3800 CD ARG C 34 18481 9886 22484 1075 1135 -1596 C ATOM 3801 NE ARG C 34 14.062 10.578 0.900 1.00110.49 N ANISOU 3801 NE ARG C 34 16051 6481 19450 660 1174 -1645 N ATOM 3802 CZ ARG C 34 13.186 10.913 1.842 1.00107.47 C ANISOU 3802 CZ ARG C 34 16041 5798 18995 756 1209 -1807 C ATOM 3803 NH1 ARG C 34 12.000 10.317 1.882 1.00104.15 N ANISOU 3803 NH1 ARG C 34 15500 5698 18376 1201 1170 -1905 N ATOM 3804 NH2 ARG C 34 13.489 11.839 2.739 1.00104.71 N ANISOU 3804 NH2 ARG C 34 16126 5121 18537 352 1231 -1871 N ATOM 3805 N MET C 35 17.155 5.225 1.213 1.00116.27 N ANISOU 3805 N MET C 35 14517 9079 20582 581 90 -1825 N ATOM 3806 CA MET C 35 18.393 4.488 1.435 1.00119.03 C ANISOU 3806 CA MET C 35 14463 9810 20954 479 -255 -1903 C ATOM 3807 C MET C 35 18.204 3.026 1.056 1.00119.50 C ANISOU 3807 C MET C 35 14147 10099 21160 877 -294 -1877 C ATOM 3808 O MET C 35 17.394 2.321 1.667 1.00112.24 O ANISOU 3808 O MET C 35 13482 8966 20199 1145 -196 -1873 O ATOM 3809 CB MET C 35 18.838 4.606 2.890 1.00138.61 C ANISOU 3809 CB MET C 35 17259 12208 23197 338 -531 -2030 C ATOM 3810 CG MET C 35 20.166 3.951 3.176 1.00164.59 C ANISOU 3810 CG MET C 35 20132 15959 26446 325 -966 -2185 C ATOM 3811 SD MET C 35 21.511 4.761 2.300 1.00172.59 S ANISOU 3811 SD MET C 35 20600 17360 27615 -196 -1016 -2412 S ATOM 3812 CE MET C 35 22.656 3.397 2.184 1.00163.41 C ANISOU 3812 CE MET C 35 18746 16827 26515 92 -1487 -2586 C ATOM 3813 N TYR C 36 18.967 2.573 0.064 1.00120.70 N ANISOU 3813 N TYR C 36 13711 10661 21491 876 -382 -1896 N ATOM 3814 CA TYR C 36 18.954 1.184 -0.384 1.00107.20 C ANISOU 3814 CA TYR C 36 11577 9190 19964 1222 -416 -1912 C ATOM 3815 C TYR C 36 20.391 0.693 -0.477 1.00119.16 C ANISOU 3815 C TYR C 36 12595 11145 21534 1149 -796 -2029 C ATOM 3816 O TYR C 36 21.170 1.197 -1.293 1.00105.79 O ANISOU 3816 O TYR C 36 10502 9764 19931 861 -821 -2111 O ATOM 3817 CB TYR C 36 18.239 1.042 -1.728 1.00 97.99 C ANISOU 3817 CB TYR C 36 10083 8155 18992 1388 -102 -1895 C ATOM 3818 CG TYR C 36 16.741 1.206 -1.638 1.00102.98 C ANISOU 3818 CG TYR C 36 11064 8467 19596 1608 233 -1915 C ATOM 3819 CD1 TYR C 36 15.928 0.131 -1.303 1.00 97.31 C ANISOU 3819 CD1 TYR C 36 10360 7629 18986 1881 415 -2042 C ATOM 3820 CD2 TYR C 36 16.141 2.437 -1.867 1.00 87.24 C ANISOU 3820 CD2 TYR C 36 9404 6276 17469 1546 402 -1861 C ATOM 3821 CE1 TYR C 36 14.559 0.273 -1.215 1.00103.55 C ANISOU 3821 CE1 TYR C 36 11395 8266 19685 2007 740 -2166 C ATOM 3822 CE2 TYR C 36 14.770 2.589 -1.778 1.00101.39 C ANISOU 3822 CE2 TYR C 36 11445 7847 19233 1807 666 -1974 C ATOM 3823 CZ TYR C 36 13.983 1.504 -1.452 1.00100.41 C ANISOU 3823 CZ TYR C 36 11237 7759 19155 2000 825 -2155 C ATOM 3824 OH TYR C 36 12.616 1.647 -1.361 1.00127.20 O ANISOU 3824 OH TYR C 36 14849 11278 22204 2089 1054 -2268 O ATOM 3825 N ASP C 37 20.742 -0.281 0.359 1.00136.08 N ANISOU 3825 N ASP C 37 16588 14063 21055 2463 -1697 -1302 N ATOM 3826 CA ASP C 37 22.062 -0.897 0.305 1.00126.44 C ANISOU 3826 CA ASP C 37 15475 12767 19799 2540 -2371 -1568 C ATOM 3827 C ASP C 37 22.084 -1.906 -0.837 1.00121.46 C ANISOU 3827 C ASP C 37 14447 12272 19430 2489 -2597 -1492 C ATOM 3828 O ASP C 37 21.316 -2.874 -0.833 1.00145.37 O ANISOU 3828 O ASP C 37 17598 15289 22348 2355 -2505 -1262 O ATOM 3829 CB ASP C 37 22.394 -1.569 1.635 1.00130.35 C ANISOU 3829 CB ASP C 37 16684 13022 19822 2511 -2664 -1597 C ATOM 3830 CG ASP C 37 23.858 -1.959 1.746 1.00144.46 C ANISOU 3830 CG ASP C 37 18559 14723 21607 2617 -3343 -1816 C ATOM 3831 OD1 ASP C 37 24.622 -1.701 0.791 1.00146.18 O ANISOU 3831 OD1 ASP C 37 18303 15048 22189 2729 -3560 -1992 O ATOM 3832 OD2 ASP C 37 24.243 -2.526 2.789 1.00152.49 O ANISOU 3832 OD2 ASP C 37 20095 15582 22264 2577 -3662 -1775 O ATOM 3833 N PHE C 38 22.959 -1.678 -1.813 1.00102.70 N ANISOU 3833 N PHE C 38 11615 10022 17384 2557 -2862 -1703 N ATOM 3834 CA PHE C 38 22.984 -2.454 -3.046 1.00104.85 C ANISOU 3834 CA PHE C 38 11459 10454 17927 2442 -2976 -1693 C ATOM 3835 C PHE C 38 24.085 -3.507 -2.981 1.00104.81 C ANISOU 3835 C PHE C 38 11653 10217 17951 2543 -3499 -1905 C ATOM 3836 O PHE C 38 25.267 -3.170 -2.855 1.00119.64 O ANISOU 3836 O PHE C 38 13518 12015 19924 2727 -3859 -2149 O ATOM 3837 CB PHE C 38 23.191 -1.534 -4.248 1.00 91.58 C ANISOU 3837 CB PHE C 38 9104 9083 16611 2409 -2879 -1773 C ATOM 3838 CG PHE C 38 23.229 -2.253 -5.560 1.00110.68 C ANISOU 3838 CG PHE C 38 11083 11715 19256 2200 -2961 -1798 C ATOM 3839 CD1 PHE C 38 22.064 -2.740 -6.130 1.00110.77 C ANISOU 3839 CD1 PHE C 38 10901 11953 19235 1889 -2648 -1490 C ATOM 3840 CD2 PHE C 38 24.428 -2.444 -6.224 1.00101.53 C ANISOU 3840 CD2 PHE C 38 9706 10543 18325 2269 -3329 -2134 C ATOM 3841 CE1 PHE C 38 22.094 -3.404 -7.339 1.00102.60 C ANISOU 3841 CE1 PHE C 38 9502 11138 18342 1596 -2697 -1546 C ATOM 3842 CE2 PHE C 38 24.465 -3.106 -7.433 1.00 95.61 C ANISOU 3842 CE2 PHE C 38 8591 9976 17760 2019 -3340 -2210 C ATOM 3843 CZ PHE C 38 23.296 -3.586 -7.992 1.00111.21 C ANISOU 3843 CZ PHE C 38 10416 12187 19652 1654 -3021 -1932 C ATOM 3844 N THR C 39 23.696 -4.779 -3.078 1.00122.80 N ANISOU 3844 N THR C 39 14096 12378 20183 2419 -3519 -1786 N ATOM 3845 CA THR C 39 24.641 -5.886 -3.088 1.00118.17 C ANISOU 3845 CA THR C 39 13661 11511 19726 2522 -3925 -1932 C ATOM 3846 C THR C 39 24.361 -6.804 -4.268 1.00 99.76 C ANISOU 3846 C THR C 39 11042 9235 17626 2292 -3792 -1975 C ATOM 3847 O THR C 39 23.218 -6.950 -4.709 1.00107.64 O ANISOU 3847 O THR C 39 11929 10445 18524 2000 -3432 -1781 O ATOM 3848 CB THR C 39 24.588 -6.707 -1.788 1.00119.71 C ANISOU 3848 CB THR C 39 14485 11379 19620 2596 -4104 -1748 C ATOM 3849 OG1 THR C 39 23.272 -7.246 -1.613 1.00134.79 O ANISOU 3849 OG1 THR C 39 16600 13314 21302 2372 -3753 -1478 O ATOM 3850 CG2 THR C 39 24.951 -5.845 -0.589 1.00127.66 C ANISOU 3850 CG2 THR C 39 15825 12353 20326 2730 -4253 -1739 C ATOM 3851 N ARG C 40 25.427 -7.422 -4.773 1.00112.25 N ANISOU 3851 N ARG C 40 12503 10627 19520 2395 -4065 -2225 N ATOM 3852 CA ARG C 40 25.344 -8.436 -5.813 1.00107.33 C ANISOU 3852 CA ARG C 40 11705 9955 19122 2156 -3926 -2348 C ATOM 3853 C ARG C 40 26.305 -9.561 -5.475 1.00122.74 C ANISOU 3853 C ARG C 40 13916 11408 21313 2380 -4209 -2451 C ATOM 3854 O ARG C 40 27.397 -9.317 -4.954 1.00134.75 O ANISOU 3854 O ARG C 40 15466 12756 22975 2717 -4578 -2516 O ATOM 3855 CB ARG C 40 25.682 -7.867 -7.195 1.00102.11 C ANISOU 3855 CB ARG C 40 10441 9630 18725 1987 -3832 -2610 C ATOM 3856 CG ARG C 40 24.625 -6.947 -7.760 1.00 95.61 C ANISOU 3856 CG ARG C 40 9264 9317 17747 1690 -3508 -2423 C ATOM 3857 CD ARG C 40 25.106 -6.281 -9.033 1.00105.66 C ANISOU 3857 CD ARG C 40 9931 10942 19274 1540 -3493 -2650 C ATOM 3858 NE ARG C 40 26.192 -5.346 -8.754 1.00103.57 N ANISOU 3858 NE ARG C 40 9544 10634 19174 1911 -3786 -2836 N ATOM 3859 CZ ARG C 40 26.833 -4.643 -9.681 1.00108.46 C ANISOU 3859 CZ ARG C 40 9667 11514 20030 1873 -3849 -3053 C ATOM 3860 NH1 ARG C 40 26.491 -4.752 -10.958 1.00114.99 N ANISOU 3860 NH1 ARG C 40 10063 12689 20937 1456 -3640 -3105 N ATOM 3861 NH2 ARG C 40 27.810 -3.821 -9.326 1.00100.71 N ANISOU 3861 NH2 ARG C 40 8635 10476 19155 2197 -4117 -3202 N ATOM 3862 N GLY C 41 25.899 -10.790 -5.772 1.00120.70 N ANISOU 3862 N GLY C 41 13825 10915 21119 2176 -4022 -2433 N ATOM 3863 CA GLY C 41 26.767 -11.917 -5.513 1.00107.84 C ANISOU 3863 CA GLY C 41 12407 8751 19817 2397 -4212 -2491 C ATOM 3864 C GLY C 41 26.145 -13.260 -5.815 1.00129.30 C ANISOU 3864 C GLY C 41 15365 11181 22583 2119 -3913 -2467 C ATOM 3865 O GLY C 41 25.287 -13.382 -6.693 1.00134.05 O ANISOU 3865 O GLY C 41 15828 12045 23058 1672 -3545 -2550 O ATOM 3866 N CYS C 42 26.577 -14.280 -5.081 1.00138.65 N ANISOU 3866 N CYS C 42 16900 11831 23949 2352 -4073 -2320 N ATOM 3867 CA CYS C 42 26.108 -15.640 -5.267 1.00134.57 C ANISOU 3867 CA CYS C 42 16662 10926 23542 2130 -3789 -2296 C ATOM 3868 C CYS C 42 25.403 -16.101 -3.998 1.00131.19 C ANISOU 3868 C CYS C 42 16748 10333 22763 2176 -3894 -1858 C ATOM 3869 O CYS C 42 25.678 -15.603 -2.902 1.00119.98 O ANISOU 3869 O CYS C 42 15491 8942 21153 2466 -4256 -1599 O ATOM 3870 CB CYS C 42 27.272 -16.577 -5.605 1.00125.51 C ANISOU 3870 CB CYS C 42 15449 9195 23042 2368 -3809 -2492 C ATOM 3871 SG CYS C 42 26.773 -18.222 -6.105 1.00181.92 S ANISOU 3871 SG CYS C 42 22896 15804 30420 2032 -3321 -2592 S ATOM 3872 N ALA C 43 24.482 -17.049 -4.154 1.00121.37 N ANISOU 3872 N ALA C 43 15774 8941 21399 1834 -3567 -1782 N ATOM 3873 CA ALA C 43 23.716 -17.538 -3.017 1.00123.49 C ANISOU 3873 CA ALA C 43 16532 9075 21313 1822 -3628 -1367 C ATOM 3874 C ALA C 43 23.127 -18.900 -3.350 1.00134.73 C ANISOU 3874 C ALA C 43 18231 10130 22831 1503 -3282 -1364 C ATOM 3875 O ALA C 43 22.942 -19.252 -4.519 1.00132.96 O ANISOU 3875 O ALA C 43 17827 9934 22757 1140 -2914 -1688 O ATOM 3876 CB ALA C 43 22.606 -16.557 -2.623 1.00120.16 C ANISOU 3876 CB ALA C 43 16142 9215 20299 1632 -3553 -1167 C ATOM 3877 N ALA C 44 22.836 -19.664 -2.296 1.00132.17 N ANISOU 3877 N ALA C 44 18365 9467 22387 1597 -3399 -995 N ATOM 3878 CA ALA C 44 22.160 -20.945 -2.468 1.00136.58 C ANISOU 3878 CA ALA C 44 19249 9667 22977 1274 -3068 -942 C ATOM 3879 C ALA C 44 20.657 -20.756 -2.609 1.00136.81 C ANISOU 3879 C ALA C 44 19385 10180 22416 766 -2773 -825 C ATOM 3880 O ALA C 44 20.018 -21.420 -3.433 1.00149.49 O ANISOU 3880 O ALA C 44 21026 11776 23997 286 -2375 -981 O ATOM 3881 CB ALA C 44 22.475 -21.870 -1.292 1.00144.03 C ANISOU 3881 CB ALA C 44 20613 10043 24068 1577 -3323 -544 C ATOM 3882 N THR C 45 20.082 -19.860 -1.812 1.00140.29 N ANISOU 3882 N THR C 45 19876 11044 22384 836 -2936 -543 N ATOM 3883 CA THR C 45 18.690 -19.463 -1.937 1.00148.00 C ANISOU 3883 CA THR C 45 20844 12540 22848 416 -2654 -380 C ATOM 3884 C THR C 45 18.613 -17.944 -1.987 1.00139.86 C ANISOU 3884 C THR C 45 19441 12073 21627 525 -2715 -393 C ATOM 3885 O THR C 45 19.520 -17.241 -1.533 1.00121.41 O ANISOU 3885 O THR C 45 17018 9699 19415 937 -3029 -455 O ATOM 3886 CB THR C 45 17.834 -19.995 -0.777 1.00160.40 C ANISOU 3886 CB THR C 45 22916 13999 24028 362 -2672 50 C ATOM 3887 OG1 THR C 45 16.453 -19.696 -1.024 1.00161.47 O ANISOU 3887 OG1 THR C 45 22991 14633 23728 -75 -2342 222 O ATOM 3888 CG2 THR C 45 18.260 -19.361 0.539 1.00159.10 C ANISOU 3888 CG2 THR C 45 22943 13820 23688 789 -3055 285 C ATOM 3889 N CYS C 46 17.525 -17.445 -2.556 1.00158.47 N ANISOU 3889 N CYS C 46 21560 14952 23700 132 -2400 -306 N ATOM 3890 CA CYS C 46 17.322 -16.004 -2.620 1.00164.59 C ANISOU 3890 CA CYS C 46 21959 16235 24344 222 -2378 -259 C ATOM 3891 C CYS C 46 17.096 -15.457 -1.216 1.00160.29 C ANISOU 3891 C CYS C 46 21735 15673 23495 519 -2511 22 C ATOM 3892 O CYS C 46 16.317 -16.037 -0.450 1.00168.96 O ANISOU 3892 O CYS C 46 23232 16674 24293 403 -2427 314 O ATOM 3893 CB CYS C 46 16.135 -15.667 -3.515 1.00173.60 C ANISOU 3893 CB CYS C 46 22733 17937 25288 -283 -1997 -111 C ATOM 3894 SG CYS C 46 16.374 -16.129 -5.236 1.00177.96 S ANISOU 3894 SG CYS C 46 22879 18646 26093 -771 -1820 -464 S ATOM 3895 N PRO C 47 17.762 -14.367 -0.837 1.00144.74 N ANISOU 3895 N PRO C 47 20348 11431 23216 1425 3654 1931 N ATOM 3896 CA PRO C 47 17.541 -13.796 0.495 1.00143.12 C ANISOU 3896 CA PRO C 47 19822 11552 23006 1781 3425 1706 C ATOM 3897 C PRO C 47 16.083 -13.412 0.704 1.00136.47 C ANISOU 3897 C PRO C 47 18770 10752 22331 1092 3485 1579 C ATOM 3898 O PRO C 47 15.355 -13.103 -0.243 1.00118.76 O ANISOU 3898 O PRO C 47 16226 8458 20439 341 3457 1570 O ATOM 3899 CB PRO C 47 18.451 -12.561 0.507 1.00143.40 C ANISOU 3899 CB PRO C 47 18867 12004 23613 2138 2749 1504 C ATOM 3900 CG PRO C 47 19.505 -12.863 -0.507 1.00135.24 C ANISOU 3900 CG PRO C 47 17861 10879 22644 2298 2772 1726 C ATOM 3901 CD PRO C 47 18.810 -13.648 -1.582 1.00131.67 C ANISOU 3901 CD PRO C 47 18010 9999 22021 1651 3237 1951 C ATOM 3902 N LYS C 48 15.661 -13.451 1.965 1.00138.34 N ANISOU 3902 N LYS C 48 19165 11136 22262 1421 3579 1490 N ATOM 3903 CA LYS C 48 14.309 -13.038 2.314 1.00147.18 C ANISOU 3903 CA LYS C 48 20018 12403 23500 892 3640 1384 C ATOM 3904 C LYS C 48 14.116 -11.554 2.028 1.00147.05 C ANISOU 3904 C LYS C 48 18956 12760 24157 696 3004 1113 C ATOM 3905 O LYS C 48 14.891 -10.712 2.490 1.00139.43 O ANISOU 3905 O LYS C 48 17494 12048 23434 1255 2487 900 O ATOM 3906 CB LYS C 48 14.032 -13.337 3.787 1.00142.25 C ANISOU 3906 CB LYS C 48 19773 11909 22368 1458 3874 1377 C ATOM 3907 CG LYS C 48 12.655 -12.906 4.258 1.00140.07 C ANISOU 3907 CG LYS C 48 19191 11867 22161 1023 3971 1302 C ATOM 3908 CD LYS C 48 11.562 -13.745 3.622 1.00151.24 C ANISOU 3908 CD LYS C 48 21003 12974 23489 83 4565 1520 C ATOM 3909 CE LYS C 48 10.197 -13.371 4.174 1.00160.62 C ANISOU 3909 CE LYS C 48 21837 14490 24700 -298 4710 1480 C ATOM 3910 NZ LYS C 48 9.102 -14.133 3.514 1.00161.77 N ANISOU 3910 NZ LYS C 48 22226 14405 24834 -1315 5237 1643 N ATOM 3911 N ALA C 49 13.079 -11.237 1.256 1.00141.20 N ANISOU 3911 N ALA C 49 17894 12045 23711 -96 3039 1107 N ATOM 3912 CA ALA C 49 12.767 -9.861 0.886 1.00127.48 C ANISOU 3912 CA ALA C 49 15253 10612 22571 -299 2512 894 C ATOM 3913 C ALA C 49 11.901 -9.242 1.978 1.00123.36 C ANISOU 3913 C ALA C 49 14448 10441 21984 -139 2404 703 C ATOM 3914 O ALA C 49 10.756 -9.658 2.184 1.00121.91 O ANISOU 3914 O ALA C 49 14437 10336 21547 -543 2789 782 O ATOM 3915 CB ALA C 49 12.067 -9.811 -0.468 1.00114.73 C ANISOU 3915 CB ALA C 49 13437 8935 21221 -1100 2595 979 C ATOM 3916 N GLU C 50 12.444 -8.247 2.672 1.00130.16 N ANISOU 3916 N GLU C 50 14860 11520 23073 446 1877 441 N ATOM 3917 CA GLU C 50 11.738 -7.589 3.759 1.00146.57 C ANISOU 3917 CA GLU C 50 16702 13939 25048 756 1712 224 C ATOM 3918 C GLU C 50 10.904 -6.432 3.209 1.00137.49 C ANISOU 3918 C GLU C 50 14861 13002 24378 340 1403 84 C ATOM 3919 O GLU C 50 10.689 -6.306 2.000 1.00112.60 O ANISOU 3919 O GLU C 50 11482 9753 21549 -245 1422 197 O ATOM 3920 CB GLU C 50 12.728 -7.117 4.824 1.00159.53 C ANISOU 3920 CB GLU C 50 18270 15702 26643 1644 1259 -55 C ATOM 3921 CG GLU C 50 13.482 -8.235 5.524 1.00169.06 C ANISOU 3921 CG GLU C 50 20176 16803 27257 2227 1570 76 C ATOM 3922 CD GLU C 50 12.582 -9.107 6.376 1.00175.81 C ANISOU 3922 CD GLU C 50 21643 17708 27448 2331 2179 273 C ATOM 3923 OE1 GLU C 50 11.582 -8.586 6.914 1.00175.66 O ANISOU 3923 OE1 GLU C 50 21384 17971 27388 2296 2171 178 O ATOM 3924 OE2 GLU C 50 12.877 -10.313 6.510 1.00177.49 O ANISOU 3924 OE2 GLU C 50 22596 17672 27171 2474 2700 548 O ATOM 3925 N TYR C 51 10.415 -5.580 4.105 1.00136.86 N ANISOU 3925 N TYR C 51 14481 13231 24289 718 1121 -162 N ATOM 3926 CA TYR C 51 9.615 -4.428 3.712 1.00146.15 C ANISOU 3926 CA TYR C 51 15054 14627 25848 474 825 -303 C ATOM 3927 C TYR C 51 10.423 -3.488 2.822 1.00143.93 C ANISOU 3927 C TYR C 51 14324 14123 26240 388 336 -414 C ATOM 3928 O TYR C 51 11.504 -3.029 3.208 1.00152.04 O ANISOU 3928 O TYR C 51 15250 15007 27514 837 -81 -623 O ATOM 3929 CB TYR C 51 9.120 -3.706 4.966 1.00154.95 C ANISOU 3929 CB TYR C 51 16033 16078 26762 1074 587 -570 C ATOM 3930 CG TYR C 51 8.253 -2.492 4.717 1.00157.74 C ANISOU 3930 CG TYR C 51 15839 16682 27415 976 293 -726 C ATOM 3931 CD1 TYR C 51 6.945 -2.626 4.271 1.00159.60 C ANISOU 3931 CD1 TYR C 51 15902 17237 27502 484 648 -538 C ATOM 3932 CD2 TYR C 51 8.734 -1.213 4.963 1.00153.96 C ANISOU 3932 CD2 TYR C 51 15023 16128 27346 1401 -342 -1077 C ATOM 3933 CE1 TYR C 51 6.147 -1.517 4.054 1.00164.44 C ANISOU 3933 CE1 TYR C 51 16028 18136 28316 501 390 -666 C ATOM 3934 CE2 TYR C 51 7.944 -0.100 4.754 1.00163.45 C ANISOU 3934 CE2 TYR C 51 15818 17511 28775 1392 -584 -1206 C ATOM 3935 CZ TYR C 51 6.652 -0.256 4.298 1.00175.47 C ANISOU 3935 CZ TYR C 51 17184 19399 30088 987 -211 -985 C ATOM 3936 OH TYR C 51 5.864 0.854 4.087 1.00185.36 O ANISOU 3936 OH TYR C 51 18041 20884 31502 1075 -442 -1098 O ATOM 3937 N ARG C 52 9.898 -3.228 1.621 1.00126.16 N ANISOU 3937 N ARG C 52 11794 11862 24277 -191 408 -264 N ATOM 3938 CA ARG C 52 10.490 -2.295 0.656 1.00121.06 C ANISOU 3938 CA ARG C 52 10722 11005 24269 -313 47 -283 C ATOM 3939 C ARG C 52 11.856 -2.765 0.157 1.00107.08 C ANISOU 3939 C ARG C 52 9095 8891 22698 -285 35 -150 C ATOM 3940 O ARG C 52 12.747 -1.957 -0.108 1.00124.71 O ANISOU 3940 O ARG C 52 10983 10933 25470 -144 -341 -234 O ATOM 3941 CB ARG C 52 10.588 -0.878 1.228 1.00123.92 C ANISOU 3941 CB ARG C 52 10675 11390 25020 100 -505 -615 C ATOM 3942 CG ARG C 52 9.251 -0.190 1.401 1.00126.28 C ANISOU 3942 CG ARG C 52 10746 12033 25203 90 -525 -704 C ATOM 3943 CD ARG C 52 9.417 1.229 1.919 1.00121.99 C ANISOU 3943 CD ARG C 52 9900 11408 25045 537 -1083 -1050 C ATOM 3944 NE ARG C 52 8.124 1.877 2.119 1.00124.34 N ANISOU 3944 NE ARG C 52 10020 12074 25150 639 -1083 -1120 N ATOM 3945 CZ ARG C 52 7.968 3.094 2.625 1.00131.36 C ANISOU 3945 CZ ARG C 52 10734 12937 26240 1075 -1510 -1423 C ATOM 3946 NH1 ARG C 52 9.028 3.804 2.983 1.00154.17 N ANISOU 3946 NH1 ARG C 52 13583 15410 29585 1366 -1998 -1720 N ATOM 3947 NH2 ARG C 52 6.752 3.600 2.773 1.00127.57 N ANISOU 3947 NH2 ARG C 52 10114 12856 25502 1224 -1457 -1445 N ATOM 3948 N ASP C 53 12.024 -4.074 0.008 1.00114.33 N ANISOU 3948 N ASP C 53 10527 9723 23189 -422 472 74 N ATOM 3949 CA ASP C 53 13.219 -4.627 -0.609 1.00106.48 C ANISOU 3949 CA ASP C 53 9710 8453 22294 -383 539 259 C ATOM 3950 C ASP C 53 12.903 -5.116 -2.016 1.00106.39 C ANISOU 3950 C ASP C 53 9806 8325 22293 -943 859 551 C ATOM 3951 O ASP C 53 11.790 -5.566 -2.300 1.00116.25 O ANISOU 3951 O ASP C 53 11221 9693 23256 -1373 1155 609 O ATOM 3952 CB ASP C 53 13.802 -5.775 0.221 1.00125.61 C ANISOU 3952 CB ASP C 53 12737 10817 24173 12 792 301 C ATOM 3953 CG ASP C 53 14.430 -5.298 1.515 1.00143.24 C ANISOU 3953 CG ASP C 53 14844 13187 26395 698 398 -9 C ATOM 3954 OD1 ASP C 53 14.863 -4.127 1.576 1.00148.75 O ANISOU 3954 OD1 ASP C 53 14972 13908 27638 840 -125 -250 O ATOM 3955 OD2 ASP C 53 14.510 -6.102 2.466 1.00156.04 O ANISOU 3955 OD2 ASP C 53 16963 14872 27451 1111 613 -19 O ATOM 3956 N VAL C 54 13.891 -5.005 -2.900 1.00104.37 N ANISOU 3956 N VAL C 54 9419 7870 22368 -923 784 720 N ATOM 3957 CA VAL C 54 13.787 -5.473 -4.278 1.00117.40 C ANISOU 3957 CA VAL C 54 11211 9403 23995 -1320 1057 997 C ATOM 3958 C VAL C 54 14.944 -6.429 -4.532 1.00107.84 C ANISOU 3958 C VAL C 54 10433 7968 22575 -1076 1266 1208 C ATOM 3959 O VAL C 54 16.113 -6.030 -4.456 1.00115.64 O ANISOU 3959 O VAL C 54 11144 8908 23886 -704 1042 1242 O ATOM 3960 CB VAL C 54 13.807 -4.311 -5.283 1.00114.83 C ANISOU 3960 CB VAL C 54 10292 9083 24255 -1461 819 1077 C ATOM 3961 CG1 VAL C 54 13.795 -4.841 -6.710 1.00112.60 C ANISOU 3961 CG1 VAL C 54 10198 8713 23873 -1746 1096 1367 C ATOM 3962 CG2 VAL C 54 12.627 -3.383 -5.045 1.00132.31 C ANISOU 3962 CG2 VAL C 54 12134 11537 26598 -1616 633 880 C ATOM 3963 N ILE C 55 14.620 -7.683 -4.837 1.00108.60 N ANISOU 3963 N ILE C 55 11200 7929 22133 -1286 1695 1341 N ATOM 3964 CA ILE C 55 15.613 -8.733 -5.035 1.00128.86 C ANISOU 3964 CA ILE C 55 14334 10263 24365 -993 1956 1547 C ATOM 3965 C ILE C 55 15.312 -9.443 -6.347 1.00122.55 C ANISOU 3965 C ILE C 55 13926 9283 23354 -1384 2263 1745 C ATOM 3966 O ILE C 55 14.192 -9.922 -6.556 1.00116.16 O ANISOU 3966 O ILE C 55 13402 8451 22280 -1892 2471 1667 O ATOM 3967 CB ILE C 55 15.622 -9.741 -3.869 1.00124.05 C ANISOU 3967 CB ILE C 55 14392 9565 23175 -713 2220 1489 C ATOM 3968 CG1 ILE C 55 15.966 -9.037 -2.556 1.00133.36 C ANISOU 3968 CG1 ILE C 55 15199 10973 24498 -218 1871 1254 C ATOM 3969 CG2 ILE C 55 16.621 -10.855 -4.138 1.00117.27 C ANISOU 3969 CG2 ILE C 55 14200 8452 21906 -346 2523 1723 C ATOM 3970 CD1 ILE C 55 15.746 -9.893 -1.331 1.00138.79 C ANISOU 3970 CD1 ILE C 55 16510 11640 24584 95 2144 1197 C ATOM 3971 N ASN C 56 16.309 -9.513 -7.225 1.00122.85 N ANISOU 3971 N ASN C 56 13990 9918 22767 713 488 1687 N ATOM 3972 CA ASN C 56 16.197 -10.203 -8.502 1.00123.92 C ANISOU 3972 CA ASN C 56 13973 10226 22883 511 180 1093 C ATOM 3973 C ASN C 56 17.114 -11.419 -8.495 1.00128.75 C ANISOU 3973 C ASN C 56 14995 10430 23494 696 270 744 C ATOM 3974 O ASN C 56 18.298 -11.306 -8.162 1.00119.37 O ANISOU 3974 O ASN C 56 14115 9315 21925 1092 333 836 O ATOM 3975 CB ASN C 56 16.557 -9.272 -9.662 1.00130.54 C ANISOU 3975 CB ASN C 56 14553 11896 23148 604 -176 986 C ATOM 3976 CG ASN C 56 15.532 -8.172 -9.867 1.00143.42 C ANISOU 3976 CG ASN C 56 15770 13954 24768 442 -271 1276 C ATOM 3977 OD1 ASN C 56 14.326 -8.413 -9.810 1.00160.09 O ANISOU 3977 OD1 ASN C 56 17619 15900 27309 125 -297 1210 O ATOM 3978 ND2 ASN C 56 16.009 -6.953 -10.099 1.00121.46 N ANISOU 3978 ND2 ASN C 56 12921 11705 21524 669 -277 1581 N ATOM 3979 N CYS C 57 16.567 -12.576 -8.859 1.00136.29 N ANISOU 3979 N CYS C 57 15926 10960 24898 417 298 301 N ATOM 3980 CA CYS C 57 17.320 -13.820 -8.893 1.00131.51 C ANISOU 3980 CA CYS C 57 15709 9897 24362 563 435 -47 C ATOM 3981 C CYS C 57 17.282 -14.433 -10.286 1.00137.21 C ANISOU 3981 C CYS C 57 16188 10892 25054 337 70 -756 C ATOM 3982 O CYS C 57 16.329 -14.238 -11.046 1.00162.25 O ANISOU 3982 O CYS C 57 18875 14385 28386 4 -193 -1052 O ATOM 3983 CB CYS C 57 16.777 -14.835 -7.887 1.00143.94 C ANISOU 3983 CB CYS C 57 17568 10514 26609 485 979 66 C ATOM 3984 SG CYS C 57 17.027 -14.435 -6.148 1.00136.51 S ANISOU 3984 SG CYS C 57 17066 9165 25639 938 1472 858 S ATOM 3985 N CYS C 58 18.325 -15.198 -10.594 1.00131.80 N ANISOU 3985 N CYS C 58 15831 10100 24146 563 48 -1059 N ATOM 3986 CA CYS C 58 18.507 -15.836 -11.891 1.00148.75 C ANISOU 3986 CA CYS C 58 17811 12515 26193 430 -297 -1750 C ATOM 3987 C CYS C 58 19.684 -16.796 -11.791 1.00138.02 C ANISOU 3987 C CYS C 58 16949 10797 24696 722 -151 -1939 C ATOM 3988 O CYS C 58 20.507 -16.700 -10.876 1.00133.16 O ANISOU 3988 O CYS C 58 16759 9971 23863 1118 102 -1535 O ATOM 3989 CB CYS C 58 18.723 -14.795 -12.994 1.00153.71 C ANISOU 3989 CB CYS C 58 18111 14108 26183 519 -794 -1832 C ATOM 3990 SG CYS C 58 20.055 -13.625 -12.649 1.00163.54 S ANISOU 3990 SG CYS C 58 19632 15800 26708 1012 -776 -1305 S ATOM 3991 N GLY C 59 19.747 -17.732 -12.735 1.00141.05 N ANISOU 3991 N GLY C 59 17252 11140 25199 555 -321 -2597 N ATOM 3992 CA GLY C 59 20.759 -18.771 -12.692 1.00142.66 C ANISOU 3992 CA GLY C 59 17919 10945 25342 796 -159 -2825 C ATOM 3993 C GLY C 59 21.658 -18.822 -13.910 1.00142.43 C ANISOU 3993 C GLY C 59 17844 11520 24754 930 -616 -3286 C ATOM 3994 O GLY C 59 22.106 -19.898 -14.315 1.00146.07 O ANISOU 3994 O GLY C 59 18490 11687 25321 932 -586 -3748 O ATOM 3995 N THR C 60 21.936 -17.663 -14.497 1.00147.47 N ANISOU 3995 N THR C 60 18257 12970 24805 1060 -986 -3148 N ATOM 3996 CA THR C 60 22.778 -17.546 -15.677 1.00157.02 C ANISOU 3996 CA THR C 60 19424 14801 25434 1233 -1380 -3514 C ATOM 3997 C THR C 60 24.096 -16.879 -15.293 1.00147.63 C ANISOU 3997 C THR C 60 18562 13841 23691 1678 -1314 -3157 C ATOM 3998 O THR C 60 24.170 -16.148 -14.301 1.00163.63 O ANISOU 3998 O THR C 60 20680 15795 25699 1828 -1080 -2631 O ATOM 3999 CB THR C 60 22.054 -16.739 -16.768 1.00173.90 C ANISOU 3999 CB THR C 60 21043 17706 27323 1102 -1788 -3677 C ATOM 4000 OG1 THR C 60 20.795 -17.359 -17.061 1.00194.09 O ANISOU 4000 OG1 THR C 60 23217 20087 30439 701 -1864 -4112 O ATOM 4001 CG2 THR C 60 22.867 -16.670 -18.054 1.00168.67 C ANISOU 4001 CG2 THR C 60 20360 17677 26049 1332 -2155 -4057 C ATOM 4002 N ASP C 61 25.145 -17.157 -16.067 1.00132.74 N ANISOU 4002 N ASP C 61 16823 12230 21383 1889 -1509 -3502 N ATOM 4003 CA ASP C 61 26.438 -16.522 -15.839 1.00128.23 C ANISOU 4003 CA ASP C 61 16481 11926 20314 2291 -1453 -3304 C ATOM 4004 C ASP C 61 26.323 -15.008 -15.967 1.00127.75 C ANISOU 4004 C ASP C 61 16144 12435 19958 2347 -1478 -2922 C ATOM 4005 O ASP C 61 25.996 -14.490 -17.039 1.00125.39 O ANISOU 4005 O ASP C 61 15567 12665 19409 2278 -1716 -3033 O ATOM 4006 CB ASP C 61 27.474 -17.059 -16.828 1.00129.58 C ANISOU 4006 CB ASP C 61 16795 12333 20108 2459 -1675 -3794 C ATOM 4007 CG ASP C 61 27.927 -18.467 -16.496 1.00142.36 C ANISOU 4007 CG ASP C 61 18787 13352 21950 2527 -1552 -4098 C ATOM 4008 OD1 ASP C 61 27.939 -18.821 -15.300 1.00140.71 O ANISOU 4008 OD1 ASP C 61 18857 12601 22005 2660 -1216 -3821 O ATOM 4009 OD2 ASP C 61 28.279 -19.219 -17.431 1.00135.53 O ANISOU 4009 OD2 ASP C 61 17958 12561 20978 2493 -1765 -4600 O ATOM 4010 N LYS C 62 26.594 -14.305 -14.863 1.00120.43 N ANISOU 4010 N LYS C 62 15301 11405 19051 2520 -1203 -2482 N ATOM 4011 CA LYS C 62 26.602 -12.841 -14.830 1.00125.12 C ANISOU 4011 CA LYS C 62 15655 12454 19429 2588 -1117 -2112 C ATOM 4012 C LYS C 62 25.257 -12.259 -15.261 1.00130.75 C ANISOU 4012 C LYS C 62 16008 13399 20273 2296 -1225 -1902 C ATOM 4013 O LYS C 62 25.192 -11.296 -16.029 1.00129.24 O ANISOU 4013 O LYS C 62 15600 13739 19767 2350 -1282 -1795 O ATOM 4014 CB LYS C 62 27.739 -12.272 -15.681 1.00118.08 C ANISOU 4014 CB LYS C 62 14763 12050 18053 2831 -1156 -2307 C ATOM 4015 CG LYS C 62 29.122 -12.509 -15.102 1.00116.37 C ANISOU 4015 CG LYS C 62 14812 11705 17698 3163 -1009 -2492 C ATOM 4016 CD LYS C 62 30.198 -11.890 -15.974 1.00128.67 C ANISOU 4016 CD LYS C 62 16321 13714 18855 3357 -984 -2715 C ATOM 4017 CE LYS C 62 31.580 -12.141 -15.398 1.00145.78 C ANISOU 4017 CE LYS C 62 18688 15793 20909 3692 -860 -3002 C ATOM 4018 NZ LYS C 62 32.653 -11.558 -16.247 1.00157.18 N ANISOU 4018 NZ LYS C 62 20062 17622 22036 3852 -772 -3272 N ATOM 4019 N CYS C 63 24.172 -12.845 -14.759 1.00126.30 N ANISOU 4019 N CYS C 63 15384 12425 20178 2021 -1211 -1848 N ATOM 4020 CA CYS C 63 22.833 -12.350 -15.044 1.00122.55 C ANISOU 4020 CA CYS C 63 14532 12151 19878 1747 -1319 -1699 C ATOM 4021 C CYS C 63 22.352 -11.316 -14.036 1.00117.63 C ANISOU 4021 C CYS C 63 13808 11481 19406 1727 -1061 -1098 C ATOM 4022 O CYS C 63 21.303 -10.700 -14.258 1.00118.22 O ANISOU 4022 O CYS C 63 13561 11797 19560 1549 -1135 -912 O ATOM 4023 CB CYS C 63 21.840 -13.516 -15.097 1.00126.45 C ANISOU 4023 CB CYS C 63 14931 12223 20890 1406 -1408 -2053 C ATOM 4024 SG CYS C 63 21.686 -14.426 -13.547 1.00134.98 S ANISOU 4024 SG CYS C 63 16355 12343 22588 1331 -973 -1845 S ATOM 4025 N ASN C 64 23.083 -11.106 -12.942 1.00117.00 N ANISOU 4025 N ASN C 64 13971 11136 19348 1941 -777 -826 N ATOM 4026 CA ASN C 64 22.727 -10.105 -11.947 1.00112.02 C ANISOU 4026 CA ASN C 64 13234 10483 18844 1959 -528 -295 C ATOM 4027 C ASN C 64 23.499 -8.802 -12.125 1.00106.87 C ANISOU 4027 C ASN C 64 12467 10319 17819 2183 -409 -118 C ATOM 4028 O ASN C 64 23.643 -8.041 -11.164 1.00103.61 O ANISOU 4028 O ASN C 64 12018 9861 17488 2290 -154 215 O ATOM 4029 CB ASN C 64 22.939 -10.655 -10.535 1.00114.33 C ANISOU 4029 CB ASN C 64 13825 10201 19414 2111 -260 -124 C ATOM 4030 CG ASN C 64 24.376 -11.076 -10.277 1.00123.06 C ANISOU 4030 CG ASN C 64 15251 11264 20241 2518 -202 -376 C ATOM 4031 OD1 ASN C 64 25.238 -10.966 -11.148 1.00112.56 O ANISOU 4031 OD1 ASN C 64 13912 10294 18562 2629 -348 -692 O ATOM 4032 ND2 ASN C 64 24.644 -11.540 -9.062 1.00124.01 N ANISOU 4032 ND2 ASN C 64 15659 10967 20491 2795 29 -237 N ATOM 4033 N LYS C 65 24.002 -8.533 -13.327 1.00107.75 N ANISOU 4033 N LYS C 65 12517 10874 17550 2270 -540 -354 N ATOM 4034 CA LYS C 65 24.680 -7.272 -13.608 1.00105.16 C ANISOU 4034 CA LYS C 65 12072 10951 16933 2465 -312 -192 C ATOM 4035 C LYS C 65 23.720 -6.096 -13.456 1.00122.38 C ANISOU 4035 C LYS C 65 13972 13329 19199 2349 -153 307 C ATOM 4036 O LYS C 65 22.653 -6.070 -14.069 1.00128.15 O ANISOU 4036 O LYS C 65 14534 14244 19913 2197 -349 394 O ATOM 4037 CB LYS C 65 25.278 -7.282 -15.017 1.00107.31 C ANISOU 4037 CB LYS C 65 12369 11622 16780 2609 -435 -505 C ATOM 4038 CG LYS C 65 25.955 -5.978 -15.421 1.00116.76 C ANISOU 4038 CG LYS C 65 13465 13175 17723 2819 -78 -332 C ATOM 4039 CD LYS C 65 27.210 -5.717 -14.603 1.00132.98 C ANISOU 4039 CD LYS C 65 15591 15066 19870 2985 229 -472 C ATOM 4040 CE LYS C 65 27.980 -4.517 -15.136 1.00140.07 C ANISOU 4040 CE LYS C 65 16369 16253 20598 3162 666 -428 C ATOM 4041 NZ LYS C 65 27.225 -3.245 -14.970 1.00149.15 N ANISOU 4041 NZ LYS C 65 17283 17529 21858 3096 994 91 N ATOM 4042 OXT LYS C 65 23.988 -5.147 -12.720 1.00122.20 O ANISOU 4042 OXT LYS C 65 13859 13305 19264 2423 173 594 O TER 4043 LYS C 65 HETATM 4044 C1 ACM A 501 16.400 39.234 16.572 1.00159.75 C HETATM 4045 O ACM A 501 17.034 38.847 17.495 1.00182.76 O HETATM 4046 N ACM A 501 15.710 40.511 16.627 1.00164.45 N HETATM 4047 C2 ACM A 501 16.307 38.377 15.314 1.00134.16 C HETATM 4048 CAA Y01 A 502 -3.803 26.388 4.521 1.00141.55 C HETATM 4049 CBA Y01 A 502 -4.573 26.400 5.842 1.00140.44 C HETATM 4050 CAB Y01 A 502 -5.386 27.706 5.919 1.00135.61 C HETATM 4051 CAN Y01 A 502 -3.565 26.358 7.018 1.00133.54 C HETATM 4052 CAJ Y01 A 502 -3.594 24.983 7.755 1.00118.97 C HETATM 4053 CAO Y01 A 502 -3.061 23.847 6.815 1.00110.08 C HETATM 4054 CBB Y01 A 502 -2.445 22.708 7.647 1.00117.41 C HETATM 4055 CAC Y01 A 502 -1.470 23.314 8.621 1.00115.92 C HETATM 4056 CBE Y01 A 502 -3.586 21.927 8.385 1.00118.06 C HETATM 4057 CAP Y01 A 502 -4.775 21.731 7.444 1.00118.31 C HETATM 4058 CAQ Y01 A 502 -5.410 20.286 7.771 1.00122.30 C HETATM 4059 CBG Y01 A 502 -4.624 19.961 9.050 1.00112.50 C HETATM 4060 CBI Y01 A 502 -3.231 20.536 8.787 1.00116.66 C HETATM 4061 CAE Y01 A 502 -2.549 19.797 7.613 1.00108.63 C HETATM 4062 CAU Y01 A 502 -2.412 20.362 10.099 1.00115.52 C HETATM 4063 CAS Y01 A 502 -2.417 18.918 10.553 1.00124.98 C HETATM 4064 CBF Y01 A 502 -3.767 18.315 10.693 1.00109.55 C HETATM 4065 CBD Y01 A 502 -4.561 18.466 9.408 1.00111.48 C HETATM 4066 CAK Y01 A 502 -5.978 17.998 9.672 1.00123.53 C HETATM 4067 CAI Y01 A 502 -6.031 16.635 10.365 1.00130.95 C HETATM 4068 CAZ Y01 A 502 -4.963 16.082 10.931 1.00122.51 C HETATM 4069 CAV Y01 A 502 -5.089 14.690 11.497 1.00117.62 C HETATM 4070 CBH Y01 A 502 -3.637 16.791 11.045 1.00102.29 C HETATM 4071 CAD Y01 A 502 -2.644 16.135 10.091 1.00 92.48 C HETATM 4072 CAT Y01 A 502 -3.137 16.645 12.480 1.00101.47 C HETATM 4073 CAR Y01 A 502 -3.202 15.184 13.046 1.00107.56 C HETATM 4074 CBC Y01 A 502 -4.618 14.598 12.930 1.00116.11 C HETATM 4075 OAW Y01 A 502 -4.602 13.237 13.292 1.00110.36 O HETATM 4076 CAY Y01 A 502 -4.673 12.966 14.689 1.00117.53 C HETATM 4077 OAG Y01 A 502 -4.900 13.838 15.477 1.00114.07 O HETATM 4078 CAM Y01 A 502 -4.448 11.515 15.160 1.00123.36 C HETATM 4079 CAL Y01 A 502 -3.859 10.743 13.966 1.00133.41 C HETATM 4080 CAX Y01 A 502 -3.818 9.243 14.274 1.00140.25 C HETATM 4081 OAH Y01 A 502 -4.142 8.824 15.422 1.00145.97 O HETATM 4082 OAF Y01 A 502 -3.456 8.439 13.379 1.00139.74 O HETATM 4083 CAA Y01 A 503 7.551 27.539 8.882 1.00113.83 C HETATM 4084 CBA Y01 A 503 7.174 27.866 10.325 1.00111.50 C HETATM 4085 CAB Y01 A 503 7.097 29.393 10.492 1.00107.88 C HETATM 4086 CAN Y01 A 503 5.802 27.229 10.653 1.00115.36 C HETATM 4087 CAJ Y01 A 503 5.903 25.676 10.534 1.00111.49 C HETATM 4088 CAO Y01 A 503 6.493 25.101 11.865 1.00115.97 C HETATM 4089 CBB Y01 A 503 6.740 23.584 11.762 1.00127.11 C HETATM 4090 CAC Y01 A 503 8.039 23.370 11.033 1.00131.69 C HETATM 4091 CBE Y01 A 503 6.786 23.013 13.223 1.00132.44 C HETATM 4092 CAP Y01 A 503 5.577 23.579 13.967 1.00135.69 C HETATM 4093 CAQ Y01 A 503 4.795 22.344 14.642 1.00136.77 C HETATM 4094 CBG Y01 A 503 5.950 21.337 14.678 1.00141.85 C HETATM 4095 CBI Y01 A 503 6.672 21.527 13.344 1.00137.07 C HETATM 4096 CAE Y01 A 503 5.814 20.934 12.207 1.00147.75 C HETATM 4097 CAU Y01 A 503 7.999 20.728 13.474 1.00127.05 C HETATM 4098 CAS Y01 A 503 7.730 19.285 13.866 1.00121.93 C HETATM 4099 CBF Y01 A 503 6.812 19.074 15.019 1.00132.84 C HETATM 4100 CBD Y01 A 503 5.529 19.864 14.827 1.00143.13 C HETATM 4101 CAK Y01 A 503 4.646 19.719 16.052 1.00152.89 C HETATM 4102 CAI Y01 A 503 4.581 18.290 16.601 1.00152.94 C HETATM 4103 CAZ Y01 A 503 5.388 17.318 16.185 1.00147.85 C HETATM 4104 CAV Y01 A 503 5.148 15.909 16.679 1.00150.75 C HETATM 4105 CBH Y01 A 503 6.460 17.551 15.150 1.00142.32 C HETATM 4106 CAD Y01 A 503 5.956 17.042 13.804 1.00144.51 C HETATM 4107 CAT Y01 A 503 7.722 16.796 15.557 1.00142.25 C HETATM 4108 CAR Y01 A 503 7.493 15.316 16.024 1.00150.86 C HETATM 4109 CBC Y01 A 503 6.431 15.241 17.136 1.00155.17 C HETATM 4110 OAW Y01 A 503 6.217 13.904 17.576 1.00158.26 O HETATM 4111 CAY Y01 A 503 5.556 12.953 16.731 1.00156.04 C HETATM 4112 OAG Y01 A 503 5.490 13.081 15.542 1.00153.22 O HETATM 4113 CAM Y01 A 503 4.920 11.701 17.375 1.00153.94 C HETATM 4114 CAL Y01 A 503 5.769 10.472 17.003 1.00157.39 C HETATM 4115 CAX Y01 A 503 5.282 9.897 15.666 1.00169.26 C HETATM 4116 OAH Y01 A 503 6.089 9.741 14.704 1.00171.17 O HETATM 4117 OAF Y01 A 503 4.074 9.583 15.531 1.00175.00 O HETATM 4118 CAA Y01 A 504 23.248 29.554 -9.723 1.00125.78 C HETATM 4119 CBA Y01 A 504 24.099 29.030 -8.570 1.00129.05 C HETATM 4120 CAB Y01 A 504 24.726 27.685 -8.982 1.00120.73 C HETATM 4121 CAN Y01 A 504 25.223 30.051 -8.272 1.00119.39 C HETATM 4122 CAJ Y01 A 504 24.634 31.373 -7.689 1.00 90.86 C HETATM 4123 CAO Y01 A 504 25.840 32.337 -7.464 1.00 99.40 C HETATM 4124 CBB Y01 A 504 25.482 33.596 -6.654 1.00107.45 C HETATM 4125 CAC Y01 A 504 24.898 33.189 -5.329 1.00103.26 C HETATM 4126 CBE Y01 A 504 26.817 34.392 -6.455 1.00115.46 C HETATM 4127 CAP Y01 A 504 27.650 34.233 -7.729 1.00129.07 C HETATM 4128 CAQ Y01 A 504 28.010 35.706 -8.263 1.00137.34 C HETATM 4129 CBG Y01 A 504 27.899 36.433 -6.919 1.00135.85 C HETATM 4130 CBI Y01 A 504 26.648 35.862 -6.254 1.00116.88 C HETATM 4131 CAE Y01 A 504 25.375 36.381 -6.957 1.00124.57 C HETATM 4132 CAU Y01 A 504 26.690 36.371 -4.785 1.00108.73 C HETATM 4133 CAS Y01 A 504 26.918 37.872 -4.699 1.00115.67 C HETATM 4134 CBF Y01 A 504 27.970 38.455 -5.582 1.00138.39 C HETATM 4135 CBD Y01 A 504 27.789 37.961 -7.007 1.00149.91 C HETATM 4136 CAK Y01 A 504 28.918 38.463 -7.883 1.00167.08 C HETATM 4137 CAI Y01 A 504 29.216 39.945 -7.663 1.00174.12 C HETATM 4138 CAZ Y01 A 504 28.559 40.660 -6.757 1.00170.35 C HETATM 4139 CAV Y01 A 504 28.727 42.159 -6.779 1.00171.08 C HETATM 4140 CBH Y01 A 504 27.916 40.028 -5.547 1.00154.05 C HETATM 4141 CAD Y01 A 504 26.462 40.487 -5.465 1.00158.32 C HETATM 4142 CAT Y01 A 504 28.676 40.538 -4.330 1.00148.37 C HETATM 4143 CAR Y01 A 504 28.798 42.100 -4.268 1.00153.57 C HETATM 4144 CBC Y01 A 504 29.391 42.724 -5.541 1.00170.20 C HETATM 4145 OAW Y01 A 504 29.152 44.115 -5.513 1.00188.47 O HETATM 4146 CAY Y01 A 504 30.264 44.918 -5.123 1.00202.79 C HETATM 4147 OAG Y01 A 504 31.378 44.496 -5.229 1.00204.97 O HETATM 4148 CAM Y01 A 504 30.021 46.338 -4.561 1.00206.90 C HETATM 4149 CAL Y01 A 504 30.731 47.379 -5.445 1.00204.69 C HETATM 4150 CAX Y01 A 504 30.089 47.415 -6.840 1.00201.86 C HETATM 4151 OAH Y01 A 504 30.824 47.439 -7.869 1.00200.15 O HETATM 4152 OAF Y01 A 504 28.838 47.425 -6.959 1.00198.59 O HETATM 4153 CAA Y01 A 505 18.598 28.608 -12.671 1.00143.71 C HETATM 4154 CBA Y01 A 505 18.877 27.901 -11.347 1.00138.00 C HETATM 4155 CAB Y01 A 505 19.639 26.593 -11.625 1.00127.84 C HETATM 4156 CAN Y01 A 505 19.746 28.811 -10.447 1.00144.93 C HETATM 4157 CAJ Y01 A 505 19.101 30.222 -10.271 1.00153.88 C HETATM 4158 CAO Y01 A 505 20.031 31.040 -9.311 1.00157.10 C HETATM 4159 CBB Y01 A 505 19.627 32.519 -9.199 1.00165.31 C HETATM 4160 CAC Y01 A 505 18.662 32.634 -8.051 1.00157.52 C HETATM 4161 CBE Y01 A 505 20.942 33.337 -8.942 1.00185.91 C HETATM 4162 CAP Y01 A 505 21.971 32.958 -10.008 1.00196.50 C HETATM 4163 CAQ Y01 A 505 22.711 34.311 -10.477 1.00197.98 C HETATM 4164 CBG Y01 A 505 22.267 35.239 -9.338 1.00191.75 C HETATM 4165 CBI Y01 A 505 20.822 34.820 -9.053 1.00187.44 C HETATM 4166 CAE Y01 A 505 19.912 35.197 -10.244 1.00190.86 C HETATM 4167 CAU Y01 A 505 20.394 35.584 -7.767 1.00180.36 C HETATM 4168 CAS Y01 A 505 20.623 37.072 -7.920 1.00178.49 C HETATM 4169 CBF Y01 A 505 21.991 37.456 -8.347 1.00178.81 C HETATM 4170 CBD Y01 A 505 22.341 36.748 -9.643 1.00187.66 C HETATM 4171 CAK Y01 A 505 23.756 37.103 -10.066 1.00185.69 C HETATM 4172 CAI Y01 A 505 24.186 38.535 -9.725 1.00180.17 C HETATM 4173 CAZ Y01 A 505 23.371 39.422 -9.159 1.00178.63 C HETATM 4174 CAV Y01 A 505 23.771 40.882 -9.140 1.00175.40 C HETATM 4175 CBH Y01 A 505 22.058 39.009 -8.548 1.00176.04 C HETATM 4176 CAD Y01 A 505 20.914 39.456 -9.453 1.00179.25 C HETATM 4177 CAT Y01 A 505 21.929 39.704 -7.199 1.00169.40 C HETATM 4178 CAR Y01 A 505 22.113 41.254 -7.303 1.00166.90 C HETATM 4179 CBC Y01 A 505 23.510 41.610 -7.834 1.00172.57 C HETATM 4180 OAW Y01 A 505 23.587 43.000 -8.085 1.00184.35 O HETATM 4181 CAY Y01 A 505 23.889 43.849 -6.975 1.00199.42 C HETATM 4182 OAG Y01 A 505 23.632 43.517 -5.855 1.00207.67 O HETATM 4183 CAM Y01 A 505 24.552 45.221 -7.227 1.00202.75 C HETATM 4184 CAL Y01 A 505 23.540 46.340 -6.921 1.00204.91 C HETATM 4185 CAX Y01 A 505 22.462 46.393 -8.013 1.00211.99 C HETATM 4186 OAH Y01 A 505 22.785 46.253 -9.227 1.00215.00 O HETATM 4187 OAF Y01 A 505 21.259 46.579 -7.698 1.00216.34 O HETATM 4188 C10 OIN A 506 19.656 16.479 0.957 1.00133.19 C HETATM 4189 N OIN A 506 19.850 16.848 2.390 1.00115.19 N HETATM 4190 C11 OIN A 506 20.312 18.101 2.468 1.00 98.66 C HETATM 4191 C17 OIN A 506 19.012 18.959 2.368 1.00114.12 C HETATM 4192 C16 OIN A 506 17.912 17.989 2.663 1.00100.90 C HETATM 4193 C15 OIN A 506 18.703 16.700 3.048 1.00115.22 C HETATM 4194 C14 OIN A 506 18.885 16.693 4.582 1.00116.46 C HETATM 4195 C13 OIN A 506 20.354 17.288 5.005 1.00113.58 C HETATM 4196 C12 OIN A 506 20.950 18.362 3.799 1.00102.63 C HETATM 4197 O2 OIN A 506 21.137 16.318 5.131 1.00107.60 O HETATM 4198 C7 OIN A 506 22.296 16.571 5.909 1.00 92.88 C HETATM 4199 O3 OIN A 506 22.208 17.144 6.950 1.00 97.46 O HETATM 4200 C9 OIN A 506 23.650 16.093 5.410 1.00102.21 C HETATM 4201 C8 OIN A 506 24.599 15.875 6.609 1.00106.06 C HETATM 4202 OH OIN A 506 23.998 14.998 7.541 1.00 85.33 O HETATM 4203 C6 OIN A 506 24.252 17.142 4.461 1.00102.65 C HETATM 4204 C5 OIN A 506 24.543 16.797 3.150 1.00 87.16 C HETATM 4205 C4 OIN A 506 25.090 17.743 2.288 1.00 85.89 C HETATM 4206 C3 OIN A 506 25.340 19.025 2.742 1.00 95.79 C HETATM 4207 C2 OIN A 506 25.050 19.371 4.054 1.00 98.70 C HETATM 4208 C1 OIN A 506 24.504 18.423 4.916 1.00103.65 C HETATM 4209 O HOH A 601 14.688 5.997 -12.087 1.00113.33 O HETATM 4210 O HOH A 602 69.241 59.812 18.005 1.00128.08 O HETATM 4211 O HOH A 603 14.325 13.104 -16.301 1.00 95.45 O HETATM 4212 O HOH A 604 69.315 55.411 28.754 1.00 88.40 O HETATM 4213 O HOH A 605 26.223 0.944 -5.435 1.00 90.50 O HETATM 4214 O HOH A 606 23.381 51.767 28.550 1.00110.74 O HETATM 4215 O HOH C 101 17.586 -18.711 -14.946 1.00 96.78 O CONECT 609 1259 CONECT 1259 609 CONECT 3129 3145 CONECT 3145 3129 CONECT 3366 4047 CONECT 3544 3706 CONECT 3656 3871 CONECT 3706 3544 CONECT 3871 3656 CONECT 3894 3984 CONECT 3984 3894 CONECT 3990 4024 CONECT 4024 3990 CONECT 4044 4045 4046 4047 CONECT 4045 4044 CONECT 4046 4044 CONECT 4047 3366 4044 CONECT 4048 4049 CONECT 4049 4048 4050 4051 CONECT 4050 4049 CONECT 4051 4049 4052 CONECT 4052 4051 4053 CONECT 4053 4052 4054 CONECT 4054 4053 4055 4056 CONECT 4055 4054 CONECT 4056 4054 4057 4060 CONECT 4057 4056 4058 CONECT 4058 4057 4059 CONECT 4059 4058 4060 4065 CONECT 4060 4056 4059 4061 4062 CONECT 4061 4060 CONECT 4062 4060 4063 CONECT 4063 4062 4064 CONECT 4064 4063 4065 4070 CONECT 4065 4059 4064 4066 CONECT 4066 4065 4067 CONECT 4067 4066 4068 CONECT 4068 4067 4069 4070 CONECT 4069 4068 4074 CONECT 4070 4064 4068 4071 4072 CONECT 4071 4070 CONECT 4072 4070 4073 CONECT 4073 4072 4074 CONECT 4074 4069 4073 4075 CONECT 4075 4074 4076 CONECT 4076 4075 4077 4078 CONECT 4077 4076 CONECT 4078 4076 4079 CONECT 4079 4078 4080 CONECT 4080 4079 4081 4082 CONECT 4081 4080 CONECT 4082 4080 CONECT 4083 4084 CONECT 4084 4083 4085 4086 CONECT 4085 4084 CONECT 4086 4084 4087 CONECT 4087 4086 4088 CONECT 4088 4087 4089 CONECT 4089 4088 4090 4091 CONECT 4090 4089 CONECT 4091 4089 4092 4095 CONECT 4092 4091 4093 CONECT 4093 4092 4094 CONECT 4094 4093 4095 4100 CONECT 4095 4091 4094 4096 4097 CONECT 4096 4095 CONECT 4097 4095 4098 CONECT 4098 4097 4099 CONECT 4099 4098 4100 4105 CONECT 4100 4094 4099 4101 CONECT 4101 4100 4102 CONECT 4102 4101 4103 CONECT 4103 4102 4104 4105 CONECT 4104 4103 4109 CONECT 4105 4099 4103 4106 4107 CONECT 4106 4105 CONECT 4107 4105 4108 CONECT 4108 4107 4109 CONECT 4109 4104 4108 4110 CONECT 4110 4109 4111 CONECT 4111 4110 4112 4113 CONECT 4112 4111 CONECT 4113 4111 4114 CONECT 4114 4113 4115 CONECT 4115 4114 4116 4117 CONECT 4116 4115 CONECT 4117 4115 CONECT 4118 4119 CONECT 4119 4118 4120 4121 CONECT 4120 4119 CONECT 4121 4119 4122 CONECT 4122 4121 4123 CONECT 4123 4122 4124 CONECT 4124 4123 4125 4126 CONECT 4125 4124 CONECT 4126 4124 4127 4130 CONECT 4127 4126 4128 CONECT 4128 4127 4129 CONECT 4129 4128 4130 4135 CONECT 4130 4126 4129 4131 4132 CONECT 4131 4130 CONECT 4132 4130 4133 CONECT 4133 4132 4134 CONECT 4134 4133 4135 4140 CONECT 4135 4129 4134 4136 CONECT 4136 4135 4137 CONECT 4137 4136 4138 CONECT 4138 4137 4139 4140 CONECT 4139 4138 4144 CONECT 4140 4134 4138 4141 4142 CONECT 4141 4140 CONECT 4142 4140 4143 CONECT 4143 4142 4144 CONECT 4144 4139 4143 4145 CONECT 4145 4144 4146 CONECT 4146 4145 4147 4148 CONECT 4147 4146 CONECT 4148 4146 4149 CONECT 4149 4148 4150 CONECT 4150 4149 4151 4152 CONECT 4151 4150 CONECT 4152 4150 CONECT 4153 4154 CONECT 4154 4153 4155 4156 CONECT 4155 4154 CONECT 4156 4154 4157 CONECT 4157 4156 4158 CONECT 4158 4157 4159 CONECT 4159 4158 4160 4161 CONECT 4160 4159 CONECT 4161 4159 4162 4165 CONECT 4162 4161 4163 CONECT 4163 4162 4164 CONECT 4164 4163 4165 4170 CONECT 4165 4161 4164 4166 4167 CONECT 4166 4165 CONECT 4167 4165 4168 CONECT 4168 4167 4169 CONECT 4169 4168 4170 4175 CONECT 4170 4164 4169 4171 CONECT 4171 4170 4172 CONECT 4172 4171 4173 CONECT 4173 4172 4174 4175 CONECT 4174 4173 4179 CONECT 4175 4169 4173 4176 4177 CONECT 4176 4175 CONECT 4177 4175 4178 CONECT 4178 4177 4179 CONECT 4179 4174 4178 4180 CONECT 4180 4179 4181 CONECT 4181 4180 4182 4183 CONECT 4182 4181 CONECT 4183 4181 4184 CONECT 4184 4183 4185 CONECT 4185 4184 4186 4187 CONECT 4186 4185 CONECT 4187 4185 CONECT 4188 4189 CONECT 4189 4188 4190 4193 CONECT 4190 4189 4191 4196 CONECT 4191 4190 4192 CONECT 4192 4191 4193 CONECT 4193 4189 4192 4194 CONECT 4194 4193 4195 CONECT 4195 4194 4196 4197 CONECT 4196 4190 4195 CONECT 4197 4195 4198 CONECT 4198 4197 4199 4200 CONECT 4199 4198 CONECT 4200 4198 4201 4203 CONECT 4201 4200 4202 CONECT 4202 4201 CONECT 4203 4200 4204 4208 CONECT 4204 4203 4205 CONECT 4205 4204 4206 CONECT 4206 4205 4207 CONECT 4207 4206 4208 CONECT 4208 4203 4207 MASTER 504 0 6 21 8 0 12 6 4213 2 178 45 END