HEADER SIGNALING PROTEIN 24-NOV-14 4X1H TITLE OPSIN/G(ALPHA) PEPTIDE COMPLEX STABILIZED BY NONYL-GLUCOSIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: C-TERMINAL DERIVED PEPTIDE OF GUANINE NUCLEOTIDE-BINDING COMPND 6 PROTEIN G(T) SUBUNIT ALPHA-1; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 TISSUE: RETINA; SOURCE 6 MOL_ID: 2; SOURCE 7 SYNTHETIC: YES; SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 9 ORGANISM_TAXID: 9913 KEYWDS RHODOPSIN, GPCR, MEMBRANE PROTEIN, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR E.BLANKENSHIP,D.T.LODOWSKI REVDAT 7 29-JUL-20 4X1H 1 COMPND REMARK HETNAM LINK REVDAT 7 2 1 SITE ATOM REVDAT 6 11-DEC-19 4X1H 1 REMARK REVDAT 5 22-NOV-17 4X1H 1 REMARK REVDAT 4 06-SEP-17 4X1H 1 JRNL REMARK REVDAT 3 16-DEC-15 4X1H 1 JRNL REVDAT 2 18-NOV-15 4X1H 1 JRNL REVDAT 1 04-NOV-15 4X1H 0 JRNL AUTH E.BLANKENSHIP,A.VAHEDI-FARIDI,D.T.LODOWSKI JRNL TITL THE HIGH-RESOLUTION STRUCTURE OF ACTIVATED OPSIN REVEALS A JRNL TITL 2 CONSERVED SOLVENT NETWORK IN THE TRANSMEMBRANE REGION JRNL TITL 3 ESSENTIAL FOR ACTIVATION. JRNL REF STRUCTURE V. 23 2358 2015 JRNL REFN ISSN 0969-2126 JRNL PMID 26526852 JRNL DOI 10.1016/J.STR.2015.09.015 REMARK 2 REMARK 2 RESOLUTION. 2.29 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1839) 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) : 2.29 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.91 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8 REMARK 3 NUMBER OF REFLECTIONS : 50642 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 2554 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 39.9135 - 5.9952 0.95 2861 146 0.1945 0.1799 REMARK 3 2 5.9952 - 4.7611 0.98 2882 143 0.1877 0.2039 REMARK 3 3 4.7611 - 4.1600 0.99 2884 158 0.1878 0.1870 REMARK 3 4 4.1600 - 3.7799 0.98 2857 155 0.1908 0.1944 REMARK 3 5 3.7799 - 3.5092 0.93 2697 153 0.1941 0.2112 REMARK 3 6 3.5092 - 3.3024 0.96 2766 179 0.2167 0.2288 REMARK 3 7 3.3024 - 3.1371 0.96 2775 142 0.2157 0.2432 REMARK 3 8 3.1371 - 3.0006 0.95 2745 158 0.2213 0.2493 REMARK 3 9 3.0006 - 2.8851 0.94 2703 139 0.2262 0.2713 REMARK 3 10 2.8851 - 2.7856 0.85 2515 125 0.2370 0.2729 REMARK 3 11 2.7856 - 2.6985 0.86 2496 135 0.2629 0.3427 REMARK 3 12 2.6985 - 2.6214 0.89 2613 114 0.2852 0.3164 REMARK 3 13 2.6214 - 2.5524 0.90 2607 121 0.2780 0.2908 REMARK 3 14 2.5524 - 2.4901 0.90 2574 155 0.2815 0.2726 REMARK 3 15 2.4901 - 2.4335 0.90 2603 137 0.3164 0.3474 REMARK 3 16 2.4335 - 2.3817 0.90 2587 146 0.3369 0.3743 REMARK 3 17 2.3817 - 2.3341 0.89 2577 131 0.3386 0.3425 REMARK 3 18 2.3341 - 2.2900 0.81 2346 117 0.3672 0.3405 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.090 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.004 2972 REMARK 3 ANGLE : 0.878 4046 REMARK 3 CHIRALITY : 0.036 465 REMARK 3 PLANARITY : 0.004 488 REMARK 3 DIHEDRAL : 13.420 1082 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 16 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7998 -65.4033 -38.4804 REMARK 3 T TENSOR REMARK 3 T11: 0.5952 T22: 0.3035 REMARK 3 T33: 0.9137 T12: -0.0511 REMARK 3 T13: -0.0094 T23: 0.1878 REMARK 3 L TENSOR REMARK 3 L11: 4.3454 L22: 9.4111 REMARK 3 L33: 3.6838 L12: -3.7707 REMARK 3 L13: -1.1687 L23: 5.4167 REMARK 3 S TENSOR REMARK 3 S11: -0.0899 S12: 0.1805 S13: -0.1110 REMARK 3 S21: 0.4486 S22: 0.1161 S23: 1.1012 REMARK 3 S31: 0.6999 S32: -0.2875 S33: -0.0174 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 140 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.7868 -38.1699 -40.1027 REMARK 3 T TENSOR REMARK 3 T11: 0.3487 T22: 0.2448 REMARK 3 T33: 0.6120 T12: 0.0085 REMARK 3 T13: 0.0516 T23: 0.0714 REMARK 3 L TENSOR REMARK 3 L11: 1.3209 L22: 2.3769 REMARK 3 L33: 1.2240 L12: -0.8568 REMARK 3 L13: -0.0239 L23: 0.1424 REMARK 3 S TENSOR REMARK 3 S11: -0.0543 S12: -0.0749 S13: -0.0358 REMARK 3 S21: 0.2766 S22: 0.0101 S23: -0.3866 REMARK 3 S31: 0.0365 S32: -0.0135 S33: 0.0254 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 168 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.5914 -25.9207 -24.6398 REMARK 3 T TENSOR REMARK 3 T11: 0.6098 T22: 0.3557 REMARK 3 T33: 0.4004 T12: 0.0961 REMARK 3 T13: 0.1178 T23: 0.0222 REMARK 3 L TENSOR REMARK 3 L11: 5.8354 L22: 2.7707 REMARK 3 L33: 4.3955 L12: 0.4622 REMARK 3 L13: 0.6078 L23: 0.1150 REMARK 3 S TENSOR REMARK 3 S11: -0.3995 S12: -0.6658 S13: 0.4105 REMARK 3 S21: 0.7293 S22: 0.1418 S23: 0.6164 REMARK 3 S31: -0.5508 S32: -0.2201 S33: 0.2163 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 169 THROUGH 185 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.7642 -51.7568 -31.3877 REMARK 3 T TENSOR REMARK 3 T11: 0.6307 T22: 0.3554 REMARK 3 T33: 0.7749 T12: 0.1155 REMARK 3 T13: 0.1258 T23: 0.1674 REMARK 3 L TENSOR REMARK 3 L11: 2.9529 L22: 3.2721 REMARK 3 L33: 2.6611 L12: -1.8031 REMARK 3 L13: -2.2404 L23: 2.8112 REMARK 3 S TENSOR REMARK 3 S11: -0.6457 S12: -0.1799 S13: -0.5955 REMARK 3 S21: 0.6260 S22: 0.2994 S23: 0.2285 REMARK 3 S31: 0.3123 S32: -0.2001 S33: 0.2338 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 186 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.2418 -52.5469 -29.1612 REMARK 3 T TENSOR REMARK 3 T11: 0.7197 T22: 0.4380 REMARK 3 T33: 0.8706 T12: 0.0188 REMARK 3 T13: 0.2001 T23: 0.1965 REMARK 3 L TENSOR REMARK 3 L11: 3.8289 L22: 0.4076 REMARK 3 L33: 2.8306 L12: -0.9699 REMARK 3 L13: -1.2147 L23: 0.8776 REMARK 3 S TENSOR REMARK 3 S11: -0.2181 S12: -0.3094 S13: -0.9232 REMARK 3 S21: 0.3426 S22: 0.1043 S23: 0.0796 REMARK 3 S31: 0.8015 S32: -0.1626 S33: -0.0413 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 213 THROUGH 240 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5810 -25.4130 -36.9252 REMARK 3 T TENSOR REMARK 3 T11: 0.3819 T22: 0.4732 REMARK 3 T33: 0.7845 T12: 0.0600 REMARK 3 T13: 0.1538 T23: -0.0006 REMARK 3 L TENSOR REMARK 3 L11: 3.9705 L22: 7.7854 REMARK 3 L33: 6.3582 L12: -4.3828 REMARK 3 L13: 3.3223 L23: -5.8634 REMARK 3 S TENSOR REMARK 3 S11: -0.3453 S12: -0.3235 S13: 0.4224 REMARK 3 S21: 0.4063 S22: 0.3585 S23: 0.7425 REMARK 3 S31: -0.3517 S32: -0.7067 S33: -0.0694 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 277 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.2040 -35.4983 -42.5854 REMARK 3 T TENSOR REMARK 3 T11: 0.3277 T22: 0.3766 REMARK 3 T33: 0.6612 T12: -0.0022 REMARK 3 T13: 0.1161 T23: -0.0394 REMARK 3 L TENSOR REMARK 3 L11: 5.7948 L22: 6.4099 REMARK 3 L33: 2.9001 L12: -5.0213 REMARK 3 L13: 1.2670 L23: -1.1336 REMARK 3 S TENSOR REMARK 3 S11: -0.1855 S12: -0.1389 S13: 0.0704 REMARK 3 S21: 0.0477 S22: 0.1240 S23: -0.2363 REMARK 3 S31: 0.1319 S32: -0.3690 S33: 0.0838 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 306 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.7290 -46.3657 -43.7458 REMARK 3 T TENSOR REMARK 3 T11: 0.7080 T22: 0.3519 REMARK 3 T33: 1.1024 T12: 0.0391 REMARK 3 T13: 0.1933 T23: 0.0452 REMARK 3 L TENSOR REMARK 3 L11: 0.7960 L22: 0.2944 REMARK 3 L33: 2.5966 L12: 0.3129 REMARK 3 L13: 1.2797 L23: 0.2059 REMARK 3 S TENSOR REMARK 3 S11: -0.0355 S12: -0.1077 S13: -1.1566 REMARK 3 S21: 0.8417 S22: 0.0154 S23: 0.3736 REMARK 3 S31: 1.0210 S32: 0.0694 S33: -0.1585 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 307 THROUGH 326 ) REMARK 3 ORIGIN FOR THE GROUP (A): 14.6797 -16.9530 -48.2677 REMARK 3 T TENSOR REMARK 3 T11: 0.5237 T22: 0.3421 REMARK 3 T33: 0.8125 T12: 0.0914 REMARK 3 T13: 0.0550 T23: 0.0746 REMARK 3 L TENSOR REMARK 3 L11: 5.7608 L22: 8.9413 REMARK 3 L33: 9.0282 L12: 6.3862 REMARK 3 L13: -4.4993 L23: -2.4053 REMARK 3 S TENSOR REMARK 3 S11: 0.1532 S12: 0.0768 S13: 0.1745 REMARK 3 S21: -0.0388 S22: 0.1251 S23: 0.0566 REMARK 3 S31: -0.3562 S32: 0.0972 S33: -0.3973 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 340 THROUGH 350 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6051 -14.9053 -38.9274 REMARK 3 T TENSOR REMARK 3 T11: 0.6174 T22: 0.5003 REMARK 3 T33: 0.8582 T12: 0.1955 REMARK 3 T13: 0.1419 T23: 0.1375 REMARK 3 L TENSOR REMARK 3 L11: 9.9619 L22: 4.1923 REMARK 3 L33: 2.9687 L12: -2.9519 REMARK 3 L13: 4.9010 L23: -0.0929 REMARK 3 S TENSOR REMARK 3 S11: -0.2639 S12: 0.3075 S13: 0.8262 REMARK 3 S21: 0.9278 S22: 0.2487 S23: 0.9118 REMARK 3 S31: -1.4576 S32: -0.7778 S33: 0.1742 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 4X1H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-14. REMARK 100 THE DEPOSITION ID IS D_1000204877. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-AUG-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920 REMARK 200 MONOCHROMATOR : CRYO-COOLED SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : XDS, AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57205 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.230 REMARK 200 RESOLUTION RANGE LOW (A) : 39.910 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.02600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 56.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.23 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.85000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3CAP 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: 3.1M AMMONIUM SULFATE, 100MM CITRATE, REMARK 280 PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 121.06800 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.89864 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.57367 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.06800 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.89864 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.57367 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.06800 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.89864 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.57367 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.06800 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 69.89864 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.57367 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.06800 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 69.89864 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.57367 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.06800 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 69.89864 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.57367 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 139.79728 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.14733 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 139.79728 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.14733 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 139.79728 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 73.14733 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 139.79728 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.14733 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 139.79728 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 73.14733 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 139.79728 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 73.14733 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: 5130 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17540 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 400 REMARK 400 COMPOUND REMARK 400 THE C-TERMINAL DERIVED PEPTIDE OF GUANINE NUCLEOTIDE-BINDING REMARK 400 PROTEIN G(T) IS DERIVED FROM 340-350 POSITIONS IN THE TRANSDUCIN REMARK 400 ALPHA SUBUNIT UTILIZING A PHAGE DISPLAY LIBRARY DERIVED FROM THE C REMARK 400 TERMINAL REGION OF TRANSDUCIN (ARIS, L, ET AL 2001) WITH SEQUENCE " REMARK 400 IKENLKDCGLF". THE CONSTRUCT IN THIS STRUCTURE HAS THE FOLLOWING REMARK 400 SEQUENCE: "VLEDLKSCGLF." HENCE THERE ARE THE FOLLOWING MUTATIONS REMARK 400 I340V, K341L, N342D, AND D346S. 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 PRO A 327 REMARK 465 LEU A 328 REMARK 465 GLY A 329 REMARK 465 ASP A 330 REMARK 465 ASP A 331 REMARK 465 GLU A 332 REMARK 465 ALA A 333 REMARK 465 SER A 334 REMARK 465 THR A 335 REMARK 465 THR A 336 REMARK 465 VAL A 337 REMARK 465 SER A 338 REMARK 465 LYS A 339 REMARK 465 THR A 340 REMARK 465 GLU A 341 REMARK 465 THR A 342 REMARK 465 SER A 343 REMARK 465 GLN A 344 REMARK 465 VAL A 345 REMARK 465 ALA A 346 REMARK 465 PRO A 347 REMARK 465 ALA A 348 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 2 -12.33 72.81 REMARK 500 GLN A 28 43.13 -102.49 REMARK 500 SER A 176 -160.66 62.22 REMARK 500 PHE A 212 -56.53 -139.53 REMARK 500 GLN A 237 54.07 -149.30 REMARK 500 HIS A 278 67.05 -111.81 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 PLM A 1322 DBREF 4X1H A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 4X1H C 340 350 PDB 4X1H 4X1H 340 350 SEQRES 1 A 348 MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE SEQRES 2 A 348 SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA SEQRES 3 A 348 PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET SEQRES 4 A 348 LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE SEQRES 5 A 348 PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS SEQRES 6 A 348 LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN SEQRES 7 A 348 LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE SEQRES 8 A 348 THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL SEQRES 9 A 348 PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA SEQRES 10 A 348 THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL SEQRES 11 A 348 LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET SEQRES 12 A 348 SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY SEQRES 13 A 348 VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA SEQRES 14 A 348 PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY SEQRES 15 A 348 MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS SEQRES 16 A 348 GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE SEQRES 17 A 348 VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE SEQRES 18 A 348 CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA SEQRES 19 A 348 ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU SEQRES 20 A 348 LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA SEQRES 21 A 348 PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE SEQRES 22 A 348 TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE SEQRES 23 A 348 PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA SEQRES 24 A 348 VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN SEQRES 25 A 348 PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS SEQRES 26 A 348 ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER SEQRES 27 A 348 LYS THR GLU THR SER GLN VAL ALA PRO ALA SEQRES 1 C 11 VAL LEU GLU ASP LEU LYS SER CYS GLY LEU PHE HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET BMA B 4 11 HET NAG D 1 14 HET NAG D 2 14 HET BNG A 407 21 HET BNG A 410 21 HET PLM A1322 7 HET PLM A1323 17 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM BNG NONYL BETA-D-GLUCOPYRANOSIDE HETNAM PLM PALMITIC ACID FORMUL 3 NAG 4(C8 H15 N O6) FORMUL 3 BMA 2(C6 H12 O6) FORMUL 5 BNG 2(C15 H30 O6) FORMUL 7 PLM 2(C16 H32 O2) FORMUL 9 HOH *65(H2 O) HELIX 1 AA1 GLU A 33 HIS A 65 1 33 HELIX 2 AA2 LYS A 66 ARG A 69 5 4 HELIX 3 AA3 THR A 70 LEU A 72 5 3 HELIX 4 AA4 ASN A 73 GLY A 90 1 18 HELIX 5 AA5 GLY A 90 LEU A 99 1 10 HELIX 6 AA6 PHE A 105 LYS A 141 1 37 HELIX 7 AA7 GLY A 149 ALA A 169 1 21 HELIX 8 AA8 PRO A 170 VAL A 173 5 4 HELIX 9 AA9 HIS A 195 THR A 198 5 4 HELIX 10 AB1 ASN A 199 HIS A 211 1 13 HELIX 11 AB2 PHE A 212 GLN A 236 1 25 HELIX 12 AB3 SER A 240 HIS A 278 1 39 HELIX 13 AB4 GLY A 284 THR A 297 1 14 HELIX 14 AB5 THR A 297 ILE A 307 1 11 HELIX 15 AB6 ASN A 310 CYS A 322 1 13 HELIX 16 AB7 LEU C 341 CYS C 347 1 7 SHEET 1 AA1 2 THR A 4 GLY A 6 0 SHEET 2 AA1 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.04 LINK ND2 ASN A 2 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.44 LINK SG CYS A 322 C1 PLM A1322 1555 1555 1.77 LINK SG CYS A 323 C1 PLM A1323 1555 1555 1.77 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.46 LINK O2 BMA B 3 C1 BMA B 4 1555 1555 1.47 LINK O3 NAG D 1 C1 NAG D 2 1555 1555 1.44 CRYST1 242.136 242.136 109.721 90.00 90.00 120.00 H 3 2 18 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 0.004130 0.002384 0.000000 0.00000 SCALE2 0.000000 0.004769 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009114 0.00000 ATOM 1 N MET A 1 13.998 -71.447 -40.909 1.00126.30 N ANISOU 1 N MET A 1 14705 11909 21376 -1742 96 744 N ATOM 2 CA MET A 1 13.411 -70.552 -39.919 1.00125.14 C ANISOU 2 CA MET A 1 14485 11806 21257 -1755 461 826 C ATOM 3 C MET A 1 13.673 -69.091 -40.268 1.00110.13 C ANISOU 3 C MET A 1 12444 10148 19254 -1568 115 967 C ATOM 4 O MET A 1 13.400 -68.192 -39.467 1.00107.96 O ANISOU 4 O MET A 1 12134 9911 18975 -1546 355 1073 O ATOM 5 CB MET A 1 13.949 -70.872 -38.526 1.00130.80 C ANISOU 5 CB MET A 1 15784 12440 21472 -1725 969 1085 C ATOM 6 CG MET A 1 15.441 -71.139 -38.485 1.00131.21 C ANISOU 6 CG MET A 1 16369 12549 20935 -1526 789 1322 C ATOM 7 SD MET A 1 15.970 -71.654 -36.843 1.00131.74 S ANISOU 7 SD MET A 1 17148 12446 20462 -1421 1267 1534 S ATOM 8 CE MET A 1 14.650 -72.791 -36.421 1.00134.15 C ANISOU 8 CE MET A 1 17375 12429 21166 -1716 1789 1370 C ATOM 9 N ASN A 2 14.229 -68.875 -41.458 1.00 97.69 N ANISOU 9 N ASN A 2 10870 8853 17394 -1351 -424 941 N ATOM 10 CA ASN A 2 14.295 -67.555 -42.088 1.00 92.94 C ANISOU 10 CA ASN A 2 10157 8543 16613 -1104 -779 1005 C ATOM 11 C ASN A 2 15.287 -66.564 -41.484 1.00 74.59 C ANISOU 11 C ASN A 2 8143 6340 13857 -972 -642 1339 C ATOM 12 O ASN A 2 15.572 -65.532 -42.087 1.00 80.60 O ANISOU 12 O ASN A 2 8906 7296 14421 -770 -888 1431 O ATOM 13 CB ASN A 2 12.895 -66.935 -42.098 1.00100.51 C ANISOU 13 CB ASN A 2 10604 9467 18117 -1137 -828 747 C ATOM 14 CG ASN A 2 11.902 -67.813 -42.807 1.00125.61 C ANISOU 14 CG ASN A 2 13370 12540 21818 -1224 -1045 287 C ATOM 15 OD1 ASN A 2 12.238 -68.416 -43.828 1.00126.48 O ANISOU 15 OD1 ASN A 2 13552 12749 21754 -1095 -1432 165 O ATOM 16 ND2 ASN A 2 10.682 -67.918 -42.280 1.00156.38 N ANISOU 16 ND2 ASN A 2 16802 16221 26393 -1441 -784 -26 N ATOM 17 N GLY A 3 15.819 -66.870 -40.308 1.00 61.89 N ANISOU 17 N GLY A 3 6821 4588 12106 -1053 -252 1494 N ATOM 18 CA GLY A 3 16.756 -65.963 -39.672 1.00 57.76 C ANISOU 18 CA GLY A 3 6531 4170 11244 -899 -161 1704 C ATOM 19 C GLY A 3 17.939 -66.672 -39.050 1.00 55.85 C ANISOU 19 C GLY A 3 6730 3861 10630 -830 -37 1786 C ATOM 20 O GLY A 3 17.920 -67.887 -38.855 1.00 54.72 O ANISOU 20 O GLY A 3 6780 3531 10482 -921 77 1744 O ATOM 21 N THR A 4 18.977 -65.904 -38.746 1.00 55.51 N ANISOU 21 N THR A 4 6837 3947 10308 -646 -75 1861 N ATOM 22 CA THR A 4 20.143 -66.423 -38.049 1.00 58.87 C ANISOU 22 CA THR A 4 7646 4323 10399 -494 -28 1850 C ATOM 23 C THR A 4 20.437 -65.551 -36.836 1.00 47.78 C ANISOU 23 C THR A 4 6332 2926 8896 -330 145 1867 C ATOM 24 O THR A 4 20.765 -64.380 -36.979 1.00 57.11 O ANISOU 24 O THR A 4 7314 4244 10140 -254 69 1860 O ATOM 25 CB THR A 4 21.376 -66.466 -38.961 1.00 54.31 C ANISOU 25 CB THR A 4 7120 3913 9601 -381 -305 1763 C ATOM 26 OG1 THR A 4 21.070 -67.208 -40.148 1.00 47.26 O ANISOU 26 OG1 THR A 4 6149 3052 8755 -494 -494 1724 O ATOM 27 CG2 THR A 4 22.537 -67.120 -38.243 1.00 47.91 C ANISOU 27 CG2 THR A 4 6662 3040 8502 -188 -324 1652 C ATOM 28 N GLU A 5 20.312 -66.126 -35.645 1.00 60.20 N ANISOU 28 N GLU A 5 8243 4320 10311 -253 392 1887 N ATOM 29 CA GLU A 5 20.503 -65.373 -34.409 1.00 49.71 C ANISOU 29 CA GLU A 5 7054 2953 8880 -40 550 1898 C ATOM 30 C GLU A 5 21.956 -65.320 -33.956 1.00 65.02 C ANISOU 30 C GLU A 5 9256 4966 10483 312 325 1721 C ATOM 31 O GLU A 5 22.759 -66.207 -34.259 1.00 55.52 O ANISOU 31 O GLU A 5 8282 3737 9078 412 139 1627 O ATOM 32 CB GLU A 5 19.657 -65.971 -33.280 1.00 54.30 C ANISOU 32 CB GLU A 5 7958 3322 9353 -64 955 1975 C ATOM 33 CG GLU A 5 18.161 -65.876 -33.489 1.00 63.89 C ANISOU 33 CG GLU A 5 8815 4530 10930 -393 1210 1989 C ATOM 34 CD GLU A 5 17.382 -66.544 -32.374 1.00 81.40 C ANISOU 34 CD GLU A 5 11353 6515 13060 -444 1697 2035 C ATOM 35 OE1 GLU A 5 17.527 -67.775 -32.199 1.00 87.22 O ANISOU 35 OE1 GLU A 5 12479 7077 13584 -449 1807 2058 O ATOM 36 OE2 GLU A 5 16.633 -65.838 -31.667 1.00 82.96 O ANISOU 36 OE2 GLU A 5 11423 6694 13405 -472 1994 2046 O ATOM 37 N GLY A 6 22.273 -64.267 -33.211 1.00 60.95 N ANISOU 37 N GLY A 6 8667 4537 9953 519 321 1615 N ATOM 38 CA GLY A 6 23.584 -64.087 -32.620 1.00 51.05 C ANISOU 38 CA GLY A 6 7585 3346 8466 905 86 1329 C ATOM 39 C GLY A 6 23.452 -63.173 -31.420 1.00 59.44 C ANISOU 39 C GLY A 6 8681 4419 9484 1152 184 1241 C ATOM 40 O GLY A 6 22.426 -62.510 -31.261 1.00 64.07 O ANISOU 40 O GLY A 6 9059 5003 10283 967 428 1409 O ATOM 41 N PRO A 7 24.489 -63.131 -30.570 1.00 57.60 N ANISOU 41 N PRO A 7 8693 4203 8989 1608 -42 922 N ATOM 42 CA PRO A 7 24.505 -62.359 -29.318 1.00 63.35 C ANISOU 42 CA PRO A 7 9530 4948 9593 1962 -22 754 C ATOM 43 C PRO A 7 23.949 -60.923 -29.420 1.00 75.53 C ANISOU 43 C PRO A 7 10526 6605 11565 1757 107 773 C ATOM 44 O PRO A 7 23.133 -60.535 -28.577 1.00 78.60 O ANISOU 44 O PRO A 7 11020 6954 11892 1814 346 882 O ATOM 45 CB PRO A 7 25.987 -62.356 -28.955 1.00 62.49 C ANISOU 45 CB PRO A 7 9493 4910 9341 2440 -460 246 C ATOM 46 CG PRO A 7 26.459 -63.700 -29.446 1.00 54.48 C ANISOU 46 CG PRO A 7 8816 3804 8081 2461 -602 275 C ATOM 47 CD PRO A 7 25.721 -63.926 -30.740 1.00 51.78 C ANISOU 47 CD PRO A 7 8168 3466 8039 1871 -379 641 C ATOM 48 N ASN A 8 24.357 -60.154 -30.425 1.00 49.98 N ANISOU 48 N ASN A 8 6763 3480 8749 1531 -6 678 N ATOM 49 CA ASN A 8 23.806 -58.804 -30.584 1.00 60.13 C ANISOU 49 CA ASN A 8 7588 4820 10440 1350 123 728 C ATOM 50 C ASN A 8 23.283 -58.526 -31.980 1.00 53.58 C ANISOU 50 C ASN A 8 6429 4003 9927 925 207 997 C ATOM 51 O ASN A 8 23.414 -57.409 -32.474 1.00 47.57 O ANISOU 51 O ASN A 8 5299 3264 9514 825 219 954 O ATOM 52 CB ASN A 8 24.850 -57.735 -30.252 1.00 49.14 C ANISOU 52 CB ASN A 8 5886 3488 9298 1591 -61 283 C ATOM 53 CG ASN A 8 25.413 -57.878 -28.864 1.00 61.70 C ANISOU 53 CG ASN A 8 7781 5089 10573 2120 -249 -85 C ATOM 54 OD1 ASN A 8 24.778 -57.502 -27.882 1.00 70.98 O ANISOU 54 OD1 ASN A 8 9094 6263 11613 2296 -138 -54 O ATOM 55 ND2 ASN A 8 26.625 -58.403 -28.774 1.00 61.59 N ANISOU 55 ND2 ASN A 8 7880 5089 10434 2420 -557 -481 N ATOM 56 N PHE A 9 22.706 -59.530 -32.628 1.00 51.82 N ANISOU 56 N PHE A 9 6366 3741 9581 710 260 1254 N ATOM 57 CA PHE A 9 22.184 -59.318 -33.973 1.00 51.69 C ANISOU 57 CA PHE A 9 6093 3749 9800 398 266 1466 C ATOM 58 C PHE A 9 21.152 -60.354 -34.398 1.00 51.13 C ANISOU 58 C PHE A 9 6140 3621 9667 187 337 1692 C ATOM 59 O PHE A 9 20.963 -61.385 -33.751 1.00 48.99 O ANISOU 59 O PHE A 9 6188 3251 9174 231 438 1714 O ATOM 60 CB PHE A 9 23.331 -59.288 -35.000 1.00 45.05 C ANISOU 60 CB PHE A 9 5171 2952 8995 376 123 1345 C ATOM 61 CG PHE A 9 24.112 -60.579 -35.101 1.00 55.09 C ANISOU 61 CG PHE A 9 6725 4223 9982 460 -14 1225 C ATOM 62 CD1 PHE A 9 23.663 -61.626 -35.895 1.00 52.01 C ANISOU 62 CD1 PHE A 9 6473 3820 9467 287 -48 1410 C ATOM 63 CD2 PHE A 9 25.312 -60.731 -34.424 1.00 50.41 C ANISOU 63 CD2 PHE A 9 6232 3638 9283 744 -154 867 C ATOM 64 CE1 PHE A 9 24.386 -62.808 -35.992 1.00 46.86 C ANISOU 64 CE1 PHE A 9 6082 3151 8573 372 -184 1289 C ATOM 65 CE2 PHE A 9 26.039 -61.910 -34.519 1.00 57.84 C ANISOU 65 CE2 PHE A 9 7438 4568 9970 864 -324 723 C ATOM 66 CZ PHE A 9 25.578 -62.946 -35.303 1.00 44.81 C ANISOU 66 CZ PHE A 9 5949 2894 8184 664 -323 959 C ATOM 67 N TYR A 10 20.488 -60.052 -35.506 1.00 51.65 N ANISOU 67 N TYR A 10 5962 3718 9943 -14 286 1832 N ATOM 68 CA TYR A 10 19.581 -60.976 -36.156 1.00 52.49 C ANISOU 68 CA TYR A 10 6072 3819 10051 -200 268 1917 C ATOM 69 C TYR A 10 19.673 -60.771 -37.662 1.00 51.35 C ANISOU 69 C TYR A 10 5800 3766 9946 -260 47 1967 C ATOM 70 O TYR A 10 19.195 -59.775 -38.190 1.00 52.07 O ANISOU 70 O TYR A 10 5685 3890 10208 -255 -11 2030 O ATOM 71 CB TYR A 10 18.143 -60.773 -35.672 1.00 47.91 C ANISOU 71 CB TYR A 10 5300 3177 9728 -318 451 1952 C ATOM 72 CG TYR A 10 17.151 -61.672 -36.372 1.00 51.82 C ANISOU 72 CG TYR A 10 5685 3606 10400 -517 427 1951 C ATOM 73 CD1 TYR A 10 17.017 -63.009 -36.006 1.00 60.04 C ANISOU 73 CD1 TYR A 10 6964 4519 11331 -611 598 1919 C ATOM 74 CD2 TYR A 10 16.357 -61.191 -37.406 1.00 57.61 C ANISOU 74 CD2 TYR A 10 6089 4348 11452 -582 213 1956 C ATOM 75 CE1 TYR A 10 16.117 -63.841 -36.648 1.00 60.22 C ANISOU 75 CE1 TYR A 10 6820 4443 11619 -810 590 1847 C ATOM 76 CE2 TYR A 10 15.451 -62.014 -38.053 1.00 60.29 C ANISOU 76 CE2 TYR A 10 6262 4629 12017 -725 126 1844 C ATOM 77 CZ TYR A 10 15.335 -63.338 -37.672 1.00 68.70 C ANISOU 77 CZ TYR A 10 7483 5535 13086 -878 335 1793 C ATOM 78 OH TYR A 10 14.431 -64.152 -38.321 1.00 71.07 O ANISOU 78 OH TYR A 10 7548 5746 13709 -1037 260 1610 O ATOM 79 N VAL A 11 20.300 -61.708 -38.355 1.00 52.02 N ANISOU 79 N VAL A 11 6057 3848 9860 -279 -78 1954 N ATOM 80 CA VAL A 11 20.380 -61.611 -39.803 1.00 52.21 C ANISOU 80 CA VAL A 11 6044 3929 9865 -296 -268 2020 C ATOM 81 C VAL A 11 19.136 -62.245 -40.422 1.00 55.26 C ANISOU 81 C VAL A 11 6314 4302 10381 -393 -416 2023 C ATOM 82 O VAL A 11 18.830 -63.407 -40.164 1.00 54.62 O ANISOU 82 O VAL A 11 6288 4147 10317 -496 -389 1950 O ATOM 83 CB VAL A 11 21.655 -62.285 -40.340 1.00 54.16 C ANISOU 83 CB VAL A 11 6495 4222 9860 -256 -335 1934 C ATOM 84 CG1 VAL A 11 21.726 -62.153 -41.854 1.00 45.53 C ANISOU 84 CG1 VAL A 11 5437 3200 8661 -241 -476 2004 C ATOM 85 CG2 VAL A 11 22.884 -61.666 -39.686 1.00 44.44 C ANISOU 85 CG2 VAL A 11 5283 2986 8615 -148 -210 1801 C ATOM 86 N PRO A 12 18.398 -61.471 -41.230 1.00 57.31 N ANISOU 86 N PRO A 12 6412 4602 10762 -333 -578 2070 N ATOM 87 CA PRO A 12 17.178 -61.985 -41.866 1.00 54.37 C ANISOU 87 CA PRO A 12 5851 4225 10580 -361 -805 1955 C ATOM 88 C PRO A 12 17.475 -62.940 -43.020 1.00 57.23 C ANISOU 88 C PRO A 12 6360 4655 10731 -319 -1059 1884 C ATOM 89 O PRO A 12 16.937 -62.775 -44.115 1.00 58.52 O ANISOU 89 O PRO A 12 6484 4883 10868 -163 -1374 1826 O ATOM 90 CB PRO A 12 16.490 -60.716 -42.373 1.00 52.60 C ANISOU 90 CB PRO A 12 5481 4027 10476 -194 -972 2001 C ATOM 91 CG PRO A 12 17.617 -59.749 -42.596 1.00 51.13 C ANISOU 91 CG PRO A 12 5539 3854 10033 -77 -857 2201 C ATOM 92 CD PRO A 12 18.613 -60.039 -41.509 1.00 48.58 C ANISOU 92 CD PRO A 12 5290 3507 9660 -201 -562 2191 C ATOM 93 N PHE A 13 18.327 -63.926 -42.766 1.00 50.35 N ANISOU 93 N PHE A 13 5680 3765 9687 -408 -955 1862 N ATOM 94 CA PHE A 13 18.696 -64.911 -43.770 1.00 56.22 C ANISOU 94 CA PHE A 13 6559 4569 10232 -378 -1175 1768 C ATOM 95 C PHE A 13 19.000 -66.247 -43.097 1.00 50.45 C ANISOU 95 C PHE A 13 5926 3721 9520 -532 -1046 1675 C ATOM 96 O PHE A 13 19.697 -66.292 -42.083 1.00 63.87 O ANISOU 96 O PHE A 13 7786 5352 11129 -554 -811 1736 O ATOM 97 CB PHE A 13 19.904 -64.429 -44.577 1.00 56.78 C ANISOU 97 CB PHE A 13 6889 4753 9931 -232 -1193 1874 C ATOM 98 CG PHE A 13 20.091 -65.153 -45.880 1.00 55.68 C ANISOU 98 CG PHE A 13 6893 4711 9550 -129 -1457 1783 C ATOM 99 CD1 PHE A 13 19.439 -64.723 -47.025 1.00 54.19 C ANISOU 99 CD1 PHE A 13 6738 4599 9253 85 -1739 1784 C ATOM 100 CD2 PHE A 13 20.914 -66.266 -45.959 1.00 60.87 C ANISOU 100 CD2 PHE A 13 7685 5383 10059 -194 -1457 1672 C ATOM 101 CE1 PHE A 13 19.607 -65.388 -48.226 1.00 57.05 C ANISOU 101 CE1 PHE A 13 7275 5064 9336 239 -2004 1675 C ATOM 102 CE2 PHE A 13 21.085 -66.937 -47.157 1.00 52.21 C ANISOU 102 CE2 PHE A 13 6714 4388 8736 -87 -1702 1562 C ATOM 103 CZ PHE A 13 20.432 -66.495 -48.293 1.00 54.94 C ANISOU 103 CZ PHE A 13 7103 4824 8948 132 -1969 1564 C ATOM 104 N SER A 14 18.472 -67.329 -43.662 1.00 58.47 N ANISOU 104 N SER A 14 6867 4692 10654 -598 -1221 1501 N ATOM 105 CA SER A 14 18.670 -68.663 -43.102 1.00 58.06 C ANISOU 105 CA SER A 14 6949 4463 10648 -742 -1081 1421 C ATOM 106 C SER A 14 20.111 -69.136 -43.254 1.00 58.65 C ANISOU 106 C SER A 14 7347 4605 10331 -645 -1126 1444 C ATOM 107 O SER A 14 20.725 -68.950 -44.300 1.00 57.40 O ANISOU 107 O SER A 14 7241 4630 9937 -521 -1337 1417 O ATOM 108 CB SER A 14 17.733 -69.669 -43.768 1.00 55.70 C ANISOU 108 CB SER A 14 6428 4071 10663 -845 -1263 1167 C ATOM 109 OG SER A 14 18.060 -70.992 -43.379 1.00 56.22 O ANISOU 109 OG SER A 14 6686 3930 10746 -970 -1124 1106 O ATOM 110 N ASN A 15 20.641 -69.763 -42.210 1.00 55.76 N ANISOU 110 N ASN A 15 7227 4073 9888 -669 -917 1470 N ATOM 111 CA ASN A 15 22.005 -70.275 -42.254 1.00 49.87 C ANISOU 111 CA ASN A 15 6757 3372 8822 -540 -1003 1407 C ATOM 112 C ASN A 15 22.053 -71.782 -42.503 1.00 50.26 C ANISOU 112 C ASN A 15 6955 3269 8872 -594 -1099 1275 C ATOM 113 O ASN A 15 22.963 -72.466 -42.034 1.00 56.52 O ANISOU 113 O ASN A 15 8045 3970 9459 -485 -1103 1220 O ATOM 114 CB ASN A 15 22.743 -69.943 -40.955 1.00 49.49 C ANISOU 114 CB ASN A 15 6936 3247 8622 -408 -817 1454 C ATOM 115 CG ASN A 15 24.248 -69.962 -41.123 1.00 49.81 C ANISOU 115 CG ASN A 15 7112 3409 8404 -220 -961 1295 C ATOM 116 OD1 ASN A 15 24.754 -69.837 -42.239 1.00 46.03 O ANISOU 116 OD1 ASN A 15 6523 3104 7864 -221 -1105 1210 O ATOM 117 ND2 ASN A 15 24.972 -70.115 -40.016 1.00 47.70 N ANISOU 117 ND2 ASN A 15 7095 3041 7986 -27 -920 1213 N ATOM 118 N LYS A 16 21.083 -72.300 -43.249 1.00 52.26 N ANISOU 118 N LYS A 16 6991 3482 9385 -729 -1213 1176 N ATOM 119 CA LYS A 16 21.064 -73.726 -43.558 1.00 67.54 C ANISOU 119 CA LYS A 16 9017 5246 11399 -798 -1304 1012 C ATOM 120 C LYS A 16 22.131 -74.082 -44.592 1.00 63.84 C ANISOU 120 C LYS A 16 8638 4997 10622 -649 -1621 873 C ATOM 121 O LYS A 16 22.436 -75.251 -44.794 1.00 73.12 O ANISOU 121 O LYS A 16 9944 6050 11787 -656 -1724 726 O ATOM 122 CB LYS A 16 19.683 -74.164 -44.051 1.00 63.85 C ANISOU 122 CB LYS A 16 8203 4655 11403 -983 -1347 840 C ATOM 123 CG LYS A 16 19.203 -73.465 -45.309 1.00 79.69 C ANISOU 123 CG LYS A 16 9883 6956 13441 -881 -1708 709 C ATOM 124 CD LYS A 16 17.802 -73.931 -45.690 1.00 89.48 C ANISOU 124 CD LYS A 16 10713 8054 15233 -1017 -1807 414 C ATOM 125 CE LYS A 16 17.253 -73.138 -46.867 1.00 97.73 C ANISOU 125 CE LYS A 16 11488 9387 16258 -803 -2239 255 C ATOM 126 NZ LYS A 16 18.107 -73.272 -48.082 1.00102.33 N ANISOU 126 NZ LYS A 16 12278 10240 16362 -549 -2613 205 N ATOM 127 N THR A 17 22.702 -73.071 -45.239 1.00 59.16 N ANISOU 127 N THR A 17 8200 3075 11204 359 898 432 N ATOM 128 CA THR A 17 23.785 -73.302 -46.191 1.00 61.84 C ANISOU 128 CA THR A 17 8520 3401 11574 509 880 331 C ATOM 129 C THR A 17 25.145 -72.942 -45.594 1.00 57.49 C ANISOU 129 C THR A 17 7939 2912 10992 664 845 430 C ATOM 130 O THR A 17 26.183 -73.120 -46.233 1.00 69.61 O ANISOU 130 O THR A 17 9446 4446 12557 804 837 370 O ATOM 131 CB THR A 17 23.572 -72.512 -47.494 1.00 65.47 C ANISOU 131 CB THR A 17 8882 3962 12032 505 906 178 C ATOM 132 OG1 THR A 17 23.312 -71.132 -47.189 1.00 69.19 O ANISOU 132 OG1 THR A 17 9252 4598 12440 458 921 233 O ATOM 133 CG2 THR A 17 22.398 -73.090 -48.272 1.00 59.19 C ANISOU 133 CG2 THR A 17 8125 3079 11287 384 913 42 C ATOM 134 N GLY A 18 25.131 -72.443 -44.364 1.00 56.93 N ANISOU 134 N GLY A 18 7874 2894 10863 643 823 580 N ATOM 135 CA GLY A 18 26.354 -72.103 -43.660 1.00 60.21 C ANISOU 135 CA GLY A 18 8264 3361 11253 783 767 676 C ATOM 136 C GLY A 18 27.068 -70.848 -44.138 1.00 55.31 C ANISOU 136 C GLY A 18 7488 2905 10623 850 763 642 C ATOM 137 O GLY A 18 28.222 -70.631 -43.781 1.00 61.73 O ANISOU 137 O GLY A 18 8253 3757 11446 979 710 692 O ATOM 138 N VAL A 19 26.395 -70.016 -44.930 1.00 53.94 N ANISOU 138 N VAL A 19 7233 2827 10435 767 815 558 N ATOM 139 CA VAL A 19 27.041 -68.827 -45.506 1.00 62.19 C ANISOU 139 CA VAL A 19 8134 4020 11476 828 827 521 C ATOM 140 C VAL A 19 26.837 -67.544 -44.700 1.00 57.55 C ANISOU 140 C VAL A 19 7481 3560 10826 775 804 614 C ATOM 141 O VAL A 19 27.495 -66.538 -44.957 1.00 62.62 O ANISOU 141 O VAL A 19 8004 4317 11472 830 801 609 O ATOM 142 CB VAL A 19 26.550 -68.552 -46.948 1.00 53.05 C ANISOU 142 CB VAL A 19 6930 2896 10330 796 898 369 C ATOM 143 CG1 VAL A 19 26.706 -69.801 -47.813 1.00 53.69 C ANISOU 143 CG1 VAL A 19 7088 2847 10464 852 917 257 C ATOM 144 CG2 VAL A 19 25.112 -68.055 -46.944 1.00 51.09 C ANISOU 144 CG2 VAL A 19 6692 2681 10040 632 923 351 C ATOM 145 N VAL A 20 25.927 -67.570 -43.734 1.00 57.63 N ANISOU 145 N VAL A 20 7569 3548 10779 671 793 700 N ATOM 146 CA VAL A 20 25.622 -66.373 -42.961 1.00 60.07 C ANISOU 146 CA VAL A 20 7835 3971 11017 620 774 782 C ATOM 147 C VAL A 20 26.788 -65.992 -42.047 1.00 58.10 C ANISOU 147 C VAL A 20 7560 3758 10758 738 685 879 C ATOM 148 O VAL A 20 27.398 -66.847 -41.409 1.00 58.03 O ANISOU 148 O VAL A 20 7630 3657 10761 820 630 939 O ATOM 149 CB VAL A 20 24.335 -66.562 -42.130 1.00 58.89 C ANISOU 149 CB VAL A 20 7784 3787 10805 487 801 852 C ATOM 150 CG1 VAL A 20 24.083 -65.352 -41.239 1.00 49.19 C ANISOU 150 CG1 VAL A 20 6528 2671 9491 454 781 942 C ATOM 151 CG2 VAL A 20 23.152 -66.798 -43.054 1.00 49.62 C ANISOU 151 CG2 VAL A 20 6602 2591 9659 362 874 745 C ATOM 152 N ARG A 21 27.103 -64.701 -42.008 1.00 59.20 N ANISOU 152 N ARG A 21 7588 4025 10881 749 662 888 N ATOM 153 CA ARG A 21 28.164 -64.188 -41.148 1.00 52.10 C ANISOU 153 CA ARG A 21 6645 3167 9984 850 559 966 C ATOM 154 C ARG A 21 27.632 -63.104 -40.218 1.00 56.07 C ANISOU 154 C ARG A 21 7157 3749 10399 789 522 1043 C ATOM 155 O ARG A 21 26.626 -62.460 -40.520 1.00 52.64 O ANISOU 155 O ARG A 21 6708 3373 9919 678 590 1017 O ATOM 156 CB ARG A 21 29.317 -63.633 -41.989 1.00 48.58 C ANISOU 156 CB ARG A 21 6034 2796 9630 942 553 899 C ATOM 157 CG ARG A 21 29.928 -64.632 -42.964 1.00 49.67 C ANISOU 157 CG ARG A 21 6157 2865 9850 1021 599 818 C ATOM 158 CD ARG A 21 30.626 -65.780 -42.248 1.00 51.41 C ANISOU 158 CD ARG A 21 6464 2974 10096 1123 523 873 C ATOM 159 NE ARG A 21 31.219 -66.715 -43.199 1.00 62.00 N ANISOU 159 NE ARG A 21 7794 4250 11515 1206 570 790 N ATOM 160 CZ ARG A 21 30.678 -67.877 -43.558 1.00 61.56 C ANISOU 160 CZ ARG A 21 7860 4073 11456 1184 615 750 C ATOM 161 NH1 ARG A 21 29.521 -68.274 -43.037 1.00 54.23 N ANISOU 161 NH1 ARG A 21 7065 3077 10463 1071 626 789 N ATOM 162 NH2 ARG A 21 31.300 -68.645 -44.439 1.00 64.70 N ANISOU 162 NH2 ARG A 21 8246 4416 11922 1274 653 668 N ATOM 163 N SER A 22 28.300 -62.906 -39.085 1.00 48.39 N ANISOU 163 N SER A 22 6212 2775 9400 870 409 1134 N ATOM 164 CA SER A 22 27.996 -61.782 -38.208 1.00 61.18 C ANISOU 164 CA SER A 22 7835 4470 10939 840 355 1199 C ATOM 165 C SER A 22 28.076 -60.458 -38.971 1.00 47.38 C ANISOU 165 C SER A 22 5926 2864 9211 796 376 1122 C ATOM 166 O SER A 22 29.048 -60.213 -39.677 1.00 48.65 O ANISOU 166 O SER A 22 5951 3058 9477 861 362 1065 O ATOM 167 CB SER A 22 28.958 -61.755 -37.022 1.00 48.70 C ANISOU 167 CB SER A 22 6292 2867 9344 965 200 1283 C ATOM 168 OG SER A 22 28.835 -60.534 -36.314 1.00 52.00 O ANISOU 168 OG SER A 22 6692 3384 9681 946 129 1314 O ATOM 169 N PRO A 23 27.047 -59.602 -38.840 1.00 57.41 N ANISOU 169 N PRO A 23 7213 4234 10368 686 419 1118 N ATOM 170 CA PRO A 23 27.034 -58.307 -39.533 1.00 50.51 C ANISOU 170 CA PRO A 23 6203 3507 9480 638 440 1047 C ATOM 171 C PRO A 23 28.082 -57.325 -39.009 1.00 51.08 C ANISOU 171 C PRO A 23 6183 3652 9575 706 318 1062 C ATOM 172 O PRO A 23 28.233 -56.239 -39.571 1.00 52.95 O ANISOU 172 O PRO A 23 6300 3994 9823 675 333 1010 O ATOM 173 CB PRO A 23 25.620 -57.779 -39.260 1.00 52.09 C ANISOU 173 CB PRO A 23 6471 3773 9548 517 500 1057 C ATOM 174 CG PRO A 23 25.235 -58.409 -37.980 1.00 44.77 C ANISOU 174 CG PRO A 23 5700 2762 8549 527 468 1162 C ATOM 175 CD PRO A 23 25.824 -59.801 -38.042 1.00 44.94 C ANISOU 175 CD PRO A 23 5776 2629 8670 603 461 1186 C ATOM 176 N PHE A 24 28.780 -57.700 -37.941 1.00 56.25 N ANISOU 176 N PHE A 24 6894 4242 10238 800 192 1133 N ATOM 177 CA PHE A 24 29.863 -56.888 -37.402 1.00 57.14 C ANISOU 177 CA PHE A 24 6911 4405 10396 874 47 1137 C ATOM 178 C PHE A 24 31.225 -57.369 -37.897 1.00 56.72 C ANISOU 178 C PHE A 24 6728 4300 10524 983 4 1110 C ATOM 179 O PHE A 24 32.247 -56.774 -37.568 1.00 64.49 O ANISOU 179 O PHE A 24 7597 5315 11591 1048 -118 1104 O ATOM 180 CB PHE A 24 29.852 -56.906 -35.870 1.00 49.07 C ANISOU 180 CB PHE A 24 6029 3355 9261 927 -92 1222 C ATOM 181 CG PHE A 24 28.558 -56.457 -35.263 1.00 55.66 C ANISOU 181 CG PHE A 24 6997 4237 9914 837 -42 1259 C ATOM 182 CD1 PHE A 24 28.116 -55.154 -35.427 1.00 55.25 C ANISOU 182 CD1 PHE A 24 6881 4307 9804 758 -25 1212 C ATOM 183 CD2 PHE A 24 27.786 -57.335 -34.515 1.00 61.83 C ANISOU 183 CD2 PHE A 24 7968 4936 10589 834 -2 1344 C ATOM 184 CE1 PHE A 24 26.920 -54.732 -34.864 1.00 47.37 C ANISOU 184 CE1 PHE A 24 6000 3356 8644 685 27 1243 C ATOM 185 CE2 PHE A 24 26.590 -56.921 -33.951 1.00 64.78 C ANISOU 185 CE2 PHE A 24 8453 5356 10805 755 63 1382 C ATOM 186 CZ PHE A 24 26.158 -55.617 -34.127 1.00 54.23 C ANISOU 186 CZ PHE A 24 7045 4150 9411 684 75 1327 C ATOM 187 N GLU A 25 31.245 -58.440 -38.686 1.00 52.53 N ANISOU 187 N GLU A 25 6207 3685 10065 1007 102 1089 N ATOM 188 CA GLU A 25 32.515 -59.076 -39.034 1.00 55.69 C ANISOU 188 CA GLU A 25 6507 4021 10633 1132 65 1072 C ATOM 189 C GLU A 25 32.768 -59.258 -40.533 1.00 52.37 C ANISOU 189 C GLU A 25 5972 3623 10304 1126 210 984 C ATOM 190 O GLU A 25 33.916 -59.262 -40.971 1.00 58.25 O ANISOU 190 O GLU A 25 6572 4387 11173 1206 197 950 O ATOM 191 CB GLU A 25 32.615 -60.439 -38.342 1.00 51.26 C ANISOU 191 CB GLU A 25 6098 3348 10030 1206 11 1127 C ATOM 192 CG GLU A 25 32.706 -60.358 -36.822 1.00 65.08 C ANISOU 192 CG GLU A 25 7962 5069 11695 1262 -152 1220 C ATOM 193 CD GLU A 25 33.975 -59.674 -36.348 1.00 88.46 C ANISOU 193 CD GLU A 25 10780 8080 14749 1358 -324 1211 C ATOM 194 OE1 GLU A 25 33.891 -58.524 -35.867 1.00 90.16 O ANISOU 194 OE1 GLU A 25 10955 8365 14937 1324 -403 1215 O ATOM 195 OE2 GLU A 25 35.059 -60.286 -36.457 1.00108.69 O ANISOU 195 OE2 GLU A 25 13268 10616 17413 1465 -383 1192 O ATOM 196 N ALA A 26 31.710 -59.407 -41.322 1.00 47.43 N ANISOU 196 N ALA A 26 5409 2994 9616 1037 348 945 N ATOM 197 CA ALA A 26 31.890 -59.787 -42.720 1.00 50.72 C ANISOU 197 CA ALA A 26 5764 3414 10095 1053 480 859 C ATOM 198 C ALA A 26 30.739 -59.290 -43.588 1.00 53.13 C ANISOU 198 C ALA A 26 6095 3784 10306 938 602 801 C ATOM 199 O ALA A 26 29.623 -59.125 -43.100 1.00 49.34 O ANISOU 199 O ALA A 26 5718 3322 9706 840 595 825 O ATOM 200 CB ALA A 26 32.033 -61.306 -42.831 1.00 48.00 C ANISOU 200 CB ALA A 26 5519 2959 9761 1113 492 846 C ATOM 201 N PRO A 27 31.014 -59.038 -44.880 1.00 55.75 N ANISOU 201 N PRO A 27 6337 4167 10680 957 713 724 N ATOM 202 CA PRO A 27 30.000 -58.503 -45.798 1.00 48.29 C ANISOU 202 CA PRO A 27 5414 3304 9629 864 815 660 C ATOM 203 C PRO A 27 28.757 -59.384 -45.886 1.00 52.93 C ANISOU 203 C PRO A 27 6153 3823 10136 793 843 629 C ATOM 204 O PRO A 27 28.847 -60.603 -45.782 1.00 50.82 O ANISOU 204 O PRO A 27 5963 3425 9921 837 836 626 O ATOM 205 CB PRO A 27 30.737 -58.449 -47.141 1.00 51.28 C ANISOU 205 CB PRO A 27 5696 3710 10077 942 930 591 C ATOM 206 CG PRO A 27 32.180 -58.320 -46.765 1.00 50.77 C ANISOU 206 CG PRO A 27 5495 3631 10163 1043 882 636 C ATOM 207 CD PRO A 27 32.339 -59.137 -45.520 1.00 52.15 C ANISOU 207 CD PRO A 27 5742 3701 10370 1075 749 700 C ATOM 208 N GLN A 28 27.601 -58.756 -46.065 1.00 48.93 N ANISOU 208 N GLN A 28 5680 3395 9515 683 873 605 N ATOM 209 CA GLN A 28 26.337 -59.476 -46.081 1.00 44.69 C ANISOU 209 CA GLN A 28 5262 2799 8919 597 893 575 C ATOM 210 C GLN A 28 25.835 -59.654 -47.507 1.00 49.62 C ANISOU 210 C GLN A 28 5894 3445 9516 586 979 454 C ATOM 211 O GLN A 28 24.648 -59.489 -47.784 1.00 45.56 O ANISOU 211 O GLN A 28 5420 2968 8924 492 997 409 O ATOM 212 CB GLN A 28 25.302 -58.736 -45.234 1.00 50.00 C ANISOU 212 CB GLN A 28 5968 3541 9489 486 860 627 C ATOM 213 CG GLN A 28 25.747 -58.501 -43.797 1.00 52.51 C ANISOU 213 CG GLN A 28 6302 3845 9804 506 768 740 C ATOM 214 CD GLN A 28 25.788 -59.782 -42.990 1.00 57.83 C ANISOU 214 CD GLN A 28 7088 4367 10520 533 733 802 C ATOM 215 OE1 GLN A 28 24.774 -60.468 -42.844 1.00 51.15 O ANISOU 215 OE1 GLN A 28 6337 3449 9647 458 771 805 O ATOM 216 NE2 GLN A 28 26.967 -60.120 -42.471 1.00 51.24 N ANISOU 216 NE2 GLN A 28 6237 3471 9759 644 660 853 N ATOM 217 N TYR A 29 26.744 -60.007 -48.410 1.00 55.72 N ANISOU 217 N TYR A 29 6628 4192 10352 693 1030 399 N ATOM 218 CA TYR A 29 26.421 -60.088 -49.830 1.00 58.17 C ANISOU 218 CA TYR A 29 6952 4532 10616 712 1111 281 C ATOM 219 C TYR A 29 25.588 -61.319 -50.200 1.00 63.91 C ANISOU 219 C TYR A 29 7796 5140 11346 678 1110 195 C ATOM 220 O TYR A 29 25.365 -61.585 -51.381 1.00 66.87 O ANISOU 220 O TYR A 29 8204 5518 11687 711 1160 80 O ATOM 221 CB TYR A 29 27.712 -60.064 -50.657 1.00 50.85 C ANISOU 221 CB TYR A 29 5952 3617 9752 850 1184 255 C ATOM 222 CG TYR A 29 28.466 -58.750 -50.567 1.00 55.95 C ANISOU 222 CG TYR A 29 6466 4384 10408 871 1206 320 C ATOM 223 CD1 TYR A 29 27.790 -57.549 -50.383 1.00 52.32 C ANISOU 223 CD1 TYR A 29 5982 4043 9856 779 1192 347 C ATOM 224 CD2 TYR A 29 29.853 -58.713 -50.655 1.00 50.78 C ANISOU 224 CD2 TYR A 29 5704 3718 9870 982 1239 352 C ATOM 225 CE1 TYR A 29 28.472 -56.347 -50.299 1.00 46.76 C ANISOU 225 CE1 TYR A 29 5162 3431 9174 791 1210 403 C ATOM 226 CE2 TYR A 29 30.542 -57.520 -50.571 1.00 57.14 C ANISOU 226 CE2 TYR A 29 6377 4620 10712 989 1259 409 C ATOM 227 CZ TYR A 29 29.848 -56.339 -50.394 1.00 55.74 C ANISOU 227 CZ TYR A 29 6189 4549 10440 890 1243 434 C ATOM 228 OH TYR A 29 30.539 -55.151 -50.310 1.00 57.04 O ANISOU 228 OH TYR A 29 6224 4793 10655 891 1261 488 O ATOM 229 N TYR A 30 25.125 -62.062 -49.197 1.00 63.82 N ANISOU 229 N TYR A 30 7853 5019 11378 615 1053 250 N ATOM 230 CA TYR A 30 24.262 -63.221 -49.436 1.00 67.69 C ANISOU 230 CA TYR A 30 8447 5377 11896 560 1049 177 C ATOM 231 C TYR A 30 22.788 -62.858 -49.232 1.00 60.23 C ANISOU 231 C TYR A 30 7520 4480 10884 409 1034 163 C ATOM 232 O TYR A 30 21.899 -63.563 -49.707 1.00 68.69 O ANISOU 232 O TYR A 30 8648 5476 11973 345 1033 72 O ATOM 233 CB TYR A 30 24.653 -64.395 -48.525 1.00 62.34 C ANISOU 233 CB TYR A 30 7841 4520 11324 587 1015 250 C ATOM 234 CG TYR A 30 24.861 -63.991 -47.088 1.00 57.96 C ANISOU 234 CG TYR A 30 7276 3980 10764 566 964 403 C ATOM 235 CD1 TYR A 30 23.779 -63.795 -46.239 1.00 46.02 C ANISOU 235 CD1 TYR A 30 5806 2476 9202 439 948 466 C ATOM 236 CD2 TYR A 30 26.138 -63.785 -46.583 1.00 49.14 C ANISOU 236 CD2 TYR A 30 6106 2876 9690 678 928 479 C ATOM 237 CE1 TYR A 30 23.962 -63.407 -44.929 1.00 56.91 C ANISOU 237 CE1 TYR A 30 7196 3874 10553 434 902 601 C ATOM 238 CE2 TYR A 30 26.332 -63.397 -45.270 1.00 51.98 C ANISOU 238 CE2 TYR A 30 6467 3263 10019 668 859 605 C ATOM 239 CZ TYR A 30 25.240 -63.208 -44.450 1.00 52.64 C ANISOU 239 CZ TYR A 30 6616 3349 10037 551 849 666 C ATOM 240 OH TYR A 30 25.425 -62.824 -43.142 1.00 60.03 O ANISOU 240 OH TYR A 30 7575 4309 10925 556 782 787 O ATOM 241 N LEU A 31 22.525 -61.760 -48.529 1.00 56.68 N ANISOU 241 N LEU A 31 7017 4152 10367 354 1019 247 N ATOM 242 CA LEU A 31 21.147 -61.315 -48.354 1.00 60.88 C ANISOU 242 CA LEU A 31 7550 4745 10837 223 1013 235 C ATOM 243 C LEU A 31 20.800 -60.196 -49.324 1.00 50.22 C ANISOU 243 C LEU A 31 6137 3559 9386 222 1031 158 C ATOM 244 O LEU A 31 19.638 -59.816 -49.450 1.00 59.11 O ANISOU 244 O LEU A 31 7253 4746 10462 130 1023 119 O ATOM 245 CB LEU A 31 20.882 -60.871 -46.910 1.00 63.25 C ANISOU 245 CB LEU A 31 7852 5066 11114 161 990 373 C ATOM 246 CG LEU A 31 21.803 -59.900 -46.173 1.00 64.17 C ANISOU 246 CG LEU A 31 7919 5270 11193 223 961 474 C ATOM 247 CD1 LEU A 31 21.674 -58.490 -46.694 1.00 68.23 C ANISOU 247 CD1 LEU A 31 8350 5956 11619 216 973 444 C ATOM 248 CD2 LEU A 31 21.480 -59.938 -44.695 1.00 71.90 C ANISOU 248 CD2 LEU A 31 8952 6213 12153 175 932 599 C ATOM 249 N ALA A 32 21.813 -59.667 -50.003 1.00 53.59 N ANISOU 249 N ALA A 32 6519 4052 9790 330 1060 142 N ATOM 250 CA ALA A 32 21.596 -58.672 -51.050 1.00 49.78 C ANISOU 250 CA ALA A 32 5997 3711 9207 352 1092 74 C ATOM 251 C ALA A 32 22.811 -58.588 -51.966 1.00 49.76 C ANISOU 251 C ALA A 32 5971 3725 9211 487 1152 44 C ATOM 252 O ALA A 32 23.948 -58.707 -51.507 1.00 52.47 O ANISOU 252 O ALA A 32 6276 4029 9632 556 1163 116 O ATOM 253 CB ALA A 32 21.283 -57.303 -50.442 1.00 53.14 C ANISOU 253 CB ALA A 32 6361 4268 9562 298 1080 154 C ATOM 254 N GLU A 33 22.566 -58.400 -53.260 1.00 42.37 N ANISOU 254 N GLU A 33 5058 2847 8192 534 1193 -62 N ATOM 255 CA GLU A 33 23.648 -58.237 -54.231 1.00 48.78 C ANISOU 255 CA GLU A 33 5855 3687 8991 669 1278 -89 C ATOM 256 C GLU A 33 24.494 -56.994 -53.928 1.00 55.98 C ANISOU 256 C GLU A 33 6664 4699 9907 697 1324 21 C ATOM 257 O GLU A 33 23.988 -56.017 -53.376 1.00 50.25 O ANISOU 257 O GLU A 33 5899 4057 9137 619 1292 79 O ATOM 258 CB GLU A 33 23.077 -58.147 -55.647 1.00 48.43 C ANISOU 258 CB GLU A 33 5878 3701 8824 715 1310 -219 C ATOM 259 CG GLU A 33 22.461 -59.439 -56.146 1.00 62.16 C ANISOU 259 CG GLU A 33 7716 5325 10575 712 1263 -353 C ATOM 260 CD GLU A 33 23.500 -60.518 -56.363 1.00 84.13 C ANISOU 260 CD GLU A 33 10534 7984 13448 820 1307 -378 C ATOM 261 OE1 GLU A 33 23.401 -61.581 -55.716 1.00 97.19 O ANISOU 261 OE1 GLU A 33 12222 9497 15211 778 1255 -379 O ATOM 262 OE2 GLU A 33 24.420 -60.300 -57.181 1.00 98.58 O ANISOU 262 OE2 GLU A 33 12360 9852 15243 952 1403 -392 O ATOM 263 N PRO A 34 25.793 -57.041 -54.271 1.00 50.87 N ANISOU 263 N PRO A 34 5965 4036 9325 810 1401 46 N ATOM 264 CA PRO A 34 26.685 -55.894 -54.062 1.00 42.04 C ANISOU 264 CA PRO A 34 4732 2998 8243 835 1451 143 C ATOM 265 C PRO A 34 26.130 -54.581 -54.621 1.00 52.30 C ANISOU 265 C PRO A 34 6023 4429 9418 805 1491 147 C ATOM 266 O PRO A 34 26.204 -53.559 -53.936 1.00 42.40 O ANISOU 266 O PRO A 34 4697 3233 8180 748 1465 231 O ATOM 267 CB PRO A 34 27.957 -56.313 -54.797 1.00 43.34 C ANISOU 267 CB PRO A 34 4859 3126 8484 974 1558 130 C ATOM 268 CG PRO A 34 27.984 -57.812 -54.613 1.00 44.30 C ANISOU 268 CG PRO A 34 5052 3111 8670 1005 1512 75 C ATOM 269 CD PRO A 34 26.536 -58.254 -54.668 1.00 43.94 C ANISOU 269 CD PRO A 34 5123 3045 8527 912 1437 -5 C ATOM 270 N TRP A 35 25.559 -54.613 -55.823 1.00 43.56 N ANISOU 270 N TRP A 35 4999 3363 8186 847 1541 54 N ATOM 271 CA TRP A 35 25.026 -53.408 -56.449 1.00 50.84 C ANISOU 271 CA TRP A 35 5932 4407 8979 839 1580 57 C ATOM 272 C TRP A 35 23.882 -52.813 -55.635 1.00 50.67 C ANISOU 272 C TRP A 35 5908 4433 8912 711 1474 80 C ATOM 273 O TRP A 35 23.635 -51.608 -55.698 1.00 49.66 O ANISOU 273 O TRP A 35 5753 4396 8719 689 1492 125 O ATOM 274 CB TRP A 35 24.564 -53.690 -57.888 1.00 51.03 C ANISOU 274 CB TRP A 35 6070 4460 8860 924 1632 -60 C ATOM 275 CG TRP A 35 23.295 -54.487 -58.019 1.00 44.95 C ANISOU 275 CG TRP A 35 5394 3658 8025 870 1523 -178 C ATOM 276 CD1 TRP A 35 23.193 -55.835 -58.209 1.00 52.29 C ANISOU 276 CD1 TRP A 35 6393 4482 8995 892 1485 -275 C ATOM 277 CD2 TRP A 35 21.950 -53.984 -57.993 1.00 45.46 C ANISOU 277 CD2 TRP A 35 5488 3792 7993 786 1436 -215 C ATOM 278 NE1 TRP A 35 21.873 -56.205 -58.293 1.00 43.06 N ANISOU 278 NE1 TRP A 35 5284 3305 7771 815 1379 -372 N ATOM 279 CE2 TRP A 35 21.089 -55.090 -58.162 1.00 45.66 C ANISOU 279 CE2 TRP A 35 5584 3747 8018 751 1346 -338 C ATOM 280 CE3 TRP A 35 21.391 -52.710 -57.837 1.00 52.93 C ANISOU 280 CE3 TRP A 35 6400 4846 8864 738 1423 -160 C ATOM 281 CZ2 TRP A 35 19.697 -54.961 -58.180 1.00 49.04 C ANISOU 281 CZ2 TRP A 35 6033 4215 8384 668 1246 -406 C ATOM 282 CZ3 TRP A 35 20.010 -52.583 -57.854 1.00 45.63 C ANISOU 282 CZ3 TRP A 35 5506 3966 7865 667 1325 -226 C ATOM 283 CH2 TRP A 35 19.179 -53.704 -58.024 1.00 44.97 C ANISOU 283 CH2 TRP A 35 5477 3817 7794 631 1238 -348 C ATOM 284 N GLN A 36 23.196 -53.647 -54.858 1.00 44.19 N ANISOU 284 N GLN A 36 5116 3544 8132 631 1376 55 N ATOM 285 CA GLN A 36 22.102 -53.159 -54.023 1.00 55.05 C ANISOU 285 CA GLN A 36 6484 4959 9472 514 1291 81 C ATOM 286 C GLN A 36 22.631 -52.389 -52.817 1.00 45.26 C ANISOU 286 C GLN A 36 5163 3733 8298 471 1268 203 C ATOM 287 O GLN A 36 21.993 -51.445 -52.351 1.00 48.34 O ANISOU 287 O GLN A 36 5535 4195 8635 407 1235 240 O ATOM 288 CB GLN A 36 21.209 -54.314 -53.571 1.00 38.87 C ANISOU 288 CB GLN A 36 4489 2824 7457 440 1214 25 C ATOM 289 CG GLN A 36 20.308 -54.846 -54.662 1.00 50.66 C ANISOU 289 CG GLN A 36 6055 4318 8874 450 1198 -113 C ATOM 290 CD GLN A 36 19.516 -56.064 -54.216 1.00 56.68 C ANISOU 290 CD GLN A 36 6857 4971 9709 368 1127 -169 C ATOM 291 OE1 GLN A 36 20.072 -57.005 -53.659 1.00 52.72 O ANISOU 291 OE1 GLN A 36 6368 4350 9312 370 1126 -140 O ATOM 292 NE2 GLN A 36 18.210 -56.040 -54.448 1.00 54.94 N ANISOU 292 NE2 GLN A 36 6650 4784 9443 295 1070 -245 N ATOM 293 N PHE A 37 23.793 -52.799 -52.316 1.00 48.35 N ANISOU 293 N PHE A 37 5508 4054 8806 513 1276 258 N ATOM 294 CA PHE A 37 24.487 -52.062 -51.259 1.00 50.97 C ANISOU 294 CA PHE A 37 5759 4396 9210 491 1241 362 C ATOM 295 C PHE A 37 25.002 -50.732 -51.789 1.00 51.42 C ANISOU 295 C PHE A 37 5748 4540 9250 521 1310 397 C ATOM 296 O PHE A 37 25.003 -49.719 -51.082 1.00 42.40 O ANISOU 296 O PHE A 37 4558 3439 8112 473 1271 459 O ATOM 297 CB PHE A 37 25.642 -52.890 -50.686 1.00 38.46 C ANISOU 297 CB PHE A 37 4136 2714 7764 544 1221 401 C ATOM 298 CG PHE A 37 25.194 -53.962 -49.734 1.00 45.83 C ANISOU 298 CG PHE A 37 5135 3553 8724 501 1137 409 C ATOM 299 CD1 PHE A 37 24.865 -55.226 -50.196 1.00 50.45 C ANISOU 299 CD1 PHE A 37 5797 4054 9318 518 1150 340 C ATOM 300 CD2 PHE A 37 25.086 -53.698 -48.376 1.00 43.00 C ANISOU 300 CD2 PHE A 37 4774 3185 8378 446 1049 488 C ATOM 301 CE1 PHE A 37 24.442 -56.215 -49.321 1.00 53.81 C ANISOU 301 CE1 PHE A 37 6289 4379 9779 473 1087 359 C ATOM 302 CE2 PHE A 37 24.662 -54.683 -47.495 1.00 47.20 C ANISOU 302 CE2 PHE A 37 5382 3627 8926 413 990 511 C ATOM 303 CZ PHE A 37 24.339 -55.943 -47.970 1.00 51.88 C ANISOU 303 CZ PHE A 37 6044 4128 9541 421 1015 452 C ATOM 304 N SER A 38 25.444 -50.746 -53.042 1.00 39.84 N ANISOU 304 N SER A 38 4283 3090 7762 605 1418 358 N ATOM 305 CA SER A 38 25.861 -49.531 -53.718 1.00 39.61 C ANISOU 305 CA SER A 38 4206 3135 7708 638 1511 396 C ATOM 306 C SER A 38 24.692 -48.544 -53.854 1.00 41.02 C ANISOU 306 C SER A 38 4434 3403 7749 581 1487 388 C ATOM 307 O SER A 38 24.873 -47.338 -53.696 1.00 46.24 O ANISOU 307 O SER A 38 5045 4109 8414 560 1506 450 O ATOM 308 CB SER A 38 26.441 -49.866 -55.088 1.00 39.17 C ANISOU 308 CB SER A 38 4173 3079 7629 752 1647 354 C ATOM 309 OG SER A 38 27.657 -50.576 -54.962 1.00 49.18 O ANISOU 309 OG SER A 38 5370 4273 9043 815 1686 373 O ATOM 310 N MET A 39 23.491 -49.055 -54.119 1.00 42.55 N ANISOU 310 N MET A 39 4718 3613 7836 555 1439 309 N ATOM 311 CA MET A 39 22.312 -48.195 -54.251 1.00 43.38 C ANISOU 311 CA MET A 39 4863 3804 7818 510 1406 293 C ATOM 312 C MET A 39 21.864 -47.682 -52.888 1.00 45.76 C ANISOU 312 C MET A 39 5126 4111 8148 412 1315 350 C ATOM 313 O MET A 39 21.333 -46.581 -52.775 1.00 41.79 O ANISOU 313 O MET A 39 4619 3676 7582 384 1304 376 O ATOM 314 CB MET A 39 21.169 -48.933 -54.953 1.00 40.48 C ANISOU 314 CB MET A 39 4584 3449 7347 512 1370 180 C ATOM 315 CG MET A 39 21.412 -49.156 -56.445 1.00 45.48 C ANISOU 315 CG MET A 39 5284 4101 7895 625 1454 112 C ATOM 316 SD MET A 39 21.929 -47.640 -57.295 1.00 52.70 S ANISOU 316 SD MET A 39 6193 5102 8728 702 1575 183 S ATOM 317 CE MET A 39 20.499 -46.583 -56.977 1.00 43.01 C ANISOU 317 CE MET A 39 4982 3965 7393 630 1484 183 C ATOM 318 N LEU A 40 22.097 -48.473 -51.848 1.00 43.86 N ANISOU 318 N LEU A 40 4869 3797 7998 372 1252 372 N ATOM 319 CA LEU A 40 21.907 -47.986 -50.486 1.00 43.11 C ANISOU 319 CA LEU A 40 4749 3702 7929 301 1174 437 C ATOM 320 C LEU A 40 22.846 -46.807 -50.217 1.00 49.58 C ANISOU 320 C LEU A 40 5494 4543 8802 316 1189 509 C ATOM 321 O LEU A 40 22.435 -45.788 -49.663 1.00 46.98 O ANISOU 321 O LEU A 40 5158 4259 8434 274 1153 541 O ATOM 322 CB LEU A 40 22.148 -49.111 -49.479 1.00 44.63 C ANISOU 322 CB LEU A 40 4954 3802 8201 278 1113 457 C ATOM 323 CG LEU A 40 22.217 -48.749 -47.996 1.00 46.98 C ANISOU 323 CG LEU A 40 5240 4085 8524 231 1031 530 C ATOM 324 CD1 LEU A 40 21.000 -47.954 -47.581 1.00 39.44 C ANISOU 324 CD1 LEU A 40 4315 3204 7467 167 1006 531 C ATOM 325 CD2 LEU A 40 22.333 -50.019 -47.164 1.00 50.56 C ANISOU 325 CD2 LEU A 40 5735 4441 9033 223 982 549 C ATOM 326 N ALA A 41 24.104 -46.944 -50.625 1.00 39.35 N ANISOU 326 N ALA A 41 4138 3208 7606 377 1245 530 N ATOM 327 CA ALA A 41 25.083 -45.880 -50.456 1.00 38.29 C ANISOU 327 CA ALA A 41 3912 3078 7558 387 1266 594 C ATOM 328 C ALA A 41 24.682 -44.645 -51.266 1.00 39.08 C ANISOU 328 C ALA A 41 4023 3252 7574 390 1340 601 C ATOM 329 O ALA A 41 24.811 -43.513 -50.799 1.00 48.28 O ANISOU 329 O ALA A 41 5149 4433 8764 356 1317 648 O ATOM 330 CB ALA A 41 26.468 -46.362 -50.868 1.00 37.88 C ANISOU 330 CB ALA A 41 3777 2970 7644 456 1332 611 C ATOM 331 N ALA A 42 24.198 -44.881 -52.483 1.00 37.10 N ANISOU 331 N ALA A 42 3837 3039 7221 439 1422 552 N ATOM 332 CA ALA A 42 23.772 -43.810 -53.372 1.00 36.18 C ANISOU 332 CA ALA A 42 3754 2991 7002 463 1496 560 C ATOM 333 C ALA A 42 22.639 -43.008 -52.747 1.00 53.94 C ANISOU 333 C ALA A 42 6038 5292 9166 398 1411 560 C ATOM 334 O ALA A 42 22.631 -41.775 -52.808 1.00 39.50 O ANISOU 334 O ALA A 42 4198 3491 7320 392 1436 606 O ATOM 335 CB ALA A 42 23.343 -44.378 -54.724 1.00 37.70 C ANISOU 335 CB ALA A 42 4034 3216 7076 540 1570 491 C ATOM 336 N TYR A 43 21.685 -43.706 -52.135 1.00 43.24 N ANISOU 336 N TYR A 43 4724 3941 7763 351 1320 513 N ATOM 337 CA TYR A 43 20.556 -43.021 -51.529 1.00 43.89 C ANISOU 337 CA TYR A 43 4834 4076 7767 297 1252 510 C ATOM 338 C TYR A 43 20.983 -42.233 -50.292 1.00 49.25 C ANISOU 338 C TYR A 43 5465 4731 8517 249 1195 575 C ATOM 339 O TYR A 43 20.520 -41.108 -50.081 1.00 48.42 O ANISOU 339 O TYR A 43 5368 4665 8363 233 1180 595 O ATOM 340 CB TYR A 43 19.433 -43.996 -51.170 1.00 38.32 C ANISOU 340 CB TYR A 43 4170 3375 7014 254 1186 449 C ATOM 341 CG TYR A 43 18.141 -43.254 -50.892 1.00 42.86 C ANISOU 341 CG TYR A 43 4768 4022 7495 218 1144 434 C ATOM 342 CD1 TYR A 43 17.482 -42.577 -51.912 1.00 55.29 C ANISOU 342 CD1 TYR A 43 6373 5669 8967 261 1172 400 C ATOM 343 CD2 TYR A 43 17.608 -43.190 -49.611 1.00 43.32 C ANISOU 343 CD2 TYR A 43 4821 4076 7563 153 1081 458 C ATOM 344 CE1 TYR A 43 16.315 -41.871 -51.669 1.00 56.84 C ANISOU 344 CE1 TYR A 43 6580 5931 9087 240 1131 386 C ATOM 345 CE2 TYR A 43 16.435 -42.489 -49.357 1.00 51.10 C ANISOU 345 CE2 TYR A 43 5818 5128 8469 130 1055 445 C ATOM 346 CZ TYR A 43 15.796 -41.829 -50.392 1.00 56.63 C ANISOU 346 CZ TYR A 43 6535 5900 9084 172 1077 407 C ATOM 347 OH TYR A 43 14.633 -41.131 -50.153 1.00 62.48 O ANISOU 347 OH TYR A 43 7277 6708 9754 159 1048 391 O ATOM 348 N MET A 44 21.855 -42.821 -49.478 1.00 42.70 N ANISOU 348 N MET A 44 4592 3833 7798 236 1152 602 N ATOM 349 CA MET A 44 22.427 -42.112 -48.334 1.00 54.05 C ANISOU 349 CA MET A 44 5987 5240 9309 204 1081 653 C ATOM 350 C MET A 44 23.169 -40.861 -48.793 1.00 56.52 C ANISOU 350 C MET A 44 6241 5553 9680 219 1133 693 C ATOM 351 O MET A 44 23.097 -39.813 -48.149 1.00 44.50 O ANISOU 351 O MET A 44 4712 4034 8163 189 1083 716 O ATOM 352 CB MET A 44 23.372 -43.017 -47.538 1.00 52.36 C ANISOU 352 CB MET A 44 5735 4951 9209 208 1021 672 C ATOM 353 CG MET A 44 22.686 -44.178 -46.834 1.00 53.26 C ANISOU 353 CG MET A 44 5916 5045 9277 186 964 653 C ATOM 354 SD MET A 44 21.455 -43.619 -45.638 1.00 47.33 S ANISOU 354 SD MET A 44 5235 4335 8413 128 889 662 S ATOM 355 CE MET A 44 19.943 -44.147 -46.434 1.00 36.49 C ANISOU 355 CE MET A 44 3917 3018 6929 106 949 603 C ATOM 356 N PHE A 45 23.878 -40.979 -49.912 1.00 49.28 N ANISOU 356 N PHE A 45 5287 4626 8810 269 1242 701 N ATOM 357 CA PHE A 45 24.582 -39.850 -50.502 1.00 47.09 C ANISOU 357 CA PHE A 45 4956 4341 8597 284 1327 750 C ATOM 358 C PHE A 45 23.595 -38.755 -50.917 1.00 54.27 C ANISOU 358 C PHE A 45 5934 5308 9378 282 1352 752 C ATOM 359 O PHE A 45 23.827 -37.562 -50.678 1.00 46.16 O ANISOU 359 O PHE A 45 4879 4262 8395 258 1351 794 O ATOM 360 CB PHE A 45 25.411 -40.313 -51.701 1.00 34.80 C ANISOU 360 CB PHE A 45 3364 2768 7090 351 1466 760 C ATOM 361 CG PHE A 45 26.228 -39.225 -52.337 1.00 45.82 C ANISOU 361 CG PHE A 45 4695 4144 8572 367 1582 826 C ATOM 362 CD1 PHE A 45 27.244 -38.598 -51.632 1.00 38.84 C ANISOU 362 CD1 PHE A 45 3691 3195 7872 323 1549 872 C ATOM 363 CD2 PHE A 45 25.991 -38.840 -53.648 1.00 36.89 C ANISOU 363 CD2 PHE A 45 3625 3050 7340 428 1725 841 C ATOM 364 CE1 PHE A 45 28.005 -37.607 -52.222 1.00 44.28 C ANISOU 364 CE1 PHE A 45 4309 3850 8666 326 1668 937 C ATOM 365 CE2 PHE A 45 26.750 -37.845 -54.245 1.00 48.68 C ANISOU 365 CE2 PHE A 45 5067 4514 8916 442 1854 917 C ATOM 366 CZ PHE A 45 27.756 -37.228 -53.530 1.00 46.98 C ANISOU 366 CZ PHE A 45 4718 4226 8906 384 1832 967 C ATOM 367 N LEU A 46 22.489 -39.164 -51.532 1.00 45.69 N ANISOU 367 N LEU A 46 4935 4285 8140 308 1366 703 N ATOM 368 CA LEU A 46 21.440 -38.229 -51.922 1.00 44.35 C ANISOU 368 CA LEU A 46 4833 4177 7839 319 1374 697 C ATOM 369 C LEU A 46 20.886 -37.492 -50.699 1.00 46.83 C ANISOU 369 C LEU A 46 5149 4494 8148 260 1269 704 C ATOM 370 O LEU A 46 20.740 -36.270 -50.710 1.00 42.26 O ANISOU 370 O LEU A 46 4583 3920 7554 260 1279 735 O ATOM 371 CB LEU A 46 20.316 -38.958 -52.656 1.00 48.79 C ANISOU 371 CB LEU A 46 5473 4806 8258 355 1373 626 C ATOM 372 CG LEU A 46 19.113 -38.135 -53.122 1.00 46.47 C ANISOU 372 CG LEU A 46 5247 4586 7822 381 1364 607 C ATOM 373 CD1 LEU A 46 19.520 -37.154 -54.205 1.00 53.58 C ANISOU 373 CD1 LEU A 46 6179 5493 8686 450 1473 659 C ATOM 374 CD2 LEU A 46 18.006 -39.038 -53.617 1.00 43.97 C ANISOU 374 CD2 LEU A 46 4982 4328 7399 400 1324 518 C ATOM 375 N LEU A 47 20.603 -38.240 -49.638 1.00 44.32 N ANISOU 375 N LEU A 47 4831 4168 7842 217 1175 677 N ATOM 376 CA LEU A 47 20.066 -37.658 -48.410 1.00 46.23 C ANISOU 376 CA LEU A 47 5090 4415 8062 174 1082 680 C ATOM 377 C LEU A 47 21.054 -36.704 -47.741 1.00 42.47 C ANISOU 377 C LEU A 47 4565 3876 7697 153 1045 724 C ATOM 378 O LEU A 47 20.646 -35.728 -47.131 1.00 44.25 O ANISOU 378 O LEU A 47 4816 4106 7890 137 996 727 O ATOM 379 CB LEU A 47 19.658 -38.757 -47.425 1.00 46.28 C ANISOU 379 CB LEU A 47 5115 4415 8054 140 1008 655 C ATOM 380 CG LEU A 47 18.465 -39.625 -47.833 1.00 50.00 C ANISOU 380 CG LEU A 47 5629 4940 8430 139 1024 604 C ATOM 381 CD1 LEU A 47 18.099 -40.585 -46.713 1.00 40.27 C ANISOU 381 CD1 LEU A 47 4416 3684 7201 97 964 599 C ATOM 382 CD2 LEU A 47 17.278 -38.750 -48.204 1.00 45.06 C ANISOU 382 CD2 LEU A 47 5036 4390 7695 151 1035 581 C ATOM 383 N ILE A 48 22.347 -36.994 -47.847 1.00 42.31 N ANISOU 383 N ILE A 48 4468 3793 7816 155 1063 750 N ATOM 384 CA ILE A 48 23.368 -36.105 -47.294 1.00 45.09 C ANISOU 384 CA ILE A 48 4750 4076 8307 129 1021 784 C ATOM 385 C ILE A 48 23.492 -34.817 -48.116 1.00 45.01 C ANISOU 385 C ILE A 48 4729 4055 8316 137 1111 821 C ATOM 386 O ILE A 48 23.551 -33.717 -47.565 1.00 50.76 O ANISOU 386 O ILE A 48 5456 4749 9083 109 1060 831 O ATOM 387 CB ILE A 48 24.744 -36.799 -47.237 1.00 41.47 C ANISOU 387 CB ILE A 48 4188 3553 8016 133 1019 801 C ATOM 388 CG1 ILE A 48 24.725 -37.938 -46.216 1.00 49.88 C ANISOU 388 CG1 ILE A 48 5272 4609 9073 129 908 776 C ATOM 389 CG2 ILE A 48 25.848 -35.797 -46.885 1.00 34.22 C ANISOU 389 CG2 ILE A 48 3170 2559 7272 103 986 831 C ATOM 390 CD1 ILE A 48 25.881 -38.893 -46.364 1.00 49.54 C ANISOU 390 CD1 ILE A 48 5141 4514 9167 154 919 786 C ATOM 391 N MET A 49 23.522 -34.967 -49.438 1.00 45.11 N ANISOU 391 N MET A 49 4748 4093 8297 181 1246 840 N ATOM 392 CA MET A 49 23.732 -33.845 -50.348 1.00 42.97 C ANISOU 392 CA MET A 49 4478 3804 8043 201 1359 892 C ATOM 393 C MET A 49 22.545 -32.883 -50.373 1.00 51.47 C ANISOU 393 C MET A 49 5652 4925 8980 212 1340 885 C ATOM 394 O MET A 49 22.698 -31.715 -50.721 1.00 49.57 O ANISOU 394 O MET A 49 5420 4647 8769 215 1394 932 O ATOM 395 CB MET A 49 24.021 -34.360 -51.762 1.00 41.48 C ANISOU 395 CB MET A 49 4298 3638 7825 266 1514 915 C ATOM 396 CG MET A 49 25.365 -35.058 -51.918 1.00 44.56 C ANISOU 396 CG MET A 49 4577 3973 8381 269 1571 938 C ATOM 397 SD MET A 49 26.775 -33.950 -51.710 1.00 59.42 S ANISOU 397 SD MET A 49 6318 5746 10511 219 1618 1013 S ATOM 398 CE MET A 49 27.317 -34.413 -50.064 1.00 62.96 C ANISOU 398 CE MET A 49 6676 6148 11100 154 1414 967 C ATOM 399 N LEU A 50 21.364 -33.375 -50.015 1.00 45.96 N ANISOU 399 N LEU A 50 5023 4300 8139 220 1268 829 N ATOM 400 CA LEU A 50 20.186 -32.523 -49.914 1.00 48.91 C ANISOU 400 CA LEU A 50 5475 4721 8389 236 1237 814 C ATOM 401 C LEU A 50 19.936 -32.124 -48.465 1.00 52.77 C ANISOU 401 C LEU A 50 5966 5188 8894 189 1113 790 C ATOM 402 O LEU A 50 19.704 -30.955 -48.166 1.00 53.55 O ANISOU 402 O LEU A 50 6095 5264 8989 187 1090 801 O ATOM 403 CB LEU A 50 18.954 -33.226 -50.484 1.00 42.04 C ANISOU 403 CB LEU A 50 4667 3948 7358 279 1243 763 C ATOM 404 CG LEU A 50 19.003 -33.597 -51.968 1.00 48.18 C ANISOU 404 CG LEU A 50 5474 4759 8074 346 1350 769 C ATOM 405 CD1 LEU A 50 17.681 -34.204 -52.422 1.00 44.72 C ANISOU 405 CD1 LEU A 50 5093 4414 7485 385 1317 700 C ATOM 406 CD2 LEU A 50 19.363 -32.392 -52.810 1.00 48.60 C ANISOU 406 CD2 LEU A 50 5556 4782 8126 391 1448 838 C ATOM 407 N GLY A 51 20.004 -33.105 -47.572 1.00 43.02 N ANISOU 407 N GLY A 51 4713 3956 7675 158 1035 758 N ATOM 408 CA GLY A 51 19.685 -32.906 -46.170 1.00 48.33 C ANISOU 408 CA GLY A 51 5413 4620 8331 129 920 733 C ATOM 409 C GLY A 51 20.615 -31.973 -45.419 1.00 50.77 C ANISOU 409 C GLY A 51 5690 4840 8760 100 851 748 C ATOM 410 O GLY A 51 20.156 -31.145 -44.638 1.00 51.05 O ANISOU 410 O GLY A 51 5776 4867 8752 99 783 728 O ATOM 411 N PHE A 52 21.920 -32.100 -45.634 1.00 42.86 N ANISOU 411 N PHE A 52 4600 3769 7918 80 863 775 N ATOM 412 CA PHE A 52 22.847 -31.235 -44.917 1.00 53.66 C ANISOU 412 CA PHE A 52 5919 5043 9428 44 780 778 C ATOM 413 C PHE A 52 22.728 -29.767 -45.350 1.00 49.52 C ANISOU 413 C PHE A 52 5413 4477 8927 41 826 801 C ATOM 414 O PHE A 52 22.610 -28.902 -44.488 1.00 42.27 O ANISOU 414 O PHE A 52 4530 3515 8015 26 729 772 O ATOM 415 CB PHE A 52 24.301 -31.696 -45.065 1.00 48.86 C ANISOU 415 CB PHE A 52 5185 4366 9015 21 783 802 C ATOM 416 CG PHE A 52 25.300 -30.658 -44.620 1.00 48.46 C ANISOU 416 CG PHE A 52 5056 4209 9147 -22 716 805 C ATOM 417 CD1 PHE A 52 25.573 -30.470 -43.273 1.00 57.39 C ANISOU 417 CD1 PHE A 52 6194 5297 10315 -42 538 756 C ATOM 418 CD2 PHE A 52 25.940 -29.849 -45.544 1.00 56.33 C ANISOU 418 CD2 PHE A 52 5980 5145 10279 -42 830 857 C ATOM 419 CE1 PHE A 52 26.482 -29.506 -42.860 1.00 56.00 C ANISOU 419 CE1 PHE A 52 5941 5015 10320 -85 456 744 C ATOM 420 CE2 PHE A 52 26.846 -28.881 -45.136 1.00 57.35 C ANISOU 420 CE2 PHE A 52 6025 5163 10604 -95 769 857 C ATOM 421 CZ PHE A 52 27.117 -28.711 -43.794 1.00 53.52 C ANISOU 421 CZ PHE A 52 5536 4633 10166 -119 572 793 C ATOM 422 N PRO A 53 22.773 -29.476 -46.670 1.00 46.73 N ANISOU 422 N PRO A 53 5047 4128 8580 62 973 852 N ATOM 423 CA PRO A 53 22.690 -28.056 -47.041 1.00 50.07 C ANISOU 423 CA PRO A 53 5498 4495 9031 62 1019 885 C ATOM 424 C PRO A 53 21.395 -27.382 -46.590 1.00 47.81 C ANISOU 424 C PRO A 53 5327 4253 8585 94 964 848 C ATOM 425 O PRO A 53 21.458 -26.285 -46.050 1.00 54.57 O ANISOU 425 O PRO A 53 6207 5038 9491 76 907 839 O ATOM 426 CB PRO A 53 22.774 -28.086 -48.570 1.00 52.31 C ANISOU 426 CB PRO A 53 5781 4799 9296 103 1196 950 C ATOM 427 CG PRO A 53 23.477 -29.351 -48.880 1.00 50.65 C ANISOU 427 CG PRO A 53 5494 4610 9142 102 1234 953 C ATOM 428 CD PRO A 53 22.989 -30.325 -47.858 1.00 39.40 C ANISOU 428 CD PRO A 53 4089 3240 7641 94 1103 885 C ATOM 429 N ILE A 54 20.250 -28.033 -46.774 1.00 48.63 N ANISOU 429 N ILE A 54 5495 4468 8513 139 977 822 N ATOM 430 CA ILE A 54 18.978 -27.401 -46.443 1.00 50.41 C ANISOU 430 CA ILE A 54 5814 4745 8596 179 943 790 C ATOM 431 C ILE A 54 18.844 -27.185 -44.931 1.00 52.44 C ANISOU 431 C ILE A 54 6099 4978 8848 156 808 736 C ATOM 432 O ILE A 54 18.334 -26.154 -44.494 1.00 50.61 O ANISOU 432 O ILE A 54 5930 4723 8576 177 770 717 O ATOM 433 CB ILE A 54 17.764 -28.216 -46.984 1.00 51.19 C ANISOU 433 CB ILE A 54 5950 4969 8529 228 983 768 C ATOM 434 CG1 ILE A 54 16.470 -27.423 -46.822 1.00 72.35 C ANISOU 434 CG1 ILE A 54 8706 7699 11082 279 964 742 C ATOM 435 CG2 ILE A 54 17.627 -29.554 -46.299 1.00 57.49 C ANISOU 435 CG2 ILE A 54 6725 5816 9302 201 929 729 C ATOM 436 CD1 ILE A 54 15.246 -28.179 -47.277 1.00 89.29 C ANISOU 436 CD1 ILE A 54 10869 9966 13092 322 986 709 C ATOM 437 N ASN A 55 19.326 -28.128 -44.128 1.00 43.52 N ANISOU 437 N ASN A 55 4936 3849 7753 124 734 713 N ATOM 438 CA ASN A 55 19.197 -27.991 -42.683 1.00 43.14 C ANISOU 438 CA ASN A 55 4936 3782 7672 119 605 663 C ATOM 439 C ASN A 55 20.257 -27.073 -42.084 1.00 54.02 C ANISOU 439 C ASN A 55 6288 5039 9197 84 511 649 C ATOM 440 O ASN A 55 19.992 -26.356 -41.119 1.00 50.01 O ANISOU 440 O ASN A 55 5852 4500 8650 97 415 603 O ATOM 441 CB ASN A 55 19.246 -29.361 -42.012 1.00 40.98 C ANISOU 441 CB ASN A 55 4656 3553 7362 110 559 649 C ATOM 442 CG ASN A 55 17.979 -30.161 -42.242 1.00 47.93 C ANISOU 442 CG ASN A 55 5576 4543 8093 137 624 643 C ATOM 443 OD1 ASN A 55 16.944 -29.882 -41.638 1.00 48.75 O ANISOU 443 OD1 ASN A 55 5750 4694 8078 166 610 617 O ATOM 444 ND2 ASN A 55 18.053 -31.160 -43.114 1.00 49.53 N ANISOU 444 ND2 ASN A 55 5729 4781 8310 130 697 664 N ATOM 445 N PHE A 56 21.456 -27.093 -42.656 1.00 48.80 N ANISOU 445 N PHE A 56 5524 4306 8714 41 538 685 N ATOM 446 CA PHE A 56 22.511 -26.209 -42.192 1.00 45.40 C ANISOU 446 CA PHE A 56 5042 3748 8461 -4 450 670 C ATOM 447 C PHE A 56 22.189 -24.765 -42.577 1.00 49.32 C ANISOU 447 C PHE A 56 5584 4181 8973 0 493 681 C ATOM 448 O PHE A 56 22.458 -23.836 -41.812 1.00 47.77 O ANISOU 448 O PHE A 56 5413 3894 8845 -19 384 636 O ATOM 449 CB PHE A 56 23.872 -26.627 -42.760 1.00 38.53 C ANISOU 449 CB PHE A 56 4025 2817 7799 -51 488 712 C ATOM 450 CG PHE A 56 24.994 -25.718 -42.354 1.00 45.51 C ANISOU 450 CG PHE A 56 4827 3562 8903 -109 399 695 C ATOM 451 CD1 PHE A 56 25.642 -25.898 -41.142 1.00 59.63 C ANISOU 451 CD1 PHE A 56 6589 5304 10765 -127 211 629 C ATOM 452 CD2 PHE A 56 25.387 -24.673 -43.170 1.00 50.61 C ANISOU 452 CD2 PHE A 56 5426 4118 9686 -144 498 744 C ATOM 453 CE1 PHE A 56 26.669 -25.058 -40.760 1.00 62.53 C ANISOU 453 CE1 PHE A 56 6868 5537 11352 -184 109 598 C ATOM 454 CE2 PHE A 56 26.411 -23.825 -42.792 1.00 58.09 C ANISOU 454 CE2 PHE A 56 6284 4923 10863 -209 416 724 C ATOM 455 CZ PHE A 56 27.054 -24.020 -41.585 1.00 60.99 C ANISOU 455 CZ PHE A 56 6611 5246 11316 -233 213 645 C ATOM 456 N LEU A 57 21.611 -24.585 -43.763 1.00 44.70 N ANISOU 456 N LEU A 57 5020 3641 8325 31 643 738 N ATOM 457 CA LEU A 57 21.223 -23.261 -44.239 1.00 48.84 C ANISOU 457 CA LEU A 57 5601 4107 8847 50 698 763 C ATOM 458 C LEU A 57 20.143 -22.640 -43.353 1.00 49.98 C ANISOU 458 C LEU A 57 5867 4277 8847 98 611 698 C ATOM 459 O LEU A 57 20.106 -21.421 -43.171 1.00 56.71 O ANISOU 459 O LEU A 57 6767 5036 9743 100 583 686 O ATOM 460 CB LEU A 57 20.735 -23.327 -45.690 1.00 48.72 C ANISOU 460 CB LEU A 57 5604 4152 8755 96 868 837 C ATOM 461 CG LEU A 57 20.324 -21.988 -46.313 1.00 63.29 C ANISOU 461 CG LEU A 57 7521 5937 10589 131 940 879 C ATOM 462 CD1 LEU A 57 21.510 -21.027 -46.384 1.00 60.27 C ANISOU 462 CD1 LEU A 57 7077 5385 10438 62 955 919 C ATOM 463 CD2 LEU A 57 19.706 -22.189 -47.690 1.00 64.48 C ANISOU 463 CD2 LEU A 57 7712 6169 10618 201 1086 943 C ATOM 464 N THR A 58 19.263 -23.479 -42.812 1.00 49.56 N ANISOU 464 N THR A 58 5861 4342 8627 137 577 659 N ATOM 465 CA THR A 58 18.232 -23.021 -41.887 1.00 53.31 C ANISOU 465 CA THR A 58 6444 4851 8959 190 507 597 C ATOM 466 C THR A 58 18.874 -22.371 -40.662 1.00 58.10 C ANISOU 466 C THR A 58 7081 5352 9644 166 357 533 C ATOM 467 O THR A 58 18.452 -21.301 -40.216 1.00 56.07 O ANISOU 467 O THR A 58 6908 5043 9354 199 312 493 O ATOM 468 CB THR A 58 17.308 -24.180 -41.446 1.00 46.92 C ANISOU 468 CB THR A 58 5662 4180 7986 224 509 574 C ATOM 469 OG1 THR A 58 16.614 -24.699 -42.588 1.00 44.33 O ANISOU 469 OG1 THR A 58 5309 3946 7588 250 630 616 O ATOM 470 CG2 THR A 58 16.282 -23.706 -40.411 1.00 40.79 C ANISOU 470 CG2 THR A 58 4992 3438 7068 283 454 515 C ATOM 471 N LEU A 59 19.910 -23.011 -40.132 1.00 51.34 N ANISOU 471 N LEU A 59 6158 4457 8892 114 269 518 N ATOM 472 CA LEU A 59 20.629 -22.475 -38.985 1.00 47.58 C ANISOU 472 CA LEU A 59 5703 3877 8499 93 100 446 C ATOM 473 C LEU A 59 21.422 -21.242 -39.379 1.00 55.11 C ANISOU 473 C LEU A 59 6609 4678 9653 41 89 451 C ATOM 474 O LEU A 59 21.551 -20.294 -38.606 1.00 46.14 O ANISOU 474 O LEU A 59 5533 3446 8554 43 -30 382 O ATOM 475 CB LEU A 59 21.564 -23.531 -38.393 1.00 46.71 C ANISOU 475 CB LEU A 59 5523 3768 8458 60 2 432 C ATOM 476 CG LEU A 59 20.901 -24.856 -38.016 1.00 54.90 C ANISOU 476 CG LEU A 59 6603 4936 9320 102 22 440 C ATOM 477 CD1 LEU A 59 21.921 -25.825 -37.432 1.00 47.87 C ANISOU 477 CD1 LEU A 59 5651 4027 8510 78 -85 430 C ATOM 478 CD2 LEU A 59 19.759 -24.609 -37.045 1.00 58.81 C ANISOU 478 CD2 LEU A 59 7250 5489 9608 174 -17 389 C ATOM 479 N TYR A 60 21.949 -21.257 -40.596 1.00 55.34 N ANISOU 479 N TYR A 60 6535 4680 9813 -2 220 534 N ATOM 480 CA TYR A 60 22.844 -20.203 -41.034 1.00 53.35 C ANISOU 480 CA TYR A 60 6215 4270 9784 -66 233 558 C ATOM 481 C TYR A 60 22.114 -18.882 -41.275 1.00 58.43 C ANISOU 481 C TYR A 60 6964 4852 10384 -31 276 561 C ATOM 482 O TYR A 60 22.606 -17.825 -40.880 1.00 56.38 O ANISOU 482 O TYR A 60 6711 4444 10266 -70 194 521 O ATOM 483 CB TYR A 60 23.594 -20.625 -42.297 1.00 48.92 C ANISOU 483 CB TYR A 60 5523 3701 9363 -111 390 659 C ATOM 484 CG TYR A 60 24.576 -19.576 -42.757 1.00 56.00 C ANISOU 484 CG TYR A 60 6335 4427 10515 -186 428 698 C ATOM 485 CD1 TYR A 60 25.794 -19.406 -42.109 1.00 61.58 C ANISOU 485 CD1 TYR A 60 6925 5014 11460 -267 298 651 C ATOM 486 CD2 TYR A 60 24.280 -18.740 -43.824 1.00 59.92 C ANISOU 486 CD2 TYR A 60 6868 4876 11022 -174 591 783 C ATOM 487 CE1 TYR A 60 26.692 -18.437 -42.516 1.00 68.54 C ANISOU 487 CE1 TYR A 60 7712 5726 12604 -348 338 686 C ATOM 488 CE2 TYR A 60 25.174 -17.769 -44.241 1.00 60.11 C ANISOU 488 CE2 TYR A 60 6818 4730 11293 -248 643 831 C ATOM 489 CZ TYR A 60 26.378 -17.622 -43.584 1.00 64.19 C ANISOU 489 CZ TYR A 60 7203 5143 12043 -338 519 777 C ATOM 490 OH TYR A 60 27.271 -16.655 -43.995 1.00 69.64 O ANISOU 490 OH TYR A 60 7805 5742 12913 -405 565 804 O ATOM 491 N VAL A 61 20.948 -18.931 -41.915 1.00 48.31 N ANISOU 491 N VAL A 61 5763 3676 8915 44 394 601 N ATOM 492 CA VAL A 61 20.199 -17.705 -42.177 1.00 51.30 C ANISOU 492 CA VAL A 61 6247 4002 9243 95 435 608 C ATOM 493 C VAL A 61 19.641 -17.122 -40.882 1.00 49.96 C ANISOU 493 C VAL A 61 6191 3808 8982 139 286 499 C ATOM 494 O VAL A 61 19.408 -15.918 -40.783 1.00 60.15 O ANISOU 494 O VAL A 61 7559 4994 10300 161 267 477 O ATOM 495 CB VAL A 61 19.045 -17.928 -43.185 1.00 52.65 C ANISOU 495 CB VAL A 61 6471 4302 9232 180 581 671 C ATOM 496 CG1 VAL A 61 19.606 -18.356 -44.536 1.00 49.51 C ANISOU 496 CG1 VAL A 61 5989 3913 8910 152 733 778 C ATOM 497 CG2 VAL A 61 18.033 -18.948 -42.658 1.00 54.07 C ANISOU 497 CG2 VAL A 61 6688 4654 9202 239 550 623 C ATOM 498 N THR A 62 19.442 -17.978 -39.887 1.00 51.67 N ANISOU 498 N THR A 62 6428 4117 9088 159 186 432 N ATOM 499 CA THR A 62 18.920 -17.534 -38.604 1.00 56.74 C ANISOU 499 CA THR A 62 7191 4749 9617 215 53 328 C ATOM 500 C THR A 62 19.977 -16.699 -37.886 1.00 62.12 C ANISOU 500 C THR A 62 7868 5254 10483 156 -105 255 C ATOM 501 O THR A 62 19.655 -15.775 -37.140 1.00 58.02 O ANISOU 501 O THR A 62 7461 4660 9924 199 -198 173 O ATOM 502 CB THR A 62 18.482 -18.732 -37.741 1.00 46.60 C ANISOU 502 CB THR A 62 5938 3606 8163 254 4 291 C ATOM 503 OG1 THR A 62 17.467 -19.461 -38.440 1.00 56.57 O ANISOU 503 OG1 THR A 62 7193 5020 9281 298 147 351 O ATOM 504 CG2 THR A 62 17.923 -18.271 -36.408 1.00 43.79 C ANISOU 504 CG2 THR A 62 5725 3244 7669 327 -115 189 C ATOM 505 N VAL A 63 21.243 -17.017 -38.142 1.00 62.85 N ANISOU 505 N VAL A 63 7823 5273 10785 60 -134 281 N ATOM 506 CA VAL A 63 22.358 -16.249 -37.598 1.00 50.33 C ANISOU 506 CA VAL A 63 6193 3507 9424 -14 -285 213 C ATOM 507 C VAL A 63 22.488 -14.883 -38.300 1.00 53.55 C ANISOU 507 C VAL A 63 6604 3755 9989 -49 -215 247 C ATOM 508 O VAL A 63 22.865 -13.894 -37.675 1.00 56.46 O ANISOU 508 O VAL A 63 7010 3967 10473 -75 -347 164 O ATOM 509 CB VAL A 63 23.695 -17.040 -37.715 1.00 47.98 C ANISOU 509 CB VAL A 63 5718 3181 9330 -106 -329 236 C ATOM 510 CG1 VAL A 63 24.868 -16.216 -37.203 1.00 47.40 C ANISOU 510 CG1 VAL A 63 5572 2915 9523 -190 -493 161 C ATOM 511 CG2 VAL A 63 23.612 -18.350 -36.948 1.00 45.44 C ANISOU 511 CG2 VAL A 63 5410 2998 8860 -64 -412 202 C ATOM 512 N AGLN A 64 22.132 -14.827 -39.581 0.50 49.86 N ANISOU 512 N AGLN A 64 6111 3322 9512 -43 -12 367 N ATOM 513 N BGLN A 64 22.175 -14.837 -39.593 0.50 49.53 N ANISOU 513 N BGLN A 64 6064 3277 9478 -46 -12 369 N ATOM 514 CA AGLN A 64 22.310 -13.606 -40.366 0.50 56.01 C ANISOU 514 CA AGLN A 64 6894 3944 10442 -75 81 426 C ATOM 515 CA BGLN A 64 22.296 -13.597 -40.361 0.50 55.98 C ANISOU 515 CA BGLN A 64 6893 3941 10436 -73 81 426 C ATOM 516 C AGLN A 64 21.070 -12.700 -40.398 0.50 51.83 C ANISOU 516 C AGLN A 64 6535 3416 9743 29 119 415 C ATOM 517 C BGLN A 64 21.079 -12.683 -40.220 0.50 51.71 C ANISOU 517 C BGLN A 64 6526 3396 9725 29 93 397 C ATOM 518 O AGLN A 64 21.189 -11.492 -40.616 0.50 57.90 O ANISOU 518 O AGLN A 64 7347 4019 10632 13 133 424 O ATOM 519 O BGLN A 64 21.218 -11.459 -40.152 0.50 59.50 O ANISOU 519 O BGLN A 64 7566 4212 10829 14 63 375 O ATOM 520 CB AGLN A 64 22.727 -13.965 -41.796 0.50 61.94 C ANISOU 520 CB AGLN A 64 7535 4713 11286 -115 288 573 C ATOM 521 CB BGLN A 64 22.525 -13.903 -41.846 0.50 61.88 C ANISOU 521 CB BGLN A 64 7551 4717 11245 -99 300 576 C ATOM 522 CG AGLN A 64 23.924 -14.911 -41.879 0.50 63.29 C ANISOU 522 CG AGLN A 64 7529 4892 11626 -204 278 594 C ATOM 523 CG BGLN A 64 23.925 -14.379 -42.191 0.50 65.03 C ANISOU 523 CG BGLN A 64 7763 5051 11893 -212 324 622 C ATOM 524 CD AGLN A 64 25.222 -14.279 -41.395 0.50 60.41 C ANISOU 524 CD AGLN A 64 7051 4349 11553 -317 158 543 C ATOM 525 CD BGLN A 64 24.208 -14.304 -43.681 0.50 69.51 C ANISOU 525 CD BGLN A 64 8269 5635 12508 -228 553 766 C ATOM 526 OE1AGLN A 64 25.323 -13.063 -41.259 0.50 55.88 O ANISOU 526 OE1AGLN A 64 6522 3659 11050 -341 121 512 O ATOM 527 OE1BGLN A 64 23.308 -14.052 -44.483 0.50 67.02 O ANISOU 527 OE1BGLN A 64 8056 5363 12045 -149 689 840 O ATOM 528 NE2AGLN A 64 26.223 -15.111 -41.137 0.50 69.05 N ANISOU 528 NE2AGLN A 64 7993 5464 12777 -379 91 525 N ATOM 529 NE2BGLN A 64 25.466 -14.510 -44.058 0.50 68.81 N ANISOU 529 NE2BGLN A 64 8014 5531 12602 -316 593 801 N ATOM 530 N HIS A 65 19.890 -13.276 -40.184 1.00 48.48 N ANISOU 530 N HIS A 65 6197 3169 9054 134 139 396 N ATOM 531 CA HIS A 65 18.645 -12.497 -40.190 1.00 51.02 C ANISOU 531 CA HIS A 65 6665 3511 9209 247 175 381 C ATOM 532 C HIS A 65 17.968 -12.459 -38.821 1.00 54.65 C ANISOU 532 C HIS A 65 7241 4020 9504 324 33 250 C ATOM 533 O HIS A 65 17.394 -13.452 -38.378 1.00 51.65 O ANISOU 533 O HIS A 65 6870 3806 8949 371 27 228 O ATOM 534 CB HIS A 65 17.675 -13.058 -41.230 1.00 41.34 C ANISOU 534 CB HIS A 65 5443 2451 7814 322 341 475 C ATOM 535 CG HIS A 65 18.226 -13.080 -42.623 1.00 48.42 C ANISOU 535 CG HIS A 65 6257 3311 8828 275 495 607 C ATOM 536 ND1 HIS A 65 17.955 -12.090 -43.545 1.00 45.90 N ANISOU 536 ND1 HIS A 65 5999 2905 8536 314 605 687 N ATOM 537 CD2 HIS A 65 19.031 -13.970 -43.251 1.00 48.34 C ANISOU 537 CD2 HIS A 65 6121 3337 8907 203 564 675 C ATOM 538 CE1 HIS A 65 18.569 -12.369 -44.680 1.00 53.85 C ANISOU 538 CE1 HIS A 65 6926 3899 9633 269 742 803 C ATOM 539 NE2 HIS A 65 19.230 -13.504 -44.528 1.00 52.99 N ANISOU 539 NE2 HIS A 65 6700 3866 9566 201 722 794 N ATOM 540 N LYS A 66 18.015 -11.302 -38.166 1.00 59.40 N ANISOU 540 N LYS A 66 7940 4469 10160 341 -71 166 N ATOM 541 CA LYS A 66 17.578 -11.205 -36.774 1.00 64.77 C ANISOU 541 CA LYS A 66 8740 5170 10698 413 -220 29 C ATOM 542 C LYS A 66 16.069 -11.352 -36.602 1.00 59.74 C ANISOU 542 C LYS A 66 8209 4693 9794 555 -144 20 C ATOM 543 O LYS A 66 15.598 -11.700 -35.521 1.00 63.98 O ANISOU 543 O LYS A 66 8828 5312 10169 623 -222 -66 O ATOM 544 CB LYS A 66 18.040 -9.880 -36.160 1.00 67.83 C ANISOU 544 CB LYS A 66 9213 5339 11222 399 -357 -70 C ATOM 545 CG LYS A 66 17.344 -8.642 -36.686 1.00 67.56 C ANISOU 545 CG LYS A 66 9277 5206 11186 466 -276 -47 C ATOM 546 CD LYS A 66 17.884 -7.411 -35.975 1.00 84.93 C ANISOU 546 CD LYS A 66 11562 7174 13535 442 -431 -162 C ATOM 547 CE LYS A 66 17.367 -6.124 -36.585 1.00 88.46 C ANISOU 547 CE LYS A 66 12101 7484 14026 494 -348 -126 C ATOM 548 NZ LYS A 66 18.013 -4.934 -35.964 1.00 92.51 N ANISOU 548 NZ LYS A 66 12683 7742 14724 450 -501 -237 N ATOM 549 N LYS A 67 15.316 -11.091 -37.666 1.00 48.26 N ANISOU 549 N LYS A 67 6753 3287 8299 605 9 111 N ATOM 550 CA LYS A 67 13.866 -11.254 -37.622 1.00 49.76 C ANISOU 550 CA LYS A 67 7010 3634 8261 738 87 108 C ATOM 551 C LYS A 67 13.457 -12.725 -37.505 1.00 54.17 C ANISOU 551 C LYS A 67 7499 4401 8683 740 132 131 C ATOM 552 O LYS A 67 12.318 -13.028 -37.152 1.00 52.93 O ANISOU 552 O LYS A 67 7386 4380 8345 838 175 108 O ATOM 553 CB LYS A 67 13.219 -10.626 -38.858 1.00 52.55 C ANISOU 553 CB LYS A 67 7370 3981 8615 795 221 200 C ATOM 554 CG LYS A 67 13.346 -9.104 -38.915 1.00 63.83 C ANISOU 554 CG LYS A 67 8898 5206 10148 822 192 180 C ATOM 555 CD LYS A 67 12.814 -8.458 -37.646 1.00 71.20 C ANISOU 555 CD LYS A 67 9969 6100 10983 914 83 44 C ATOM 556 CE LYS A 67 12.975 -6.944 -37.679 1.00 88.49 C ANISOU 556 CE LYS A 67 12265 8068 13290 938 44 14 C ATOM 557 NZ LYS A 67 12.504 -6.298 -36.421 1.00 88.08 N ANISOU 557 NZ LYS A 67 12360 7968 13140 1036 -69 -132 N ATOM 558 N LEU A 68 14.385 -13.635 -37.792 1.00 41.96 N ANISOU 558 N LEU A 68 5839 2870 7234 633 127 177 N ATOM 559 CA LEU A 68 14.094 -15.066 -37.690 1.00 41.27 C ANISOU 559 CA LEU A 68 5687 2958 7037 626 166 200 C ATOM 560 C LEU A 68 14.192 -15.542 -36.245 1.00 51.53 C ANISOU 560 C LEU A 68 7048 4285 8245 641 47 109 C ATOM 561 O LEU A 68 13.616 -16.568 -35.879 1.00 51.28 O ANISOU 561 O LEU A 68 7010 4398 8076 670 84 115 O ATOM 562 CB LEU A 68 15.040 -15.879 -38.577 1.00 38.44 C ANISOU 562 CB LEU A 68 5190 2603 6811 519 212 284 C ATOM 563 CG LEU A 68 14.843 -15.759 -40.090 1.00 53.06 C ANISOU 563 CG LEU A 68 6985 4474 8703 520 356 388 C ATOM 564 CD1 LEU A 68 15.862 -16.604 -40.836 1.00 37.54 C ANISOU 564 CD1 LEU A 68 4893 2508 6862 422 401 459 C ATOM 565 CD2 LEU A 68 13.430 -16.149 -40.495 1.00 43.02 C ANISOU 565 CD2 LEU A 68 5731 3366 7247 616 449 406 C ATOM 566 N ARG A 69 14.910 -14.786 -35.420 1.00 51.25 N ANISOU 566 N ARG A 69 7082 4106 8286 626 -97 25 N ATOM 567 CA ARG A 69 15.142 -15.187 -34.035 1.00 53.25 C ANISOU 567 CA ARG A 69 7412 4371 8448 650 -233 -66 C ATOM 568 C ARG A 69 13.985 -14.829 -33.117 1.00 61.27 C ANISOU 568 C ARG A 69 8582 5449 9250 785 -229 -137 C ATOM 569 O ARG A 69 14.146 -14.059 -32.173 1.00 67.31 O ANISOU 569 O ARG A 69 9471 6117 9987 833 -354 -242 O ATOM 570 CB ARG A 69 16.427 -14.557 -33.512 1.00 53.04 C ANISOU 570 CB ARG A 69 7393 4163 8596 582 -413 -141 C ATOM 571 CG ARG A 69 17.668 -15.095 -34.187 1.00 52.11 C ANISOU 571 CG ARG A 69 7111 3995 8693 451 -426 -79 C ATOM 572 CD ARG A 69 18.906 -14.370 -33.700 1.00 63.84 C ANISOU 572 CD ARG A 69 8582 5290 10383 379 -608 -160 C ATOM 573 NE ARG A 69 19.743 -13.985 -34.827 1.00 75.30 N ANISOU 573 NE ARG A 69 9891 6630 12092 268 -544 -82 N ATOM 574 CZ ARG A 69 20.151 -12.746 -35.067 1.00 76.83 C ANISOU 574 CZ ARG A 69 10090 6640 12461 227 -576 -106 C ATOM 575 NH1 ARG A 69 19.817 -11.764 -34.243 1.00 80.52 N ANISOU 575 NH1 ARG A 69 10703 7013 12877 289 -690 -218 N ATOM 576 NH2 ARG A 69 20.907 -12.495 -36.125 1.00 93.32 N ANISOU 576 NH2 ARG A 69 12045 8634 14780 126 -487 -16 N ATOM 577 N THR A 70 12.823 -15.406 -33.399 1.00 59.53 N ANISOU 577 N THR A 70 8346 5389 8882 847 -84 -85 N ATOM 578 CA THR A 70 11.629 -15.202 -32.589 1.00 62.92 C ANISOU 578 CA THR A 70 8896 5901 9110 978 -42 -138 C ATOM 579 C THR A 70 11.301 -16.502 -31.860 1.00 61.87 C ANISOU 579 C THR A 70 8769 5910 8830 994 -9 -123 C ATOM 580 O THR A 70 11.596 -17.580 -32.371 1.00 61.66 O ANISOU 580 O THR A 70 8627 5951 8850 914 36 -48 O ATOM 581 CB THR A 70 10.432 -14.767 -33.453 1.00 60.67 C ANISOU 581 CB THR A 70 8582 5686 8785 1049 105 -92 C ATOM 582 OG1 THR A 70 10.066 -15.837 -34.333 1.00 73.61 O ANISOU 582 OG1 THR A 70 10085 7460 10425 1003 223 3 O ATOM 583 CG2 THR A 70 10.797 -13.560 -34.278 1.00 52.35 C ANISOU 583 CG2 THR A 70 7527 4485 7879 1031 86 -84 C ATOM 584 N PRO A 71 10.703 -16.402 -30.660 1.00 61.59 N ANISOU 584 N PRO A 71 8875 5912 8614 1103 -24 -191 N ATOM 585 CA PRO A 71 10.363 -17.579 -29.848 1.00 58.02 C ANISOU 585 CA PRO A 71 8454 5581 8008 1130 20 -169 C ATOM 586 C PRO A 71 9.599 -18.659 -30.615 1.00 55.31 C ANISOU 586 C PRO A 71 7973 5387 7655 1094 190 -66 C ATOM 587 O PRO A 71 9.869 -19.843 -30.425 1.00 58.80 O ANISOU 587 O PRO A 71 8374 5888 8078 1042 204 -17 O ATOM 588 CB PRO A 71 9.497 -16.987 -28.733 1.00 49.17 C ANISOU 588 CB PRO A 71 7507 4484 6693 1279 37 -247 C ATOM 589 CG PRO A 71 10.042 -15.614 -28.559 1.00 49.32 C ANISOU 589 CG PRO A 71 7619 4339 6781 1306 -104 -346 C ATOM 590 CD PRO A 71 10.402 -15.146 -29.948 1.00 49.12 C ANISOU 590 CD PRO A 71 7451 4244 6966 1210 -88 -294 C ATOM 591 N LEU A 72 8.677 -18.255 -31.482 1.00 45.89 N ANISOU 591 N LEU A 72 6708 4246 6482 1123 306 -37 N ATOM 592 CA LEU A 72 7.891 -19.207 -32.262 1.00 50.89 C ANISOU 592 CA LEU A 72 7204 5015 7117 1092 450 44 C ATOM 593 C LEU A 72 8.728 -19.963 -33.297 1.00 60.49 C ANISOU 593 C LEU A 72 8285 6219 8478 964 435 112 C ATOM 594 O LEU A 72 8.297 -20.997 -33.817 1.00 48.84 O ANISOU 594 O LEU A 72 6705 4846 7006 923 528 171 O ATOM 595 CB LEU A 72 6.732 -18.485 -32.953 1.00 48.33 C ANISOU 595 CB LEU A 72 6838 4743 6783 1169 550 45 C ATOM 596 CG LEU A 72 5.559 -18.149 -32.028 1.00 58.10 C ANISOU 596 CG LEU A 72 8161 6050 7865 1303 629 0 C ATOM 597 CD1 LEU A 72 4.592 -17.188 -32.696 1.00 48.76 C ANISOU 597 CD1 LEU A 72 6946 4887 6694 1393 691 -13 C ATOM 598 CD2 LEU A 72 4.841 -19.424 -31.599 1.00 55.90 C ANISOU 598 CD2 LEU A 72 7828 5909 7501 1296 749 47 C ATOM 599 N ASN A 73 9.921 -19.453 -33.591 1.00 54.16 N ANISOU 599 N ASN A 73 7485 5289 7806 902 323 99 N ATOM 600 CA ASN A 73 10.803 -20.101 -34.555 1.00 41.13 C ANISOU 600 CA ASN A 73 5711 3619 6299 789 317 162 C ATOM 601 C ASN A 73 11.802 -21.054 -33.911 1.00 42.46 C ANISOU 601 C ASN A 73 5878 3766 6490 725 232 166 C ATOM 602 O ASN A 73 12.476 -21.810 -34.610 1.00 44.15 O ANISOU 602 O ASN A 73 5987 3981 6809 640 240 219 O ATOM 603 CB ASN A 73 11.562 -19.058 -35.374 1.00 45.70 C ANISOU 603 CB ASN A 73 6265 4067 7031 752 269 164 C ATOM 604 CG ASN A 73 10.720 -18.458 -36.475 1.00 51.38 C ANISOU 604 CG ASN A 73 6947 4820 7756 796 372 200 C ATOM 605 OD1 ASN A 73 9.613 -18.919 -36.747 1.00 49.75 O ANISOU 605 OD1 ASN A 73 6704 4742 7457 843 470 221 O ATOM 606 ND2 ASN A 73 11.250 -17.432 -37.131 1.00 46.07 N ANISOU 606 ND2 ASN A 73 6280 4026 7200 781 348 210 N ATOM 607 N TYR A 74 11.901 -21.010 -32.584 1.00 46.84 N ANISOU 607 N TYR A 74 6558 4301 6939 777 149 108 N ATOM 608 CA TYR A 74 12.850 -21.853 -31.857 1.00 44.11 C ANISOU 608 CA TYR A 74 6232 3929 6598 737 47 106 C ATOM 609 C TYR A 74 12.672 -23.331 -32.192 1.00 54.46 C ANISOU 609 C TYR A 74 7454 5341 7896 688 141 187 C ATOM 610 O TYR A 74 13.652 -24.051 -32.395 1.00 45.80 O ANISOU 610 O TYR A 74 6290 4211 6899 616 84 216 O ATOM 611 CB TYR A 74 12.712 -21.665 -30.340 1.00 41.30 C ANISOU 611 CB TYR A 74 6052 3564 6075 831 -37 35 C ATOM 612 CG TYR A 74 13.239 -20.357 -29.787 1.00 49.79 C ANISOU 612 CG TYR A 74 7233 4510 7176 871 -189 -67 C ATOM 613 CD1 TYR A 74 13.584 -19.304 -30.625 1.00 53.32 C ANISOU 613 CD1 TYR A 74 7620 4857 7783 829 -215 -85 C ATOM 614 CD2 TYR A 74 13.394 -20.181 -28.416 1.00 56.14 C ANISOU 614 CD2 TYR A 74 8208 5284 7840 956 -308 -147 C ATOM 615 CE1 TYR A 74 14.056 -18.105 -30.111 1.00 50.22 C ANISOU 615 CE1 TYR A 74 7322 4329 7430 858 -356 -183 C ATOM 616 CE2 TYR A 74 13.869 -18.991 -27.895 1.00 57.15 C ANISOU 616 CE2 TYR A 74 8438 5284 7992 994 -463 -256 C ATOM 617 CZ TYR A 74 14.199 -17.958 -28.746 1.00 59.58 C ANISOU 617 CZ TYR A 74 8670 5485 8481 938 -488 -276 C ATOM 618 OH TYR A 74 14.673 -16.774 -28.227 1.00 70.29 O ANISOU 618 OH TYR A 74 10127 6698 9882 968 -645 -390 O ATOM 619 N ILE A 75 11.419 -23.776 -32.249 1.00 50.03 N ANISOU 619 N ILE A 75 6887 4897 7227 727 286 220 N ATOM 620 CA ILE A 75 11.125 -25.187 -32.461 1.00 49.34 C ANISOU 620 CA ILE A 75 6726 4896 7125 682 378 289 C ATOM 621 C ILE A 75 11.472 -25.608 -33.893 1.00 49.09 C ANISOU 621 C ILE A 75 6540 4869 7245 594 418 337 C ATOM 622 O ILE A 75 11.762 -26.780 -34.152 1.00 42.08 O ANISOU 622 O ILE A 75 5586 4006 6395 535 444 385 O ATOM 623 CB ILE A 75 9.635 -25.510 -32.142 1.00 47.55 C ANISOU 623 CB ILE A 75 6516 4784 6765 742 529 307 C ATOM 624 CG1 ILE A 75 9.436 -27.016 -31.968 1.00 50.27 C ANISOU 624 CG1 ILE A 75 6823 5192 7086 697 606 374 C ATOM 625 CG2 ILE A 75 8.707 -24.970 -33.209 1.00 40.62 C ANISOU 625 CG2 ILE A 75 5542 3962 5930 753 623 309 C ATOM 626 CD1 ILE A 75 10.226 -27.596 -30.821 1.00 48.71 C ANISOU 626 CD1 ILE A 75 6741 4948 6819 710 519 381 C ATOM 627 N LEU A 76 11.458 -24.649 -34.815 1.00 44.95 N ANISOU 627 N LEU A 76 5968 4312 6799 592 425 326 N ATOM 628 CA LEU A 76 11.862 -24.904 -36.196 1.00 48.94 C ANISOU 628 CA LEU A 76 6350 4812 7432 524 462 370 C ATOM 629 C LEU A 76 13.376 -25.083 -36.287 1.00 54.79 C ANISOU 629 C LEU A 76 7056 5454 8308 455 365 379 C ATOM 630 O LEU A 76 13.877 -25.840 -37.118 1.00 50.60 O ANISOU 630 O LEU A 76 6430 4931 7866 395 398 424 O ATOM 631 CB LEU A 76 11.408 -23.764 -37.114 1.00 41.12 C ANISOU 631 CB LEU A 76 5342 3809 6472 559 502 365 C ATOM 632 CG LEU A 76 9.895 -23.616 -37.280 1.00 48.99 C ANISOU 632 CG LEU A 76 6337 4913 7364 631 600 358 C ATOM 633 CD1 LEU A 76 9.554 -22.386 -38.108 1.00 46.19 C ANISOU 633 CD1 LEU A 76 5985 4528 7036 681 617 352 C ATOM 634 CD2 LEU A 76 9.315 -24.869 -37.914 1.00 45.44 C ANISOU 634 CD2 LEU A 76 5786 4568 6909 594 687 396 C ATOM 635 N LEU A 77 14.102 -24.370 -35.435 1.00 46.70 N ANISOU 635 N LEU A 77 6106 4334 7304 467 241 330 N ATOM 636 CA LEU A 77 15.546 -24.516 -35.370 1.00 45.57 C ANISOU 636 CA LEU A 77 5919 4094 7303 404 131 328 C ATOM 637 C LEU A 77 15.859 -25.868 -34.760 1.00 46.33 C ANISOU 637 C LEU A 77 6014 4230 7360 390 103 350 C ATOM 638 O LEU A 77 16.783 -26.563 -35.189 1.00 46.93 O ANISOU 638 O LEU A 77 5999 4278 7554 331 82 382 O ATOM 639 CB LEU A 77 16.179 -23.389 -34.551 1.00 47.05 C ANISOU 639 CB LEU A 77 6185 4164 7528 424 -16 254 C ATOM 640 CG LEU A 77 16.036 -21.990 -35.148 1.00 56.34 C ANISOU 640 CG LEU A 77 7366 5267 8773 431 2 235 C ATOM 641 CD1 LEU A 77 16.618 -20.952 -34.205 1.00 65.46 C ANISOU 641 CD1 LEU A 77 8610 6297 9963 451 -158 146 C ATOM 642 CD2 LEU A 77 16.715 -21.930 -36.508 1.00 55.90 C ANISOU 642 CD2 LEU A 77 7177 5166 8896 355 67 299 C ATOM 643 N ASN A 78 15.070 -26.230 -33.756 1.00 45.77 N ANISOU 643 N ASN A 78 6049 4221 7119 451 115 337 N ATOM 644 CA ASN A 78 15.194 -27.523 -33.107 1.00 53.70 C ANISOU 644 CA ASN A 78 7079 5263 8061 450 107 369 C ATOM 645 C ASN A 78 15.032 -28.646 -34.122 1.00 53.91 C ANISOU 645 C ASN A 78 6987 5347 8148 390 222 437 C ATOM 646 O ASN A 78 15.757 -29.639 -34.088 1.00 51.15 O ANISOU 646 O ASN A 78 6600 4980 7854 356 189 468 O ATOM 647 CB ASN A 78 14.161 -27.660 -31.992 1.00 62.25 C ANISOU 647 CB ASN A 78 8298 6411 8943 531 149 360 C ATOM 648 CG ASN A 78 14.480 -28.788 -31.046 1.00 55.54 C ANISOU 648 CG ASN A 78 7520 5568 8015 548 110 391 C ATOM 649 OD1 ASN A 78 15.613 -28.921 -30.587 1.00 52.72 O ANISOU 649 OD1 ASN A 78 7184 5138 7708 544 -37 372 O ATOM 650 ND2 ASN A 78 13.486 -29.621 -30.757 1.00 51.64 N ANISOU 650 ND2 ASN A 78 7058 5155 7406 568 242 442 N ATOM 651 N LEU A 79 14.078 -28.471 -35.031 1.00 44.79 N ANISOU 651 N LEU A 79 5777 4258 6984 386 346 452 N ATOM 652 CA LEU A 79 13.863 -29.415 -36.119 1.00 46.01 C ANISOU 652 CA LEU A 79 5823 4464 7196 335 445 499 C ATOM 653 C LEU A 79 15.103 -29.556 -36.993 1.00 48.58 C ANISOU 653 C LEU A 79 6054 4724 7681 278 407 516 C ATOM 654 O LEU A 79 15.491 -30.663 -37.367 1.00 49.47 O ANISOU 654 O LEU A 79 6108 4844 7845 239 431 549 O ATOM 655 CB LEU A 79 12.677 -28.973 -36.976 1.00 39.97 C ANISOU 655 CB LEU A 79 5018 3773 6396 354 553 496 C ATOM 656 CG LEU A 79 12.370 -29.805 -38.223 1.00 47.19 C ANISOU 656 CG LEU A 79 5827 4742 7363 312 641 526 C ATOM 657 CD1 LEU A 79 12.079 -31.273 -37.868 1.00 42.17 C ANISOU 657 CD1 LEU A 79 5177 4144 6700 280 683 553 C ATOM 658 CD2 LEU A 79 11.202 -29.186 -38.980 1.00 41.61 C ANISOU 658 CD2 LEU A 79 5091 4105 6614 350 716 510 C ATOM 659 N ALA A 80 15.716 -28.422 -37.313 1.00 44.03 N ANISOU 659 N ALA A 80 5463 4076 7189 275 357 495 N ATOM 660 CA ALA A 80 16.856 -28.382 -38.216 1.00 37.45 C ANISOU 660 CA ALA A 80 4531 3177 6520 223 348 518 C ATOM 661 C ALA A 80 18.045 -29.107 -37.604 1.00 43.25 C ANISOU 661 C ALA A 80 5241 3854 7339 195 247 520 C ATOM 662 O ALA A 80 18.745 -29.854 -38.287 1.00 45.33 O ANISOU 662 O ALA A 80 5413 4106 7705 158 276 554 O ATOM 663 CB ALA A 80 17.218 -26.932 -38.554 1.00 35.58 C ANISOU 663 CB ALA A 80 4293 2861 6365 224 322 501 C ATOM 664 N VAL A 81 18.256 -28.883 -36.310 1.00 42.22 N ANISOU 664 N VAL A 81 5198 3688 7156 225 124 480 N ATOM 665 CA VAL A 81 19.319 -29.556 -35.576 1.00 43.29 C ANISOU 665 CA VAL A 81 5326 3772 7349 218 2 475 C ATOM 666 C VAL A 81 19.063 -31.065 -35.523 1.00 49.40 C ANISOU 666 C VAL A 81 6100 4607 8064 219 60 523 C ATOM 667 O VAL A 81 19.982 -31.865 -35.712 1.00 48.62 O ANISOU 667 O VAL A 81 5929 4475 8069 195 26 546 O ATOM 668 CB VAL A 81 19.455 -29.003 -34.140 1.00 46.09 C ANISOU 668 CB VAL A 81 5806 4086 7621 271 -152 414 C ATOM 669 CG1 VAL A 81 20.453 -29.834 -33.337 1.00 54.01 C ANISOU 669 CG1 VAL A 81 6815 5048 8658 282 -289 412 C ATOM 670 CG2 VAL A 81 19.878 -27.546 -34.171 1.00 49.60 C ANISOU 670 CG2 VAL A 81 6244 4444 8158 261 -232 357 C ATOM 671 N ALA A 82 17.809 -31.441 -35.279 1.00 46.24 N ANISOU 671 N ALA A 82 5774 4288 7508 247 152 538 N ATOM 672 CA ALA A 82 17.419 -32.849 -35.206 1.00 47.22 C ANISOU 672 CA ALA A 82 5904 4458 7578 240 220 584 C ATOM 673 C ALA A 82 17.724 -33.578 -36.509 1.00 41.96 C ANISOU 673 C ALA A 82 5113 3798 7030 188 302 616 C ATOM 674 O ALA A 82 18.264 -34.680 -36.498 1.00 53.91 O ANISOU 674 O ALA A 82 6601 5291 8591 175 291 645 O ATOM 675 CB ALA A 82 15.940 -32.973 -34.868 1.00 38.75 C ANISOU 675 CB ALA A 82 4905 3469 6351 267 327 594 C ATOM 676 N ASP A 83 17.373 -32.955 -37.629 1.00 46.64 N ANISOU 676 N ASP A 83 5642 4418 7663 169 381 609 N ATOM 677 CA ASP A 83 17.660 -33.515 -38.946 1.00 42.77 C ANISOU 677 CA ASP A 83 5049 3934 7267 135 461 631 C ATOM 678 C ASP A 83 19.163 -33.686 -39.178 1.00 49.20 C ANISOU 678 C ASP A 83 5786 4670 8239 114 400 642 C ATOM 679 O ASP A 83 19.588 -34.613 -39.860 1.00 56.58 O ANISOU 679 O ASP A 83 6657 5601 9241 98 446 664 O ATOM 680 CB ASP A 83 17.068 -32.635 -40.051 1.00 40.30 C ANISOU 680 CB ASP A 83 4704 3658 6951 138 544 623 C ATOM 681 CG ASP A 83 15.546 -32.574 -40.008 1.00 52.82 C ANISOU 681 CG ASP A 83 6334 5331 8404 161 611 609 C ATOM 682 OD1 ASP A 83 14.918 -33.488 -39.432 1.00 40.21 O ANISOU 682 OD1 ASP A 83 4767 3772 6739 157 632 615 O ATOM 683 OD2 ASP A 83 14.974 -31.609 -40.559 1.00 51.82 O ANISOU 683 OD2 ASP A 83 6208 5231 8249 184 647 595 O ATOM 684 N LEU A 84 19.966 -32.789 -38.613 1.00 44.22 N ANISOU 684 N LEU A 84 5155 3971 7675 118 293 621 N ATOM 685 CA LEU A 84 21.413 -32.884 -38.752 1.00 48.33 C ANISOU 685 CA LEU A 84 5580 4412 8369 96 226 626 C ATOM 686 C LEU A 84 21.968 -34.041 -37.920 1.00 49.44 C ANISOU 686 C LEU A 84 5736 4534 8514 114 139 635 C ATOM 687 O LEU A 84 22.982 -34.634 -38.279 1.00 47.72 O ANISOU 687 O LEU A 84 5425 4275 8432 103 124 651 O ATOM 688 CB LEU A 84 22.081 -31.566 -38.360 1.00 44.83 C ANISOU 688 CB LEU A 84 5123 3893 8017 87 124 592 C ATOM 689 CG LEU A 84 21.889 -30.413 -39.350 1.00 49.05 C ANISOU 689 CG LEU A 84 5621 4414 8603 66 215 599 C ATOM 690 CD1 LEU A 84 22.479 -29.136 -38.792 1.00 46.66 C ANISOU 690 CD1 LEU A 84 5318 4018 8392 53 102 558 C ATOM 691 CD2 LEU A 84 22.519 -30.741 -40.696 1.00 39.47 C ANISOU 691 CD2 LEU A 84 4287 3189 7519 38 332 646 C ATOM 692 N PHE A 85 21.299 -34.360 -36.814 1.00 48.99 N ANISOU 692 N PHE A 85 5803 4505 8307 149 90 629 N ATOM 693 CA PHE A 85 21.614 -35.570 -36.056 1.00 56.41 C ANISOU 693 CA PHE A 85 6786 5431 9217 176 31 652 C ATOM 694 C PHE A 85 21.347 -36.822 -36.891 1.00 53.40 C ANISOU 694 C PHE A 85 6360 5078 8852 155 154 694 C ATOM 695 O PHE A 85 22.065 -37.811 -36.782 1.00 56.19 O ANISOU 695 O PHE A 85 6686 5393 9269 167 118 716 O ATOM 696 CB PHE A 85 20.805 -35.638 -34.758 1.00 55.64 C ANISOU 696 CB PHE A 85 6848 5361 8931 224 -11 651 C ATOM 697 CG PHE A 85 21.463 -34.963 -33.590 1.00 58.05 C ANISOU 697 CG PHE A 85 7223 5614 9217 271 -191 608 C ATOM 698 CD1 PHE A 85 21.406 -33.587 -33.442 1.00 60.75 C ANISOU 698 CD1 PHE A 85 7581 5941 9560 272 -244 552 C ATOM 699 CD2 PHE A 85 22.126 -35.707 -32.630 1.00 61.58 C ANISOU 699 CD2 PHE A 85 7731 6024 9643 321 -316 619 C ATOM 700 CE1 PHE A 85 22.007 -32.964 -32.366 1.00 56.98 C ANISOU 700 CE1 PHE A 85 7174 5408 9066 316 -426 497 C ATOM 701 CE2 PHE A 85 22.730 -35.089 -31.549 1.00 67.86 C ANISOU 701 CE2 PHE A 85 8600 6772 10411 374 -503 568 C ATOM 702 CZ PHE A 85 22.668 -33.715 -31.417 1.00 64.69 C ANISOU 702 CZ PHE A 85 8210 6354 10015 369 -561 501 C ATOM 703 N MET A 86 20.304 -36.780 -37.715 1.00 50.51 N ANISOU 703 N MET A 86 5988 4775 8429 131 288 697 N ATOM 704 CA MET A 86 20.002 -37.893 -38.609 1.00 45.58 C ANISOU 704 CA MET A 86 5321 4172 7824 110 396 718 C ATOM 705 C MET A 86 21.046 -37.967 -39.721 1.00 51.44 C ANISOU 705 C MET A 86 5943 4880 8722 98 422 719 C ATOM 706 O MET A 86 21.444 -39.052 -40.136 1.00 52.62 O ANISOU 706 O MET A 86 6056 5008 8929 99 453 734 O ATOM 707 CB MET A 86 18.594 -37.760 -39.206 1.00 36.67 C ANISOU 707 CB MET A 86 4212 3123 6600 92 512 707 C ATOM 708 CG MET A 86 17.466 -37.712 -38.171 1.00 51.36 C ANISOU 708 CG MET A 86 6174 5024 8315 105 519 712 C ATOM 709 SD MET A 86 15.833 -37.339 -38.869 1.00 63.64 S ANISOU 709 SD MET A 86 7720 6675 9787 90 640 689 S ATOM 710 CE MET A 86 15.528 -38.817 -39.836 1.00 48.83 C ANISOU 710 CE MET A 86 5786 4806 7963 49 724 694 C ATOM 711 N VAL A 87 21.496 -36.807 -40.187 1.00 52.61 N ANISOU 711 N VAL A 87 6034 5015 8940 90 418 705 N ATOM 712 CA VAL A 87 22.434 -36.739 -41.303 1.00 53.95 C ANISOU 712 CA VAL A 87 6090 5154 9256 80 473 715 C ATOM 713 C VAL A 87 23.809 -37.310 -40.944 1.00 53.89 C ANISOU 713 C VAL A 87 6007 5074 9394 91 391 726 C ATOM 714 O VAL A 87 24.386 -38.084 -41.710 1.00 47.98 O ANISOU 714 O VAL A 87 5187 4311 8733 99 455 740 O ATOM 715 CB VAL A 87 22.590 -35.282 -41.805 1.00 55.65 C ANISOU 715 CB VAL A 87 6267 5356 9521 66 497 710 C ATOM 716 CG1 VAL A 87 23.813 -35.136 -42.716 1.00 42.01 C ANISOU 716 CG1 VAL A 87 4415 3576 7972 57 548 733 C ATOM 717 CG2 VAL A 87 21.321 -34.831 -42.528 1.00 51.68 C ANISOU 717 CG2 VAL A 87 5818 4927 8891 71 599 705 C ATOM 718 N PHE A 88 24.325 -36.944 -39.775 1.00 52.29 N ANISOU 718 N PHE A 88 5824 4828 9216 101 244 712 N ATOM 719 CA PHE A 88 25.681 -37.331 -39.394 1.00 60.52 C ANISOU 719 CA PHE A 88 6780 5801 10415 117 139 713 C ATOM 720 C PHE A 88 25.708 -38.538 -38.468 1.00 65.61 C ANISOU 720 C PHE A 88 7498 6435 10996 160 56 726 C ATOM 721 O PHE A 88 26.656 -39.319 -38.484 1.00 77.56 O ANISOU 721 O PHE A 88 8940 7903 12624 186 15 738 O ATOM 722 CB PHE A 88 26.399 -36.155 -38.738 1.00 51.19 C ANISOU 722 CB PHE A 88 5558 4563 9329 106 3 681 C ATOM 723 CG PHE A 88 26.663 -35.021 -39.676 1.00 55.60 C ANISOU 723 CG PHE A 88 6022 5101 10001 62 86 681 C ATOM 724 CD1 PHE A 88 27.723 -35.076 -40.566 1.00 54.40 C ANISOU 724 CD1 PHE A 88 5714 4907 10048 45 152 704 C ATOM 725 CD2 PHE A 88 25.846 -33.901 -39.680 1.00 60.71 C ANISOU 725 CD2 PHE A 88 6740 5768 10558 44 110 665 C ATOM 726 CE1 PHE A 88 27.970 -34.035 -41.437 1.00 56.80 C ANISOU 726 CE1 PHE A 88 5941 5184 10458 6 249 719 C ATOM 727 CE2 PHE A 88 26.086 -32.854 -40.548 1.00 52.22 C ANISOU 727 CE2 PHE A 88 5592 4662 9587 7 193 676 C ATOM 728 CZ PHE A 88 27.151 -32.921 -41.428 1.00 63.11 C ANISOU 728 CZ PHE A 88 6822 5995 11162 -14 267 708 C ATOM 729 N GLY A 89 24.667 -38.682 -37.658 1.00 63.71 N ANISOU 729 N GLY A 89 7403 6232 10574 173 40 728 N ATOM 730 CA GLY A 89 24.551 -39.834 -36.787 1.00 59.11 C ANISOU 730 CA GLY A 89 6915 5635 9910 215 -13 756 C ATOM 731 C GLY A 89 24.229 -41.083 -37.581 1.00 57.16 C ANISOU 731 C GLY A 89 6654 5397 9668 205 114 787 C ATOM 732 O GLY A 89 24.786 -42.148 -37.330 1.00 62.95 O ANISOU 732 O GLY A 89 7389 6083 10445 240 76 811 O ATOM 733 N GLY A 90 23.338 -40.940 -38.556 1.00 44.90 N ANISOU 733 N GLY A 90 5089 3897 8072 164 255 779 N ATOM 734 CA GLY A 90 22.868 -42.066 -39.335 1.00 43.78 C ANISOU 734 CA GLY A 90 4946 3763 7923 152 369 790 C ATOM 735 C GLY A 90 23.364 -42.133 -40.768 1.00 54.36 C ANISOU 735 C GLY A 90 6175 5105 9376 144 461 774 C ATOM 736 O GLY A 90 24.005 -43.111 -41.156 1.00 58.89 O ANISOU 736 O GLY A 90 6707 5635 10033 167 479 781 O ATOM 737 N PHE A 91 23.075 -41.099 -41.553 1.00 45.02 N ANISOU 737 N PHE A 91 4952 3967 8187 122 525 754 N ATOM 738 CA PHE A 91 23.248 -41.176 -43.002 1.00 40.10 C ANISOU 738 CA PHE A 91 4258 3359 7620 123 642 742 C ATOM 739 C PHE A 91 24.709 -41.375 -43.408 1.00 44.92 C ANISOU 739 C PHE A 91 4757 3911 8399 151 640 755 C ATOM 740 O PHE A 91 25.008 -42.210 -44.259 1.00 44.67 O ANISOU 740 O PHE A 91 4693 3868 8413 175 719 750 O ATOM 741 CB PHE A 91 22.690 -39.923 -43.689 1.00 45.79 C ANISOU 741 CB PHE A 91 4973 4133 8292 107 705 730 C ATOM 742 CG PHE A 91 21.210 -39.709 -43.483 1.00 48.26 C ANISOU 742 CG PHE A 91 5373 4512 8450 88 722 712 C ATOM 743 CD1 PHE A 91 20.397 -40.728 -43.009 1.00 47.56 C ANISOU 743 CD1 PHE A 91 5349 4435 8286 77 719 707 C ATOM 744 CD2 PHE A 91 20.631 -38.482 -43.776 1.00 43.60 C ANISOU 744 CD2 PHE A 91 4795 3966 7804 83 747 703 C ATOM 745 CE1 PHE A 91 19.034 -40.524 -42.822 1.00 50.63 C ANISOU 745 CE1 PHE A 91 5795 4885 8556 57 746 691 C ATOM 746 CE2 PHE A 91 19.267 -38.271 -43.593 1.00 48.01 C ANISOU 746 CE2 PHE A 91 5418 4589 8233 75 764 684 C ATOM 747 CZ PHE A 91 18.468 -39.294 -43.115 1.00 40.77 C ANISOU 747 CZ PHE A 91 4549 3690 7253 60 765 677 C ATOM 748 N THR A 92 25.610 -40.605 -42.803 1.00 43.11 N ANISOU 748 N THR A 92 4465 3643 8271 151 549 764 N ATOM 749 CA THR A 92 27.027 -40.668 -43.144 1.00 47.56 C ANISOU 749 CA THR A 92 4894 4150 9024 173 546 776 C ATOM 750 C THR A 92 27.638 -42.001 -42.719 1.00 47.07 C ANISOU 750 C THR A 92 4823 4041 9020 217 489 783 C ATOM 751 O THR A 92 28.437 -42.581 -43.448 1.00 47.78 O ANISOU 751 O THR A 92 4824 4103 9227 250 555 788 O ATOM 752 CB THR A 92 27.827 -39.522 -42.494 1.00 50.82 C ANISOU 752 CB THR A 92 5232 4523 9554 153 438 774 C ATOM 753 OG1 THR A 92 27.597 -39.517 -41.079 1.00 61.86 O ANISOU 753 OG1 THR A 92 6715 5909 10878 159 275 760 O ATOM 754 CG2 THR A 92 27.420 -38.180 -43.079 1.00 43.72 C ANISOU 754 CG2 THR A 92 4328 3648 8636 114 512 774 C ATOM 755 N THR A 93 27.263 -42.468 -41.531 1.00 45.32 N ANISOU 755 N THR A 93 4700 3809 8712 227 374 787 N ATOM 756 CA THR A 93 27.708 -43.764 -41.030 1.00 50.90 C ANISOU 756 CA THR A 93 5427 4463 9448 276 315 802 C ATOM 757 C THR A 93 27.227 -44.913 -41.919 1.00 44.04 C ANISOU 757 C THR A 93 4593 3596 8543 285 442 800 C ATOM 758 O THR A 93 27.963 -45.863 -42.168 1.00 51.28 O ANISOU 758 O THR A 93 5466 4463 9556 333 450 806 O ATOM 759 CB THR A 93 27.205 -44.009 -39.599 1.00 51.95 C ANISOU 759 CB THR A 93 5695 4586 9457 288 188 819 C ATOM 760 OG1 THR A 93 25.776 -43.937 -39.589 1.00 85.74 O ANISOU 760 OG1 THR A 93 10091 8921 13566 247 264 819 O ATOM 761 CG2 THR A 93 27.751 -42.964 -38.652 1.00 48.00 C ANISOU 761 CG2 THR A 93 5175 4075 8987 294 35 806 C ATOM 762 N THR A 94 25.985 -44.823 -42.386 1.00 39.26 N ANISOU 762 N THR A 94 4065 3046 7805 244 533 785 N ATOM 763 CA THR A 94 25.401 -45.860 -43.235 1.00 41.75 C ANISOU 763 CA THR A 94 4421 3362 8082 245 638 766 C ATOM 764 C THR A 94 26.022 -45.831 -44.628 1.00 49.47 C ANISOU 764 C THR A 94 5305 4344 9146 273 749 743 C ATOM 765 O THR A 94 26.186 -46.873 -45.258 1.00 54.88 O ANISOU 765 O THR A 94 5995 4997 9862 307 807 725 O ATOM 766 CB THR A 94 23.870 -45.707 -43.348 1.00 44.33 C ANISOU 766 CB THR A 94 4839 3749 8256 192 690 747 C ATOM 767 OG1 THR A 94 23.285 -45.807 -42.041 1.00 48.44 O ANISOU 767 OG1 THR A 94 5450 4262 8692 173 612 777 O ATOM 768 CG2 THR A 94 23.277 -46.795 -44.246 1.00 37.89 C ANISOU 768 CG2 THR A 94 4056 2924 7418 189 779 712 C ATOM 769 N LEU A 95 26.365 -44.637 -45.102 1.00 41.61 N ANISOU 769 N LEU A 95 4237 3385 8189 263 785 746 N ATOM 770 CA LEU A 95 27.121 -44.495 -46.344 1.00 50.52 C ANISOU 770 CA LEU A 95 5273 4513 9409 299 903 742 C ATOM 771 C LEU A 95 28.416 -45.291 -46.237 1.00 54.95 C ANISOU 771 C LEU A 95 5744 5004 10131 356 882 754 C ATOM 772 O LEU A 95 28.800 -46.008 -47.158 1.00 46.24 O ANISOU 772 O LEU A 95 4616 3884 9070 407 981 739 O ATOM 773 CB LEU A 95 27.438 -43.023 -46.634 1.00 42.41 C ANISOU 773 CB LEU A 95 4175 3512 8426 275 935 762 C ATOM 774 CG LEU A 95 27.558 -42.492 -48.074 1.00 55.75 C ANISOU 774 CG LEU A 95 5830 5233 10118 297 1098 766 C ATOM 775 CD1 LEU A 95 28.208 -41.114 -48.078 1.00 56.02 C ANISOU 775 CD1 LEU A 95 5772 5255 10257 270 1113 804 C ATOM 776 CD2 LEU A 95 28.313 -43.414 -49.005 1.00 41.40 C ANISOU 776 CD2 LEU A 95 3965 3390 8375 364 1205 759 C ATOM 777 N TYR A 96 29.082 -45.161 -45.097 1.00 37.01 N ANISOU 777 N TYR A 96 3426 2690 7945 357 744 777 N ATOM 778 CA TYR A 96 30.384 -45.779 -44.908 1.00 43.30 C ANISOU 778 CA TYR A 96 4115 3421 8914 417 702 789 C ATOM 779 C TYR A 96 30.252 -47.293 -44.756 1.00 48.42 C ANISOU 779 C TYR A 96 4841 4023 9533 466 688 782 C ATOM 780 O TYR A 96 30.988 -48.055 -45.388 1.00 49.92 O ANISOU 780 O TYR A 96 4969 4174 9824 530 753 774 O ATOM 781 CB TYR A 96 31.078 -45.164 -43.693 1.00 49.26 C ANISOU 781 CB TYR A 96 4807 4146 9762 409 530 805 C ATOM 782 CG TYR A 96 32.499 -45.628 -43.476 1.00 48.11 C ANISOU 782 CG TYR A 96 4519 3937 9822 474 466 813 C ATOM 783 CD1 TYR A 96 33.550 -45.083 -44.205 1.00 52.06 C ANISOU 783 CD1 TYR A 96 4838 4426 10515 483 544 818 C ATOM 784 CD2 TYR A 96 32.791 -46.593 -42.527 1.00 48.27 C ANISOU 784 CD2 TYR A 96 4583 3907 9852 530 329 821 C ATOM 785 CE1 TYR A 96 34.853 -45.504 -43.999 1.00 55.19 C ANISOU 785 CE1 TYR A 96 5082 4767 11121 544 484 823 C ATOM 786 CE2 TYR A 96 34.082 -47.015 -42.312 1.00 49.55 C ANISOU 786 CE2 TYR A 96 4609 4013 10207 600 255 825 C ATOM 787 CZ TYR A 96 35.111 -46.471 -43.049 1.00 56.31 C ANISOU 787 CZ TYR A 96 5267 4863 11265 606 330 822 C ATOM 788 OH TYR A 96 36.399 -46.901 -42.828 1.00 68.42 O ANISOU 788 OH TYR A 96 6644 6343 13011 679 256 823 O ATOM 789 N THR A 97 29.303 -47.729 -43.936 1.00 44.53 N ANISOU 789 N THR A 97 4487 3528 8905 439 615 786 N ATOM 790 CA THR A 97 29.141 -49.156 -43.682 1.00 49.29 C ANISOU 790 CA THR A 97 5174 4067 9486 478 598 789 C ATOM 791 C THR A 97 28.599 -49.903 -44.902 1.00 43.47 C ANISOU 791 C THR A 97 4478 3331 8706 483 740 747 C ATOM 792 O THR A 97 29.036 -51.016 -45.191 1.00 45.23 O ANISOU 792 O THR A 97 4705 3488 8992 542 764 736 O ATOM 793 CB THR A 97 28.218 -49.409 -42.490 1.00 46.30 C ANISOU 793 CB THR A 97 4937 3679 8975 443 507 816 C ATOM 794 OG1 THR A 97 26.935 -48.833 -42.753 1.00 43.34 O ANISOU 794 OG1 THR A 97 4631 3375 8461 368 571 798 O ATOM 795 CG2 THR A 97 28.806 -48.794 -41.227 1.00 40.76 C ANISOU 795 CG2 THR A 97 4219 2969 8298 460 348 849 C ATOM 796 N SER A 98 27.662 -49.291 -45.621 1.00 44.59 N ANISOU 796 N SER A 98 4655 3545 8742 430 825 717 N ATOM 797 CA SER A 98 27.110 -49.915 -46.825 1.00 48.01 C ANISOU 797 CA SER A 98 5134 3986 9123 440 941 662 C ATOM 798 C SER A 98 28.187 -50.174 -47.877 1.00 40.46 C ANISOU 798 C SER A 98 4090 3009 8275 522 1037 644 C ATOM 799 O SER A 98 28.119 -51.159 -48.610 1.00 48.26 O ANISOU 799 O SER A 98 5120 3959 9256 566 1101 598 O ATOM 800 CB SER A 98 25.994 -49.053 -47.427 1.00 45.70 C ANISOU 800 CB SER A 98 4882 3783 8699 383 998 633 C ATOM 801 OG SER A 98 26.483 -47.775 -47.801 1.00 49.06 O ANISOU 801 OG SER A 98 5224 4263 9153 385 1036 653 O ATOM 802 N LEU A 99 29.182 -49.293 -47.947 1.00 48.05 N ANISOU 802 N LEU A 99 4926 3988 9342 543 1052 676 N ATOM 803 CA LEU A 99 30.287 -49.465 -48.887 1.00 47.95 C ANISOU 803 CA LEU A 99 4811 3957 9451 623 1162 671 C ATOM 804 C LEU A 99 31.214 -50.612 -48.463 1.00 49.19 C ANISOU 804 C LEU A 99 4926 4025 9739 698 1112 676 C ATOM 805 O LEU A 99 32.045 -51.080 -49.249 1.00 50.79 O ANISOU 805 O LEU A 99 5061 4200 10037 781 1210 662 O ATOM 806 CB LEU A 99 31.070 -48.157 -49.027 1.00 50.79 C ANISOU 806 CB LEU A 99 5034 4352 9913 611 1200 713 C ATOM 807 CG LEU A 99 30.330 -47.046 -49.782 1.00 49.53 C ANISOU 807 CG LEU A 99 4911 4271 9636 566 1292 711 C ATOM 808 CD1 LEU A 99 31.138 -45.770 -49.850 1.00 44.73 C ANISOU 808 CD1 LEU A 99 4170 3675 9151 546 1330 761 C ATOM 809 CD2 LEU A 99 29.963 -47.504 -51.178 1.00 45.23 C ANISOU 809 CD2 LEU A 99 4439 3753 8994 621 1443 667 C ATOM 810 N HIS A 100 31.058 -51.068 -47.222 1.00 53.28 N ANISOU 810 N HIS A 100 5494 4497 10255 679 964 700 N ATOM 811 CA HIS A 100 31.775 -52.241 -46.729 1.00 50.45 C ANISOU 811 CA HIS A 100 5128 4046 9997 756 899 710 C ATOM 812 C HIS A 100 30.923 -53.501 -46.859 1.00 46.84 C ANISOU 812 C HIS A 100 4823 3531 9444 760 915 676 C ATOM 813 O HIS A 100 31.442 -54.613 -46.911 1.00 55.75 O ANISOU 813 O HIS A 100 5963 4574 10647 837 914 667 O ATOM 814 CB HIS A 100 32.178 -52.063 -45.266 1.00 50.76 C ANISOU 814 CB HIS A 100 5146 4055 10085 752 720 761 C ATOM 815 CG HIS A 100 33.304 -51.103 -45.057 1.00 58.78 C ANISOU 815 CG HIS A 100 5986 5092 11256 767 674 783 C ATOM 816 ND1 HIS A 100 33.133 -49.737 -45.084 1.00 50.75 N ANISOU 816 ND1 HIS A 100 4917 4145 10223 694 680 789 N ATOM 817 CD2 HIS A 100 34.617 -51.314 -44.803 1.00 55.27 C ANISOU 817 CD2 HIS A 100 5397 4600 11002 846 614 796 C ATOM 818 CE1 HIS A 100 34.294 -49.147 -44.861 1.00 48.59 C ANISOU 818 CE1 HIS A 100 4473 3859 10130 717 628 804 C ATOM 819 NE2 HIS A 100 35.211 -50.081 -44.688 1.00 54.26 N ANISOU 819 NE2 HIS A 100 5125 4513 10980 809 585 807 N ATOM 820 N GLY A 101 29.607 -53.317 -46.877 1.00 44.71 N ANISOU 820 N GLY A 101 4666 3301 9021 674 925 657 N ATOM 821 CA GLY A 101 28.690 -54.436 -46.970 1.00 44.11 C ANISOU 821 CA GLY A 101 4724 3165 8870 655 936 623 C ATOM 822 C GLY A 101 28.282 -54.983 -45.615 1.00 50.14 C ANISOU 822 C GLY A 101 5578 3864 9607 623 822 678 C ATOM 823 O GLY A 101 27.623 -56.017 -45.540 1.00 46.86 O ANISOU 823 O GLY A 101 5270 3374 9160 605 829 664 O ATOM 824 N TYR A 102 28.679 -54.294 -44.546 1.00 42.09 N ANISOU 824 N TYR A 102 4523 2868 8601 618 719 740 N ATOM 825 CA TYR A 102 28.282 -54.683 -43.192 1.00 42.39 C ANISOU 825 CA TYR A 102 4666 2856 8585 599 614 803 C ATOM 826 C TYR A 102 28.630 -53.586 -42.195 1.00 48.61 C ANISOU 826 C TYR A 102 5412 3700 9358 591 503 849 C ATOM 827 O TYR A 102 29.303 -52.613 -42.542 1.00 47.85 O ANISOU 827 O TYR A 102 5191 3663 9327 600 501 833 O ATOM 828 CB TYR A 102 28.941 -56.003 -42.774 1.00 45.63 C ANISOU 828 CB TYR A 102 5119 3140 9079 685 566 832 C ATOM 829 CG TYR A 102 30.438 -55.927 -42.547 1.00 46.16 C ANISOU 829 CG TYR A 102 5066 3185 9290 790 488 852 C ATOM 830 CD1 TYR A 102 31.325 -55.928 -43.618 1.00 44.40 C ANISOU 830 CD1 TYR A 102 4711 2969 9189 852 566 804 C ATOM 831 CD2 TYR A 102 30.964 -55.872 -41.260 1.00 49.38 C ANISOU 831 CD2 TYR A 102 5490 3563 9711 836 336 916 C ATOM 832 CE1 TYR A 102 32.700 -55.870 -43.411 1.00 49.89 C ANISOU 832 CE1 TYR A 102 5272 3642 10041 947 500 821 C ATOM 833 CE2 TYR A 102 32.331 -55.818 -41.044 1.00 46.60 C ANISOU 833 CE2 TYR A 102 5011 3190 9507 935 246 925 C ATOM 834 CZ TYR A 102 33.192 -55.815 -42.122 1.00 50.29 C ANISOU 834 CZ TYR A 102 5326 3664 10118 985 331 878 C ATOM 835 OH TYR A 102 34.549 -55.756 -41.909 1.00 56.87 O ANISOU 835 OH TYR A 102 6009 4477 11122 1080 247 886 O ATOM 836 N PHE A 103 28.169 -53.742 -40.958 1.00 46.39 N ANISOU 836 N PHE A 103 5243 3392 8991 577 415 906 N ATOM 837 CA PHE A 103 28.375 -52.714 -39.945 1.00 46.67 C ANISOU 837 CA PHE A 103 5270 3478 8985 574 298 939 C ATOM 838 C PHE A 103 29.756 -52.840 -39.314 1.00 47.99 C ANISOU 838 C PHE A 103 5367 3596 9271 674 159 963 C ATOM 839 O PHE A 103 29.934 -53.525 -38.307 1.00 51.83 O ANISOU 839 O PHE A 103 5950 4015 9730 733 58 1016 O ATOM 840 CB PHE A 103 27.285 -52.778 -38.869 1.00 44.59 C ANISOU 840 CB PHE A 103 5167 3215 8561 530 270 989 C ATOM 841 CG PHE A 103 27.140 -51.500 -38.097 1.00 48.41 C ANISOU 841 CG PHE A 103 5655 3776 8964 508 188 997 C ATOM 842 CD1 PHE A 103 26.388 -50.454 -38.605 1.00 45.06 C ANISOU 842 CD1 PHE A 103 5198 3444 8479 429 259 958 C ATOM 843 CD2 PHE A 103 27.784 -51.329 -36.883 1.00 46.53 C ANISOU 843 CD2 PHE A 103 5457 3513 8708 575 30 1036 C ATOM 844 CE1 PHE A 103 26.264 -49.266 -37.908 1.00 45.78 C ANISOU 844 CE1 PHE A 103 5299 3596 8500 414 184 959 C ATOM 845 CE2 PHE A 103 27.667 -50.146 -36.182 1.00 51.00 C ANISOU 845 CE2 PHE A 103 6036 4142 9198 560 -55 1030 C ATOM 846 CZ PHE A 103 26.905 -49.111 -36.694 1.00 47.55 C ANISOU 846 CZ PHE A 103 5567 3792 8708 477 27 991 C ATOM 847 N VAL A 104 30.728 -52.158 -39.911 1.00 58.77 N ANISOU 847 N VAL A 104 6562 4995 10773 696 155 927 N ATOM 848 CA VAL A 104 32.132 -52.297 -39.529 1.00 52.18 C ANISOU 848 CA VAL A 104 5615 4114 10098 792 33 936 C ATOM 849 C VAL A 104 32.483 -51.726 -38.158 1.00 50.61 C ANISOU 849 C VAL A 104 5441 3918 9870 820 -167 963 C ATOM 850 O VAL A 104 33.568 -51.979 -37.641 1.00 57.13 O ANISOU 850 O VAL A 104 6197 4697 10813 911 -304 971 O ATOM 851 CB VAL A 104 33.047 -51.618 -40.560 1.00 61.65 C ANISOU 851 CB VAL A 104 6605 5350 11468 795 101 893 C ATOM 852 CG1 VAL A 104 33.040 -52.393 -41.856 1.00 59.86 C ANISOU 852 CG1 VAL A 104 6354 5104 11288 816 275 865 C ATOM 853 CG2 VAL A 104 32.606 -50.175 -40.788 1.00 57.71 C ANISOU 853 CG2 VAL A 104 6064 4940 10924 702 135 872 C ATOM 854 N PHE A 105 31.576 -50.957 -37.568 1.00 52.55 N ANISOU 854 N PHE A 105 5789 4218 9958 753 -190 970 N ATOM 855 CA PHE A 105 31.885 -50.266 -36.321 1.00 50.61 C ANISOU 855 CA PHE A 105 5577 3982 9670 783 -380 979 C ATOM 856 C PHE A 105 31.616 -51.137 -35.098 1.00 52.61 C ANISOU 856 C PHE A 105 6022 4176 9789 854 -484 1042 C ATOM 857 O PHE A 105 31.860 -50.723 -33.964 1.00 54.91 O ANISOU 857 O PHE A 105 6378 4469 10016 903 -655 1052 O ATOM 858 CB PHE A 105 31.093 -48.960 -36.240 1.00 55.10 C ANISOU 858 CB PHE A 105 6170 4633 10132 691 -357 953 C ATOM 859 CG PHE A 105 31.479 -47.959 -37.294 1.00 51.43 C ANISOU 859 CG PHE A 105 5524 4216 9801 632 -279 903 C ATOM 860 CD1 PHE A 105 32.808 -47.596 -37.463 1.00 55.40 C ANISOU 860 CD1 PHE A 105 5839 4695 10514 668 -360 876 C ATOM 861 CD2 PHE A 105 30.525 -47.409 -38.133 1.00 48.99 C ANISOU 861 CD2 PHE A 105 5228 3969 9416 545 -119 886 C ATOM 862 CE1 PHE A 105 33.172 -46.684 -38.436 1.00 60.24 C ANISOU 862 CE1 PHE A 105 6290 5342 11258 612 -265 844 C ATOM 863 CE2 PHE A 105 30.882 -46.498 -39.107 1.00 56.23 C ANISOU 863 CE2 PHE A 105 5998 4922 10445 500 -37 852 C ATOM 864 CZ PHE A 105 32.206 -46.132 -39.256 1.00 61.09 C ANISOU 864 CZ PHE A 105 6434 5508 11268 531 -101 837 C ATOM 865 N GLY A 106 31.120 -52.347 -35.329 1.00 61.74 N ANISOU 865 N GLY A 106 7278 5275 10903 865 -380 1083 N ATOM 866 CA GLY A 106 30.876 -53.281 -34.246 1.00 59.43 C ANISOU 866 CA GLY A 106 7176 4910 10495 935 -451 1159 C ATOM 867 C GLY A 106 29.692 -52.899 -33.376 1.00 56.87 C ANISOU 867 C GLY A 106 7034 4622 9950 888 -435 1200 C ATOM 868 O GLY A 106 29.030 -51.889 -33.628 1.00 61.63 O ANISOU 868 O GLY A 106 7611 5312 10495 799 -375 1162 O ATOM 869 N PRO A 107 29.421 -53.712 -32.341 1.00 57.77 N ANISOU 869 N PRO A 107 7340 4669 9941 954 -480 1283 N ATOM 870 CA PRO A 107 28.302 -53.523 -31.408 1.00 49.81 C ANISOU 870 CA PRO A 107 6528 3684 8715 928 -445 1341 C ATOM 871 C PRO A 107 28.306 -52.166 -30.703 1.00 57.20 C ANISOU 871 C PRO A 107 7473 4708 9552 932 -563 1303 C ATOM 872 O PRO A 107 27.240 -51.573 -30.532 1.00 62.13 O ANISOU 872 O PRO A 107 8170 5393 10041 861 -472 1306 O ATOM 873 CB PRO A 107 28.487 -54.665 -30.394 1.00 60.43 C ANISOU 873 CB PRO A 107 8058 4922 9982 1041 -512 1443 C ATOM 874 CG PRO A 107 29.855 -55.232 -30.651 1.00 56.03 C ANISOU 874 CG PRO A 107 7389 4299 9600 1142 -636 1424 C ATOM 875 CD PRO A 107 30.145 -54.970 -32.088 1.00 52.06 C ANISOU 875 CD PRO A 107 6662 3832 9285 1064 -541 1336 C ATOM 876 N THR A 108 29.477 -51.675 -30.311 1.00 57.01 N ANISOU 876 N THR A 108 7371 4686 9605 1014 -766 1262 N ATOM 877 CA THR A 108 29.574 -50.372 -29.655 1.00 60.63 C ANISOU 877 CA THR A 108 7834 5213 9989 1020 -901 1210 C ATOM 878 C THR A 108 29.108 -49.256 -30.581 1.00 55.96 C ANISOU 878 C THR A 108 7105 4706 9452 894 -789 1136 C ATOM 879 O THR A 108 28.304 -48.410 -30.192 1.00 54.41 O ANISOU 879 O THR A 108 6989 4570 9114 853 -765 1123 O ATOM 880 CB THR A 108 31.010 -50.079 -29.188 1.00 61.89 C ANISOU 880 CB THR A 108 7897 5348 10269 1124 -1153 1163 C ATOM 881 OG1 THR A 108 31.350 -50.968 -28.117 1.00 69.61 O ANISOU 881 OG1 THR A 108 9044 6257 11148 1262 -1287 1233 O ATOM 882 CG2 THR A 108 31.132 -48.640 -28.699 1.00 61.43 C ANISOU 882 CG2 THR A 108 7813 5353 10173 1108 -1290 1085 C ATOM 883 N GLY A 109 29.608 -49.267 -31.812 1.00 55.23 N ANISOU 883 N GLY A 109 6813 4614 9557 843 -715 1093 N ATOM 884 CA GLY A 109 29.184 -48.313 -32.818 1.00 45.14 C ANISOU 884 CA GLY A 109 5412 3408 8331 732 -592 1035 C ATOM 885 C GLY A 109 27.706 -48.452 -33.129 1.00 54.76 C ANISOU 885 C GLY A 109 6734 4665 9406 650 -401 1062 C ATOM 886 O GLY A 109 27.037 -47.473 -33.456 1.00 56.01 O ANISOU 886 O GLY A 109 6870 4895 9518 577 -334 1025 O ATOM 887 N CYS A 110 27.199 -49.676 -33.021 1.00 49.42 N ANISOU 887 N CYS A 110 6168 3936 8673 663 -317 1126 N ATOM 888 CA CYS A 110 25.791 -49.952 -33.280 1.00 44.28 C ANISOU 888 CA CYS A 110 5603 3309 7911 581 -139 1152 C ATOM 889 C CYS A 110 24.901 -49.213 -32.287 1.00 49.20 C ANISOU 889 C CYS A 110 6364 3988 8344 573 -149 1173 C ATOM 890 O CYS A 110 23.865 -48.656 -32.661 1.00 44.52 O ANISOU 890 O CYS A 110 5766 3461 7689 493 -30 1152 O ATOM 891 CB CYS A 110 25.523 -51.458 -33.217 1.00 50.17 C ANISOU 891 CB CYS A 110 6445 3964 8654 600 -65 1221 C ATOM 892 SG CYS A 110 23.889 -51.966 -33.811 1.00 56.03 S ANISOU 892 SG CYS A 110 7238 4715 9334 482 159 1236 S ATOM 893 N ASN A 111 25.310 -49.215 -31.022 1.00 47.56 N ANISOU 893 N ASN A 111 6283 3752 8036 668 -293 1211 N ATOM 894 CA ASN A 111 24.593 -48.466 -29.997 1.00 53.22 C ANISOU 894 CA ASN A 111 7144 4519 8558 685 -315 1225 C ATOM 895 C ASN A 111 24.719 -46.964 -30.207 1.00 53.68 C ANISOU 895 C ASN A 111 7106 4655 8636 652 -379 1135 C ATOM 896 O ASN A 111 23.744 -46.231 -30.074 1.00 54.37 O ANISOU 896 O ASN A 111 7244 4806 8608 609 -299 1122 O ATOM 897 CB ASN A 111 25.094 -48.840 -28.605 1.00 49.52 C ANISOU 897 CB ASN A 111 6851 3999 7966 815 -471 1283 C ATOM 898 CG ASN A 111 24.590 -50.190 -28.156 1.00 61.02 C ANISOU 898 CG ASN A 111 8465 5381 9340 845 -371 1396 C ATOM 899 OD1 ASN A 111 23.405 -50.357 -27.864 1.00 62.06 O ANISOU 899 OD1 ASN A 111 8711 5528 9342 803 -215 1453 O ATOM 900 ND2 ASN A 111 25.487 -51.163 -28.092 1.00 72.36 N ANISOU 900 ND2 ASN A 111 9903 6728 10861 920 -455 1433 N ATOM 901 N LEU A 112 25.927 -46.519 -30.540 1.00 57.22 N ANISOU 901 N LEU A 112 7411 5089 9242 673 -517 1074 N ATOM 902 CA LEU A 112 26.185 -45.111 -30.827 1.00 53.46 C ANISOU 902 CA LEU A 112 6825 4664 8825 635 -577 990 C ATOM 903 C LEU A 112 25.351 -44.612 -31.997 1.00 56.19 C ANISOU 903 C LEU A 112 7076 5069 9204 525 -392 963 C ATOM 904 O LEU A 112 24.616 -43.628 -31.882 1.00 60.59 O ANISOU 904 O LEU A 112 7669 5684 9670 491 -358 934 O ATOM 905 CB LEU A 112 27.670 -44.895 -31.124 1.00 56.74 C ANISOU 905 CB LEU A 112 7071 5038 9450 664 -730 940 C ATOM 906 CG LEU A 112 28.572 -44.641 -29.920 1.00 64.23 C ANISOU 906 CG LEU A 112 8077 5951 10377 767 -982 916 C ATOM 907 CD1 LEU A 112 30.038 -44.809 -30.291 1.00 61.80 C ANISOU 907 CD1 LEU A 112 7578 5591 10311 799 -1112 882 C ATOM 908 CD2 LEU A 112 28.310 -43.241 -29.391 1.00 65.25 C ANISOU 908 CD2 LEU A 112 8247 6121 10425 752 -1068 849 C ATOM 909 N GLU A 113 25.478 -45.299 -33.127 1.00 57.54 N ANISOU 909 N GLU A 113 7135 5225 9503 482 -279 970 N ATOM 910 CA GLU A 113 24.761 -44.924 -34.335 1.00 50.10 C ANISOU 910 CA GLU A 113 6106 4337 8594 393 -115 941 C ATOM 911 C GLU A 113 23.255 -45.043 -34.111 1.00 60.45 C ANISOU 911 C GLU A 113 7537 5693 9739 353 12 969 C ATOM 912 O GLU A 113 22.482 -44.192 -34.544 1.00 56.58 O ANISOU 912 O GLU A 113 7022 5268 9207 301 88 937 O ATOM 913 CB GLU A 113 25.210 -45.799 -35.505 1.00 45.28 C ANISOU 913 CB GLU A 113 5381 3693 8131 376 -28 941 C ATOM 914 CG GLU A 113 24.868 -45.251 -36.872 1.00 65.03 C ANISOU 914 CG GLU A 113 7769 6247 10693 307 103 897 C ATOM 915 CD GLU A 113 23.835 -46.086 -37.597 1.00 80.84 C ANISOU 915 CD GLU A 113 9805 8262 12648 262 256 905 C ATOM 916 OE1 GLU A 113 24.025 -46.356 -38.804 1.00 93.53 O ANISOU 916 OE1 GLU A 113 11322 9871 14347 245 342 877 O ATOM 917 OE2 GLU A 113 22.836 -46.473 -36.958 1.00 71.38 O ANISOU 917 OE2 GLU A 113 8726 7070 11326 247 292 938 O ATOM 918 N GLY A 114 22.847 -46.096 -33.411 1.00 64.38 N ANISOU 918 N GLY A 114 8162 6151 10150 381 37 1035 N ATOM 919 CA GLY A 114 21.444 -46.314 -33.116 1.00 55.08 C ANISOU 919 CA GLY A 114 7089 5004 8835 342 168 1072 C ATOM 920 C GLY A 114 20.865 -45.234 -32.223 1.00 57.41 C ANISOU 920 C GLY A 114 7476 5359 8978 362 137 1063 C ATOM 921 O GLY A 114 19.753 -44.758 -32.457 1.00 47.90 O ANISOU 921 O GLY A 114 6273 4218 7709 311 251 1051 O ATOM 922 N PHE A 115 21.617 -44.841 -31.200 1.00 52.80 N ANISOU 922 N PHE A 115 6971 4754 8338 445 -24 1063 N ATOM 923 CA PHE A 115 21.148 -43.830 -30.261 1.00 55.51 C ANISOU 923 CA PHE A 115 7424 5144 8523 483 -70 1046 C ATOM 924 C PHE A 115 20.954 -42.467 -30.931 1.00 53.35 C ANISOU 924 C PHE A 115 7044 4932 8294 432 -61 964 C ATOM 925 O PHE A 115 19.903 -41.846 -30.780 1.00 51.50 O ANISOU 925 O PHE A 115 6860 4758 7950 414 27 956 O ATOM 926 CB PHE A 115 22.115 -43.699 -29.081 1.00 50.78 C ANISOU 926 CB PHE A 115 6931 4501 7862 592 -276 1045 C ATOM 927 CG PHE A 115 21.786 -42.562 -28.149 1.00 61.47 C ANISOU 927 CG PHE A 115 8402 5897 9058 642 -350 1005 C ATOM 928 CD1 PHE A 115 20.797 -42.701 -27.189 1.00 65.98 C ANISOU 928 CD1 PHE A 115 9161 6493 9414 689 -269 1061 C ATOM 929 CD2 PHE A 115 22.466 -41.356 -28.234 1.00 59.60 C ANISOU 929 CD2 PHE A 115 8086 5666 8892 644 -494 912 C ATOM 930 CE1 PHE A 115 20.492 -41.657 -26.331 1.00 62.96 C ANISOU 930 CE1 PHE A 115 8898 6148 8875 748 -333 1017 C ATOM 931 CE2 PHE A 115 22.166 -40.310 -27.380 1.00 61.77 C ANISOU 931 CE2 PHE A 115 8477 5968 9023 695 -571 864 C ATOM 932 CZ PHE A 115 21.179 -40.461 -26.427 1.00 58.42 C ANISOU 932 CZ PHE A 115 8252 5576 8369 753 -492 913 C ATOM 933 N PHE A 116 21.956 -42.003 -31.672 1.00 52.75 N ANISOU 933 N PHE A 116 6820 4838 8384 412 -143 910 N ATOM 934 CA PHE A 116 21.904 -40.652 -32.236 1.00 57.34 C ANISOU 934 CA PHE A 116 7314 5459 9014 371 -146 841 C ATOM 935 C PHE A 116 20.943 -40.530 -33.416 1.00 56.83 C ANISOU 935 C PHE A 116 7169 5452 8972 294 34 836 C ATOM 936 O PHE A 116 20.321 -39.481 -33.609 1.00 51.92 O ANISOU 936 O PHE A 116 6542 4879 8306 273 71 800 O ATOM 937 CB PHE A 116 23.305 -40.194 -32.648 1.00 48.51 C ANISOU 937 CB PHE A 116 6056 4293 8082 371 -276 795 C ATOM 938 CG PHE A 116 24.174 -39.814 -31.485 1.00 49.26 C ANISOU 938 CG PHE A 116 6214 4343 8160 444 -489 765 C ATOM 939 CD1 PHE A 116 23.916 -38.659 -30.762 1.00 56.73 C ANISOU 939 CD1 PHE A 116 7243 5304 9008 468 -574 713 C ATOM 940 CD2 PHE A 116 25.240 -40.612 -31.106 1.00 50.64 C ANISOU 940 CD2 PHE A 116 6371 4458 8413 499 -616 783 C ATOM 941 CE1 PHE A 116 24.708 -38.306 -29.686 1.00 61.30 C ANISOU 941 CE1 PHE A 116 7888 5838 9565 542 -790 671 C ATOM 942 CE2 PHE A 116 26.036 -40.265 -30.031 1.00 53.89 C ANISOU 942 CE2 PHE A 116 6840 4830 8807 576 -836 746 C ATOM 943 CZ PHE A 116 25.770 -39.109 -29.321 1.00 59.24 C ANISOU 943 CZ PHE A 116 7604 5523 9383 596 -928 686 C ATOM 944 N ALA A 117 20.816 -41.598 -34.198 1.00 47.37 N ANISOU 944 N ALA A 117 5915 4244 7839 258 135 867 N ATOM 945 CA ALA A 117 19.874 -41.615 -35.315 1.00 56.21 C ANISOU 945 CA ALA A 117 6969 5417 8973 194 288 854 C ATOM 946 C ALA A 117 18.432 -41.637 -34.810 1.00 60.79 C ANISOU 946 C ALA A 117 7643 6049 9404 182 386 875 C ATOM 947 O ALA A 117 17.545 -40.981 -35.374 1.00 50.91 O ANISOU 947 O ALA A 117 6355 4863 8127 149 468 845 O ATOM 948 CB ALA A 117 20.136 -42.808 -36.215 1.00 51.18 C ANISOU 948 CB ALA A 117 6261 4744 8439 168 354 870 C ATOM 949 N THR A 118 18.205 -42.399 -33.746 1.00 52.98 N ANISOU 949 N THR A 118 6775 5030 8323 215 383 932 N ATOM 950 CA THR A 118 16.886 -42.482 -33.133 1.00 57.93 C ANISOU 950 CA THR A 118 7495 5701 8816 209 491 965 C ATOM 951 C THR A 118 16.580 -41.184 -32.399 1.00 57.09 C ANISOU 951 C THR A 118 7457 5643 8591 254 447 935 C ATOM 952 O THR A 118 15.459 -40.673 -32.468 1.00 54.35 O ANISOU 952 O THR A 118 7111 5361 8178 236 547 922 O ATOM 953 CB THR A 118 16.778 -43.668 -32.153 1.00 48.72 C ANISOU 953 CB THR A 118 6455 4477 7579 239 516 1050 C ATOM 954 OG1 THR A 118 17.091 -44.889 -32.838 1.00 54.28 O ANISOU 954 OG1 THR A 118 7100 5120 8402 199 551 1074 O ATOM 955 CG2 THR A 118 15.376 -43.760 -31.581 1.00 41.59 C ANISOU 955 CG2 THR A 118 5630 3617 6556 225 659 1093 C ATOM 956 N LEU A 119 17.584 -40.655 -31.703 1.00 50.96 N ANISOU 956 N LEU A 119 6735 4831 7796 317 289 915 N ATOM 957 CA LEU A 119 17.448 -39.380 -31.007 1.00 57.32 C ANISOU 957 CA LEU A 119 7614 5666 8499 367 220 869 C ATOM 958 C LEU A 119 17.024 -38.282 -31.974 1.00 57.28 C ANISOU 958 C LEU A 119 7499 5712 8552 320 267 808 C ATOM 959 O LEU A 119 16.073 -37.547 -31.715 1.00 56.55 O ANISOU 959 O LEU A 119 7454 5673 8359 336 329 790 O ATOM 960 CB LEU A 119 18.758 -38.990 -30.323 1.00 52.84 C ANISOU 960 CB LEU A 119 7087 5040 7950 429 14 837 C ATOM 961 CG LEU A 119 18.698 -37.795 -29.370 1.00 55.17 C ANISOU 961 CG LEU A 119 7495 5345 8121 497 -89 783 C ATOM 962 CD1 LEU A 119 17.963 -38.166 -28.087 1.00 50.99 C ANISOU 962 CD1 LEU A 119 7166 4835 7372 576 -49 833 C ATOM 963 CD2 LEU A 119 20.095 -37.273 -29.067 1.00 53.88 C ANISOU 963 CD2 LEU A 119 7309 5118 8047 531 -310 724 C ATOM 964 N GLY A 120 17.727 -38.192 -33.099 1.00 54.63 N ANISOU 964 N GLY A 120 7023 5356 8378 272 248 782 N ATOM 965 CA GLY A 120 17.433 -37.196 -34.115 1.00 45.16 C ANISOU 965 CA GLY A 120 5726 4194 7238 235 294 735 C ATOM 966 C GLY A 120 16.025 -37.302 -34.665 1.00 51.30 C ANISOU 966 C GLY A 120 6485 5048 7961 205 450 742 C ATOM 967 O GLY A 120 15.337 -36.293 -34.833 1.00 50.49 O ANISOU 967 O GLY A 120 6380 4992 7813 213 483 709 O ATOM 968 N GLY A 121 15.593 -38.529 -34.944 1.00 43.85 N ANISOU 968 N GLY A 121 5521 4109 7031 170 538 782 N ATOM 969 CA GLY A 121 14.270 -38.765 -35.498 1.00 42.08 C ANISOU 969 CA GLY A 121 5256 3950 6782 133 674 781 C ATOM 970 C GLY A 121 13.158 -38.438 -34.524 1.00 46.66 C ANISOU 970 C GLY A 121 5925 4578 7226 164 736 796 C ATOM 971 O GLY A 121 12.081 -37.988 -34.922 1.00 56.76 O ANISOU 971 O GLY A 121 7159 5924 8481 153 821 772 O ATOM 972 N GLU A 122 13.426 -38.653 -33.239 1.00 46.46 N ANISOU 972 N GLU A 122 6028 4519 7105 214 694 834 N ATOM 973 CA GLU A 122 12.423 -38.439 -32.203 1.00 43.86 C ANISOU 973 CA GLU A 122 5803 4231 6629 257 770 859 C ATOM 974 C GLU A 122 12.307 -36.969 -31.808 1.00 47.41 C ANISOU 974 C GLU A 122 6304 4713 6996 319 716 803 C ATOM 975 O GLU A 122 11.218 -36.502 -31.490 1.00 47.63 O ANISOU 975 O GLU A 122 6359 4802 6938 345 810 799 O ATOM 976 CB GLU A 122 12.740 -39.296 -30.977 1.00 49.38 C ANISOU 976 CB GLU A 122 6647 4878 7237 301 755 930 C ATOM 977 CG GLU A 122 12.497 -40.789 -31.196 1.00 52.24 C ANISOU 977 CG GLU A 122 6982 5205 7663 242 851 999 C ATOM 978 CD GLU A 122 11.029 -41.119 -31.421 1.00 65.19 C ANISOU 978 CD GLU A 122 8567 6898 9304 189 1032 1021 C ATOM 979 OE1 GLU A 122 10.198 -40.742 -30.569 1.00 78.17 O ANISOU 979 OE1 GLU A 122 10291 8585 10826 233 1116 1045 O ATOM 980 OE2 GLU A 122 10.704 -41.752 -32.448 1.00 66.42 O ANISOU 980 OE2 GLU A 122 8597 7053 9587 108 1089 1008 O ATOM 981 N ILE A 123 13.424 -36.245 -31.829 1.00 38.82 N ANISOU 981 N ILE A 123 5223 3579 5948 343 566 759 N ATOM 982 CA ILE A 123 13.406 -34.805 -31.579 1.00 42.80 C ANISOU 982 CA ILE A 123 5767 4094 6402 392 501 695 C ATOM 983 C ILE A 123 12.617 -34.112 -32.678 1.00 47.21 C ANISOU 983 C ILE A 123 6213 4708 7015 360 586 662 C ATOM 984 O ILE A 123 11.805 -33.226 -32.409 1.00 48.10 O ANISOU 984 O ILE A 123 6365 4865 7047 405 627 632 O ATOM 985 CB ILE A 123 14.822 -34.200 -31.517 1.00 44.84 C ANISOU 985 CB ILE A 123 6025 4275 6737 404 320 651 C ATOM 986 CG1 ILE A 123 15.580 -34.723 -30.298 1.00 38.79 C ANISOU 986 CG1 ILE A 123 5387 3457 5896 461 203 670 C ATOM 987 CG2 ILE A 123 14.748 -32.673 -31.455 1.00 39.53 C ANISOU 987 CG2 ILE A 123 5377 3599 6045 439 262 579 C ATOM 988 CD1 ILE A 123 17.059 -34.373 -30.294 1.00 41.87 C ANISOU 988 CD1 ILE A 123 5742 3767 6401 463 13 626 C ATOM 989 N ALA A 124 12.852 -34.534 -33.918 1.00 43.27 N ANISOU 989 N ALA A 124 5584 4209 6648 293 612 666 N ATOM 990 CA ALA A 124 12.129 -33.992 -35.061 1.00 44.08 C ANISOU 990 CA ALA A 124 5585 4365 6796 270 685 638 C ATOM 991 C ALA A 124 10.636 -34.237 -34.909 1.00 55.07 C ANISOU 991 C ALA A 124 6972 5839 8115 277 816 648 C ATOM 992 O ALA A 124 9.827 -33.323 -35.072 1.00 58.09 O ANISOU 992 O ALA A 124 7342 6273 8458 312 853 616 O ATOM 993 CB ALA A 124 12.637 -34.603 -36.351 1.00 32.57 C ANISOU 993 CB ALA A 124 4011 2893 5469 209 695 644 C ATOM 994 N LEU A 125 10.288 -35.478 -34.582 1.00 46.07 N ANISOU 994 N LEU A 125 5835 4703 6968 244 886 696 N ATOM 995 CA LEU A 125 8.904 -35.893 -34.396 1.00 42.81 C ANISOU 995 CA LEU A 125 5395 4355 6515 235 1022 715 C ATOM 996 C LEU A 125 8.198 -35.064 -33.329 1.00 46.96 C ANISOU 996 C LEU A 125 6017 4920 6907 313 1063 711 C ATOM 997 O LEU A 125 7.103 -34.549 -33.553 1.00 40.16 O ANISOU 997 O LEU A 125 5101 4128 6030 332 1144 687 O ATOM 998 CB LEU A 125 8.850 -37.381 -34.033 1.00 45.28 C ANISOU 998 CB LEU A 125 5719 4634 6849 185 1085 779 C ATOM 999 CG LEU A 125 7.663 -37.923 -33.231 1.00 58.36 C ANISOU 999 CG LEU A 125 7404 6327 8446 184 1230 828 C ATOM 1000 CD1 LEU A 125 6.354 -37.718 -33.966 1.00 46.00 C ANISOU 1000 CD1 LEU A 125 5702 4841 6934 155 1329 792 C ATOM 1001 CD2 LEU A 125 7.867 -39.402 -32.922 1.00 64.40 C ANISOU 1001 CD2 LEU A 125 8194 7028 9249 130 1277 900 C ATOM 1002 N TRP A 126 8.823 -34.935 -32.166 1.00 42.19 N ANISOU 1002 N TRP A 126 5558 4270 6201 369 1002 730 N ATOM 1003 CA TRP A 126 8.201 -34.204 -31.075 1.00 46.12 C ANISOU 1003 CA TRP A 126 6173 4800 6550 458 1043 723 C ATOM 1004 C TRP A 126 8.264 -32.696 -31.306 1.00 58.55 C ANISOU 1004 C TRP A 126 7755 6382 8108 513 967 646 C ATOM 1005 O TRP A 126 7.513 -31.945 -30.686 1.00 50.69 O ANISOU 1005 O TRP A 126 6825 5427 7007 589 1019 624 O ATOM 1006 CB TRP A 126 8.845 -34.587 -29.739 1.00 38.83 C ANISOU 1006 CB TRP A 126 5426 3823 5503 515 991 764 C ATOM 1007 CG TRP A 126 8.370 -35.924 -29.271 1.00 59.87 C ANISOU 1007 CG TRP A 126 8114 6488 8144 486 1118 854 C ATOM 1008 CD1 TRP A 126 9.062 -37.101 -29.299 1.00 60.28 C ANISOU 1008 CD1 TRP A 126 8171 6478 8252 437 1090 910 C ATOM 1009 CD2 TRP A 126 7.074 -36.233 -28.743 1.00 58.86 C ANISOU 1009 CD2 TRP A 126 7999 6417 7948 501 1307 904 C ATOM 1010 NE1 TRP A 126 8.283 -38.119 -28.802 1.00 61.27 N ANISOU 1010 NE1 TRP A 126 8325 6609 8345 418 1247 995 N ATOM 1011 CE2 TRP A 126 7.057 -37.613 -28.457 1.00 59.58 C ANISOU 1011 CE2 TRP A 126 8110 6469 8061 452 1388 994 C ATOM 1012 CE3 TRP A 126 5.930 -35.474 -28.479 1.00 52.53 C ANISOU 1012 CE3 TRP A 126 7190 5691 7078 554 1423 882 C ATOM 1013 CZ2 TRP A 126 5.941 -38.249 -27.920 1.00 56.12 C ANISOU 1013 CZ2 TRP A 126 7679 6059 7586 444 1588 1069 C ATOM 1014 CZ3 TRP A 126 4.824 -36.106 -27.943 1.00 52.13 C ANISOU 1014 CZ3 TRP A 126 7138 5678 6990 552 1621 952 C ATOM 1015 CH2 TRP A 126 4.838 -37.482 -27.671 1.00 51.45 C ANISOU 1015 CH2 TRP A 126 7067 5547 6936 492 1705 1048 C ATOM 1016 N SER A 127 9.146 -32.257 -32.203 1.00 44.84 N ANISOU 1016 N SER A 127 5953 4603 6480 478 856 609 N ATOM 1017 CA SER A 127 9.174 -30.853 -32.600 1.00 44.85 C ANISOU 1017 CA SER A 127 5949 4600 6493 517 799 545 C ATOM 1018 C SER A 127 7.926 -30.540 -33.414 1.00 48.41 C ANISOU 1018 C SER A 127 6294 5134 6967 519 912 532 C ATOM 1019 O SER A 127 7.357 -29.458 -33.295 1.00 48.55 O ANISOU 1019 O SER A 127 6339 5174 6932 587 923 491 O ATOM 1020 CB SER A 127 10.438 -30.518 -33.408 1.00 34.86 C ANISOU 1020 CB SER A 127 4630 3260 5354 472 676 524 C ATOM 1021 OG SER A 127 11.592 -30.480 -32.583 1.00 40.33 O ANISOU 1021 OG SER A 127 5415 3873 6034 487 544 515 O ATOM 1022 N LEU A 128 7.505 -31.495 -34.239 1.00 44.93 N ANISOU 1022 N LEU A 128 5732 4733 6606 450 985 561 N ATOM 1023 CA LEU A 128 6.322 -31.312 -35.071 1.00 56.24 C ANISOU 1023 CA LEU A 128 7049 6247 8073 451 1072 541 C ATOM 1024 C LEU A 128 5.071 -31.273 -34.204 1.00 60.07 C ANISOU 1024 C LEU A 128 7555 6799 8471 503 1191 549 C ATOM 1025 O LEU A 128 4.096 -30.583 -34.522 1.00 49.93 O ANISOU 1025 O LEU A 128 6212 5578 7180 550 1242 516 O ATOM 1026 CB LEU A 128 6.207 -32.425 -36.115 1.00 50.57 C ANISOU 1026 CB LEU A 128 6204 5547 7464 364 1104 557 C ATOM 1027 CG LEU A 128 7.327 -32.523 -37.152 1.00 52.32 C ANISOU 1027 CG LEU A 128 6389 5714 7775 320 1015 551 C ATOM 1028 CD1 LEU A 128 6.907 -33.431 -38.296 1.00 44.23 C ANISOU 1028 CD1 LEU A 128 5243 4726 6837 260 1055 545 C ATOM 1029 CD2 LEU A 128 7.721 -31.149 -37.668 1.00 50.32 C ANISOU 1029 CD2 LEU A 128 6154 5441 7524 369 948 516 C ATOM 1030 N VAL A 129 5.113 -32.017 -33.106 1.00 52.40 N ANISOU 1030 N VAL A 129 6669 5812 7430 502 1241 597 N ATOM 1031 CA VAL A 129 4.018 -32.021 -32.150 1.00 51.72 C ANISOU 1031 CA VAL A 129 6620 5781 7249 557 1376 619 C ATOM 1032 C VAL A 129 3.962 -30.692 -31.401 1.00 55.86 C ANISOU 1032 C VAL A 129 7269 6305 7648 674 1344 574 C ATOM 1033 O VAL A 129 2.901 -30.076 -31.298 1.00 49.13 O ANISOU 1033 O VAL A 129 6386 5519 6763 738 1433 550 O ATOM 1034 CB VAL A 129 4.153 -33.177 -31.142 1.00 51.73 C ANISOU 1034 CB VAL A 129 6707 5753 7194 535 1445 696 C ATOM 1035 CG1 VAL A 129 3.058 -33.103 -30.096 1.00 45.32 C ANISOU 1035 CG1 VAL A 129 5951 4996 6272 604 1606 728 C ATOM 1036 CG2 VAL A 129 4.123 -34.519 -31.866 1.00 46.71 C ANISOU 1036 CG2 VAL A 129 5951 5106 6692 419 1485 738 C ATOM 1037 N VAL A 130 5.110 -30.255 -30.888 1.00 55.91 N ANISOU 1037 N VAL A 130 7411 6234 7597 705 1209 555 N ATOM 1038 CA VAL A 130 5.197 -29.018 -30.119 1.00 52.85 C ANISOU 1038 CA VAL A 130 7162 5825 7092 814 1153 499 C ATOM 1039 C VAL A 130 4.785 -27.825 -30.977 1.00 49.35 C ANISOU 1039 C VAL A 130 6645 5400 6705 846 1131 437 C ATOM 1040 O VAL A 130 4.070 -26.934 -30.527 1.00 44.87 O ANISOU 1040 O VAL A 130 6131 4862 6055 944 1176 399 O ATOM 1041 CB VAL A 130 6.625 -28.813 -29.562 1.00 56.21 C ANISOU 1041 CB VAL A 130 7723 6151 7483 824 979 478 C ATOM 1042 CG1 VAL A 130 6.876 -27.345 -29.182 1.00 38.60 C ANISOU 1042 CG1 VAL A 130 5601 3875 5191 914 876 394 C ATOM 1043 CG2 VAL A 130 6.852 -29.729 -28.370 1.00 39.10 C ANISOU 1043 CG2 VAL A 130 5689 3971 5197 848 1001 532 C ATOM 1044 N LEU A 131 5.220 -27.841 -32.228 1.00 43.17 N ANISOU 1044 N LEU A 131 5744 4599 6058 772 1070 432 N ATOM 1045 CA LEU A 131 4.868 -26.816 -33.189 1.00 38.53 C ANISOU 1045 CA LEU A 131 5086 4024 5529 800 1052 389 C ATOM 1046 C LEU A 131 3.353 -26.711 -33.363 1.00 51.76 C ANISOU 1046 C LEU A 131 6672 5805 7189 850 1185 383 C ATOM 1047 O LEU A 131 2.798 -25.610 -33.392 1.00 49.93 O ANISOU 1047 O LEU A 131 6460 5588 6925 939 1191 339 O ATOM 1048 CB LEU A 131 5.546 -27.111 -34.525 1.00 36.38 C ANISOU 1048 CB LEU A 131 4706 3725 5393 713 991 402 C ATOM 1049 CG LEU A 131 5.309 -26.119 -35.657 1.00 45.07 C ANISOU 1049 CG LEU A 131 5745 4828 6551 741 968 372 C ATOM 1050 CD1 LEU A 131 5.750 -24.713 -35.268 1.00 52.77 C ANISOU 1050 CD1 LEU A 131 6835 5724 7492 813 888 328 C ATOM 1051 CD2 LEU A 131 6.038 -26.598 -36.895 1.00 41.12 C ANISOU 1051 CD2 LEU A 131 5157 4303 6164 659 927 396 C ATOM 1052 N ALA A 132 2.690 -27.859 -33.473 1.00 57.63 N ANISOU 1052 N ALA A 132 7312 6614 7970 793 1290 425 N ATOM 1053 CA ALA A 132 1.235 -27.900 -33.581 1.00 50.19 C ANISOU 1053 CA ALA A 132 6258 5772 7040 828 1421 420 C ATOM 1054 C ALA A 132 0.586 -27.330 -32.328 1.00 51.04 C ANISOU 1054 C ALA A 132 6470 5906 7018 939 1511 412 C ATOM 1055 O ALA A 132 -0.369 -26.553 -32.412 1.00 52.01 O ANISOU 1055 O ALA A 132 6547 6086 7129 1024 1567 376 O ATOM 1056 CB ALA A 132 0.752 -29.323 -33.827 1.00 49.72 C ANISOU 1056 CB ALA A 132 6072 5757 7063 730 1511 467 C ATOM 1057 N ILE A 133 1.107 -27.717 -31.168 1.00 43.91 N ANISOU 1057 N ILE A 133 5714 4961 6009 948 1523 444 N ATOM 1058 CA ILE A 133 0.572 -27.234 -29.899 1.00 44.08 C ANISOU 1058 CA ILE A 133 5866 5002 5878 1065 1612 438 C ATOM 1059 C ILE A 133 0.712 -25.719 -29.774 1.00 57.25 C ANISOU 1059 C ILE A 133 7636 6637 7481 1178 1524 358 C ATOM 1060 O ILE A 133 -0.244 -25.032 -29.414 1.00 63.87 O ANISOU 1060 O ILE A 133 8481 7527 8259 1285 1617 328 O ATOM 1061 CB ILE A 133 1.266 -27.910 -28.705 1.00 49.77 C ANISOU 1061 CB ILE A 133 6759 5675 6478 1067 1613 486 C ATOM 1062 CG1 ILE A 133 0.958 -29.407 -28.697 1.00 50.92 C ANISOU 1062 CG1 ILE A 133 6817 5848 6683 968 1732 575 C ATOM 1063 CG2 ILE A 133 0.814 -27.284 -27.395 1.00 42.95 C ANISOU 1063 CG2 ILE A 133 6066 4826 5429 1210 1690 469 C ATOM 1064 CD1 ILE A 133 1.655 -30.159 -27.593 1.00 49.46 C ANISOU 1064 CD1 ILE A 133 6804 5609 6380 973 1731 636 C ATOM 1065 N GLU A 134 1.900 -25.205 -30.086 1.00 53.92 N ANISOU 1065 N GLU A 134 7285 6121 7083 1154 1350 323 N ATOM 1066 CA GLU A 134 2.167 -23.772 -30.009 1.00 50.40 C ANISOU 1066 CA GLU A 134 6939 5613 6597 1244 1251 247 C ATOM 1067 C GLU A 134 1.271 -22.981 -30.956 1.00 49.52 C ANISOU 1067 C GLU A 134 6706 5549 6559 1289 1289 217 C ATOM 1068 O GLU A 134 0.726 -21.940 -30.589 1.00 48.85 O ANISOU 1068 O GLU A 134 6689 5466 6407 1409 1310 164 O ATOM 1069 CB GLU A 134 3.643 -23.489 -30.315 1.00 47.67 C ANISOU 1069 CB GLU A 134 6652 5149 6310 1182 1064 225 C ATOM 1070 CG GLU A 134 4.591 -24.037 -29.256 1.00 55.29 C ANISOU 1070 CG GLU A 134 7761 6057 7191 1169 989 235 C ATOM 1071 CD GLU A 134 6.056 -23.803 -29.581 1.00 61.96 C ANISOU 1071 CD GLU A 134 8630 6786 8125 1101 802 211 C ATOM 1072 OE1 GLU A 134 6.363 -23.366 -30.713 1.00 62.18 O ANISOU 1072 OE1 GLU A 134 8556 6782 8289 1046 755 205 O ATOM 1073 OE2 GLU A 134 6.902 -24.059 -28.696 1.00 56.92 O ANISOU 1073 OE2 GLU A 134 8115 6090 7421 1107 705 201 O ATOM 1074 N ARG A 135 1.122 -23.485 -32.175 1.00 46.20 N ANISOU 1074 N ARG A 135 6116 5167 6271 1203 1293 247 N ATOM 1075 CA ARG A 135 0.285 -22.845 -33.178 1.00 44.13 C ANISOU 1075 CA ARG A 135 5734 4955 6079 1248 1314 223 C ATOM 1076 C ARG A 135 -1.175 -22.860 -32.750 1.00 60.23 C ANISOU 1076 C ARG A 135 7701 7104 8081 1333 1468 217 C ATOM 1077 O ARG A 135 -1.907 -21.890 -32.960 1.00 54.39 O ANISOU 1077 O ARG A 135 6941 6390 7335 1440 1485 174 O ATOM 1078 CB ARG A 135 0.461 -23.535 -34.533 1.00 39.23 C ANISOU 1078 CB ARG A 135 4960 4356 5589 1142 1280 254 C ATOM 1079 CG ARG A 135 1.749 -23.141 -35.240 1.00 39.48 C ANISOU 1079 CG ARG A 135 5043 4283 5676 1089 1143 254 C ATOM 1080 CD ARG A 135 2.034 -24.005 -36.454 1.00 43.46 C ANISOU 1080 CD ARG A 135 5419 4808 6285 987 1122 288 C ATOM 1081 NE ARG A 135 3.107 -23.428 -37.255 1.00 53.62 N ANISOU 1081 NE ARG A 135 6744 6002 7628 960 1018 292 N ATOM 1082 CZ ARG A 135 3.615 -23.976 -38.353 1.00 53.65 C ANISOU 1082 CZ ARG A 135 6672 5999 7712 885 989 320 C ATOM 1083 NH1 ARG A 135 3.159 -25.143 -38.796 1.00 46.26 N ANISOU 1083 NH1 ARG A 135 5623 5141 6813 826 1037 337 N ATOM 1084 NH2 ARG A 135 4.587 -23.355 -39.005 1.00 52.09 N ANISOU 1084 NH2 ARG A 135 6517 5712 7564 870 917 331 N ATOM 1085 N TYR A 136 -1.587 -23.965 -32.139 1.00 59.55 N ANISOU 1085 N TYR A 136 7573 7076 7978 1287 1586 263 N ATOM 1086 CA TYR A 136 -2.937 -24.089 -31.611 1.00 54.33 C ANISOU 1086 CA TYR A 136 6835 6514 7294 1358 1758 269 C ATOM 1087 C TYR A 136 -3.181 -23.065 -30.509 1.00 61.81 C ANISOU 1087 C TYR A 136 7946 7446 8092 1510 1800 228 C ATOM 1088 O TYR A 136 -4.190 -22.358 -30.517 1.00 57.56 O ANISOU 1088 O TYR A 136 7352 6966 7551 1620 1876 192 O ATOM 1089 CB TYR A 136 -3.172 -25.505 -31.087 1.00 50.89 C ANISOU 1089 CB TYR A 136 6347 6118 6872 1268 1884 341 C ATOM 1090 CG TYR A 136 -4.334 -25.625 -30.135 1.00 51.58 C ANISOU 1090 CG TYR A 136 6414 6283 6901 1347 2086 362 C ATOM 1091 CD1 TYR A 136 -5.639 -25.450 -30.576 1.00 52.82 C ANISOU 1091 CD1 TYR A 136 6380 6537 7153 1389 2190 343 C ATOM 1092 CD2 TYR A 136 -4.128 -25.925 -28.794 1.00 50.80 C ANISOU 1092 CD2 TYR A 136 6486 6163 6654 1387 2177 404 C ATOM 1093 CE1 TYR A 136 -6.710 -25.563 -29.705 1.00 48.09 C ANISOU 1093 CE1 TYR A 136 5744 6010 6519 1461 2396 367 C ATOM 1094 CE2 TYR A 136 -5.191 -26.040 -27.916 1.00 52.81 C ANISOU 1094 CE2 TYR A 136 6728 6487 6849 1466 2388 433 C ATOM 1095 CZ TYR A 136 -6.479 -25.858 -28.378 1.00 55.57 C ANISOU 1095 CZ TYR A 136 6871 6932 7312 1499 2504 417 C ATOM 1096 OH TYR A 136 -7.539 -25.974 -27.512 1.00 64.64 O ANISOU 1096 OH TYR A 136 7990 8152 8419 1577 2732 451 O ATOM 1097 N VAL A 137 -2.247 -22.986 -29.568 1.00 55.09 N ANISOU 1097 N VAL A 137 7299 6514 7118 1524 1742 226 N ATOM 1098 CA VAL A 137 -2.350 -22.049 -28.455 1.00 58.89 C ANISOU 1098 CA VAL A 137 7970 6968 7438 1672 1762 175 C ATOM 1099 C VAL A 137 -2.397 -20.592 -28.932 1.00 62.87 C ANISOU 1099 C VAL A 137 8506 7425 7957 1768 1665 93 C ATOM 1100 O VAL A 137 -3.232 -19.810 -28.481 1.00 63.03 O ANISOU 1100 O VAL A 137 8562 7478 7909 1909 1748 50 O ATOM 1101 CB VAL A 137 -1.176 -22.237 -27.472 1.00 56.21 C ANISOU 1101 CB VAL A 137 7849 6537 6971 1663 1667 174 C ATOM 1102 CG1 VAL A 137 -1.110 -21.095 -26.481 1.00 57.67 C ANISOU 1102 CG1 VAL A 137 8248 6671 6994 1820 1632 95 C ATOM 1103 CG2 VAL A 137 -1.307 -23.570 -26.747 1.00 58.18 C ANISOU 1103 CG2 VAL A 137 8108 6833 7164 1613 1794 261 C ATOM 1104 N VAL A 138 -1.516 -20.242 -29.864 1.00 63.12 N ANISOU 1104 N VAL A 138 8522 7375 8084 1696 1503 78 N ATOM 1105 CA VAL A 138 -1.416 -18.869 -30.351 1.00 62.96 C ANISOU 1105 CA VAL A 138 8549 7284 8088 1776 1404 13 C ATOM 1106 C VAL A 138 -2.630 -18.426 -31.177 1.00 62.81 C ANISOU 1106 C VAL A 138 8372 7350 8143 1848 1481 5 C ATOM 1107 O VAL A 138 -3.168 -17.339 -30.965 1.00 61.21 O ANISOU 1107 O VAL A 138 8229 7133 7895 1986 1495 -51 O ATOM 1108 CB VAL A 138 -0.137 -18.677 -31.195 1.00 53.29 C ANISOU 1108 CB VAL A 138 7338 5947 6963 1670 1232 16 C ATOM 1109 CG1 VAL A 138 -0.166 -17.343 -31.925 1.00 59.70 C ANISOU 1109 CG1 VAL A 138 8167 6688 7828 1740 1157 -28 C ATOM 1110 CG2 VAL A 138 1.096 -18.774 -30.310 1.00 50.27 C ANISOU 1110 CG2 VAL A 138 7124 5461 6513 1630 1123 -2 C ATOM 1111 N VAL A 139 -3.064 -19.269 -32.109 1.00 62.28 N ANISOU 1111 N VAL A 139 8107 7368 8190 1761 1521 54 N ATOM 1112 CA VAL A 139 -4.139 -18.899 -33.028 1.00 59.94 C ANISOU 1112 CA VAL A 139 7647 7150 7977 1824 1558 42 C ATOM 1113 C VAL A 139 -5.537 -19.121 -32.434 1.00 64.50 C ANISOU 1113 C VAL A 139 8121 7852 8535 1912 1735 38 C ATOM 1114 O VAL A 139 -6.404 -18.255 -32.536 1.00 63.24 O ANISOU 1114 O VAL A 139 7926 7728 8376 2047 1771 -4 O ATOM 1115 CB VAL A 139 -4.027 -19.680 -34.357 1.00 47.98 C ANISOU 1115 CB VAL A 139 5963 5673 6595 1702 1507 82 C ATOM 1116 CG1 VAL A 139 -5.205 -19.359 -35.271 1.00 48.86 C ANISOU 1116 CG1 VAL A 139 5903 5877 6785 1779 1531 62 C ATOM 1117 CG2 VAL A 139 -2.709 -19.360 -35.055 1.00 46.53 C ANISOU 1117 CG2 VAL A 139 5868 5371 6441 1631 1354 91 C ATOM 1118 N CYS A 140 -5.752 -20.276 -31.813 1.00 62.51 N ANISOU 1118 N CYS A 140 7819 7660 8273 1838 1852 85 N ATOM 1119 CA CYS A 140 -7.071 -20.618 -31.282 1.00 62.50 C ANISOU 1119 CA CYS A 140 7694 7774 8279 1901 2044 96 C ATOM 1120 C CYS A 140 -7.318 -19.978 -29.926 1.00 63.41 C ANISOU 1120 C CYS A 140 7981 7878 8233 2045 2149 70 C ATOM 1121 O CYS A 140 -8.467 -19.811 -29.515 1.00 70.20 O ANISOU 1121 O CYS A 140 8758 8825 9090 2150 2307 62 O ATOM 1122 CB CYS A 140 -7.228 -22.136 -31.175 1.00 57.64 C ANISOU 1122 CB CYS A 140 6955 7215 7731 1759 2145 167 C ATOM 1123 SG CYS A 140 -6.968 -22.989 -32.737 1.00 63.75 S ANISOU 1123 SG CYS A 140 7536 8001 8686 1595 2025 185 S ATOM 1124 N LYS A 141 -6.232 -19.630 -29.241 1.00 71.41 N ANISOU 1124 N LYS A 141 8057 7441 11633 3200 1040 -83 N ATOM 1125 CA LYS A 141 -6.296 -18.959 -27.943 1.00 77.66 C ANISOU 1125 CA LYS A 141 9000 8110 12399 3504 1249 -404 C ATOM 1126 C LYS A 141 -7.195 -19.679 -26.942 1.00 74.61 C ANISOU 1126 C LYS A 141 8331 8097 11921 3619 1685 -581 C ATOM 1127 O LYS A 141 -8.221 -19.141 -26.537 1.00 71.73 O ANISOU 1127 O LYS A 141 7720 7778 11754 3980 1815 -765 O ATOM 1128 CB LYS A 141 -6.781 -17.514 -28.113 1.00 68.93 C ANISOU 1128 CB LYS A 141 7899 6650 11641 3902 1034 -503 C ATOM 1129 CG LYS A 141 -5.908 -16.663 -29.017 1.00 68.14 C ANISOU 1129 CG LYS A 141 8102 6139 11649 3793 606 -305 C ATOM 1130 CD LYS A 141 -6.476 -15.259 -29.172 1.00 82.95 C ANISOU 1130 CD LYS A 141 9986 7633 13898 4194 386 -374 C ATOM 1131 CE LYS A 141 -5.559 -14.383 -30.009 1.00 85.55 C ANISOU 1131 CE LYS A 141 10661 7555 14288 4028 -25 -135 C ATOM 1132 NZ LYS A 141 -6.097 -13.005 -30.170 1.00 94.55 N ANISOU 1132 NZ LYS A 141 11890 8399 15637 4312 -200 -132 N ATOM 1133 N PRO A 142 -6.811 -20.898 -26.533 1.00 78.97 N ANISOU 1133 N PRO A 142 8910 8917 12179 3315 1916 -516 N ATOM 1134 CA PRO A 142 -7.629 -21.645 -25.575 1.00 77.82 C ANISOU 1134 CA PRO A 142 8505 9142 11923 3368 2343 -626 C ATOM 1135 C PRO A 142 -7.521 -21.079 -24.162 1.00 84.43 C ANISOU 1135 C PRO A 142 9531 9984 12566 3626 2593 -947 C ATOM 1136 O PRO A 142 -8.369 -21.362 -23.317 1.00 87.96 O ANISOU 1136 O PRO A 142 9742 10756 12923 3722 2900 -1090 O ATOM 1137 CB PRO A 142 -7.046 -23.055 -25.647 1.00 74.31 C ANISOU 1137 CB PRO A 142 8115 8882 11239 2943 2446 -415 C ATOM 1138 CG PRO A 142 -5.617 -22.838 -26.007 1.00 67.03 C ANISOU 1138 CG PRO A 142 7615 7683 10171 2761 2169 -341 C ATOM 1139 CD PRO A 142 -5.599 -21.643 -26.920 1.00 68.76 C ANISOU 1139 CD PRO A 142 7879 7594 10651 2919 1800 -328 C ATOM 1140 N MET A 143 -6.485 -20.281 -23.922 1.00 93.36 N ANISOU 1140 N MET A 143 11083 10796 13593 3665 2405 -1072 N ATOM 1141 CA MET A 143 -6.278 -19.657 -22.620 1.00 97.88 C ANISOU 1141 CA MET A 143 11873 11365 13951 3863 2563 -1423 C ATOM 1142 C MET A 143 -6.409 -18.138 -22.703 1.00 98.58 C ANISOU 1142 C MET A 143 12065 11079 14310 4155 2292 -1680 C ATOM 1143 O MET A 143 -5.810 -17.500 -23.567 1.00107.01 O ANISOU 1143 O MET A 143 13336 11744 15579 4140 1956 -1558 O ATOM 1144 CB MET A 143 -4.906 -20.036 -22.065 1.00 98.56 C ANISOU 1144 CB MET A 143 12372 11422 13655 3624 2575 -1405 C ATOM 1145 CG MET A 143 -4.710 -21.529 -21.891 1.00 94.50 C ANISOU 1145 CG MET A 143 11780 11251 12877 3296 2784 -1149 C ATOM 1146 SD MET A 143 -3.024 -21.961 -21.428 1.00103.52 S ANISOU 1146 SD MET A 143 13373 12346 13612 2997 2683 -1074 S ATOM 1147 CE MET A 143 -2.119 -21.396 -22.867 1.00 99.58 C ANISOU 1147 CE MET A 143 13047 11430 13358 2829 2190 -908 C ATOM 1148 N SER A 144 -7.196 -17.562 -21.802 1.00101.09 N ANISOU 1148 N SER A 144 12235 11520 14654 4399 2441 -2032 N ATOM 1149 CA SER A 144 -7.397 -16.118 -21.783 1.00110.60 C ANISOU 1149 CA SER A 144 13501 12326 16194 4668 2232 -2311 C ATOM 1150 C SER A 144 -6.181 -15.403 -21.201 1.00113.14 C ANISOU 1150 C SER A 144 14299 12318 16372 4582 2132 -2501 C ATOM 1151 O SER A 144 -5.520 -15.922 -20.300 1.00118.51 O ANISOU 1151 O SER A 144 15176 13232 16622 4427 2309 -2599 O ATOM 1152 CB SER A 144 -8.654 -15.758 -20.987 1.00115.20 C ANISOU 1152 CB SER A 144 13736 13116 16919 4924 2510 -2633 C ATOM 1153 OG SER A 144 -8.577 -16.246 -19.659 1.00119.45 O ANISOU 1153 OG SER A 144 14319 14030 17038 4841 2871 -2851 O ATOM 1154 N ASN A 145 -5.893 -14.218 -21.736 1.00111.53 N ANISOU 1154 N ASN A 145 14286 11574 16516 4662 1861 -2498 N ATOM 1155 CA ASN A 145 -4.789 -13.377 -21.272 1.00112.09 C ANISOU 1155 CA ASN A 145 14812 11293 16484 4570 1728 -2669 C ATOM 1156 C ASN A 145 -3.425 -14.064 -21.314 1.00105.77 C ANISOU 1156 C ASN A 145 14316 10562 15312 4244 1592 -2538 C ATOM 1157 O ASN A 145 -2.548 -13.762 -20.504 1.00108.76 O ANISOU 1157 O ASN A 145 15002 10888 15436 4138 1588 -2764 O ATOM 1158 CB ASN A 145 -5.065 -12.882 -19.851 1.00118.57 C ANISOU 1158 CB ASN A 145 15689 12222 17140 4724 2025 -3119 C ATOM 1159 CG ASN A 145 -6.317 -12.040 -19.764 1.00129.91 C ANISOU 1159 CG ASN A 145 16923 13526 18912 5087 2180 -3238 C ATOM 1160 OD1 ASN A 145 -6.649 -11.306 -20.694 1.00132.98 O ANISOU 1160 OD1 ASN A 145 17312 13550 19666 5242 1961 -3027 O ATOM 1161 ND2 ASN A 145 -7.024 -12.142 -18.644 1.00138.11 N ANISOU 1161 ND2 ASN A 145 17805 14890 19779 5238 2555 -3547 N ATOM 1162 N PHE A 146 -3.249 -14.981 -22.260 1.00 88.60 N ANISOU 1162 N PHE A 146 12064 8505 13093 4088 1502 -2157 N ATOM 1163 CA PHE A 146 -1.982 -15.687 -22.407 1.00 86.12 C ANISOU 1163 CA PHE A 146 12041 8232 12450 3783 1433 -1961 C ATOM 1164 C PHE A 146 -1.181 -15.151 -23.588 1.00 89.72 C ANISOU 1164 C PHE A 146 12700 8269 13121 3599 1019 -1698 C ATOM 1165 O PHE A 146 -1.723 -14.952 -24.676 1.00 93.71 O ANISOU 1165 O PHE A 146 13020 8636 13949 3642 840 -1450 O ATOM 1166 CB PHE A 146 -2.222 -17.187 -22.578 1.00 76.64 C ANISOU 1166 CB PHE A 146 10602 7485 11032 3603 1673 -1680 C ATOM 1167 CG PHE A 146 -0.962 -17.982 -22.771 1.00 79.40 C ANISOU 1167 CG PHE A 146 11145 7931 11093 3191 1573 -1445 C ATOM 1168 CD1 PHE A 146 -0.212 -18.391 -21.681 1.00 84.11 C ANISOU 1168 CD1 PHE A 146 11946 8731 11279 3088 1727 -1581 C ATOM 1169 CD2 PHE A 146 -0.526 -18.323 -24.042 1.00 75.45 C ANISOU 1169 CD2 PHE A 146 10605 7347 10716 2922 1323 -1093 C ATOM 1170 CE1 PHE A 146 0.949 -19.121 -21.853 1.00 79.18 C ANISOU 1170 CE1 PHE A 146 11472 8198 10415 2747 1625 -1364 C ATOM 1171 CE2 PHE A 146 0.635 -19.052 -24.221 1.00 75.77 C ANISOU 1171 CE2 PHE A 146 10795 7489 10505 2577 1246 -908 C ATOM 1172 CZ PHE A 146 1.372 -19.453 -23.125 1.00 77.64 C ANISOU 1172 CZ PHE A 146 11222 7903 10375 2501 1393 -1039 C ATOM 1173 N ARG A 147 0.110 -14.918 -23.367 1.00 81.90 N ANISOU 1173 N ARG A 147 12052 7131 11937 3346 853 -1733 N ATOM 1174 CA ARG A 147 1.010 -14.496 -24.436 1.00 75.21 C ANISOU 1174 CA ARG A 147 11370 5973 11232 3063 474 -1451 C ATOM 1175 C ARG A 147 2.219 -15.419 -24.521 1.00 71.16 C ANISOU 1175 C ARG A 147 10957 5720 10362 2650 454 -1253 C ATOM 1176 O ARG A 147 2.976 -15.554 -23.562 1.00 73.78 O ANISOU 1176 O ARG A 147 11484 6164 10385 2563 535 -1455 O ATOM 1177 CB ARG A 147 1.469 -13.050 -24.229 1.00 76.27 C ANISOU 1177 CB ARG A 147 11774 5627 11577 3087 236 -1656 C ATOM 1178 CG ARG A 147 0.357 -12.021 -24.345 1.00 95.96 C ANISOU 1178 CG ARG A 147 14102 7878 14482 3376 241 -1739 C ATOM 1179 CD ARG A 147 0.917 -10.615 -24.479 1.00105.50 C ANISOU 1179 CD ARG A 147 15568 8603 15916 3282 -10 -1776 C ATOM 1180 NE ARG A 147 -0.140 -9.616 -24.617 1.00112.78 N ANISOU 1180 NE ARG A 147 16385 9267 17199 3593 7 -1819 N ATOM 1181 CZ ARG A 147 0.077 -8.332 -24.883 1.00122.08 C ANISOU 1181 CZ ARG A 147 17757 9992 18636 3580 -201 -1799 C ATOM 1182 NH1 ARG A 147 1.316 -7.890 -25.045 1.00123.18 N ANISOU 1182 NH1 ARG A 147 18174 9902 18726 3237 -437 -1737 N ATOM 1183 NH2 ARG A 147 -0.944 -7.490 -24.991 1.00128.12 N ANISOU 1183 NH2 ARG A 147 18433 10538 19710 3911 -176 -1833 N ATOM 1184 N PHE A 148 2.391 -16.053 -25.676 1.00 67.90 N ANISOU 1184 N PHE A 148 10395 5421 9984 2411 339 -871 N ATOM 1185 CA PHE A 148 3.508 -16.964 -25.900 1.00 67.41 C ANISOU 1185 CA PHE A 148 10386 5602 9627 2047 315 -677 C ATOM 1186 C PHE A 148 4.827 -16.198 -25.980 1.00 69.03 C ANISOU 1186 C PHE A 148 10890 5552 9787 1808 37 -683 C ATOM 1187 O PHE A 148 5.005 -15.337 -26.842 1.00 72.32 O ANISOU 1187 O PHE A 148 11379 5649 10452 1727 -241 -533 O ATOM 1188 CB PHE A 148 3.286 -17.775 -27.179 1.00 58.87 C ANISOU 1188 CB PHE A 148 9055 4700 8612 1874 263 -318 C ATOM 1189 CG PHE A 148 4.320 -18.838 -27.414 1.00 64.45 C ANISOU 1189 CG PHE A 148 9772 5678 9038 1552 279 -153 C ATOM 1190 CD1 PHE A 148 4.166 -20.104 -26.877 1.00 55.95 C ANISOU 1190 CD1 PHE A 148 8571 4938 7751 1541 554 -162 C ATOM 1191 CD2 PHE A 148 5.444 -18.574 -28.181 1.00 70.94 C ANISOU 1191 CD2 PHE A 148 10716 6415 9822 1264 22 21 C ATOM 1192 CE1 PHE A 148 5.115 -21.085 -27.096 1.00 55.50 C ANISOU 1192 CE1 PHE A 148 8521 5090 7477 1285 559 -19 C ATOM 1193 CE2 PHE A 148 6.396 -19.552 -28.401 1.00 66.60 C ANISOU 1193 CE2 PHE A 148 10145 6129 9029 1005 46 145 C ATOM 1194 CZ PHE A 148 6.230 -20.808 -27.859 1.00 58.26 C ANISOU 1194 CZ PHE A 148 8974 5370 7793 1034 308 116 C ATOM 1195 N GLY A 149 5.750 -16.516 -25.079 1.00 61.91 N ANISOU 1195 N GLY A 149 10150 4809 8564 1682 105 -835 N ATOM 1196 CA GLY A 149 7.026 -15.828 -25.030 1.00 56.18 C ANISOU 1196 CA GLY A 149 9681 3890 7775 1436 -147 -875 C ATOM 1197 C GLY A 149 8.224 -16.753 -25.132 1.00 63.12 C ANISOU 1197 C GLY A 149 10549 5088 8346 1120 -164 -705 C ATOM 1198 O GLY A 149 8.084 -17.945 -25.415 1.00 66.26 O ANISOU 1198 O GLY A 149 10749 5809 8617 1082 -4 -523 O ATOM 1199 N GLU A 150 9.405 -16.192 -24.889 1.00 64.80 N ANISOU 1199 N GLU A 150 10964 5197 8458 896 -364 -780 N ATOM 1200 CA GLU A 150 10.662 -16.922 -25.000 1.00 67.87 C ANISOU 1200 CA GLU A 150 11331 5877 8581 601 -419 -632 C ATOM 1201 C GLU A 150 10.715 -18.131 -24.069 1.00 68.83 C ANISOU 1201 C GLU A 150 11380 6406 8367 697 -164 -696 C ATOM 1202 O GLU A 150 11.166 -19.205 -24.466 1.00 62.03 O ANISOU 1202 O GLU A 150 10371 5826 7373 573 -107 -479 O ATOM 1203 CB GLU A 150 11.843 -15.991 -24.708 1.00 69.60 C ANISOU 1203 CB GLU A 150 11770 5917 8758 361 -675 -758 C ATOM 1204 CG GLU A 150 13.203 -16.609 -25.003 1.00 78.99 C ANISOU 1204 CG GLU A 150 12890 7403 9721 38 -773 -578 C ATOM 1205 CD GLU A 150 14.355 -15.719 -24.587 1.00 96.24 C ANISOU 1205 CD GLU A 150 15262 9457 11849 -215 -1018 -728 C ATOM 1206 OE1 GLU A 150 15.435 -15.816 -25.206 1.00104.61 O ANISOU 1206 OE1 GLU A 150 16247 10646 12852 -532 -1172 -533 O ATOM 1207 OE2 GLU A 150 14.184 -14.926 -23.638 1.00104.33 O ANISOU 1207 OE2 GLU A 150 16494 10267 12881 -105 -1052 -1062 O ATOM 1208 N ASN A 151 10.250 -17.952 -22.835 1.00 63.50 N ANISOU 1208 N ASN A 151 10811 5761 7556 922 -10 -992 N ATOM 1209 CA ASN A 151 10.280 -19.022 -21.842 1.00 64.66 C ANISOU 1209 CA ASN A 151 10914 6297 7357 1011 228 -1027 C ATOM 1210 C ASN A 151 9.440 -20.232 -22.240 1.00 68.91 C ANISOU 1210 C ASN A 151 11210 7040 7931 1107 474 -792 C ATOM 1211 O ASN A 151 9.827 -21.371 -21.990 1.00 65.95 O ANISOU 1211 O ASN A 151 10760 6956 7341 1050 589 -640 O ATOM 1212 CB ASN A 151 9.815 -18.500 -20.483 1.00 65.05 C ANISOU 1212 CB ASN A 151 11117 6364 7236 1240 361 -1400 C ATOM 1213 CG ASN A 151 10.891 -17.713 -19.768 1.00 75.85 C ANISOU 1213 CG ASN A 151 12724 7678 8417 1103 147 -1656 C ATOM 1214 OD1 ASN A 151 12.082 -17.907 -20.014 1.00 73.75 O ANISOU 1214 OD1 ASN A 151 12475 7505 8041 838 -44 -1520 O ATOM 1215 ND2 ASN A 151 10.479 -16.819 -18.876 1.00 79.17 N ANISOU 1215 ND2 ASN A 151 13315 7963 8803 1282 176 -2054 N ATOM 1216 N HIS A 152 8.290 -19.983 -22.858 1.00 72.49 N ANISOU 1216 N HIS A 152 11537 7329 8676 1251 541 -760 N ATOM 1217 CA HIS A 152 7.432 -21.071 -23.310 1.00 66.39 C ANISOU 1217 CA HIS A 152 10517 6733 7976 1308 753 -557 C ATOM 1218 C HIS A 152 8.095 -21.827 -24.454 1.00 60.21 C ANISOU 1218 C HIS A 152 9616 6025 7237 1062 635 -267 C ATOM 1219 O HIS A 152 7.976 -23.048 -24.556 1.00 61.47 O ANISOU 1219 O HIS A 152 9631 6398 7326 1028 794 -112 O ATOM 1220 CB HIS A 152 6.065 -20.539 -23.747 1.00 60.22 C ANISOU 1220 CB HIS A 152 9596 5777 7506 1516 813 -602 C ATOM 1221 CG HIS A 152 5.361 -19.747 -22.690 1.00 63.42 C ANISOU 1221 CG HIS A 152 10089 6106 7901 1797 942 -928 C ATOM 1222 ND1 HIS A 152 5.139 -18.391 -22.799 1.00 65.26 N ANISOU 1222 ND1 HIS A 152 10442 5981 8371 1927 771 -1124 N ATOM 1223 CD2 HIS A 152 4.836 -20.120 -21.499 1.00 55.49 C ANISOU 1223 CD2 HIS A 152 9069 5343 6671 1977 1233 -1101 C ATOM 1224 CE1 HIS A 152 4.504 -17.963 -21.723 1.00 63.62 C ANISOU 1224 CE1 HIS A 152 10284 5794 8094 2196 955 -1448 C ATOM 1225 NE2 HIS A 152 4.310 -18.992 -20.917 1.00 70.63 N ANISOU 1225 NE2 HIS A 152 11085 7075 8677 2223 1244 -1438 N ATOM 1226 N ALA A 153 8.799 -21.091 -25.308 1.00 56.62 N ANISOU 1226 N ALA A 153 9226 5390 6898 883 360 -201 N ATOM 1227 CA ALA A 153 9.472 -21.677 -26.460 1.00 59.04 C ANISOU 1227 CA ALA A 153 9413 5797 7224 645 244 43 C ATOM 1228 C ALA A 153 10.615 -22.588 -26.025 1.00 61.00 C ANISOU 1228 C ALA A 153 9677 6298 7201 520 274 87 C ATOM 1229 O ALA A 153 10.873 -23.620 -26.647 1.00 52.27 O ANISOU 1229 O ALA A 153 8422 5363 6076 427 323 248 O ATOM 1230 CB ALA A 153 9.987 -20.588 -27.380 1.00 51.35 C ANISOU 1230 CB ALA A 153 8510 4600 6400 466 -46 119 C ATOM 1231 N ILE A 154 11.296 -22.191 -24.956 1.00 58.32 N ANISOU 1231 N ILE A 154 9516 5982 6659 531 232 -74 N ATOM 1232 CA ILE A 154 12.411 -22.959 -24.422 1.00 61.89 C ANISOU 1232 CA ILE A 154 9983 6688 6846 443 229 -32 C ATOM 1233 C ILE A 154 11.910 -24.257 -23.790 1.00 66.29 C ANISOU 1233 C ILE A 154 10456 7451 7279 597 498 42 C ATOM 1234 O ILE A 154 12.506 -25.318 -23.969 1.00 59.73 O ANISOU 1234 O ILE A 154 9530 6792 6372 537 529 198 O ATOM 1235 CB ILE A 154 13.204 -22.136 -23.392 1.00 59.39 C ANISOU 1235 CB ILE A 154 9872 6366 6326 410 93 -240 C ATOM 1236 CG1 ILE A 154 13.821 -20.910 -24.071 1.00 59.29 C ANISOU 1236 CG1 ILE A 154 9940 6120 6465 197 -189 -277 C ATOM 1237 CG2 ILE A 154 14.282 -22.984 -22.736 1.00 57.44 C ANISOU 1237 CG2 ILE A 154 9613 6426 5785 357 86 -181 C ATOM 1238 CD1 ILE A 154 14.477 -19.941 -23.116 1.00 58.78 C ANISOU 1238 CD1 ILE A 154 10090 5982 6261 139 -347 -531 C ATOM 1239 N MET A 155 10.801 -24.167 -23.063 1.00 70.76 N ANISOU 1239 N MET A 155 11050 7993 7844 797 696 -65 N ATOM 1240 CA MET A 155 10.170 -25.346 -22.482 1.00 64.79 C ANISOU 1240 CA MET A 155 10206 7417 6995 917 971 39 C ATOM 1241 C MET A 155 9.762 -26.340 -23.563 1.00 58.12 C ANISOU 1241 C MET A 155 9151 6562 6369 849 1045 245 C ATOM 1242 O MET A 155 9.962 -27.546 -23.415 1.00 63.97 O ANISOU 1242 O MET A 155 9828 7432 7048 833 1161 401 O ATOM 1243 CB MET A 155 8.951 -24.948 -21.652 1.00 70.43 C ANISOU 1243 CB MET A 155 10943 8127 7691 1127 1184 -122 C ATOM 1244 CG MET A 155 9.290 -24.240 -20.357 1.00 91.30 C ANISOU 1244 CG MET A 155 13795 10855 10041 1219 1175 -359 C ATOM 1245 SD MET A 155 7.813 -23.844 -19.406 1.00112.12 S ANISOU 1245 SD MET A 155 16418 13547 12637 1490 1473 -581 S ATOM 1246 CE MET A 155 7.067 -25.470 -19.278 1.00108.17 C ANISOU 1246 CE MET A 155 15710 13285 12105 1502 1797 -273 C ATOM 1247 N GLY A 156 9.190 -25.824 -24.647 1.00 51.69 N ANISOU 1247 N GLY A 156 8236 5588 5817 809 963 243 N ATOM 1248 CA GLY A 156 8.782 -26.654 -25.766 1.00 47.45 C ANISOU 1248 CA GLY A 156 7496 5058 5475 723 1001 393 C ATOM 1249 C GLY A 156 9.940 -27.432 -26.361 1.00 54.51 C ANISOU 1249 C GLY A 156 8353 6049 6310 562 900 508 C ATOM 1250 O GLY A 156 9.813 -28.621 -26.653 1.00 55.68 O ANISOU 1250 O GLY A 156 8382 6260 6514 537 1018 609 O ATOM 1251 N VAL A 157 11.074 -26.763 -26.542 1.00 59.05 N ANISOU 1251 N VAL A 157 9021 6629 6787 449 683 479 N ATOM 1252 CA VAL A 157 12.264 -27.416 -27.076 1.00 60.58 C ANISOU 1252 CA VAL A 157 9151 6955 6911 313 588 563 C ATOM 1253 C VAL A 157 12.798 -28.460 -26.097 1.00 63.22 C ANISOU 1253 C VAL A 157 9518 7425 7079 404 703 616 C ATOM 1254 O VAL A 157 13.119 -29.587 -26.487 1.00 59.81 O ANISOU 1254 O VAL A 157 8974 7058 6691 390 760 709 O ATOM 1255 CB VAL A 157 13.367 -26.395 -27.393 1.00 51.23 C ANISOU 1255 CB VAL A 157 8036 5778 5651 151 336 529 C ATOM 1256 CG1 VAL A 157 14.702 -27.099 -27.646 1.00 50.95 C ANISOU 1256 CG1 VAL A 157 7916 5946 5498 47 265 592 C ATOM 1257 CG2 VAL A 157 12.965 -25.553 -28.588 1.00 46.96 C ANISOU 1257 CG2 VAL A 157 7443 5114 5286 27 205 560 C ATOM 1258 N ALA A 158 12.877 -28.083 -24.825 1.00 50.94 N ANISOU 1258 N ALA A 158 8119 5907 5329 506 730 554 N ATOM 1259 CA ALA A 158 13.349 -28.985 -23.786 1.00 52.07 C ANISOU 1259 CA ALA A 158 8310 6202 5273 603 820 642 C ATOM 1260 C ALA A 158 12.467 -30.227 -23.696 1.00 64.08 C ANISOU 1260 C ALA A 158 9747 7697 6905 690 1067 785 C ATOM 1261 O ALA A 158 12.951 -31.326 -23.416 1.00 67.93 O ANISOU 1261 O ALA A 158 10211 8249 7351 730 1119 934 O ATOM 1262 CB ALA A 158 13.394 -28.268 -22.449 1.00 52.37 C ANISOU 1262 CB ALA A 158 8531 6318 5048 691 815 527 C ATOM 1263 N PHE A 159 11.171 -30.040 -23.935 1.00 60.17 N ANISOU 1263 N PHE A 159 9196 7094 6572 718 1209 746 N ATOM 1264 CA PHE A 159 10.211 -31.135 -23.892 1.00 53.30 C ANISOU 1264 CA PHE A 159 8223 6190 5839 755 1446 872 C ATOM 1265 C PHE A 159 10.518 -32.180 -24.960 1.00 57.94 C ANISOU 1265 C PHE A 159 8671 6712 6632 658 1421 957 C ATOM 1266 O PHE A 159 10.410 -33.381 -24.711 1.00 55.89 O ANISOU 1266 O PHE A 159 8380 6421 6434 679 1559 1099 O ATOM 1267 CB PHE A 159 8.784 -30.606 -24.064 1.00 54.04 C ANISOU 1267 CB PHE A 159 8234 6213 6086 791 1574 787 C ATOM 1268 CG PHE A 159 7.738 -31.687 -24.113 1.00 50.83 C ANISOU 1268 CG PHE A 159 7682 5782 5849 781 1811 910 C ATOM 1269 CD1 PHE A 159 7.321 -32.317 -22.955 1.00 58.21 C ANISOU 1269 CD1 PHE A 159 8660 6806 6652 854 2041 1033 C ATOM 1270 CD2 PHE A 159 7.176 -32.072 -25.320 1.00 52.35 C ANISOU 1270 CD2 PHE A 159 7690 5881 6320 674 1798 908 C ATOM 1271 CE1 PHE A 159 6.361 -33.316 -22.995 1.00 58.08 C ANISOU 1271 CE1 PHE A 159 8502 6753 6812 802 2262 1168 C ATOM 1272 CE2 PHE A 159 6.217 -33.067 -25.369 1.00 50.06 C ANISOU 1272 CE2 PHE A 159 7257 5558 6206 628 2002 1003 C ATOM 1273 CZ PHE A 159 5.809 -33.690 -24.204 1.00 56.06 C ANISOU 1273 CZ PHE A 159 8059 6376 6867 683 2238 1141 C ATOM 1274 N THR A 160 10.904 -31.724 -26.146 1.00 54.15 N ANISOU 1274 N THR A 160 8113 6208 6255 546 1245 869 N ATOM 1275 CA THR A 160 11.221 -32.644 -27.228 1.00 55.24 C ANISOU 1275 CA THR A 160 8111 6322 6558 456 1221 890 C ATOM 1276 C THR A 160 12.471 -33.464 -26.908 1.00 57.59 C ANISOU 1276 C THR A 160 8438 6680 6764 502 1178 963 C ATOM 1277 O THR A 160 12.540 -34.646 -27.234 1.00 50.29 O ANISOU 1277 O THR A 160 7436 5685 5986 511 1254 1013 O ATOM 1278 CB THR A 160 11.427 -31.907 -28.555 1.00 43.55 C ANISOU 1278 CB THR A 160 6536 4870 5140 317 1041 790 C ATOM 1279 OG1 THR A 160 12.579 -31.060 -28.462 1.00 51.54 O ANISOU 1279 OG1 THR A 160 7629 5978 5975 276 852 762 O ATOM 1280 CG2 THR A 160 10.202 -31.075 -28.891 1.00 47.17 C ANISOU 1280 CG2 THR A 160 6954 5259 5708 302 1050 746 C ATOM 1281 N ATRP A 161 13.448 -32.817 -26.277 0.51 53.12 N ANISOU 1281 N ATRP A 161 7975 6237 5972 533 1042 958 N ATOM 1282 N BTRP A 161 13.452 -32.843 -26.263 0.49 53.14 N ANISOU 1282 N BTRP A 161 7977 6239 5974 536 1045 961 N ATOM 1283 CA ATRP A 161 14.683 -33.476 -25.866 0.51 52.44 C ANISOU 1283 CA ATRP A 161 7895 6251 5777 603 972 1037 C ATOM 1284 CA BTRP A 161 14.683 -33.547 -25.915 0.49 52.27 C ANISOU 1284 CA BTRP A 161 7866 6225 5770 603 977 1040 C ATOM 1285 C ATRP A 161 14.394 -34.600 -24.879 0.51 56.75 C ANISOU 1285 C ATRP A 161 8505 6734 6321 745 1139 1220 C ATOM 1286 C BTRP A 161 14.449 -34.599 -24.832 0.49 56.75 C ANISOU 1286 C BTRP A 161 8510 6743 6310 750 1133 1225 C ATOM 1287 O ATRP A 161 14.904 -35.711 -25.018 0.51 59.63 O ANISOU 1287 O ATRP A 161 8813 7048 6796 811 1156 1314 O ATOM 1288 O BTRP A 161 15.054 -35.669 -24.862 0.49 60.64 O ANISOU 1288 O BTRP A 161 8956 7202 6883 826 1138 1326 O ATOM 1289 CB ATRP A 161 15.652 -32.468 -25.236 0.51 49.75 C ANISOU 1289 CB ATRP A 161 7648 6079 5177 590 787 992 C ATOM 1290 CB BTRP A 161 15.761 -32.556 -25.473 0.49 49.79 C ANISOU 1290 CB BTRP A 161 7621 6086 5213 575 775 986 C ATOM 1291 CG ATRP A 161 16.166 -31.423 -26.185 0.51 45.91 C ANISOU 1291 CG ATRP A 161 7099 5648 4695 419 603 862 C ATOM 1292 CG BTRP A 161 16.503 -31.952 -26.627 0.49 46.83 C ANISOU 1292 CG BTRP A 161 7128 5793 4874 415 602 880 C ATOM 1293 CD1ATRP A 161 15.874 -31.303 -27.513 0.51 40.45 C ANISOU 1293 CD1ATRP A 161 6283 4911 4175 292 586 806 C ATOM 1294 CD1BTRP A 161 16.071 -30.949 -27.444 0.49 40.25 C ANISOU 1294 CD1BTRP A 161 6279 4911 4102 266 533 790 C ATOM 1295 CD2ATRP A 161 17.067 -30.351 -25.874 0.51 42.94 C ANISOU 1295 CD2ATRP A 161 6784 5395 4136 330 403 794 C ATOM 1296 CD2BTRP A 161 17.807 -32.319 -27.097 0.49 51.23 C ANISOU 1296 CD2BTRP A 161 7548 6517 5399 388 483 876 C ATOM 1297 NE1ATRP A 161 16.536 -30.224 -28.047 0.51 40.61 N ANISOU 1297 NE1ATRP A 161 6287 5017 4124 130 397 744 N ATOM 1298 NE1BTRP A 161 17.024 -30.668 -28.393 0.49 41.97 N ANISOU 1298 NE1BTRP A 161 6373 5268 4307 118 385 752 N ATOM 1299 CE2ATRP A 161 17.274 -29.623 -27.061 0.51 42.00 C ANISOU 1299 CE2ATRP A 161 6576 5277 4106 140 283 730 C ATOM 1300 CE2BTRP A 161 18.100 -31.494 -28.200 0.49 50.90 C ANISOU 1300 CE2BTRP A 161 7413 6549 5378 191 363 785 C ATOM 1301 CE3ATRP A 161 17.717 -29.939 -24.707 0.51 48.70 C ANISOU 1301 CE3ATRP A 161 7633 6247 4625 372 305 781 C ATOM 1302 CE3BTRP A 161 18.755 -33.264 -26.691 0.49 48.97 C ANISOU 1302 CE3BTRP A 161 7195 6335 5075 524 465 952 C ATOM 1303 CZ2ATRP A 161 18.105 -28.504 -27.116 0.51 46.91 C ANISOU 1303 CZ2ATRP A 161 7226 5978 4618 -25 77 673 C ATOM 1304 CZ2BTRP A 161 19.300 -31.584 -28.902 0.49 44.59 C ANISOU 1304 CZ2BTRP A 161 6441 5961 4538 105 252 752 C ATOM 1305 CZ3ATRP A 161 18.542 -28.829 -24.764 0.51 52.16 C ANISOU 1305 CZ3ATRP A 161 8093 6771 4956 212 90 681 C ATOM 1306 CZ3BTRP A 161 19.943 -33.351 -27.388 0.49 45.91 C ANISOU 1306 CZ3BTRP A 161 6626 6140 4677 473 344 898 C ATOM 1307 CH2ATRP A 161 18.728 -28.124 -25.959 0.51 48.05 C ANISOU 1307 CH2ATRP A 161 7484 6209 4562 8 -18 636 C ATOM 1308 CH2BTRP A 161 20.206 -32.517 -28.481 0.49 44.05 C ANISOU 1308 CH2BTRP A 161 6285 6011 4439 256 251 790 C ATOM 1309 N VAL A 162 13.568 -34.297 -23.882 1.00 56.38 N ANISOU 1309 N VAL A 162 8576 6692 6154 796 1265 1276 N ATOM 1310 CA VAL A 162 13.209 -35.258 -22.843 1.00 53.87 C ANISOU 1310 CA VAL A 162 8331 6350 5786 903 1439 1496 C ATOM 1311 C VAL A 162 12.421 -36.440 -23.413 1.00 64.78 C ANISOU 1311 C VAL A 162 9614 7512 7488 865 1611 1590 C ATOM 1312 O VAL A 162 12.696 -37.594 -23.081 1.00 71.10 O ANISOU 1312 O VAL A 162 10433 8215 8368 933 1669 1785 O ATOM 1313 CB VAL A 162 12.384 -34.587 -21.722 1.00 57.04 C ANISOU 1313 CB VAL A 162 8854 6858 5961 946 1569 1501 C ATOM 1314 CG1 VAL A 162 11.763 -35.631 -20.805 1.00 52.17 C ANISOU 1314 CG1 VAL A 162 8282 6225 5314 1008 1797 1763 C ATOM 1315 CG2 VAL A 162 13.254 -33.633 -20.926 1.00 55.97 C ANISOU 1315 CG2 VAL A 162 8846 6935 5484 991 1398 1413 C ATOM 1316 N MET A 163 11.448 -36.154 -24.274 1.00 60.80 N ANISOU 1316 N MET A 163 9004 6917 7181 754 1676 1453 N ATOM 1317 CA MET A 163 10.654 -37.208 -24.903 1.00 65.64 C ANISOU 1317 CA MET A 163 9504 7329 8108 676 1818 1493 C ATOM 1318 C MET A 163 11.511 -38.080 -25.821 1.00 60.45 C ANISOU 1318 C MET A 163 8770 6559 7640 667 1716 1443 C ATOM 1319 O MET A 163 11.330 -39.294 -25.887 1.00 61.52 O ANISOU 1319 O MET A 163 8883 6490 7999 667 1816 1540 O ATOM 1320 CB MET A 163 9.487 -36.613 -25.695 1.00 56.21 C ANISOU 1320 CB MET A 163 8181 6117 7059 559 1864 1336 C ATOM 1321 CG MET A 163 8.433 -35.935 -24.841 1.00 52.14 C ANISOU 1321 CG MET A 163 7694 5687 6431 593 2014 1365 C ATOM 1322 SD MET A 163 7.747 -37.027 -23.578 1.00 65.66 S ANISOU 1322 SD MET A 163 9454 7364 8129 620 2300 1646 S ATOM 1323 CE MET A 163 7.006 -38.307 -24.590 1.00 66.17 C ANISOU 1323 CE MET A 163 9343 7177 8624 448 2397 1670 C ATOM 1324 N ALA A 164 12.443 -37.453 -26.528 1.00 51.16 N ANISOU 1324 N ALA A 164 7548 5511 6381 655 1522 1284 N ATOM 1325 CA ALA A 164 13.326 -38.180 -27.433 1.00 55.84 C ANISOU 1325 CA ALA A 164 8040 6061 7116 663 1434 1190 C ATOM 1326 C ALA A 164 14.264 -39.107 -26.662 1.00 61.57 C ANISOU 1326 C ALA A 164 8831 6732 7832 839 1422 1362 C ATOM 1327 O ALA A 164 14.538 -40.223 -27.096 1.00 67.58 O ANISOU 1327 O ALA A 164 9534 7315 8829 893 1450 1351 O ATOM 1328 CB ALA A 164 14.120 -37.212 -28.287 1.00 42.38 C ANISOU 1328 CB ALA A 164 6254 4568 5280 592 1247 1010 C ATOM 1329 N LEU A 165 14.753 -38.637 -25.518 1.00 59.41 N ANISOU 1329 N LEU A 165 8676 6609 7288 938 1368 1513 N ATOM 1330 CA LEU A 165 15.595 -39.454 -24.652 1.00 57.79 C ANISOU 1330 CA LEU A 165 8535 6387 7034 1121 1334 1731 C ATOM 1331 C LEU A 165 14.791 -40.592 -24.041 1.00 60.86 C ANISOU 1331 C LEU A 165 9008 6515 7601 1161 1525 1978 C ATOM 1332 O LEU A 165 15.329 -41.661 -23.763 1.00 68.84 O ANISOU 1332 O LEU A 165 10040 7368 8747 1302 1515 2153 O ATOM 1333 CB LEU A 165 16.230 -38.603 -23.549 1.00 57.28 C ANISOU 1333 CB LEU A 165 8576 6598 6591 1190 1215 1822 C ATOM 1334 CG LEU A 165 17.412 -37.736 -23.989 1.00 71.51 C ANISOU 1334 CG LEU A 165 10287 8646 8237 1166 990 1644 C ATOM 1335 CD1 LEU A 165 17.791 -36.742 -22.902 1.00 74.58 C ANISOU 1335 CD1 LEU A 165 10794 9286 8257 1174 877 1680 C ATOM 1336 CD2 LEU A 165 18.604 -38.613 -24.359 1.00 69.61 C ANISOU 1336 CD2 LEU A 165 9913 8414 8120 1308 884 1666 C ATOM 1337 N ALA A 166 13.496 -40.358 -23.848 1.00 58.76 N ANISOU 1337 N ALA A 166 8777 6197 7353 1035 1696 2002 N ATOM 1338 CA ALA A 166 12.605 -41.367 -23.283 1.00 58.88 C ANISOU 1338 CA ALA A 166 8835 6000 7536 1005 1886 2226 C ATOM 1339 C ALA A 166 12.419 -42.532 -24.251 1.00 61.64 C ANISOU 1339 C ALA A 166 9104 6001 8318 955 1939 2172 C ATOM 1340 O ALA A 166 11.912 -43.591 -23.883 1.00 65.48 O ANISOU 1340 O ALA A 166 9586 6296 8997 909 2017 2302 O ATOM 1341 CB ALA A 166 11.259 -40.750 -22.931 1.00 54.92 C ANISOU 1341 CB ALA A 166 8311 5603 6953 866 2034 2184 C ATOM 1342 N CYS A 167 12.835 -42.321 -25.494 1.00 65.45 N ANISOU 1342 N CYS A 167 9461 6489 8917 921 1829 1871 N ATOM 1343 CA CYS A 167 12.728 -43.338 -26.524 1.00 63.33 C ANISOU 1343 CA CYS A 167 9097 5935 9029 871 1854 1713 C ATOM 1344 C CYS A 167 14.094 -43.921 -26.889 1.00 65.03 C ANISOU 1344 C CYS A 167 9275 6103 9330 1062 1713 1634 C ATOM 1345 O CYS A 167 14.238 -45.135 -27.057 1.00 55.12 O ANISOU 1345 O CYS A 167 8028 4519 8395 1138 1749 1662 O ATOM 1346 CB CYS A 167 12.056 -42.752 -27.764 1.00 63.19 C ANISOU 1346 CB CYS A 167 8931 6006 9073 675 1845 1392 C ATOM 1347 SG CYS A 167 12.271 -43.743 -29.248 1.00 84.33 S ANISOU 1347 SG CYS A 167 11466 8470 12103 623 1811 1065 S ATOM 1348 N ALA A 168 15.092 -43.046 -26.994 1.00 53.06 N ANISOU 1348 N ALA A 168 7709 4908 7544 1141 1552 1533 N ATOM 1349 CA ALA A 168 16.412 -43.423 -27.491 1.00 55.33 C ANISOU 1349 CA ALA A 168 7893 5246 7885 1311 1417 1403 C ATOM 1350 C ALA A 168 17.315 -44.050 -26.425 1.00 60.58 C ANISOU 1350 C ALA A 168 8637 5856 8525 1571 1350 1694 C ATOM 1351 O ALA A 168 18.150 -44.901 -26.736 1.00 62.34 O ANISOU 1351 O ALA A 168 8783 5946 8957 1762 1291 1643 O ATOM 1352 CB ALA A 168 17.098 -42.207 -28.097 1.00 45.06 C ANISOU 1352 CB ALA A 168 6472 4340 6311 1244 1276 1189 C ATOM 1353 N ALA A 169 17.156 -43.620 -25.177 1.00 59.89 N ANISOU 1353 N ALA A 169 8489 5945 8321 2264 434 1718 N ATOM 1354 CA ALA A 169 18.026 -44.075 -24.090 1.00 50.87 C ANISOU 1354 CA ALA A 169 7465 4826 7038 2497 399 1744 C ATOM 1355 C ALA A 169 17.718 -45.480 -23.537 1.00 55.88 C ANISOU 1355 C ALA A 169 8231 5375 7625 2597 622 1921 C ATOM 1356 O ALA A 169 18.652 -46.231 -23.262 1.00 65.25 O ANISOU 1356 O ALA A 169 9498 6535 8759 2736 603 1949 O ATOM 1357 CB ALA A 169 18.006 -43.060 -22.950 1.00 50.51 C ANISOU 1357 CB ALA A 169 7472 4899 6820 2698 292 1687 C ATOM 1358 N PRO A 170 16.426 -45.837 -23.347 1.00 55.05 N ANISOU 1358 N PRO A 170 8155 5215 7546 2542 855 2027 N ATOM 1359 CA PRO A 170 16.157 -47.175 -22.792 1.00 57.68 C ANISOU 1359 CA PRO A 170 8644 5416 7857 2633 1140 2194 C ATOM 1360 C PRO A 170 16.794 -48.372 -23.532 1.00 58.99 C ANISOU 1360 C PRO A 170 8799 5452 8164 2541 1230 2226 C ATOM 1361 O PRO A 170 17.216 -49.310 -22.855 1.00 57.10 O ANISOU 1361 O PRO A 170 8714 5171 7812 2678 1345 2308 O ATOM 1362 CB PRO A 170 14.627 -47.265 -22.845 1.00 62.95 C ANISOU 1362 CB PRO A 170 9256 6031 8632 2482 1393 2216 C ATOM 1363 CG PRO A 170 14.177 -45.857 -22.702 1.00 55.68 C ANISOU 1363 CG PRO A 170 8251 5258 7648 2487 1205 2116 C ATOM 1364 CD PRO A 170 15.184 -45.043 -23.464 1.00 53.44 C ANISOU 1364 CD PRO A 170 7862 5059 7385 2435 895 1989 C ATOM 1365 N PRO A 171 16.874 -48.354 -24.878 1.00 58.09 N ANISOU 1365 N PRO A 171 8487 5329 8254 2273 1160 2110 N ATOM 1366 CA PRO A 171 17.555 -49.499 -25.498 1.00 54.21 C ANISOU 1366 CA PRO A 171 7990 4718 7890 2200 1243 2131 C ATOM 1367 C PRO A 171 19.040 -49.616 -25.143 1.00 60.07 C ANISOU 1367 C PRO A 171 8820 5487 8516 2408 1052 2124 C ATOM 1368 O PRO A 171 19.633 -50.662 -25.391 1.00 74.05 O ANISOU 1368 O PRO A 171 10617 7170 10347 2395 1129 2147 O ATOM 1369 CB PRO A 171 17.381 -49.236 -26.999 1.00 50.88 C ANISOU 1369 CB PRO A 171 7338 4326 7667 1898 1161 1981 C ATOM 1370 CG PRO A 171 16.158 -48.400 -27.092 1.00 56.92 C ANISOU 1370 CG PRO A 171 8012 5179 8437 1817 1167 1927 C ATOM 1371 CD PRO A 171 16.206 -47.512 -25.889 1.00 57.02 C ANISOU 1371 CD PRO A 171 8154 5272 8240 2045 1063 1976 C ATOM 1372 N LEU A 172 19.630 -48.567 -24.577 1.00 72.30 N ANISOU 1372 N LEU A 172 10380 7185 9907 2572 797 2036 N ATOM 1373 CA LEU A 172 21.030 -48.620 -24.164 1.00 63.29 C ANISOU 1373 CA LEU A 172 9268 6123 8654 2770 589 1941 C ATOM 1374 C LEU A 172 21.181 -49.279 -22.801 1.00 67.86 C ANISOU 1374 C LEU A 172 10037 6770 8976 3039 644 2020 C ATOM 1375 O LEU A 172 22.278 -49.700 -22.431 1.00 73.40 O ANISOU 1375 O LEU A 172 10778 7531 9579 3231 515 1960 O ATOM 1376 CB LEU A 172 21.645 -47.217 -24.118 1.00 59.05 C ANISOU 1376 CB LEU A 172 8623 5732 8081 2808 309 1738 C ATOM 1377 CG LEU A 172 21.770 -46.392 -25.400 1.00 56.83 C ANISOU 1377 CG LEU A 172 8151 5442 8001 2495 218 1577 C ATOM 1378 CD1 LEU A 172 22.339 -45.028 -25.065 1.00 50.59 C ANISOU 1378 CD1 LEU A 172 7290 4771 7163 2556 10 1369 C ATOM 1379 CD2 LEU A 172 22.643 -47.087 -26.425 1.00 55.63 C ANISOU 1379 CD2 LEU A 172 7912 5205 8019 2343 208 1508 C ATOM 1380 N VAL A 173 20.085 -49.368 -22.052 1.00 65.45 N ANISOU 1380 N VAL A 173 9855 6454 8559 3075 847 2148 N ATOM 1381 CA VAL A 173 20.159 -49.854 -20.677 1.00 65.71 C ANISOU 1381 CA VAL A 173 10105 6556 8308 3360 926 2233 C ATOM 1382 C VAL A 173 19.267 -51.060 -20.384 1.00 74.32 C ANISOU 1382 C VAL A 173 11365 7472 9399 3330 1333 2428 C ATOM 1383 O VAL A 173 18.997 -51.362 -19.221 1.00 79.97 O ANISOU 1383 O VAL A 173 12294 8216 9875 3552 1482 2529 O ATOM 1384 CB VAL A 173 19.809 -48.735 -19.670 1.00 69.29 C ANISOU 1384 CB VAL A 173 10601 7175 8550 3528 811 2187 C ATOM 1385 CG1 VAL A 173 20.922 -47.703 -19.622 1.00 76.41 C ANISOU 1385 CG1 VAL A 173 11370 8259 9402 3651 437 1962 C ATOM 1386 CG2 VAL A 173 18.477 -48.084 -20.022 1.00 60.73 C ANISOU 1386 CG2 VAL A 173 9447 6025 7602 3324 947 2231 C ATOM 1387 N GLY A 174 18.813 -51.752 -21.424 1.00 76.47 N ANISOU 1387 N GLY A 174 11549 7560 9947 3066 1541 2468 N ATOM 1388 CA GLY A 174 18.134 -53.020 -21.222 1.00 68.03 C ANISOU 1388 CA GLY A 174 10621 6296 8932 3031 1964 2614 C ATOM 1389 C GLY A 174 16.676 -53.123 -21.634 1.00 74.24 C ANISOU 1389 C GLY A 174 11340 6918 9952 2793 2300 2655 C ATOM 1390 O GLY A 174 16.119 -54.218 -21.640 1.00 81.35 O ANISOU 1390 O GLY A 174 12313 7618 10976 2715 2696 2733 O ATOM 1391 N TRP A 175 16.043 -52.001 -21.960 1.00 69.09 N ANISOU 1391 N TRP A 175 10541 6335 9376 2689 2169 2585 N ATOM 1392 CA TRP A 175 14.671 -52.050 -22.462 1.00 72.73 C ANISOU 1392 CA TRP A 175 10895 6638 10101 2473 2464 2588 C ATOM 1393 C TRP A 175 14.698 -51.973 -23.984 1.00 71.17 C ANISOU 1393 C TRP A 175 10425 6422 10196 2194 2351 2449 C ATOM 1394 O TRP A 175 14.948 -50.913 -24.554 1.00 68.87 O ANISOU 1394 O TRP A 175 9967 6318 9881 2124 2007 2315 O ATOM 1395 CB TRP A 175 13.820 -50.923 -21.874 1.00 69.59 C ANISOU 1395 CB TRP A 175 10501 6326 9613 2546 2420 2588 C ATOM 1396 CG TRP A 175 12.347 -51.191 -21.980 1.00 75.89 C ANISOU 1396 CG TRP A 175 11202 7007 10625 2339 2780 2537 C ATOM 1397 CD1 TRP A 175 11.751 -52.386 -22.275 1.00 67.99 C ANISOU 1397 CD1 TRP A 175 10184 5778 9870 2166 3205 2535 C ATOM 1398 CD2 TRP A 175 11.283 -50.247 -21.799 1.00 72.08 C ANISOU 1398 CD2 TRP A 175 10589 6645 10151 2265 2750 2423 C ATOM 1399 NE1 TRP A 175 10.384 -52.242 -22.286 1.00 69.88 N ANISOU 1399 NE1 TRP A 175 10268 6001 10282 1982 3441 2396 N ATOM 1400 CE2 TRP A 175 10.072 -50.939 -21.997 1.00 66.35 C ANISOU 1400 CE2 TRP A 175 9753 5773 9685 2049 3156 2334 C ATOM 1401 CE3 TRP A 175 11.238 -48.884 -21.489 1.00 71.11 C ANISOU 1401 CE3 TRP A 175 10422 6734 9863 2359 2435 2367 C ATOM 1402 CZ2 TRP A 175 8.830 -50.315 -21.893 1.00 69.41 C ANISOU 1402 CZ2 TRP A 175 9976 6239 10158 1940 3229 2182 C ATOM 1403 CZ3 TRP A 175 10.004 -48.267 -21.388 1.00 66.71 C ANISOU 1403 CZ3 TRP A 175 9728 6239 9381 2258 2512 2251 C ATOM 1404 CH2 TRP A 175 8.818 -48.982 -21.590 1.00 66.57 C ANISOU 1404 CH2 TRP A 175 9592 6092 9611 2057 2893 2156 C ATOM 1405 N SER A 176 14.423 -53.110 -24.621 1.00 70.11 N ANISOU 1405 N SER A 176 10223 6108 10308 2002 2642 2426 N ATOM 1406 CA SER A 176 14.700 -53.334 -26.040 1.00 62.79 C ANISOU 1406 CA SER A 176 9041 5213 9603 1737 2523 2256 C ATOM 1407 C SER A 176 16.208 -53.236 -26.282 1.00 63.02 C ANISOU 1407 C SER A 176 9125 5298 9522 1859 2215 2288 C ATOM 1408 O SER A 176 17.001 -53.363 -25.342 1.00 62.05 O ANISOU 1408 O SER A 176 9208 5203 9165 2115 2143 2394 O ATOM 1409 CB SER A 176 13.932 -52.352 -26.932 1.00 59.88 C ANISOU 1409 CB SER A 176 8388 5042 9323 1525 2323 2039 C ATOM 1410 OG SER A 176 14.107 -52.662 -28.304 1.00 58.10 O ANISOU 1410 OG SER A 176 7938 4849 9289 1292 2246 1874 O ATOM 1411 N ARG A 177 16.607 -53.019 -27.531 1.00 62.07 N ANISOU 1411 N ARG A 177 8789 5263 9532 1651 2009 2128 N ATOM 1412 CA ARG A 177 18.026 -52.983 -27.876 1.00 58.96 C ANISOU 1412 CA ARG A 177 8412 4902 9088 1719 1758 2113 C ATOM 1413 C ARG A 177 18.258 -52.434 -29.275 1.00 58.12 C ANISOU 1413 C ARG A 177 8074 4909 9100 1475 1539 1925 C ATOM 1414 O ARG A 177 17.345 -52.428 -30.103 1.00 58.66 O ANISOU 1414 O ARG A 177 7968 5013 9309 1258 1614 1811 O ATOM 1415 CB ARG A 177 18.633 -54.384 -27.773 1.00 54.81 C ANISOU 1415 CB ARG A 177 8004 4177 8643 1781 1977 2215 C ATOM 1416 CG ARG A 177 17.962 -55.388 -28.692 1.00 57.25 C ANISOU 1416 CG ARG A 177 8161 4343 9247 1494 2272 2136 C ATOM 1417 CD ARG A 177 18.698 -56.708 -28.706 1.00 64.77 C ANISOU 1417 CD ARG A 177 9200 5147 10265 1521 2443 2186 C ATOM 1418 NE ARG A 177 18.067 -57.680 -29.593 1.00 58.55 N ANISOU 1418 NE ARG A 177 8254 4187 9805 1243 2760 2092 N ATOM 1419 CZ ARG A 177 18.615 -58.843 -29.923 1.00 63.29 C ANISOU 1419 CZ ARG A 177 8851 4683 10514 1183 2910 2069 C ATOM 1420 NH1 ARG A 177 19.805 -59.168 -29.439 1.00 56.77 N ANISOU 1420 NH1 ARG A 177 8183 3894 9494 1400 2763 2153 N ATOM 1421 NH2 ARG A 177 17.980 -59.676 -30.737 1.00 57.01 N ANISOU 1421 NH2 ARG A 177 7877 3753 10031 911 3203 1934 N ATOM 1422 N TYR A 178 19.483 -51.976 -29.529 1.00 50.24 N ANISOU 1422 N TYR A 178 7077 3972 8040 1528 1279 1873 N ATOM 1423 CA TYR A 178 19.893 -51.574 -30.870 1.00 49.51 C ANISOU 1423 CA TYR A 178 6816 3943 8051 1313 1119 1715 C ATOM 1424 C TYR A 178 20.616 -52.733 -31.543 1.00 51.82 C ANISOU 1424 C TYR A 178 7063 4118 8506 1208 1211 1687 C ATOM 1425 O TYR A 178 21.522 -53.318 -30.965 1.00 56.11 O ANISOU 1425 O TYR A 178 7717 4583 9020 1371 1215 1753 O ATOM 1426 CB TYR A 178 20.800 -50.334 -30.835 1.00 54.03 C ANISOU 1426 CB TYR A 178 7402 4622 8506 1389 834 1635 C ATOM 1427 CG TYR A 178 20.106 -49.067 -30.385 1.00 53.47 C ANISOU 1427 CG TYR A 178 7351 4662 8302 1457 737 1633 C ATOM 1428 CD1 TYR A 178 19.140 -48.463 -31.179 1.00 51.14 C ANISOU 1428 CD1 TYR A 178 6960 4434 8037 1311 735 1579 C ATOM 1429 CD2 TYR A 178 20.427 -48.469 -29.175 1.00 54.57 C ANISOU 1429 CD2 TYR A 178 7604 4854 8278 1690 639 1668 C ATOM 1430 CE1 TYR A 178 18.501 -47.304 -30.773 1.00 47.69 C ANISOU 1430 CE1 TYR A 178 6548 4088 7486 1389 652 1580 C ATOM 1431 CE2 TYR A 178 19.796 -47.309 -28.759 1.00 49.64 C ANISOU 1431 CE2 TYR A 178 6991 4321 7548 1745 563 1655 C ATOM 1432 CZ TYR A 178 18.833 -46.732 -29.560 1.00 55.11 C ANISOU 1432 CZ TYR A 178 7596 5054 8288 1590 577 1621 C ATOM 1433 OH TYR A 178 18.208 -45.575 -29.149 1.00 58.05 O ANISOU 1433 OH TYR A 178 7987 5507 8560 1660 505 1611 O ATOM 1434 N ILE A 179 20.194 -53.072 -32.756 1.00 46.61 N ANISOU 1434 N ILE A 179 6239 3462 8010 958 1280 1575 N ATOM 1435 CA ILE A 179 20.852 -54.101 -33.558 1.00 46.03 C ANISOU 1435 CA ILE A 179 6092 3288 8109 821 1362 1514 C ATOM 1436 C ILE A 179 20.831 -53.636 -35.006 1.00 44.75 C ANISOU 1436 C ILE A 179 5763 3233 8007 598 1241 1344 C ATOM 1437 O ILE A 179 20.042 -52.757 -35.357 1.00 51.80 O ANISOU 1437 O ILE A 179 6601 4257 8822 562 1158 1290 O ATOM 1438 CB ILE A 179 20.162 -55.502 -33.437 1.00 58.46 C ANISOU 1438 CB ILE A 179 7650 4701 9863 751 1709 1556 C ATOM 1439 CG1 ILE A 179 18.701 -55.445 -33.888 1.00 53.79 C ANISOU 1439 CG1 ILE A 179 6895 4178 9364 581 1846 1444 C ATOM 1440 CG2 ILE A 179 20.270 -56.064 -32.022 1.00 49.49 C ANISOU 1440 CG2 ILE A 179 6745 3418 8643 1010 1879 1761 C ATOM 1441 CD1 ILE A 179 18.044 -56.817 -33.976 1.00 54.86 C ANISOU 1441 CD1 ILE A 179 6954 4143 9745 446 2225 1401 C ATOM 1442 N PRO A 180 21.708 -54.196 -35.854 1.00 47.23 N ANISOU 1442 N PRO A 180 6013 3494 8438 474 1230 1259 N ATOM 1443 CA PRO A 180 21.621 -53.836 -37.276 1.00 43.58 C ANISOU 1443 CA PRO A 180 5418 3133 8008 278 1150 1104 C ATOM 1444 C PRO A 180 20.264 -54.223 -37.863 1.00 51.28 C ANISOU 1444 C PRO A 180 6236 4188 9061 151 1281 1006 C ATOM 1445 O PRO A 180 19.681 -55.225 -37.449 1.00 47.88 O ANISOU 1445 O PRO A 180 5756 3664 8771 121 1511 1016 O ATOM 1446 CB PRO A 180 22.759 -54.642 -37.912 1.00 43.84 C ANISOU 1446 CB PRO A 180 5410 3067 8182 171 1175 1035 C ATOM 1447 CG PRO A 180 23.738 -54.846 -36.798 1.00 43.86 C ANISOU 1447 CG PRO A 180 5544 2963 8158 367 1143 1140 C ATOM 1448 CD PRO A 180 22.895 -55.021 -35.563 1.00 48.30 C ANISOU 1448 CD PRO A 180 6209 3495 8648 542 1259 1294 C ATOM 1449 N GLU A 181 19.757 -53.420 -38.793 1.00 60.66 N ANISOU 1449 N GLU A 181 7350 5543 10155 97 1152 897 N ATOM 1450 CA GLU A 181 18.443 -53.665 -39.378 1.00 60.48 C ANISOU 1450 CA GLU A 181 7143 5655 10182 17 1225 745 C ATOM 1451 C GLU A 181 18.562 -53.867 -40.880 1.00 45.04 C ANISOU 1451 C GLU A 181 5053 3809 8249 -124 1171 558 C ATOM 1452 O GLU A 181 19.522 -53.404 -41.501 1.00 49.40 O ANISOU 1452 O GLU A 181 5701 4355 8716 -137 1049 577 O ATOM 1453 CB GLU A 181 17.487 -52.502 -39.076 1.00 68.56 C ANISOU 1453 CB GLU A 181 8193 6829 11028 153 1102 762 C ATOM 1454 CG GLU A 181 17.934 -51.167 -39.663 1.00 76.06 C ANISOU 1454 CG GLU A 181 9266 7871 11761 238 873 792 C ATOM 1455 CD GLU A 181 16.944 -50.038 -39.413 1.00101.75 C ANISOU 1455 CD GLU A 181 12550 11266 14845 391 762 808 C ATOM 1456 OE1 GLU A 181 15.807 -50.320 -38.972 1.00107.74 O ANISOU 1456 OE1 GLU A 181 13183 12093 15659 410 843 745 O ATOM 1457 OE2 GLU A 181 17.306 -48.864 -39.658 1.00105.20 O ANISOU 1457 OE2 GLU A 181 13137 11727 15108 489 618 871 O ATOM 1458 N GLY A 182 17.575 -54.546 -41.456 1.00 46.42 N ANISOU 1458 N GLY A 182 5003 4092 8544 -227 1277 352 N ATOM 1459 CA GLY A 182 17.514 -54.775 -42.889 1.00 53.20 C ANISOU 1459 CA GLY A 182 5706 5104 9402 -333 1219 133 C ATOM 1460 C GLY A 182 18.774 -55.367 -43.490 1.00 51.72 C ANISOU 1460 C GLY A 182 5557 4794 9300 -461 1249 137 C ATOM 1461 O GLY A 182 19.109 -56.530 -43.256 1.00 51.69 O ANISOU 1461 O GLY A 182 5482 4627 9532 -585 1444 116 O ATOM 1462 N MET A 183 19.479 -54.554 -44.269 1.00 45.51 N ANISOU 1462 N MET A 183 4897 4066 8327 -426 1080 165 N ATOM 1463 CA MET A 183 20.690 -54.993 -44.949 1.00 46.46 C ANISOU 1463 CA MET A 183 5050 4084 8518 -552 1104 141 C ATOM 1464 C MET A 183 21.903 -54.945 -44.023 1.00 53.14 C ANISOU 1464 C MET A 183 6062 4701 9426 -526 1120 326 C ATOM 1465 O MET A 183 23.037 -55.144 -44.466 1.00 49.63 O ANISOU 1465 O MET A 183 5658 4159 9039 -612 1124 307 O ATOM 1466 CB MET A 183 20.929 -54.144 -46.197 1.00 51.78 C ANISOU 1466 CB MET A 183 5810 4899 8967 -522 964 81 C ATOM 1467 CG MET A 183 19.851 -54.324 -47.256 1.00 62.92 C ANISOU 1467 CG MET A 183 7040 6577 10292 -513 920 -149 C ATOM 1468 SD MET A 183 20.022 -53.197 -48.654 1.00 69.65 S ANISOU 1468 SD MET A 183 8076 7603 10786 -378 759 -171 S ATOM 1469 CE MET A 183 21.619 -53.697 -49.299 1.00 66.05 C ANISOU 1469 CE MET A 183 7703 6949 10444 -579 864 -167 C ATOM 1470 N GLN A 184 21.640 -54.670 -42.744 1.00 43.54 N ANISOU 1470 N GLN A 184 4930 3422 8192 -392 1125 477 N ATOM 1471 CA GLN A 184 22.609 -54.831 -41.659 1.00 54.07 C ANISOU 1471 CA GLN A 184 6386 4572 9586 -315 1144 621 C ATOM 1472 C GLN A 184 23.722 -53.783 -41.692 1.00 51.90 C ANISOU 1472 C GLN A 184 6258 4266 9195 -260 992 658 C ATOM 1473 O GLN A 184 24.804 -54.005 -41.148 1.00 57.05 O ANISOU 1473 O GLN A 184 6961 4795 9922 -225 983 686 O ATOM 1474 CB GLN A 184 23.221 -56.245 -41.689 1.00 48.41 C ANISOU 1474 CB GLN A 184 5590 3701 9102 -422 1307 583 C ATOM 1475 CG GLN A 184 22.206 -57.391 -41.703 1.00 44.90 C ANISOU 1475 CG GLN A 184 4989 3235 8836 -515 1531 510 C ATOM 1476 CD GLN A 184 21.342 -57.428 -40.458 1.00 53.92 C ANISOU 1476 CD GLN A 184 6192 4329 9967 -380 1641 639 C ATOM 1477 OE1 GLN A 184 21.808 -57.784 -39.373 1.00 49.92 O ANISOU 1477 OE1 GLN A 184 5828 3660 9480 -244 1719 805 O ATOM 1478 NE2 GLN A 184 20.074 -57.059 -40.608 1.00 49.44 N ANISOU 1478 NE2 GLN A 184 5521 3911 9354 -393 1649 552 N ATOM 1479 N CYS A 185 23.447 -52.642 -42.314 1.00 45.90 N ANISOU 1479 N CYS A 185 5566 3614 8259 -238 890 639 N ATOM 1480 CA CYS A 185 24.436 -51.574 -42.425 1.00 50.70 C ANISOU 1480 CA CYS A 185 6318 4161 8785 -211 810 647 C ATOM 1481 C CYS A 185 24.105 -50.383 -41.539 1.00 52.81 C ANISOU 1481 C CYS A 185 6707 4449 8907 -43 724 748 C ATOM 1482 O CYS A 185 24.957 -49.527 -41.301 1.00 57.91 O ANISOU 1482 O CYS A 185 7456 5017 9531 -12 685 738 O ATOM 1483 CB CYS A 185 24.565 -51.116 -43.875 1.00 50.85 C ANISOU 1483 CB CYS A 185 6380 4229 8711 -305 815 560 C ATOM 1484 SG CYS A 185 25.351 -52.345 -44.929 1.00 55.12 S ANISOU 1484 SG CYS A 185 6796 4718 9429 -520 914 412 S ATOM 1485 N SER A 186 22.863 -50.320 -41.069 1.00 52.76 N ANISOU 1485 N SER A 186 6238 5020 8787 1220 1310 171 N ATOM 1486 CA SER A 186 22.477 -49.298 -40.105 1.00 55.55 C ANISOU 1486 CA SER A 186 6621 5412 9075 1161 1345 310 C ATOM 1487 C SER A 186 21.808 -49.965 -38.912 1.00 52.45 C ANISOU 1487 C SER A 186 6364 4844 8718 1146 1343 433 C ATOM 1488 O SER A 186 21.253 -51.057 -39.033 1.00 60.33 O ANISOU 1488 O SER A 186 7433 5682 9808 1125 1349 420 O ATOM 1489 CB SER A 186 21.560 -48.243 -40.746 1.00 57.53 C ANISOU 1489 CB SER A 186 6802 5788 9269 1052 1422 331 C ATOM 1490 OG SER A 186 20.568 -48.827 -41.571 1.00 73.57 O ANISOU 1490 OG SER A 186 8817 7808 11328 992 1445 272 O ATOM 1491 N CYS A 187 21.880 -49.313 -37.756 1.00 53.11 N ANISOU 1491 N CYS A 187 6479 4965 8737 1153 1344 543 N ATOM 1492 CA CYS A 187 21.348 -49.872 -36.519 1.00 46.84 C ANISOU 1492 CA CYS A 187 5803 4045 7947 1162 1345 685 C ATOM 1493 C CYS A 187 20.107 -49.118 -36.060 1.00 59.92 C ANISOU 1493 C CYS A 187 7472 5738 9557 1032 1405 776 C ATOM 1494 O CYS A 187 19.978 -47.918 -36.288 1.00 54.91 O ANISOU 1494 O CYS A 187 6760 5240 8863 978 1435 753 O ATOM 1495 CB CYS A 187 22.416 -49.851 -35.420 1.00 47.48 C ANISOU 1495 CB CYS A 187 5896 4184 7961 1307 1289 736 C ATOM 1496 SG CYS A 187 23.734 -51.088 -35.643 1.00 58.78 S ANISOU 1496 SG CYS A 187 7350 5542 9443 1508 1216 674 S ATOM 1497 N GLY A 188 19.190 -49.830 -35.413 1.00 52.59 N ANISOU 1497 N GLY A 188 6642 4679 8660 984 1433 885 N ATOM 1498 CA GLY A 188 17.980 -49.212 -34.914 1.00 53.20 C ANISOU 1498 CA GLY A 188 6726 4803 8683 869 1487 971 C ATOM 1499 C GLY A 188 17.332 -50.051 -33.836 1.00 55.95 C ANISOU 1499 C GLY A 188 7189 5022 9050 854 1513 1123 C ATOM 1500 O GLY A 188 17.859 -51.093 -33.450 1.00 56.73 O ANISOU 1500 O GLY A 188 7371 4977 9207 948 1498 1181 O ATOM 1501 N ILE A 189 16.185 -49.591 -33.350 1.00 47.81 N ANISOU 1501 N ILE A 189 6159 4042 7964 747 1563 1199 N ATOM 1502 CA ILE A 189 15.432 -50.302 -32.327 1.00 56.84 C ANISOU 1502 CA ILE A 189 7398 5085 9113 711 1607 1359 C ATOM 1503 C ILE A 189 14.995 -51.669 -32.840 1.00 55.46 C ANISOU 1503 C ILE A 189 7296 4680 9096 640 1660 1346 C ATOM 1504 O ILE A 189 14.537 -51.797 -33.974 1.00 58.46 O ANISOU 1504 O ILE A 189 7618 5047 9547 538 1680 1198 O ATOM 1505 CB ILE A 189 14.189 -49.491 -31.878 1.00 63.16 C ANISOU 1505 CB ILE A 189 8162 6014 9821 594 1654 1411 C ATOM 1506 CG1 ILE A 189 14.618 -48.219 -31.142 1.00 71.77 C ANISOU 1506 CG1 ILE A 189 9194 7298 10777 668 1617 1424 C ATOM 1507 CG2 ILE A 189 13.279 -50.331 -30.998 1.00 55.03 C ANISOU 1507 CG2 ILE A 189 7219 4880 8809 524 1720 1569 C ATOM 1508 CD1 ILE A 189 13.462 -47.327 -30.730 1.00 74.09 C ANISOU 1508 CD1 ILE A 189 9447 7725 10980 577 1660 1456 C ATOM 1509 N ASP A 190 15.163 -52.692 -32.008 1.00 59.99 N ANISOU 1509 N ASP A 190 7990 5078 9726 703 1689 1497 N ATOM 1510 CA ASP A 190 14.694 -54.030 -32.339 1.00 60.27 C ANISOU 1510 CA ASP A 190 8112 4842 9945 621 1770 1499 C ATOM 1511 C ASP A 190 13.200 -54.128 -32.040 1.00 65.39 C ANISOU 1511 C ASP A 190 8764 5472 10607 420 1869 1558 C ATOM 1512 O ASP A 190 12.794 -54.305 -30.892 1.00 67.13 O ANISOU 1512 O ASP A 190 9058 5668 10781 422 1922 1762 O ATOM 1513 CB ASP A 190 15.480 -55.086 -31.561 1.00 55.73 C ANISOU 1513 CB ASP A 190 7678 4062 9436 789 1787 1666 C ATOM 1514 CG ASP A 190 15.025 -56.499 -31.865 1.00 62.55 C ANISOU 1514 CG ASP A 190 8650 4588 10530 703 1898 1673 C ATOM 1515 OD1 ASP A 190 14.299 -56.701 -32.861 1.00 69.06 O ANISOU 1515 OD1 ASP A 190 9415 5355 11468 518 1939 1484 O ATOM 1516 OD2 ASP A 190 15.410 -57.418 -31.113 1.00 60.77 O ANISOU 1516 OD2 ASP A 190 8563 4154 10371 829 1952 1863 O ATOM 1517 N TYR A 191 12.385 -53.999 -33.081 1.00 59.91 N ANISOU 1517 N TYR A 191 7976 4826 9960 255 1895 1373 N ATOM 1518 CA TYR A 191 10.937 -54.020 -32.922 1.00 65.51 C ANISOU 1518 CA TYR A 191 8652 5571 10667 55 1984 1386 C ATOM 1519 C TYR A 191 10.352 -55.233 -33.624 1.00 72.16 C ANISOU 1519 C TYR A 191 9507 6190 11720 -108 2079 1254 C ATOM 1520 O TYR A 191 9.154 -55.279 -33.897 1.00 81.71 O ANISOU 1520 O TYR A 191 10639 7461 12944 -302 2149 1168 O ATOM 1521 CB TYR A 191 10.310 -52.732 -33.476 1.00 61.36 C ANISOU 1521 CB TYR A 191 7976 5349 9988 1 1945 1272 C ATOM 1522 CG TYR A 191 10.545 -52.531 -34.959 1.00 62.15 C ANISOU 1522 CG TYR A 191 7963 5538 10114 -1 1903 1037 C ATOM 1523 CD1 TYR A 191 11.682 -51.883 -35.420 1.00 49.57 C ANISOU 1523 CD1 TYR A 191 6337 4030 8465 155 1817 989 C ATOM 1524 CD2 TYR A 191 9.631 -52.998 -35.898 1.00 64.87 C ANISOU 1524 CD2 TYR A 191 8215 5905 10528 -158 1957 853 C ATOM 1525 CE1 TYR A 191 11.905 -51.706 -36.775 1.00 59.27 C ANISOU 1525 CE1 TYR A 191 7456 5362 9701 165 1788 795 C ATOM 1526 CE2 TYR A 191 9.846 -52.827 -37.255 1.00 63.56 C ANISOU 1526 CE2 TYR A 191 7926 5866 10357 -138 1918 639 C ATOM 1527 CZ TYR A 191 10.983 -52.181 -37.688 1.00 65.88 C ANISOU 1527 CZ TYR A 191 8201 6241 10589 29 1835 625 C ATOM 1528 OH TYR A 191 11.194 -52.005 -39.037 1.00 72.00 O ANISOU 1528 OH TYR A 191 8847 7166 11343 59 1805 432 O ATOM 1529 N TYR A 192 11.196 -56.220 -33.914 1.00 61.60 N ANISOU 1529 N TYR A 192 8256 4599 10549 -30 2085 1220 N ATOM 1530 CA TYR A 192 10.769 -57.325 -34.761 1.00 64.31 C ANISOU 1530 CA TYR A 192 8592 4727 11118 -182 2170 1027 C ATOM 1531 C TYR A 192 11.247 -58.709 -34.311 1.00 73.38 C ANISOU 1531 C TYR A 192 9918 5469 12494 -136 2262 1135 C ATOM 1532 O TYR A 192 10.773 -59.717 -34.830 1.00 83.32 O ANISOU 1532 O TYR A 192 11189 6491 13978 -291 2369 988 O ATOM 1533 CB TYR A 192 11.216 -57.068 -36.205 1.00 64.16 C ANISOU 1533 CB TYR A 192 8434 4847 11096 -152 2085 738 C ATOM 1534 CG TYR A 192 12.665 -56.667 -36.362 1.00 71.41 C ANISOU 1534 CG TYR A 192 9370 5821 11942 88 1964 758 C ATOM 1535 CD1 TYR A 192 13.055 -55.331 -36.274 1.00 64.37 C ANISOU 1535 CD1 TYR A 192 8404 5218 10834 192 1869 810 C ATOM 1536 CD2 TYR A 192 13.643 -57.620 -36.611 1.00 58.47 C ANISOU 1536 CD2 TYR A 192 7814 3942 10458 206 1957 711 C ATOM 1537 CE1 TYR A 192 14.379 -54.962 -36.423 1.00 57.80 C ANISOU 1537 CE1 TYR A 192 7572 4447 9945 386 1773 808 C ATOM 1538 CE2 TYR A 192 14.968 -57.261 -36.761 1.00 84.62 C ANISOU 1538 CE2 TYR A 192 11123 7335 13693 422 1847 714 C ATOM 1539 CZ TYR A 192 15.331 -55.932 -36.666 1.00 72.82 C ANISOU 1539 CZ TYR A 192 9544 6143 11983 500 1757 758 C ATOM 1540 OH TYR A 192 16.652 -55.580 -36.815 1.00 79.06 O ANISOU 1540 OH TYR A 192 10315 7021 12705 692 1661 743 O ATOM 1541 N THR A 193 12.177 -58.771 -33.361 1.00 74.24 N ANISOU 1541 N THR A 193 10159 5501 12550 83 2231 1382 N ATOM 1542 CA THR A 193 12.547 -60.066 -32.784 1.00 81.39 C ANISOU 1542 CA THR A 193 11250 6020 13653 158 2341 1548 C ATOM 1543 C THR A 193 12.030 -60.164 -31.353 1.00 89.18 C ANISOU 1543 C THR A 193 12348 6961 14576 158 2438 1885 C ATOM 1544 O THR A 193 12.120 -59.204 -30.585 1.00 84.13 O ANISOU 1544 O THR A 193 11671 6602 13694 253 2360 2033 O ATOM 1545 CB THR A 193 14.082 -60.326 -32.793 1.00 73.69 C ANISOU 1545 CB THR A 193 10350 4972 12677 455 2249 1589 C ATOM 1546 OG1 THR A 193 14.691 -59.766 -31.620 1.00 69.60 O ANISOU 1546 OG1 THR A 193 9880 4617 11946 667 2187 1857 O ATOM 1547 CG2 THR A 193 14.731 -59.754 -34.046 1.00 79.75 C ANISOU 1547 CG2 THR A 193 10970 5939 13394 497 2111 1295 C ATOM 1548 N PRO A 194 11.469 -61.328 -30.999 1.00 88.44 N ANISOU 1548 N PRO A 194 12384 6515 14706 44 2622 2000 N ATOM 1549 CA PRO A 194 10.972 -61.592 -29.645 1.00 93.31 C ANISOU 1549 CA PRO A 194 13097 7123 15233 47 2711 2317 C ATOM 1550 C PRO A 194 12.114 -61.837 -28.663 1.00 99.23 C ANISOU 1550 C PRO A 194 13966 7890 15847 375 2647 2581 C ATOM 1551 O PRO A 194 12.428 -62.985 -28.350 1.00118.04 O ANISOU 1551 O PRO A 194 16476 10040 18332 456 2709 2682 O ATOM 1552 CB PRO A 194 10.120 -62.850 -29.827 1.00 96.35 C ANISOU 1552 CB PRO A 194 13535 7221 15851 -184 2869 2244 C ATOM 1553 CG PRO A 194 10.743 -63.548 -30.992 1.00 96.81 C ANISOU 1553 CG PRO A 194 13601 7049 16132 -168 2855 1977 C ATOM 1554 CD PRO A 194 11.229 -62.461 -31.910 1.00 94.19 C ANISOU 1554 CD PRO A 194 13136 6916 15736 -111 2727 1775 C ATOM 1555 N HIS A 195 12.732 -60.760 -28.191 1.00 85.60 N ANISOU 1555 N HIS A 195 12188 6443 13893 567 2531 2685 N ATOM 1556 CA HIS A 195 13.855 -60.859 -27.266 1.00 83.40 C ANISOU 1556 CA HIS A 195 11985 6248 13455 895 2462 2910 C ATOM 1557 C HIS A 195 13.385 -60.535 -25.851 1.00 93.84 C ANISOU 1557 C HIS A 195 13319 7773 14562 941 2500 3203 C ATOM 1558 O HIS A 195 13.458 -59.385 -25.411 1.00 97.35 O ANISOU 1558 O HIS A 195 13674 8512 14804 1012 2428 3255 O ATOM 1559 CB HIS A 195 14.988 -59.917 -27.696 1.00 77.04 C ANISOU 1559 CB HIS A 195 11084 5661 12525 1092 2295 2782 C ATOM 1560 CG HIS A 195 16.332 -60.289 -27.147 1.00 79.32 C ANISOU 1560 CG HIS A 195 11447 5955 12734 1441 2237 2935 C ATOM 1561 ND1 HIS A 195 17.053 -59.459 -26.314 1.00 76.13 N ANISOU 1561 ND1 HIS A 195 10968 5909 12050 1659 2118 3031 N ATOM 1562 CD2 HIS A 195 17.089 -61.399 -27.318 1.00 83.96 C ANISOU 1562 CD2 HIS A 195 12136 6335 13430 1590 2242 2938 C ATOM 1563 CE1 HIS A 195 18.193 -60.044 -25.992 1.00 80.38 C ANISOU 1563 CE1 HIS A 195 11578 6400 12563 1965 2091 3148 C ATOM 1564 NE2 HIS A 195 18.240 -61.222 -26.588 1.00 81.66 N ANISOU 1564 NE2 HIS A 195 11846 6236 12944 1923 2154 3086 N ATOM 1565 N GLU A 196 12.898 -61.553 -25.146 1.00 96.21 N ANISOU 1565 N GLU A 196 13726 7916 14912 903 2622 3388 N ATOM 1566 CA GLU A 196 12.305 -61.370 -23.821 1.00 98.08 C ANISOU 1566 CA GLU A 196 13969 8338 14957 923 2681 3663 C ATOM 1567 C GLU A 196 13.318 -60.885 -22.788 1.00 87.38 C ANISOU 1567 C GLU A 196 12606 7261 13333 1271 2588 3880 C ATOM 1568 O GLU A 196 12.947 -60.336 -21.751 1.00 89.81 O ANISOU 1568 O GLU A 196 12867 7832 13424 1318 2597 4066 O ATOM 1569 CB GLU A 196 11.667 -62.674 -23.332 1.00107.06 C ANISOU 1569 CB GLU A 196 15231 9218 16229 826 2845 3822 C ATOM 1570 CG GLU A 196 10.522 -63.187 -24.192 1.00115.38 C ANISOU 1570 CG GLU A 196 16275 10028 17536 464 2959 3615 C ATOM 1571 CD GLU A 196 10.988 -64.128 -25.286 1.00129.26 C ANISOU 1571 CD GLU A 196 18099 11445 19570 433 2980 3405 C ATOM 1572 OE1 GLU A 196 12.174 -64.055 -25.673 1.00129.61 O ANISOU 1572 OE1 GLU A 196 18159 11488 19600 661 2869 3344 O ATOM 1573 OE2 GLU A 196 10.168 -64.947 -25.754 1.00136.45 O ANISOU 1573 OE2 GLU A 196 19036 12099 20711 182 3111 3289 O ATOM 1574 N GLU A 197 14.596 -61.096 -23.076 1.00 81.35 N ANISOU 1574 N GLU A 197 11872 6462 12573 1520 2500 3840 N ATOM 1575 CA GLU A 197 15.663 -60.730 -22.155 1.00 80.21 C ANISOU 1575 CA GLU A 197 11704 6598 12173 1876 2411 4019 C ATOM 1576 C GLU A 197 15.775 -59.212 -22.011 1.00 84.59 C ANISOU 1576 C GLU A 197 12105 7510 12525 1915 2300 3955 C ATOM 1577 O GLU A 197 16.242 -58.710 -20.989 1.00 87.01 O ANISOU 1577 O GLU A 197 12349 8146 12565 2146 2242 4108 O ATOM 1578 CB GLU A 197 16.986 -61.339 -22.626 1.00 79.17 C ANISOU 1578 CB GLU A 197 11627 6348 12108 2120 2341 3953 C ATOM 1579 CG GLU A 197 16.898 -62.849 -22.839 1.00 98.44 C ANISOU 1579 CG GLU A 197 14225 8404 14773 2084 2457 4002 C ATOM 1580 CD GLU A 197 18.205 -63.467 -23.295 1.00122.75 C ANISOU 1580 CD GLU A 197 17356 11376 17910 2338 2387 3935 C ATOM 1581 OE1 GLU A 197 18.819 -62.939 -24.246 1.00127.07 O ANISOU 1581 OE1 GLU A 197 17823 11959 18497 2353 2272 3686 O ATOM 1582 OE2 GLU A 197 18.618 -64.487 -22.703 1.00136.29 O ANISOU 1582 OE2 GLU A 197 19186 12973 19626 2529 2453 4136 O ATOM 1583 N THR A 198 15.336 -58.484 -23.035 1.00 69.80 N ANISOU 1583 N THR A 198 10136 5645 10742 1667 2243 3656 N ATOM 1584 CA THR A 198 15.293 -57.027 -22.971 1.00 81.72 C ANISOU 1584 CA THR A 198 11456 7556 12037 1610 2101 3460 C ATOM 1585 C THR A 198 13.853 -56.519 -23.035 1.00 84.80 C ANISOU 1585 C THR A 198 11792 7989 12439 1309 2164 3409 C ATOM 1586 O THR A 198 13.622 -55.314 -23.176 1.00 73.21 O ANISOU 1586 O THR A 198 10178 6793 10844 1221 2069 3222 O ATOM 1587 CB THR A 198 16.120 -56.367 -24.106 1.00 69.09 C ANISOU 1587 CB THR A 198 9750 6028 10473 1606 1955 3124 C ATOM 1588 OG1 THR A 198 15.828 -56.999 -25.359 1.00 74.03 O ANISOU 1588 OG1 THR A 198 10435 6327 11367 1434 2008 2971 O ATOM 1589 CG2 THR A 198 17.609 -56.482 -23.822 1.00 64.99 C ANISOU 1589 CG2 THR A 198 9217 5630 9846 1924 1855 3141 C ATOM 1590 N ASN A 199 12.899 -57.445 -22.924 1.00 82.12 N ANISOU 1590 N ASN A 199 11568 7377 12258 1156 2336 3576 N ATOM 1591 CA ASN A 199 11.471 -57.122 -22.947 1.00 77.76 C ANISOU 1591 CA ASN A 199 10962 6863 11720 868 2415 3541 C ATOM 1592 C ASN A 199 11.069 -56.260 -24.137 1.00 69.64 C ANISOU 1592 C ASN A 199 9801 5921 10737 662 2329 3191 C ATOM 1593 O ASN A 199 10.523 -55.169 -23.967 1.00 72.81 O ANISOU 1593 O ASN A 199 10076 6610 10977 586 2270 3101 O ATOM 1594 CB ASN A 199 11.065 -56.423 -21.651 1.00 77.35 C ANISOU 1594 CB ASN A 199 10838 7158 11393 934 2405 3717 C ATOM 1595 CG ASN A 199 11.252 -57.302 -20.437 1.00 87.61 C ANISOU 1595 CG ASN A 199 12259 8404 12624 1129 2519 4102 C ATOM 1596 OD1 ASN A 199 12.086 -57.021 -19.578 1.00 92.47 O ANISOU 1596 OD1 ASN A 199 12842 9274 13017 1407 2439 4223 O ATOM 1597 ND2 ASN A 199 10.474 -58.376 -20.359 1.00 88.60 N ANISOU 1597 ND2 ASN A 199 12483 8278 12903 968 2663 4200 N ATOM 1598 N ASN A 200 11.342 -56.756 -25.338 1.00 64.41 N ANISOU 1598 N ASN A 200 9165 5019 10289 592 2327 3000 N ATOM 1599 CA ASN A 200 11.086 -56.004 -26.557 1.00 65.25 C ANISOU 1599 CA ASN A 200 9142 5222 10427 439 2247 2680 C ATOM 1600 C ASN A 200 9.607 -55.699 -26.772 1.00 60.79 C ANISOU 1600 C ASN A 200 8497 4733 9867 168 2321 2603 C ATOM 1601 O ASN A 200 9.250 -54.600 -27.188 1.00 63.28 O ANISOU 1601 O ASN A 200 8679 5298 10067 106 2242 2435 O ATOM 1602 CB ASN A 200 11.643 -56.760 -27.765 1.00 62.80 C ANISOU 1602 CB ASN A 200 8872 4648 10341 427 2245 2500 C ATOM 1603 CG ASN A 200 13.154 -56.658 -27.872 1.00 67.84 C ANISOU 1603 CG ASN A 200 9523 5320 10932 689 2124 2472 C ATOM 1604 OD1 ASN A 200 13.835 -56.303 -26.909 1.00 64.58 O ANISOU 1604 OD1 ASN A 200 9117 5077 10344 895 2066 2627 O ATOM 1605 ND2 ASN A 200 13.684 -56.965 -29.049 1.00 69.18 N ANISOU 1605 ND2 ASN A 200 9678 5362 11247 685 2085 2257 N ATOM 1606 N GLU A 201 8.757 -56.676 -26.476 1.00 68.33 N ANISOU 1606 N GLU A 201 9532 5472 10959 13 2483 2731 N ATOM 1607 CA GLU A 201 7.322 -56.566 -26.719 1.00 68.67 C ANISOU 1607 CA GLU A 201 9488 5576 11026 -263 2571 2640 C ATOM 1608 C GLU A 201 6.712 -55.339 -26.051 1.00 72.04 C ANISOU 1608 C GLU A 201 9800 6380 11193 -264 2511 2675 C ATOM 1609 O GLU A 201 6.002 -54.562 -26.690 1.00 68.09 O ANISOU 1609 O GLU A 201 9164 6075 10631 -388 2471 2475 O ATOM 1610 CB GLU A 201 6.609 -57.831 -26.234 1.00 72.52 C ANISOU 1610 CB GLU A 201 10090 5768 11696 -417 2778 2822 C ATOM 1611 CG GLU A 201 5.096 -57.704 -26.182 1.00 89.94 C ANISOU 1611 CG GLU A 201 12196 8090 13887 -697 2882 2771 C ATOM 1612 CD GLU A 201 4.416 -58.988 -25.761 1.00103.21 C ANISOU 1612 CD GLU A 201 13974 9490 15750 -870 3077 2902 C ATOM 1613 OE1 GLU A 201 4.859 -60.068 -26.206 1.00109.11 O ANISOU 1613 OE1 GLU A 201 14822 9921 16713 -872 3118 2841 O ATOM 1614 OE2 GLU A 201 3.443 -58.918 -24.980 1.00106.44 O ANISOU 1614 OE2 GLU A 201 14345 10048 16050 -989 3149 3022 O ATOM 1615 N SER A 202 7.007 -55.165 -24.768 1.00 73.13 N ANISOU 1615 N SER A 202 9985 6634 11168 -103 2506 2926 N ATOM 1616 CA SER A 202 6.462 -54.052 -24.004 1.00 65.95 C ANISOU 1616 CA SER A 202 8967 6079 10011 -87 2456 2960 C ATOM 1617 C SER A 202 6.991 -52.706 -24.503 1.00 72.39 C ANISOU 1617 C SER A 202 9666 7137 10700 13 2291 2742 C ATOM 1618 O SER A 202 6.272 -51.707 -24.477 1.00 72.88 O ANISOU 1618 O SER A 202 9613 7445 10632 -51 2259 2647 O ATOM 1619 CB SER A 202 6.776 -54.228 -22.516 1.00 62.56 C ANISOU 1619 CB SER A 202 8601 5743 9426 89 2485 3266 C ATOM 1620 OG SER A 202 8.170 -54.192 -22.275 1.00 74.60 O ANISOU 1620 OG SER A 202 10172 7274 10899 353 2386 3310 O ATOM 1621 N PHE A 203 8.238 -52.680 -24.968 1.00 66.51 N ANISOU 1621 N PHE A 203 8952 6315 10002 169 2199 2664 N ATOM 1622 CA PHE A 203 8.827 -51.438 -25.464 1.00 62.78 C ANISOU 1622 CA PHE A 203 8376 6039 9437 254 2067 2467 C ATOM 1623 C PHE A 203 8.192 -51.012 -26.782 1.00 61.06 C ANISOU 1623 C PHE A 203 8072 5832 9295 96 2063 2235 C ATOM 1624 O PHE A 203 7.979 -49.825 -27.016 1.00 63.30 O ANISOU 1624 O PHE A 203 8254 6326 9471 102 2008 2115 O ATOM 1625 CB PHE A 203 10.341 -51.576 -25.640 1.00 59.04 C ANISOU 1625 CB PHE A 203 7943 5494 8994 452 1980 2439 C ATOM 1626 CG PHE A 203 11.022 -50.288 -26.028 1.00 59.61 C ANISOU 1626 CG PHE A 203 7909 5763 8978 532 1866 2252 C ATOM 1627 CD1 PHE A 203 11.377 -49.361 -25.062 1.00 59.74 C ANISOU 1627 CD1 PHE A 203 7860 6026 8815 650 1808 2273 C ATOM 1628 CD2 PHE A 203 11.297 -50.002 -27.356 1.00 57.39 C ANISOU 1628 CD2 PHE A 203 7585 5425 8797 484 1830 2048 C ATOM 1629 CE1 PHE A 203 11.998 -48.175 -25.412 1.00 57.95 C ANISOU 1629 CE1 PHE A 203 7535 5943 8539 701 1729 2089 C ATOM 1630 CE2 PHE A 203 11.920 -48.819 -27.711 1.00 48.92 C ANISOU 1630 CE2 PHE A 203 6421 4508 7660 549 1753 1899 C ATOM 1631 CZ PHE A 203 12.270 -47.904 -26.738 1.00 57.67 C ANISOU 1631 CZ PHE A 203 7474 5821 8619 647 1710 1917 C ATOM 1632 N VAL A 204 7.903 -51.985 -27.640 1.00 62.85 N ANISOU 1632 N VAL A 204 8336 5838 9706 -32 2128 2167 N ATOM 1633 CA VAL A 204 7.255 -51.710 -28.917 1.00 71.80 C ANISOU 1633 CA VAL A 204 9367 7019 10894 -173 2130 1940 C ATOM 1634 C VAL A 204 5.851 -51.142 -28.693 1.00 66.97 C ANISOU 1634 C VAL A 204 8658 6618 10170 -314 2180 1927 C ATOM 1635 O VAL A 204 5.419 -50.233 -29.402 1.00 57.50 O ANISOU 1635 O VAL A 204 7343 5611 8893 -333 2142 1776 O ATOM 1636 CB VAL A 204 7.173 -52.980 -29.792 1.00 68.70 C ANISOU 1636 CB VAL A 204 9018 6360 10726 -295 2201 1843 C ATOM 1637 CG1 VAL A 204 6.449 -52.688 -31.094 1.00 73.82 C ANISOU 1637 CG1 VAL A 204 9526 7126 11395 -430 2200 1590 C ATOM 1638 CG2 VAL A 204 8.563 -53.506 -30.077 1.00 75.90 C ANISOU 1638 CG2 VAL A 204 10017 7079 11742 -136 2147 1838 C ATOM 1639 N ILE A 205 5.148 -51.681 -27.701 1.00 61.41 N ANISOU 1639 N ILE A 205 7998 5887 9449 -398 2272 2099 N ATOM 1640 CA ILE A 205 3.833 -51.175 -27.327 1.00 66.30 C ANISOU 1640 CA ILE A 205 8520 6729 9943 -521 2320 2104 C ATOM 1641 C ILE A 205 3.950 -49.752 -26.787 1.00 63.36 C ANISOU 1641 C ILE A 205 8081 6634 9359 -375 2229 2112 C ATOM 1642 O ILE A 205 3.176 -48.870 -27.156 1.00 62.79 O ANISOU 1642 O ILE A 205 7895 6775 9188 -413 2214 1997 O ATOM 1643 CB ILE A 205 3.163 -52.072 -26.274 1.00 62.34 C ANISOU 1643 CB ILE A 205 8083 6140 9463 -632 2450 2316 C ATOM 1644 CG1 ILE A 205 2.971 -53.485 -26.826 1.00 66.60 C ANISOU 1644 CG1 ILE A 205 8689 6363 10251 -804 2571 2289 C ATOM 1645 CG2 ILE A 205 1.823 -51.495 -25.847 1.00 62.35 C ANISOU 1645 CG2 ILE A 205 7966 6411 9312 -752 2494 2314 C ATOM 1646 CD1 ILE A 205 2.478 -54.471 -25.799 1.00 63.83 C ANISOU 1646 CD1 ILE A 205 8432 5857 9962 -905 2728 2534 C ATOM 1647 N TYR A 206 4.930 -49.543 -25.913 1.00 61.50 N ANISOU 1647 N TYR A 206 7911 6398 9058 -201 2172 2238 N ATOM 1648 CA TYR A 206 5.221 -48.225 -25.367 1.00 57.35 C ANISOU 1648 CA TYR A 206 7321 6107 8361 -60 2089 2213 C ATOM 1649 C TYR A 206 5.529 -47.224 -26.477 1.00 59.51 C ANISOU 1649 C TYR A 206 7524 6438 8650 -18 2022 2007 C ATOM 1650 O TYR A 206 5.040 -46.097 -26.451 1.00 59.24 O ANISOU 1650 O TYR A 206 7405 6597 8507 4 2006 1935 O ATOM 1651 CB TYR A 206 6.387 -48.307 -24.380 1.00 64.43 C ANISOU 1651 CB TYR A 206 8281 6998 9202 122 2038 2339 C ATOM 1652 CG TYR A 206 7.151 -47.014 -24.212 1.00 68.91 C ANISOU 1652 CG TYR A 206 8780 7736 9668 269 1939 2222 C ATOM 1653 CD1 TYR A 206 6.630 -45.968 -23.461 1.00 69.08 C ANISOU 1653 CD1 TYR A 206 8714 8003 9529 297 1926 2199 C ATOM 1654 CD2 TYR A 206 8.399 -46.842 -24.797 1.00 66.63 C ANISOU 1654 CD2 TYR A 206 8506 7360 9452 371 1870 2121 C ATOM 1655 CE1 TYR A 206 7.329 -44.785 -23.305 1.00 60.56 C ANISOU 1655 CE1 TYR A 206 7569 7050 8390 413 1856 2066 C ATOM 1656 CE2 TYR A 206 9.104 -45.664 -24.647 1.00 66.12 C ANISOU 1656 CE2 TYR A 206 8369 7434 9318 477 1801 1997 C ATOM 1657 CZ TYR A 206 8.564 -44.640 -23.899 1.00 63.78 C ANISOU 1657 CZ TYR A 206 7993 7354 8886 492 1800 1966 C ATOM 1658 OH TYR A 206 9.264 -43.467 -23.746 1.00 63.69 O ANISOU 1658 OH TYR A 206 7909 7452 8838 581 1751 1818 O ATOM 1659 N MET A 207 6.336 -47.645 -27.446 1.00 59.64 N ANISOU 1659 N MET A 207 7576 6283 8800 2 1995 1922 N ATOM 1660 CA MET A 207 6.652 -46.824 -28.613 1.00 54.16 C ANISOU 1660 CA MET A 207 6817 5633 8127 40 1951 1749 C ATOM 1661 C MET A 207 5.408 -46.443 -29.390 1.00 59.67 C ANISOU 1661 C MET A 207 7417 6467 8789 -65 1994 1650 C ATOM 1662 O MET A 207 5.173 -45.268 -29.680 1.00 57.89 O ANISOU 1662 O MET A 207 7120 6400 8476 -4 1980 1584 O ATOM 1663 CB MET A 207 7.608 -47.562 -29.547 1.00 54.92 C ANISOU 1663 CB MET A 207 6960 5536 8372 63 1925 1679 C ATOM 1664 CG MET A 207 9.035 -47.572 -29.080 1.00 68.03 C ANISOU 1664 CG MET A 207 8680 7123 10045 215 1860 1721 C ATOM 1665 SD MET A 207 9.723 -45.923 -29.169 1.00 84.83 S ANISOU 1665 SD MET A 207 10728 9418 12084 333 1801 1618 S ATOM 1666 CE MET A 207 9.736 -45.670 -30.946 1.00 87.56 C ANISOU 1666 CE MET A 207 11016 9741 12514 299 1808 1458 C ATOM 1667 N PHE A 208 4.627 -47.461 -29.734 1.00 57.05 N ANISOU 1667 N PHE A 208 7078 6070 8528 -219 2058 1635 N ATOM 1668 CA PHE A 208 3.431 -47.300 -30.545 1.00 58.15 C ANISOU 1668 CA PHE A 208 7100 6367 8629 -328 2101 1513 C ATOM 1669 C PHE A 208 2.451 -46.318 -29.915 1.00 61.19 C ANISOU 1669 C PHE A 208 7409 6999 8840 -314 2115 1549 C ATOM 1670 O PHE A 208 1.920 -45.443 -30.591 1.00 59.94 O ANISOU 1670 O PHE A 208 7151 7028 8594 -270 2111 1454 O ATOM 1671 CB PHE A 208 2.752 -48.657 -30.755 1.00 54.00 C ANISOU 1671 CB PHE A 208 6573 5723 8222 -526 2182 1481 C ATOM 1672 CG PHE A 208 1.608 -48.619 -31.724 1.00 55.47 C ANISOU 1672 CG PHE A 208 6607 6097 8372 -644 2222 1304 C ATOM 1673 CD1 PHE A 208 1.837 -48.699 -33.089 1.00 55.89 C ANISOU 1673 CD1 PHE A 208 6586 6174 8476 -631 2198 1120 C ATOM 1674 CD2 PHE A 208 0.303 -48.509 -31.272 1.00 52.43 C ANISOU 1674 CD2 PHE A 208 6135 5904 7884 -760 2284 1312 C ATOM 1675 CE1 PHE A 208 0.784 -48.664 -33.987 1.00 53.09 C ANISOU 1675 CE1 PHE A 208 6065 6049 8059 -720 2230 943 C ATOM 1676 CE2 PHE A 208 -0.755 -48.473 -32.166 1.00 59.85 C ANISOU 1676 CE2 PHE A 208 6908 7063 8768 -857 2317 1130 C ATOM 1677 CZ PHE A 208 -0.512 -48.552 -33.525 1.00 56.91 C ANISOU 1677 CZ PHE A 208 6457 6731 8438 -832 2289 943 C ATOM 1678 N VAL A 209 2.222 -46.468 -28.615 1.00 60.26 N ANISOU 1678 N VAL A 209 7337 6894 8666 -333 2137 1694 N ATOM 1679 CA VAL A 209 1.240 -45.655 -27.914 1.00 60.65 C ANISOU 1679 CA VAL A 209 7309 7186 8549 -328 2155 1725 C ATOM 1680 C VAL A 209 1.753 -44.245 -27.644 1.00 65.93 C ANISOU 1680 C VAL A 209 7967 7960 9124 -145 2094 1707 C ATOM 1681 O VAL A 209 1.129 -43.261 -28.041 1.00 62.05 O ANISOU 1681 O VAL A 209 7391 7642 8543 -93 2098 1629 O ATOM 1682 CB VAL A 209 0.832 -46.303 -26.579 1.00 59.82 C ANISOU 1682 CB VAL A 209 7245 7083 8401 -404 2207 1893 C ATOM 1683 CG1 VAL A 209 -0.089 -45.376 -25.795 1.00 58.99 C ANISOU 1683 CG1 VAL A 209 7052 7255 8106 -374 2214 1913 C ATOM 1684 CG2 VAL A 209 0.155 -47.644 -26.829 1.00 54.81 C ANISOU 1684 CG2 VAL A 209 6616 6330 7879 -615 2304 1907 C ATOM 1685 N VAL A 210 2.897 -44.157 -26.974 1.00 63.38 N ANISOU 1685 N VAL A 210 7722 7532 8826 -44 2045 1770 N ATOM 1686 CA VAL A 210 3.426 -42.877 -26.520 1.00 56.10 C ANISOU 1686 CA VAL A 210 6783 6699 7835 104 2001 1732 C ATOM 1687 C VAL A 210 4.079 -42.062 -27.636 1.00 59.62 C ANISOU 1687 C VAL A 210 7217 7086 8352 189 1981 1613 C ATOM 1688 O VAL A 210 3.933 -40.842 -27.687 1.00 58.21 O ANISOU 1688 O VAL A 210 6994 7001 8124 275 1990 1553 O ATOM 1689 CB VAL A 210 4.451 -43.080 -25.384 1.00 53.70 C ANISOU 1689 CB VAL A 210 6538 6349 7517 183 1957 1814 C ATOM 1690 CG1 VAL A 210 5.087 -41.754 -24.978 1.00 53.82 C ANISOU 1690 CG1 VAL A 210 6514 6450 7485 315 1917 1720 C ATOM 1691 CG2 VAL A 210 3.785 -43.736 -24.189 1.00 51.01 C ANISOU 1691 CG2 VAL A 210 6202 6103 7076 130 1991 1963 C ATOM 1692 N HIS A 211 4.793 -42.728 -28.535 1.00 49.58 N ANISOU 1692 N HIS A 211 5985 5654 7200 170 1966 1584 N ATOM 1693 CA HIS A 211 5.574 -42.009 -29.532 1.00 45.37 C ANISOU 1693 CA HIS A 211 5441 5066 6729 257 1953 1493 C ATOM 1694 C HIS A 211 4.995 -42.124 -30.934 1.00 47.01 C ANISOU 1694 C HIS A 211 5592 5314 6955 224 1985 1425 C ATOM 1695 O HIS A 211 5.660 -41.785 -31.914 1.00 49.51 O ANISOU 1695 O HIS A 211 5901 5583 7328 288 1981 1367 O ATOM 1696 CB HIS A 211 7.024 -42.498 -29.516 1.00 53.43 C ANISOU 1696 CB HIS A 211 6529 5920 7852 298 1902 1490 C ATOM 1697 CG HIS A 211 7.712 -42.278 -28.205 1.00 59.31 C ANISOU 1697 CG HIS A 211 7300 6679 8555 363 1865 1532 C ATOM 1698 ND1 HIS A 211 8.370 -41.107 -27.899 1.00 54.58 N ANISOU 1698 ND1 HIS A 211 6670 6123 7945 451 1854 1456 N ATOM 1699 CD2 HIS A 211 7.824 -43.068 -27.111 1.00 65.93 C ANISOU 1699 CD2 HIS A 211 8181 7517 9353 359 1844 1637 C ATOM 1700 CE1 HIS A 211 8.870 -41.190 -26.678 1.00 58.20 C ANISOU 1700 CE1 HIS A 211 7132 6635 8345 497 1816 1483 C ATOM 1701 NE2 HIS A 211 8.551 -42.370 -26.178 1.00 65.64 N ANISOU 1701 NE2 HIS A 211 8122 7563 9257 457 1807 1610 N ATOM 1702 N PHE A 212 3.753 -42.586 -31.037 1.00 48.14 N ANISOU 1702 N PHE A 212 5679 5574 7037 127 2020 1423 N ATOM 1703 CA PHE A 212 3.082 -42.569 -32.330 1.00 61.39 C ANISOU 1703 CA PHE A 212 7264 7369 8690 114 2049 1333 C ATOM 1704 C PHE A 212 1.619 -42.163 -32.217 1.00 62.25 C ANISOU 1704 C PHE A 212 7273 7721 8656 92 2093 1323 C ATOM 1705 O PHE A 212 1.194 -41.210 -32.865 1.00 61.59 O ANISOU 1705 O PHE A 212 7120 7796 8486 205 2117 1293 O ATOM 1706 CB PHE A 212 3.183 -43.926 -33.029 1.00 59.76 C ANISOU 1706 CB PHE A 212 7055 7064 8588 -7 2046 1265 C ATOM 1707 CG PHE A 212 2.343 -44.019 -34.272 1.00 59.12 C ANISOU 1707 CG PHE A 212 6842 7167 8454 -35 2075 1140 C ATOM 1708 CD1 PHE A 212 2.687 -43.310 -35.411 1.00 57.80 C ANISOU 1708 CD1 PHE A 212 6618 7091 8252 98 2071 1086 C ATOM 1709 CD2 PHE A 212 1.199 -44.799 -34.295 1.00 61.30 C ANISOU 1709 CD2 PHE A 212 7035 7552 8705 -193 2116 1072 C ATOM 1710 CE1 PHE A 212 1.912 -43.384 -36.555 1.00 54.17 C ANISOU 1710 CE1 PHE A 212 6014 6857 7710 102 2095 970 C ATOM 1711 CE2 PHE A 212 0.419 -44.878 -35.437 1.00 53.67 C ANISOU 1711 CE2 PHE A 212 5915 6808 7668 -213 2138 924 C ATOM 1712 CZ PHE A 212 0.776 -44.169 -36.568 1.00 50.79 C ANISOU 1712 CZ PHE A 212 5488 6565 7246 -53 2122 874 C ATOM 1713 N ILE A 213 0.855 -42.890 -31.404 1.00 52.21 N ANISOU 1713 N ILE A 213 7613 6032 6191 237 2504 354 N ATOM 1714 CA ILE A 213 -0.571 -42.623 -31.248 1.00 59.54 C ANISOU 1714 CA ILE A 213 8301 6888 7434 -18 2394 353 C ATOM 1715 C ILE A 213 -0.809 -41.251 -30.617 1.00 64.31 C ANISOU 1715 C ILE A 213 8526 7710 8199 -27 2553 306 C ATOM 1716 O ILE A 213 -1.547 -40.433 -31.159 1.00 61.74 O ANISOU 1716 O ILE A 213 8033 7363 8064 -87 2455 281 O ATOM 1717 CB ILE A 213 -1.268 -43.700 -30.390 1.00 53.92 C ANISOU 1717 CB ILE A 213 7562 6091 6836 -204 2392 479 C ATOM 1718 CG1 ILE A 213 -1.239 -45.060 -31.095 1.00 59.18 C ANISOU 1718 CG1 ILE A 213 8676 6419 7392 -234 2095 514 C ATOM 1719 CG2 ILE A 213 -2.711 -43.300 -30.105 1.00 43.20 C ANISOU 1719 CG2 ILE A 213 5811 4752 5849 -424 2359 614 C ATOM 1720 CD1 ILE A 213 -1.932 -45.067 -32.439 1.00 60.07 C ANISOU 1720 CD1 ILE A 213 8992 6235 7596 -307 1681 477 C ATOM 1721 N ILE A 214 -0.179 -41.009 -29.472 1.00 57.84 N ANISOU 1721 N ILE A 214 7631 7066 7279 61 2757 284 N ATOM 1722 CA ILE A 214 -0.285 -39.723 -28.793 1.00 61.57 C ANISOU 1722 CA ILE A 214 7893 7672 7827 120 2731 192 C ATOM 1723 C ILE A 214 0.163 -38.537 -29.673 1.00 62.41 C ANISOU 1723 C ILE A 214 7950 7757 8006 163 2665 141 C ATOM 1724 O ILE A 214 -0.568 -37.557 -29.777 1.00 64.32 O ANISOU 1724 O ILE A 214 8035 7991 8412 154 2646 80 O ATOM 1725 CB ILE A 214 0.509 -39.723 -27.469 1.00 58.51 C ANISOU 1725 CB ILE A 214 7553 7407 7269 224 2690 149 C ATOM 1726 CG1 ILE A 214 -0.152 -40.668 -26.465 1.00 59.47 C ANISOU 1726 CG1 ILE A 214 7659 7590 7348 217 2782 227 C ATOM 1727 CG2 ILE A 214 0.604 -38.316 -26.896 1.00 58.35 C ANISOU 1727 CG2 ILE A 214 7479 7427 7264 334 2697 27 C ATOM 1728 CD1 ILE A 214 0.476 -40.640 -25.095 1.00 63.50 C ANISOU 1728 CD1 ILE A 214 8239 8222 7665 353 2771 174 C ATOM 1729 N PRO A 215 1.349 -38.618 -30.318 1.00 64.88 N ANISOU 1729 N PRO A 215 8368 8075 8210 238 2602 219 N ATOM 1730 CA PRO A 215 1.680 -37.516 -31.232 1.00 65.81 C ANISOU 1730 CA PRO A 215 8376 8183 8445 274 2520 269 C ATOM 1731 C PRO A 215 0.649 -37.321 -32.344 1.00 68.65 C ANISOU 1731 C PRO A 215 8723 8441 8919 229 2421 234 C ATOM 1732 O PRO A 215 0.374 -36.185 -32.734 1.00 70.30 O ANISOU 1732 O PRO A 215 8776 8636 9300 212 2331 213 O ATOM 1733 CB PRO A 215 3.028 -37.946 -31.824 1.00 57.10 C ANISOU 1733 CB PRO A 215 7362 7152 7183 426 2542 486 C ATOM 1734 CG PRO A 215 3.623 -38.819 -30.789 1.00 56.13 C ANISOU 1734 CG PRO A 215 7326 7086 6915 430 2519 480 C ATOM 1735 CD PRO A 215 2.467 -39.575 -30.209 1.00 62.14 C ANISOU 1735 CD PRO A 215 8179 7772 7658 326 2561 320 C ATOM 1736 N LEU A 216 0.086 -38.418 -32.837 1.00 62.94 N ANISOU 1736 N LEU A 216 8190 7611 8114 201 2378 235 N ATOM 1737 CA LEU A 216 -0.887 -38.363 -33.922 1.00 64.67 C ANISOU 1737 CA LEU A 216 8451 7685 8437 143 2186 215 C ATOM 1738 C LEU A 216 -2.180 -37.699 -33.459 1.00 65.39 C ANISOU 1738 C LEU A 216 8239 7783 8822 -26 2164 172 C ATOM 1739 O LEU A 216 -2.759 -36.876 -34.173 1.00 54.80 O ANISOU 1739 O LEU A 216 6778 6409 7636 -45 2049 158 O ATOM 1740 CB LEU A 216 -1.164 -39.770 -34.453 1.00 64.68 C ANISOU 1740 CB LEU A 216 8805 7479 8290 135 2019 230 C ATOM 1741 CG LEU A 216 -1.789 -39.930 -35.838 1.00 71.36 C ANISOU 1741 CG LEU A 216 9898 8098 9115 160 1702 211 C ATOM 1742 CD1 LEU A 216 -1.306 -41.226 -36.462 1.00 79.56 C ANISOU 1742 CD1 LEU A 216 11501 8920 9807 357 1540 205 C ATOM 1743 CD2 LEU A 216 -3.300 -39.935 -35.740 1.00 79.37 C ANISOU 1743 CD2 LEU A 216 10692 8979 10485 -151 1475 230 C ATOM 1744 N ILE A 217 -2.625 -38.057 -32.260 1.00 58.41 N ANISOU 1744 N ILE A 217 7227 6971 7995 -96 2308 191 N ATOM 1745 CA ILE A 217 -3.849 -37.499 -31.697 1.00 62.80 C ANISOU 1745 CA ILE A 217 7476 7598 8787 -148 2380 239 C ATOM 1746 C ILE A 217 -3.708 -35.997 -31.463 1.00 65.93 C ANISOU 1746 C ILE A 217 7757 8079 9213 3 2442 119 C ATOM 1747 O ILE A 217 -4.603 -35.216 -31.787 1.00 59.40 O ANISOU 1747 O ILE A 217 6742 7252 8575 11 2401 135 O ATOM 1748 CB ILE A 217 -4.217 -38.188 -30.374 1.00 54.18 C ANISOU 1748 CB ILE A 217 6284 6619 7682 -144 2601 356 C ATOM 1749 CG1 ILE A 217 -4.611 -39.643 -30.627 1.00 55.33 C ANISOU 1749 CG1 ILE A 217 6501 6617 7907 -355 2460 535 C ATOM 1750 CG2 ILE A 217 -5.355 -37.454 -29.681 1.00 53.60 C ANISOU 1750 CG2 ILE A 217 5887 6700 7780 -40 2782 466 C ATOM 1751 CD1 ILE A 217 -4.966 -40.399 -29.366 1.00 54.55 C ANISOU 1751 CD1 ILE A 217 6260 6636 7829 -364 2689 739 C ATOM 1752 N VAL A 218 -2.568 -35.605 -30.906 1.00 67.13 N ANISOU 1752 N VAL A 218 8037 8271 9198 117 2486 20 N ATOM 1753 CA VAL A 218 -2.285 -34.211 -30.599 1.00 61.41 C ANISOU 1753 CA VAL A 218 7291 7534 8509 238 2425 -95 C ATOM 1754 C VAL A 218 -2.199 -33.345 -31.855 1.00 57.67 C ANISOU 1754 C VAL A 218 6751 6970 8192 192 2239 -76 C ATOM 1755 O VAL A 218 -2.802 -32.273 -31.922 1.00 55.99 O ANISOU 1755 O VAL A 218 6443 6713 8117 252 2178 -138 O ATOM 1756 CB VAL A 218 -0.977 -34.082 -29.800 1.00 54.87 C ANISOU 1756 CB VAL A 218 6623 6702 7521 301 2381 -146 C ATOM 1757 CG1 VAL A 218 -0.527 -32.627 -29.732 1.00 53.48 C ANISOU 1757 CG1 VAL A 218 6471 6403 7447 356 2147 -227 C ATOM 1758 CG2 VAL A 218 -1.164 -34.661 -28.400 1.00 46.01 C ANISOU 1758 CG2 VAL A 218 5599 5672 6210 423 2565 -196 C ATOM 1759 N ILE A 219 -1.453 -33.808 -32.850 1.00 56.98 N ANISOU 1759 N ILE A 219 6735 6862 8051 143 2170 33 N ATOM 1760 CA ILE A 219 -1.310 -33.059 -34.092 1.00 57.95 C ANISOU 1760 CA ILE A 219 6803 6934 8282 155 2034 114 C ATOM 1761 C ILE A 219 -2.650 -32.910 -34.811 1.00 59.91 C ANISOU 1761 C ILE A 219 6966 7128 8669 108 1965 79 C ATOM 1762 O ILE A 219 -2.959 -31.847 -35.349 1.00 62.15 O ANISOU 1762 O ILE A 219 7136 7370 9109 128 1868 79 O ATOM 1763 CB ILE A 219 -0.294 -33.722 -35.027 1.00 45.12 C ANISOU 1763 CB ILE A 219 5314 5344 6485 241 2046 296 C ATOM 1764 CG1 ILE A 219 1.116 -33.557 -34.463 1.00 53.04 C ANISOU 1764 CG1 ILE A 219 6277 6426 7452 284 2082 447 C ATOM 1765 CG2 ILE A 219 -0.350 -33.112 -36.412 1.00 42.40 C ANISOU 1765 CG2 ILE A 219 4945 4974 6193 324 1951 417 C ATOM 1766 CD1 ILE A 219 2.161 -34.318 -35.242 1.00 49.98 C ANISOU 1766 CD1 ILE A 219 5997 6140 6854 465 2187 709 C ATOM 1767 N PHE A 220 -3.450 -33.970 -34.803 1.00 57.01 N ANISOU 1767 N PHE A 220 6638 6742 8283 23 1972 88 N ATOM 1768 CA PHE A 220 -4.771 -33.933 -35.422 1.00 57.51 C ANISOU 1768 CA PHE A 220 6573 6739 8541 -73 1836 126 C ATOM 1769 C PHE A 220 -5.725 -32.993 -34.688 1.00 57.94 C ANISOU 1769 C PHE A 220 6337 6875 8803 -35 1944 118 C ATOM 1770 O PHE A 220 -6.464 -32.234 -35.318 1.00 55.43 O ANISOU 1770 O PHE A 220 5869 6529 8663 -31 1844 144 O ATOM 1771 CB PHE A 220 -5.376 -35.335 -35.484 1.00 55.29 C ANISOU 1771 CB PHE A 220 6379 6363 8265 -227 1725 213 C ATOM 1772 CG PHE A 220 -5.176 -36.021 -36.801 1.00 66.49 C ANISOU 1772 CG PHE A 220 8135 7590 9538 -223 1441 215 C ATOM 1773 CD1 PHE A 220 -4.046 -36.789 -37.035 1.00 74.45 C ANISOU 1773 CD1 PHE A 220 9509 8560 10219 -74 1468 187 C ATOM 1774 CD2 PHE A 220 -6.118 -35.900 -37.808 1.00 71.09 C ANISOU 1774 CD2 PHE A 220 8713 8023 10273 -310 1133 255 C ATOM 1775 CE1 PHE A 220 -3.859 -37.428 -38.250 1.00 68.62 C ANISOU 1775 CE1 PHE A 220 9197 7632 9244 61 1216 179 C ATOM 1776 CE2 PHE A 220 -5.938 -36.535 -39.026 1.00 83.52 C ANISOU 1776 CE2 PHE A 220 10725 9378 11631 -228 815 224 C ATOM 1777 CZ PHE A 220 -4.807 -37.301 -39.245 1.00 80.04 C ANISOU 1777 CZ PHE A 220 10718 8894 10801 -6 869 175 C ATOM 1778 N PHE A 221 -5.717 -33.056 -33.360 1.00 49.64 N ANISOU 1778 N PHE A 221 5243 5931 7689 55 2161 95 N ATOM 1779 CA PHE A 221 -6.570 -32.192 -32.558 1.00 43.97 C ANISOU 1779 CA PHE A 221 4339 5308 7060 239 2319 99 C ATOM 1780 C PHE A 221 -6.205 -30.726 -32.762 1.00 61.35 C ANISOU 1780 C PHE A 221 6614 7423 9273 386 2217 -59 C ATOM 1781 O PHE A 221 -7.061 -29.894 -33.064 1.00 60.43 O ANISOU 1781 O PHE A 221 6346 7304 9311 479 2200 -33 O ATOM 1782 CB PHE A 221 -6.465 -32.546 -31.073 1.00 49.10 C ANISOU 1782 CB PHE A 221 5043 6085 7527 415 2578 95 C ATOM 1783 CG PHE A 221 -7.157 -31.560 -30.161 1.00 61.84 C ANISOU 1783 CG PHE A 221 6608 7795 9094 773 2770 72 C ATOM 1784 CD1 PHE A 221 -8.518 -31.655 -29.919 1.00 63.93 C ANISOU 1784 CD1 PHE A 221 6545 8234 9512 899 2989 345 C ATOM 1785 CD2 PHE A 221 -6.443 -30.541 -29.544 1.00 63.58 C ANISOU 1785 CD2 PHE A 221 7131 7911 9114 1018 2701 -182 C ATOM 1786 CE1 PHE A 221 -9.156 -30.751 -29.085 1.00 67.17 C ANISOU 1786 CE1 PHE A 221 6969 8761 9790 1344 3191 353 C ATOM 1787 CE2 PHE A 221 -7.076 -29.636 -28.710 1.00 63.69 C ANISOU 1787 CE2 PHE A 221 7238 7964 8998 1448 2843 -240 C ATOM 1788 CZ PHE A 221 -8.433 -29.742 -28.480 1.00 66.24 C ANISOU 1788 CZ PHE A 221 7257 8510 9402 1667 3153 25 C ATOM 1789 N CYS A 222 -4.924 -30.422 -32.590 1.00 56.83 N ANISOU 1789 N CYS A 222 6256 6765 8571 393 2118 -176 N ATOM 1790 CA CYS A 222 -4.440 -29.053 -32.651 1.00 55.12 C ANISOU 1790 CA CYS A 222 6127 6402 8414 484 1932 -279 C ATOM 1791 C CYS A 222 -4.664 -28.418 -34.016 1.00 52.18 C ANISOU 1791 C CYS A 222 5624 5961 8243 395 1776 -196 C ATOM 1792 O CYS A 222 -5.149 -27.295 -34.107 1.00 52.17 O ANISOU 1792 O CYS A 222 5591 5868 8364 508 1690 -250 O ATOM 1793 CB CYS A 222 -2.957 -29.005 -32.280 1.00 45.52 C ANISOU 1793 CB CYS A 222 5087 5098 7109 426 1782 -297 C ATOM 1794 SG CYS A 222 -2.683 -29.120 -30.497 1.00 58.14 S ANISOU 1794 SG CYS A 222 6948 6686 8455 627 1838 -471 S ATOM 1795 N TYR A 223 -4.317 -29.136 -35.078 1.00 46.99 N ANISOU 1795 N TYR A 223 4940 5335 7579 249 1739 -67 N ATOM 1796 CA TYR A 223 -4.471 -28.582 -36.415 1.00 53.13 C ANISOU 1796 CA TYR A 223 5642 6061 8484 222 1599 30 C ATOM 1797 C TYR A 223 -5.922 -28.633 -36.871 1.00 56.07 C ANISOU 1797 C TYR A 223 5865 6454 8984 208 1590 39 C ATOM 1798 O TYR A 223 -6.315 -27.894 -37.771 1.00 54.40 O ANISOU 1798 O TYR A 223 5572 6191 8905 225 1467 84 O ATOM 1799 CB TYR A 223 -3.570 -29.311 -37.410 1.00 43.70 C ANISOU 1799 CB TYR A 223 4557 4898 7148 196 1573 185 C ATOM 1800 CG TYR A 223 -2.136 -28.831 -37.370 1.00 45.90 C ANISOU 1800 CG TYR A 223 4839 5174 7426 224 1544 341 C ATOM 1801 CD1 TYR A 223 -1.835 -27.503 -37.091 1.00 48.60 C ANISOU 1801 CD1 TYR A 223 5080 5397 7988 205 1388 367 C ATOM 1802 CD2 TYR A 223 -1.083 -29.705 -37.607 1.00 45.56 C ANISOU 1802 CD2 TYR A 223 4892 5228 7190 277 1637 511 C ATOM 1803 CE1 TYR A 223 -0.522 -27.058 -37.052 1.00 46.35 C ANISOU 1803 CE1 TYR A 223 4730 5079 7803 164 1276 610 C ATOM 1804 CE2 TYR A 223 0.231 -29.272 -37.571 1.00 42.79 C ANISOU 1804 CE2 TYR A 223 4441 4910 6906 295 1611 776 C ATOM 1805 CZ TYR A 223 0.508 -27.950 -37.291 1.00 49.47 C ANISOU 1805 CZ TYR A 223 5125 5625 8045 202 1406 850 C ATOM 1806 OH TYR A 223 1.817 -27.517 -37.258 1.00 45.79 O ANISOU 1806 OH TYR A 223 4495 5162 7741 156 1298 1210 O ATOM 1807 N GLY A 224 -6.712 -29.505 -36.251 1.00 54.01 N ANISOU 1807 N GLY A 224 5529 6275 8719 167 1704 55 N ATOM 1808 CA GLY A 224 -8.138 -29.546 -36.512 1.00 52.66 C ANISOU 1808 CA GLY A 224 5114 6141 8753 131 1678 171 C ATOM 1809 C GLY A 224 -8.800 -28.308 -35.935 1.00 59.97 C ANISOU 1809 C GLY A 224 5884 7111 9791 354 1796 143 C ATOM 1810 O GLY A 224 -9.605 -27.655 -36.595 1.00 61.29 O ANISOU 1810 O GLY A 224 5879 7266 10142 383 1709 218 O ATOM 1811 N GLN A 225 -8.450 -27.988 -34.693 1.00 54.06 N ANISOU 1811 N GLN A 225 5250 6396 8893 558 1975 29 N ATOM 1812 CA GLN A 225 -8.928 -26.778 -34.040 1.00 52.31 C ANISOU 1812 CA GLN A 225 5048 6161 8667 888 2064 -51 C ATOM 1813 C GLN A 225 -8.517 -25.535 -34.818 1.00 63.97 C ANISOU 1813 C GLN A 225 6630 7436 10241 895 1813 -157 C ATOM 1814 O GLN A 225 -9.309 -24.608 -34.983 1.00 62.46 O ANISOU 1814 O GLN A 225 6354 7218 10160 1085 1811 -144 O ATOM 1815 CB GLN A 225 -8.392 -26.700 -32.609 1.00 51.05 C ANISOU 1815 CB GLN A 225 5164 5997 8236 1143 2200 -209 C ATOM 1816 CG GLN A 225 -9.064 -27.655 -31.648 1.00 53.07 C ANISOU 1816 CG GLN A 225 5282 6494 8390 1278 2534 -45 C ATOM 1817 CD GLN A 225 -10.506 -27.274 -31.375 1.00 66.10 C ANISOU 1817 CD GLN A 225 6646 8334 10135 1599 2793 185 C ATOM 1818 OE1 GLN A 225 -10.846 -26.092 -31.309 1.00 77.02 O ANISOU 1818 OE1 GLN A 225 8135 9645 11483 1925 2786 88 O ATOM 1819 NE2 GLN A 225 -11.362 -28.274 -31.224 1.00 73.71 N ANISOU 1819 NE2 GLN A 225 7229 9531 11245 1516 3008 543 N ATOM 1820 N LEU A 226 -7.275 -25.528 -35.292 1.00 57.28 N ANISOU 1820 N LEU A 226 5936 6459 9369 705 1618 -202 N ATOM 1821 CA LEU A 226 -6.739 -24.396 -36.038 1.00 62.70 C ANISOU 1821 CA LEU A 226 6675 6954 10195 676 1368 -202 C ATOM 1822 C LEU A 226 -7.516 -24.161 -37.332 1.00 61.53 C ANISOU 1822 C LEU A 226 6317 6842 10221 618 1314 -70 C ATOM 1823 O LEU A 226 -7.862 -23.024 -37.654 1.00 59.49 O ANISOU 1823 O LEU A 226 6035 6465 10104 727 1201 -79 O ATOM 1824 CB LEU A 226 -5.253 -24.613 -36.338 1.00 47.63 C ANISOU 1824 CB LEU A 226 4858 4976 8262 490 1225 -117 C ATOM 1825 CG LEU A 226 -4.422 -23.359 -36.616 1.00 56.11 C ANISOU 1825 CG LEU A 226 5984 5813 9522 456 929 -44 C ATOM 1826 CD1 LEU A 226 -2.980 -23.577 -36.202 1.00 72.25 C ANISOU 1826 CD1 LEU A 226 8103 7795 11555 321 796 68 C ATOM 1827 CD2 LEU A 226 -4.488 -22.994 -38.079 1.00 56.45 C ANISOU 1827 CD2 LEU A 226 5848 5878 9723 388 871 173 C ATOM 1828 N VAL A 227 -7.782 -25.233 -38.072 1.00 54.61 N ANISOU 1828 N VAL A 227 5340 6089 9321 462 1343 44 N ATOM 1829 CA VAL A 227 -8.557 -25.122 -39.301 1.00 59.79 C ANISOU 1829 CA VAL A 227 5854 6753 10109 412 1221 160 C ATOM 1830 C VAL A 227 -9.967 -24.613 -38.996 1.00 58.70 C ANISOU 1830 C VAL A 227 5481 6673 10149 540 1289 196 C ATOM 1831 O VAL A 227 -10.497 -23.763 -39.711 1.00 61.66 O ANISOU 1831 O VAL A 227 5753 7000 10674 602 1181 248 O ATOM 1832 CB VAL A 227 -8.630 -26.466 -40.046 1.00 52.85 C ANISOU 1832 CB VAL A 227 5031 5920 9131 250 1138 245 C ATOM 1833 CG1 VAL A 227 -9.696 -26.428 -41.135 1.00 48.77 C ANISOU 1833 CG1 VAL A 227 4394 5378 8760 200 931 353 C ATOM 1834 CG2 VAL A 227 -7.273 -26.806 -40.641 1.00 57.14 C ANISOU 1834 CG2 VAL A 227 5816 6433 9461 251 1103 276 C ATOM 1835 N PHE A 228 -10.557 -25.118 -37.917 1.00 49.21 N ANISOU 1835 N PHE A 228 4174 5600 8924 623 1499 220 N ATOM 1836 CA PHE A 228 -11.891 -24.690 -37.511 1.00 61.06 C ANISOU 1836 CA PHE A 228 5395 7227 10579 833 1651 362 C ATOM 1837 C PHE A 228 -11.906 -23.205 -37.151 1.00 58.35 C ANISOU 1837 C PHE A 228 5187 6777 10208 1173 1687 221 C ATOM 1838 O PHE A 228 -12.799 -22.469 -37.561 1.00 57.58 O ANISOU 1838 O PHE A 228 4905 6700 10272 1323 1679 327 O ATOM 1839 CB PHE A 228 -12.389 -25.526 -36.331 1.00 57.34 C ANISOU 1839 CB PHE A 228 4779 6952 10054 929 1938 498 C ATOM 1840 CG PHE A 228 -13.791 -25.195 -35.906 1.00 74.53 C ANISOU 1840 CG PHE A 228 6582 9336 12400 1205 2169 786 C ATOM 1841 CD1 PHE A 228 -14.878 -25.689 -36.609 1.00 74.78 C ANISOU 1841 CD1 PHE A 228 6173 9473 12766 994 2058 1148 C ATOM 1842 CD2 PHE A 228 -14.023 -24.386 -34.805 1.00 88.88 C ANISOU 1842 CD2 PHE A 228 8507 11232 14029 1718 2472 733 C ATOM 1843 CE1 PHE A 228 -16.169 -25.385 -36.219 1.00 82.98 C ANISOU 1843 CE1 PHE A 228 6779 10747 14003 1260 2291 1527 C ATOM 1844 CE2 PHE A 228 -15.310 -24.078 -34.411 1.00 88.54 C ANISOU 1844 CE2 PHE A 228 8143 11431 14068 2056 2728 1059 C ATOM 1845 CZ PHE A 228 -16.385 -24.578 -35.119 1.00 87.66 C ANISOU 1845 CZ PHE A 228 7559 11465 14282 1781 2614 1467 C ATOM 1846 N THR A 229 -10.904 -22.772 -36.392 1.00 62.70 N ANISOU 1846 N THR A 229 6087 7174 10562 1293 1668 -10 N ATOM 1847 CA THR A 229 -10.785 -21.376 -35.985 1.00 65.19 C ANISOU 1847 CA THR A 229 6665 7274 10832 1609 1574 -182 C ATOM 1848 C THR A 229 -10.675 -20.440 -37.189 1.00 63.43 C ANISOU 1848 C THR A 229 6404 6872 10825 1489 1304 -150 C ATOM 1849 O THR A 229 -11.343 -19.403 -37.246 1.00 70.17 O ANISOU 1849 O THR A 229 7273 7637 11750 1759 1279 -163 O ATOM 1850 CB THR A 229 -9.565 -21.171 -35.063 1.00 62.98 C ANISOU 1850 CB THR A 229 6809 6775 10347 1652 1433 -415 C ATOM 1851 OG1 THR A 229 -9.826 -21.778 -33.792 1.00 65.71 O ANISOU 1851 OG1 THR A 229 7259 7275 10434 1913 1709 -465 O ATOM 1852 CG2 THR A 229 -9.280 -19.689 -34.857 1.00 65.14 C ANISOU 1852 CG2 THR A 229 7433 6688 10631 1884 1140 -592 C ATOM 1853 N VAL A 230 -9.843 -20.816 -38.155 1.00 52.12 N ANISOU 1853 N VAL A 230 4933 5403 9469 1141 1130 -76 N ATOM 1854 CA VAL A 230 -9.606 -19.983 -39.330 1.00 60.28 C ANISOU 1854 CA VAL A 230 5926 6293 10684 1046 901 19 C ATOM 1855 C VAL A 230 -10.801 -20.043 -40.284 1.00 57.94 C ANISOU 1855 C VAL A 230 5347 6145 10523 1052 933 168 C ATOM 1856 O VAL A 230 -11.146 -19.050 -40.927 1.00 60.47 O ANISOU 1856 O VAL A 230 5622 6361 10993 1140 810 219 O ATOM 1857 CB VAL A 230 -8.309 -20.402 -40.063 1.00 51.89 C ANISOU 1857 CB VAL A 230 4902 5203 9610 777 773 141 C ATOM 1858 CG1 VAL A 230 -8.062 -19.523 -41.268 1.00 56.86 C ANISOU 1858 CG1 VAL A 230 5463 5723 10418 735 586 323 C ATOM 1859 CG2 VAL A 230 -7.122 -20.313 -39.115 1.00 56.11 C ANISOU 1859 CG2 VAL A 230 5651 5586 10081 735 684 64 C ATOM 1860 N LYS A 231 -11.439 -21.205 -40.360 1.00 54.18 N ANISOU 1860 N LYS A 231 4683 5880 10021 942 1047 263 N ATOM 1861 CA LYS A 231 -12.657 -21.357 -41.148 1.00 64.66 C ANISOU 1861 CA LYS A 231 5721 7323 11524 910 993 447 C ATOM 1862 C LYS A 231 -13.751 -20.456 -40.589 1.00 58.93 C ANISOU 1862 C LYS A 231 4815 6652 10925 1232 1144 504 C ATOM 1863 O LYS A 231 -14.505 -19.821 -41.333 1.00 54.42 O ANISOU 1863 O LYS A 231 4066 6081 10531 1298 1047 628 O ATOM 1864 CB LYS A 231 -13.128 -22.812 -41.145 1.00 74.66 C ANISOU 1864 CB LYS A 231 6834 8737 12797 695 997 579 C ATOM 1865 CG LYS A 231 -13.388 -23.399 -42.519 1.00 86.31 C ANISOU 1865 CG LYS A 231 8294 10171 14330 468 681 696 C ATOM 1866 CD LYS A 231 -12.102 -23.854 -43.184 1.00 82.63 C ANISOU 1866 CD LYS A 231 8190 9601 13604 377 567 585 C ATOM 1867 CE LYS A 231 -12.390 -24.640 -44.454 1.00 76.97 C ANISOU 1867 CE LYS A 231 7602 8815 12827 247 231 669 C ATOM 1868 NZ LYS A 231 -11.144 -25.064 -45.143 1.00 70.75 N ANISOU 1868 NZ LYS A 231 7210 7966 11706 305 188 608 N ATOM 1869 N GLU A 232 -13.825 -20.412 -39.264 1.00 60.41 N ANISOU 1869 N GLU A 232 5080 6895 10979 1495 1397 428 N ATOM 1870 CA GLU A 232 -14.852 -19.653 -38.566 1.00 57.98 C ANISOU 1870 CA GLU A 232 4662 6679 10689 1950 1627 510 C ATOM 1871 C GLU A 232 -14.621 -18.152 -38.709 1.00 69.86 C ANISOU 1871 C GLU A 232 6455 7911 12177 2216 1481 328 C ATOM 1872 O GLU A 232 -15.566 -17.388 -38.912 1.00 63.64 O ANISOU 1872 O GLU A 232 5516 7164 11500 2504 1543 452 O ATOM 1873 CB GLU A 232 -14.881 -20.051 -37.090 1.00 75.22 C ANISOU 1873 CB GLU A 232 6956 8991 12632 2255 1952 476 C ATOM 1874 CG GLU A 232 -15.998 -19.421 -36.290 1.00 98.16 C ANISOU 1874 CG GLU A 232 9755 12069 15473 2861 2290 640 C ATOM 1875 CD GLU A 232 -15.954 -19.818 -34.829 1.00117.42 C ANISOU 1875 CD GLU A 232 12407 14655 17554 3212 2600 606 C ATOM 1876 OE1 GLU A 232 -14.916 -20.359 -34.391 1.00117.33 O ANISOU 1876 OE1 GLU A 232 12663 14520 17397 3046 2545 385 O ATOM 1877 OE2 GLU A 232 -16.958 -19.590 -34.120 1.00132.23 O ANISOU 1877 OE2 GLU A 232 14237 16783 19223 3591 2835 802 O ATOM 1878 N ALA A 233 -13.361 -17.736 -38.604 1.00 65.65 N ANISOU 1878 N ALA A 233 6320 7084 11539 2109 1255 80 N ATOM 1879 CA ALA A 233 -13.009 -16.324 -38.729 1.00 63.90 C ANISOU 1879 CA ALA A 233 6406 6514 11359 2286 1003 -64 C ATOM 1880 C ALA A 233 -13.322 -15.813 -40.130 1.00 58.39 C ANISOU 1880 C ALA A 233 5473 5791 10922 2118 833 106 C ATOM 1881 O ALA A 233 -13.825 -14.703 -40.298 1.00 60.89 O ANISOU 1881 O ALA A 233 5857 5957 11323 2387 757 102 O ATOM 1882 CB ALA A 233 -11.538 -16.107 -38.402 1.00 62.78 C ANISOU 1882 CB ALA A 233 6643 6055 11157 2093 711 -245 C ATOM 1883 N ALA A 234 -13.025 -16.632 -41.133 1.00 55.57 N ANISOU 1883 N ALA A 234 4894 5571 10651 1724 765 252 N ATOM 1884 CA ALA A 234 -13.273 -16.252 -42.516 1.00 60.98 C ANISOU 1884 CA ALA A 234 5405 6248 11518 1594 595 421 C ATOM 1885 C ALA A 234 -14.772 -16.162 -42.789 1.00 67.07 C ANISOU 1885 C ALA A 234 5850 7212 12420 1772 701 582 C ATOM 1886 O ALA A 234 -15.226 -15.294 -43.533 1.00 63.03 O ANISOU 1886 O ALA A 234 5263 6628 12058 1869 582 671 O ATOM 1887 CB ALA A 234 -12.613 -17.238 -43.466 1.00 54.45 C ANISOU 1887 CB ALA A 234 4527 5519 10642 1250 503 528 C ATOM 1888 N ALA A 235 -15.535 -17.061 -42.174 1.00 58.54 N ANISOU 1888 N ALA A 235 4538 6385 11319 1810 917 679 N ATOM 1889 CA ALA A 235 -16.983 -17.078 -42.338 1.00 67.03 C ANISOU 1889 CA ALA A 235 5195 7686 12588 1958 1020 958 C ATOM 1890 C ALA A 235 -17.614 -15.816 -41.757 1.00 65.06 C ANISOU 1890 C ALA A 235 4993 7393 12335 2487 1196 952 C ATOM 1891 O ALA A 235 -18.578 -15.287 -42.305 1.00 67.51 O ANISOU 1891 O ALA A 235 5026 7787 12836 2637 1185 1169 O ATOM 1892 CB ALA A 235 -17.575 -18.315 -41.686 1.00 62.52 C ANISOU 1892 CB ALA A 235 4321 7387 12046 1876 1213 1163 C ATOM 1893 N GLN A 236 -17.056 -15.337 -40.650 1.00 65.75 N ANISOU 1893 N GLN A 236 5482 7321 12178 2801 1322 700 N ATOM 1894 CA GLN A 236 -17.566 -14.155 -39.970 1.00 69.81 C ANISOU 1894 CA GLN A 236 6220 7726 12580 3414 1460 633 C ATOM 1895 C GLN A 236 -16.993 -12.869 -40.562 1.00 69.80 C ANISOU 1895 C GLN A 236 6575 7308 12639 3430 1111 439 C ATOM 1896 O GLN A 236 -17.276 -11.775 -40.074 1.00 73.40 O ANISOU 1896 O GLN A 236 7350 7551 12986 3935 1115 324 O ATOM 1897 CB GLN A 236 -17.250 -14.226 -38.475 1.00 71.56 C ANISOU 1897 CB GLN A 236 6834 7908 12448 3817 1682 430 C ATOM 1898 CG GLN A 236 -17.762 -15.483 -37.784 1.00108.94 C ANISOU 1898 CG GLN A 236 11257 13074 17061 3770 2015 650 C ATOM 1899 CD GLN A 236 -17.552 -15.458 -36.280 1.00119.64 C ANISOU 1899 CD GLN A 236 13061 14434 17962 4214 2220 452 C ATOM 1900 OE1 GLN A 236 -17.342 -14.398 -35.689 1.00130.65 O ANISOU 1900 OE1 GLN A 236 15007 15542 19093 4665 2122 169 O ATOM 1901 NE2 GLN A 236 -17.606 -16.631 -35.654 1.00111.65 N ANISOU 1901 NE2 GLN A 236 11862 13713 16847 4072 2448 596 N ATOM 1902 N GLN A 237 -16.193 -13.001 -41.616 1.00 66.35 N ANISOU 1902 N GLN A 237 6103 6746 12363 2919 809 439 N ATOM 1903 CA GLN A 237 -15.544 -11.846 -42.223 1.00 66.54 C ANISOU 1903 CA GLN A 237 6396 6383 12504 2869 468 357 C ATOM 1904 C GLN A 237 -15.328 -12.034 -43.724 1.00 65.00 C ANISOU 1904 C GLN A 237 5926 6256 12516 2455 287 565 C ATOM 1905 O GLN A 237 -14.216 -11.877 -44.227 1.00 62.34 O ANISOU 1905 O GLN A 237 5728 5724 12234 2173 58 575 O ATOM 1906 CB GLN A 237 -14.213 -11.564 -41.526 1.00 66.04 C ANISOU 1906 CB GLN A 237 6807 5947 12336 2775 226 118 C ATOM 1907 CG GLN A 237 -13.715 -10.139 -41.694 1.00 86.13 C ANISOU 1907 CG GLN A 237 9715 7991 15022 2862 -170 47 C ATOM 1908 CD GLN A 237 -12.543 -9.821 -40.790 1.00 81.74 C ANISOU 1908 CD GLN A 237 9656 7008 14394 2805 -502 -165 C ATOM 1909 OE1 GLN A 237 -12.117 -10.655 -39.992 1.00 68.14 O ANISOU 1909 OE1 GLN A 237 8020 5394 12475 2745 -390 -286 O ATOM 1910 NE2 GLN A 237 -12.018 -8.604 -40.905 1.00 75.64 N ANISOU 1910 NE2 GLN A 237 9216 5713 13809 2805 -968 -186 N ATOM 1911 N GLN A 238 -16.407 -12.345 -44.436 1.00 64.69 N ANISOU 1911 N GLN A 238 5497 6493 12587 2461 376 779 N ATOM 1912 CA GLN A 238 -16.328 -12.641 -45.864 1.00 63.02 C ANISOU 1912 CA GLN A 238 5095 6361 12490 2144 187 961 C ATOM 1913 C GLN A 238 -16.052 -11.415 -46.732 1.00 63.94 C ANISOU 1913 C GLN A 238 5319 6229 12746 2192 -35 1032 C ATOM 1914 O GLN A 238 -15.711 -11.552 -47.906 1.00 73.84 O ANISOU 1914 O GLN A 238 6511 7513 14031 1984 -187 1187 O ATOM 1915 CB GLN A 238 -17.616 -13.317 -46.328 1.00 64.28 C ANISOU 1915 CB GLN A 238 4838 6830 12758 2120 233 1184 C ATOM 1916 CG GLN A 238 -17.783 -14.728 -45.800 1.00 70.58 C ANISOU 1916 CG GLN A 238 5479 7855 13484 1931 351 1216 C ATOM 1917 CD GLN A 238 -19.041 -15.388 -46.316 1.00 90.24 C ANISOU 1917 CD GLN A 238 7527 10583 16178 1827 264 1519 C ATOM 1918 OE1 GLN A 238 -19.771 -14.814 -47.127 1.00 98.28 O ANISOU 1918 OE1 GLN A 238 8357 11615 17371 1895 112 1693 O ATOM 1919 NE2 GLN A 238 -19.304 -16.600 -45.848 1.00 94.36 N ANISOU 1919 NE2 GLN A 238 7867 11271 16715 1638 313 1621 N ATOM 1920 N GLU A 239 -16.191 -10.223 -46.161 1.00 66.55 N ANISOU 1920 N GLU A 239 5855 6297 13135 2509 -64 934 N ATOM 1921 CA GLU A 239 -15.872 -8.998 -46.891 1.00 67.89 C ANISOU 1921 CA GLU A 239 6151 6165 13479 2539 -317 1022 C ATOM 1922 C GLU A 239 -14.352 -8.822 -47.036 1.00 68.68 C ANISOU 1922 C GLU A 239 6467 5996 13631 2238 -545 1053 C ATOM 1923 O GLU A 239 -13.886 -8.010 -47.835 1.00 72.41 O ANISOU 1923 O GLU A 239 6956 6263 14293 2154 -763 1252 O ATOM 1924 CB GLU A 239 -16.499 -7.770 -46.205 1.00 71.90 C ANISOU 1924 CB GLU A 239 6891 6405 14020 3009 -338 901 C ATOM 1925 CG GLU A 239 -15.875 -7.344 -44.871 1.00 73.56 C ANISOU 1925 CG GLU A 239 7603 6255 14091 3208 -430 612 C ATOM 1926 CD GLU A 239 -16.333 -8.180 -43.678 1.00 73.79 C ANISOU 1926 CD GLU A 239 7653 6537 13845 3456 -94 452 C ATOM 1927 OE1 GLU A 239 -16.112 -7.742 -42.530 1.00 76.33 O ANISOU 1927 OE1 GLU A 239 8449 6581 13971 3795 -141 198 O ATOM 1928 OE2 GLU A 239 -16.902 -9.275 -43.878 1.00 71.95 O ANISOU 1928 OE2 GLU A 239 6997 6754 13588 3325 180 597 O ATOM 1929 N SER A 240 -13.585 -9.597 -46.273 1.00 64.63 N ANISOU 1929 N SER A 240 6071 5505 12980 2078 -489 925 N ATOM 1930 CA SER A 240 -12.124 -9.544 -46.345 1.00 68.72 C ANISOU 1930 CA SER A 240 6710 5820 13582 1783 -692 1040 C ATOM 1931 C SER A 240 -11.556 -10.635 -47.250 1.00 60.76 C ANISOU 1931 C SER A 240 5476 5139 12472 1519 -562 1262 C ATOM 1932 O SER A 240 -11.564 -11.813 -46.891 1.00 59.51 O ANISOU 1932 O SER A 240 5284 5227 12101 1446 -374 1145 O ATOM 1933 CB SER A 240 -11.517 -9.667 -44.946 1.00 69.00 C ANISOU 1933 CB SER A 240 7055 5643 13520 1793 -762 786 C ATOM 1934 OG SER A 240 -10.116 -9.866 -45.014 1.00 71.16 O ANISOU 1934 OG SER A 240 7340 5801 13896 1460 -938 968 O ATOM 1935 N ALA A 241 -11.055 -10.238 -48.415 1.00 66.73 N ANISOU 1935 N ALA A 241 7469 6201 11683 3194 -97 164 N ATOM 1936 CA ALA A 241 -10.497 -11.184 -49.378 1.00 71.91 C ANISOU 1936 CA ALA A 241 8066 7012 12247 2977 222 458 C ATOM 1937 C ALA A 241 -9.257 -11.887 -48.824 1.00 67.57 C ANISOU 1937 C ALA A 241 7409 6260 12003 2673 212 403 C ATOM 1938 O ALA A 241 -9.034 -13.070 -49.085 1.00 64.31 O ANISOU 1938 O ALA A 241 6958 6139 11338 2502 387 439 O ATOM 1939 CB ALA A 241 -10.166 -10.476 -50.684 1.00 66.43 C ANISOU 1939 CB ALA A 241 7403 6068 11769 3067 467 932 C ATOM 1940 N THR A 242 -8.463 -11.147 -48.055 1.00 74.64 N ANISOU 1940 N THR A 242 8257 6636 13465 2624 -34 293 N ATOM 1941 CA THR A 242 -7.230 -11.672 -47.474 1.00 75.97 C ANISOU 1941 CA THR A 242 8303 6553 14008 2362 -109 220 C ATOM 1942 C THR A 242 -7.517 -12.790 -46.480 1.00 64.25 C ANISOU 1942 C THR A 242 6852 5484 12078 2321 -217 -147 C ATOM 1943 O THR A 242 -6.801 -13.793 -46.436 1.00 58.83 O ANISOU 1943 O THR A 242 6088 4879 11387 2097 -103 -116 O ATOM 1944 CB THR A 242 -6.425 -10.562 -46.768 1.00 67.60 C ANISOU 1944 CB THR A 242 7193 4865 13628 2328 -461 98 C ATOM 1945 OG1 THR A 242 -6.148 -9.511 -47.697 1.00 77.73 O ANISOU 1945 OG1 THR A 242 8444 5816 15274 2294 -322 491 O ATOM 1946 CG2 THR A 242 -5.114 -11.108 -46.235 1.00 67.48 C ANISOU 1946 CG2 THR A 242 7036 4661 13943 2019 -554 30 C ATOM 1947 N THR A 243 -8.570 -12.610 -45.686 1.00 60.58 N ANISOU 1947 N THR A 243 6497 5281 11240 2567 -410 -461 N ATOM 1948 CA THR A 243 -8.966 -13.619 -44.710 1.00 59.43 C ANISOU 1948 CA THR A 243 6375 5550 10656 2589 -460 -741 C ATOM 1949 C THR A 243 -9.435 -14.895 -45.421 1.00 58.35 C ANISOU 1949 C THR A 243 6178 5903 10088 2426 -133 -567 C ATOM 1950 O THR A 243 -9.221 -16.002 -44.930 1.00 54.57 O ANISOU 1950 O THR A 243 5660 5636 9437 2287 -82 -654 O ATOM 1951 CB THR A 243 -10.074 -13.099 -43.771 1.00 67.53 C ANISOU 1951 CB THR A 243 7515 6787 11355 2961 -669 -1042 C ATOM 1952 OG1 THR A 243 -9.678 -11.840 -43.213 1.00 67.65 O ANISOU 1952 OG1 THR A 243 7620 6302 11780 3158 -1030 -1240 O ATOM 1953 CG2 THR A 243 -10.322 -14.078 -42.639 1.00 58.54 C ANISOU 1953 CG2 THR A 243 6392 6023 9828 3030 -692 -1273 C ATOM 1954 N GLN A 244 -10.055 -14.741 -46.587 1.00 55.88 N ANISOU 1954 N GLN A 244 5867 5743 9621 2466 57 -331 N ATOM 1955 CA GLN A 244 -10.455 -15.899 -47.379 1.00 53.25 C ANISOU 1955 CA GLN A 244 5488 5808 8934 2339 287 -204 C ATOM 1956 C GLN A 244 -9.228 -16.629 -47.932 1.00 63.09 C ANISOU 1956 C GLN A 244 6703 6897 10373 2082 458 -20 C ATOM 1957 O GLN A 244 -9.176 -17.859 -47.924 1.00 56.81 O ANISOU 1957 O GLN A 244 5870 6346 9367 1924 546 -61 O ATOM 1958 CB GLN A 244 -11.385 -15.484 -48.522 1.00 54.33 C ANISOU 1958 CB GLN A 244 5663 6132 8847 2517 384 -34 C ATOM 1959 CG GLN A 244 -12.563 -14.617 -48.091 1.00 57.07 C ANISOU 1959 CG GLN A 244 6030 6606 9046 2805 228 -178 C ATOM 1960 CD GLN A 244 -13.296 -15.178 -46.886 1.00 59.73 C ANISOU 1960 CD GLN A 244 6290 7264 9143 2854 133 -444 C ATOM 1961 OE1 GLN A 244 -13.471 -14.492 -45.878 1.00 56.82 O ANISOU 1961 OE1 GLN A 244 5968 6805 8815 3057 -35 -633 O ATOM 1962 NE2 GLN A 244 -13.733 -16.427 -46.986 1.00 53.16 N ANISOU 1962 NE2 GLN A 244 5337 6794 8065 2703 241 -448 N ATOM 1963 N LYS A 245 -8.244 -15.871 -48.411 1.00 67.96 N ANISOU 1963 N LYS A 245 7311 7086 11424 2052 514 206 N ATOM 1964 CA LYS A 245 -7.001 -16.459 -48.906 1.00 55.10 C ANISOU 1964 CA LYS A 245 5618 5288 10032 1847 707 424 C ATOM 1965 C LYS A 245 -6.289 -17.213 -47.788 1.00 53.45 C ANISOU 1965 C LYS A 245 5340 5024 9946 1655 568 187 C ATOM 1966 O LYS A 245 -5.812 -18.335 -47.987 1.00 56.29 O ANISOU 1966 O LYS A 245 5673 5530 10185 1496 712 228 O ATOM 1967 CB LYS A 245 -6.074 -15.386 -49.488 1.00 67.39 C ANISOU 1967 CB LYS A 245 7108 6346 12149 1861 806 762 C ATOM 1968 CG LYS A 245 -6.523 -14.806 -50.823 1.00 81.98 C ANISOU 1968 CG LYS A 245 9039 8251 13858 2075 1051 1121 C ATOM 1969 CD LYS A 245 -5.486 -13.836 -51.379 1.00 98.38 C ANISOU 1969 CD LYS A 245 11005 9805 16568 2074 1224 1553 C ATOM 1970 CE LYS A 245 -5.903 -13.266 -52.730 1.00103.18 C ANISOU 1970 CE LYS A 245 11725 10487 16993 2354 1519 1974 C ATOM 1971 NZ LYS A 245 -7.110 -12.397 -52.639 1.00101.01 N ANISOU 1971 NZ LYS A 245 11573 10281 16524 2583 1325 1832 N ATOM 1972 N ALA A 246 -6.230 -16.591 -46.613 1.00 58.37 N ANISOU 1972 N ALA A 246 5958 5436 10783 1716 266 -78 N ATOM 1973 CA ALA A 246 -5.590 -17.191 -45.447 1.00 57.07 C ANISOU 1973 CA ALA A 246 5762 5220 10700 1619 82 -335 C ATOM 1974 C ALA A 246 -6.190 -18.552 -45.120 1.00 63.85 C ANISOU 1974 C ALA A 246 6658 6564 11038 1571 187 -450 C ATOM 1975 O ALA A 246 -5.469 -19.521 -44.879 1.00 59.00 O ANISOU 1975 O ALA A 246 6004 5974 10440 1402 240 -462 O ATOM 1976 CB ALA A 246 -5.705 -16.268 -44.251 1.00 54.26 C ANISOU 1976 CB ALA A 246 5464 4639 10513 1821 -305 -658 C ATOM 1977 N GLU A 247 -7.515 -18.615 -45.118 1.00 56.62 N ANISOU 1977 N GLU A 247 5791 6013 9708 1719 217 -513 N ATOM 1978 CA GLU A 247 -8.223 -19.845 -44.811 1.00 53.58 C ANISOU 1978 CA GLU A 247 5384 6053 8920 1669 316 -579 C ATOM 1979 C GLU A 247 -7.877 -20.952 -45.805 1.00 59.55 C ANISOU 1979 C GLU A 247 6104 6913 9609 1442 533 -402 C ATOM 1980 O GLU A 247 -7.637 -22.096 -45.415 1.00 52.73 O ANISOU 1980 O GLU A 247 5213 6172 8649 1300 582 -449 O ATOM 1981 CB GLU A 247 -9.731 -19.585 -44.787 1.00 60.87 C ANISOU 1981 CB GLU A 247 6296 7310 9520 1870 317 -623 C ATOM 1982 CG GLU A 247 -10.578 -20.831 -44.654 1.00 75.58 C ANISOU 1982 CG GLU A 247 8059 9579 11077 1790 440 -619 C ATOM 1983 CD GLU A 247 -11.091 -21.320 -45.989 1.00 94.63 C ANISOU 1983 CD GLU A 247 10418 12151 13385 1683 552 -478 C ATOM 1984 OE1 GLU A 247 -11.861 -20.578 -46.636 1.00104.81 O ANISOU 1984 OE1 GLU A 247 11711 13515 14598 1843 525 -436 O ATOM 1985 OE2 GLU A 247 -10.718 -22.440 -46.395 1.00 99.74 O ANISOU 1985 OE2 GLU A 247 11040 12840 14015 1475 637 -432 O ATOM 1986 N LYS A 248 -7.848 -20.605 -47.087 1.00 53.62 N ANISOU 1986 N LYS A 248 5377 6109 8889 1456 659 -197 N ATOM 1987 CA LYS A 248 -7.466 -21.553 -48.125 1.00 50.67 C ANISOU 1987 CA LYS A 248 5018 5821 8411 1336 844 -45 C ATOM 1988 C LYS A 248 -6.035 -22.060 -47.921 1.00 54.60 C ANISOU 1988 C LYS A 248 5486 6082 9176 1164 913 14 C ATOM 1989 O LYS A 248 -5.782 -23.265 -47.943 1.00 51.73 O ANISOU 1989 O LYS A 248 5125 5845 8684 1033 978 -20 O ATOM 1990 CB LYS A 248 -7.602 -20.917 -49.510 1.00 58.92 C ANISOU 1990 CB LYS A 248 6135 6845 9409 1492 975 190 C ATOM 1991 CG LYS A 248 -9.026 -20.852 -50.038 1.00 74.39 C ANISOU 1991 CG LYS A 248 8125 9122 11018 1658 914 130 C ATOM 1992 CD LYS A 248 -9.067 -20.187 -51.409 1.00 93.27 C ANISOU 1992 CD LYS A 248 10628 11489 13322 1881 1041 376 C ATOM 1993 CE LYS A 248 -10.467 -20.198 -52.008 1.00103.10 C ANISOU 1993 CE LYS A 248 11903 13064 14207 2073 931 286 C ATOM 1994 NZ LYS A 248 -10.898 -21.566 -52.413 1.00109.29 N ANISOU 1994 NZ LYS A 248 12678 14122 14725 2000 862 135 N ATOM 1995 N GLU A 249 -5.108 -21.131 -47.710 1.00 53.72 N ANISOU 1995 N GLU A 249 5327 5599 9487 1166 876 101 N ATOM 1996 CA GLU A 249 -3.696 -21.472 -47.577 1.00 58.31 C ANISOU 1996 CA GLU A 249 5822 5919 10413 1014 931 188 C ATOM 1997 C GLU A 249 -3.425 -22.290 -46.315 1.00 51.89 C ANISOU 1997 C GLU A 249 4993 5158 9565 910 764 -76 C ATOM 1998 O GLU A 249 -2.648 -23.244 -46.341 1.00 54.54 O ANISOU 1998 O GLU A 249 5300 5495 9928 779 856 -41 O ATOM 1999 CB GLU A 249 -2.841 -20.199 -47.581 1.00 66.37 C ANISOU 1999 CB GLU A 249 6728 6475 12015 1030 877 341 C ATOM 2000 CG GLU A 249 -1.365 -20.422 -47.275 1.00 92.33 C ANISOU 2000 CG GLU A 249 9852 9444 15787 868 872 413 C ATOM 2001 CD GLU A 249 -0.658 -21.274 -48.320 1.00104.63 C ANISOU 2001 CD GLU A 249 11377 11093 17286 810 1226 713 C ATOM 2002 OE1 GLU A 249 -1.121 -21.312 -49.480 1.00119.49 O ANISOU 2002 OE1 GLU A 249 13359 13167 18875 940 1482 940 O ATOM 2003 OE2 GLU A 249 0.368 -21.903 -47.977 1.00 90.28 O ANISOU 2003 OE2 GLU A 249 9448 9163 15692 679 1233 709 O ATOM 2004 N VAL A 250 -4.066 -21.918 -45.212 1.00 52.75 N ANISOU 2004 N VAL A 250 5137 5323 9581 1018 533 -325 N ATOM 2005 CA VAL A 250 -3.873 -22.631 -43.956 1.00 47.04 C ANISOU 2005 CA VAL A 250 4434 4680 8761 1008 389 -550 C ATOM 2006 C VAL A 250 -4.409 -24.060 -44.049 1.00 51.57 C ANISOU 2006 C VAL A 250 5032 5607 8953 910 560 -530 C ATOM 2007 O VAL A 250 -3.768 -25.006 -43.587 1.00 55.00 O ANISOU 2007 O VAL A 250 5464 6045 9390 810 575 -567 O ATOM 2008 CB VAL A 250 -4.549 -21.904 -42.787 1.00 51.47 C ANISOU 2008 CB VAL A 250 5064 5278 9213 1251 134 -801 C ATOM 2009 CG1 VAL A 250 -4.682 -22.828 -41.593 1.00 51.52 C ANISOU 2009 CG1 VAL A 250 5127 5512 8936 1324 82 -968 C ATOM 2010 CG2 VAL A 250 -3.764 -20.650 -42.415 1.00 51.65 C ANISOU 2010 CG2 VAL A 250 5065 4853 9708 1340 -152 -913 C ATOM 2011 N THR A 251 -5.575 -24.217 -44.664 1.00 50.21 N ANISOU 2011 N THR A 251 4871 5703 8504 941 663 -474 N ATOM 2012 CA THR A 251 -6.152 -25.542 -44.850 1.00 51.11 C ANISOU 2012 CA THR A 251 4969 6089 8363 828 778 -457 C ATOM 2013 C THR A 251 -5.217 -26.406 -45.690 1.00 52.93 C ANISOU 2013 C THR A 251 5220 6223 8667 667 905 -350 C ATOM 2014 O THR A 251 -5.014 -27.580 -45.392 1.00 46.76 O ANISOU 2014 O THR A 251 4439 5507 7822 550 941 -380 O ATOM 2015 CB THR A 251 -7.534 -25.478 -45.523 1.00 48.54 C ANISOU 2015 CB THR A 251 4608 6017 7817 888 807 -428 C ATOM 2016 OG1 THR A 251 -8.447 -24.765 -44.679 1.00 47.52 O ANISOU 2016 OG1 THR A 251 4443 6017 7596 1068 721 -513 O ATOM 2017 CG2 THR A 251 -8.073 -26.883 -45.767 1.00 43.22 C ANISOU 2017 CG2 THR A 251 3876 5542 7004 741 864 -425 C ATOM 2018 N ARG A 252 -4.635 -25.811 -46.727 1.00 47.55 N ANISOU 2018 N ARG A 252 4562 5383 8124 699 992 -200 N ATOM 2019 CA ARG A 252 -3.725 -26.529 -47.612 1.00 47.97 C ANISOU 2019 CA ARG A 252 4646 5368 8211 633 1153 -65 C ATOM 2020 C ARG A 252 -2.478 -26.997 -46.859 1.00 56.43 C ANISOU 2020 C ARG A 252 5664 6250 9524 518 1143 -87 C ATOM 2021 O ARG A 252 -2.072 -28.152 -46.982 1.00 59.32 O ANISOU 2021 O ARG A 252 6064 6669 9806 434 1214 -94 O ATOM 2022 CB ARG A 252 -3.330 -25.651 -48.804 1.00 59.48 C ANISOU 2022 CB ARG A 252 6125 6702 9772 764 1308 177 C ATOM 2023 CG ARG A 252 -2.494 -26.368 -49.862 1.00 67.21 C ANISOU 2023 CG ARG A 252 7163 7676 10698 801 1528 355 C ATOM 2024 CD ARG A 252 -2.137 -25.441 -51.020 1.00 74.30 C ANISOU 2024 CD ARG A 252 8080 8478 11673 1001 1747 673 C ATOM 2025 NE ARG A 252 -1.033 -24.539 -50.693 1.00 85.55 N ANISOU 2025 NE ARG A 252 9327 9553 13626 946 1825 882 N ATOM 2026 CZ ARG A 252 0.234 -24.754 -51.037 1.00 84.67 C ANISOU 2026 CZ ARG A 252 9114 9275 13782 936 2042 1123 C ATOM 2027 NH1 ARG A 252 0.560 -25.841 -51.723 1.00 78.75 N ANISOU 2027 NH1 ARG A 252 8473 8705 12743 1019 2216 1171 N ATOM 2028 NH2 ARG A 252 1.177 -23.881 -50.700 1.00 77.74 N ANISOU 2028 NH2 ARG A 252 8008 8034 13496 859 2067 1313 N ATOM 2029 N AMET A 253 -1.881 -26.099 -46.079 0.57 55.58 N ANISOU 2029 N AMET A 253 5476 5906 9735 535 1015 -122 N ATOM 2030 N BMET A 253 -1.884 -26.102 -46.075 0.43 55.49 N ANISOU 2030 N BMET A 253 5465 5895 9723 535 1014 -123 N ATOM 2031 CA AMET A 253 -0.678 -26.426 -45.315 0.57 53.72 C ANISOU 2031 CA AMET A 253 5168 5471 9774 455 937 -174 C ATOM 2032 CA BMET A 253 -0.680 -26.431 -45.318 0.43 53.30 C ANISOU 2032 CA BMET A 253 5115 5419 9719 455 938 -173 C ATOM 2033 C AMET A 253 -0.942 -27.493 -44.254 0.57 52.21 C ANISOU 2033 C AMET A 253 5040 5456 9340 425 844 -363 C ATOM 2034 C BMET A 253 -0.944 -27.498 -44.259 0.43 51.97 C ANISOU 2034 C BMET A 253 5011 5427 9309 425 845 -363 C ATOM 2035 O AMET A 253 -0.095 -28.351 -44.006 0.57 50.44 O ANISOU 2035 O AMET A 253 4804 5179 9182 349 869 -366 O ATOM 2036 O BMET A 253 -0.103 -28.363 -44.019 0.43 50.70 O ANISOU 2036 O BMET A 253 4839 5215 9211 348 872 -365 O ATOM 2037 CB AMET A 253 -0.102 -25.172 -44.653 0.57 46.14 C ANISOU 2037 CB AMET A 253 4101 4185 9244 508 716 -236 C ATOM 2038 CB BMET A 253 -0.100 -25.177 -44.662 0.43 47.24 C ANISOU 2038 CB BMET A 253 4241 4326 9384 507 718 -234 C ATOM 2039 CG AMET A 253 0.466 -24.148 -45.626 0.57 51.95 C ANISOU 2039 CG AMET A 253 4711 4642 10388 508 836 33 C ATOM 2040 CG BMET A 253 1.151 -25.430 -43.832 0.43 49.98 C ANISOU 2040 CG BMET A 253 4484 4440 10066 450 554 -331 C ATOM 2041 SD AMET A 253 1.783 -24.809 -46.674 0.57 53.74 S ANISOU 2041 SD AMET A 253 4812 4765 10843 418 1165 367 S ATOM 2042 SD BMET A 253 2.486 -26.228 -44.758 0.43 54.91 S ANISOU 2042 SD BMET A 253 4975 4955 10931 314 833 -55 S ATOM 2043 CE AMET A 253 2.942 -25.401 -45.440 0.57 54.24 C ANISOU 2043 CE AMET A 253 4751 4648 11209 310 930 165 C ATOM 2044 CE BMET A 253 2.819 -24.996 -46.011 0.43 56.04 C ANISOU 2044 CE BMET A 253 4961 4847 11485 334 1041 308 C ATOM 2045 N VAL A 254 -2.111 -27.436 -43.626 1.00 48.36 N ANISOU 2045 N VAL A 254 4610 5181 8584 510 764 -485 N ATOM 2046 CA VAL A 254 -2.458 -28.403 -42.590 1.00 56.10 C ANISOU 2046 CA VAL A 254 5636 6342 9340 524 735 -585 C ATOM 2047 C VAL A 254 -2.598 -29.796 -43.199 1.00 54.07 C ANISOU 2047 C VAL A 254 5393 6209 8941 364 907 -492 C ATOM 2048 O VAL A 254 -2.184 -30.790 -42.601 1.00 53.75 O ANISOU 2048 O VAL A 254 5377 6176 8869 316 922 -508 O ATOM 2049 CB VAL A 254 -3.751 -28.011 -41.853 1.00 54.25 C ANISOU 2049 CB VAL A 254 5421 6332 8859 691 679 -662 C ATOM 2050 CG1 VAL A 254 -4.314 -29.198 -41.073 1.00 53.69 C ANISOU 2050 CG1 VAL A 254 5358 6491 8551 692 773 -635 C ATOM 2051 CG2 VAL A 254 -3.484 -26.846 -40.918 1.00 49.17 C ANISOU 2051 CG2 VAL A 254 4818 5551 8313 917 441 -832 C ATOM 2052 N ILE A 255 -3.151 -29.856 -44.405 1.00 48.46 N ANISOU 2052 N ILE A 255 4685 5574 8153 314 1004 -411 N ATOM 2053 CA ILE A 255 -3.288 -31.116 -45.118 1.00 47.23 C ANISOU 2053 CA ILE A 255 4565 5491 7890 200 1092 -378 C ATOM 2054 C ILE A 255 -1.907 -31.660 -45.487 1.00 49.72 C ANISOU 2054 C ILE A 255 4922 5633 8335 155 1169 -327 C ATOM 2055 O ILE A 255 -1.632 -32.849 -45.322 1.00 55.26 O ANISOU 2055 O ILE A 255 5663 6332 9002 74 1192 -348 O ATOM 2056 CB ILE A 255 -4.160 -30.955 -46.384 1.00 45.72 C ANISOU 2056 CB ILE A 255 4396 5414 7563 235 1108 -355 C ATOM 2057 CG1 ILE A 255 -5.604 -30.623 -45.990 1.00 45.73 C ANISOU 2057 CG1 ILE A 255 4308 5607 7460 266 1030 -401 C ATOM 2058 CG2 ILE A 255 -4.130 -32.226 -47.231 1.00 48.25 C ANISOU 2058 CG2 ILE A 255 4788 5751 7793 169 1123 -380 C ATOM 2059 CD1 ILE A 255 -6.517 -30.365 -47.169 1.00 45.13 C ANISOU 2059 CD1 ILE A 255 4237 5648 7261 332 986 -408 C ATOM 2060 N ILE A 256 -1.036 -30.781 -45.971 1.00 51.66 N ANISOU 2060 N ILE A 256 5138 5720 8770 218 1221 -231 N ATOM 2061 CA ILE A 256 0.316 -31.171 -46.348 1.00 47.16 C ANISOU 2061 CA ILE A 256 4553 4992 8375 206 1332 -131 C ATOM 2062 C ILE A 256 1.088 -31.697 -45.135 1.00 51.26 C ANISOU 2062 C ILE A 256 5030 5414 9033 144 1231 -223 C ATOM 2063 O ILE A 256 1.797 -32.700 -45.223 1.00 47.21 O ANISOU 2063 O ILE A 256 4547 4868 8522 108 1299 -205 O ATOM 2064 CB ILE A 256 1.078 -29.994 -46.988 1.00 56.14 C ANISOU 2064 CB ILE A 256 5589 5948 9796 284 1434 60 C ATOM 2065 CG1 ILE A 256 0.444 -29.616 -48.329 1.00 48.44 C ANISOU 2065 CG1 ILE A 256 4698 5090 8617 415 1582 197 C ATOM 2066 CG2 ILE A 256 2.549 -30.339 -47.191 1.00 52.28 C ANISOU 2066 CG2 ILE A 256 5005 5284 9575 275 1565 202 C ATOM 2067 CD1 ILE A 256 0.954 -28.286 -48.890 1.00 45.87 C ANISOU 2067 CD1 ILE A 256 4262 4581 8585 512 1709 447 C ATOM 2068 N MET A 257 0.930 -31.034 -43.995 1.00 50.82 N ANISOU 2068 N MET A 257 4931 5321 9058 182 1050 -338 N ATOM 2069 CA MET A 257 1.642 -31.434 -42.786 1.00 47.56 C ANISOU 2069 CA MET A 257 4508 4832 8732 204 909 -449 C ATOM 2070 C MET A 257 1.148 -32.767 -42.242 1.00 53.68 C ANISOU 2070 C MET A 257 5388 5780 9227 174 953 -482 C ATOM 2071 O MET A 257 1.944 -33.616 -41.844 1.00 49.08 O ANISOU 2071 O MET A 257 4828 5137 8685 161 951 -489 O ATOM 2072 CB MET A 257 1.519 -30.356 -41.713 1.00 41.19 C ANISOU 2072 CB MET A 257 3676 3956 8018 341 658 -606 C ATOM 2073 CG MET A 257 2.317 -29.101 -42.038 1.00 41.90 C ANISOU 2073 CG MET A 257 3618 3753 8551 348 547 -582 C ATOM 2074 SD MET A 257 2.274 -27.871 -40.734 1.00 52.13 S ANISOU 2074 SD MET A 257 4911 4892 10005 550 139 -854 S ATOM 2075 CE MET A 257 0.545 -27.368 -40.754 1.00 47.30 C ANISOU 2075 CE MET A 257 4431 4557 8983 668 198 -880 C ATOM 2076 N VAL A 258 -0.170 -32.941 -42.225 1.00 47.18 N ANISOU 2076 N VAL A 258 4604 5153 8168 167 996 -477 N ATOM 2077 CA VAL A 258 -0.773 -34.166 -41.723 1.00 50.07 C ANISOU 2077 CA VAL A 258 5016 5648 8360 121 1060 -445 C ATOM 2078 C VAL A 258 -0.371 -35.360 -42.588 1.00 53.25 C ANISOU 2078 C VAL A 258 5461 5978 8792 -17 1156 -395 C ATOM 2079 O VAL A 258 0.035 -36.400 -42.073 1.00 53.45 O ANISOU 2079 O VAL A 258 5533 5961 8816 -44 1179 -375 O ATOM 2080 CB VAL A 258 -2.310 -34.046 -41.663 1.00 52.17 C ANISOU 2080 CB VAL A 258 5236 6117 8470 124 1098 -408 C ATOM 2081 CG1 VAL A 258 -2.947 -35.410 -41.517 1.00 53.81 C ANISOU 2081 CG1 VAL A 258 5421 6388 8635 8 1192 -311 C ATOM 2082 CG2 VAL A 258 -2.723 -33.131 -40.513 1.00 46.00 C ANISOU 2082 CG2 VAL A 258 4450 5443 7583 339 1020 -457 C ATOM 2083 N ILE A 259 -0.464 -35.194 -43.902 1.00 47.61 N ANISOU 2083 N ILE A 259 4757 5248 8083 -55 1204 -380 N ATOM 2084 CA ILE A 259 -0.079 -36.241 -44.841 1.00 42.44 C ANISOU 2084 CA ILE A 259 4187 4530 7408 -103 1263 -375 C ATOM 2085 C ILE A 259 1.408 -36.586 -44.747 1.00 51.96 C ANISOU 2085 C ILE A 259 5413 5590 8740 -64 1317 -344 C ATOM 2086 O ILE A 259 1.782 -37.760 -44.775 1.00 55.65 O ANISOU 2086 O ILE A 259 5958 5997 9190 -93 1337 -358 O ATOM 2087 CB ILE A 259 -0.429 -35.835 -46.289 1.00 49.36 C ANISOU 2087 CB ILE A 259 5110 5453 8192 -38 1294 -372 C ATOM 2088 CG1 ILE A 259 -1.947 -35.898 -46.492 1.00 58.04 C ANISOU 2088 CG1 ILE A 259 6182 6686 9183 -89 1194 -436 C ATOM 2089 CG2 ILE A 259 0.269 -36.739 -47.291 1.00 47.94 C ANISOU 2089 CG2 ILE A 259 5059 5204 7951 29 1355 -382 C ATOM 2090 CD1 ILE A 259 -2.389 -35.559 -47.896 1.00 61.05 C ANISOU 2090 CD1 ILE A 259 6639 7135 9423 28 1169 -470 C ATOM 2091 N ALA A 260 2.252 -35.566 -44.622 1.00 51.39 N ANISOU 2091 N ALA A 260 5247 5435 8845 3 1324 -300 N ATOM 2092 CA ALA A 260 3.688 -35.781 -44.504 1.00 44.64 C ANISOU 2092 CA ALA A 260 4337 4431 8192 39 1361 -253 C ATOM 2093 C ALA A 260 4.030 -36.538 -43.228 1.00 54.51 C ANISOU 2093 C ALA A 260 5612 5652 9446 31 1251 -332 C ATOM 2094 O ALA A 260 4.934 -37.380 -43.219 1.00 48.50 O ANISOU 2094 O ALA A 260 4873 4811 8744 48 1290 -314 O ATOM 2095 CB ALA A 260 4.435 -34.458 -44.545 1.00 43.48 C ANISOU 2095 CB ALA A 260 4015 4149 8355 85 1346 -177 C ATOM 2096 N PHE A 261 3.311 -36.233 -42.154 1.00 45.53 N ANISOU 2096 N PHE A 261 4486 4597 8217 54 1128 -405 N ATOM 2097 CA PHE A 261 3.522 -36.928 -40.893 1.00 58.47 C ANISOU 2097 CA PHE A 261 6184 6248 9784 123 1046 -447 C ATOM 2098 C PHE A 261 3.210 -38.416 -41.037 1.00 61.03 C ANISOU 2098 C PHE A 261 6614 6592 9981 41 1162 -379 C ATOM 2099 O PHE A 261 3.990 -39.271 -40.608 1.00 48.58 O ANISOU 2099 O PHE A 261 5090 4938 8431 80 1159 -368 O ATOM 2100 CB PHE A 261 2.664 -36.317 -39.789 1.00 53.36 C ANISOU 2100 CB PHE A 261 5557 5734 8982 246 941 -503 C ATOM 2101 CG PHE A 261 2.878 -36.946 -38.446 1.00 58.69 C ANISOU 2101 CG PHE A 261 6324 6458 9517 413 877 -517 C ATOM 2102 CD1 PHE A 261 3.900 -36.510 -37.623 1.00 68.80 C ANISOU 2102 CD1 PHE A 261 7605 7647 10889 599 655 -656 C ATOM 2103 CD2 PHE A 261 2.058 -37.972 -38.006 1.00 63.72 C ANISOU 2103 CD2 PHE A 261 7036 7215 9958 408 1027 -377 C ATOM 2104 CE1 PHE A 261 4.101 -37.085 -36.386 1.00 67.55 C ANISOU 2104 CE1 PHE A 261 7569 7559 10537 827 581 -675 C ATOM 2105 CE2 PHE A 261 2.256 -38.555 -36.768 1.00 63.04 C ANISOU 2105 CE2 PHE A 261 7053 7189 9711 618 1015 -331 C ATOM 2106 CZ PHE A 261 3.279 -38.110 -35.957 1.00 54.00 C ANISOU 2106 CZ PHE A 261 5957 5994 8565 854 790 -491 C ATOM 2107 N LEU A 262 2.069 -38.717 -41.646 1.00 53.24 N ANISOU 2107 N LEU A 262 5647 5682 8899 -67 1232 -342 N ATOM 2108 CA LEU A 262 1.643 -40.098 -41.830 1.00 57.23 C ANISOU 2108 CA LEU A 262 6224 6142 9380 -170 1286 -293 C ATOM 2109 C LEU A 262 2.614 -40.849 -42.733 1.00 60.71 C ANISOU 2109 C LEU A 262 6748 6438 9881 -172 1312 -331 C ATOM 2110 O LEU A 262 2.970 -41.989 -42.455 1.00 57.45 O ANISOU 2110 O LEU A 262 6415 5919 9494 -183 1323 -309 O ATOM 2111 CB LEU A 262 0.228 -40.151 -42.404 1.00 48.62 C ANISOU 2111 CB LEU A 262 5086 5126 8263 -288 1285 -281 C ATOM 2112 CG LEU A 262 -0.872 -39.659 -41.462 1.00 57.32 C ANISOU 2112 CG LEU A 262 6084 6390 9306 -266 1309 -193 C ATOM 2113 CD1 LEU A 262 -2.195 -39.521 -42.197 1.00 51.67 C ANISOU 2113 CD1 LEU A 262 5266 5747 8619 -378 1284 -195 C ATOM 2114 CD2 LEU A 262 -1.014 -40.600 -40.271 1.00 55.24 C ANISOU 2114 CD2 LEU A 262 5826 6120 9041 -238 1395 -35 C ATOM 2115 N ILE A 263 3.054 -40.200 -43.804 1.00 58.24 N ANISOU 2115 N ILE A 263 6424 6124 9581 -122 1344 -363 N ATOM 2116 CA ILE A 263 4.014 -40.813 -44.716 1.00 55.93 C ANISOU 2116 CA ILE A 263 6214 5737 9300 -40 1414 -372 C ATOM 2117 C ILE A 263 5.297 -41.194 -43.974 1.00 54.70 C ANISOU 2117 C ILE A 263 6031 5486 9266 26 1429 -338 C ATOM 2118 O ILE A 263 5.915 -42.217 -44.259 1.00 52.04 O ANISOU 2118 O ILE A 263 5792 5058 8924 80 1465 -348 O ATOM 2119 CB ILE A 263 4.348 -39.873 -45.894 1.00 56.26 C ANISOU 2119 CB ILE A 263 6222 5827 9329 73 1516 -327 C ATOM 2120 CG1 ILE A 263 3.153 -39.767 -46.842 1.00 53.05 C ANISOU 2120 CG1 ILE A 263 5900 5514 8744 73 1473 -393 C ATOM 2121 CG2 ILE A 263 5.571 -40.363 -46.658 1.00 59.71 C ANISOU 2121 CG2 ILE A 263 6707 6197 9782 237 1653 -272 C ATOM 2122 CD1 ILE A 263 3.412 -38.882 -48.045 1.00 62.73 C ANISOU 2122 CD1 ILE A 263 7133 6810 9891 252 1603 -310 C ATOM 2123 N CYS A 264 5.671 -40.382 -42.993 1.00 55.71 N ANISOU 2123 N CYS A 264 6034 5628 9506 48 1363 -325 N ATOM 2124 CA CYS A 264 6.914 -40.598 -42.263 1.00 58.57 C ANISOU 2124 CA CYS A 264 6341 5899 10015 139 1314 -323 C ATOM 2125 C CYS A 264 6.838 -41.752 -41.266 1.00 56.62 C ANISOU 2125 C CYS A 264 6220 5630 9661 160 1264 -330 C ATOM 2126 O CYS A 264 7.794 -42.513 -41.130 1.00 50.00 O ANISOU 2126 O CYS A 264 5413 4702 8884 237 1270 -322 O ATOM 2127 CB CYS A 264 7.323 -39.322 -41.526 1.00 42.19 C ANISOU 2127 CB CYS A 264 4096 3808 8125 190 1169 -362 C ATOM 2128 SG CYS A 264 8.924 -39.417 -40.679 1.00 52.12 S ANISOU 2128 SG CYS A 264 5224 4928 9652 321 1014 -406 S ATOM 2129 N TRP A 265 5.711 -41.886 -40.573 1.00 55.29 N ANISOU 2129 N TRP A 265 6112 5547 9347 116 1241 -308 N ATOM 2130 CA TRP A 265 5.649 -42.781 -39.419 1.00 59.80 C ANISOU 2130 CA TRP A 265 6781 6113 9828 191 1229 -243 C ATOM 2131 C TRP A 265 4.696 -43.966 -39.557 1.00 63.41 C ANISOU 2131 C TRP A 265 7328 6517 10249 65 1330 -131 C ATOM 2132 O TRP A 265 4.848 -44.966 -38.856 1.00 65.97 O ANISOU 2132 O TRP A 265 7740 6767 10559 120 1365 -27 O ATOM 2133 CB TRP A 265 5.280 -41.982 -38.167 1.00 55.69 C ANISOU 2133 CB TRP A 265 6241 5734 9184 343 1138 -249 C ATOM 2134 CG TRP A 265 6.399 -41.115 -37.691 1.00 63.27 C ANISOU 2134 CG TRP A 265 7128 6666 10246 509 942 -391 C ATOM 2135 CD1 TRP A 265 6.438 -39.750 -37.690 1.00 64.77 C ANISOU 2135 CD1 TRP A 265 7201 6872 10535 545 798 -510 C ATOM 2136 CD2 TRP A 265 7.657 -41.554 -37.165 1.00 73.19 C ANISOU 2136 CD2 TRP A 265 8394 7829 11587 657 826 -442 C ATOM 2137 NE1 TRP A 265 7.640 -39.313 -37.185 1.00 72.17 N ANISOU 2137 NE1 TRP A 265 8054 7705 11664 689 573 -640 N ATOM 2138 CE2 TRP A 265 8.406 -40.401 -36.857 1.00 73.57 C ANISOU 2138 CE2 TRP A 265 8299 7830 11824 766 584 -605 C ATOM 2139 CE3 TRP A 265 8.220 -42.812 -36.920 1.00 80.24 C ANISOU 2139 CE3 TRP A 265 9392 8651 12443 717 881 -369 C ATOM 2140 CZ2 TRP A 265 9.689 -40.467 -36.317 1.00 82.37 C ANISOU 2140 CZ2 TRP A 265 9345 8840 13113 925 374 -709 C ATOM 2141 CZ3 TRP A 265 9.493 -42.875 -36.385 1.00 77.96 C ANISOU 2141 CZ3 TRP A 265 9063 8291 12267 897 705 -461 C ATOM 2142 CH2 TRP A 265 10.213 -41.710 -36.088 1.00 80.88 C ANISOU 2142 CH2 TRP A 265 9262 8625 12844 996 445 -634 C ATOM 2143 N LEU A 266 3.716 -43.857 -40.446 1.00 63.14 N ANISOU 2143 N LEU A 266 7258 6494 10238 -93 1354 -146 N ATOM 2144 CA LEU A 266 2.756 -44.942 -40.639 1.00 62.07 C ANISOU 2144 CA LEU A 266 7150 6249 10185 -243 1384 -62 C ATOM 2145 C LEU A 266 3.399 -46.248 -41.142 1.00 66.69 C ANISOU 2145 C LEU A 266 7868 6600 10871 -258 1359 -101 C ATOM 2146 O LEU A 266 2.979 -47.329 -40.726 1.00 63.94 O ANISOU 2146 O LEU A 266 7551 6097 10647 -330 1379 23 O ATOM 2147 CB LEU A 266 1.644 -44.500 -41.594 1.00 55.33 C ANISOU 2147 CB LEU A 266 6215 5443 9365 -385 1338 -131 C ATOM 2148 CG LEU A 266 0.278 -45.150 -41.419 1.00 63.93 C ANISOU 2148 CG LEU A 266 7204 6474 10613 -553 1343 -7 C ATOM 2149 CD1 LEU A 266 -0.169 -45.020 -39.976 1.00 67.57 C ANISOU 2149 CD1 LEU A 266 7579 7065 11029 -483 1493 240 C ATOM 2150 CD2 LEU A 266 -0.716 -44.494 -42.357 1.00 63.01 C ANISOU 2150 CD2 LEU A 266 6988 6438 10514 -648 1249 -116 C ATOM 2151 N PRO A 267 4.407 -46.162 -42.039 1.00 66.24 N ANISOU 2151 N PRO A 267 7881 6506 10782 -166 1331 -244 N ATOM 2152 CA PRO A 267 5.089 -47.410 -42.408 1.00 63.61 C ANISOU 2152 CA PRO A 267 7697 5963 10508 -112 1307 -289 C ATOM 2153 C PRO A 267 5.722 -48.143 -41.224 1.00 61.63 C ANISOU 2153 C PRO A 267 7495 5633 10290 -31 1348 -156 C ATOM 2154 O PRO A 267 5.508 -49.349 -41.074 1.00 61.54 O ANISOU 2154 O PRO A 267 7580 5410 10391 -78 1333 -94 O ATOM 2155 CB PRO A 267 6.167 -46.939 -43.384 1.00 60.07 C ANISOU 2155 CB PRO A 267 7275 5568 9982 51 1340 -401 C ATOM 2156 CG PRO A 267 5.586 -45.731 -44.007 1.00 58.83 C ANISOU 2156 CG PRO A 267 7019 5576 9758 14 1351 -435 C ATOM 2157 CD PRO A 267 4.824 -45.048 -42.913 1.00 65.31 C ANISOU 2157 CD PRO A 267 7709 6509 10595 -96 1343 -341 C ATOM 2158 N TYR A 268 6.489 -47.430 -40.406 1.00 57.15 N ANISOU 2158 N TYR A 268 6863 5207 9646 109 1369 -122 N ATOM 2159 CA TYR A 268 7.100 -48.027 -39.222 1.00 63.33 C ANISOU 2159 CA TYR A 268 7709 5952 10402 255 1377 -12 C ATOM 2160 C TYR A 268 6.033 -48.560 -38.274 1.00 68.88 C ANISOU 2160 C TYR A 268 8438 6642 11091 207 1454 204 C ATOM 2161 O TYR A 268 6.140 -49.679 -37.773 1.00 71.61 O ANISOU 2161 O TYR A 268 8887 6831 11490 251 1504 351 O ATOM 2162 CB TYR A 268 7.990 -47.013 -38.496 1.00 56.72 C ANISOU 2162 CB TYR A 268 6780 5270 9502 437 1301 -68 C ATOM 2163 CG TYR A 268 9.469 -47.225 -38.731 1.00 66.75 C ANISOU 2163 CG TYR A 268 8032 6466 10864 580 1252 -149 C ATOM 2164 CD1 TYR A 268 10.020 -48.501 -38.709 1.00 71.91 C ANISOU 2164 CD1 TYR A 268 8822 6963 11537 658 1280 -106 C ATOM 2165 CD2 TYR A 268 10.314 -46.150 -38.986 1.00 62.86 C ANISOU 2165 CD2 TYR A 268 7355 6037 10491 638 1181 -247 C ATOM 2166 CE1 TYR A 268 11.371 -48.702 -38.925 1.00 71.81 C ANISOU 2166 CE1 TYR A 268 8769 6900 11615 814 1250 -167 C ATOM 2167 CE2 TYR A 268 11.665 -46.341 -39.206 1.00 70.04 C ANISOU 2167 CE2 TYR A 268 8180 6877 11553 767 1158 -279 C ATOM 2168 CZ TYR A 268 12.189 -47.619 -39.173 1.00 77.16 C ANISOU 2168 CZ TYR A 268 9224 7664 12427 866 1198 -243 C ATOM 2169 OH TYR A 268 13.535 -47.811 -39.392 1.00 77.45 O ANISOU 2169 OH TYR A 268 9156 7652 12621 1021 1190 -262 O ATOM 2170 N ALA A 269 5.002 -47.756 -38.037 1.00 67.15 N ANISOU 2170 N ALA A 269 8111 6585 10817 137 1490 260 N ATOM 2171 CA ALA A 269 3.911 -48.165 -37.164 1.00 64.94 C ANISOU 2171 CA ALA A 269 7801 6329 10542 118 1625 530 C ATOM 2172 C ALA A 269 3.184 -49.369 -37.754 1.00 67.02 C ANISOU 2172 C ALA A 269 8052 6314 11097 -120 1657 637 C ATOM 2173 O ALA A 269 2.811 -50.293 -37.032 1.00 66.14 O ANISOU 2173 O ALA A 269 7951 6074 11106 -115 1784 917 O ATOM 2174 CB ALA A 269 2.945 -47.013 -36.937 1.00 65.48 C ANISOU 2174 CB ALA A 269 7737 6638 10504 110 1659 552 C ATOM 2175 N GLY A 270 2.996 -49.359 -39.070 1.00 61.18 N ANISOU 2175 N GLY A 270 7294 5464 10488 -297 1524 416 N ATOM 2176 CA GLY A 270 2.307 -50.443 -39.746 1.00 56.29 C ANISOU 2176 CA GLY A 270 6665 4538 10185 -507 1445 423 C ATOM 2177 C GLY A 270 3.079 -51.748 -39.694 1.00 64.22 C ANISOU 2177 C GLY A 270 7838 5246 11316 -452 1414 444 C ATOM 2178 O GLY A 270 2.534 -52.792 -39.336 1.00 61.66 O ANISOU 2178 O GLY A 270 7486 4654 11289 -565 1445 654 O ATOM 2179 N VAL A 271 4.356 -51.687 -40.053 1.00 65.72 N ANISOU 2179 N VAL A 271 8181 5468 11323 -271 1362 252 N ATOM 2180 CA VAL A 271 5.209 -52.867 -40.037 1.00 65.63 C ANISOU 2180 CA VAL A 271 8345 5199 11392 -167 1328 246 C ATOM 2181 C VAL A 271 5.335 -53.440 -38.625 1.00 69.09 C ANISOU 2181 C VAL A 271 8805 5600 11846 -68 1485 573 C ATOM 2182 O VAL A 271 5.178 -54.644 -38.424 1.00 66.61 O ANISOU 2182 O VAL A 271 8561 4971 11777 -116 1493 727 O ATOM 2183 CB VAL A 271 6.603 -52.550 -40.596 1.00 59.96 C ANISOU 2183 CB VAL A 271 7732 4585 10466 52 1291 24 C ATOM 2184 CG1 VAL A 271 7.547 -53.715 -40.355 1.00 64.81 C ANISOU 2184 CG1 VAL A 271 8517 4977 11131 210 1281 51 C ATOM 2185 CG2 VAL A 271 6.507 -52.236 -42.083 1.00 54.55 C ANISOU 2185 CG2 VAL A 271 7079 3903 9744 34 1176 -249 C ATOM 2186 N ALA A 272 5.601 -52.575 -37.651 1.00 65.17 N ANISOU 2186 N ALA A 272 8261 5409 11090 102 1592 679 N ATOM 2187 CA ALA A 272 5.718 -53.005 -36.261 1.00 64.43 C ANISOU 2187 CA ALA A 272 8225 5349 10906 299 1743 991 C ATOM 2188 C ALA A 272 4.438 -53.678 -35.791 1.00 74.82 C ANISOU 2188 C ALA A 272 9446 6510 12472 147 1916 1359 C ATOM 2189 O ALA A 272 4.477 -54.726 -35.147 1.00 80.70 O ANISOU 2189 O ALA A 272 10266 7047 13348 218 2036 1650 O ATOM 2190 CB ALA A 272 6.052 -51.827 -35.362 1.00 61.06 C ANISOU 2190 CB ALA A 272 7772 5292 10136 550 1761 977 C ATOM 2191 N PHE A 273 3.304 -53.068 -36.121 1.00 75.66 N ANISOU 2191 N PHE A 273 9360 6706 12681 -57 1939 1377 N ATOM 2192 CA PHE A 273 2.008 -53.610 -35.740 1.00 78.14 C ANISOU 2192 CA PHE A 273 9492 6877 13320 -228 2114 1756 C ATOM 2193 C PHE A 273 1.774 -54.973 -36.389 1.00 85.94 C ANISOU 2193 C PHE A 273 10474 7360 14820 -477 2005 1788 C ATOM 2194 O PHE A 273 1.215 -55.878 -35.768 1.00 81.41 O ANISOU 2194 O PHE A 273 9811 6542 14579 -537 2180 2201 O ATOM 2195 CB PHE A 273 0.888 -52.638 -36.123 1.00 80.83 C ANISOU 2195 CB PHE A 273 9600 7413 13698 -400 2112 1709 C ATOM 2196 CG PHE A 273 -0.488 -53.126 -35.768 1.00 96.93 C ANISOU 2196 CG PHE A 273 11371 9315 16142 -586 2302 2123 C ATOM 2197 CD1 PHE A 273 -1.001 -52.932 -34.496 1.00104.70 C ANISOU 2197 CD1 PHE A 273 12265 10533 16982 -370 2648 2582 C ATOM 2198 CD2 PHE A 273 -1.272 -53.777 -36.709 1.00102.58 C ANISOU 2198 CD2 PHE A 273 11909 9665 17401 -944 2124 2060 C ATOM 2199 CE1 PHE A 273 -2.268 -53.381 -34.167 1.00107.13 C ANISOU 2199 CE1 PHE A 273 12267 10720 17717 -530 2882 3039 C ATOM 2200 CE2 PHE A 273 -2.538 -54.230 -36.386 1.00106.56 C ANISOU 2200 CE2 PHE A 273 12094 10025 18369 -1133 2273 2453 C ATOM 2201 CZ PHE A 273 -3.037 -54.031 -35.114 1.00105.41 C ANISOU 2201 CZ PHE A 273 11822 10143 18086 -926 2669 2954 C ATOM 2202 N TYR A 274 2.206 -55.112 -37.640 1.00 86.87 N ANISOU 2202 N TYR A 274 10690 7308 15009 -587 1712 1362 N ATOM 2203 CA TYR A 274 2.043 -56.367 -38.368 1.00 81.38 C ANISOU 2203 CA TYR A 274 10036 6108 14778 -773 1511 1281 C ATOM 2204 C TYR A 274 2.866 -57.475 -37.723 1.00 82.39 C ANISOU 2204 C TYR A 274 10355 5986 14965 -611 1595 1476 C ATOM 2205 O TYR A 274 2.348 -58.552 -37.432 1.00 78.37 O ANISOU 2205 O TYR A 274 9777 5119 14881 -740 1619 1748 O ATOM 2206 CB TYR A 274 2.442 -56.198 -39.838 1.00 73.86 C ANISOU 2206 CB TYR A 274 9217 5099 13748 -791 1182 751 C ATOM 2207 CG TYR A 274 2.265 -57.451 -40.668 1.00 86.72 C ANISOU 2207 CG TYR A 274 10933 6198 15819 -919 887 570 C ATOM 2208 CD1 TYR A 274 1.047 -57.744 -41.269 1.00 87.21 C ANISOU 2208 CD1 TYR A 274 10808 6099 16229 -1172 642 493 C ATOM 2209 CD2 TYR A 274 3.316 -58.342 -40.851 1.00 97.44 C ANISOU 2209 CD2 TYR A 274 12561 7320 17143 -736 796 438 C ATOM 2210 CE1 TYR A 274 0.881 -58.889 -42.029 1.00 88.50 C ANISOU 2210 CE1 TYR A 274 11067 5909 16651 -1228 284 265 C ATOM 2211 CE2 TYR A 274 3.158 -59.490 -41.607 1.00100.19 C ANISOU 2211 CE2 TYR A 274 13022 7319 17727 -789 463 224 C ATOM 2212 CZ TYR A 274 1.939 -59.758 -42.195 1.00 99.50 C ANISOU 2212 CZ TYR A 274 12761 7087 17957 -1034 197 128 C ATOM 2213 OH TYR A 274 1.779 -60.899 -42.949 1.00113.63 O ANISOU 2213 OH TYR A 274 14673 8516 19986 -1059 -171 -118 O ATOM 2214 N ILE A 275 4.149 -57.202 -37.501 1.00 76.61 N ANISOU 2214 N ILE A 275 9833 5473 13801 -317 1615 1332 N ATOM 2215 CA ILE A 275 5.048 -58.165 -36.876 1.00 79.49 C ANISOU 2215 CA ILE A 275 10397 5654 14154 -105 1682 1490 C ATOM 2216 C ILE A 275 4.561 -58.529 -35.475 1.00 90.17 C ANISOU 2216 C ILE A 275 11680 7010 15571 -18 1996 2052 C ATOM 2217 O ILE A 275 4.625 -59.690 -35.069 1.00 88.76 O ANISOU 2217 O ILE A 275 11578 6476 15673 6 2071 2331 O ATOM 2218 CB ILE A 275 6.491 -57.622 -36.806 1.00 70.93 C ANISOU 2218 CB ILE A 275 9481 4867 12601 212 1644 1247 C ATOM 2219 CG1 ILE A 275 6.978 -57.260 -38.210 1.00 69.95 C ANISOU 2219 CG1 ILE A 275 9407 4759 12410 175 1414 777 C ATOM 2220 CG2 ILE A 275 7.422 -58.644 -36.173 1.00 65.22 C ANISOU 2220 CG2 ILE A 275 8960 3957 11865 456 1689 1397 C ATOM 2221 CD1 ILE A 275 8.381 -56.715 -38.258 1.00 73.59 C ANISOU 2221 CD1 ILE A 275 9951 5482 12529 456 1397 578 C ATOM 2222 N PHE A 276 4.061 -57.534 -34.748 1.00 89.63 N ANISOU 2222 N PHE A 276 11478 7343 15234 68 2192 2235 N ATOM 2223 CA PHE A 276 3.502 -57.758 -33.420 1.00 88.16 C ANISOU 2223 CA PHE A 276 11229 7241 15028 234 2542 2804 C ATOM 2224 C PHE A 276 2.302 -58.695 -33.502 1.00100.50 C ANISOU 2224 C PHE A 276 12562 8377 17247 -84 2668 3197 C ATOM 2225 O PHE A 276 2.209 -59.669 -32.753 1.00108.02 O ANISOU 2225 O PHE A 276 13516 9217 18312 14 2827 3567 O ATOM 2226 CB PHE A 276 3.095 -56.430 -32.773 1.00 87.58 C ANISOU 2226 CB PHE A 276 11061 7688 14529 414 2689 2858 C ATOM 2227 CG PHE A 276 2.786 -56.537 -31.306 1.00 93.97 C ANISOU 2227 CG PHE A 276 11894 8698 15111 770 3059 3406 C ATOM 2228 CD1 PHE A 276 1.507 -56.852 -30.872 1.00105.84 C ANISOU 2228 CD1 PHE A 276 13154 10126 16936 662 3386 3939 C ATOM 2229 CD2 PHE A 276 3.773 -56.319 -30.360 1.00 90.56 C ANISOU 2229 CD2 PHE A 276 11720 8540 14147 1256 3079 3402 C ATOM 2230 CE1 PHE A 276 1.221 -56.952 -29.522 1.00107.59 C ANISOU 2230 CE1 PHE A 276 13412 10569 16899 1069 3788 4502 C ATOM 2231 CE2 PHE A 276 3.493 -56.416 -29.009 1.00 99.08 C ANISOU 2231 CE2 PHE A 276 12874 9840 14933 1682 3414 3900 C ATOM 2232 CZ PHE A 276 2.215 -56.734 -28.590 1.00106.76 C ANISOU 2232 CZ PHE A 276 13625 10763 16175 1608 3801 4473 C ATOM 2233 N THR A 277 1.391 -58.397 -34.424 1.00103.39 N ANISOU 2233 N THR A 277 12689 8708 17888 -432 2473 2966 N ATOM 2234 CA THR A 277 0.188 -59.202 -34.608 1.00110.95 C ANISOU 2234 CA THR A 277 13351 9468 19335 -720 2406 3126 C ATOM 2235 C THR A 277 0.518 -60.555 -35.233 1.00122.01 C ANISOU 2235 C THR A 277 14862 10414 21084 -858 2107 2942 C ATOM 2236 O THR A 277 -0.054 -61.580 -34.858 1.00131.36 O ANISOU 2236 O THR A 277 15897 11368 22646 -951 2160 3246 O ATOM 2237 CB THR A 277 -0.846 -58.475 -35.493 1.00106.87 C ANISOU 2237 CB THR A 277 12574 9040 18993 -1003 2213 2876 C ATOM 2238 OG1 THR A 277 -1.056 -57.147 -34.998 1.00106.11 O ANISOU 2238 OG1 THR A 277 12411 9365 18540 -860 2462 2991 O ATOM 2239 CG2 THR A 277 -2.169 -59.223 -35.496 1.00122.87 C ANISOU 2239 CG2 THR A 277 14249 10885 21551 -1242 2177 3111 C ATOM 2240 N HIS A 278 1.443 -60.551 -36.188 1.00142.89 N ANISOU 2240 N HIS A 278 20794 11071 22427 -2318 2506 2530 N ATOM 2241 CA HIS A 278 1.823 -61.771 -36.894 1.00136.30 C ANISOU 2241 CA HIS A 278 20167 9866 21757 -2272 2260 2447 C ATOM 2242 C HIS A 278 3.248 -62.189 -36.545 1.00143.61 C ANISOU 2242 C HIS A 278 21370 10538 22657 -1953 2024 2491 C ATOM 2243 O HIS A 278 4.138 -62.142 -37.395 1.00146.40 O ANISOU 2243 O HIS A 278 21673 10839 23113 -1656 1896 2282 O ATOM 2244 CB HIS A 278 1.704 -61.587 -38.413 1.00125.64 C ANISOU 2244 CB HIS A 278 18550 8593 20596 -2188 2257 2134 C ATOM 2245 CG HIS A 278 0.318 -61.276 -38.892 1.00128.19 C ANISOU 2245 CG HIS A 278 18599 9152 20957 -2483 2450 2064 C ATOM 2246 ND1 HIS A 278 -0.674 -60.798 -38.064 1.00139.50 N ANISOU 2246 ND1 HIS A 278 19938 10820 22245 -2742 2662 2228 N ATOM 2247 CD2 HIS A 278 -0.237 -61.374 -40.123 1.00128.78 C ANISOU 2247 CD2 HIS A 278 18463 9281 21184 -2548 2455 1839 C ATOM 2248 CE1 HIS A 278 -1.780 -60.615 -38.763 1.00144.38 C ANISOU 2248 CE1 HIS A 278 20300 11631 22927 -2947 2784 2105 C ATOM 2249 NE2 HIS A 278 -1.541 -60.957 -40.016 1.00139.44 N ANISOU 2249 NE2 HIS A 278 19602 10898 22482 -2838 2661 1873 N ATOM 2250 N GLN A 279 3.468 -62.587 -35.296 1.00146.35 N ANISOU 2250 N GLN A 279 21996 10750 22861 -2009 1960 2758 N ATOM 2251 CA GLN A 279 4.776 -63.088 -34.889 1.00145.32 C ANISOU 2251 CA GLN A 279 22148 10367 22700 -1719 1710 2814 C ATOM 2252 C GLN A 279 4.941 -64.541 -35.323 1.00132.82 C ANISOU 2252 C GLN A 279 20859 8346 21260 -1734 1428 2788 C ATOM 2253 O GLN A 279 4.027 -65.353 -35.181 1.00125.56 O ANISOU 2253 O GLN A 279 20068 7258 20380 -2059 1405 2906 O ATOM 2254 CB GLN A 279 4.975 -62.947 -33.378 1.00149.25 C ANISOU 2254 CB GLN A 279 22821 10897 22992 -1766 1729 3107 C ATOM 2255 CG GLN A 279 5.782 -61.716 -32.984 1.00140.08 C ANISOU 2255 CG GLN A 279 21513 10030 21683 -1494 1824 3092 C ATOM 2256 CD GLN A 279 6.093 -61.663 -31.502 1.00141.81 C ANISOU 2256 CD GLN A 279 21926 10262 21693 -1513 1807 3371 C ATOM 2257 OE1 GLN A 279 5.597 -62.474 -30.721 1.00153.80 O ANISOU 2257 OE1 GLN A 279 23656 11603 23177 -1762 1753 3590 O ATOM 2258 NE2 GLN A 279 6.925 -60.704 -31.107 1.00129.13 N ANISOU 2258 NE2 GLN A 279 20241 8877 19946 -1258 1841 3369 N ATOM 2259 N GLY A 280 6.117 -64.854 -35.856 1.00128.08 N ANISOU 2259 N GLY A 280 20362 7572 20728 -1375 1204 2631 N ATOM 2260 CA GLY A 280 6.358 -66.138 -36.484 1.00134.78 C ANISOU 2260 CA GLY A 280 21469 8024 21718 -1321 925 2537 C ATOM 2261 C GLY A 280 6.157 -66.008 -37.980 1.00140.72 C ANISOU 2261 C GLY A 280 21986 8859 22621 -1251 967 2221 C ATOM 2262 O GLY A 280 5.332 -66.699 -38.568 1.00150.69 O ANISOU 2262 O GLY A 280 23291 9977 23987 -1482 944 2169 O ATOM 2263 N SER A 281 6.914 -65.107 -38.595 1.00140.76 N ANISOU 2263 N SER A 281 21729 9115 22638 -943 1021 2014 N ATOM 2264 CA SER A 281 6.770 -64.832 -40.019 1.00146.22 C ANISOU 2264 CA SER A 281 22131 9949 23478 -869 1067 1711 C ATOM 2265 C SER A 281 8.076 -64.332 -40.630 1.00142.97 C ANISOU 2265 C SER A 281 21582 9665 23077 -434 967 1495 C ATOM 2266 O SER A 281 8.900 -63.719 -39.951 1.00141.28 O ANISOU 2266 O SER A 281 21368 9575 22739 -231 963 1581 O ATOM 2267 CB SER A 281 5.653 -63.812 -40.248 1.00151.39 C ANISOU 2267 CB SER A 281 22406 10968 24146 -1133 1371 1690 C ATOM 2268 OG SER A 281 5.703 -62.777 -39.281 1.00148.22 O ANISOU 2268 OG SER A 281 21901 10826 23588 -1142 1548 1854 O ATOM 2269 N ASP A 282 8.252 -64.599 -41.920 1.00135.19 N ANISOU 2269 N ASP A 282 20471 8668 22228 -300 881 1217 N ATOM 2270 CA ASP A 282 9.474 -64.240 -42.627 1.00117.18 C ANISOU 2270 CA ASP A 282 18045 6520 19959 106 766 988 C ATOM 2271 C ASP A 282 9.438 -62.804 -43.132 1.00102.94 C ANISOU 2271 C ASP A 282 15781 5163 18166 130 959 862 C ATOM 2272 O ASP A 282 8.488 -62.399 -43.801 1.00104.75 O ANISOU 2272 O ASP A 282 15746 5563 18491 -96 1117 764 O ATOM 2273 CB ASP A 282 9.702 -65.197 -43.797 1.00115.50 C ANISOU 2273 CB ASP A 282 17901 6116 19867 247 584 738 C ATOM 2274 CG ASP A 282 11.019 -64.954 -44.505 1.00128.36 C ANISOU 2274 CG ASP A 282 19394 7891 21485 681 448 501 C ATOM 2275 OD1 ASP A 282 11.905 -64.298 -43.916 1.00129.70 O ANISOU 2275 OD1 ASP A 282 19527 8218 21536 900 434 566 O ATOM 2276 OD2 ASP A 282 11.171 -65.430 -45.651 1.00135.28 O ANISOU 2276 OD2 ASP A 282 20195 8745 22460 800 354 252 O ATOM 2277 N PHE A 283 10.483 -62.045 -42.813 1.00103.66 N ANISOU 2277 N PHE A 283 15792 5443 18151 405 931 863 N ATOM 2278 CA PHE A 283 10.610 -60.661 -43.262 1.00 93.68 C ANISOU 2278 CA PHE A 283 14129 4590 16874 457 1076 747 C ATOM 2279 C PHE A 283 11.971 -60.407 -43.899 1.00 91.33 C ANISOU 2279 C PHE A 283 13709 4437 16555 852 903 542 C ATOM 2280 O PHE A 283 12.995 -60.446 -43.221 1.00100.40 O ANISOU 2280 O PHE A 283 15024 5550 17574 1103 781 635 O ATOM 2281 CB PHE A 283 10.398 -59.695 -42.096 1.00110.68 C ANISOU 2281 CB PHE A 283 16266 6917 18871 344 1260 992 C ATOM 2282 CG PHE A 283 9.038 -59.786 -41.478 1.00133.80 C ANISOU 2282 CG PHE A 283 19253 9792 21792 -44 1454 1180 C ATOM 2283 CD1 PHE A 283 7.931 -59.281 -42.137 1.00144.20 C ANISOU 2283 CD1 PHE A 283 20289 11298 23202 -292 1640 1075 C ATOM 2284 CD2 PHE A 283 8.864 -60.376 -40.237 1.00143.15 C ANISOU 2284 CD2 PHE A 283 20765 10760 22864 -162 1441 1456 C ATOM 2285 CE1 PHE A 283 6.674 -59.364 -41.574 1.00151.49 C ANISOU 2285 CE1 PHE A 283 21247 12212 24102 -638 1817 1238 C ATOM 2286 CE2 PHE A 283 7.610 -60.460 -39.667 1.00149.50 C ANISOU 2286 CE2 PHE A 283 21604 11554 23644 -525 1616 1625 C ATOM 2287 CZ PHE A 283 6.512 -59.956 -40.338 1.00152.85 C ANISOU 2287 CZ PHE A 283 21738 12183 24156 -759 1808 1514 C ATOM 2288 N GLY A 284 11.974 -60.137 -45.201 1.00 88.11 N ANISOU 2288 N GLY A 284 12999 4220 16260 901 888 263 N ATOM 2289 CA GLY A 284 13.207 -59.903 -45.931 1.00 94.69 C ANISOU 2289 CA GLY A 284 13672 5243 17064 1254 723 43 C ATOM 2290 C GLY A 284 13.964 -58.669 -45.475 1.00 88.30 C ANISOU 2290 C GLY A 284 12697 4744 16108 1403 763 102 C ATOM 2291 O GLY A 284 13.388 -57.775 -44.851 1.00 87.10 O ANISOU 2291 O GLY A 284 12472 4722 15901 1207 955 263 O ATOM 2292 N PRO A 285 15.269 -58.612 -45.785 1.00 84.57 N ANISOU 2292 N PRO A 285 12167 4412 15554 1756 580 -30 N ATOM 2293 CA PRO A 285 16.115 -57.465 -45.435 1.00 83.05 C ANISOU 2293 CA PRO A 285 11812 4539 15206 1922 583 11 C ATOM 2294 C PRO A 285 15.710 -56.200 -46.184 1.00 82.17 C ANISOU 2294 C PRO A 285 11304 4792 15125 1778 713 -125 C ATOM 2295 O PRO A 285 15.789 -55.103 -45.631 1.00 94.26 O ANISOU 2295 O PRO A 285 12745 6527 16541 1744 815 0 O ATOM 2296 CB PRO A 285 17.516 -57.922 -45.850 1.00 86.72 C ANISOU 2296 CB PRO A 285 12280 5078 15593 2322 336 -152 C ATOM 2297 CG PRO A 285 17.280 -58.937 -46.913 1.00 83.56 C ANISOU 2297 CG PRO A 285 11876 4536 15335 2336 244 -380 C ATOM 2298 CD PRO A 285 16.017 -59.645 -46.522 1.00 85.62 C ANISOU 2298 CD PRO A 285 12378 4434 15721 2023 359 -233 C ATOM 2299 N ILE A 286 15.278 -56.361 -47.432 1.00 86.52 N ANISOU 2299 N ILE A 286 11636 5422 15814 1694 701 -377 N ATOM 2300 CA ILE A 286 14.831 -55.237 -48.246 1.00 91.56 C ANISOU 2300 CA ILE A 286 11907 6397 16485 1540 804 -529 C ATOM 2301 C ILE A 286 13.476 -54.731 -47.753 1.00 91.28 C ANISOU 2301 C ILE A 286 11873 6305 16503 1190 1054 -368 C ATOM 2302 O ILE A 286 13.173 -53.539 -47.842 1.00 97.77 O ANISOU 2302 O ILE A 286 12476 7388 17284 1079 1169 -380 O ATOM 2303 CB ILE A 286 14.732 -55.622 -49.739 1.00 98.39 C ANISOU 2303 CB ILE A 286 12546 7369 17468 1538 712 -840 C ATOM 2304 CG1 ILE A 286 16.015 -56.317 -50.202 1.00104.49 C ANISOU 2304 CG1 ILE A 286 13347 8181 18173 1888 469 -999 C ATOM 2305 CG2 ILE A 286 14.458 -54.398 -50.597 1.00101.36 C ANISOU 2305 CG2 ILE A 286 12539 8134 17841 1409 779 -1006 C ATOM 2306 CD1 ILE A 286 17.243 -55.435 -50.151 1.00 97.28 C ANISOU 2306 CD1 ILE A 286 12262 7630 17069 2133 362 -1042 C ATOM 2307 N PHE A 287 12.670 -55.645 -47.220 1.00 79.93 N ANISOU 2307 N PHE A 287 10689 4541 15138 1018 1126 -219 N ATOM 2308 CA PHE A 287 11.353 -55.297 -46.696 1.00 81.13 C ANISOU 2308 CA PHE A 287 10852 4657 15318 684 1361 -60 C ATOM 2309 C PHE A 287 11.443 -54.408 -45.456 1.00 73.11 C ANISOU 2309 C PHE A 287 9921 3726 14132 669 1485 193 C ATOM 2310 O PHE A 287 10.636 -53.501 -45.276 1.00 77.78 O ANISOU 2310 O PHE A 287 10374 4480 14699 466 1671 245 O ATOM 2311 CB PHE A 287 10.565 -56.569 -46.375 1.00 86.99 C ANISOU 2311 CB PHE A 287 11861 5044 16146 511 1380 50 C ATOM 2312 CG PHE A 287 9.251 -56.315 -45.692 1.00 98.63 C ANISOU 2312 CG PHE A 287 13366 6497 17611 175 1613 237 C ATOM 2313 CD1 PHE A 287 8.156 -55.867 -46.412 1.00105.05 C ANISOU 2313 CD1 PHE A 287 13919 7480 18517 -67 1757 117 C ATOM 2314 CD2 PHE A 287 9.107 -56.537 -44.331 1.00 98.48 C ANISOU 2314 CD2 PHE A 287 13629 6317 17473 104 1680 529 C ATOM 2315 CE1 PHE A 287 6.946 -55.635 -45.786 1.00108.09 C ANISOU 2315 CE1 PHE A 287 14313 7884 18871 -358 1966 275 C ATOM 2316 CE2 PHE A 287 7.901 -56.309 -43.701 1.00 96.84 C ANISOU 2316 CE2 PHE A 287 13431 6132 17233 -201 1892 691 C ATOM 2317 CZ PHE A 287 6.819 -55.858 -44.429 1.00104.96 C ANISOU 2317 CZ PHE A 287 14189 7341 18351 -426 2037 560 C ATOM 2318 N MET A 288 12.430 -54.672 -44.606 1.00 85.91 N ANISOU 2318 N MET A 288 11774 5246 15621 893 1373 345 N ATOM 2319 CA MET A 288 12.613 -53.918 -43.368 1.00 81.54 C ANISOU 2319 CA MET A 288 11337 4769 14876 900 1470 604 C ATOM 2320 C MET A 288 13.125 -52.507 -43.640 1.00 82.97 C ANISOU 2320 C MET A 288 11259 5307 14959 1004 1484 530 C ATOM 2321 O MET A 288 12.985 -51.611 -42.805 1.00 89.69 O ANISOU 2321 O MET A 288 12135 6319 15626 940 1593 707 O ATOM 2322 CB MET A 288 13.582 -54.650 -42.433 1.00 89.09 C ANISOU 2322 CB MET A 288 12615 5528 15707 1122 1319 778 C ATOM 2323 CG MET A 288 13.098 -56.016 -41.972 1.00 79.88 C ANISOU 2323 CG MET A 288 11760 3985 14605 1009 1286 891 C ATOM 2324 SD MET A 288 11.581 -55.909 -40.997 1.00 94.46 S ANISOU 2324 SD MET A 288 13714 5760 16418 600 1549 1144 S ATOM 2325 CE MET A 288 12.166 -54.988 -39.583 1.00106.80 C ANISOU 2325 CE MET A 288 15393 7485 17702 693 1608 1415 C ATOM 2326 N THR A 289 13.715 -52.317 -44.815 1.00 75.11 N ANISOU 2326 N THR A 289 10015 4503 14020 1148 1343 257 N ATOM 2327 CA THR A 289 14.305 -51.036 -45.177 1.00 81.66 C ANISOU 2327 CA THR A 289 10590 5797 14639 1225 1276 160 C ATOM 2328 C THR A 289 13.243 -50.041 -45.653 1.00 70.94 C ANISOU 2328 C THR A 289 8992 4665 13297 961 1428 77 C ATOM 2329 O THR A 289 13.456 -48.828 -45.597 1.00 66.62 O ANISOU 2329 O THR A 289 8304 4466 12542 955 1417 80 O ATOM 2330 CB THR A 289 15.386 -51.206 -46.269 1.00 77.40 C ANISOU 2330 CB THR A 289 9861 5436 14112 1470 1048 -105 C ATOM 2331 OG1 THR A 289 16.283 -52.260 -45.897 1.00 71.40 O ANISOU 2331 OG1 THR A 289 9326 4434 13368 1730 901 -56 O ATOM 2332 CG2 THR A 289 16.187 -49.918 -46.448 1.00 81.77 C ANISOU 2332 CG2 THR A 289 10201 6472 14396 1558 951 -154 C ATOM 2333 N ILE A 290 12.100 -50.551 -46.108 1.00 63.81 N ANISOU 2333 N ILE A 290 8053 3560 12634 742 1559 5 N ATOM 2334 CA ILE A 290 11.029 -49.684 -46.611 1.00 71.55 C ANISOU 2334 CA ILE A 290 8798 4740 13647 496 1701 -91 C ATOM 2335 C ILE A 290 10.534 -48.655 -45.579 1.00 74.69 C ANISOU 2335 C ILE A 290 9245 5299 13834 378 1848 117 C ATOM 2336 O ILE A 290 10.448 -47.466 -45.899 1.00 70.65 O ANISOU 2336 O ILE A 290 8533 5120 13190 338 1842 34 O ATOM 2337 CB ILE A 290 9.816 -50.504 -47.118 1.00 73.96 C ANISOU 2337 CB ILE A 290 9085 4776 14239 264 1833 -168 C ATOM 2338 CG1 ILE A 290 10.249 -51.504 -48.189 1.00 76.93 C ANISOU 2338 CG1 ILE A 290 9409 5076 14746 372 1657 -385 C ATOM 2339 CG2 ILE A 290 8.729 -49.577 -47.651 1.00 66.82 C ANISOU 2339 CG2 ILE A 290 7925 4099 13366 28 1973 -278 C ATOM 2340 CD1 ILE A 290 9.099 -52.272 -48.803 1.00 65.69 C ANISOU 2340 CD1 ILE A 290 7944 3532 13482 139 1731 -467 C ATOM 2341 N PRO A 291 10.207 -49.092 -44.342 1.00 74.77 N ANISOU 2341 N PRO A 291 9528 5078 13803 321 1971 385 N ATOM 2342 CA PRO A 291 9.777 -48.048 -43.402 1.00 63.75 C ANISOU 2342 CA PRO A 291 8159 3874 12187 230 2102 559 C ATOM 2343 C PRO A 291 10.907 -47.086 -43.040 1.00 70.88 C ANISOU 2343 C PRO A 291 9062 5063 12806 437 1958 609 C ATOM 2344 O PRO A 291 10.646 -45.928 -42.714 1.00 62.44 O ANISOU 2344 O PRO A 291 7921 4251 11551 381 2008 651 O ATOM 2345 CB PRO A 291 9.319 -48.842 -42.175 1.00 71.90 C ANISOU 2345 CB PRO A 291 9493 4596 13231 138 2244 834 C ATOM 2346 CG PRO A 291 10.037 -50.142 -42.268 1.00 69.80 C ANISOU 2346 CG PRO A 291 9414 4007 13101 282 2110 843 C ATOM 2347 CD PRO A 291 10.144 -50.435 -43.731 1.00 73.45 C ANISOU 2347 CD PRO A 291 9650 4493 13764 317 1997 540 C ATOM 2348 N ALA A 292 12.146 -47.565 -43.105 1.00 74.73 N ANISOU 2348 N ALA A 292 9630 5509 13254 675 1770 600 N ATOM 2349 CA ALA A 292 13.310 -46.724 -42.841 1.00 65.58 C ANISOU 2349 CA ALA A 292 8459 4635 11824 870 1613 639 C ATOM 2350 C ALA A 292 13.474 -45.679 -43.939 1.00 60.46 C ANISOU 2350 C ALA A 292 7501 4360 11111 855 1511 405 C ATOM 2351 O ALA A 292 13.824 -44.530 -43.668 1.00 52.72 O ANISOU 2351 O ALA A 292 6476 3671 9886 877 1456 452 O ATOM 2352 CB ALA A 292 14.566 -47.573 -42.721 1.00 72.90 C ANISOU 2352 CB ALA A 292 9525 5438 12737 1132 1435 664 C ATOM 2353 N PHE A 293 13.217 -46.093 -45.176 1.00 59.72 N ANISOU 2353 N PHE A 293 7208 4249 11236 808 1475 157 N ATOM 2354 CA PHE A 293 13.253 -45.201 -46.332 1.00 51.99 C ANISOU 2354 CA PHE A 293 5926 3600 10228 759 1382 -81 C ATOM 2355 C PHE A 293 12.361 -43.974 -46.138 1.00 68.91 C ANISOU 2355 C PHE A 293 7986 5937 12258 571 1493 -51 C ATOM 2356 O PHE A 293 12.800 -42.841 -46.332 1.00 64.20 O ANISOU 2356 O PHE A 293 7279 5662 11450 592 1379 -92 O ATOM 2357 CB PHE A 293 12.838 -45.977 -47.588 1.00 73.32 C ANISOU 2357 CB PHE A 293 8454 6185 13220 697 1375 -333 C ATOM 2358 CG PHE A 293 12.510 -45.107 -48.769 1.00 70.66 C ANISOU 2358 CG PHE A 293 7810 6140 12897 577 1329 -570 C ATOM 2359 CD1 PHE A 293 13.512 -44.648 -49.609 1.00 77.36 C ANISOU 2359 CD1 PHE A 293 8469 7294 13629 694 1122 -739 C ATOM 2360 CD2 PHE A 293 11.195 -44.771 -49.056 1.00 72.31 C ANISOU 2360 CD2 PHE A 293 7915 6327 13232 341 1488 -628 C ATOM 2361 CE1 PHE A 293 13.208 -43.858 -50.702 1.00 76.85 C ANISOU 2361 CE1 PHE A 293 8133 7493 13572 567 1070 -951 C ATOM 2362 CE2 PHE A 293 10.886 -43.977 -50.146 1.00 71.76 C ANISOU 2362 CE2 PHE A 293 7575 6514 13178 231 1434 -847 C ATOM 2363 CZ PHE A 293 11.894 -43.520 -50.970 1.00 73.71 C ANISOU 2363 CZ PHE A 293 7651 7049 13308 339 1222 -1005 C ATOM 2364 N PHE A 294 11.111 -44.205 -45.748 1.00 71.43 N ANISOU 2364 N PHE A 294 8365 6067 12709 388 1705 21 N ATOM 2365 CA PHE A 294 10.158 -43.115 -45.562 1.00 65.14 C ANISOU 2365 CA PHE A 294 7486 5443 11820 223 1818 32 C ATOM 2366 C PHE A 294 10.524 -42.239 -44.370 1.00 60.45 C ANISOU 2366 C PHE A 294 7060 4986 10924 296 1813 252 C ATOM 2367 O PHE A 294 10.453 -41.013 -44.450 1.00 51.70 O ANISOU 2367 O PHE A 294 5860 4148 9634 268 1760 213 O ATOM 2368 CB PHE A 294 8.738 -43.665 -45.396 1.00 73.13 C ANISOU 2368 CB PHE A 294 8512 6235 13039 14 2053 57 C ATOM 2369 CG PHE A 294 8.138 -44.178 -46.674 1.00 68.91 C ANISOU 2369 CG PHE A 294 7767 5634 12780 -106 2067 -186 C ATOM 2370 CD1 PHE A 294 7.488 -43.316 -47.544 1.00 62.80 C ANISOU 2370 CD1 PHE A 294 6745 5086 12033 -230 2068 -380 C ATOM 2371 CD2 PHE A 294 8.233 -45.518 -47.011 1.00 69.28 C ANISOU 2371 CD2 PHE A 294 7878 5387 13059 -92 2065 -223 C ATOM 2372 CE1 PHE A 294 6.938 -43.783 -48.724 1.00 60.90 C ANISOU 2372 CE1 PHE A 294 6308 4786 12043 -344 2079 -602 C ATOM 2373 CE2 PHE A 294 7.685 -45.992 -48.189 1.00 67.09 C ANISOU 2373 CE2 PHE A 294 7414 5045 13033 -203 2072 -448 C ATOM 2374 CZ PHE A 294 7.037 -45.124 -49.046 1.00 66.41 C ANISOU 2374 CZ PHE A 294 7067 5194 12970 -333 2086 -636 C ATOM 2375 N ALA A 295 10.927 -42.865 -43.269 1.00 55.22 N ANISOU 2375 N ALA A 295 6654 4128 10200 389 1856 482 N ATOM 2376 CA ALA A 295 11.251 -42.118 -42.056 1.00 65.56 C ANISOU 2376 CA ALA A 295 8143 5541 11225 456 1863 706 C ATOM 2377 C ALA A 295 12.504 -41.243 -42.203 1.00 66.08 C ANISOU 2377 C ALA A 295 8174 5895 11040 618 1632 686 C ATOM 2378 O ALA A 295 12.521 -40.101 -41.743 1.00 56.69 O ANISOU 2378 O ALA A 295 7009 4919 9613 611 1603 755 O ATOM 2379 CB ALA A 295 11.416 -43.076 -40.885 1.00 52.93 C ANISOU 2379 CB ALA A 295 6830 3651 9629 512 1954 956 C ATOM 2380 N LYS A 296 13.544 -41.776 -42.842 1.00 59.95 N ANISOU 2380 N LYS A 296 7339 5133 10305 760 1462 589 N ATOM 2381 CA ALYS A 296 14.819 -41.070 -42.980 0.59 56.27 C ANISOU 2381 CA ALYS A 296 6834 4955 9593 909 1237 578 C ATOM 2382 CA BLYS A 296 14.813 -41.063 -42.969 0.41 55.55 C ANISOU 2382 CA BLYS A 296 6743 4862 9499 908 1238 580 C ATOM 2383 C LYS A 296 14.738 -39.902 -43.959 1.00 47.70 C ANISOU 2383 C LYS A 296 5506 4201 8418 815 1121 384 C ATOM 2384 O LYS A 296 15.360 -38.858 -43.753 1.00 44.84 O ANISOU 2384 O LYS A 296 5151 4104 7782 850 982 436 O ATOM 2385 CB ALYS A 296 15.919 -42.036 -43.429 0.59 48.06 C ANISOU 2385 CB ALYS A 296 5777 3857 8626 1095 1090 508 C ATOM 2386 CB BLYS A 296 15.924 -42.031 -43.385 0.41 48.08 C ANISOU 2386 CB BLYS A 296 5788 3857 8624 1097 1092 517 C ATOM 2387 CG ALYS A 296 16.383 -43.019 -42.366 0.59 50.63 C ANISOU 2387 CG ALYS A 296 6377 3904 8956 1242 1126 723 C ATOM 2388 CG BLYS A 296 16.363 -42.979 -42.281 0.41 50.62 C ANISOU 2388 CG BLYS A 296 6390 3902 8942 1239 1133 739 C ATOM 2389 CD ALYS A 296 17.454 -43.949 -42.926 0.59 59.42 C ANISOU 2389 CD ALYS A 296 7454 4978 10145 1450 960 613 C ATOM 2390 CD BLYS A 296 17.429 -43.946 -42.772 0.41 59.23 C ANISOU 2390 CD BLYS A 296 7460 4936 10109 1449 973 644 C ATOM 2391 CE ALYS A 296 17.807 -45.067 -41.954 0.59 59.60 C ANISOU 2391 CE ALYS A 296 7763 4669 10215 1594 988 806 C ATOM 2392 CE BLYS A 296 17.871 -44.891 -41.665 0.41 59.25 C ANISOU 2392 CE BLYS A 296 7761 4645 10106 1598 993 866 C ATOM 2393 NZ ALYS A 296 18.815 -46.004 -42.535 0.59 56.30 N ANISOU 2393 NZ ALYS A 296 7309 4205 9877 1822 814 675 N ATOM 2394 NZ BLYS A 296 18.483 -44.157 -40.524 0.41 55.26 N ANISOU 2394 NZ BLYS A 296 7422 4277 9298 1673 959 1103 N ATOM 2395 N THR A 297 13.973 -40.086 -45.031 1.00 45.87 N ANISOU 2395 N THR A 297 5067 3948 8411 685 1167 166 N ATOM 2396 CA THR A 297 13.823 -39.064 -46.064 1.00 51.60 C ANISOU 2396 CA THR A 297 5558 4965 9081 579 1054 -34 C ATOM 2397 C THR A 297 13.098 -37.821 -45.524 1.00 53.51 C ANISOU 2397 C THR A 297 5851 5333 9148 469 1104 43 C ATOM 2398 O THR A 297 13.090 -36.770 -46.163 1.00 44.58 O ANISOU 2398 O THR A 297 4583 4458 7897 396 974 -78 O ATOM 2399 CB THR A 297 13.077 -39.643 -47.288 1.00 48.72 C ANISOU 2399 CB THR A 297 4975 4514 9021 462 1111 -279 C ATOM 2400 OG1 THR A 297 13.715 -40.862 -47.684 1.00 57.31 O ANISOU 2400 OG1 THR A 297 6051 5452 10272 585 1067 -344 O ATOM 2401 CG2 THR A 297 13.093 -38.681 -48.466 1.00 52.64 C ANISOU 2401 CG2 THR A 297 5221 5318 9461 364 961 -498 C ATOM 2402 N SER A 298 12.520 -37.936 -44.329 1.00 51.40 N ANISOU 2402 N SER A 298 5789 4890 8849 464 1279 245 N ATOM 2403 CA SER A 298 11.880 -36.795 -43.679 1.00 47.08 C ANISOU 2403 CA SER A 298 5314 4460 8113 396 1326 327 C ATOM 2404 C SER A 298 12.903 -35.726 -43.318 1.00 50.12 C ANISOU 2404 C SER A 298 5785 5099 8161 489 1116 417 C ATOM 2405 O SER A 298 12.546 -34.572 -43.102 1.00 48.37 O ANISOU 2405 O SER A 298 5588 5035 7756 438 1072 426 O ATOM 2406 CB SER A 298 11.113 -37.232 -42.427 1.00 41.90 C ANISOU 2406 CB SER A 298 4859 3579 7483 379 1562 532 C ATOM 2407 OG SER A 298 11.991 -37.531 -41.353 1.00 46.70 O ANISOU 2407 OG SER A 298 5701 4112 7932 521 1539 764 O ATOM 2408 N ALA A 299 14.177 -36.106 -43.265 1.00 43.23 N ANISOU 2408 N ALA A 299 4958 4269 7198 626 974 479 N ATOM 2409 CA ALA A 299 15.244 -35.137 -43.027 1.00 37.37 C ANISOU 2409 CA ALA A 299 4278 3792 6130 698 753 558 C ATOM 2410 C ALA A 299 15.372 -34.155 -44.194 1.00 42.97 C ANISOU 2410 C ALA A 299 4776 4795 6755 596 555 355 C ATOM 2411 O ALA A 299 16.013 -33.115 -44.070 1.00 40.09 O ANISOU 2411 O ALA A 299 4458 4670 6104 598 364 406 O ATOM 2412 CB ALA A 299 16.568 -35.846 -42.788 1.00 38.42 C ANISOU 2412 CB ALA A 299 4476 3925 6198 869 648 652 C ATOM 2413 N VAL A 300 14.777 -34.500 -45.332 1.00 45.66 N ANISOU 2413 N VAL A 300 4895 5113 7341 495 589 129 N ATOM 2414 CA VAL A 300 14.756 -33.608 -46.484 1.00 35.80 C ANISOU 2414 CA VAL A 300 3443 4122 6037 373 414 -73 C ATOM 2415 C VAL A 300 13.379 -32.929 -46.661 1.00 49.33 C ANISOU 2415 C VAL A 300 5114 5804 7825 228 512 -165 C ATOM 2416 O VAL A 300 13.316 -31.714 -46.810 1.00 44.92 O ANISOU 2416 O VAL A 300 4559 5442 7064 159 363 -195 O ATOM 2417 CB VAL A 300 15.139 -34.352 -47.784 1.00 38.32 C ANISOU 2417 CB VAL A 300 3516 4492 6552 361 346 -290 C ATOM 2418 CG1 VAL A 300 14.987 -33.439 -48.992 1.00 39.82 C ANISOU 2418 CG1 VAL A 300 3494 4939 6697 207 179 -500 C ATOM 2419 CG2 VAL A 300 16.578 -34.881 -47.701 1.00 36.96 C ANISOU 2419 CG2 VAL A 300 3359 4419 6267 522 210 -229 C ATOM 2420 N TYR A 301 12.276 -33.679 -46.625 1.00 43.82 N ANISOU 2420 N TYR A 301 4383 4866 7400 179 749 -207 N ATOM 2421 CA TYR A 301 10.995 -33.052 -46.966 1.00 45.35 C ANISOU 2421 CA TYR A 301 4489 5071 7672 43 826 -331 C ATOM 2422 C TYR A 301 10.334 -32.300 -45.804 1.00 48.00 C ANISOU 2422 C TYR A 301 5016 5385 7836 60 918 -179 C ATOM 2423 O TYR A 301 9.515 -31.416 -46.043 1.00 47.36 O ANISOU 2423 O TYR A 301 4884 5396 7716 -20 899 -279 O ATOM 2424 CB TYR A 301 10.011 -34.075 -47.567 1.00 45.98 C ANISOU 2424 CB TYR A 301 4415 4947 8110 -45 1029 -469 C ATOM 2425 CG TYR A 301 9.637 -35.275 -46.721 1.00 48.15 C ANISOU 2425 CG TYR A 301 4817 4927 8552 -3 1271 -322 C ATOM 2426 CD1 TYR A 301 8.773 -35.155 -45.639 1.00 45.18 C ANISOU 2426 CD1 TYR A 301 4586 4443 8136 -20 1461 -175 C ATOM 2427 CD2 TYR A 301 10.100 -36.542 -47.048 1.00 52.44 C ANISOU 2427 CD2 TYR A 301 5330 5300 9294 44 1303 -343 C ATOM 2428 CE1 TYR A 301 8.414 -36.263 -44.881 1.00 50.11 C ANISOU 2428 CE1 TYR A 301 5330 4806 8905 -13 1676 -33 C ATOM 2429 CE2 TYR A 301 9.746 -37.653 -46.301 1.00 58.33 C ANISOU 2429 CE2 TYR A 301 6213 5758 10191 64 1502 -206 C ATOM 2430 CZ TYR A 301 8.905 -37.508 -45.219 1.00 56.81 C ANISOU 2430 CZ TYR A 301 6168 5469 9949 23 1689 -44 C ATOM 2431 OH TYR A 301 8.561 -38.615 -44.474 1.00 54.20 O ANISOU 2431 OH TYR A 301 5980 4859 9753 16 1878 105 O ATOM 2432 N ASN A 302 10.688 -32.617 -44.561 1.00 36.38 N ANISOU 2432 N ASN A 302 3765 3803 6253 170 1005 54 N ATOM 2433 CA ASN A 302 10.233 -31.787 -43.445 1.00 46.51 C ANISOU 2433 CA ASN A 302 5239 5111 7322 203 1056 200 C ATOM 2434 C ASN A 302 10.785 -30.343 -43.496 1.00 49.37 C ANISOU 2434 C ASN A 302 5666 5726 7366 218 790 195 C ATOM 2435 O ASN A 302 10.015 -29.398 -43.345 1.00 57.31 O ANISOU 2435 O ASN A 302 6700 6804 8270 184 777 149 O ATOM 2436 CB ASN A 302 10.577 -32.432 -42.098 1.00 35.76 C ANISOU 2436 CB ASN A 302 4108 3586 5894 314 1192 459 C ATOM 2437 CG ASN A 302 9.548 -33.458 -41.664 1.00 50.52 C ANISOU 2437 CG ASN A 302 5982 5211 8003 263 1486 501 C ATOM 2438 OD1 ASN A 302 8.449 -33.527 -42.215 1.00 51.82 O ANISOU 2438 OD1 ASN A 302 5989 5348 8352 147 1605 350 O ATOM 2439 ND2 ASN A 302 9.896 -34.252 -40.663 1.00 44.46 N ANISOU 2439 ND2 ASN A 302 5398 4270 7225 338 1599 713 N ATOM 2440 N PRO A 303 12.108 -30.158 -43.698 1.00 52.51 N ANISOU 2440 N PRO A 303 6092 6266 7594 267 567 242 N ATOM 2441 CA PRO A 303 12.531 -28.753 -43.814 1.00 39.74 C ANISOU 2441 CA PRO A 303 4538 4886 5673 243 303 233 C ATOM 2442 C PRO A 303 11.992 -28.051 -45.064 1.00 43.86 C ANISOU 2442 C PRO A 303 4867 5545 6252 103 170 -11 C ATOM 2443 O PRO A 303 11.803 -26.837 -45.048 1.00 49.72 O ANISOU 2443 O PRO A 303 5687 6419 6785 67 5 -35 O ATOM 2444 CB PRO A 303 14.069 -28.841 -43.859 1.00 43.87 C ANISOU 2444 CB PRO A 303 5097 5551 6021 302 103 328 C ATOM 2445 CG PRO A 303 14.384 -30.258 -44.198 1.00 47.29 C ANISOU 2445 CG PRO A 303 5407 5848 6712 348 231 298 C ATOM 2446 CD PRO A 303 13.262 -31.080 -43.645 1.00 45.98 C ANISOU 2446 CD PRO A 303 5278 5402 6791 358 534 331 C ATOM 2447 N VAL A 304 11.740 -28.797 -46.132 1.00 39.36 N ANISOU 2447 N VAL A 304 4060 4937 5958 27 229 -191 N ATOM 2448 CA VAL A 304 11.084 -28.218 -47.292 1.00 37.96 C ANISOU 2448 CA VAL A 304 3695 4863 5865 -111 134 -425 C ATOM 2449 C VAL A 304 9.697 -27.670 -46.911 1.00 50.22 C ANISOU 2449 C VAL A 304 5291 6338 7452 -133 263 -468 C ATOM 2450 O VAL A 304 9.341 -26.547 -47.266 1.00 49.33 O ANISOU 2450 O VAL A 304 5183 6354 7205 -190 96 -567 O ATOM 2451 CB VAL A 304 10.952 -29.245 -48.427 1.00 35.64 C ANISOU 2451 CB VAL A 304 3143 4511 5888 -182 214 -606 C ATOM 2452 CG1 VAL A 304 9.961 -28.767 -49.479 1.00 36.02 C ANISOU 2452 CG1 VAL A 304 3005 4610 6072 -325 186 -841 C ATOM 2453 CG2 VAL A 304 12.307 -29.514 -49.049 1.00 35.81 C ANISOU 2453 CG2 VAL A 304 3080 4691 5835 -169 25 -623 C ATOM 2454 N ILE A 305 8.936 -28.459 -46.159 1.00 47.96 N ANISOU 2454 N ILE A 305 5044 5849 7329 -84 551 -391 N ATOM 2455 CA ILE A 305 7.576 -28.092 -45.769 1.00 40.04 C ANISOU 2455 CA ILE A 305 4050 4791 6372 -98 709 -437 C ATOM 2456 C ILE A 305 7.541 -27.040 -44.658 1.00 42.52 C ANISOU 2456 C ILE A 305 4608 5173 6376 1 641 -299 C ATOM 2457 O ILE A 305 6.757 -26.095 -44.709 1.00 46.27 O ANISOU 2457 O ILE A 305 5091 5726 6765 -8 583 -399 O ATOM 2458 CB ILE A 305 6.787 -29.339 -45.315 1.00 43.74 C ANISOU 2458 CB ILE A 305 4475 5040 7104 -103 1042 -388 C ATOM 2459 CG1 ILE A 305 6.609 -30.300 -46.489 1.00 47.72 C ANISOU 2459 CG1 ILE A 305 4738 5465 7928 -210 1104 -558 C ATOM 2460 CG2 ILE A 305 5.421 -28.958 -44.738 1.00 37.20 C ANISOU 2460 CG2 ILE A 305 3661 4193 6281 -108 1219 -411 C ATOM 2461 CD1 ILE A 305 6.046 -31.631 -46.089 1.00 43.41 C ANISOU 2461 CD1 ILE A 305 4175 4687 7633 -230 1393 -490 C ATOM 2462 N TYR A 306 8.402 -27.199 -43.660 1.00 45.33 N ANISOU 2462 N TYR A 306 5167 5499 6559 104 637 -74 N ATOM 2463 CA TYR A 306 8.337 -26.357 -42.471 1.00 45.23 C ANISOU 2463 CA TYR A 306 5400 5522 6265 209 610 77 C ATOM 2464 C TYR A 306 9.260 -25.133 -42.502 1.00 47.81 C ANISOU 2464 C TYR A 306 5876 6028 6262 230 274 114 C ATOM 2465 O TYR A 306 9.085 -24.212 -41.706 1.00 40.47 O ANISOU 2465 O TYR A 306 5144 5144 5088 306 203 190 O ATOM 2466 CB TYR A 306 8.650 -27.197 -41.235 1.00 36.48 C ANISOU 2466 CB TYR A 306 4452 4267 5141 304 810 317 C ATOM 2467 CG TYR A 306 7.543 -28.157 -40.880 1.00 51.49 C ANISOU 2467 CG TYR A 306 6276 5999 7291 277 1141 318 C ATOM 2468 CD1 TYR A 306 6.458 -27.734 -40.129 1.00 45.22 C ANISOU 2468 CD1 TYR A 306 5539 5210 6432 307 1291 329 C ATOM 2469 CD2 TYR A 306 7.569 -29.478 -41.311 1.00 42.05 C ANISOU 2469 CD2 TYR A 306 4948 4648 6382 217 1294 302 C ATOM 2470 CE1 TYR A 306 5.440 -28.594 -39.802 1.00 52.07 C ANISOU 2470 CE1 TYR A 306 6325 5956 7505 257 1591 336 C ATOM 2471 CE2 TYR A 306 6.542 -30.355 -40.987 1.00 46.11 C ANISOU 2471 CE2 TYR A 306 5403 5007 7111 164 1584 314 C ATOM 2472 CZ TYR A 306 5.480 -29.901 -40.231 1.00 51.03 C ANISOU 2472 CZ TYR A 306 6074 5661 7654 174 1735 336 C ATOM 2473 OH TYR A 306 4.444 -30.739 -39.891 1.00 45.72 O ANISOU 2473 OH TYR A 306 5334 4869 7170 99 2022 355 O ATOM 2474 N ILE A 307 10.237 -25.125 -43.404 1.00 48.36 N ANISOU 2474 N ILE A 307 6322 3774 8280 550 417 725 N ATOM 2475 CA ILE A 307 11.170 -24.002 -43.496 1.00 45.41 C ANISOU 2475 CA ILE A 307 5790 3453 8010 689 344 769 C ATOM 2476 C ILE A 307 11.064 -23.317 -44.851 1.00 48.93 C ANISOU 2476 C ILE A 307 6068 3987 8535 759 380 733 C ATOM 2477 O ILE A 307 10.811 -22.114 -44.924 1.00 47.43 O ANISOU 2477 O ILE A 307 5750 3869 8401 791 404 735 O ATOM 2478 CB ILE A 307 12.635 -24.447 -43.260 1.00 47.51 C ANISOU 2478 CB ILE A 307 6060 3636 8357 824 228 917 C ATOM 2479 CG1 ILE A 307 12.769 -25.219 -41.944 1.00 48.23 C ANISOU 2479 CG1 ILE A 307 6326 3658 8343 735 110 1070 C ATOM 2480 CG2 ILE A 307 13.572 -23.248 -43.280 1.00 46.02 C ANISOU 2480 CG2 ILE A 307 5694 3569 8221 861 149 945 C ATOM 2481 CD1 ILE A 307 12.482 -24.388 -40.716 1.00 60.20 C ANISOU 2481 CD1 ILE A 307 7931 5292 9650 472 48 1045 C ATOM 2482 N MET A 308 11.240 -24.078 -45.927 1.00 44.96 N ANISOU 2482 N MET A 308 5621 3442 8018 745 424 708 N ATOM 2483 CA MET A 308 11.220 -23.499 -47.268 1.00 44.85 C ANISOU 2483 CA MET A 308 5520 3529 7991 708 432 696 C ATOM 2484 C MET A 308 9.858 -22.954 -47.672 1.00 45.36 C ANISOU 2484 C MET A 308 5431 3808 7994 580 362 768 C ATOM 2485 O MET A 308 9.774 -21.958 -48.397 1.00 55.78 O ANISOU 2485 O MET A 308 6611 5233 9352 616 297 869 O ATOM 2486 CB MET A 308 11.684 -24.523 -48.302 1.00 46.16 C ANISOU 2486 CB MET A 308 5876 3570 8091 601 581 609 C ATOM 2487 CG MET A 308 13.196 -24.693 -48.357 1.00 79.47 C ANISOU 2487 CG MET A 308 10092 7596 12505 812 703 599 C ATOM 2488 SD MET A 308 13.717 -25.905 -49.586 1.00 93.72 S ANISOU 2488 SD MET A 308 12177 9125 14305 691 1087 440 S ATOM 2489 CE MET A 308 12.799 -25.355 -51.025 1.00 94.91 C ANISOU 2489 CE MET A 308 12441 9527 14093 249 1039 353 C ATOM 2490 N MET A 309 8.790 -23.599 -47.213 1.00 46.24 N ANISOU 2490 N MET A 309 5539 3996 8033 432 372 759 N ATOM 2491 CA MET A 309 7.438 -23.154 -47.539 1.00 47.82 C ANISOU 2491 CA MET A 309 5462 4463 8246 322 295 896 C ATOM 2492 C MET A 309 6.954 -22.130 -46.508 1.00 47.89 C ANISOU 2492 C MET A 309 5258 4435 8502 538 393 952 C ATOM 2493 O MET A 309 5.815 -21.660 -46.550 1.00 54.92 O ANISOU 2493 O MET A 309 5826 5496 9545 554 408 1104 O ATOM 2494 CB MET A 309 6.487 -24.352 -47.632 1.00 49.64 C ANISOU 2494 CB MET A 309 5757 4836 8266 -26 300 847 C ATOM 2495 CG MET A 309 6.782 -25.254 -48.835 1.00 50.88 C ANISOU 2495 CG MET A 309 6186 5012 8133 -358 299 771 C ATOM 2496 SD MET A 309 5.664 -26.657 -49.040 1.00 63.22 S ANISOU 2496 SD MET A 309 7929 6745 9347 -928 356 675 S ATOM 2497 CE MET A 309 4.117 -25.827 -49.416 1.00 70.49 C ANISOU 2497 CE MET A 309 8234 8250 10300 -1105 59 996 C ATOM 2498 N ASN A 310 7.844 -21.799 -45.581 1.00 46.70 N ANISOU 2498 N ASN A 310 5286 4061 8397 670 491 840 N ATOM 2499 CA ASN A 310 7.628 -20.724 -44.626 1.00 48.83 C ANISOU 2499 CA ASN A 310 5503 4213 8836 786 687 822 C ATOM 2500 C ASN A 310 8.167 -19.431 -45.240 1.00 51.94 C ANISOU 2500 C ASN A 310 5828 4537 9369 972 706 917 C ATOM 2501 O ASN A 310 9.356 -19.333 -45.543 1.00 48.54 O ANISOU 2501 O ASN A 310 5545 4057 8841 975 615 872 O ATOM 2502 CB ASN A 310 8.311 -21.062 -43.294 1.00 46.60 C ANISOU 2502 CB ASN A 310 5521 3777 8407 667 751 669 C ATOM 2503 CG ASN A 310 8.125 -19.994 -42.236 1.00 51.77 C ANISOU 2503 CG ASN A 310 6259 4279 9131 629 1037 577 C ATOM 2504 OD1 ASN A 310 8.477 -18.832 -42.432 1.00 56.95 O ANISOU 2504 OD1 ASN A 310 6902 4831 9903 736 1160 590 O ATOM 2505 ND2 ASN A 310 7.593 -20.395 -41.090 1.00 50.50 N ANISOU 2505 ND2 ASN A 310 6262 4062 8865 416 1202 458 N ATOM 2506 N LYS A 311 7.288 -18.452 -45.433 1.00 53.59 N ANISOU 2506 N LYS A 311 5795 4728 9840 1136 853 1075 N ATOM 2507 CA LYS A 311 7.632 -17.251 -46.194 1.00 61.47 C ANISOU 2507 CA LYS A 311 6745 5630 10981 1322 872 1237 C ATOM 2508 C LYS A 311 8.800 -16.465 -45.592 1.00 59.12 C ANISOU 2508 C LYS A 311 6769 5081 10615 1296 1052 1049 C ATOM 2509 O LYS A 311 9.654 -15.958 -46.321 1.00 56.92 O ANISOU 2509 O LYS A 311 6580 4777 10271 1309 965 1083 O ATOM 2510 CB LYS A 311 6.406 -16.346 -46.326 1.00 59.98 C ANISOU 2510 CB LYS A 311 6212 5392 11187 1575 1061 1515 C ATOM 2511 CG LYS A 311 6.630 -15.136 -47.223 1.00 81.79 C ANISOU 2511 CG LYS A 311 8932 8025 14121 1795 1061 1784 C ATOM 2512 CD LYS A 311 5.332 -14.627 -47.845 1.00 92.78 C ANISOU 2512 CD LYS A 311 9822 9524 15905 2064 1026 2267 C ATOM 2513 CE LYS A 311 4.597 -13.645 -46.942 1.00105.68 C ANISOU 2513 CE LYS A 311 11375 10866 17915 2298 1553 2262 C ATOM 2514 NZ LYS A 311 3.961 -14.295 -45.762 1.00112.54 N ANISOU 2514 NZ LYS A 311 12146 11682 18931 2252 1853 2033 N ATOM 2515 N GLN A 312 8.844 -16.381 -44.267 1.00 60.75 N ANISOU 2515 N GLN A 312 7172 5133 10778 1168 1303 844 N ATOM 2516 CA GLN A 312 9.910 -15.654 -43.582 1.00 55.11 C ANISOU 2516 CA GLN A 312 6786 4249 9905 989 1457 667 C ATOM 2517 C GLN A 312 11.278 -16.299 -43.816 1.00 57.50 C ANISOU 2517 C GLN A 312 7158 4743 9946 840 1112 628 C ATOM 2518 O GLN A 312 12.254 -15.615 -44.133 1.00 62.90 O ANISOU 2518 O GLN A 312 7933 5405 10562 777 1104 604 O ATOM 2519 CB GLN A 312 9.614 -15.572 -42.082 1.00 84.44 C ANISOU 2519 CB GLN A 312 10753 7810 13522 736 1778 457 C ATOM 2520 CG GLN A 312 10.308 -14.419 -41.376 1.00104.16 C ANISOU 2520 CG GLN A 312 13632 10068 15876 471 2109 277 C ATOM 2521 CD GLN A 312 10.001 -14.365 -39.889 1.00117.79 C ANISOU 2521 CD GLN A 312 15706 11644 17406 78 2466 38 C ATOM 2522 OE1 GLN A 312 9.520 -15.338 -39.303 1.00122.31 O ANISOU 2522 OE1 GLN A 312 16251 12341 17881 -30 2364 13 O ATOM 2523 NE2 GLN A 312 10.280 -13.223 -39.272 1.00117.96 N ANISOU 2523 NE2 GLN A 312 16129 11370 17321 -212 2932 -160 N ATOM 2524 N PHE A 313 11.345 -17.619 -43.665 1.00 47.70 N ANISOU 2524 N PHE A 313 5860 3665 8598 792 871 638 N ATOM 2525 CA PHE A 313 12.592 -18.343 -43.869 1.00 44.89 C ANISOU 2525 CA PHE A 313 5496 3440 8121 741 611 661 C ATOM 2526 C PHE A 313 12.991 -18.340 -45.340 1.00 52.47 C ANISOU 2526 C PHE A 313 6323 4449 9165 889 528 721 C ATOM 2527 O PHE A 313 14.160 -18.139 -45.674 1.00 47.73 O ANISOU 2527 O PHE A 313 5702 3893 8541 858 474 709 O ATOM 2528 CB PHE A 313 12.476 -19.782 -43.350 1.00 44.73 C ANISOU 2528 CB PHE A 313 5494 3475 8026 703 459 697 C ATOM 2529 CG PHE A 313 12.813 -19.927 -41.893 1.00 46.16 C ANISOU 2529 CG PHE A 313 5853 3670 8015 454 412 694 C ATOM 2530 CD1 PHE A 313 14.133 -20.036 -41.482 1.00 47.28 C ANISOU 2530 CD1 PHE A 313 5971 3935 8057 339 193 811 C ATOM 2531 CD2 PHE A 313 11.815 -19.943 -40.933 1.00 47.17 C ANISOU 2531 CD2 PHE A 313 6156 3721 8046 280 583 603 C ATOM 2532 CE1 PHE A 313 14.452 -20.163 -40.138 1.00 49.54 C ANISOU 2532 CE1 PHE A 313 6429 4306 8088 9 66 884 C ATOM 2533 CE2 PHE A 313 12.126 -20.072 -39.586 1.00 51.76 C ANISOU 2533 CE2 PHE A 313 6985 4326 8354 -68 536 602 C ATOM 2534 CZ PHE A 313 13.447 -20.182 -39.190 1.00 50.41 C ANISOU 2534 CZ PHE A 313 6815 4317 8022 -228 236 766 C ATOM 2535 N ARG A 314 12.011 -18.555 -46.211 1.00 47.92 N ANISOU 2535 N ARG A 314 5652 3899 8657 983 521 794 N ATOM 2536 CA ARG A 314 12.260 -18.621 -47.645 1.00 54.60 C ANISOU 2536 CA ARG A 314 6454 4809 9483 997 444 852 C ATOM 2537 C ARG A 314 12.882 -17.321 -48.153 1.00 53.28 C ANISOU 2537 C ARG A 314 6330 4577 9339 1015 513 875 C ATOM 2538 O ARG A 314 13.870 -17.344 -48.884 1.00 54.46 O ANISOU 2538 O ARG A 314 6517 4750 9427 951 500 822 O ATOM 2539 CB ARG A 314 10.959 -18.921 -48.394 1.00 49.78 C ANISOU 2539 CB ARG A 314 5731 4319 8865 971 367 991 C ATOM 2540 CG ARG A 314 11.120 -19.277 -49.867 1.00 49.16 C ANISOU 2540 CG ARG A 314 5700 4350 8629 813 266 1039 C ATOM 2541 CD ARG A 314 9.851 -18.910 -50.638 1.00 59.38 C ANISOU 2541 CD ARG A 314 6818 5840 9901 743 108 1315 C ATOM 2542 NE ARG A 314 8.645 -19.397 -49.970 1.00 67.74 N ANISOU 2542 NE ARG A 314 7681 7017 11039 745 83 1382 N ATOM 2543 CZ ARG A 314 7.478 -18.762 -49.973 1.00 87.72 C ANISOU 2543 CZ ARG A 314 9891 9678 13761 854 23 1667 C ATOM 2544 NH1 ARG A 314 6.436 -19.285 -49.339 1.00105.49 N ANISOU 2544 NH1 ARG A 314 11931 12053 16096 822 50 1690 N ATOM 2545 NH2 ARG A 314 7.351 -17.605 -50.604 1.00 91.06 N ANISOU 2545 NH2 ARG A 314 10182 10089 14326 1009 -38 1959 N ATOM 2546 N ASN A 315 12.311 -16.188 -47.754 1.00 51.12 N ANISOU 2546 N ASN A 315 6076 4174 9174 1094 659 943 N ATOM 2547 CA ASN A 315 12.837 -14.892 -48.174 1.00 47.55 C ANISOU 2547 CA ASN A 315 5749 3581 8738 1096 788 971 C ATOM 2548 C ASN A 315 14.263 -14.660 -47.703 1.00 46.03 C ANISOU 2548 C ASN A 315 5687 3396 8407 903 836 776 C ATOM 2549 O ASN A 315 15.103 -14.173 -48.455 1.00 53.82 O ANISOU 2549 O ASN A 315 6735 4388 9325 816 850 752 O ATOM 2550 CB ASN A 315 11.938 -13.769 -47.673 1.00 49.74 C ANISOU 2550 CB ASN A 315 6068 3608 9222 1247 1061 1073 C ATOM 2551 CG ASN A 315 10.622 -13.719 -48.411 1.00 63.94 C ANISOU 2551 CG ASN A 315 7613 5446 11234 1475 979 1399 C ATOM 2552 OD1 ASN A 315 10.461 -14.362 -49.449 1.00 75.97 O ANISOU 2552 OD1 ASN A 315 9006 7213 12646 1417 682 1545 O ATOM 2553 ND2 ASN A 315 9.673 -12.953 -47.887 1.00 60.66 N ANISOU 2553 ND2 ASN A 315 7116 4801 11130 1697 1269 1535 N ATOM 2554 N CYS A 316 14.535 -15.028 -46.457 1.00 47.83 N ANISOU 2554 N CYS A 316 5940 3665 8567 780 840 665 N ATOM 2555 CA CYS A 316 15.866 -14.875 -45.890 1.00 46.50 C ANISOU 2555 CA CYS A 316 5809 3613 8246 528 799 563 C ATOM 2556 C CYS A 316 16.884 -15.797 -46.565 1.00 59.93 C ANISOU 2556 C CYS A 316 7276 5511 9982 568 605 594 C ATOM 2557 O CYS A 316 18.036 -15.410 -46.764 1.00 55.64 O ANISOU 2557 O CYS A 316 6666 5079 9396 417 606 554 O ATOM 2558 CB CYS A 316 15.822 -15.123 -44.380 1.00 47.44 C ANISOU 2558 CB CYS A 316 6020 3779 8227 312 782 514 C ATOM 2559 SG CYS A 316 14.982 -13.791 -43.471 1.00 55.66 S ANISOU 2559 SG CYS A 316 7442 4502 9205 126 1223 371 S ATOM 2560 N AMET A 317 16.454 -17.008 -46.911 0.63 53.18 N ANISOU 2560 N AMET A 317 6307 4676 9222 749 505 652 N ATOM 2561 N BMET A 317 16.457 -17.004 -46.926 0.37 54.24 N ANISOU 2561 N BMET A 317 6442 4811 9357 749 506 651 N ATOM 2562 CA AMET A 317 17.314 -17.954 -47.619 0.63 56.91 C ANISOU 2562 CA AMET A 317 6611 5215 9798 825 473 659 C ATOM 2563 CA BMET A 317 17.339 -17.946 -47.612 0.37 56.45 C ANISOU 2563 CA BMET A 317 6549 5159 9739 823 473 659 C ATOM 2564 C AMET A 317 17.668 -17.456 -49.015 0.63 55.37 C ANISOU 2564 C AMET A 317 6462 4986 9590 783 608 588 C ATOM 2565 C BMET A 317 17.665 -17.484 -49.031 0.37 55.55 C ANISOU 2565 C BMET A 317 6483 5008 9615 785 608 587 C ATOM 2566 O AMET A 317 18.816 -17.557 -49.449 0.63 57.50 O ANISOU 2566 O AMET A 317 6597 5314 9936 741 691 535 O ATOM 2567 O BMET A 317 18.796 -17.631 -49.495 0.37 57.08 O ANISOU 2567 O BMET A 317 6544 5256 9889 749 695 534 O ATOM 2568 CB AMET A 317 16.642 -19.324 -47.717 0.63 57.18 C ANISOU 2568 CB AMET A 317 6648 5183 9896 962 447 695 C ATOM 2569 CB BMET A 317 16.716 -19.343 -47.647 0.37 57.43 C ANISOU 2569 CB BMET A 317 6668 5220 9932 963 441 699 C ATOM 2570 CG AMET A 317 16.737 -20.152 -46.455 0.63 60.13 C ANISOU 2570 CG AMET A 317 6964 5582 10303 1001 315 799 C ATOM 2571 CG BMET A 317 16.713 -20.049 -46.302 0.37 60.96 C ANISOU 2571 CG BMET A 317 7075 5698 10391 983 300 803 C ATOM 2572 SD AMET A 317 16.022 -21.791 -46.671 0.63 68.49 S ANISOU 2572 SD AMET A 317 8119 6482 11421 1124 370 817 S ATOM 2573 SD BMET A 317 16.126 -21.750 -46.405 0.37 67.11 S ANISOU 2573 SD BMET A 317 7925 6326 11248 1123 336 843 S ATOM 2574 CE AMET A 317 16.607 -22.606 -45.188 0.63 60.22 C ANISOU 2574 CE AMET A 317 6989 5450 10443 1186 185 1038 C ATOM 2575 CE BMET A 317 14.456 -21.499 -46.997 0.37 64.90 C ANISOU 2575 CE BMET A 317 7815 6034 10809 1021 390 744 C ATOM 2576 N VAL A 318 16.669 -16.930 -49.716 1.00 52.80 N ANISOU 2576 N VAL A 318 6302 4580 9179 777 629 623 N ATOM 2577 CA VAL A 318 16.863 -16.400 -51.062 1.00 58.14 C ANISOU 2577 CA VAL A 318 7100 5229 9762 664 710 612 C ATOM 2578 C VAL A 318 17.813 -15.211 -51.031 1.00 58.98 C ANISOU 2578 C VAL A 318 7263 5319 9829 534 819 546 C ATOM 2579 O VAL A 318 18.694 -15.082 -51.881 1.00 64.34 O ANISOU 2579 O VAL A 318 7964 6021 10460 389 939 450 O ATOM 2580 CB VAL A 318 15.524 -15.973 -51.702 1.00 57.47 C ANISOU 2580 CB VAL A 318 7128 5113 9596 677 616 801 C ATOM 2581 CG1 VAL A 318 15.763 -15.184 -52.977 1.00 61.72 C ANISOU 2581 CG1 VAL A 318 7846 5623 9981 508 650 866 C ATOM 2582 CG2 VAL A 318 14.670 -17.190 -51.989 1.00 54.52 C ANISOU 2582 CG2 VAL A 318 6713 4828 9175 655 512 842 C ATOM 2583 N THR A 319 17.638 -14.349 -50.038 1.00 59.51 N ANISOU 2583 N THR A 319 7395 5327 9888 524 838 564 N ATOM 2584 CA THR A 319 18.515 -13.198 -49.874 1.00 58.23 C ANISOU 2584 CA THR A 319 7359 5139 9629 302 981 472 C ATOM 2585 C THR A 319 19.954 -13.645 -49.645 1.00 59.01 C ANISOU 2585 C THR A 319 7200 5483 9739 136 953 364 C ATOM 2586 O THR A 319 20.885 -13.103 -50.238 1.00 60.46 O ANISOU 2586 O THR A 319 7390 5722 9861 -66 1076 271 O ATOM 2587 CB THR A 319 18.065 -12.313 -48.705 1.00 49.17 C ANISOU 2587 CB THR A 319 6404 3842 8436 230 1099 459 C ATOM 2588 OG1 THR A 319 16.772 -11.770 -48.993 1.00 56.33 O ANISOU 2588 OG1 THR A 319 7471 4481 9450 454 1204 610 O ATOM 2589 CG2 THR A 319 19.046 -11.184 -48.486 1.00 59.26 C ANISOU 2589 CG2 THR A 319 7880 5098 9537 -123 1285 320 C ATOM 2590 N THR A 320 20.125 -14.654 -48.799 1.00 59.34 N ANISOU 2590 N THR A 320 6982 5678 9887 227 791 420 N ATOM 2591 CA THR A 320 21.451 -15.157 -48.465 1.00 50.96 C ANISOU 2591 CA THR A 320 5548 4881 8933 143 714 449 C ATOM 2592 C THR A 320 22.108 -15.847 -49.656 1.00 58.91 C ANISOU 2592 C THR A 320 6357 5878 10150 274 878 398 C ATOM 2593 O THR A 320 23.294 -15.652 -49.920 1.00 64.66 O ANISOU 2593 O THR A 320 6828 6773 10966 137 977 358 O ATOM 2594 CB THR A 320 21.391 -16.138 -47.279 1.00 60.81 C ANISOU 2594 CB THR A 320 6580 6258 10265 249 471 624 C ATOM 2595 OG1 THR A 320 20.948 -15.442 -46.108 1.00 56.06 O ANISOU 2595 OG1 THR A 320 6208 5683 9409 -7 384 623 O ATOM 2596 CG2 THR A 320 22.767 -16.745 -47.010 1.00 54.63 C ANISOU 2596 CG2 THR A 320 5294 5767 9694 247 349 790 C ATOM 2597 N LEU A 321 21.334 -16.647 -50.380 1.00 58.78 N ANISOU 2597 N LEU A 321 6472 5668 10194 475 954 380 N ATOM 2598 CA LEU A 321 21.882 -17.420 -51.489 1.00 58.78 C ANISOU 2598 CA LEU A 321 6392 5583 10360 530 1221 279 C ATOM 2599 C LEU A 321 22.114 -16.568 -52.728 1.00 62.81 C ANISOU 2599 C LEU A 321 7149 6036 10681 268 1436 114 C ATOM 2600 O LEU A 321 22.891 -16.938 -53.605 1.00 68.69 O ANISOU 2600 O LEU A 321 7826 6736 11535 194 1745 -28 O ATOM 2601 CB LEU A 321 20.958 -18.589 -51.835 1.00 59.06 C ANISOU 2601 CB LEU A 321 6591 5426 10424 688 1270 282 C ATOM 2602 CG LEU A 321 20.951 -19.742 -50.835 1.00 57.09 C ANISOU 2602 CG LEU A 321 6120 5155 10416 957 1170 434 C ATOM 2603 CD1 LEU A 321 19.949 -20.792 -51.257 1.00 61.25 C ANISOU 2603 CD1 LEU A 321 6916 5467 10887 1007 1270 387 C ATOM 2604 CD2 LEU A 321 22.343 -20.339 -50.722 1.00 57.57 C ANISOU 2604 CD2 LEU A 321 5749 5251 10876 1128 1344 510 C ATOM 2605 N CYS A 322 21.440 -15.427 -52.803 1.00 66.58 N ANISOU 2605 N CYS A 322 7933 6472 10891 126 1323 147 N ATOM 2606 CA CYS A 322 21.559 -14.577 -53.980 1.00 72.49 C ANISOU 2606 CA CYS A 322 8988 7137 11418 -136 1483 64 C ATOM 2607 C CYS A 322 22.316 -13.294 -53.667 1.00 79.74 C ANISOU 2607 C CYS A 322 9943 8115 12238 -359 1542 11 C ATOM 2608 O CYS A 322 22.162 -12.289 -54.362 1.00 80.59 O ANISOU 2608 O CYS A 322 10406 8093 12123 -559 1623 11 O ATOM 2609 CB CYS A 322 20.175 -14.265 -54.547 1.00 67.30 C ANISOU 2609 CB CYS A 322 8676 6346 10549 -131 1330 230 C ATOM 2610 SG CYS A 322 19.212 -15.760 -54.882 1.00 72.70 S ANISOU 2610 SG CYS A 322 9352 7025 11244 -27 1248 276 S ATOM 2611 N CYS A 323 23.131 -13.347 -52.616 1.00 77.64 N ANISOU 2611 N CYS A 323 9332 8058 12110 -373 1487 -2 N ATOM 2612 CA CYS A 323 24.058 -12.271 -52.272 1.00 79.68 C ANISOU 2612 CA CYS A 323 9579 8458 12237 -716 1564 -89 C ATOM 2613 C CYS A 323 23.387 -10.909 -52.079 1.00 82.16 C ANISOU 2613 C CYS A 323 10398 8544 12274 -882 1597 -77 C ATOM 2614 O CYS A 323 23.779 -9.927 -52.708 1.00 99.10 O ANISOU 2614 O CYS A 323 12833 10588 14231 -1167 1799 -173 O ATOM 2615 CB CYS A 323 25.139 -12.153 -53.351 1.00 87.65 C ANISOU 2615 CB CYS A 323 10504 9538 13262 -952 1854 -264 C ATOM 2616 SG CYS A 323 25.820 -13.733 -53.921 1.00 98.84 S ANISOU 2616 SG CYS A 323 11432 11027 15096 -703 2053 -311 S ATOM 2617 N GLY A 324 22.382 -10.848 -51.209 1.00 68.64 N ANISOU 2617 N GLY A 324 8813 6703 10565 -703 1467 40 N ATOM 2618 CA GLY A 324 21.720 -9.591 -50.902 1.00 67.52 C ANISOU 2618 CA GLY A 324 9132 6256 10267 -794 1617 62 C ATOM 2619 C GLY A 324 20.513 -9.280 -51.771 1.00 76.69 C ANISOU 2619 C GLY A 324 10578 7084 11476 -513 1646 255 C ATOM 2620 O GLY A 324 19.682 -8.450 -51.410 1.00 90.40 O ANISOU 2620 O GLY A 324 12603 8506 13240 -406 1781 367 O ATOM 2621 N LYS A 325 20.417 -9.942 -52.919 1.00 86.24 N ANISOU 2621 N LYS A 325 11704 8362 12701 -423 1543 321 N ATOM 2622 CA LYS A 325 19.282 -9.770 -53.825 1.00104.89 C ANISOU 2622 CA LYS A 325 14266 10534 15052 -242 1452 592 C ATOM 2623 C LYS A 325 17.983 -10.286 -53.203 1.00109.71 C ANISOU 2623 C LYS A 325 14709 11118 15858 111 1278 791 C ATOM 2624 O LYS A 325 17.940 -11.386 -52.652 1.00110.41 O ANISOU 2624 O LYS A 325 14516 11397 16036 205 1154 704 O ATOM 2625 CB LYS A 325 19.554 -10.485 -55.154 1.00111.71 C ANISOU 2625 CB LYS A 325 15127 11539 15780 -398 1392 570 C ATOM 2626 CG LYS A 325 18.337 -10.671 -56.055 1.00108.44 C ANISOU 2626 CG LYS A 325 14829 11090 15283 -314 1168 897 C ATOM 2627 CD LYS A 325 17.798 -9.347 -56.569 1.00110.40 C ANISOU 2627 CD LYS A 325 15407 11086 15453 -306 1158 1232 C ATOM 2628 CE LYS A 325 16.711 -9.569 -57.610 1.00109.95 C ANISOU 2628 CE LYS A 325 15396 11113 15268 -317 840 1652 C ATOM 2629 NZ LYS A 325 15.614 -10.439 -57.102 1.00107.30 N ANISOU 2629 NZ LYS A 325 14703 10944 15121 -47 602 1809 N ATOM 2630 N ASN A 326 16.927 -9.482 -53.298 1.00109.62 N ANISOU 2630 N ASN A 326 14854 10852 15946 316 1297 1088 N ATOM 2631 CA ASN A 326 15.627 -9.844 -52.743 1.00109.15 C ANISOU 2631 CA ASN A 326 14584 10767 16122 649 1188 1301 C ATOM 2632 C ASN A 326 15.009 -11.055 -53.431 1.00116.65 C ANISOU 2632 C ASN A 326 15288 12006 17026 677 862 1435 C ATOM 2633 O ASN A 326 13.883 -11.447 -53.121 1.00120.69 O ANISOU 2633 O ASN A 326 15581 12571 17706 895 734 1633 O ATOM 2634 CB ASN A 326 14.666 -8.661 -52.835 1.00117.47 C ANISOU 2634 CB ASN A 326 15783 11460 17390 913 1334 1664 C ATOM 2635 CG ASN A 326 15.213 -7.417 -52.168 1.00125.86 C ANISOU 2635 CG ASN A 326 17217 12132 18471 828 1776 1500 C ATOM 2636 OD1 ASN A 326 15.982 -7.501 -51.209 1.00127.16 O ANISOU 2636 OD1 ASN A 326 17447 12347 18519 590 1940 1128 O ATOM 2637 ND2 ASN A 326 14.821 -6.254 -52.673 1.00128.10 N ANISOU 2637 ND2 ASN A 326 17769 12023 18879 977 1971 1808 N TER 2638 ASN A 326 ATOM 2639 N VAL C 340 -7.150 -12.602 -36.829 1.00 99.57 N ANISOU 2639 N VAL C 340 11672 11064 15096 4119 2595 1152 N ATOM 2640 CA VAL C 340 -6.509 -13.913 -36.787 1.00 88.02 C ANISOU 2640 CA VAL C 340 10048 9823 13572 3751 2688 1284 C ATOM 2641 C VAL C 340 -5.279 -13.923 -37.687 1.00 63.80 C ANISOU 2641 C VAL C 340 7104 6557 10579 3464 2375 1392 C ATOM 2642 O VAL C 340 -4.404 -14.778 -37.560 1.00 67.34 O ANISOU 2642 O VAL C 340 7588 7113 10886 3087 2310 1378 O ATOM 2643 CB VAL C 340 -7.487 -15.038 -37.220 1.00 82.57 C ANISOU 2643 CB VAL C 340 8768 9550 13055 3550 2744 1440 C ATOM 2644 CG1 VAL C 340 -7.634 -15.078 -38.733 1.00 79.09 C ANISOU 2644 CG1 VAL C 340 8051 9161 12839 3380 2386 1533 C ATOM 2645 CG2 VAL C 340 -7.025 -16.378 -36.702 1.00 64.86 C ANISOU 2645 CG2 VAL C 340 6376 7500 10769 3247 2864 1533 C ATOM 2646 N LEU C 341 -5.207 -12.947 -38.585 1.00 68.52 N ANISOU 2646 N LEU C 341 7792 6933 11311 3516 2083 1484 N ATOM 2647 CA LEU C 341 -4.158 -12.902 -39.592 1.00 66.31 C ANISOU 2647 CA LEU C 341 7563 6641 10990 3119 1715 1640 C ATOM 2648 C LEU C 341 -2.770 -12.694 -38.989 1.00 63.92 C ANISOU 2648 C LEU C 341 7755 6068 10462 2842 1580 1524 C ATOM 2649 O LEU C 341 -1.806 -13.321 -39.417 1.00 58.58 O ANISOU 2649 O LEU C 341 7028 5566 9663 2440 1421 1570 O ATOM 2650 CB LEU C 341 -4.453 -11.801 -40.611 1.00 64.62 C ANISOU 2650 CB LEU C 341 7328 6255 10969 3259 1447 1868 C ATOM 2651 CG LEU C 341 -5.734 -11.974 -41.430 1.00 66.75 C ANISOU 2651 CG LEU C 341 7101 6803 11458 3497 1479 1983 C ATOM 2652 CD1 LEU C 341 -5.932 -10.805 -42.380 1.00 69.13 C ANISOU 2652 CD1 LEU C 341 7450 6906 11911 3615 1168 2235 C ATOM 2653 CD2 LEU C 341 -5.693 -13.281 -42.196 1.00 70.81 C ANISOU 2653 CD2 LEU C 341 7145 7835 11923 3227 1427 2014 C ATOM 2654 N AGLU C 342 -2.687 -11.812 -37.998 0.47 66.20 N ANISOU 2654 N AGLU C 342 8496 5941 10715 3098 1611 1327 N ATOM 2655 N BGLU C 342 -2.665 -11.822 -37.993 0.53 66.02 N ANISOU 2655 N BGLU C 342 8478 5918 10689 3090 1610 1326 N ATOM 2656 CA AGLU C 342 -1.424 -11.489 -37.345 0.47 66.34 C ANISOU 2656 CA AGLU C 342 9007 5619 10582 2898 1432 1170 C ATOM 2657 CA BGLU C 342 -1.364 -11.523 -37.403 0.53 66.20 C ANISOU 2657 CA BGLU C 342 8979 5610 10562 2865 1418 1184 C ATOM 2658 C AGLU C 342 -0.832 -12.713 -36.658 0.47 62.57 C ANISOU 2658 C AGLU C 342 8543 5400 9831 2639 1600 1021 C ATOM 2659 C BGLU C 342 -0.810 -12.708 -36.620 0.53 62.62 C ANISOU 2659 C BGLU C 342 8564 5398 9830 2640 1601 1013 C ATOM 2660 O AGLU C 342 0.378 -12.936 -36.696 0.47 58.69 O ANISOU 2660 O AGLU C 342 8235 4827 9237 2264 1393 995 O ATOM 2661 O BGLU C 342 0.403 -12.899 -36.553 0.53 59.05 O ANISOU 2661 O BGLU C 342 8331 4840 9267 2286 1402 964 O ATOM 2662 CB AGLU C 342 -1.620 -10.359 -36.333 0.47 71.41 C ANISOU 2662 CB AGLU C 342 10093 5779 11260 3342 1395 884 C ATOM 2663 CB BGLU C 342 -1.444 -10.288 -36.504 0.53 71.14 C ANISOU 2663 CB BGLU C 342 10070 5705 11255 3268 1324 929 C ATOM 2664 CG AGLU C 342 -2.150 -9.066 -36.938 0.47 83.52 C ANISOU 2664 CG AGLU C 342 11647 6935 13153 3611 1130 1006 C ATOM 2665 CG BGLU C 342 -1.089 -8.993 -37.222 0.53 78.31 C ANISOU 2665 CG BGLU C 342 11140 6114 12501 3237 880 1125 C ATOM 2666 CD AGLU C 342 -2.505 -8.032 -35.885 0.47103.18 C ANISOU 2666 CD AGLU C 342 14484 9034 15685 4095 1024 586 C ATOM 2667 CD BGLU C 342 0.296 -9.036 -37.848 0.53 79.22 C ANISOU 2667 CD BGLU C 342 11328 6145 12627 2676 574 1376 C ATOM 2668 OE1AGLU C 342 -2.502 -8.378 -34.685 0.47110.92 O ANISOU 2668 OE1AGLU C 342 15636 10164 16345 4282 1246 217 O ATOM 2669 OE1BGLU C 342 1.220 -9.602 -37.225 0.53 79.90 O ANISOU 2669 OE1BGLU C 342 11616 6246 12496 2436 593 1184 O ATOM 2670 OE2AGLU C 342 -2.787 -6.872 -36.256 0.47107.94 O ANISOU 2670 OE2AGLU C 342 15135 9252 16624 4247 652 604 O ATOM 2671 OE2BGLU C 342 0.462 -8.509 -38.967 0.53 77.58 O ANISOU 2671 OE2BGLU C 342 10951 5896 12632 2483 318 1791 O ATOM 2672 N ASP C 343 -1.696 -13.504 -36.033 1.00 66.70 N ANISOU 2672 N ASP C 343 8838 6235 10268 2833 1963 960 N ATOM 2673 CA ASP C 343 -1.270 -14.710 -35.338 1.00 61.22 C ANISOU 2673 CA ASP C 343 8115 5779 9368 2600 2112 894 C ATOM 2674 C ASP C 343 -0.774 -15.752 -36.335 1.00 56.65 C ANISOU 2674 C ASP C 343 7156 5470 8898 2142 1915 1036 C ATOM 2675 O ASP C 343 0.233 -16.419 -36.100 1.00 57.35 O ANISOU 2675 O ASP C 343 7361 5572 8856 1809 1782 942 O ATOM 2676 CB ASP C 343 -2.406 -15.271 -34.488 1.00 70.11 C ANISOU 2676 CB ASP C 343 9002 7206 10431 2910 2550 921 C ATOM 2677 CG ASP C 343 -2.666 -14.436 -33.252 1.00 82.63 C ANISOU 2677 CG ASP C 343 10997 8650 11748 3393 2756 677 C ATOM 2678 OD1 ASP C 343 -1.696 -13.839 -32.739 1.00 73.16 O ANISOU 2678 OD1 ASP C 343 10323 7109 10364 3387 2539 428 O ATOM 2679 OD2 ASP C 343 -3.830 -14.372 -32.798 1.00 91.77 O ANISOU 2679 OD2 ASP C 343 11926 10057 12884 3804 3110 707 O ATOM 2680 N LEU C 344 -1.475 -15.868 -37.459 1.00 61.78 N ANISOU 2680 N LEU C 344 7346 6344 9785 2169 1856 1214 N ATOM 2681 CA LEU C 344 -1.075 -16.772 -38.531 1.00 52.23 C ANISOU 2681 CA LEU C 344 5733 5448 8665 1840 1606 1274 C ATOM 2682 C LEU C 344 0.279 -16.377 -39.110 1.00 54.29 C ANISOU 2682 C LEU C 344 6225 5635 8768 1531 1286 1261 C ATOM 2683 O LEU C 344 1.131 -17.229 -39.355 1.00 50.06 O ANISOU 2683 O LEU C 344 5569 5297 8153 1213 1104 1159 O ATOM 2684 CB LEU C 344 -2.137 -16.795 -39.636 1.00 55.26 C ANISOU 2684 CB LEU C 344 5609 6086 9302 2023 1566 1432 C ATOM 2685 CG LEU C 344 -3.482 -17.432 -39.273 1.00 57.17 C ANISOU 2685 CG LEU C 344 5441 6476 9805 2261 1835 1482 C ATOM 2686 CD1 LEU C 344 -4.466 -17.292 -40.419 1.00 53.83 C ANISOU 2686 CD1 LEU C 344 4589 6248 9614 2433 1709 1584 C ATOM 2687 CD2 LEU C 344 -3.296 -18.901 -38.898 1.00 58.28 C ANISOU 2687 CD2 LEU C 344 5292 6797 10054 2001 1815 1433 C ATOM 2688 N LYS C 345 0.473 -15.081 -39.333 1.00 56.42 N ANISOU 2688 N LYS C 345 6788 5616 9033 1625 1193 1380 N ATOM 2689 CA LYS C 345 1.743 -14.587 -39.848 1.00 54.84 C ANISOU 2689 CA LYS C 345 6772 5327 8736 1316 905 1470 C ATOM 2690 C LYS C 345 2.861 -14.862 -38.849 1.00 53.15 C ANISOU 2690 C LYS C 345 6945 4879 8372 1085 864 1228 C ATOM 2691 O LYS C 345 3.970 -15.235 -39.226 1.00 54.07 O ANISOU 2691 O LYS C 345 7022 5136 8385 736 662 1207 O ATOM 2692 CB LYS C 345 1.654 -13.093 -40.160 1.00 52.81 C ANISOU 2692 CB LYS C 345 6745 4698 8624 1461 774 1714 C ATOM 2693 CG LYS C 345 0.697 -12.770 -41.299 1.00 84.80 C ANISOU 2693 CG LYS C 345 10417 8997 12808 1653 743 2002 C ATOM 2694 CD LYS C 345 0.499 -11.269 -41.470 1.00 96.88 C ANISOU 2694 CD LYS C 345 12189 10060 14560 1825 579 2258 C ATOM 2695 CE LYS C 345 -0.547 -10.971 -42.536 1.00100.70 C ANISOU 2695 CE LYS C 345 12308 10779 15175 2055 543 2541 C ATOM 2696 NZ LYS C 345 -0.764 -9.509 -42.724 1.00109.49 N ANISOU 2696 NZ LYS C 345 13640 11388 16572 2220 320 2823 N ATOM 2697 N SER C 346 2.550 -14.693 -37.571 1.00 52.50 N ANISOU 2697 N SER C 346 7213 4487 8248 1316 1055 1028 N ATOM 2698 CA SER C 346 3.511 -14.930 -36.503 1.00 57.24 C ANISOU 2698 CA SER C 346 8218 4855 8676 1172 1013 772 C ATOM 2699 C SER C 346 3.966 -16.393 -36.456 1.00 64.73 C ANISOU 2699 C SER C 346 8925 6146 9522 870 1002 667 C ATOM 2700 O SER C 346 5.062 -16.697 -35.981 1.00 67.17 O ANISOU 2700 O SER C 346 9480 6330 9713 621 847 491 O ATOM 2701 CB SER C 346 2.901 -14.519 -35.160 1.00 65.56 C ANISOU 2701 CB SER C 346 9633 5653 9622 1586 1248 571 C ATOM 2702 OG SER C 346 3.892 -14.451 -34.153 1.00 97.04 O ANISOU 2702 OG SER C 346 14091 9349 13429 1513 1131 305 O ATOM 2703 N CYS C 347 3.116 -17.288 -36.956 1.00 63.72 N ANISOU 2703 N CYS C 347 8301 6408 9503 905 1113 760 N ATOM 2704 CA CYS C 347 3.381 -18.727 -36.949 1.00 59.22 C ANISOU 2704 CA CYS C 347 7426 6114 8962 658 1028 658 C ATOM 2705 C CYS C 347 3.970 -19.228 -38.267 1.00 54.74 C ANISOU 2705 C CYS C 347 6453 5894 8450 403 708 632 C ATOM 2706 O CYS C 347 4.267 -20.413 -38.408 1.00 58.15 O ANISOU 2706 O CYS C 347 6590 6546 8958 216 529 476 O ATOM 2707 CB CYS C 347 2.093 -19.501 -36.650 1.00 56.30 C ANISOU 2707 CB CYS C 347 6688 5930 8772 850 1272 770 C ATOM 2708 SG CYS C 347 1.508 -19.376 -34.949 1.00 57.54 S ANISOU 2708 SG CYS C 347 7199 5911 8752 1127 1685 800 S ATOM 2709 N GLY C 348 4.130 -18.328 -39.231 1.00 53.28 N ANISOU 2709 N GLY C 348 6231 5787 8227 422 609 788 N ATOM 2710 CA GLY C 348 4.654 -18.698 -40.533 1.00 50.27 C ANISOU 2710 CA GLY C 348 5435 5873 7790 256 341 790 C ATOM 2711 C GLY C 348 3.666 -19.492 -41.368 1.00 57.11 C ANISOU 2711 C GLY C 348 5721 7161 8817 429 286 774 C ATOM 2712 O GLY C 348 4.057 -20.223 -42.277 1.00 64.54 O ANISOU 2712 O GLY C 348 6251 8559 9713 343 14 619 O ATOM 2713 N LEU C 349 2.380 -19.338 -41.058 1.00 56.67 N ANISOU 2713 N LEU C 349 5605 6965 8961 707 519 899 N ATOM 2714 CA LEU C 349 1.309 -20.054 -41.746 1.00 57.03 C ANISOU 2714 CA LEU C 349 5089 7320 9261 896 457 889 C ATOM 2715 C LEU C 349 0.678 -19.244 -42.875 1.00 63.17 C ANISOU 2715 C LEU C 349 5667 8319 10015 1134 425 1103 C ATOM 2716 O LEU C 349 -0.042 -19.791 -43.710 1.00 71.90 O ANISOU 2716 O LEU C 349 6275 9756 11288 1301 273 1054 O ATOM 2717 CB LEU C 349 0.224 -20.460 -40.747 1.00 57.84 C ANISOU 2717 CB LEU C 349 5148 7188 9641 1050 735 944 C ATOM 2718 CG LEU C 349 0.617 -21.562 -39.768 1.00 57.94 C ANISOU 2718 CG LEU C 349 5184 7084 9747 829 715 808 C ATOM 2719 CD1 LEU C 349 -0.483 -21.799 -38.747 1.00 52.85 C ANISOU 2719 CD1 LEU C 349 4485 6283 9314 994 1066 999 C ATOM 2720 CD2 LEU C 349 0.926 -22.836 -40.536 1.00 50.79 C ANISOU 2720 CD2 LEU C 349 3763 6470 9064 670 283 574 C ATOM 2721 N PHE C 350 0.942 -17.942 -42.891 1.00 60.94 N ANISOU 2721 N PHE C 350 5765 7820 9569 1160 519 1341 N ATOM 2722 CA PHE C 350 0.379 -17.061 -43.911 1.00 69.79 C ANISOU 2722 CA PHE C 350 6744 9096 10678 1371 469 1625 C ATOM 2723 C PHE C 350 1.210 -15.789 -44.051 1.00 75.02 C ANISOU 2723 C PHE C 350 7791 9546 11168 1236 420 1916 C ATOM 2724 O PHE C 350 1.212 -15.136 -45.095 1.00 68.44 O ANISOU 2724 O PHE C 350 6810 8955 10238 1280 284 2231 O ATOM 2725 CB PHE C 350 -1.075 -16.715 -43.577 1.00 66.10 C ANISOU 2725 CB PHE C 350 6227 8392 10497 1725 691 1706 C ATOM 2726 CG PHE C 350 -1.774 -15.919 -44.644 1.00 67.46 C ANISOU 2726 CG PHE C 350 6211 8714 10707 1972 595 1975 C ATOM 2727 CD1 PHE C 350 -1.964 -16.449 -45.912 1.00 64.89 C ANISOU 2727 CD1 PHE C 350 5390 8949 10316 2045 348 1974 C ATOM 2728 CD2 PHE C 350 -2.259 -14.648 -44.376 1.00 67.89 C ANISOU 2728 CD2 PHE C 350 6576 8350 10868 2171 704 2198 C ATOM 2729 CE1 PHE C 350 -2.611 -15.720 -46.897 1.00 68.22 C ANISOU 2729 CE1 PHE C 350 5647 9538 10734 2291 242 2247 C ATOM 2730 CE2 PHE C 350 -2.910 -13.915 -45.354 1.00 64.27 C ANISOU 2730 CE2 PHE C 350 5947 7997 10476 2394 575 2476 C ATOM 2731 CZ PHE C 350 -3.087 -14.453 -46.616 1.00 62.42 C ANISOU 2731 CZ PHE C 350 5235 8348 10133 2445 360 2528 C ATOM 2732 OXT PHE C 350 1.910 -15.390 -43.121 1.00 85.90 O ANISOU 2732 OXT PHE C 350 9615 10495 12526 1077 481 1868 O TER 2733 PHE C 350 HETATM 2734 C1 NAG B 1 26.414 -70.152 -40.046 1.00 42.72 C HETATM 2735 C2 NAG B 1 27.038 -69.482 -38.816 1.00 45.97 C HETATM 2736 C3 NAG B 1 28.562 -69.635 -38.834 1.00 46.10 C HETATM 2737 C4 NAG B 1 28.984 -71.081 -39.074 1.00 48.52 C HETATM 2738 C5 NAG B 1 28.262 -71.647 -40.294 1.00 49.57 C HETATM 2739 C6 NAG B 1 28.514 -73.122 -40.512 1.00 53.47 C HETATM 2740 C7 NAG B 1 26.259 -67.452 -37.657 1.00 44.15 C HETATM 2741 C8 NAG B 1 25.960 -65.988 -37.799 1.00 48.52 C HETATM 2742 N2 NAG B 1 26.679 -68.073 -38.764 1.00 39.94 N HETATM 2743 O3 NAG B 1 29.085 -69.180 -37.591 1.00 50.00 O HETATM 2744 O4 NAG B 1 30.384 -71.103 -39.330 1.00 49.03 O HETATM 2745 O5 NAG B 1 26.846 -71.500 -40.128 1.00 52.92 O HETATM 2746 O6 NAG B 1 27.838 -73.906 -39.539 1.00 49.84 O HETATM 2747 O7 NAG B 1 26.129 -68.040 -36.591 1.00 49.53 O HETATM 2748 C1 NAG B 2 31.166 -72.061 -38.589 1.00 41.15 C HETATM 2749 C2 NAG B 2 32.369 -72.293 -39.483 1.00 39.99 C HETATM 2750 C3 NAG B 2 33.368 -73.242 -38.823 1.00 44.91 C HETATM 2751 C4 NAG B 2 33.754 -72.737 -37.435 1.00 39.62 C HETATM 2752 C5 NAG B 2 32.483 -72.518 -36.619 1.00 43.15 C HETATM 2753 C6 NAG B 2 32.745 -71.911 -35.264 1.00 40.58 C HETATM 2754 C7 NAG B 2 31.856 -72.046 -41.878 1.00 52.44 C HETATM 2755 C8 NAG B 2 31.418 -72.750 -43.125 1.00 36.28 C HETATM 2756 N2 NAG B 2 31.958 -72.806 -40.781 1.00 49.08 N HETATM 2757 O3 NAG B 2 34.490 -73.300 -39.696 1.00 49.45 O HETATM 2758 O4 NAG B 2 34.597 -73.637 -36.711 1.00 61.59 O HETATM 2759 O5 NAG B 2 31.595 -71.620 -37.304 1.00 37.73 O HETATM 2760 O6 NAG B 2 31.520 -71.646 -34.596 1.00 41.83 O HETATM 2761 O7 NAG B 2 32.108 -70.844 -41.864 1.00 67.87 O HETATM 2762 C1 BMA B 3 35.952 -73.786 -37.239 1.00 85.67 C HETATM 2763 C2 BMA B 3 37.121 -74.023 -36.176 1.00102.00 C HETATM 2764 C3 BMA B 3 38.058 -75.126 -36.739 1.00115.31 C HETATM 2765 C4 BMA B 3 38.377 -74.960 -38.239 1.00112.71 C HETATM 2766 C5 BMA B 3 37.082 -74.886 -39.062 1.00103.72 C HETATM 2767 C6 BMA B 3 36.919 -76.047 -40.035 1.00 95.74 C HETATM 2768 O2 BMA B 3 36.710 -74.441 -34.847 1.00106.33 O HETATM 2769 O3 BMA B 3 37.548 -76.433 -36.478 1.00130.12 O HETATM 2770 O4 BMA B 3 39.162 -73.788 -38.445 1.00116.92 O HETATM 2771 O5 BMA B 3 35.959 -74.887 -38.160 1.00 99.51 O HETATM 2772 O6 BMA B 3 37.359 -75.628 -41.321 1.00 94.44 O HETATM 2773 C1 BMA B 4 37.679 -74.060 -33.817 1.00117.39 C HETATM 2774 C2 BMA B 4 37.226 -74.673 -32.457 1.00122.65 C HETATM 2775 C3 BMA B 4 38.272 -74.393 -31.367 1.00125.26 C HETATM 2776 C4 BMA B 4 39.675 -74.825 -31.813 1.00137.09 C HETATM 2777 C5 BMA B 4 40.033 -74.108 -33.116 1.00136.51 C HETATM 2778 C6 BMA B 4 41.407 -74.503 -33.660 1.00125.77 C HETATM 2779 O2 BMA B 4 37.117 -76.085 -32.552 1.00129.79 O HETATM 2780 O3 BMA B 4 37.940 -75.034 -30.141 1.00122.34 O HETATM 2781 O4 BMA B 4 40.632 -74.506 -30.810 1.00144.02 O HETATM 2782 O5 BMA B 4 39.040 -74.460 -34.105 1.00130.59 O HETATM 2783 O6 BMA B 4 42.365 -74.419 -32.607 1.00113.23 O HETATM 2784 C1 NAG D 1 9.802 -68.788 -43.021 1.00116.01 C HETATM 2785 C2 NAG D 1 8.436 -69.169 -42.440 1.00129.09 C HETATM 2786 C3 NAG D 1 7.786 -70.232 -43.330 1.00143.94 C HETATM 2787 C4 NAG D 1 7.761 -69.780 -44.787 1.00147.11 C HETATM 2788 C5 NAG D 1 9.146 -69.327 -45.242 1.00140.57 C HETATM 2789 C6 NAG D 1 9.151 -68.731 -46.631 1.00137.62 C HETATM 2790 C7 NAG D 1 8.717 -68.853 -40.016 1.00117.78 C HETATM 2791 C8 NAG D 1 8.837 -69.533 -38.685 1.00110.51 C HETATM 2792 N2 NAG D 1 8.566 -69.657 -41.075 1.00124.74 N HETATM 2793 O3 NAG D 1 6.490 -70.630 -42.882 1.00150.40 O HETATM 2794 O4 NAG D 1 7.340 -70.859 -45.613 1.00152.08 O HETATM 2795 O5 NAG D 1 9.637 -68.313 -44.355 1.00131.53 O HETATM 2796 O6 NAG D 1 10.360 -69.023 -47.317 1.00133.47 O HETATM 2797 O7 NAG D 1 8.756 -67.632 -40.128 1.00118.90 O HETATM 2798 C1 NAG D 2 5.437 -69.651 -42.829 1.00150.28 C HETATM 2799 C2 NAG D 2 4.302 -69.978 -43.816 1.00150.78 C HETATM 2800 C3 NAG D 2 3.127 -69.028 -43.614 1.00148.80 C HETATM 2801 C4 NAG D 2 2.665 -69.060 -42.166 1.00143.93 C HETATM 2802 C5 NAG D 2 3.832 -68.721 -41.248 1.00138.93 C HETATM 2803 C6 NAG D 2 3.477 -68.856 -39.785 1.00127.54 C HETATM 2804 C7 NAG D 2 4.275 -70.715 -46.161 1.00143.44 C HETATM 2805 C8 NAG D 2 4.861 -70.517 -47.528 1.00137.89 C HETATM 2806 N2 NAG D 2 4.759 -69.926 -45.195 1.00147.94 N HETATM 2807 O3 NAG D 2 2.058 -69.407 -44.474 1.00149.32 O HETATM 2808 O4 NAG D 2 1.614 -68.121 -41.968 1.00142.44 O HETATM 2809 O5 NAG D 2 4.924 -69.622 -41.489 1.00144.85 O HETATM 2810 O6 NAG D 2 2.080 -69.035 -39.602 1.00120.55 O HETATM 2811 O7 NAG D 2 3.403 -71.549 -45.943 1.00145.30 O HETATM 2812 C1 BNG A 407 13.177 -45.507 -36.092 1.00101.92 C HETATM 2813 C2 BNG A 407 13.279 -44.290 -35.178 1.00 98.53 C HETATM 2814 C3 BNG A 407 13.471 -43.021 -35.994 1.00 96.48 C HETATM 2815 C4 BNG A 407 14.676 -43.182 -36.909 1.00105.55 C HETATM 2816 C5 BNG A 407 14.521 -44.424 -37.782 1.00104.58 C HETATM 2817 C6 BNG A 407 15.764 -44.638 -38.641 1.00108.34 C HETATM 2818 C1' BNG A 407 11.927 -47.466 -35.592 1.00 86.17 C HETATM 2819 C2' BNG A 407 11.671 -48.411 -34.425 1.00 80.76 C HETATM 2820 C3' BNG A 407 10.328 -48.147 -33.755 1.00 75.22 C HETATM 2821 C4' BNG A 407 9.217 -48.933 -34.441 1.00 80.40 C HETATM 2822 C5' BNG A 407 8.133 -49.334 -33.445 1.00 85.59 C HETATM 2823 C6' BNG A 407 7.213 -48.166 -33.114 1.00 83.07 C HETATM 2824 C7' BNG A 407 6.184 -47.957 -34.218 1.00 78.23 C HETATM 2825 C8' BNG A 407 5.515 -46.596 -34.079 1.00 75.85 C HETATM 2826 C9' BNG A 407 6.544 -45.490 -34.162 1.00 77.65 C HETATM 2827 O1 BNG A 407 13.079 -46.682 -35.286 1.00 97.68 O HETATM 2828 O2 BNG A 407 12.090 -44.190 -34.382 1.00 92.48 O HETATM 2829 O3 BNG A 407 13.673 -41.908 -35.115 1.00 77.17 O HETATM 2830 O4 BNG A 407 14.808 -42.019 -37.735 1.00106.54 O HETATM 2831 O5 BNG A 407 14.294 -45.595 -36.987 1.00105.02 O HETATM 2832 O6 BNG A 407 16.869 -45.009 -37.807 1.00109.71 O HETATM 2833 C1 BNG A 410 17.645 -14.795 -28.993 1.00127.82 C HETATM 2834 C2 BNG A 410 18.013 -14.349 -27.580 1.00132.15 C HETATM 2835 C3 BNG A 410 17.221 -13.104 -27.209 1.00128.85 C HETATM 2836 C4 BNG A 410 17.458 -12.017 -28.252 1.00130.11 C HETATM 2837 C5 BNG A 410 17.173 -12.543 -29.659 1.00121.22 C HETATM 2838 C6 BNG A 410 17.510 -11.503 -30.724 1.00102.80 C HETATM 2839 C1' BNG A 410 17.872 -16.503 -30.596 1.00 95.64 C HETATM 2840 C2' BNG A 410 18.416 -17.903 -30.851 1.00 79.55 C HETATM 2841 C3' BNG A 410 17.590 -18.965 -30.134 1.00 84.03 C HETATM 2842 C4' BNG A 410 17.933 -20.350 -30.674 1.00 83.78 C HETATM 2843 C5' BNG A 410 17.126 -21.453 -29.996 1.00 83.10 C HETATM 2844 C6' BNG A 410 17.187 -22.727 -30.834 1.00 79.93 C HETATM 2845 C7' BNG A 410 17.049 -23.987 -29.986 1.00 71.05 C HETATM 2846 C8' BNG A 410 17.204 -25.228 -30.856 1.00 66.67 C HETATM 2847 C9' BNG A 410 18.013 -26.293 -30.148 1.00 68.43 C HETATM 2848 O1 BNG A 410 18.356 -15.981 -29.359 1.00112.28 O HETATM 2849 O2 BNG A 410 17.738 -15.397 -26.643 1.00132.74 O HETATM 2850 O3 BNG A 410 17.619 -12.644 -25.912 1.00123.27 O HETATM 2851 O4 BNG A 410 16.600 -10.904 -27.981 1.00134.84 O HETATM 2852 O5 BNG A 410 17.909 -13.742 -29.927 1.00127.69 O HETATM 2853 O6 BNG A 410 18.929 -11.439 -30.905 1.00 87.92 O HETATM 2854 C1 PLM A1322 20.019 -16.298 -56.359 1.00 60.43 C HETATM 2855 O2 PLM A1322 20.896 -15.711 -57.019 1.00 77.93 O HETATM 2856 C2 PLM A1322 19.623 -17.698 -56.779 1.00 60.98 C HETATM 2857 C3 PLM A1322 20.662 -18.673 -56.256 1.00 66.95 C HETATM 2858 C4 PLM A1322 20.269 -20.105 -56.593 1.00 71.82 C HETATM 2859 C5 PLM A1322 20.892 -21.072 -55.594 1.00 72.12 C HETATM 2860 C6 PLM A1322 20.408 -22.495 -55.848 1.00 74.58 C HETATM 2861 C1 PLM A1323 25.293 -14.341 -55.494 1.00 65.52 C HETATM 2862 O2 PLM A1323 24.477 -13.732 -56.213 1.00 79.61 O HETATM 2863 C2 PLM A1323 25.447 -15.835 -55.692 1.00 69.14 C HETATM 2864 C3 PLM A1323 24.602 -16.313 -56.867 1.00 67.21 C HETATM 2865 C4 PLM A1323 24.630 -17.837 -56.912 1.00 64.63 C HETATM 2866 C5 PLM A1323 24.075 -18.416 -58.211 1.00 64.43 C HETATM 2867 C6 PLM A1323 24.369 -19.913 -58.281 1.00 62.47 C HETATM 2868 C7 PLM A1323 23.591 -20.592 -59.405 1.00 66.13 C HETATM 2869 C8 PLM A1323 23.993 -22.052 -59.611 1.00 64.72 C HETATM 2870 C9 PLM A1323 23.559 -22.964 -58.465 1.00 70.36 C HETATM 2871 CA PLM A1323 23.269 -24.378 -58.969 1.00 69.13 C HETATM 2872 CB PLM A1323 23.796 -25.450 -58.019 1.00 67.21 C HETATM 2873 CC PLM A1323 23.614 -26.847 -58.605 1.00 68.79 C HETATM 2874 CD PLM A1323 24.546 -27.852 -57.936 1.00 66.62 C HETATM 2875 CE PLM A1323 24.292 -29.265 -58.451 1.00 66.64 C HETATM 2876 CF PLM A1323 25.209 -30.266 -57.760 1.00 65.74 C HETATM 2877 CG PLM A1323 24.863 -31.688 -58.139 1.00 61.46 C HETATM 2878 O HOH A 501 -11.996 -12.632 -39.003 1.00 63.27 O HETATM 2879 O HOH A 502 33.154 -51.622 -51.330 1.00 51.04 O HETATM 2880 O HOH A 503 32.189 -71.232 -32.280 1.00 56.63 O HETATM 2881 O HOH A 504 29.525 -60.623 -33.982 1.00 44.16 O HETATM 2882 O HOH A 505 20.304 -61.991 -29.928 1.00 54.17 O HETATM 2883 O HOH A 506 25.509 -73.518 -38.497 1.00 45.87 O HETATM 2884 O HOH A 507 21.815 -10.649 -37.450 1.00 59.34 O HETATM 2885 O HOH A 508 19.271 -70.049 -39.613 1.00 44.47 O HETATM 2886 O HOH A 509 -12.389 -18.091 -35.131 1.00 63.83 O HETATM 2887 O HOH A 510 -16.810 -8.927 -40.187 1.00 47.70 O HETATM 2888 O HOH A 511 19.189 -62.152 -31.935 1.00 53.99 O HETATM 2889 O HOH A 512 -19.142 -12.651 -43.331 1.00 47.54 O HETATM 2890 O HOH A 513 23.442 -70.688 -37.611 1.00 49.44 O HETATM 2891 O HOH A 514 26.292 -56.741 -57.615 1.00 43.21 O HETATM 2892 O HOH A 515 28.655 -52.770 -56.595 1.00 53.44 O HETATM 2893 O HOH A 516 15.998 -2.707 -36.104 1.00 74.10 O HETATM 2894 O HOH A 517 -10.588 -21.912 -55.161 1.00 81.90 O HETATM 2895 O HOH A 518 20.603 -69.114 -35.544 1.00 42.21 O HETATM 2896 O HOH A 519 29.117 -52.920 -52.415 1.00 40.56 O HETATM 2897 O HOH A 520 34.411 -67.178 -45.529 1.00 73.44 O HETATM 2898 O HOH A 521 28.517 -60.672 -31.604 1.00 51.52 O HETATM 2899 O HOH A 522 21.032 -57.571 -36.707 1.00 42.46 O HETATM 2900 O HOH A 523 21.112 -51.797 -27.354 1.00 57.18 O HETATM 2901 O HOH A 524 9.120 -22.288 -30.696 1.00 49.14 O HETATM 2902 O HOH A 525 9.368 -24.157 -28.757 1.00 53.29 O HETATM 2903 O HOH A 526 3.555 -29.762 -37.121 1.00 33.01 O HETATM 2904 O HOH A 527 15.673 -46.869 -34.318 1.00 52.90 O HETATM 2905 O HOH A 528 3.972 -25.364 -41.422 1.00 50.66 O HETATM 2906 O HOH A 529 5.935 -22.144 -33.081 1.00 52.48 O HETATM 2907 O HOH A 530 5.458 -24.021 -43.335 1.00 49.99 O HETATM 2908 O HOH A 531 6.599 -23.372 -41.095 1.00 40.88 O HETATM 2909 O HOH A 532 4.354 -33.227 -40.769 1.00 38.16 O HETATM 2910 O HOH A 533 18.462 -51.939 -45.027 1.00 79.24 O HETATM 2911 O HOH A 534 21.025 -51.415 -43.224 1.00 53.30 O HETATM 2912 O HOH A 535 26.289 -60.536 -31.548 1.00 71.22 O HETATM 2913 O HOH A 536 15.992 -57.023 -40.351 1.00 62.48 O HETATM 2914 O HOH A 537 6.829 -20.613 -36.431 1.00 59.19 O HETATM 2915 O HOH A 538 17.751 -57.406 -38.433 1.00 45.68 O HETATM 2916 O HOH A 539 7.574 -18.785 -38.484 1.00 53.42 O HETATM 2917 O HOH A 540 3.750 -22.125 -44.523 1.00 57.81 O HETATM 2918 O HOH A 541 17.061 -46.949 -48.223 1.00 55.57 O HETATM 2919 O HOH A 542 29.193 -65.686 -46.658 1.00 58.23 O HETATM 2920 O HOH A 543 2.631 -52.625 -31.871 1.00 66.03 O HETATM 2921 O HOH A 544 -8.809 -7.479 -47.016 1.00 49.49 O HETATM 2922 O HOH A 545 6.311 -34.976 -41.417 1.00 40.54 O HETATM 2923 O HOH A 546 8.173 -45.194 -41.290 1.00 50.73 O HETATM 2924 O HOH A 547 20.991 -44.076 -41.719 1.00 68.79 O HETATM 2925 O HOH A 548 13.457 -58.980 -49.085 1.00 52.45 O HETATM 2926 O HOH A 549 2.754 -17.827 -18.086 1.00 71.44 O HETATM 2927 O HOH A 550 -9.959 -25.386 -28.280 1.00 67.79 O HETATM 2928 O HOH A 551 14.135 -14.540 -29.451 1.00 77.60 O HETATM 2929 O HOH A 552 36.044 -54.434 -44.706 1.00 65.48 O HETATM 2930 O HOH A 553 21.323 -70.552 -46.077 1.00 68.09 O HETATM 2931 O HOH A 554 10.620 -66.300 -38.751 1.00 78.66 O HETATM 2932 O HOH A 555 28.734 -72.651 -46.683 1.00 65.27 O HETATM 2933 O HOH A 556 11.420 -37.880 -37.759 1.00 81.49 O HETATM 2934 O HOH A 557 4.590 -21.555 -35.465 1.00 58.08 O HETATM 2935 O HOH A 558 17.145 -53.208 -35.970 1.00 59.67 O HETATM 2936 O HOH A 559 17.588 -47.004 -45.757 1.00 63.45 O HETATM 2937 O HOH A 560 8.037 -42.752 -33.253 1.00 67.87 O HETATM 2938 O HOH A 561 -14.734 -20.032 -43.705 1.00 65.99 O HETATM 2939 O HOH A 562 7.277 -15.175 -32.494 1.00 64.99 O HETATM 2940 O HOH A 563 19.541 -70.473 -47.535 1.00 76.44 O HETATM 2941 O HOH C 501 -5.970 -15.661 -33.579 1.00 56.71 O HETATM 2942 O HOH C 502 -5.612 -9.830 -37.184 1.00 69.60 O CONECT 16 2784 CONECT 117 2734 CONECT 892 1496 CONECT 1496 892 CONECT 2610 2854 CONECT 2616 2861 CONECT 2734 117 2735 2745 CONECT 2735 2734 2736 2742 CONECT 2736 2735 2737 2743 CONECT 2737 2736 2738 2744 CONECT 2738 2737 2739 2745 CONECT 2739 2738 2746 CONECT 2740 2741 2742 2747 CONECT 2741 2740 CONECT 2742 2735 2740 CONECT 2743 2736 CONECT 2744 2737 2748 CONECT 2745 2734 2738 CONECT 2746 2739 CONECT 2747 2740 CONECT 2748 2744 2749 2759 CONECT 2749 2748 2750 2756 CONECT 2750 2749 2751 2757 CONECT 2751 2750 2752 2758 CONECT 2752 2751 2753 2759 CONECT 2753 2752 2760 CONECT 2754 2755 2756 2761 CONECT 2755 2754 CONECT 2756 2749 2754 CONECT 2757 2750 CONECT 2758 2751 2762 CONECT 2759 2748 2752 CONECT 2760 2753 CONECT 2761 2754 CONECT 2762 2758 2763 2771 CONECT 2763 2762 2764 2768 CONECT 2764 2763 2765 2769 CONECT 2765 2764 2766 2770 CONECT 2766 2765 2767 2771 CONECT 2767 2766 2772 CONECT 2768 2763 2773 CONECT 2769 2764 CONECT 2770 2765 CONECT 2771 2762 2766 CONECT 2772 2767 CONECT 2773 2768 2774 2782 CONECT 2774 2773 2775 2779 CONECT 2775 2774 2776 2780 CONECT 2776 2775 2777 2781 CONECT 2777 2776 2778 2782 CONECT 2778 2777 2783 CONECT 2779 2774 CONECT 2780 2775 CONECT 2781 2776 CONECT 2782 2773 2777 CONECT 2783 2778 CONECT 2784 16 2785 2795 CONECT 2785 2784 2786 2792 CONECT 2786 2785 2787 2793 CONECT 2787 2786 2788 2794 CONECT 2788 2787 2789 2795 CONECT 2789 2788 2796 CONECT 2790 2791 2792 2797 CONECT 2791 2790 CONECT 2792 2785 2790 CONECT 2793 2786 2798 CONECT 2794 2787 CONECT 2795 2784 2788 CONECT 2796 2789 CONECT 2797 2790 CONECT 2798 2793 2799 2809 CONECT 2799 2798 2800 2806 CONECT 2800 2799 2801 2807 CONECT 2801 2800 2802 2808 CONECT 2802 2801 2803 2809 CONECT 2803 2802 2810 CONECT 2804 2805 2806 2811 CONECT 2805 2804 CONECT 2806 2799 2804 CONECT 2807 2800 CONECT 2808 2801 CONECT 2809 2798 2802 CONECT 2810 2803 CONECT 2811 2804 CONECT 2812 2813 2827 2831 CONECT 2813 2812 2814 2828 CONECT 2814 2813 2815 2829 CONECT 2815 2814 2816 2830 CONECT 2816 2815 2817 2831 CONECT 2817 2816 2832 CONECT 2818 2819 2827 CONECT 2819 2818 2820 CONECT 2820 2819 2821 CONECT 2821 2820 2822 CONECT 2822 2821 2823 CONECT 2823 2822 2824 CONECT 2824 2823 2825 CONECT 2825 2824 2826 CONECT 2826 2825 CONECT 2827 2812 2818 CONECT 2828 2813 CONECT 2829 2814 CONECT 2830 2815 CONECT 2831 2812 2816 CONECT 2832 2817 CONECT 2833 2834 2848 2852 CONECT 2834 2833 2835 2849 CONECT 2835 2834 2836 2850 CONECT 2836 2835 2837 2851 CONECT 2837 2836 2838 2852 CONECT 2838 2837 2853 CONECT 2839 2840 2848 CONECT 2840 2839 2841 CONECT 2841 2840 2842 CONECT 2842 2841 2843 CONECT 2843 2842 2844 CONECT 2844 2843 2845 CONECT 2845 2844 2846 CONECT 2846 2845 2847 CONECT 2847 2846 CONECT 2848 2833 2839 CONECT 2849 2834 CONECT 2850 2835 CONECT 2851 2836 CONECT 2852 2833 2837 CONECT 2853 2838 CONECT 2854 2610 2855 2856 CONECT 2855 2854 CONECT 2856 2854 2857 CONECT 2857 2856 2858 CONECT 2858 2857 2859 CONECT 2859 2858 2860 CONECT 2860 2859 CONECT 2861 2616 2862 2863 CONECT 2862 2861 CONECT 2863 2861 2864 CONECT 2864 2863 2865 CONECT 2865 2864 2866 CONECT 2866 2865 2867 CONECT 2867 2866 2868 CONECT 2868 2867 2869 CONECT 2869 2868 2870 CONECT 2870 2869 2871 CONECT 2871 2870 2872 CONECT 2872 2871 2873 CONECT 2873 2872 2874 CONECT 2874 2873 2875 CONECT 2875 2874 2876 CONECT 2876 2875 2877 CONECT 2877 2876 MASTER 483 0 10 16 4 0 0 6 2886 2 150 28 END