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*** 5WGD_A ***elNémo ID: 2404102226553446872Job options:ID = 2404102226553446872 JOBID = 5WGD_A USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 5WGD_A HEADER TRANSCRIPTION 14-JUL-17 5WGD TITLE ESTROGEN RECEPTOR ALPHA LIGAND BINDING DOMAIN IN COMPLEX WITH TITLE 2 ESTRADIOL AND SRC2-LP1 CAVEAT 5WGD ILE E 4 HAS WRONG CHIRALITY AT ATOM CB ILE F 3 HAS WRONG CAVEAT 2 5WGD CHIRALITY AT ATOM CB THE MODELED PEPTIDE SRC2-LP1 HAVE CAVEAT 3 5WGD DIFFERENT SEQUENCE IDENTITY BETWEEN THE CHAINS E AND F COMPND MOL_ID: 1; COMPND 2 MOLECULE: ESTROGEN RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3 COMPND 5 GROUP A MEMBER 1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: (ACE)HKILHKLLQDS(NH2); COMPND 10 CHAIN: E; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: (ACE)AILHKLLQDS(NH2); COMPND 14 CHAIN: F; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ESR1, ESR, NR3A1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 11 ORGANISM_TAXID: 32630; SOURCE 12 MOL_ID: 3; SOURCE 13 SYNTHETIC: YES; SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 15 ORGANISM_TAXID: 32630 KEYWDS BREAST CANCER, STAPLED PEPTIDES, SYNTHETIC PEPTIDES, HORMONE, KEYWDS 2 TRANSCRIPTION EXPDTA X-RAY DIFFRACTION AUTHOR S.W.FANNING,T.E.SPELTZ,C.G.MAYNE,Z.SIDDIQUI,G.L.GREENE,E.TAJKHORSHID, AUTHOR 2 T.W.MOORE REVDAT 3 04-OCT-23 5WGD 1 REMARK REVDAT 2 26-FEB-20 5WGD 1 REMARK LINK SITE REVDAT 1 13-JUN-18 5WGD 0 JRNL AUTH T.E.SPELTZ,C.G.MAYNE,S.W.FANNING,Z.SIDDIQUI,E.TAJKHORSHID, JRNL AUTH 2 G.L.GREENE,T.W.MOORE JRNL TITL A "CROSS-STITCHED" PEPTIDE WITH IMPROVED HELICITY AND JRNL TITL 2 PROTEOLYTIC STABILITY. JRNL REF ORG. BIOMOL. CHEM. V. 16 3702 2018 JRNL REFN ESSN 1477-0539 JRNL PMID 29725689 JRNL DOI 10.1039/C8OB00790J REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.60 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 3 NUMBER OF REFLECTIONS : 42687 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.177 REMARK 3 R VALUE (WORKING SET) : 0.176 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 2083 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 26.6019 - 4.4420 0.94 2895 134 0.1777 0.1860 REMARK 3 2 4.4420 - 3.5283 0.99 2961 162 0.1435 0.1678 REMARK 3 3 3.5283 - 3.0831 0.99 2969 145 0.1647 0.1951 REMARK 3 4 3.0831 - 2.8015 0.98 2943 148 0.1744 0.2094 REMARK 3 5 2.8015 - 2.6009 0.99 2980 144 0.1872 0.2500 REMARK 3 6 2.6009 - 2.4477 0.98 2913 169 0.1761 0.2356 REMARK 3 7 2.4477 - 2.3252 0.98 2938 126 0.1747 0.1964 REMARK 3 8 2.3252 - 2.2240 0.97 2883 161 0.1745 0.2055 REMARK 3 9 2.2240 - 2.1384 0.96 2885 149 0.1695 0.2088 REMARK 3 10 2.1384 - 2.0647 0.95 2846 141 0.1837 0.2086 REMARK 3 11 2.0647 - 2.0001 0.95 2804 139 0.2012 0.2642 REMARK 3 12 2.0001 - 1.9430 0.93 2721 166 0.2066 0.2586 REMARK 3 13 1.9430 - 1.8918 0.84 2529 136 0.2266 0.2635 REMARK 3 14 1.8918 - 1.8457 0.66 1979 99 0.2601 0.2929 REMARK 3 15 1.8457 - 1.8038 0.46 1358 64 0.2674 0.3654 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.740 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 : 0.006 3856 REMARK 3 ANGLE : 1.294 5234 REMARK 3 CHIRALITY : 0.087 629 REMARK 3 PLANARITY : 0.004 647 REMARK 3 DIHEDRAL : 13.767 1476 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 308 THROUGH 321 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.9359 9.8127 50.8525 REMARK 3 T TENSOR REMARK 3 T11: 0.2710 T22: 0.3198 REMARK 3 T33: 0.3305 T12: 0.0096 REMARK 3 T13: -0.0629 T23: 0.1482 REMARK 3 L TENSOR REMARK 3 L11: 3.7785 L22: 3.8852 REMARK 3 L33: 4.0491 L12: 0.6897 REMARK 3 L13: 0.3364 L23: -1.9229 REMARK 3 S TENSOR REMARK 3 S11: 0.3643 S12: 0.8972 S13: 1.0373 REMARK 3 S21: -0.3650 S22: 0.2010 S23: 0.8095 REMARK 3 S31: -0.4646 S32: -0.5116 S33: -0.2643 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 322 THROUGH 338 ) REMARK 3 ORIGIN FOR THE GROUP (A): 64.9234 -6.8265 51.4401 REMARK 3 T TENSOR REMARK 3 T11: 0.1760 T22: 0.1958 REMARK 3 T33: 0.2080 T12: 0.0008 REMARK 3 T13: 0.0520 T23: -0.0188 REMARK 3 L TENSOR REMARK 3 L11: 7.0034 L22: 6.6760 REMARK 3 L33: 1.7600 L12: -5.6516 REMARK 3 L13: 2.5373 L23: -1.6472 REMARK 3 S TENSOR REMARK 3 S11: 0.0301 S12: 0.1091 S13: 0.3198 REMARK 3 S21: -0.2750 S22: 0.0131 S23: -0.6534 REMARK 3 S31: 0.1354 S32: 0.0044 S33: -0.0020 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 363 ) REMARK 3 ORIGIN FOR THE GROUP (A): 61.8509 2.4905 56.0915 REMARK 3 T TENSOR REMARK 3 T11: 0.1368 T22: 0.1519 REMARK 3 T33: 0.0965 T12: -0.0194 REMARK 3 T13: 0.0261 T23: -0.0138 REMARK 3 L TENSOR REMARK 3 L11: 6.4524 L22: 5.7644 REMARK 3 L33: 0.8651 L12: -4.8660 REMARK 3 L13: 1.0669 L23: -1.2197 REMARK 3 S TENSOR REMARK 3 S11: 0.2394 S12: 0.2826 S13: -0.0263 REMARK 3 S21: -0.4382 S22: -0.1552 S23: -0.1524 REMARK 3 S31: -0.0198 S32: 0.2234 S33: -0.0541 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 394 ) REMARK 3 ORIGIN FOR THE GROUP (A): 52.8324 9.2752 61.2977 REMARK 3 T TENSOR REMARK 3 T11: 0.0742 T22: 0.1091 REMARK 3 T33: 0.0823 T12: -0.0117 REMARK 3 T13: 0.0312 T23: 0.0059 REMARK 3 L TENSOR REMARK 3 L11: 1.6512 L22: 5.3452 REMARK 3 L33: 1.9223 L12: 0.3611 REMARK 3 L13: -0.0919 L23: 0.6179 REMARK 3 S TENSOR REMARK 3 S11: 0.0404 S12: -0.0212 S13: 0.2247 REMARK 3 S21: 0.0183 S22: -0.0055 S23: 0.1983 REMARK 3 S31: -0.2085 S32: 0.0385 S33: -0.0339 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 395 THROUGH 407 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.2121 -11.9736 55.4434 REMARK 3 T TENSOR REMARK 3 T11: 0.1737 T22: 0.1063 REMARK 3 T33: 0.2218 T12: 0.0033 REMARK 3 T13: 0.0374 T23: -0.0539 REMARK 3 L TENSOR REMARK 3 L11: 2.2810 L22: 3.9800 REMARK 3 L33: 2.8338 L12: 0.5533 REMARK 3 L13: -0.4435 L23: -0.4207 REMARK 3 S TENSOR REMARK 3 S11: -0.1880 S12: 0.1295 S13: -0.6861 REMARK 3 S21: -0.4005 S22: -0.1022 S23: 0.1810 REMARK 3 S31: 0.4756 S32: 0.1086 S33: 0.0654 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 408 THROUGH 420 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.7320 -14.6461 63.1754 REMARK 3 T TENSOR REMARK 3 T11: 0.2707 T22: 0.1530 REMARK 3 T33: 0.2860 T12: 0.0492 REMARK 3 T13: 0.0866 T23: 0.0383 REMARK 3 L TENSOR REMARK 3 L11: 1.9465 L22: 1.4872 REMARK 3 L33: 8.6686 L12: -0.6693 REMARK 3 L13: 3.6061 L23: -1.2577 REMARK 3 S TENSOR REMARK 3 S11: 0.1104 S12: -0.0592 S13: -0.5305 REMARK 3 S21: -0.0554 S22: 0.2103 S23: -0.0315 REMARK 3 S31: 0.5160 S32: 0.0989 S33: -0.2539 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 421 THROUGH 438 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.2345 -10.8413 65.4097 REMARK 3 T TENSOR REMARK 3 T11: 0.1687 T22: 0.1158 REMARK 3 T33: 0.2073 T12: 0.0011 REMARK 3 T13: 0.0456 T23: 0.0078 REMARK 3 L TENSOR REMARK 3 L11: 2.1079 L22: 3.2734 REMARK 3 L33: 3.2934 L12: -0.3510 REMARK 3 L13: 1.4411 L23: -0.3474 REMARK 3 S TENSOR REMARK 3 S11: -0.1664 S12: -0.1927 S13: -0.7225 REMARK 3 S21: 0.1724 S22: 0.0032 S23: 0.3595 REMARK 3 S31: 0.1650 S32: 0.0110 S33: 0.1147 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 439 THROUGH 473 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.1555 4.7401 61.4634 REMARK 3 T TENSOR REMARK 3 T11: 0.0961 T22: 0.1263 REMARK 3 T33: 0.0848 T12: 0.0070 REMARK 3 T13: 0.0129 T23: 0.0321 REMARK 3 L TENSOR REMARK 3 L11: 4.9988 L22: 2.7157 REMARK 3 L33: 2.5317 L12: 1.3068 REMARK 3 L13: 0.4791 L23: 0.6029 REMARK 3 S TENSOR REMARK 3 S11: 0.0634 S12: 0.0025 S13: 0.0717 REMARK 3 S21: 0.0250 S22: -0.1117 S23: 0.0877 REMARK 3 S31: -0.1468 S32: -0.2451 S33: 0.1005 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 474 THROUGH 496 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.0313 6.5305 60.1066 REMARK 3 T TENSOR REMARK 3 T11: 0.1410 T22: 0.2517 REMARK 3 T33: 0.1391 T12: 0.0600 REMARK 3 T13: 0.0012 T23: 0.0491 REMARK 3 L TENSOR REMARK 3 L11: 5.9857 L22: 2.8486 REMARK 3 L33: 2.7409 L12: 1.2586 REMARK 3 L13: -0.3707 L23: -0.1464 REMARK 3 S TENSOR REMARK 3 S11: 0.0685 S12: 0.4305 S13: 0.3798 REMARK 3 S21: -0.3535 S22: -0.0993 S23: -0.0147 REMARK 3 S31: -0.3724 S32: -0.2602 S33: -0.0376 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 497 THROUGH 530 ) REMARK 3 ORIGIN FOR THE GROUP (A): 49.1241 -1.4424 69.1733 REMARK 3 T TENSOR REMARK 3 T11: 0.1238 T22: 0.1456 REMARK 3 T33: 0.0750 T12: 0.0020 REMARK 3 T13: 0.0155 T23: 0.0088 REMARK 3 L TENSOR REMARK 3 L11: 5.6956 L22: 0.6980 REMARK 3 L33: 0.2016 L12: -0.3538 REMARK 3 L13: -0.2944 L23: 0.1759 REMARK 3 S TENSOR REMARK 3 S11: -0.1340 S12: -0.1725 S13: -0.0999 REMARK 3 S21: 0.0339 S22: 0.0801 S23: -0.0231 REMARK 3 S31: 0.0285 S32: 0.0564 S33: 0.0326 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 531 THROUGH 537 ) REMARK 3 ORIGIN FOR THE GROUP (A): 73.9424 0.5801 65.4339 REMARK 3 T TENSOR REMARK 3 T11: 0.1090 T22: 0.2104 REMARK 3 T33: 0.2608 T12: -0.0119 REMARK 3 T13: -0.0200 T23: -0.0002 REMARK 3 L TENSOR REMARK 3 L11: 7.6330 L22: 3.5546 REMARK 3 L33: 4.3171 L12: -5.0197 REMARK 3 L13: 2.9835 L23: -1.1431 REMARK 3 S TENSOR REMARK 3 S11: 0.6066 S12: 0.1831 S13: -0.3470 REMARK 3 S21: -0.2897 S22: 0.0216 S23: 0.1274 REMARK 3 S31: 0.2984 S32: 0.0848 S33: -0.2377 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 538 THROUGH 547 ) REMARK 3 ORIGIN FOR THE GROUP (A): 65.6380 9.6159 65.6502 REMARK 3 T TENSOR REMARK 3 T11: 0.1875 T22: 0.1660 REMARK 3 T33: 0.3192 T12: -0.0192 REMARK 3 T13: 0.0053 T23: 0.0162 REMARK 3 L TENSOR REMARK 3 L11: 8.5588 L22: 2.9089 REMARK 3 L33: 7.0822 L12: -3.1488 REMARK 3 L13: -1.7405 L23: -0.3180 REMARK 3 S TENSOR REMARK 3 S11: 0.0480 S12: -0.3377 S13: 0.4232 REMARK 3 S21: 0.2945 S22: 0.0041 S23: -0.4403 REMARK 3 S31: -0.4778 S32: 0.2129 S33: -0.1626 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 307 THROUGH 338 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.0578 -1.1624 89.4415 REMARK 3 T TENSOR REMARK 3 T11: 0.2369 T22: 0.3275 REMARK 3 T33: 0.1857 T12: 0.0501 REMARK 3 T13: 0.0502 T23: 0.0704 REMARK 3 L TENSOR REMARK 3 L11: 4.0818 L22: 1.9652 REMARK 3 L33: 3.8125 L12: -0.4106 REMARK 3 L13: 2.5620 L23: -0.8325 REMARK 3 S TENSOR REMARK 3 S11: -0.0434 S12: -0.8241 S13: -0.6413 REMARK 3 S21: 0.4618 S22: 0.2291 S23: 0.5138 REMARK 3 S31: 0.0241 S32: -0.7569 S33: -0.3410 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 363 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.5321 0.4017 94.9538 REMARK 3 T TENSOR REMARK 3 T11: 0.2593 T22: 0.1523 REMARK 3 T33: 0.1163 T12: 0.0429 REMARK 3 T13: -0.0374 T23: -0.0024 REMARK 3 L TENSOR REMARK 3 L11: 4.9643 L22: 3.8665 REMARK 3 L33: 3.9268 L12: 1.6793 REMARK 3 L13: 3.2009 L23: 0.8564 REMARK 3 S TENSOR REMARK 3 S11: -0.2749 S12: 0.0142 S13: 0.1501 REMARK 3 S21: 0.5179 S22: 0.1135 S23: -0.2077 REMARK 3 S31: -0.1326 S32: 0.1989 S33: 0.0882 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 364 THROUGH 371 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.7777 -14.0409 84.7976 REMARK 3 T TENSOR REMARK 3 T11: 0.3695 T22: 0.2117 REMARK 3 T33: 0.3576 T12: -0.0749 REMARK 3 T13: -0.0604 T23: 0.0386 REMARK 3 L TENSOR REMARK 3 L11: 8.5880 L22: 5.0604 REMARK 3 L33: 2.7122 L12: -6.5876 REMARK 3 L13: -1.8487 L23: 1.5314 REMARK 3 S TENSOR REMARK 3 S11: -0.2705 S12: -0.0387 S13: -1.3575 REMARK 3 S21: -0.2389 S22: 0.1576 S23: 0.9307 REMARK 3 S31: 0.4756 S32: -0.5500 S33: 0.1365 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 372 THROUGH 394 ) REMARK 3 ORIGIN FOR THE GROUP (A): 45.9471 -2.9910 85.2791 REMARK 3 T TENSOR REMARK 3 T11: 0.1098 T22: 0.1366 REMARK 3 T33: 0.0629 T12: 0.0072 REMARK 3 T13: -0.0188 T23: 0.0007 REMARK 3 L TENSOR REMARK 3 L11: 2.7527 L22: 5.1856 REMARK 3 L33: 3.3688 L12: -0.7952 REMARK 3 L13: 0.4215 L23: 0.2622 REMARK 3 S TENSOR REMARK 3 S11: 0.0335 S12: 0.0129 S13: -0.1579 REMARK 3 S21: 0.2044 S22: -0.0116 S23: -0.2056 REMARK 3 S31: 0.0987 S32: 0.1777 S33: -0.0238 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 407 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.1623 15.3727 91.5989 REMARK 3 T TENSOR REMARK 3 T11: 0.5996 T22: 0.0274 REMARK 3 T33: 0.1591 T12: 0.0852 REMARK 3 T13: -0.1129 T23: -0.1395 REMARK 3 L TENSOR REMARK 3 L11: 2.5461 L22: 1.7748 REMARK 3 L33: 0.7450 L12: -0.7028 REMARK 3 L13: 1.0743 L23: -0.9318 REMARK 3 S TENSOR REMARK 3 S11: -0.3737 S12: -0.4338 S13: 0.7774 REMARK 3 S21: 0.9427 S22: 0.3112 S23: -0.0954 REMARK 3 S31: -0.9604 S32: -0.2326 S33: 0.3165 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 408 THROUGH 420 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.7221 17.1439 90.7050 REMARK 3 T TENSOR REMARK 3 T11: 0.5787 T22: 0.2429 REMARK 3 T33: 0.4416 T12: -0.1200 REMARK 3 T13: -0.2457 T23: -0.0366 REMARK 3 L TENSOR REMARK 3 L11: 2.9425 L22: 3.6819 REMARK 3 L33: 2.1806 L12: -2.9952 REMARK 3 L13: -1.4810 L23: 1.0195 REMARK 3 S TENSOR REMARK 3 S11: -0.2003 S12: -0.0897 S13: 0.8238 REMARK 3 S21: 0.1857 S22: 0.0461 S23: -1.1086 REMARK 3 S31: -0.8830 S32: 0.4068 S33: 0.0662 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 421 THROUGH 438 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.6556 14.3093 81.1188 REMARK 3 T TENSOR REMARK 3 T11: 0.2916 T22: 0.1252 REMARK 3 T33: 0.1405 T12: -0.0301 REMARK 3 T13: -0.0167 T23: -0.0035 REMARK 3 L TENSOR REMARK 3 L11: 7.1990 L22: 5.2785 REMARK 3 L33: 5.0152 L12: 0.0800 REMARK 3 L13: 3.3616 L23: 0.1276 REMARK 3 S TENSOR REMARK 3 S11: -0.1981 S12: -0.0259 S13: 0.2865 REMARK 3 S21: 0.0790 S22: -0.0149 S23: -0.1342 REMARK 3 S31: -0.6452 S32: 0.0385 S33: 0.2171 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 439 THROUGH 473 ) REMARK 3 ORIGIN FOR THE GROUP (A): 37.9276 -0.8916 79.4853 REMARK 3 T TENSOR REMARK 3 T11: 0.1118 T22: 0.1347 REMARK 3 T33: 0.0710 T12: -0.0221 REMARK 3 T13: -0.0063 T23: 0.0030 REMARK 3 L TENSOR REMARK 3 L11: 4.0540 L22: 7.2299 REMARK 3 L33: 5.0339 L12: -1.4409 REMARK 3 L13: 0.0657 L23: 0.9370 REMARK 3 S TENSOR REMARK 3 S11: 0.0232 S12: 0.1727 S13: -0.2014 REMARK 3 S21: -0.1443 S22: -0.1461 S23: 0.1184 REMARK 3 S31: -0.0248 S32: -0.0290 S33: 0.1906 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 496 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.6425 -1.8912 74.9800 REMARK 3 T TENSOR REMARK 3 T11: 0.0836 T22: 0.2164 REMARK 3 T33: 0.1489 T12: -0.0321 REMARK 3 T13: 0.0168 T23: 0.0064 REMARK 3 L TENSOR REMARK 3 L11: 7.2562 L22: 6.3382 REMARK 3 L33: 3.3621 L12: -5.1775 REMARK 3 L13: 1.0202 L23: -1.4157 REMARK 3 S TENSOR REMARK 3 S11: -0.0256 S12: -0.1181 S13: -0.3517 REMARK 3 S21: 0.0207 S22: -0.0850 S23: 0.2923 REMARK 3 S31: 0.2032 S32: -0.1268 S33: 0.1206 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 497 THROUGH 530 ) REMARK 3 ORIGIN FOR THE GROUP (A): 46.4675 4.8192 76.8052 REMARK 3 T TENSOR REMARK 3 T11: 0.1231 T22: 0.1083 REMARK 3 T33: 0.0819 T12: -0.0264 REMARK 3 T13: 0.0389 T23: -0.0198 REMARK 3 L TENSOR REMARK 3 L11: 2.9808 L22: 2.2803 REMARK 3 L33: 4.6842 L12: -0.2791 REMARK 3 L13: 2.4702 L23: -0.8887 REMARK 3 S TENSOR REMARK 3 S11: -0.1317 S12: 0.2214 S13: 0.3550 REMARK 3 S21: 0.0425 S22: -0.0733 S23: -0.2553 REMARK 3 S31: -0.1424 S32: 0.4190 S33: 0.1298 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 531 THROUGH 537 ) REMARK 3 ORIGIN FOR THE GROUP (A): 63.4976 0.8594 95.8403 REMARK 3 T TENSOR REMARK 3 T11: 0.3736 T22: 0.5220 REMARK 3 T33: 0.5046 T12: -0.0923 REMARK 3 T13: -0.2416 T23: -0.0763 REMARK 3 L TENSOR REMARK 3 L11: 6.9333 L22: 0.6230 REMARK 3 L33: 2.2372 L12: -0.1014 REMARK 3 L13: 1.7646 L23: -1.0745 REMARK 3 S TENSOR REMARK 3 S11: -0.0762 S12: -0.2109 S13: 0.9215 REMARK 3 S21: 0.2301 S22: 0.2983 S23: 0.1900 REMARK 3 S31: -0.1520 S32: 0.1420 S33: 0.3372 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 538 THROUGH 548 ) REMARK 3 ORIGIN FOR THE GROUP (A): 56.9130 -6.9807 89.2173 REMARK 3 T TENSOR REMARK 3 T11: 0.2561 T22: 0.2826 REMARK 3 T33: 0.2993 T12: -0.0104 REMARK 3 T13: -0.0803 T23: 0.0330 REMARK 3 L TENSOR REMARK 3 L11: 6.9236 L22: 5.0920 REMARK 3 L33: 2.1642 L12: 2.0922 REMARK 3 L13: 3.7536 L23: 1.6608 REMARK 3 S TENSOR REMARK 3 S11: 0.1510 S12: -0.0089 S13: -0.7680 REMARK 3 S21: 0.3571 S22: -0.2376 S23: -0.9411 REMARK 3 S31: 0.3831 S32: 0.8309 S33: 0.1302 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 5WGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1000228993. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-BM REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45402 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4 REMARK 200 DATA REDUNDANCY : 3.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: 5DXE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3,350, MGCL2, TRIS PH 8.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.91550 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 294 REMARK 465 ASP A 295 REMARK 465 PRO A 296 REMARK 465 MET A 297 REMARK 465 ILE A 298 REMARK 465 LYS A 299 REMARK 465 ARG A 300 REMARK 465 SER A 301 REMARK 465 LYS A 302 REMARK 465 LYS A 303 REMARK 465 ASN A 304 REMARK 465 SER A 305 REMARK 465 LEU A 306 REMARK 465 ALA A 307 REMARK 465 PHE A 461 REMARK 465 LEU A 462 REMARK 465 SER A 463 REMARK 465 SER A 464 REMARK 465 THR A 465 REMARK 465 LEU A 466 REMARK 465 LYS A 467 REMARK 465 SER A 468 REMARK 465 LEU A 469 REMARK 465 GLU A 470 REMARK 465 GLU A 471 REMARK 465 LYS A 472 REMARK 465 ARG A 548 REMARK 465 LEU A 549 REMARK 465 HIS A 550 REMARK 465 ALA A 551 REMARK 465 PRO A 552 REMARK 465 THR A 553 REMARK 465 SER A 554 REMARK 465 MET B 294 REMARK 465 ASP B 295 REMARK 465 PRO B 296 REMARK 465 MET B 297 REMARK 465 ILE B 298 REMARK 465 LYS B 299 REMARK 465 ARG B 300 REMARK 465 SER B 301 REMARK 465 LYS B 302 REMARK 465 LYS B 303 REMARK 465 ASN B 304 REMARK 465 SER B 305 REMARK 465 LEU B 306 REMARK 465 GLU B 330 REMARK 465 TYR B 331 REMARK 465 ASP B 332 REMARK 465 PRO B 333 REMARK 465 THR B 334 REMARK 465 ARG B 335 REMARK 465 PRO B 336 REMARK 465 PHE B 337 REMARK 465 PHE B 461 REMARK 465 LEU B 462 REMARK 465 SER B 463 REMARK 465 SER B 464 REMARK 465 THR B 465 REMARK 465 LEU B 466 REMARK 465 LYS B 467 REMARK 465 SER B 468 REMARK 465 LEU B 469 REMARK 465 GLU B 470 REMARK 465 GLU B 471 REMARK 465 LYS B 472 REMARK 465 LEU B 549 REMARK 465 HIS B 550 REMARK 465 ALA B 551 REMARK 465 PRO B 552 REMARK 465 THR B 553 REMARK 465 SER B 554 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 309 OG REMARK 470 LEU A 310 CG CD1 CD2 REMARK 470 ARG A 335 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 362 CE NZ REMARK 470 GLU A 397 CG CD OE1 OE2 REMARK 470 GLU A 419 CG CD OE1 OE2 REMARK 470 GLU A 423 CG CD OE1 OE2 REMARK 470 MET A 437 CG SD CE REMARK 470 TYR A 459 CD1 CE1 OH REMARK 470 ASP A 473 CG OD1 OD2 REMARK 470 LYS A 492 CG CD CE NZ REMARK 470 HIS B 373 CG ND1 CD2 CE1 NE2 REMARK 470 GLU B 397 CG CD OE1 OE2 REMARK 470 ASP B 411 CG OD1 OD2 REMARK 470 GLU B 419 CG CD OE1 OE2 REMARK 470 GLU B 423 CG CD OE1 OE2 REMARK 470 TYR B 459 OH REMARK 470 LYS B 531 CG CD CE NZ REMARK 470 GLU B 542 CG CD OE1 OE2 REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2 REMARK 470 ASP E 11 OD2 REMARK 470 ASP F 10 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NZ LYS F 6 CG ASP F 10 1.37 REMARK 500 NZ LYS E 7 CG ASP E 11 1.38 REMARK 500 O HOH A 904 O HOH B 835 2.08 REMARK 500 O HOH B 838 O HOH B 855 2.10 REMARK 500 OD1 ASN B 359 OG SER F 11 2.12 REMARK 500 O HOH B 833 O HOH B 871 2.15 REMARK 500 O HOH F 103 O HOH F 104 2.16 REMARK 500 O HOH B 768 O HOH B 846 2.17 REMARK 500 O HOH B 831 O HOH B 868 2.18 REMARK 500 O HOH A 853 O HOH B 799 2.19 REMARK 500 O HOH B 834 O HOH B 847 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 HIS E 6 NE2 HIS E 6 CD2 -0.066 REMARK 500 LEU F 7 CA LEU F 7 C -0.162 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLU A 330 34.25 -92.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 879 DISTANCE = 6.14 ANGSTROMS REMARK 525 HOH B 880 DISTANCE = 7.03 ANGSTROMS REMARK 525 HOH B 881 DISTANCE = 7.79 ANGSTROMS REMARK 525 HOH B 882 DISTANCE = 8.54 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EST A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue EST B 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Ligand NH2 E 13 bound to SER E REMARK 800 12 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Ligand NH2 F 12 bound to SER F REMARK 800 11 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ACE F 1 and ALA F 2 DBREF 5WGD A 297 554 UNP P03372 ESR1_HUMAN 124 381 DBREF 5WGD B 297 554 UNP P03372 ESR1_HUMAN 124 381 DBREF 5WGD E 1 13 PDB 5WGD 5WGD 1 13 DBREF 5WGD F 1 12 PDB 5WGD 5WGD 1 12 SEQADV 5WGD MET A 294 UNP P03372 INITIATING METHIONINE SEQADV 5WGD ASP A 295 UNP P03372 EXPRESSION TAG SEQADV 5WGD PRO A 296 UNP P03372 EXPRESSION TAG SEQADV 5WGD SER A 537 UNP P03372 TYR 364 ENGINEERED MUTATION SEQADV 5WGD MET B 294 UNP P03372 INITIATING METHIONINE SEQADV 5WGD ASP B 295 UNP P03372 EXPRESSION TAG SEQADV 5WGD PRO B 296 UNP P03372 EXPRESSION TAG SEQADV 5WGD SER B 537 UNP P03372 TYR 364 ENGINEERED MUTATION SEQRES 1 A 261 MET ASP PRO MET ILE LYS ARG SER LYS LYS ASN SER LEU SEQRES 2 A 261 ALA LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU SEQRES 3 A 261 LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP SEQRES 4 A 261 PRO THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU SEQRES 5 A 261 LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE SEQRES 6 A 261 ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR SEQRES 7 A 261 LEU HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU SEQRES 8 A 261 GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU SEQRES 9 A 261 HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU SEQRES 10 A 261 ASP ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU SEQRES 11 A 261 ILE PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG SEQRES 12 A 261 MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SEQRES 13 A 261 SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU SEQRES 14 A 261 SER SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE SEQRES 15 A 261 HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS SEQRES 16 A 261 LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS SEQRES 17 A 261 GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE SEQRES 18 A 261 ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER SEQRES 19 A 261 MET LYS CYS LYS ASN VAL VAL PRO LEU SER ASP LEU LEU SEQRES 20 A 261 LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA PRO THR SEQRES 21 A 261 SER SEQRES 1 B 261 MET ASP PRO MET ILE LYS ARG SER LYS LYS ASN SER LEU SEQRES 2 B 261 ALA LEU SER LEU THR ALA ASP GLN MET VAL SER ALA LEU SEQRES 3 B 261 LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU TYR ASP SEQRES 4 B 261 PRO THR ARG PRO PHE SER GLU ALA SER MET MET GLY LEU SEQRES 5 B 261 LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS MET ILE SEQRES 6 B 261 ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP LEU THR SEQRES 7 B 261 LEU HIS ASP GLN VAL HIS LEU LEU GLU CYS ALA TRP LEU SEQRES 8 B 261 GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER MET GLU SEQRES 9 B 261 HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU LEU LEU SEQRES 10 B 261 ASP ARG ASN GLN GLY LYS CYS VAL GLU GLY MET VAL GLU SEQRES 11 B 261 ILE PHE ASP MET LEU LEU ALA THR SER SER ARG PHE ARG SEQRES 12 B 261 MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS LEU LYS SEQRES 13 B 261 SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR PHE LEU SEQRES 14 B 261 SER SER THR LEU LYS SER LEU GLU GLU LYS ASP HIS ILE SEQRES 15 B 261 HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU ILE HIS SEQRES 16 B 261 LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN GLN HIS SEQRES 17 B 261 GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER HIS ILE SEQRES 18 B 261 ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU TYR SER SEQRES 19 B 261 MET LYS CYS LYS ASN VAL VAL PRO LEU SER ASP LEU LEU SEQRES 20 B 261 LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA PRO THR SEQRES 21 B 261 SER SEQRES 1 E 13 ACE HIS LYS ILE LEU HIS LYS LEU LEU GLN ASP SER NH2 SEQRES 1 F 12 ACE ALA ILE LEU HIS LYS LEU LEU GLN ASP SER NH2 HET ACE E 1 3 HET NH2 E 13 1 HET ACE F 1 2 HET NH2 F 12 1 HET EST A 601 20 HET EST B 601 20 HETNAM ACE ACETYL GROUP HETNAM NH2 AMINO GROUP HETNAM EST ESTRADIOL FORMUL 3 ACE 2(C2 H4 O) FORMUL 3 NH2 2(H2 N) FORMUL 5 EST 2(C18 H24 O2) FORMUL 7 HOH *416(H2 O) HELIX 1 1 THR A 311 ALA A 322 1 12 HELIX 2 2 SER A 338 LYS A 362 1 25 HELIX 3 3 GLY A 366 SER A 395 1 30 HELIX 4 4 ARG A 412 LYS A 416 1 5 HELIX 5 5 MET A 421 ASN A 439 1 19 HELIX 6 6 GLN A 441 SER A 456 1 16 HELIX 7 7 HIS A 474 ALA A 493 1 20 HELIX 8 8 THR A 496 LYS A 531 1 36 HELIX 9 9 SER A 537 ALA A 546 1 10 HELIX 10 10 THR B 311 ALA B 322 1 12 HELIX 11 11 GLU B 339 ARG B 363 1 25 HELIX 12 12 GLY B 366 MET B 396 1 31 HELIX 13 13 ASN B 413 VAL B 418 1 6 HELIX 14 14 GLY B 420 ASN B 439 1 20 HELIX 15 15 GLN B 441 SER B 456 1 16 HELIX 16 16 HIS B 474 ALA B 493 1 20 HELIX 17 17 THR B 496 LYS B 531 1 36 HELIX 18 18 SER B 537 ALA B 546 1 10 HELIX 19 19 LYS E 3 LEU E 9 1 7 HELIX 20 20 ALA F 2 SER F 11 1 10 SHEET 1 1 1 LYS A 401 ALA A 405 0 SHEET 2 2 1 LEU A 408 ASP A 411 0 SHEET 3 3 1 LYS B 401 ALA B 405 0 SHEET 4 4 1 LEU B 408 ASP B 411 0 LINK C ACE E 1 N HIS E 2 1555 1555 1.32 LINK C SER E 12 N NH2 E 13 1555 1555 1.33 LINK C ACE F 1 N ALA F 2 1555 1555 1.30 LINK C SER F 11 N NH2 F 12 1555 1555 1.31 SITE 1 AC1 7 MET A 343 LEU A 346 GLU A 353 ARG A 394 SITE 2 AC1 7 HIS A 524 LEU A 525 HOH A 788 SITE 1 AC2 7 MET B 343 LEU B 346 GLU B 353 ARG B 394 SITE 2 AC2 7 HIS B 524 LEU B 525 HOH B 791 SITE 1 AC3 3 GLN E 10 ASP E 11 SER E 12 SITE 1 AC4 4 LYS B 362 LEU F 8 ASP F 10 SER F 11 SITE 1 AC5 4 ILE F 3 LEU F 4 HIS F 5 LYS F 6 CRYST1 56.037 83.831 58.375 90.00 108.32 90.00 P 1 21 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017845 0.000000 0.005907 0.00000 SCALE2 0.000000 0.011929 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018045 0.00000 ATOM 1 N LEU A 308 37.140 18.149 56.013 1.00 54.44 N ANISOU 1 N LEU A 308 7059 4452 9171 771 1404 1244 N ATOM 2 CA LEU A 308 35.849 17.955 56.658 1.00 55.51 C ANISOU 2 CA LEU A 308 7023 4596 9472 964 1553 1226 C ATOM 3 C LEU A 308 34.712 17.840 55.675 1.00 56.65 C ANISOU 3 C LEU A 308 6821 4949 9754 1183 1414 1633 C ATOM 4 O LEU A 308 33.722 17.236 55.953 1.00 58.20 O ANISOU 4 O LEU A 308 6785 5305 10024 1294 1415 1686 O ATOM 5 CB LEU A 308 35.578 19.081 57.615 1.00 59.61 C ANISOU 5 CB LEU A 308 7677 4813 10158 1070 1844 1071 C ATOM 6 CG LEU A 308 36.639 19.274 58.659 1.00 59.77 C ANISOU 6 CG LEU A 308 8046 4632 10033 849 1915 744 C ATOM 7 CD1 LEU A 308 36.106 20.196 59.713 1.00 63.80 C ANISOU 7 CD1 LEU A 308 8681 4862 10697 981 2191 601 C ATOM 8 CD2 LEU A 308 37.012 17.954 59.264 1.00 55.67 C ANISOU 8 CD2 LEU A 308 7642 4294 9215 578 1819 439 C ATOM 9 N SER A 309 34.922 18.403 54.502 1.00 57.61 N ANISOU 9 N SER A 309 6897 5110 9881 1217 1269 1924 N ATOM 10 CA SER A 309 34.025 18.351 53.361 1.00 58.81 C ANISOU 10 CA SER A 309 6736 5501 10107 1380 1096 2310 C ATOM 11 C SER A 309 33.907 17.004 52.696 1.00 53.28 C ANISOU 11 C SER A 309 5904 5210 9132 1256 749 2439 C ATOM 12 O SER A 309 32.934 16.708 52.045 1.00 55.13 O ANISOU 12 O SER A 309 5889 5716 9342 1321 546 2710 O ATOM 13 CB SER A 309 34.532 19.343 52.312 1.00 62.95 C ANISOU 13 CB SER A 309 7284 5890 10746 1465 1097 2565 C ATOM 14 N LEU A 310 34.923 16.189 52.859 1.00 50.95 N ANISOU 14 N LEU A 310 5790 4965 8603 1053 670 2227 N ATOM 15 CA LEU A 310 34.982 14.951 52.146 1.00 46.45 C ANISOU 15 CA LEU A 310 5135 4782 7733 928 339 2299 C ATOM 16 C LEU A 310 33.901 13.998 52.596 1.00 44.35 C ANISOU 16 C LEU A 310 4617 4736 7499 974 222 2297 C ATOM 17 O LEU A 310 33.567 13.925 53.738 1.00 45.54 O ANISOU 17 O LEU A 310 4760 4743 7801 1005 426 2083 O ATOM 18 CB LEU A 310 36.369 14.340 52.285 1.00 43.21 C ANISOU 18 CB LEU A 310 4982 4395 7040 675 308 1999 C ATOM 19 N THR A 311 33.351 13.292 51.644 1.00 39.16 N ANISOU 19 N THR A 311 3780 4459 6641 922 -97 2467 N ATOM 20 CA THR A 311 32.409 12.214 51.918 1.00 38.03 C ANISOU 20 CA THR A 311 3424 4570 6455 868 -266 2427 C ATOM 21 C THR A 311 33.181 10.967 52.327 1.00 33.93 C ANISOU 21 C THR A 311 3053 4185 5654 648 -419 2124 C ATOM 22 O THR A 311 34.406 10.918 52.197 1.00 31.42 O ANISOU 22 O THR A 311 3003 3823 5112 516 -404 1925 O ATOM 23 CB THR A 311 31.527 11.872 50.704 1.00 40.19 C ANISOU 23 CB THR A 311 3538 5167 6565 807 -552 2624 C ATOM 24 OG1 THR A 311 32.321 11.213 49.707 1.00 38.73 O ANISOU 24 OG1 THR A 311 3539 5198 5979 626 -806 2532 O ATOM 25 CG2 THR A 311 30.886 13.128 50.120 1.00 42.27 C ANISOU 25 CG2 THR A 311 3676 5325 7060 990 -440 2928 C ATOM 26 N ALA A 312 32.461 9.959 52.806 1.00 35.39 N ANISOU 26 N ALA A 312 3083 4549 5813 562 -546 2032 N ATOM 27 CA ALA A 312 33.081 8.700 53.201 1.00 34.84 C ANISOU 27 CA ALA A 312 3182 4609 5446 309 -690 1681 C ATOM 28 C ALA A 312 33.794 8.034 52.024 1.00 32.53 C ANISOU 28 C ALA A 312 3044 4543 4774 170 -1005 1661 C ATOM 29 O ALA A 312 34.937 7.596 52.152 1.00 29.54 O ANISOU 29 O ALA A 312 2912 4145 4165 38 -1000 1385 O ATOM 30 CB ALA A 312 32.039 7.761 53.788 1.00 36.79 C ANISOU 30 CB ALA A 312 3207 5015 5758 235 -806 1667 C ATOM 31 N ASP A 313 33.117 7.961 50.879 1.00 30.52 N ANISOU 31 N ASP A 313 2751 4445 4400 167 -1137 1780 N ATOM 32 CA ASP A 313 33.693 7.326 49.693 1.00 33.83 C ANISOU 32 CA ASP A 313 3389 5017 4447 58 -1301 1632 C ATOM 33 C ASP A 313 34.909 8.095 49.182 1.00 32.55 C ANISOU 33 C ASP A 313 3382 4806 4178 108 -1217 1687 C ATOM 34 O ASP A 313 35.881 7.497 48.717 1.00 31.26 O ANISOU 34 O ASP A 313 3433 4717 3726 25 -1259 1465 O ATOM 35 CB ASP A 313 32.649 7.198 48.578 1.00 39.70 C ANISOU 35 CB ASP A 313 4040 5909 5134 63 -1459 1785 C ATOM 36 CG ASP A 313 31.699 6.032 48.797 1.00 43.89 C ANISOU 36 CG ASP A 313 4517 6518 5642 -49 -1586 1656 C ATOM 37 OD1 ASP A 313 32.141 4.987 49.325 1.00 43.05 O ANISOU 37 OD1 ASP A 313 4562 6382 5411 -149 -1586 1349 O ATOM 38 OD2 ASP A 313 30.507 6.166 48.443 1.00 46.15 O ANISOU 38 OD2 ASP A 313 4605 6884 6047 -35 -1673 1878 O ATOM 39 N GLN A 314 34.852 9.420 49.274 1.00 31.59 N ANISOU 39 N GLN A 314 3160 4524 4317 263 -1053 1975 N ATOM 40 CA GLN A 314 35.982 10.255 48.873 1.00 31.87 C ANISOU 40 CA GLN A 314 3351 4462 4295 297 -930 2062 C ATOM 41 C GLN A 314 37.165 10.070 49.814 1.00 30.69 C ANISOU 41 C GLN A 314 3382 4167 4112 206 -792 1821 C ATOM 42 O GLN A 314 38.319 10.076 49.384 1.00 25.99 O ANISOU 42 O GLN A 314 2962 3617 3294 127 -764 1742 O ATOM 43 CB GLN A 314 35.578 11.729 48.834 1.00 34.87 C ANISOU 43 CB GLN A 314 3626 4608 5015 480 -729 2368 C ATOM 44 CG GLN A 314 34.736 12.122 47.633 1.00 37.68 C ANISOU 44 CG GLN A 314 3855 5117 5344 537 -853 2608 C ATOM 45 CD GLN A 314 34.127 13.496 47.798 1.00 39.59 C ANISOU 45 CD GLN A 314 3959 5109 5974 729 -653 2878 C ATOM 46 OE1 GLN A 314 33.826 13.918 48.913 1.00 43.06 O ANISOU 46 OE1 GLN A 314 4339 5287 6735 842 -433 2842 O ATOM 47 NE2 GLN A 314 33.950 14.206 46.691 1.00 46.58 N ANISOU 47 NE2 GLN A 314 4812 6058 6829 774 -711 3126 N ATOM 48 N MET A 315 36.869 9.914 51.102 1.00 29.82 N ANISOU 48 N MET A 315 3247 3877 4208 187 -641 1601 N ATOM 49 CA MET A 315 37.895 9.685 52.114 1.00 27.80 C ANISOU 49 CA MET A 315 3185 3468 3909 48 -474 1240 C ATOM 50 C MET A 315 38.638 8.375 51.843 1.00 23.44 C ANISOU 50 C MET A 315 2750 3157 2999 -113 -685 1003 C ATOM 51 O MET A 315 39.870 8.339 51.845 1.00 22.52 O ANISOU 51 O MET A 315 2795 3024 2736 -201 -616 852 O ATOM 52 CB MET A 315 37.272 9.674 53.515 1.00 29.97 C ANISOU 52 CB MET A 315 3407 3553 4427 55 -298 1070 C ATOM 53 CG MET A 315 38.225 9.264 54.635 1.00 29.87 C ANISOU 53 CG MET A 315 3590 3428 4332 -121 -182 699 C ATOM 54 SD MET A 315 39.581 10.432 54.876 1.00 37.41 S ANISOU 54 SD MET A 315 4771 4098 5344 -180 65 632 S ATOM 55 CE MET A 315 38.699 11.862 55.476 1.00 38.15 C ANISOU 55 CE MET A 315 4832 3822 5843 10 370 767 C ATOM 56 N VAL A 316 37.880 7.310 51.594 1.00 23.85 N ANISOU 56 N VAL A 316 2712 3422 2926 -149 -944 985 N ATOM 57 CA VAL A 316 38.450 6.001 51.279 1.00 27.07 C ANISOU 57 CA VAL A 316 3262 3988 3036 -256 -1085 704 C ATOM 58 C VAL A 316 39.334 6.062 50.037 1.00 28.36 C ANISOU 58 C VAL A 316 3554 4254 2970 -201 -1059 698 C ATOM 59 O VAL A 316 40.462 5.558 50.048 1.00 22.97 O ANISOU 59 O VAL A 316 3001 3567 2160 -219 -975 470 O ATOM 60 CB VAL A 316 37.352 4.933 51.057 1.00 29.44 C ANISOU 60 CB VAL A 316 3502 4353 3331 -237 -1161 590 C ATOM 61 CG1 VAL A 316 37.955 3.638 50.547 1.00 27.94 C ANISOU 61 CG1 VAL A 316 3457 4202 2959 -194 -1125 284 C ATOM 62 CG2 VAL A 316 36.592 4.683 52.336 1.00 28.86 C ANISOU 62 CG2 VAL A 316 3312 4201 3451 -303 -1148 558 C ATOM 63 N SER A 317 38.819 6.679 48.974 1.00 26.29 N ANISOU 63 N SER A 317 3229 4074 2685 -113 -1113 957 N ATOM 64 CA SER A 317 39.572 6.818 47.729 1.00 29.28 C ANISOU 64 CA SER A 317 3725 4560 2839 -64 -1098 984 C ATOM 65 C SER A 317 40.868 7.590 47.944 1.00 28.49 C ANISOU 65 C SER A 317 3698 4422 2706 -101 -941 1063 C ATOM 66 O SER A 317 41.917 7.200 47.433 1.00 30.54 O ANISOU 66 O SER A 317 4079 4756 2771 -102 -884 911 O ATOM 67 CB SER A 317 38.730 7.516 46.661 1.00 33.43 C ANISOU 67 CB SER A 317 4164 5163 3374 12 -1178 1284 C ATOM 68 OG SER A 317 37.487 6.858 46.505 1.00 38.15 O ANISOU 68 OG SER A 317 4678 5806 4012 15 -1328 1246 O ATOM 69 N ALA A 318 40.784 8.687 48.690 1.00 28.05 N ANISOU 69 N ALA A 318 3571 4202 2886 -106 -840 1319 N ATOM 70 CA ALA A 318 41.964 9.475 49.028 1.00 28.38 C ANISOU 70 CA ALA A 318 3702 4070 3010 -156 -589 1291 C ATOM 71 C ALA A 318 43.021 8.606 49.702 1.00 22.58 C ANISOU 71 C ALA A 318 3074 3360 2144 -283 -557 938 C ATOM 72 O ALA A 318 44.185 8.607 49.300 1.00 20.35 O ANISOU 72 O ALA A 318 2861 3178 1694 -328 -484 917 O ATOM 73 CB ALA A 318 41.588 10.642 49.928 1.00 29.45 C ANISOU 73 CB ALA A 318 3796 3841 3551 -120 -372 1373 C ATOM 74 N LEU A 319 42.609 7.856 50.717 1.00 21.59 N ANISOU 74 N LEU A 319 2944 3160 2101 -337 -610 689 N ATOM 75 CA LEU A 319 43.545 7.039 51.478 1.00 21.78 C ANISOU 75 CA LEU A 319 3055 3181 2038 -456 -595 379 C ATOM 76 C LEU A 319 44.105 5.885 50.645 1.00 21.44 C ANISOU 76 C LEU A 319 3030 3316 1801 -355 -652 217 C ATOM 77 O LEU A 319 45.299 5.590 50.716 1.00 20.95 O ANISOU 77 O LEU A 319 2996 3254 1710 -352 -555 96 O ATOM 78 CB LEU A 319 42.878 6.506 52.747 1.00 20.03 C ANISOU 78 CB LEU A 319 2815 2824 1973 -522 -622 178 C ATOM 79 CG LEU A 319 42.428 7.565 53.755 1.00 20.62 C ANISOU 79 CG LEU A 319 2864 2608 2364 -528 -411 214 C ATOM 80 CD1 LEU A 319 41.983 6.913 55.053 1.00 22.05 C ANISOU 80 CD1 LEU A 319 3048 2704 2625 -615 -415 -14 C ATOM 81 CD2 LEU A 319 43.539 8.574 54.013 1.00 24.20 C ANISOU 81 CD2 LEU A 319 3409 2885 2903 -602 -205 225 C ATOM 82 N LEU A 320 43.253 5.236 49.856 1.00 20.80 N ANISOU 82 N LEU A 320 2918 3300 1684 -215 -752 202 N ATOM 83 CA LEU A 320 43.726 4.152 48.999 1.00 22.68 C ANISOU 83 CA LEU A 320 3221 3578 1817 -46 -769 33 C ATOM 84 C LEU A 320 44.742 4.675 47.980 1.00 23.95 C ANISOU 84 C LEU A 320 3486 3833 1780 -39 -718 153 C ATOM 85 O LEU A 320 45.765 4.036 47.725 1.00 23.18 O ANISOU 85 O LEU A 320 3486 3704 1618 12 -676 35 O ATOM 86 CB LEU A 320 42.554 3.467 48.290 1.00 23.69 C ANISOU 86 CB LEU A 320 3333 3778 1890 3 -915 32 C ATOM 87 CG LEU A 320 41.675 2.567 49.165 1.00 23.60 C ANISOU 87 CG LEU A 320 3220 3722 2023 -75 -943 -71 C ATOM 88 CD1 LEU A 320 40.455 2.080 48.401 1.00 24.37 C ANISOU 88 CD1 LEU A 320 3294 3910 2057 -71 -1099 -17 C ATOM 89 CD2 LEU A 320 42.455 1.378 49.729 1.00 24.11 C ANISOU 89 CD2 LEU A 320 3291 3739 2129 -108 -869 -246 C ATOM 90 N ASP A 321 44.459 5.844 47.412 1.00 22.65 N ANISOU 90 N ASP A 321 3288 3777 1543 -94 -708 438 N ATOM 91 CA ASP A 321 45.346 6.470 46.431 1.00 28.96 C ANISOU 91 CA ASP A 321 4129 4705 2171 -88 -610 608 C ATOM 92 C ASP A 321 46.722 6.808 46.998 1.00 25.87 C ANISOU 92 C ASP A 321 3711 4327 1792 -174 -435 596 C ATOM 93 O ASP A 321 47.721 6.766 46.278 1.00 24.94 O ANISOU 93 O ASP A 321 3623 4320 1534 -146 -338 614 O ATOM 94 CB ASP A 321 44.712 7.750 45.880 1.00 34.03 C ANISOU 94 CB ASP A 321 4699 5398 2834 -96 -608 975 C ATOM 95 CG ASP A 321 43.752 7.486 44.738 1.00 43.12 C ANISOU 95 CG ASP A 321 5885 6627 3873 -10 -766 1031 C ATOM 96 OD1 ASP A 321 43.541 6.304 44.390 1.00 43.96 O ANISOU 96 OD1 ASP A 321 6101 6726 3875 43 -880 784 O ATOM 97 OD2 ASP A 321 43.202 8.466 44.191 1.00 48.52 O ANISOU 97 OD2 ASP A 321 6498 7342 4597 7 -779 1337 O ATOM 98 N ALA A 322 46.757 7.154 48.283 1.00 20.81 N ANISOU 98 N ALA A 322 2515 3452 1938 482 -456 81 N ATOM 99 CA ALA A 322 47.972 7.645 48.932 1.00 21.41 C ANISOU 99 CA ALA A 322 2601 3444 2092 533 -450 -17 C ATOM 100 C ALA A 322 48.914 6.532 49.382 1.00 21.69 C ANISOU 100 C ALA A 322 2628 3502 2109 467 -346 -8 C ATOM 101 O ALA A 322 50.022 6.809 49.847 1.00 21.59 O ANISOU 101 O ALA A 322 2613 3388 2203 496 -365 -94 O ATOM 102 CB ALA A 322 47.606 8.518 50.129 1.00 20.67 C ANISOU 102 CB ALA A 322 2424 3444 1983 776 -567 -163 C ATOM 103 N GLU A 323 48.474 5.284 49.247 1.00 20.49 N ANISOU 103 N GLU A 323 2451 3448 1887 381 -275 91 N ATOM 104 CA GLU A 323 49.220 4.138 49.773 1.00 18.43 C ANISOU 104 CA GLU A 323 2164 3219 1618 332 -186 115 C ATOM 105 C GLU A 323 50.636 4.061 49.215 1.00 18.03 C ANISOU 105 C GLU A 323 2222 3000 1630 241 -138 76 C ATOM 106 O GLU A 323 50.830 4.170 48.007 1.00 17.75 O ANISOU 106 O GLU A 323 2297 2854 1593 176 -115 123 O ATOM 107 CB GLU A 323 48.474 2.836 49.468 1.00 20.19 C ANISOU 107 CB GLU A 323 2322 3482 1869 227 -177 246 C ATOM 108 CG GLU A 323 47.442 2.470 50.520 1.00 21.81 C ANISOU 108 CG GLU A 323 2309 3880 2098 329 -128 396 C ATOM 109 CD GLU A 323 48.089 2.187 51.859 1.00 26.03 C ANISOU 109 CD GLU A 323 2788 4566 2535 483 -9 416 C ATOM 110 OE1 GLU A 323 48.544 1.041 52.082 1.00 28.56 O ANISOU 110 OE1 GLU A 323 3069 4870 2913 403 56 511 O ATOM 111 OE2 GLU A 323 48.164 3.116 52.693 1.00 25.68 O ANISOU 111 OE2 GLU A 323 2757 4649 2350 722 -15 314 O ATOM 112 N PRO A 324 51.627 3.889 50.100 1.00 15.95 N ANISOU 112 N PRO A 324 1920 2729 1412 284 -116 8 N ATOM 113 CA PRO A 324 53.017 3.742 49.672 1.00 18.13 C ANISOU 113 CA PRO A 324 2238 2842 1809 202 -53 4 C ATOM 114 C PRO A 324 53.265 2.379 49.052 1.00 19.33 C ANISOU 114 C PRO A 324 2458 3006 1879 96 46 78 C ATOM 115 O PRO A 324 52.519 1.435 49.310 1.00 19.13 O ANISOU 115 O PRO A 324 2405 3083 1779 74 26 111 O ATOM 116 CB PRO A 324 53.802 3.896 50.977 1.00 19.00 C ANISOU 116 CB PRO A 324 2269 2948 2002 317 -133 -132 C ATOM 117 CG PRO A 324 52.855 3.445 52.016 1.00 18.41 C ANISOU 117 CG PRO A 324 2155 3118 1722 464 -147 -139 C ATOM 118 CD PRO A 324 51.509 3.892 51.568 1.00 16.48 C ANISOU 118 CD PRO A 324 1901 2954 1406 473 -156 -67 C ATOM 119 N PRO A 325 54.312 2.273 48.234 1.00 20.97 N ANISOU 119 N PRO A 325 2731 3095 2140 58 148 124 N ATOM 120 CA PRO A 325 54.668 0.980 47.650 1.00 22.51 C ANISOU 120 CA PRO A 325 3018 3298 2236 24 210 144 C ATOM 121 C PRO A 325 55.275 0.018 48.655 1.00 22.56 C ANISOU 121 C PRO A 325 2951 3329 2291 -12 213 94 C ATOM 122 O PRO A 325 55.723 0.434 49.725 1.00 20.54 O ANISOU 122 O PRO A 325 2594 3078 2133 23 188 39 O ATOM 123 CB PRO A 325 55.701 1.353 46.596 1.00 23.09 C ANISOU 123 CB PRO A 325 3161 3279 2333 76 369 249 C ATOM 124 CG PRO A 325 56.284 2.637 47.073 1.00 23.75 C ANISOU 124 CG PRO A 325 3094 3244 2688 68 387 296 C ATOM 125 CD PRO A 325 55.157 3.366 47.730 1.00 21.00 C ANISOU 125 CD PRO A 325 2704 2942 2331 77 216 202 C ATOM 126 N ILE A 326 55.284 -1.262 48.305 1.00 20.07 N ANISOU 126 N ILE A 326 2698 3013 1915 -44 202 92 N ATOM 127 CA ILE A 326 56.026 -2.250 49.068 1.00 22.30 C ANISOU 127 CA ILE A 326 2928 3292 2254 -73 222 70 C ATOM 128 C ILE A 326 57.459 -2.290 48.551 1.00 22.32 C ANISOU 128 C ILE A 326 2977 3206 2296 -48 347 60 C ATOM 129 O ILE A 326 57.699 -2.569 47.378 1.00 20.62 O ANISOU 129 O ILE A 326 2891 2963 1979 14 406 79 O ATOM 130 CB ILE A 326 55.385 -3.642 48.977 1.00 26.35 C ANISOU 130 CB ILE A 326 3444 3791 2779 -124 115 89 C ATOM 131 CG1 ILE A 326 53.989 -3.607 49.600 1.00 28.91 C ANISOU 131 CG1 ILE A 326 3628 4193 3164 -147 35 192 C ATOM 132 CG2 ILE A 326 56.251 -4.676 49.684 1.00 25.47 C ANISOU 132 CG2 ILE A 326 3286 3655 2737 -146 145 88 C ATOM 133 CD1 ILE A 326 53.259 -4.935 49.558 1.00 33.93 C ANISOU 133 CD1 ILE A 326 4171 4742 3978 -222 -103 278 C ATOM 134 N LEU A 327 58.407 -1.985 49.428 1.00 19.29 N ANISOU 134 N LEU A 327 2483 2785 2060 -46 377 32 N ATOM 135 CA LEU A 327 59.808 -1.902 49.042 1.00 18.42 C ANISOU 135 CA LEU A 327 2337 2566 2095 -28 504 68 C ATOM 136 C LEU A 327 60.524 -3.235 49.217 1.00 17.93 C ANISOU 136 C LEU A 327 2301 2502 2010 -33 526 25 C ATOM 137 O LEU A 327 60.066 -4.101 49.960 1.00 16.75 O ANISOU 137 O LEU A 327 2156 2409 1798 -63 423 -27 O ATOM 138 CB LEU A 327 60.517 -0.823 49.861 1.00 21.30 C ANISOU 138 CB LEU A 327 2529 2814 2750 -19 441 34 C ATOM 139 CG LEU A 327 59.909 0.579 49.820 1.00 21.28 C ANISOU 139 CG LEU A 327 2476 2761 2848 -1 363 48 C ATOM 140 CD1 LEU A 327 60.753 1.527 50.644 1.00 21.78 C ANISOU 140 CD1 LEU A 327 2352 2629 3294 35 200 -40 C ATOM 141 CD2 LEU A 327 59.797 1.075 48.385 1.00 21.09 C ANISOU 141 CD2 LEU A 327 2503 2705 2804 3 541 248 C ATOM 142 N TYR A 328 61.655 -3.394 48.536 1.00 16.46 N ANISOU 142 N TYR A 328 2108 2251 1896 17 682 88 N ATOM 143 CA TYR A 328 62.461 -4.591 48.713 1.00 16.97 C ANISOU 143 CA TYR A 328 2186 2299 1961 33 699 34 C ATOM 144 C TYR A 328 63.591 -4.335 49.698 1.00 16.67 C ANISOU 144 C TYR A 328 1962 2162 2209 5 683 6 C ATOM 145 O TYR A 328 64.068 -3.209 49.831 1.00 17.75 O ANISOU 145 O TYR A 328 1943 2191 2611 -1 695 60 O ATOM 146 CB TYR A 328 63.009 -5.074 47.369 1.00 21.87 C ANISOU 146 CB TYR A 328 2928 2942 2441 183 872 102 C ATOM 147 CG TYR A 328 62.001 -5.901 46.611 1.00 25.17 C ANISOU 147 CG TYR A 328 3571 3420 2572 263 739 3 C ATOM 148 CD1 TYR A 328 60.884 -5.311 46.032 1.00 25.62 C ANISOU 148 CD1 TYR A 328 3723 3522 2488 291 672 16 C ATOM 149 CD2 TYR A 328 62.151 -7.275 46.496 1.00 26.59 C ANISOU 149 CD2 TYR A 328 3854 3571 2678 320 620 -128 C ATOM 150 CE1 TYR A 328 59.952 -6.065 45.351 1.00 26.25 C ANISOU 150 CE1 TYR A 328 3986 3605 2382 379 464 -112 C ATOM 151 CE2 TYR A 328 61.226 -8.039 45.814 1.00 26.28 C ANISOU 151 CE2 TYR A 328 3994 3510 2481 407 394 -261 C ATOM 152 CZ TYR A 328 60.127 -7.429 45.244 1.00 26.29 C ANISOU 152 CZ TYR A 328 4077 3543 2367 439 303 -260 C ATOM 153 OH TYR A 328 59.200 -8.185 44.566 1.00 27.84 O ANISOU 153 OH TYR A 328 4431 3669 2478 541 -3 -426 O ATOM 154 N SER A 329 64.005 -5.377 50.407 1.00 17.61 N ANISOU 154 N SER A 329 2084 2284 2323 -3 609 -84 N ATOM 155 CA SER A 329 65.145 -5.235 51.297 1.00 19.20 C ANISOU 155 CA SER A 329 2125 2381 2790 9 551 -143 C ATOM 156 C SER A 329 66.431 -5.418 50.515 1.00 20.20 C ANISOU 156 C SER A 329 2159 2410 3104 46 741 -44 C ATOM 157 O SER A 329 66.421 -5.834 49.353 1.00 20.58 O ANISOU 157 O SER A 329 2316 2523 2980 116 927 54 O ATOM 158 CB SER A 329 65.083 -6.241 52.449 1.00 21.09 C ANISOU 158 CB SER A 329 2403 2679 2932 29 403 -249 C ATOM 159 OG SER A 329 65.439 -7.539 52.013 1.00 20.58 O ANISOU 159 OG SER A 329 2415 2612 2792 22 469 -236 O ATOM 160 N GLU A 330 67.550 -5.110 51.152 1.00 18.35 N ANISOU 160 N GLU A 330 1719 2024 3229 47 679 -72 N ATOM 161 CA GLU A 330 68.839 -5.358 50.528 1.00 26.04 C ANISOU 161 CA GLU A 330 2544 2905 4443 93 881 64 C ATOM 162 C GLU A 330 69.378 -6.737 50.918 1.00 26.54 C ANISOU 162 C GLU A 330 2684 3006 4396 129 841 -57 C ATOM 163 O GLU A 330 70.593 -6.929 51.046 1.00 26.44 O ANISOU 163 O GLU A 330 2491 2877 4680 161 883 -29 O ATOM 164 CB GLU A 330 69.827 -4.250 50.895 1.00 34.29 C ANISOU 164 CB GLU A 330 3250 3695 6083 64 814 138 C ATOM 165 CG GLU A 330 69.982 -3.218 49.780 1.00 44.40 C ANISOU 165 CG GLU A 330 4360 4901 7609 75 1080 466 C ATOM 166 CD GLU A 330 70.341 -1.831 50.283 1.00 54.72 C ANISOU 166 CD GLU A 330 5347 5903 9543 1 874 507 C ATOM 167 OE1 GLU A 330 70.816 -1.709 51.432 1.00 57.91 O ANISOU 167 OE1 GLU A 330 5623 6118 10262 -18 517 261 O ATOM 168 OE2 GLU A 330 70.139 -0.858 49.521 1.00 59.60 O ANISOU 168 OE2 GLU A 330 5928 6451 10265 8 993 754 O ATOM 169 N TYR A 331 68.469 -7.698 51.086 1.00 26.20 N ANISOU 169 N TYR A 331 2874 3096 3986 121 749 -165 N ATOM 170 CA TYR A 331 68.855 -9.057 51.468 1.00 25.63 C ANISOU 170 CA TYR A 331 2875 3031 3832 149 681 -261 C ATOM 171 C TYR A 331 69.872 -9.658 50.504 1.00 25.31 C ANISOU 171 C TYR A 331 2819 2971 3827 264 885 -200 C ATOM 172 O TYR A 331 69.706 -9.600 49.285 1.00 26.51 O ANISOU 172 O TYR A 331 3066 3201 3806 379 1074 -105 O ATOM 173 CB TYR A 331 67.635 -9.977 51.553 1.00 23.44 C ANISOU 173 CB TYR A 331 2799 2844 3265 116 563 -307 C ATOM 174 CG TYR A 331 67.998 -11.427 51.804 1.00 27.08 C ANISOU 174 CG TYR A 331 3321 3265 3703 143 481 -371 C ATOM 175 CD1 TYR A 331 68.712 -11.796 52.937 1.00 29.58 C ANISOU 175 CD1 TYR A 331 3548 3538 4153 150 384 -415 C ATOM 176 CD2 TYR A 331 67.626 -12.427 50.911 1.00 27.41 C ANISOU 176 CD2 TYR A 331 3519 3290 3607 194 450 -410 C ATOM 177 CE1 TYR A 331 69.051 -13.122 53.175 1.00 29.64 C ANISOU 177 CE1 TYR A 331 3604 3492 4165 176 306 -450 C ATOM 178 CE2 TYR A 331 67.956 -13.756 51.144 1.00 29.99 C ANISOU 178 CE2 TYR A 331 3887 3530 3976 220 328 -477 C ATOM 179 CZ TYR A 331 68.670 -14.095 52.277 1.00 29.41 C ANISOU 179 CZ TYR A 331 3707 3422 4045 195 281 -474 C ATOM 180 OH TYR A 331 69.007 -15.409 52.521 1.00 29.36 O ANISOU 180 OH TYR A 331 3735 3317 4105 222 159 -517 O ATOM 181 N ASP A 332 70.923 -10.233 51.076 1.00 25.40 N ANISOU 181 N ASP A 332 2721 2899 4032 286 842 -257 N ATOM 182 CA ASP A 332 72.009 -10.836 50.316 1.00 26.89 C ANISOU 182 CA ASP A 332 2860 3077 4279 431 1040 -197 C ATOM 183 C ASP A 332 72.082 -12.325 50.629 1.00 28.76 C ANISOU 183 C ASP A 332 3251 3312 4364 470 891 -360 C ATOM 184 O ASP A 332 72.565 -12.718 51.692 1.00 26.30 O ANISOU 184 O ASP A 332 2860 2918 4216 414 726 -445 O ATOM 185 CB ASP A 332 73.331 -10.134 50.644 1.00 33.49 C ANISOU 185 CB ASP A 332 3356 3763 5607 426 1118 -90 C ATOM 186 CG ASP A 332 74.538 -10.774 49.968 1.00 42.84 C ANISOU 186 CG ASP A 332 4433 4949 6896 599 1356 15 C ATOM 187 OD1 ASP A 332 74.370 -11.645 49.086 1.00 45.83 O ANISOU 187 OD1 ASP A 332 5034 5472 6908 781 1486 -4 O ATOM 188 OD2 ASP A 332 75.672 -10.382 50.319 1.00 45.31 O ANISOU 188 OD2 ASP A 332 4438 5106 7674 578 1375 109 O ATOM 189 N PRO A 333 71.609 -13.162 49.698 1.00 29.12 N ANISOU 189 N PRO A 333 3524 3429 4113 599 908 -415 N ATOM 190 CA PRO A 333 71.529 -14.593 49.999 1.00 30.26 C ANISOU 190 CA PRO A 333 3802 3507 4186 619 694 -573 C ATOM 191 C PRO A 333 72.877 -15.314 49.934 1.00 30.48 C ANISOU 191 C PRO A 333 3757 3491 4335 767 770 -614 C ATOM 192 O PRO A 333 72.896 -16.532 50.071 1.00 23.82 O ANISOU 192 O PRO A 333 3027 2572 3453 813 588 -749 O ATOM 193 CB PRO A 333 70.576 -15.122 48.920 1.00 30.50 C ANISOU 193 CB PRO A 333 4086 3574 3930 749 606 -663 C ATOM 194 CG PRO A 333 70.780 -14.199 47.760 1.00 34.05 C ANISOU 194 CG PRO A 333 4555 4167 4217 946 894 -549 C ATOM 195 CD PRO A 333 71.120 -12.844 48.342 1.00 32.18 C ANISOU 195 CD PRO A 333 4060 3935 4233 774 1070 -353 C ATOM 196 N THR A 334 73.981 -14.594 49.744 1.00 24.72 N ANISOU 196 N THR A 334 2804 2775 3812 839 1021 -479 N ATOM 197 CA THR A 334 75.282 -15.253 49.622 1.00 26.61 C ANISOU 197 CA THR A 334 2935 2981 4193 1003 1125 -487 C ATOM 198 C THR A 334 75.922 -15.552 50.975 1.00 25.77 C ANISOU 198 C THR A 334 2671 2725 4394 851 917 -569 C ATOM 199 O THR A 334 76.879 -16.323 51.053 1.00 27.03 O ANISOU 199 O THR A 334 2770 2832 4668 962 920 -623 O ATOM 200 CB THR A 334 76.280 -14.412 48.796 1.00 29.80 C ANISOU 200 CB THR A 334 3095 3451 4778 1178 1523 -226 C ATOM 201 OG1 THR A 334 76.582 -13.197 49.497 1.00 28.89 O ANISOU 201 OG1 THR A 334 2672 3212 5093 961 1518 -81 O ATOM 202 CG2 THR A 334 75.707 -14.094 47.417 1.00 32.95 C ANISOU 202 CG2 THR A 334 3686 4054 4781 1381 1712 -108 C ATOM 203 N ARG A 335 75.392 -14.945 52.032 1.00 24.00 N ANISOU 203 N ARG A 335 2399 2451 4270 653 725 -589 N ATOM 204 CA ARG A 335 75.973 -15.090 53.367 1.00 27.89 C ANISOU 204 CA ARG A 335 2770 2829 4996 593 496 -681 C ATOM 205 C ARG A 335 74.915 -15.391 54.426 1.00 23.12 C ANISOU 205 C ARG A 335 2334 2262 4189 507 245 -744 C ATOM 206 O ARG A 335 73.763 -14.982 54.292 1.00 21.91 O ANISOU 206 O ARG A 335 2290 2195 3841 435 250 -692 O ATOM 207 CB ARG A 335 76.743 -13.821 53.749 1.00 30.28 C ANISOU 207 CB ARG A 335 2766 3018 5721 559 494 -629 C ATOM 208 N PRO A 336 75.305 -16.121 55.486 1.00 26.38 N ANISOU 208 N PRO A 336 2754 2623 4647 546 47 -818 N ATOM 209 CA PRO A 336 74.391 -16.371 56.609 1.00 25.51 C ANISOU 209 CA PRO A 336 2766 2585 4343 541 -134 -790 C ATOM 210 C PRO A 336 74.071 -15.077 57.347 1.00 23.45 C ANISOU 210 C PRO A 336 2447 2384 4079 570 -228 -818 C ATOM 211 O PRO A 336 74.821 -14.109 57.215 1.00 22.10 O ANISOU 211 O PRO A 336 2102 2118 4178 579 -243 -898 O ATOM 212 CB PRO A 336 75.168 -17.338 57.518 1.00 28.83 C ANISOU 212 CB PRO A 336 3183 2937 4833 647 -296 -842 C ATOM 213 CG PRO A 336 76.547 -17.431 56.970 1.00 32.09 C ANISOU 213 CG PRO A 336 3443 3225 5526 686 -237 -943 C ATOM 214 CD PRO A 336 76.664 -16.614 55.733 1.00 30.12 C ANISOU 214 CD PRO A 336 3092 2981 5370 636 3 -897 C ATOM 215 N PHE A 337 72.961 -15.056 58.080 1.00 20.81 N ANISOU 215 N PHE A 337 2233 2190 3486 608 -293 -734 N ATOM 216 CA PHE A 337 72.610 -13.915 58.915 1.00 21.13 C ANISOU 216 CA PHE A 337 2262 2316 3449 729 -426 -799 C ATOM 217 C PHE A 337 73.513 -13.824 60.134 1.00 24.94 C ANISOU 217 C PHE A 337 2713 2762 4001 969 -697 -973 C ATOM 218 O PHE A 337 73.917 -14.840 60.704 1.00 27.71 O ANISOU 218 O PHE A 337 3117 3119 4293 1071 -758 -947 O ATOM 219 CB PHE A 337 71.155 -14.005 59.394 1.00 29.42 C ANISOU 219 CB PHE A 337 3442 3573 4165 776 -379 -616 C ATOM 220 CG PHE A 337 70.132 -13.673 58.342 1.00 29.37 C ANISOU 220 CG PHE A 337 3452 3595 4112 582 -206 -505 C ATOM 221 CD1 PHE A 337 70.011 -12.381 57.856 1.00 30.25 C ANISOU 221 CD1 PHE A 337 3510 3693 4290 534 -186 -592 C ATOM 222 CD2 PHE A 337 69.258 -14.643 57.880 1.00 27.95 C ANISOU 222 CD2 PHE A 337 3329 3425 3867 464 -110 -313 C ATOM 223 CE1 PHE A 337 69.058 -12.072 56.898 1.00 29.28 C ANISOU 223 CE1 PHE A 337 3422 3607 4097 388 -41 -492 C ATOM 224 CE2 PHE A 337 68.303 -14.343 56.926 1.00 28.37 C ANISOU 224 CE2 PHE A 337 3405 3486 3889 320 -16 -249 C ATOM 225 CZ PHE A 337 68.201 -13.053 56.435 1.00 27.14 C ANISOU 225 CZ PHE A 337 3228 3360 3725 292 33 -339 C ATOM 226 N SER A 338 73.820 -12.598 60.536 1.00 23.94 N ANISOU 226 N SER A 338 2501 2571 4024 1083 -906 -1165 N ATOM 227 CA SER A 338 74.341 -12.352 61.869 1.00 26.17 C ANISOU 227 CA SER A 338 2840 2879 4226 1345 -1238 -1348 C ATOM 228 C SER A 338 73.374 -11.392 62.551 1.00 26.85 C ANISOU 228 C SER A 338 3057 3142 4003 1528 -1352 -1398 C ATOM 229 O SER A 338 72.453 -10.884 61.910 1.00 25.34 O ANISOU 229 O SER A 338 2848 3002 3779 1452 -1197 -1310 O ATOM 230 CB SER A 338 75.751 -11.773 61.823 1.00 27.99 C ANISOU 230 CB SER A 338 2881 2866 4887 1216 -1439 -1522 C ATOM 231 OG SER A 338 75.730 -10.444 61.337 1.00 28.41 O ANISOU 231 OG SER A 338 2786 2788 5219 1080 -1492 -1576 O ATOM 232 N GLU A 339 73.566 -11.149 63.843 1.00 18.80 N ANISOU 232 N GLU A 339 1069 2830 3243 391 140 90 N ATOM 233 CA GLU A 339 72.719 -10.191 64.542 1.00 19.77 C ANISOU 233 CA GLU A 339 1263 3045 3203 413 116 147 C ATOM 234 C GLU A 339 72.846 -8.824 63.881 1.00 16.40 C ANISOU 234 C GLU A 339 919 2635 2678 295 104 -16 C ATOM 235 O GLU A 339 71.850 -8.145 63.636 1.00 15.60 O ANISOU 235 O GLU A 339 914 2519 2494 249 117 -19 O ATOM 236 CB GLU A 339 73.094 -10.107 66.021 1.00 19.80 C ANISOU 236 CB GLU A 339 1236 3216 3073 588 50 240 C ATOM 237 CG GLU A 339 72.416 -8.977 66.782 1.00 23.47 C ANISOU 237 CG GLU A 339 1810 3809 3300 675 -6 234 C ATOM 238 CD GLU A 339 72.781 -8.979 68.257 1.00 30.90 C ANISOU 238 CD GLU A 339 2771 4932 4036 940 -102 292 C ATOM 239 OE1 GLU A 339 73.927 -8.603 68.588 1.00 33.66 O ANISOU 239 OE1 GLU A 339 3081 5338 4370 980 -269 116 O ATOM 240 OE2 GLU A 339 71.928 -9.368 69.084 1.00 31.71 O ANISOU 240 OE2 GLU A 339 2958 5085 4005 1095 -9 507 O ATOM 241 N ALA A 340 74.080 -8.452 63.567 1.00 16.45 N ANISOU 241 N ALA A 340 854 2650 2745 251 95 -118 N ATOM 242 CA ALA A 340 74.359 -7.172 62.943 1.00 20.72 C ANISOU 242 CA ALA A 340 1407 3172 3294 148 112 -208 C ATOM 243 C ALA A 340 73.768 -7.090 61.543 1.00 19.45 C ANISOU 243 C ALA A 340 1344 2947 3101 93 246 -217 C ATOM 244 O ALA A 340 73.168 -6.079 61.180 1.00 18.50 O ANISOU 244 O ALA A 340 1301 2818 2909 34 264 -232 O ATOM 245 CB ALA A 340 75.861 -6.927 62.901 1.00 17.65 C ANISOU 245 CB ALA A 340 849 2765 3091 128 97 -250 C ATOM 246 N SER A 341 73.917 -8.152 60.756 1.00 16.24 N ANISOU 246 N SER A 341 943 2496 2731 148 315 -226 N ATOM 247 CA SER A 341 73.476 -8.083 59.365 1.00 20.77 C ANISOU 247 CA SER A 341 1634 3036 3221 181 404 -281 C ATOM 248 C SER A 341 71.944 -8.066 59.273 1.00 17.84 C ANISOU 248 C SER A 341 1389 2610 2779 166 320 -302 C ATOM 249 O SER A 341 71.387 -7.398 58.405 1.00 15.66 O ANISOU 249 O SER A 341 1228 2337 2387 171 355 -342 O ATOM 250 CB SER A 341 74.059 -9.234 58.537 1.00 20.41 C ANISOU 250 CB SER A 341 1582 2961 3213 314 453 -343 C ATOM 251 OG SER A 341 73.445 -10.472 58.828 1.00 20.99 O ANISOU 251 OG SER A 341 1653 2931 3391 357 324 -382 O ATOM 252 N MET A 342 71.255 -8.774 60.160 1.00 18.92 N ANISOU 252 N MET A 342 1485 2694 3008 166 224 -240 N ATOM 253 CA MET A 342 69.795 -8.715 60.129 1.00 17.38 C ANISOU 253 CA MET A 342 1354 2419 2829 147 158 -214 C ATOM 254 C MET A 342 69.300 -7.344 60.587 1.00 15.80 C ANISOU 254 C MET A 342 1217 2306 2479 78 181 -169 C ATOM 255 O MET A 342 68.401 -6.775 59.972 1.00 14.92 O ANISOU 255 O MET A 342 1202 2159 2309 49 169 -203 O ATOM 256 CB MET A 342 69.162 -9.809 60.981 1.00 14.77 C ANISOU 256 CB MET A 342 909 1988 2716 186 102 -72 C ATOM 257 CG MET A 342 67.634 -9.774 60.957 1.00 17.79 C ANISOU 257 CG MET A 342 1296 2249 3215 168 46 1 C ATOM 258 SD MET A 342 66.937 -11.156 61.871 1.00 64.23 S ANISOU 258 SD MET A 342 6985 7956 9464 228 31 259 S ATOM 259 CE MET A 342 67.241 -12.496 60.724 0.37 17.78 C ANISOU 259 CE MET A 342 1054 1825 3875 252 -131 50 C ATOM 260 N MET A 343 69.885 -6.809 61.657 1.00 14.69 N ANISOU 260 N MET A 343 1027 2273 2284 79 181 -119 N ATOM 261 CA MET A 343 69.518 -5.460 62.097 1.00 15.23 C ANISOU 261 CA MET A 343 1155 2404 2229 45 159 -131 C ATOM 262 C MET A 343 69.788 -4.448 60.993 1.00 14.80 C ANISOU 262 C MET A 343 1148 2322 2153 -42 215 -212 C ATOM 263 O MET A 343 69.010 -3.513 60.800 1.00 15.39 O ANISOU 263 O MET A 343 1303 2387 2158 -84 214 -216 O ATOM 264 CB MET A 343 70.270 -5.058 63.369 1.00 17.59 C ANISOU 264 CB MET A 343 1394 2807 2482 116 74 -143 C ATOM 265 CG MET A 343 69.667 -5.603 64.661 1.00 18.49 C ANISOU 265 CG MET A 343 1509 3014 2502 285 48 -8 C ATOM 266 SD MET A 343 67.903 -5.248 64.874 1.00 16.87 S ANISOU 266 SD MET A 343 1395 2809 2207 330 107 128 S ATOM 267 CE MET A 343 67.852 -3.453 64.767 1.00 17.09 C ANISOU 267 CE MET A 343 1527 2863 2104 268 21 -57 C ATOM 268 N GLY A 344 70.887 -4.646 60.269 1.00 14.57 N ANISOU 268 N GLY A 344 1058 2284 2194 -43 291 -238 N ATOM 269 CA GLY A 344 71.218 -3.803 59.135 1.00 17.32 C ANISOU 269 CA GLY A 344 1426 2619 2535 -66 415 -229 C ATOM 270 C GLY A 344 70.141 -3.813 58.062 1.00 17.27 C ANISOU 270 C GLY A 344 1582 2601 2381 -19 449 -249 C ATOM 271 O GLY A 344 69.734 -2.761 57.570 1.00 16.06 O ANISOU 271 O GLY A 344 1487 2447 2167 -46 503 -216 O ATOM 272 N LEU A 345 69.681 -5.005 57.698 1.00 13.60 N ANISOU 272 N LEU A 345 1174 2102 1891 67 387 -315 N ATOM 273 CA LEU A 345 68.613 -5.143 56.713 1.00 17.67 C ANISOU 273 CA LEU A 345 1834 2575 2302 148 329 -394 C ATOM 274 C LEU A 345 67.344 -4.443 57.158 1.00 16.67 C ANISOU 274 C LEU A 345 1753 2411 2171 55 253 -360 C ATOM 275 O LEU A 345 66.739 -3.693 56.395 1.00 14.73 O ANISOU 275 O LEU A 345 1616 2175 1806 79 267 -375 O ATOM 276 CB LEU A 345 68.292 -6.613 56.450 1.00 20.63 C ANISOU 276 CB LEU A 345 2212 2849 2776 251 186 -511 C ATOM 277 CG LEU A 345 69.312 -7.504 55.752 1.00 24.67 C ANISOU 277 CG LEU A 345 2725 3383 3267 412 223 -604 C ATOM 278 CD1 LEU A 345 68.644 -8.820 55.401 1.00 23.57 C ANISOU 278 CD1 LEU A 345 2599 3079 3278 523 -4 -776 C ATOM 279 CD2 LEU A 345 69.868 -6.822 54.513 1.00 27.69 C ANISOU 279 CD2 LEU A 345 3226 3900 3397 578 390 -610 C ATOM 280 N LEU A 346 66.934 -4.704 58.393 1.00 11.96 N ANISOU 280 N LEU A 346 1072 1784 1689 -12 190 -289 N ATOM 281 CA LEU A 346 65.669 -4.175 58.884 1.00 14.72 C ANISOU 281 CA LEU A 346 1449 2102 2043 -57 141 -227 C ATOM 282 C LEU A 346 65.695 -2.657 59.008 1.00 15.95 C ANISOU 282 C LEU A 346 1658 2329 2075 -120 200 -211 C ATOM 283 O LEU A 346 64.708 -1.987 58.686 1.00 14.36 O ANISOU 283 O LEU A 346 1533 2100 1825 -140 182 -204 O ATOM 284 CB LEU A 346 65.314 -4.804 60.233 1.00 14.52 C ANISOU 284 CB LEU A 346 1312 2068 2136 -38 121 -92 C ATOM 285 CG LEU A 346 65.080 -6.314 60.229 1.00 14.31 C ANISOU 285 CG LEU A 346 1178 1910 2352 14 60 -48 C ATOM 286 CD1 LEU A 346 64.764 -6.800 61.641 1.00 15.92 C ANISOU 286 CD1 LEU A 346 1253 2135 2662 76 112 183 C ATOM 287 CD2 LEU A 346 63.963 -6.691 59.268 1.00 16.89 C ANISOU 287 CD2 LEU A 346 1520 2056 2841 19 -68 -122 C ATOM 288 N THR A 347 66.822 -2.104 59.456 1.00 14.36 N ANISOU 288 N THR A 347 1393 2186 1876 -148 244 -213 N ATOM 289 CA THR A 347 66.895 -0.656 59.636 1.00 14.78 C ANISOU 289 CA THR A 347 1452 2245 1918 -208 253 -217 C ATOM 290 C THR A 347 67.102 0.066 58.303 1.00 15.37 C ANISOU 290 C THR A 347 1565 2294 1980 -225 370 -187 C ATOM 291 O THR A 347 66.632 1.191 58.131 1.00 14.64 O ANISOU 291 O THR A 347 1507 2171 1884 -267 385 -161 O ATOM 292 CB THR A 347 68.011 -0.233 60.629 1.00 16.55 C ANISOU 292 CB THR A 347 1556 2487 2244 -216 188 -259 C ATOM 293 OG1 THR A 347 69.273 -0.770 60.214 1.00 17.00 O ANISOU 293 OG1 THR A 347 1508 2538 2415 -218 252 -251 O ATOM 294 CG2 THR A 347 67.692 -0.710 62.042 1.00 16.46 C ANISOU 294 CG2 THR A 347 1547 2552 2156 -116 77 -270 C ATOM 295 N ASN A 348 67.798 -0.576 57.366 1.00 15.61 N ANISOU 295 N ASN A 348 1591 2348 1990 -152 471 -172 N ATOM 296 CA ASN A 348 67.926 -0.036 56.014 1.00 16.43 C ANISOU 296 CA ASN A 348 1757 2478 2007 -68 626 -97 C ATOM 297 C ASN A 348 66.557 0.041 55.337 1.00 16.04 C ANISOU 297 C ASN A 348 1883 2430 1780 -5 561 -142 C ATOM 298 O ASN A 348 66.238 1.027 54.669 1.00 16.94 O ANISOU 298 O ASN A 348 2056 2556 1826 23 647 -60 O ATOM 299 CB ASN A 348 68.881 -0.883 55.165 1.00 19.81 C ANISOU 299 CB ASN A 348 2177 2970 2381 86 752 -79 C ATOM 300 CG ASN A 348 68.920 -0.439 53.708 1.00 25.86 C ANISOU 300 CG ASN A 348 3046 3818 2960 284 941 26 C ATOM 301 OD1 ASN A 348 68.108 -0.877 52.889 1.00 28.28 O ANISOU 301 OD1 ASN A 348 3540 4174 3031 453 868 -79 O ATOM 302 ND2 ASN A 348 69.869 0.433 53.379 1.00 29.57 N ANISOU 302 ND2 ASN A 348 3379 4294 3562 295 1172 244 N ATOM 303 N LEU A 349 65.759 -1.010 55.514 1.00 15.73 N ANISOU 303 N LEU A 349 1898 2355 1722 25 398 -258 N ATOM 304 CA LEU A 349 64.389 -1.036 55.011 1.00 15.73 C ANISOU 304 CA LEU A 349 2018 2309 1652 72 269 -324 C ATOM 305 C LEU A 349 63.544 0.062 55.644 1.00 13.34 C ANISOU 305 C LEU A 349 1710 1975 1385 -54 258 -251 C ATOM 306 O LEU A 349 62.883 0.816 54.942 1.00 12.64 O ANISOU 306 O LEU A 349 1716 1888 1197 -18 265 -234 O ATOM 307 CB LEU A 349 63.741 -2.398 55.269 1.00 15.08 C ANISOU 307 CB LEU A 349 1903 2119 1708 100 76 -432 C ATOM 308 CG LEU A 349 62.305 -2.582 54.782 1.00 16.42 C ANISOU 308 CG LEU A 349 2134 2175 1930 148 -119 -516 C ATOM 309 CD1 LEU A 349 62.236 -2.458 53.267 1.00 16.55 C ANISOU 309 CD1 LEU A 349 2329 2246 1713 365 -175 -654 C ATOM 310 CD2 LEU A 349 61.769 -3.928 55.239 1.00 19.49 C ANISOU 310 CD2 LEU A 349 2394 2388 2623 142 -303 -566 C ATOM 311 N ALA A 350 63.544 0.145 56.963 1.00 12.03 N ANISOU 311 N ALA A 350 1444 1794 1333 -159 238 -212 N ATOM 312 CA ALA A 350 62.792 1.186 57.670 1.00 15.42 C ANISOU 312 CA ALA A 350 1878 2208 1772 -227 219 -166 C ATOM 313 C ALA A 350 63.101 2.590 57.164 1.00 14.91 C ANISOU 313 C ALA A 350 1838 2146 1682 -265 306 -130 C ATOM 314 O ALA A 350 62.266 3.389 57.001 1.00 12.35 O ANISOU 314 O ALA A 350 1574 1792 1327 -282 294 -104 O ATOM 315 CB ALA A 350 63.037 1.114 59.171 1.00 14.55 C ANISOU 315 CB ALA A 350 1682 2133 1715 -236 189 -146 C ATOM 316 N ASP A 351 64.390 2.835 57.005 1.00 13.56 N ANISOU 316 N ASP A 351 1588 1987 1577 -274 404 -98 N ATOM 317 CA ASP A 351 64.844 4.109 56.539 1.00 16.35 C ANISOU 317 CA ASP A 351 1889 2292 2033 -312 509 -3 C ATOM 318 C ASP A 351 64.270 4.489 55.174 1.00 14.74 C ANISOU 318 C ASP A 351 1804 2117 1680 -218 619 95 C ATOM 319 O ASP A 351 63.870 5.576 54.985 1.00 14.72 O ANISOU 319 O ASP A 351 1807 2059 1725 -252 654 173 O ATOM 320 CB ASP A 351 66.346 4.161 56.518 1.00 23.48 C ANISOU 320 CB ASP A 351 2625 3170 3128 -326 611 63 C ATOM 321 CG ASP A 351 66.834 5.491 56.123 1.00 36.08 C ANISOU 321 CG ASP A 351 4088 4655 4967 -371 732 220 C ATOM 322 OD1 ASP A 351 66.926 6.365 56.971 1.00 36.15 O ANISOU 322 OD1 ASP A 351 3991 4535 5207 -472 597 154 O ATOM 323 OD2 ASP A 351 67.061 5.671 54.928 1.00 44.18 O ANISOU 323 OD2 ASP A 351 5107 5716 5962 -269 958 417 O ATOM 324 N ARG A 352 64.288 3.563 54.232 1.00 15.25 N ANISOU 324 N ARG A 352 1970 2268 1556 -64 654 76 N ATOM 325 CA ARG A 352 63.695 3.843 52.921 1.00 16.00 C ANISOU 325 CA ARG A 352 2216 2429 1434 114 720 134 C ATOM 326 C ARG A 352 62.175 4.010 52.974 1.00 14.42 C ANISOU 326 C ARG A 352 2127 2184 1169 89 535 37 C ATOM 327 O ARG A 352 61.625 4.771 52.265 1.00 14.97 O ANISOU 327 O ARG A 352 2281 2270 1137 162 579 119 O ATOM 328 CB ARG A 352 64.056 2.782 51.886 1.00 17.75 C ANISOU 328 CB ARG A 352 2545 2765 1435 362 744 72 C ATOM 329 CG ARG A 352 65.464 2.955 51.364 1.00 21.98 C ANISOU 329 CG ARG A 352 2989 3362 2001 465 986 260 C ATOM 330 CD ARG A 352 65.883 1.943 50.352 1.00 25.84 C ANISOU 330 CD ARG A 352 3590 3946 2283 728 957 176 C ATOM 331 NE ARG A 352 66.143 0.670 50.948 1.00 24.81 N ANISOU 331 NE ARG A 352 3438 3809 2180 703 850 -13 N ATOM 332 CZ ARG A 352 65.548 -0.449 50.626 1.00 24.45 C ANISOU 332 CZ ARG A 352 3520 3755 2014 839 617 -257 C ATOM 333 NH1 ARG A 352 64.655 -0.476 49.689 1.00 22.27 N ANISOU 333 NH1 ARG A 352 3397 3481 1582 1009 450 -347 N ATOM 334 NH2 ARG A 352 65.855 -1.532 51.274 1.00 23.45 N ANISOU 334 NH2 ARG A 352 3330 3581 1999 798 512 -406 N ATOM 335 N GLU A 353 61.541 3.213 53.813 1.00 30.00 N ATOM 336 CA GLU A 353 60.104 3.315 54.023 1.00 30.00 C ATOM 337 C GLU A 353 59.693 4.669 54.589 1.00 30.00 C ATOM 338 O GLU A 353 58.673 5.197 54.274 1.00 30.00 O ATOM 339 CB GLU A 353 59.596 2.223 54.918 1.00 20.00 C ATOM 340 CG GLU A 353 59.717 0.834 54.358 1.00 20.00 C ATOM 341 CD GLU A 353 58.986 -0.165 55.193 1.00 20.00 C ATOM 342 OE1 GLU A 353 59.609 -0.725 56.137 1.00 20.00 O ATOM 343 OE2 GLU A 353 57.818 -0.408 54.953 1.00 20.00 O ATOM 344 N LEU A 354 60.534 5.205 55.436 1.00 13.46 N ANISOU 344 N LEU A 354 1892 1883 1338 -246 330 -8 N ATOM 345 CA LEU A 354 60.254 6.455 56.068 1.00 16.44 C ANISOU 345 CA LEU A 354 2233 2200 1812 -328 336 27 C ATOM 346 C LEU A 354 60.079 7.591 55.079 1.00 15.43 C ANISOU 346 C LEU A 354 2149 2042 1673 -304 435 144 C ATOM 347 O LEU A 354 59.251 8.406 55.261 1.00 14.07 O ANISOU 347 O LEU A 354 2003 1813 1530 -335 395 159 O ATOM 348 CB LEU A 354 61.320 6.833 57.086 1.00 19.12 C ANISOU 348 CB LEU A 354 2444 2507 2316 -395 333 -10 C ATOM 349 CG LEU A 354 61.291 6.142 58.431 1.00 22.94 C ANISOU 349 CG LEU A 354 2898 3031 2787 -378 219 -112 C ATOM 350 CD1 LEU A 354 62.480 6.617 59.254 1.00 25.54 C ANISOU 350 CD1 LEU A 354 3112 3323 3271 -398 155 -196 C ATOM 351 CD2 LEU A 354 59.992 6.524 59.111 1.00 20.24 C ANISOU 351 CD2 LEU A 354 2618 2692 2380 -337 156 -118 C ATOM 352 N VAL A 355 60.917 7.633 54.055 1.00 16.76 N ANISOU 352 N VAL A 355 2316 2255 1797 -218 588 260 N ATOM 353 CA VAL A 355 60.787 8.675 53.046 1.00 18.24 C ANISOU 353 CA VAL A 355 2534 2435 1962 -140 732 445 C ATOM 354 C VAL A 355 59.419 8.593 52.362 1.00 15.96 C ANISOU 354 C VAL A 355 2424 2197 1445 -29 631 403 C ATOM 355 O VAL A 355 58.791 9.614 52.097 1.00 17.75 O ANISOU 355 O VAL A 355 2673 2375 1695 -30 659 500 O ATOM 356 CB VAL A 355 61.901 8.593 51.991 1.00 22.39 C ANISOU 356 CB VAL A 355 3024 3040 2443 15 948 626 C ATOM 357 CG1 VAL A 355 61.782 9.760 51.022 1.00 22.35 C ANISOU 357 CG1 VAL A 355 3006 3014 2472 114 1048 818 C ATOM 358 CG2 VAL A 355 63.272 8.587 52.663 1.00 25.56 C ANISOU 358 CG2 VAL A 355 3212 3363 3136 -100 1016 663 C ATOM 359 N HIS A 356 58.951 7.376 52.096 1.00 14.64 N ANISOU 359 N HIS A 356 2359 2095 1110 68 482 246 N ATOM 360 CA HIS A 356 57.613 7.199 51.528 1.00 13.88 C ANISOU 360 CA HIS A 356 2391 1998 884 171 305 159 C ATOM 361 C HIS A 356 56.531 7.545 52.544 1.00 13.00 C ANISOU 361 C HIS A 356 2217 1769 954 1 185 120 C ATOM 362 O HIS A 356 55.478 8.073 52.184 1.00 13.75 O ANISOU 362 O HIS A 356 2370 1831 1024 36 109 136 O ATOM 363 CB HIS A 356 57.426 5.770 51.021 1.00 16.10 C ANISOU 363 CB HIS A 356 2751 2313 1053 325 114 -34 C ATOM 364 CG HIS A 356 58.275 5.452 49.833 1.00 20.91 C ANISOU 364 CG HIS A 356 3460 3066 1418 586 209 -19 C ATOM 365 ND1 HIS A 356 57.842 5.640 48.538 1.00 23.85 N ANISOU 365 ND1 HIS A 356 3930 3496 1636 823 150 -25 N ATOM 366 CD2 HIS A 356 59.546 4.993 49.744 1.00 20.31 C ANISOU 366 CD2 HIS A 356 3326 3055 1335 626 355 23 C ATOM 367 CE1 HIS A 356 58.805 5.295 47.701 1.00 23.94 C ANISOU 367 CE1 HIS A 356 3958 3607 1529 1025 261 19 C ATOM 368 NE2 HIS A 356 59.850 4.903 48.408 1.00 23.58 N ANISOU 368 NE2 HIS A 356 3814 3563 1582 897 387 53 N ATOM 369 N MET A 357 56.794 7.257 53.814 1.00 11.50 N ANISOU 369 N MET A 357 1910 1534 924 -143 178 84 N ATOM 370 CA MET A 357 55.805 7.529 54.852 1.00 11.82 C ANISOU 370 CA MET A 357 1896 1504 1092 -229 107 79 C ATOM 371 C MET A 357 55.555 9.026 54.963 1.00 13.52 C ANISOU 371 C MET A 357 2120 1677 1340 -272 177 155 C ATOM 372 O MET A 357 54.418 9.468 55.152 1.00 12.33 O ANISOU 372 O MET A 357 1984 1478 1224 -273 120 172 O ATOM 373 CB MET A 357 56.254 6.969 56.204 1.00 12.42 C ANISOU 373 CB MET A 357 1870 1590 1259 -287 114 49 C ATOM 374 CG MET A 357 55.238 7.193 57.336 1.00 12.29 C ANISOU 374 CG MET A 357 1806 1546 1318 -286 89 86 C ATOM 375 SD MET A 357 55.880 6.774 58.964 1.00 14.62 S ANISOU 375 SD MET A 357 2022 1916 1615 -245 124 75 S ATOM 376 CE MET A 357 56.399 5.079 58.686 1.00 11.74 C ANISOU 376 CE MET A 357 1594 1560 1306 -243 100 77 C ATOM 377 N ILE A 358 56.629 9.799 54.840 1.00 12.41 N ANISOU 377 N ILE A 358 1941 1526 1248 -305 296 213 N ATOM 378 CA ILE A 358 56.551 11.247 54.956 1.00 15.08 C ANISOU 378 CA ILE A 358 2243 1768 1717 -352 345 283 C ATOM 379 C ILE A 358 55.658 11.816 53.859 1.00 16.46 C ANISOU 379 C ILE A 358 2514 1943 1799 -275 371 394 C ATOM 380 O ILE A 358 54.839 12.705 54.099 1.00 18.08 O ANISOU 380 O ILE A 358 2722 2071 2075 -301 338 413 O ATOM 381 CB ILE A 358 57.957 11.886 54.897 1.00 19.47 C ANISOU 381 CB ILE A 358 2673 2254 2471 -401 459 361 C ATOM 382 CG1 ILE A 358 58.757 11.504 56.142 1.00 18.89 C ANISOU 382 CG1 ILE A 358 2501 2159 2516 -463 367 207 C ATOM 383 CG2 ILE A 358 57.863 13.397 54.787 1.00 24.69 C ANISOU 383 CG2 ILE A 358 3261 2759 3362 -441 501 465 C ATOM 384 CD1 ILE A 358 60.234 11.816 56.039 1.00 21.32 C ANISOU 384 CD1 ILE A 358 2642 2381 3078 -511 444 271 C ATOM 385 N ASN A 359 55.783 11.277 52.654 1.00 15.78 N ANISOU 385 N ASN A 359 2518 1955 1522 -139 413 453 N ATOM 386 CA ASN A 359 54.987 11.776 51.546 1.00 18.34 C ANISOU 386 CA ASN A 359 2956 2312 1700 2 415 549 C ATOM 387 C ASN A 359 53.558 11.246 51.548 1.00 16.23 C ANISOU 387 C ASN A 359 2761 2031 1374 34 190 413 C ATOM 388 O ASN A 359 52.647 11.921 51.076 1.00 17.07 O ANISOU 388 O ASN A 359 2923 2112 1450 92 147 468 O ATOM 389 CB ASN A 359 55.682 11.456 50.240 1.00 24.84 C ANISOU 389 CB ASN A 359 3861 3278 2300 224 530 649 C ATOM 390 CG ASN A 359 56.996 12.189 50.113 1.00 29.98 C ANISOU 390 CG ASN A 359 4348 3903 3141 188 746 825 C ATOM 391 OD1 ASN A 359 57.022 13.371 49.779 1.00 32.78 O ANISOU 391 OD1 ASN A 359 4626 4191 3638 189 842 983 O ATOM 392 ND2 ASN A 359 58.096 11.501 50.411 1.00 34.11 N ANISOU 392 ND2 ASN A 359 4799 4452 3711 159 808 798 N ATOM 393 N TRP A 360 53.367 10.054 52.100 1.00 16.00 N ANISOU 393 N TRP A 360 2696 1993 1390 -3 51 262 N ATOM 394 CA TRP A 360 52.026 9.536 52.351 1.00 15.16 C ANISOU 394 CA TRP A 360 2563 1806 1390 -10 -152 178 C ATOM 395 C TRP A 360 51.279 10.408 53.356 1.00 14.30 C ANISOU 395 C TRP A 360 2375 1617 1442 -124 -108 249 C ATOM 396 O TRP A 360 50.088 10.691 53.176 1.00 15.45 O ANISOU 396 O TRP A 360 2518 1696 1654 -97 -206 270 O ATOM 397 CB TRP A 360 52.093 8.091 52.859 1.00 14.67 C ANISOU 397 CB TRP A 360 2417 1712 1447 -33 -268 67 C ATOM 398 CG TRP A 360 50.853 7.635 53.608 1.00 15.96 C ANISOU 398 CG TRP A 360 2443 1746 1877 -88 -390 80 C ATOM 399 CD1 TRP A 360 49.681 7.179 53.064 1.00 16.38 C ANISOU 399 CD1 TRP A 360 2454 1677 2094 -23 -621 27 C ATOM 400 CD2 TRP A 360 50.681 7.580 55.033 1.00 15.75 C ANISOU 400 CD2 TRP A 360 2281 1694 2007 -176 -279 179 C ATOM 401 NE1 TRP A 360 48.795 6.849 54.065 1.00 17.58 N ANISOU 401 NE1 TRP A 360 2413 1707 2559 -95 -622 136 N ATOM 402 CE2 TRP A 360 49.383 7.089 55.280 1.00 16.00 C ANISOU 402 CE2 TRP A 360 2172 1593 2314 -163 -390 245 C ATOM 403 CE3 TRP A 360 51.502 7.902 56.124 1.00 14.51 C ANISOU 403 CE3 TRP A 360 2105 1619 1787 -222 -110 219 C ATOM 404 CZ2 TRP A 360 48.882 6.910 56.576 1.00 17.22 C ANISOU 404 CZ2 TRP A 360 2172 1724 2648 -170 -266 411 C ATOM 405 CZ3 TRP A 360 51.003 7.720 57.413 1.00 13.47 C ANISOU 405 CZ3 TRP A 360 1863 1487 1769 -200 -38 321 C ATOM 406 CH2 TRP A 360 49.710 7.227 57.625 1.00 13.82 C ANISOU 406 CH2 TRP A 360 1772 1428 2051 -163 -81 447 C ATOM 407 N ALA A 361 51.971 10.816 54.419 1.00 11.92 N ANISOU 407 N ALA A 361 2009 1318 1201 -218 16 267 N ATOM 408 CA ALA A 361 51.330 11.579 55.485 1.00 12.29 C ANISOU 408 CA ALA A 361 2004 1313 1352 -254 42 292 C ATOM 409 C ALA A 361 50.767 12.877 54.928 1.00 15.84 C ANISOU 409 C ALA A 361 2504 1704 1812 -244 60 360 C ATOM 410 O ALA A 361 49.656 13.283 55.269 1.00 18.03 O ANISOU 410 O ALA A 361 2763 1931 2158 -225 25 390 O ATOM 411 CB ALA A 361 52.312 11.860 56.622 1.00 10.20 C ANISOU 411 CB ALA A 361 1693 1069 1113 -288 108 234 C ATOM 412 N LYS A 362 51.534 13.502 54.042 1.00 13.52 N ANISOU 412 N LYS A 362 2254 1413 1471 -237 139 425 N ATOM 413 CA LYS A 362 51.129 14.746 53.393 1.00 16.46 C ANISOU 413 CA LYS A 362 2659 1722 1873 -210 187 543 C ATOM 414 C LYS A 362 49.831 14.594 52.589 1.00 17.31 C ANISOU 414 C LYS A 362 2843 1845 1888 -112 72 567 C ATOM 415 O LYS A 362 49.159 15.579 52.287 1.00 17.62 O ANISOU 415 O LYS A 362 2902 1826 1967 -87 81 655 O ATOM 416 CB LYS A 362 52.257 15.251 52.487 1.00 19.01 C ANISOU 416 CB LYS A 362 2982 2058 2184 -173 344 692 C ATOM 417 CG LYS A 362 53.503 15.672 53.244 1.00 22.01 C ANISOU 417 CG LYS A 362 3227 2349 2788 -283 425 683 C ATOM 418 CD LYS A 362 54.611 16.116 52.301 1.00 24.92 C ANISOU 418 CD LYS A 362 3521 2724 3225 -235 591 873 C ATOM 419 N ARG A 363 49.477 13.359 52.253 1.00 17.15 N ANISOU 419 N ARG A 363 2849 1876 1789 -50 -70 475 N ATOM 420 CA ARG A 363 48.280 13.108 51.460 1.00 19.04 C ANISOU 420 CA ARG A 363 3137 2095 2003 62 -260 447 C ATOM 421 C ARG A 363 47.109 12.657 52.334 1.00 18.86 C ANISOU 421 C ARG A 363 2981 1962 2224 -6 -378 414 C ATOM 422 O ARG A 363 45.995 12.475 51.850 1.00 20.07 O ANISOU 422 O ARG A 363 3112 2042 2473 60 -564 394 O ATOM 423 CB ARG A 363 48.578 12.078 50.367 1.00 24.49 C ANISOU 423 CB ARG A 363 3928 2871 2507 233 -407 338 C ATOM 424 CG ARG A 363 49.537 12.599 49.299 1.00 25.83 C ANISOU 424 CG ARG A 363 4239 3185 2392 400 -250 446 C ATOM 425 CD ARG A 363 49.745 11.591 48.190 1.00 30.73 C ANISOU 425 CD ARG A 363 5000 3926 2752 664 -415 307 C ATOM 426 NE ARG A 363 48.505 11.316 47.473 1.00 34.85 N ANISOU 426 NE ARG A 363 5564 4406 3271 820 -721 155 N ATOM 427 CZ ARG A 363 48.426 10.576 46.372 1.00 39.29 C ANISOU 427 CZ ARG A 363 6190 5030 3707 1061 -883 -38 C ATOM 428 NH1 ARG A 363 47.252 10.380 45.791 1.00 39.44 N ANISOU 428 NH1 ARG A 363 6220 4963 3803 1182 -1168 -201 N ATOM 429 NH2 ARG A 363 49.521 10.036 45.853 1.00 40.08 N ANISOU 429 NH2 ARG A 363 6339 5254 3636 1197 -762 -72 N ATOM 430 N VAL A 364 47.361 12.479 53.625 1.00 16.50 N ANISOU 430 N VAL A 364 2286 1704 2279 245 -635 495 N ATOM 431 CA VAL A 364 46.277 12.202 54.562 1.00 17.76 C ANISOU 431 CA VAL A 364 2183 1866 2700 307 -636 418 C ATOM 432 C VAL A 364 45.490 13.488 54.820 1.00 19.52 C ANISOU 432 C VAL A 364 2338 1939 3138 406 -691 432 C ATOM 433 O VAL A 364 46.067 14.487 55.245 1.00 20.10 O ANISOU 433 O VAL A 364 2487 1961 3190 394 -568 439 O ATOM 434 CB VAL A 364 46.808 11.631 55.895 1.00 15.79 C ANISOU 434 CB VAL A 364 1815 1728 2455 245 -394 329 C ATOM 435 CG1 VAL A 364 45.677 11.504 56.916 1.00 17.11 C ANISOU 435 CG1 VAL A 364 1749 1871 2882 297 -338 251 C ATOM 436 CG2 VAL A 364 47.506 10.287 55.669 1.00 15.55 C ANISOU 436 CG2 VAL A 364 1828 1825 2255 170 -357 313 C ATOM 437 N PRO A 365 44.175 13.478 54.534 1.00 20.97 N ANISOU 437 N PRO A 365 2375 2043 3552 502 -884 428 N ATOM 438 CA PRO A 365 43.332 14.671 54.704 1.00 26.18 C ANISOU 438 CA PRO A 365 2964 2579 4406 587 -908 413 C ATOM 439 C PRO A 365 43.551 15.390 56.036 1.00 26.00 C ANISOU 439 C PRO A 365 2846 2508 4526 610 -673 352 C ATOM 440 O PRO A 365 43.488 14.769 57.095 1.00 23.84 O ANISOU 440 O PRO A 365 2416 2307 4335 580 -484 260 O ATOM 441 CB PRO A 365 41.917 14.102 54.614 1.00 30.31 C ANISOU 441 CB PRO A 365 3277 3113 5128 609 -1005 340 C ATOM 442 CG PRO A 365 42.063 12.964 53.646 1.00 29.21 C ANISOU 442 CG PRO A 365 3232 3053 4812 546 -1151 365 C ATOM 443 CD PRO A 365 43.420 12.355 53.948 1.00 20.91 C ANISOU 443 CD PRO A 365 2293 2102 3549 477 -1014 390 C ATOM 444 N GLY A 366 43.846 16.685 55.966 1.00 27.09 N ANISOU 444 N GLY A 366 3113 2520 4661 648 -665 396 N ATOM 445 CA GLY A 366 44.042 17.498 57.154 1.00 26.41 C ANISOU 445 CA GLY A 366 2979 2364 4693 662 -443 322 C ATOM 446 C GLY A 366 45.476 17.632 57.647 1.00 26.48 C ANISOU 446 C GLY A 366 3159 2456 4447 528 -248 307 C ATOM 447 O GLY A 366 45.790 18.559 58.393 1.00 28.42 O ANISOU 447 O GLY A 366 3447 2624 4728 519 -106 258 O ATOM 448 N PHE A 367 46.352 16.718 57.244 1.00 20.61 N ANISOU 448 N PHE A 367 2505 1859 3466 423 -246 339 N ATOM 449 CA PHE A 367 47.708 16.705 57.787 1.00 17.89 C ANISOU 449 CA PHE A 367 2263 1603 2930 298 -74 308 C ATOM 450 C PHE A 367 48.531 17.928 57.365 1.00 21.44 C ANISOU 450 C PHE A 367 2905 1941 3300 255 -59 369 C ATOM 451 O PHE A 367 49.225 18.524 58.194 1.00 21.47 O ANISOU 451 O PHE A 367 2938 1928 3291 191 85 307 O ATOM 452 CB PHE A 367 48.431 15.420 57.376 1.00 16.60 C ANISOU 452 CB PHE A 367 2127 1604 2575 214 -77 324 C ATOM 453 CG PHE A 367 49.769 15.234 58.041 1.00 18.06 C ANISOU 453 CG PHE A 367 2355 1886 2620 100 79 276 C ATOM 454 CD1 PHE A 367 49.852 14.735 59.332 1.00 19.79 C ANISOU 454 CD1 PHE A 367 2477 2183 2860 75 196 179 C ATOM 455 CD2 PHE A 367 50.943 15.549 57.373 1.00 17.54 C ANISOU 455 CD2 PHE A 367 2431 1823 2411 14 105 328 C ATOM 456 CE1 PHE A 367 51.077 14.556 59.946 1.00 19.77 C ANISOU 456 CE1 PHE A 367 2511 2260 2743 -19 284 137 C ATOM 457 CE2 PHE A 367 52.175 15.374 57.983 1.00 19.36 C ANISOU 457 CE2 PHE A 367 2655 2134 2567 -87 224 274 C ATOM 458 CZ PHE A 367 52.237 14.871 59.275 1.00 19.45 C ANISOU 458 CZ PHE A 367 2561 2223 2605 -97 288 179 C ATOM 459 N VAL A 368 48.465 18.310 56.092 1.00 22.56 N ANISOU 459 N VAL A 368 3200 1992 3379 280 -209 489 N ATOM 460 CA VAL A 368 49.289 19.427 55.626 1.00 27.39 C ANISOU 460 CA VAL A 368 4023 2483 3901 218 -169 560 C ATOM 461 C VAL A 368 48.787 20.783 56.109 1.00 28.13 C ANISOU 461 C VAL A 368 4125 2382 4181 293 -162 546 C ATOM 462 O VAL A 368 49.481 21.784 55.953 1.00 29.00 O ANISOU 462 O VAL A 368 4399 2374 4246 230 -99 586 O ATOM 463 CB VAL A 368 49.400 19.476 54.089 1.00 30.24 C ANISOU 463 CB VAL A 368 4614 2780 4097 212 -313 706 C ATOM 464 CG1 VAL A 368 50.229 18.310 53.589 1.00 31.68 C ANISOU 464 CG1 VAL A 368 4840 3131 4066 108 -253 707 C ATOM 465 CG2 VAL A 368 48.027 19.514 53.439 1.00 31.15 C ANISOU 465 CG2 VAL A 368 4716 2792 4327 366 -577 771 C ATOM 466 N ASP A 369 47.592 20.817 56.696 1.00 26.36 N ANISOU 466 N ASP A 369 3720 2111 4184 424 -207 483 N ATOM 467 CA ASP A 369 47.063 22.047 57.291 1.00 29.40 C ANISOU 467 CA ASP A 369 4087 2305 4781 511 -167 439 C ATOM 468 C ASP A 369 47.745 22.384 58.612 1.00 26.24 C ANISOU 468 C ASP A 369 3669 1933 4370 419 69 304 C ATOM 469 O ASP A 369 47.709 23.524 59.061 1.00 26.10 O ANISOU 469 O ASP A 369 3710 1747 4460 444 136 264 O ATOM 470 CB ASP A 369 45.554 21.938 57.530 1.00 35.57 C ANISOU 470 CB ASP A 369 4647 3033 5833 677 -254 390 C ATOM 471 CG ASP A 369 44.761 21.855 56.245 1.00 42.89 C ANISOU 471 CG ASP A 369 5600 3957 6741 758 -511 494 C ATOM 472 OD1 ASP A 369 45.224 22.408 55.221 1.00 45.87 O ANISOU 472 OD1 ASP A 369 6210 4262 6957 735 -614 618 O ATOM 473 OD2 ASP A 369 43.672 21.239 56.262 1.00 43.72 O ANISOU 473 OD2 ASP A 369 5496 4133 6984 826 -592 445 O ATOM 474 N LEU A 370 48.339 21.380 59.243 1.00 19.32 N ANISOU 474 N LEU A 370 2724 1254 3362 320 175 230 N ATOM 475 CA LEU A 370 49.022 21.560 60.516 1.00 18.72 C ANISOU 475 CA LEU A 370 2654 1218 3242 227 353 101 C ATOM 476 C LEU A 370 50.339 22.308 60.318 1.00 20.97 C ANISOU 476 C LEU A 370 3105 1456 3407 91 389 126 C ATOM 477 O LEU A 370 50.887 22.297 59.221 1.00 20.83 O ANISOU 477 O LEU A 370 3184 1439 3292 41 321 243 O ATOM 478 CB LEU A 370 49.283 20.201 61.161 1.00 17.87 C ANISOU 478 CB LEU A 370 2447 1322 3022 168 413 37 C ATOM 479 CG LEU A 370 48.068 19.289 61.341 1.00 18.80 C ANISOU 479 CG LEU A 370 2393 1497 3253 267 402 13 C ATOM 480 CD1 LEU A 370 48.500 17.881 61.719 1.00 20.16 C ANISOU 480 CD1 LEU A 370 2514 1867 3279 193 437 -12 C ATOM 481 CD2 LEU A 370 47.134 19.869 62.383 1.00 24.07 C ANISOU 481 CD2 LEU A 370 2987 2049 4108 348 538 -102 C ATOM 482 N THR A 371 50.847 22.945 61.371 1.00 20.55 N ANISOU 482 N THR A 371 3093 1354 3362 21 505 11 N ATOM 483 CA THR A 371 52.184 23.537 61.309 1.00 20.49 C ANISOU 483 CA THR A 371 3202 1316 3268 -136 541 10 C ATOM 484 C THR A 371 53.224 22.448 61.087 1.00 19.83 C ANISOU 484 C THR A 371 3067 1436 3033 -248 533 29 C ATOM 485 O THR A 371 52.982 21.280 61.402 1.00 19.24 O ANISOU 485 O THR A 371 2884 1523 2904 -215 517 3 O ATOM 486 CB THR A 371 52.546 24.312 62.596 1.00 23.74 C ANISOU 486 CB THR A 371 3663 1646 3710 -201 638 -144 C ATOM 487 OG1 THR A 371 52.514 23.422 63.722 1.00 24.43 O ANISOU 487 OG1 THR A 371 3675 1884 3722 -211 680 -259 O ATOM 488 CG2 THR A 371 51.582 25.463 62.823 1.00 25.40 C ANISOU 488 CG2 THR A 371 3932 1628 4090 -87 675 -178 C ATOM 489 N LEU A 372 54.377 22.831 60.548 1.00 18.37 N ANISOU 489 N LEU A 372 2952 1227 2801 -381 557 70 N ATOM 490 CA LEU A 372 55.473 21.887 60.358 1.00 20.12 C ANISOU 490 CA LEU A 372 3100 1620 2925 -488 571 70 C ATOM 491 C LEU A 372 55.861 21.237 61.681 1.00 17.38 C ANISOU 491 C LEU A 372 2650 1402 2553 -522 567 -65 C ATOM 492 O LEU A 372 56.158 20.044 61.728 1.00 18.02 O ANISOU 492 O LEU A 372 2635 1648 2564 -523 539 -67 O ATOM 493 CB LEU A 372 56.687 22.580 59.738 1.00 20.34 C ANISOU 493 CB LEU A 372 3197 1570 2962 -643 641 107 C ATOM 494 CG LEU A 372 56.506 23.057 58.299 1.00 26.16 C ANISOU 494 CG LEU A 372 4090 2187 3664 -635 660 263 C ATOM 495 CD1 LEU A 372 57.785 23.706 57.782 1.00 28.38 C ANISOU 495 CD1 LEU A 372 4384 2459 3940 -768 732 274 C ATOM 496 CD2 LEU A 372 56.092 21.885 57.424 1.00 25.42 C ANISOU 496 CD2 LEU A 372 3980 2223 3454 -557 607 348 C ATOM 497 N HIS A 373 55.839 22.018 62.758 1.00 19.84 N ANISOU 497 N HIS A 373 3008 1623 2908 -548 587 -177 N ATOM 498 CA HIS A 373 56.152 21.481 64.074 1.00 20.92 C ANISOU 498 CA HIS A 373 3110 1856 2982 -580 563 -304 C ATOM 499 C HIS A 373 55.171 20.378 64.469 1.00 20.45 C ANISOU 499 C HIS A 373 3000 1910 2861 -461 561 -305 C ATOM 500 O HIS A 373 55.576 19.348 65.009 1.00 21.76 O ANISOU 500 O HIS A 373 3117 2215 2936 -483 520 -337 O ATOM 501 CB HIS A 373 56.148 22.592 65.126 1.00 22.31 C ANISOU 501 CB HIS A 373 3399 1888 3190 -623 591 -433 C ATOM 502 CG HIS A 373 57.243 23.596 64.947 1.00 25.83 C ANISOU 502 CG HIS A 373 3885 2224 3707 -772 584 -459 C ATOM 503 ND1 HIS A 373 58.475 23.265 64.426 1.00 27.96 N ANISOU 503 ND1 HIS A 373 4057 2572 3995 -894 550 -427 N ATOM 504 CD2 HIS A 373 57.290 24.923 65.213 1.00 28.79 C ANISOU 504 CD2 HIS A 373 4372 2408 4159 -821 618 -518 C ATOM 505 CE1 HIS A 373 59.236 24.345 64.381 1.00 28.45 C ANISOU 505 CE1 HIS A 373 4149 2521 4141 -1003 556 -455 C ATOM 506 NE2 HIS A 373 58.540 25.365 64.851 1.00 28.66 N ANISOU 506 NE2 HIS A 373 4304 2396 4188 -954 581 -501 N ATOM 507 N ASP A 374 53.886 20.591 64.195 1.00 19.84 N ANISOU 507 N ASP A 374 2927 1758 2854 -337 602 -269 N ATOM 508 CA ASP A 374 52.856 19.604 64.516 1.00 18.54 C ANISOU 508 CA ASP A 374 2691 1677 2677 -235 624 -273 C ATOM 509 C ASP A 374 52.979 18.363 63.630 1.00 15.98 C ANISOU 509 C ASP A 374 2272 1500 2300 -221 555 -173 C ATOM 510 O ASP A 374 52.810 17.231 64.094 1.00 13.57 O ANISOU 510 O ASP A 374 1914 1312 1929 -206 556 -192 O ATOM 511 CB ASP A 374 51.458 20.215 64.370 1.00 20.21 C ANISOU 511 CB ASP A 374 2886 1752 3042 -105 677 -268 C ATOM 512 CG ASP A 374 51.112 21.176 65.500 1.00 30.35 C ANISOU 512 CG ASP A 374 4258 2896 4376 -95 793 -400 C ATOM 513 OD1 ASP A 374 51.962 21.406 66.384 1.00 29.40 O ANISOU 513 OD1 ASP A 374 4242 2784 4145 -200 811 -494 O ATOM 514 OD2 ASP A 374 49.981 21.706 65.493 1.00 35.50 O ANISOU 514 OD2 ASP A 374 4876 3421 5191 20 858 -418 O ATOM 515 N GLN A 375 53.272 18.579 62.353 1.00 13.85 N ANISOU 515 N GLN A 375 2009 1207 2047 -231 504 -69 N ATOM 516 CA GLN A 375 53.514 17.471 61.440 1.00 13.70 C ANISOU 516 CA GLN A 375 1936 1312 1959 -231 451 11 C ATOM 517 C GLN A 375 54.704 16.635 61.907 1.00 15.30 C ANISOU 517 C GLN A 375 2092 1648 2074 -320 451 -33 C ATOM 518 O GLN A 375 54.633 15.408 61.936 1.00 13.45 O ANISOU 518 O GLN A 375 1793 1530 1785 -293 426 -25 O ATOM 519 CB GLN A 375 53.750 17.984 60.022 1.00 14.09 C ANISOU 519 CB GLN A 375 2062 1289 2002 -247 422 123 C ATOM 520 CG GLN A 375 52.576 18.732 59.413 1.00 15.64 C ANISOU 520 CG GLN A 375 2315 1341 2287 -140 365 190 C ATOM 521 CD GLN A 375 52.876 19.176 58.000 1.00 18.84 C ANISOU 521 CD GLN A 375 2859 1666 2632 -165 322 315 C ATOM 522 OE1 GLN A 375 53.629 18.513 57.288 1.00 22.07 O ANISOU 522 OE1 GLN A 375 3298 2164 2924 -233 341 358 O ATOM 523 NE2 GLN A 375 52.313 20.312 57.592 1.00 22.09 N ANISOU 523 NE2 GLN A 375 3378 1894 3120 -109 277 375 N ATOM 524 N VAL A 376 55.785 17.308 62.293 1.00 13.19 N ANISOU 524 N VAL A 376 1848 1348 1814 -423 466 -85 N ATOM 525 CA VAL A 376 56.976 16.626 62.793 1.00 17.41 C ANISOU 525 CA VAL A 376 2313 1989 2313 -502 430 -137 C ATOM 526 C VAL A 376 56.629 15.803 64.024 1.00 16.92 C ANISOU 526 C VAL A 376 2250 2002 2179 -460 389 -204 C ATOM 527 O VAL A 376 56.983 14.630 64.143 1.00 14.72 O ANISOU 527 O VAL A 376 1909 1834 1849 -448 342 -196 O ATOM 528 CB VAL A 376 58.103 17.634 63.140 1.00 16.73 C ANISOU 528 CB VAL A 376 2237 1830 2289 -628 430 -203 C ATOM 529 CG1 VAL A 376 59.153 16.998 64.044 1.00 18.36 C ANISOU 529 CG1 VAL A 376 2363 2128 2484 -689 337 -286 C ATOM 530 CG2 VAL A 376 58.739 18.178 61.869 1.00 16.27 C ANISOU 530 CG2 VAL A 376 2175 1713 2294 -700 501 -129 C ATOM 531 N HIS A 377 55.904 16.428 64.936 1.00 15.27 N ANISOU 531 N HIS A 377 2128 1713 1959 -436 424 -268 N ATOM 532 CA HIS A 377 55.559 15.767 66.176 1.00 18.25 C ANISOU 532 CA HIS A 377 2561 2135 2238 -413 421 -334 C ATOM 533 C HIS A 377 54.716 14.502 65.980 1.00 16.50 C ANISOU 533 C HIS A 377 2286 1996 1985 -330 446 -276 C ATOM 534 O HIS A 377 54.978 13.477 66.611 1.00 14.58 O ANISOU 534 O HIS A 377 2059 1834 1647 -335 405 -287 O ATOM 535 CB HIS A 377 54.821 16.722 67.098 1.00 20.62 C ANISOU 535 CB HIS A 377 2985 2315 2535 -400 507 -422 C ATOM 536 CG HIS A 377 54.370 16.070 68.358 1.00 22.51 C ANISOU 536 CG HIS A 377 3329 2581 2644 -384 549 -488 C ATOM 537 ND1 HIS A 377 55.257 15.565 69.283 1.00 23.99 N ANISOU 537 ND1 HIS A 377 3606 2823 2684 -449 443 -536 N ATOM 538 CD2 HIS A 377 53.133 15.789 68.823 1.00 23.97 C ANISOU 538 CD2 HIS A 377 3549 2737 2822 -315 689 -506 C ATOM 539 CE1 HIS A 377 54.583 15.024 70.280 1.00 27.09 C ANISOU 539 CE1 HIS A 377 4132 3215 2948 -424 521 -574 C ATOM 540 NE2 HIS A 377 53.293 15.144 70.025 1.00 25.87 N ANISOU 540 NE2 HIS A 377 3935 3010 2884 -350 695 -562 N ATOM 541 N LEU A 378 53.703 14.569 65.121 1.00 12.76 N ANISOU 541 N LEU A 378 1757 1491 1601 -258 495 -216 N ATOM 542 CA LEU A 378 52.867 13.396 64.875 1.00 13.27 C ANISOU 542 CA LEU A 378 1755 1620 1667 -194 509 -171 C ATOM 543 C LEU A 378 53.651 12.249 64.230 1.00 12.83 C ANISOU 543 C LEU A 378 1642 1678 1555 -212 427 -114 C ATOM 544 O LEU A 378 53.480 11.085 64.605 1.00 12.68 O ANISOU 544 O LEU A 378 1611 1725 1483 -196 423 -110 O ATOM 545 CB LEU A 378 51.666 13.764 64.003 1.00 13.82 C ANISOU 545 CB LEU A 378 1758 1619 1872 -113 529 -123 C ATOM 546 CG LEU A 378 50.623 14.659 64.679 1.00 14.92 C ANISOU 546 CG LEU A 378 1912 1638 2119 -62 634 -188 C ATOM 547 CD1 LEU A 378 49.597 15.132 63.664 1.00 17.74 C ANISOU 547 CD1 LEU A 378 2182 1910 2650 29 595 -131 C ATOM 548 CD2 LEU A 378 49.934 13.938 65.830 1.00 16.05 C ANISOU 548 CD2 LEU A 378 2063 1801 2236 -54 757 -254 C ATOM 549 N LEU A 379 54.508 12.570 63.266 1.00 14.14 N ANISOU 549 N LEU A 379 1782 1852 1739 -248 385 -75 N ATOM 550 CA LEU A 379 55.296 11.536 62.605 1.00 14.49 C ANISOU 550 CA LEU A 379 1768 1987 1749 -262 342 -38 C ATOM 551 C LEU A 379 56.347 10.954 63.549 1.00 14.46 C ANISOU 551 C LEU A 379 1749 2044 1700 -301 288 -89 C ATOM 552 O LEU A 379 56.609 9.751 63.527 1.00 13.09 O ANISOU 552 O LEU A 379 1537 1940 1497 -276 251 -73 O ATOM 553 CB LEU A 379 55.954 12.089 61.338 1.00 16.59 C ANISOU 553 CB LEU A 379 2030 2228 2044 -301 357 10 C ATOM 554 CG LEU A 379 55.051 12.073 60.104 1.00 15.71 C ANISOU 554 CG LEU A 379 1956 2083 1931 -249 353 87 C ATOM 555 CD1 LEU A 379 55.627 12.937 58.989 1.00 14.29 C ANISOU 555 CD1 LEU A 379 1847 1837 1745 -301 390 140 C ATOM 556 CD2 LEU A 379 54.882 10.644 59.629 1.00 16.38 C ANISOU 556 CD2 LEU A 379 2004 2251 1968 -213 324 108 C ATOM 557 N GLU A 380 56.938 11.805 64.385 1.00 13.31 N ANISOU 557 N GLU A 380 1643 1858 1556 -358 262 -152 N ATOM 558 CA GLU A 380 57.898 11.342 65.382 1.00 14.34 C ANISOU 558 CA GLU A 380 1776 2028 1643 -391 157 -206 C ATOM 559 C GLU A 380 57.244 10.384 66.363 1.00 13.77 C ANISOU 559 C GLU A 380 1796 1981 1454 -342 139 -208 C ATOM 560 O GLU A 380 57.845 9.392 66.767 1.00 14.72 O ANISOU 560 O GLU A 380 1909 2151 1532 -329 42 -202 O ATOM 561 CB GLU A 380 58.514 12.521 66.146 1.00 18.44 C ANISOU 561 CB GLU A 380 2349 2481 2177 -471 111 -287 C ATOM 562 CG GLU A 380 59.663 13.195 65.423 1.00 18.52 C ANISOU 562 CG GLU A 380 2245 2473 2321 -552 98 -298 C ATOM 563 CD GLU A 380 60.254 14.336 66.218 1.00 22.80 C ANISOU 563 CD GLU A 380 2835 2936 2893 -646 36 -390 C ATOM 564 OE1 GLU A 380 61.416 14.704 65.947 1.00 26.63 O ANISOU 564 OE1 GLU A 380 3202 3409 3506 -732 -9 -422 O ATOM 565 OE2 GLU A 380 59.553 14.860 67.112 1.00 21.76 O ANISOU 565 OE2 GLU A 380 2858 2743 2667 -638 44 -440 O ATOM 566 N ACYS A 381 56.004 10.669 66.749 0.48 13.09 N ANISOU 566 N ACYS A 381 1798 1845 1330 -314 244 -215 N ATOM 567 N BCYS A 381 56.003 10.671 66.732 0.52 13.10 N ANISOU 567 N BCYS A 381 1798 1847 1333 -314 245 -215 N ATOM 568 CA ACYS A 381 55.312 9.791 67.685 0.48 13.54 C ANISOU 568 CA ACYS A 381 1960 1908 1277 -286 280 -217 C ATOM 569 CA BCYS A 381 55.305 9.818 67.676 0.52 13.54 C ANISOU 569 CA BCYS A 381 1959 1907 1278 -286 281 -218 C ATOM 570 C ACYS A 381 54.923 8.463 67.047 0.48 13.70 C ANISOU 570 C ACYS A 381 1903 1984 1317 -236 290 -145 C ATOM 571 C BCYS A 381 54.900 8.481 67.058 0.52 13.72 C ANISOU 571 C BCYS A 381 1907 1986 1319 -236 292 -146 C ATOM 572 O ACYS A 381 55.084 7.407 67.659 0.48 15.24 O ANISOU 572 O ACYS A 381 2164 2203 1423 -227 247 -128 O ATOM 573 O BCYS A 381 55.030 7.436 67.695 0.52 15.41 O ANISOU 573 O BCYS A 381 2191 2222 1443 -228 254 -130 O ATOM 574 CB ACYS A 381 54.062 10.469 68.248 0.48 13.34 C ANISOU 574 CB ACYS A 381 2022 1801 1246 -274 437 -260 C ATOM 575 CB BCYS A 381 54.070 10.526 68.220 0.52 13.60 C ANISOU 575 CB BCYS A 381 2053 1833 1284 -274 437 -261 C ATOM 576 SG ACYS A 381 54.414 11.816 69.385 0.48 21.04 S ANISOU 576 SG ACYS A 381 3167 2686 2140 -334 444 -371 S ATOM 577 SG BCYS A 381 53.219 9.573 69.472 0.52 18.65 S ANISOU 577 SG BCYS A 381 2850 2452 1783 -266 546 -272 S ATOM 578 N ALA A 382 54.429 8.515 65.813 1.00 11.39 N ANISOU 578 N ALA A 382 1495 1699 1132 -207 330 -103 N ATOM 579 CA ALA A 382 53.763 7.353 65.209 1.00 13.15 C ANISOU 579 CA ALA A 382 1663 1953 1381 -167 349 -51 C ATOM 580 C ALA A 382 54.552 6.498 64.213 1.00 12.31 C ANISOU 580 C ALA A 382 1480 1906 1291 -154 273 -12 C ATOM 581 O ALA A 382 54.037 5.472 63.769 1.00 9.72 O ANISOU 581 O ALA A 382 1126 1592 973 -127 280 19 O ATOM 582 CB ALA A 382 52.478 7.822 64.527 1.00 14.72 C ANISOU 582 CB ALA A 382 1800 2106 1688 -136 421 -38 C ATOM 583 N TRP A 383 55.772 6.890 63.857 1.00 13.99 N ANISOU 583 N TRP A 383 1652 2142 1521 -179 219 -23 N ATOM 584 CA TRP A 383 56.439 6.248 62.726 1.00 10.43 C ANISOU 584 CA TRP A 383 1124 1730 1108 -167 203 2 C ATOM 585 C TRP A 383 56.592 4.728 62.877 1.00 10.30 C ANISOU 585 C TRP A 383 1102 1744 1070 -126 164 16 C ATOM 586 O TRP A 383 56.356 3.997 61.924 1.00 9.02 O ANISOU 586 O TRP A 383 916 1591 920 -102 186 37 O ATOM 587 CB TRP A 383 57.810 6.885 62.465 1.00 11.16 C ANISOU 587 CB TRP A 383 1150 1831 1258 -212 186 -26 C ATOM 588 CG TRP A 383 58.852 6.630 63.517 1.00 13.28 C ANISOU 588 CG TRP A 383 1389 2115 1541 -222 83 -69 C ATOM 589 CD1 TRP A 383 59.066 7.357 64.655 1.00 15.08 C ANISOU 589 CD1 TRP A 383 1673 2316 1739 -259 14 -112 C ATOM 590 CD2 TRP A 383 59.842 5.591 63.514 1.00 12.73 C ANISOU 590 CD2 TRP A 383 1232 2077 1528 -188 11 -77 C ATOM 591 NE1 TRP A 383 60.116 6.826 65.366 1.00 16.89 N ANISOU 591 NE1 TRP A 383 1864 2562 1992 -254 -128 -141 N ATOM 592 CE2 TRP A 383 60.611 5.743 64.687 1.00 16.78 C ANISOU 592 CE2 TRP A 383 1745 2581 2049 -202 -133 -118 C ATOM 593 CE3 TRP A 383 60.147 4.544 62.636 1.00 15.59 C ANISOU 593 CE3 TRP A 383 1524 2461 1939 -141 47 -62 C ATOM 594 CZ2 TRP A 383 61.665 4.884 65.009 1.00 18.41 C ANISOU 594 CZ2 TRP A 383 1861 2798 2336 -161 -265 -133 C ATOM 595 CZ3 TRP A 383 61.194 3.692 62.956 1.00 18.07 C ANISOU 595 CZ3 TRP A 383 1743 2782 2339 -98 -46 -85 C ATOM 596 CH2 TRP A 383 61.941 3.869 64.130 1.00 19.23 C ANISOU 596 CH2 TRP A 383 1869 2918 2518 -103 -212 -116 C ATOM 597 N LEU A 384 56.963 4.241 64.058 1.00 9.16 N ANISOU 597 N LEU A 384 1003 1597 879 -117 95 4 N ATOM 598 CA LEU A 384 57.172 2.798 64.189 1.00 11.48 C ANISOU 598 CA LEU A 384 1307 1896 1160 -71 47 28 C ATOM 599 C LEU A 384 55.829 2.048 64.270 1.00 9.75 C ANISOU 599 C LEU A 384 1159 1649 899 -62 115 61 C ATOM 600 O LEU A 384 55.710 0.924 63.773 1.00 10.63 O ANISOU 600 O LEU A 384 1257 1752 1028 -33 114 81 O ATOM 601 CB LEU A 384 58.057 2.483 65.401 1.00 10.17 C ANISOU 601 CB LEU A 384 1192 1718 953 -57 -86 19 C ATOM 602 CG LEU A 384 58.451 1.007 65.580 1.00 10.83 C ANISOU 602 CG LEU A 384 1293 1783 1039 7 -165 51 C ATOM 603 CD1 LEU A 384 59.093 0.429 64.307 1.00 13.19 C ANISOU 603 CD1 LEU A 384 1442 2102 1469 47 -139 38 C ATOM 604 CD2 LEU A 384 59.371 0.830 66.787 1.00 14.23 C ANISOU 604 CD2 LEU A 384 1790 2187 1430 28 -349 49 C ATOM 605 N GLU A 385 54.818 2.670 64.872 1.00 10.43 N ANISOU 605 N GLU A 385 1306 1706 950 -91 188 56 N ATOM 606 CA GLU A 385 53.467 2.119 64.821 1.00 10.60 C ANISOU 606 CA GLU A 385 1341 1693 993 -96 279 74 C ATOM 607 C GLU A 385 52.998 1.935 63.373 1.00 10.65 C ANISOU 607 C GLU A 385 1245 1708 1092 -83 276 81 C ATOM 608 O GLU A 385 52.408 0.911 63.021 1.00 9.84 O ANISOU 608 O GLU A 385 1132 1589 1019 -81 285 95 O ATOM 609 CB GLU A 385 52.473 3.020 65.562 1.00 8.93 C ANISOU 609 CB GLU A 385 1170 1429 794 -115 378 50 C ATOM 610 CG GLU A 385 52.619 3.055 67.070 1.00 11.03 C ANISOU 610 CG GLU A 385 1587 1662 941 -134 400 39 C ATOM 611 CD GLU A 385 51.507 3.851 67.731 0.94 13.68 C ANISOU 611 CD GLU A 385 1937 1939 1323 -144 508 3 C ATOM 612 OE1 GLU A 385 51.721 5.040 68.043 0.61 14.51 O ANISOU 612 OE1 GLU A 385 2074 2031 1409 -155 522 -40 O ATOM 613 OE2 GLU A 385 50.409 3.292 67.925 0.69 13.64 O ANISOU 613 OE2 GLU A 385 1912 1891 1381 -150 588 9 O ATOM 614 N ILE A 386 53.264 2.935 62.542 1.00 8.48 N ANISOU 614 N ILE A 386 924 1444 854 -80 253 70 N ATOM 615 CA ILE A 386 52.863 2.885 61.143 1.00 10.92 C ANISOU 615 CA ILE A 386 1189 1759 1203 -72 232 82 C ATOM 616 C ILE A 386 53.653 1.815 60.372 1.00 10.91 C ANISOU 616 C ILE A 386 1190 1787 1169 -58 203 84 C ATOM 617 O ILE A 386 53.073 1.054 59.608 1.00 11.47 O ANISOU 617 O ILE A 386 1267 1841 1251 -54 182 85 O ATOM 618 CB ILE A 386 53.023 4.268 60.494 1.00 11.29 C ANISOU 618 CB ILE A 386 1227 1804 1258 -81 230 88 C ATOM 619 CG1 ILE A 386 52.036 5.251 61.138 1.00 13.43 C ANISOU 619 CG1 ILE A 386 1485 2027 1591 -79 265 79 C ATOM 620 CG2 ILE A 386 52.825 4.184 58.978 1.00 12.78 C ANISOU 620 CG2 ILE A 386 1435 1984 1438 -74 185 109 C ATOM 621 CD1 ILE A 386 52.359 6.725 60.896 1.00 16.53 C ANISOU 621 CD1 ILE A 386 1896 2389 1995 -87 268 81 C ATOM 622 N LEU A 387 54.960 1.726 60.598 1.00 10.69 N ANISOU 622 N LEU A 387 1153 1786 1123 -49 197 71 N ATOM 623 CA LEU A 387 55.736 0.651 59.980 1.00 9.71 C ANISOU 623 CA LEU A 387 1018 1668 1004 -20 192 58 C ATOM 624 C LEU A 387 55.201 -0.717 60.393 1.00 12.02 C ANISOU 624 C LEU A 387 1346 1925 1294 2 170 68 C ATOM 625 O LEU A 387 55.082 -1.627 59.569 1.00 14.95 O ANISOU 625 O LEU A 387 1735 2275 1670 16 173 54 O ATOM 626 CB LEU A 387 57.217 0.752 60.350 1.00 10.50 C ANISOU 626 CB LEU A 387 1057 1790 1144 -4 180 34 C ATOM 627 CG LEU A 387 58.004 1.878 59.689 1.00 11.78 C ANISOU 627 CG LEU A 387 1169 1971 1337 -41 234 14 C ATOM 628 CD1 LEU A 387 59.466 1.752 60.065 1.00 11.62 C ANISOU 628 CD1 LEU A 387 1038 1962 1415 -26 214 -23 C ATOM 629 CD2 LEU A 387 57.822 1.840 58.172 1.00 10.32 C ANISOU 629 CD2 LEU A 387 1046 1749 1126 -50 302 13 C ATOM 630 N MET A 388 54.866 -0.851 61.670 1.00 9.68 N ANISOU 630 N MET A 388 1088 1610 980 -3 159 89 N ATOM 631 CA MET A 388 54.425 -2.133 62.193 1.00 12.15 C ANISOU 631 CA MET A 388 1461 1869 1284 5 156 111 C ATOM 632 C MET A 388 53.042 -2.544 61.684 1.00 12.37 C ANISOU 632 C MET A 388 1485 1861 1354 -33 197 110 C ATOM 633 O MET A 388 52.824 -3.716 61.386 1.00 13.10 O ANISOU 633 O MET A 388 1604 1906 1468 -31 190 109 O ATOM 634 CB MET A 388 54.431 -2.112 63.721 1.00 9.95 C ANISOU 634 CB MET A 388 1274 1564 940 -3 150 141 C ATOM 635 CG MET A 388 55.826 -2.261 64.326 1.00 8.13 C ANISOU 635 CG MET A 388 1064 1340 684 46 42 146 C ATOM 636 SD MET A 388 55.823 -2.199 66.120 1.00 13.87 S ANISOU 636 SD MET A 388 1972 2021 1276 30 -5 184 S ATOM 637 CE MET A 388 57.479 -2.761 66.494 1.00 13.50 C ANISOU 637 CE MET A 388 1915 1961 1253 114 -208 192 C ATOM 638 N ILE A 389 52.099 -1.609 61.596 1.00 12.01 N ANISOU 638 N ILE A 389 1396 1824 1344 -66 230 104 N ATOM 639 CA ILE A 389 50.772 -2.006 61.137 1.00 12.90 C ANISOU 639 CA ILE A 389 1465 1893 1545 -101 241 94 C ATOM 640 C ILE A 389 50.857 -2.357 59.646 1.00 11.27 C ANISOU 640 C ILE A 389 1249 1691 1341 -91 157 70 C ATOM 641 O ILE A 389 50.167 -3.260 59.168 1.00 12.58 O ANISOU 641 O ILE A 389 1412 1810 1559 -116 126 52 O ATOM 642 CB ILE A 389 49.684 -0.924 61.414 1.00 11.95 C ANISOU 642 CB ILE A 389 1269 1762 1510 -124 286 86 C ATOM 643 CG1 ILE A 389 48.288 -1.524 61.189 1.00 13.98 C ANISOU 643 CG1 ILE A 389 1441 1958 1913 -165 299 69 C ATOM 644 CG2 ILE A 389 49.904 0.353 60.594 1.00 10.01 C ANISOU 644 CG2 ILE A 389 991 1553 1261 -97 224 82 C ATOM 645 CD1 ILE A 389 47.135 -0.595 61.529 1.00 15.91 C ANISOU 645 CD1 ILE A 389 1570 2171 2303 -177 360 49 C ATOM 646 N GLY A 390 51.750 -1.674 58.934 1.00 11.66 N ANISOU 646 N GLY A 390 1316 1786 1326 -63 132 65 N ATOM 647 CA GLY A 390 52.032 -1.996 57.548 1.00 13.94 C ANISOU 647 CA GLY A 390 1655 2073 1568 -57 87 39 C ATOM 648 C GLY A 390 52.571 -3.411 57.432 1.00 14.58 C ANISOU 648 C GLY A 390 1782 2122 1636 -39 101 12 C ATOM 649 O GLY A 390 52.089 -4.197 56.622 1.00 15.47 O ANISOU 649 O GLY A 390 1941 2190 1746 -56 58 -21 O ATOM 650 N LEU A 391 53.568 -3.731 58.256 1.00 13.08 N ANISOU 650 N LEU A 391 1583 1941 1447 -2 143 23 N ATOM 651 CA LEU A 391 54.141 -5.074 58.303 1.00 13.51 C ANISOU 651 CA LEU A 391 1673 1944 1516 36 149 4 C ATOM 652 C LEU A 391 53.093 -6.141 58.617 1.00 14.90 C ANISOU 652 C LEU A 391 1887 2042 1733 1 132 12 C ATOM 653 O LEU A 391 53.030 -7.176 57.952 1.00 13.20 O ANISOU 653 O LEU A 391 1723 1765 1528 3 120 -27 O ATOM 654 CB LEU A 391 55.267 -5.132 59.345 1.00 11.61 C ANISOU 654 CB LEU A 391 1404 1712 1294 91 148 28 C ATOM 655 CG LEU A 391 55.873 -6.509 59.625 1.00 12.21 C ANISOU 655 CG LEU A 391 1515 1712 1411 153 128 25 C ATOM 656 CD1 LEU A 391 56.554 -7.064 58.378 1.00 11.69 C ANISOU 656 CD1 LEU A 391 1444 1625 1374 193 174 -46 C ATOM 657 CD2 LEU A 391 56.843 -6.437 60.800 1.00 14.42 C ANISOU 657 CD2 LEU A 391 1774 1994 1713 209 67 62 C ATOM 658 N VAL A 392 52.273 -5.890 59.632 1.00 14.02 N ANISOU 658 N VAL A 392 1758 1921 1649 -40 150 54 N ATOM 659 CA VAL A 392 51.260 -6.862 60.023 1.00 15.69 C ANISOU 659 CA VAL A 392 1994 2045 1922 -94 171 64 C ATOM 660 C VAL A 392 50.261 -7.081 58.878 1.00 16.12 C ANISOU 660 C VAL A 392 2011 2072 2041 -147 118 11 C ATOM 661 O VAL A 392 49.871 -8.213 58.588 1.00 17.09 O ANISOU 661 O VAL A 392 2171 2111 2211 -180 102 -15 O ATOM 662 CB VAL A 392 50.541 -6.413 61.316 1.00 16.22 C ANISOU 662 CB VAL A 392 2053 2102 2006 -139 251 110 C ATOM 663 CG1 VAL A 392 49.318 -7.255 61.569 1.00 22.40 C ANISOU 663 CG1 VAL A 392 2831 2791 2890 -221 312 110 C ATOM 664 CG2 VAL A 392 51.503 -6.489 62.502 1.00 15.80 C ANISOU 664 CG2 VAL A 392 2099 2045 1858 -95 265 162 C ATOM 665 N TRP A 393 49.881 -6.001 58.203 1.00 11.71 N ANISOU 665 N TRP A 393 1394 1572 1484 -153 67 -5 N ATOM 666 CA TRP A 393 48.996 -6.100 57.039 1.00 12.97 C ANISOU 666 CA TRP A 393 1537 1703 1690 -193 -42 -53 C ATOM 667 C TRP A 393 49.607 -6.935 55.898 1.00 16.12 C ANISOU 667 C TRP A 393 2057 2071 1997 -178 -93 -108 C ATOM 668 O TRP A 393 48.940 -7.816 55.353 1.00 16.37 O ANISOU 668 O TRP A 393 2118 2028 2076 -227 -164 -157 O ATOM 669 CB TRP A 393 48.628 -4.702 56.525 1.00 14.08 C ANISOU 669 CB TRP A 393 1626 1896 1827 -182 -112 -44 C ATOM 670 CG TRP A 393 47.879 -4.710 55.227 1.00 16.72 C ANISOU 670 CG TRP A 393 1983 2198 2172 -208 -277 -85 C ATOM 671 CD1 TRP A 393 48.350 -4.311 54.009 1.00 21.36 C ANISOU 671 CD1 TRP A 393 2702 2802 2612 -186 -361 -99 C ATOM 672 CD2 TRP A 393 46.529 -5.145 55.013 1.00 18.56 C ANISOU 672 CD2 TRP A 393 2120 2361 2569 -267 -391 -121 C ATOM 673 NE1 TRP A 393 47.373 -4.463 53.052 1.00 23.61 N ANISOU 673 NE1 TRP A 393 3010 3034 2928 -221 -551 -136 N ATOM 674 CE2 TRP A 393 46.248 -4.977 53.641 1.00 23.15 C ANISOU 674 CE2 TRP A 393 2789 2923 3082 -270 -587 -156 C ATOM 675 CE3 TRP A 393 45.531 -5.659 55.846 1.00 19.13 C ANISOU 675 CE3 TRP A 393 2044 2377 2847 -327 -341 -131 C ATOM 676 CZ2 TRP A 393 45.010 -5.304 53.084 1.00 26.67 C ANISOU 676 CZ2 TRP A 393 3160 3298 3675 -324 -779 -204 C ATOM 677 CZ3 TRP A 393 44.299 -5.985 55.287 1.00 23.55 C ANISOU 677 CZ3 TRP A 393 2497 2866 3585 -388 -493 -183 C ATOM 678 CH2 TRP A 393 44.053 -5.807 53.921 1.00 26.57 C ANISOU 678 CH2 TRP A 393 2951 3235 3910 -382 -733 -221 C ATOM 679 N ARG A 394 50.868 -6.664 55.552 1.00 16.32 N ANISOU 679 N ARG A 394 2152 2143 1907 -117 -43 -111 N ATOM 680 CA ARG A 394 51.578 -7.417 54.510 1.00 18.66 C ANISOU 680 CA ARG A 394 2573 2403 2115 -94 -35 -176 C ATOM 681 C ARG A 394 51.663 -8.902 54.830 1.00 16.74 C ANISOU 681 C ARG A 394 2366 2065 1931 -90 -8 -206 C ATOM 682 O ARG A 394 51.750 -9.738 53.934 1.00 18.51 O ANISOU 682 O ARG A 394 2699 2221 2114 -96 -25 -280 O ATOM 683 CB ARG A 394 53.011 -6.893 54.321 1.00 19.69 C ANISOU 683 CB ARG A 394 2723 2590 2168 -30 70 -176 C ATOM 684 CG ARG A 394 53.124 -5.465 53.860 1.00 24.73 C ANISOU 684 CG ARG A 394 3364 3300 2733 -40 69 -149 C ATOM 685 CD ARG A 394 54.496 -5.176 53.278 1.00 22.14 C ANISOU 685 CD ARG A 394 3083 2996 2333 -4 197 -178 C ATOM 686 NE ARG A 394 55.579 -5.149 54.260 1.00 16.85 N ANISOU 686 NE ARG A 394 2289 2358 1757 49 280 -161 N ATOM 687 CZ ARG A 394 55.828 -4.123 55.068 1.00 16.99 C ANISOU 687 CZ ARG A 394 2207 2434 1814 47 281 -108 C ATOM 688 NH1 ARG A 394 55.045 -3.054 55.049 1.00 16.89 N ANISOU 688 NH1 ARG A 394 2199 2451 1766 4 228 -66 N ATOM 689 NH2 ARG A 394 56.855 -4.171 55.905 1.00 15.60 N ANISOU 689 NH2 ARG A 394 1929 2275 1723 93 318 -104 N ATOM 690 N SER A 395 51.667 -9.215 56.118 1.00 16.13 N ANISOU 690 N SER A 395 1875 1618 2634 -219 -28 -627 N ATOM 691 CA SER A 395 51.964 -10.558 56.584 1.00 17.58 C ANISOU 691 CA SER A 395 2073 1672 2935 -206 121 -591 C ATOM 692 C SER A 395 50.713 -11.403 56.780 1.00 21.66 C ANISOU 692 C SER A 395 2524 2063 3643 -297 130 -645 C ATOM 693 O SER A 395 50.807 -12.589 57.086 1.00 21.87 O ANISOU 693 O SER A 395 2578 1958 3773 -301 246 -620 O ATOM 694 CB SER A 395 52.755 -10.484 57.892 1.00 15.24 C ANISOU 694 CB SER A 395 1745 1433 2614 -138 242 -404 C ATOM 695 OG SER A 395 53.936 -9.726 57.716 1.00 17.12 O ANISOU 695 OG SER A 395 2019 1808 2679 -69 223 -338 O ATOM 696 N MET A 396 49.549 -10.787 56.594 1.00 20.66 N ANISOU 696 N MET A 396 2315 2013 3524 -341 11 -673 N ATOM 697 CA MET A 396 48.271 -11.465 56.813 1.00 26.27 C ANISOU 697 CA MET A 396 2936 2662 4385 -411 18 -689 C ATOM 698 C MET A 396 48.115 -12.785 56.068 1.00 30.13 C ANISOU 698 C MET A 396 3506 3027 4915 -469 17 -766 C ATOM 699 O MET A 396 47.626 -13.762 56.632 1.00 33.75 O ANISOU 699 O MET A 396 3928 3380 5517 -520 112 -746 O ATOM 700 CB MET A 396 47.118 -10.552 56.415 1.00 28.44 C ANISOU 700 CB MET A 396 3118 3029 4659 -426 -126 -718 C ATOM 701 CG MET A 396 46.577 -9.721 57.538 1.00 30.18 C ANISOU 701 CG MET A 396 3214 3303 4952 -397 -64 -649 C ATOM 702 SD MET A 396 45.041 -8.960 57.007 1.00 33.58 S ANISOU 702 SD MET A 396 3518 3784 5455 -405 -211 -692 S ATOM 703 CE MET A 396 43.877 -10.301 57.174 1.00 32.62 C ANISOU 703 CE MET A 396 3292 3560 5542 -511 -161 -728 C ATOM 704 N GLU A 397 48.518 -12.810 54.804 1.00 30.76 N ANISOU 704 N GLU A 397 3717 3113 4855 -468 -83 -850 N ATOM 705 CA GLU A 397 48.356 -14.006 53.985 1.00 34.99 C ANISOU 705 CA GLU A 397 4370 3523 5402 -534 -95 -942 C ATOM 706 C GLU A 397 49.559 -14.943 54.089 1.00 36.03 C ANISOU 706 C GLU A 397 4626 3529 5533 -465 63 -937 C ATOM 707 O GLU A 397 49.760 -15.805 53.234 1.00 36.30 O ANISOU 707 O GLU A 397 4809 3457 5526 -483 62 -1026 O ATOM 708 CB GLU A 397 48.112 -13.621 52.523 1.00 34.86 C ANISOU 708 CB GLU A 397 4469 3562 5214 -580 -269 -1034 C ATOM 709 N HIS A 398 50.351 -14.771 55.144 1.00 34.00 N ANISOU 709 N HIS A 398 4316 3278 5323 -379 201 -824 N ATOM 710 CA HIS A 398 51.494 -15.640 55.409 1.00 31.58 C ANISOU 710 CA HIS A 398 4097 2857 5046 -284 368 -772 C ATOM 711 C HIS A 398 51.535 -16.074 56.870 1.00 30.07 C ANISOU 711 C HIS A 398 3825 2602 4998 -261 511 -611 C ATOM 712 O HIS A 398 52.360 -15.574 57.631 1.00 25.71 O ANISOU 712 O HIS A 398 3245 2098 4426 -171 584 -484 O ATOM 713 CB HIS A 398 52.804 -14.934 55.059 1.00 30.49 C ANISOU 713 CB HIS A 398 4013 2804 4770 -166 398 -757 C ATOM 714 CG HIS A 398 52.908 -14.524 53.625 1.00 34.14 C ANISOU 714 CG HIS A 398 4588 3329 5053 -181 285 -893 C ATOM 715 ND1 HIS A 398 53.477 -15.328 52.661 1.00 36.69 N ANISOU 715 ND1 HIS A 398 5063 3566 5311 -140 337 -979 N ATOM 716 CD2 HIS A 398 52.514 -13.395 52.989 1.00 35.09 C ANISOU 716 CD2 HIS A 398 4709 3591 5033 -227 123 -939 C ATOM 717 CE1 HIS A 398 53.433 -14.710 51.494 1.00 37.42 C ANISOU 717 CE1 HIS A 398 5256 3742 5219 -168 216 -1075 C ATOM 718 NE2 HIS A 398 52.851 -13.537 51.665 1.00 36.34 N ANISOU 718 NE2 HIS A 398 5033 3742 5031 -222 80 -1039 N ATOM 719 N PRO A 399 50.649 -17.005 57.266 1.00 31.98 N ANISOU 719 N PRO A 399 4045 2736 5371 -344 549 -604 N ATOM 720 CA PRO A 399 50.599 -17.441 58.667 1.00 29.31 C ANISOU 720 CA PRO A 399 3655 2343 5140 -331 687 -438 C ATOM 721 C PRO A 399 51.962 -17.883 59.191 1.00 24.42 C ANISOU 721 C PRO A 399 3106 1666 4506 -186 813 -290 C ATOM 722 O PRO A 399 52.645 -18.671 58.538 1.00 26.96 O ANISOU 722 O PRO A 399 3527 1891 4827 -118 851 -330 O ATOM 723 CB PRO A 399 49.624 -18.622 58.633 1.00 32.25 C ANISOU 723 CB PRO A 399 4041 2574 5639 -438 712 -486 C ATOM 724 CG PRO A 399 48.772 -18.368 57.443 1.00 35.10 C ANISOU 724 CG PRO A 399 4393 2975 5969 -539 545 -664 C ATOM 725 CD PRO A 399 49.673 -17.725 56.430 1.00 33.97 C ANISOU 725 CD PRO A 399 4335 2907 5664 -460 465 -740 C ATOM 726 N GLY A 400 52.354 -17.356 60.346 1.00 21.44 N ANISOU 726 N GLY A 400 2680 1359 4107 -133 868 -112 N ATOM 727 CA GLY A 400 53.593 -17.758 60.988 1.00 25.33 C ANISOU 727 CA GLY A 400 3215 1826 4581 13 957 75 C ATOM 728 C GLY A 400 54.830 -17.024 60.500 1.00 26.53 C ANISOU 728 C GLY A 400 3367 2080 4633 144 923 96 C ATOM 729 O GLY A 400 55.945 -17.312 60.939 1.00 26.07 O ANISOU 729 O GLY A 400 3308 2038 4558 283 970 259 O ATOM 730 N LYS A 401 54.644 -16.076 59.590 1.00 22.33 N ANISOU 730 N LYS A 401 2821 1643 4022 102 827 -63 N ATOM 731 CA LYS A 401 55.772 -15.347 59.026 1.00 20.57 C ANISOU 731 CA LYS A 401 2584 1585 3645 205 781 -58 C ATOM 732 C LYS A 401 55.525 -13.852 58.993 1.00 17.71 C ANISOU 732 C LYS A 401 2161 1448 3118 139 646 -86 C ATOM 733 O LYS A 401 54.380 -13.406 58.965 1.00 18.91 O ANISOU 733 O LYS A 401 2291 1610 3286 23 575 -178 O ATOM 734 CB LYS A 401 56.070 -15.834 57.608 1.00 27.39 C ANISOU 734 CB LYS A 401 3543 2349 4514 238 811 -241 C ATOM 735 CG LYS A 401 56.317 -17.323 57.486 1.00 34.71 C ANISOU 735 CG LYS A 401 4541 3111 5535 284 908 -229 C ATOM 736 CD LYS A 401 56.371 -17.741 56.028 1.00 39.94 C ANISOU 736 CD LYS A 401 5320 3720 6137 269 900 -431 C ATOM 737 CE LYS A 401 57.130 -19.041 55.867 1.00 47.35 C ANISOU 737 CE LYS A 401 6323 4515 7151 379 1026 -399 C ATOM 738 NZ LYS A 401 56.559 -20.112 56.725 1.00 50.78 N ANISOU 738 NZ LYS A 401 6768 4789 7736 342 1074 -316 N ATOM 739 N LEU A 402 56.612 -13.084 58.982 1.00 17.51 N ANISOU 739 N LEU A 402 2101 1596 2955 214 613 -5 N ATOM 740 CA LEU A 402 56.538 -11.644 58.820 1.00 18.56 C ANISOU 740 CA LEU A 402 2204 1919 2928 157 493 -35 C ATOM 741 C LEU A 402 57.161 -11.271 57.483 1.00 16.58 C ANISOU 741 C LEU A 402 1999 1723 2577 186 469 -146 C ATOM 742 O LEU A 402 58.335 -11.545 57.224 1.00 15.26 O ANISOU 742 O LEU A 402 1820 1584 2395 285 545 -88 O ATOM 743 CB LEU A 402 57.234 -10.920 59.978 1.00 19.13 C ANISOU 743 CB LEU A 402 2214 2153 2903 177 466 151 C ATOM 744 CG LEU A 402 56.600 -11.116 61.360 1.00 20.61 C ANISOU 744 CG LEU A 402 2391 2311 3130 134 495 263 C ATOM 745 CD1 LEU A 402 57.498 -10.573 62.461 1.00 19.35 C ANISOU 745 CD1 LEU A 402 2203 2304 2845 157 459 450 C ATOM 746 CD2 LEU A 402 55.218 -10.467 61.418 1.00 18.25 C ANISOU 746 CD2 LEU A 402 2091 2006 2837 22 455 148 C ATOM 747 N LEU A 403 56.343 -10.665 56.632 1.00 15.76 N ANISOU 747 N LEU A 403 1945 1632 2411 101 368 -299 N ATOM 748 CA LEU A 403 56.769 -10.222 55.314 1.00 17.09 C ANISOU 748 CA LEU A 403 2194 1853 2446 104 335 -408 C ATOM 749 C LEU A 403 57.317 -8.803 55.399 1.00 16.55 C ANISOU 749 C LEU A 403 2095 1975 2219 89 261 -331 C ATOM 750 O LEU A 403 56.611 -7.842 55.088 1.00 15.26 O ANISOU 750 O LEU A 403 1959 1862 1977 18 135 -389 O ATOM 751 CB LEU A 403 55.601 -10.296 54.322 1.00 18.43 C ANISOU 751 CB LEU A 403 2451 1939 2612 12 231 -597 C ATOM 752 CG LEU A 403 55.881 -10.332 52.816 1.00 22.89 C ANISOU 752 CG LEU A 403 3165 2492 3041 5 217 -745 C ATOM 753 CD1 LEU A 403 54.662 -10.839 52.078 1.00 29.28 C ANISOU 753 CD1 LEU A 403 4053 3184 3888 -93 105 -910 C ATOM 754 CD2 LEU A 403 56.258 -8.976 52.271 1.00 24.44 C ANISOU 754 CD2 LEU A 403 3395 2854 3037 -12 129 -722 C ATOM 755 N PHE A 404 58.568 -8.673 55.836 1.00 17.50 N ANISOU 755 N PHE A 404 2150 2192 2308 155 332 -195 N ATOM 756 CA PHE A 404 59.208 -7.362 55.889 1.00 17.13 C ANISOU 756 CA PHE A 404 2077 2315 2117 119 270 -124 C ATOM 757 C PHE A 404 59.314 -6.795 54.484 1.00 15.80 C ANISOU 757 C PHE A 404 2015 2177 1811 88 247 -236 C ATOM 758 O PHE A 404 59.092 -5.598 54.259 1.00 14.96 O ANISOU 758 O PHE A 404 1950 2149 1586 16 142 -241 O ATOM 759 CB PHE A 404 60.587 -7.449 56.552 1.00 14.79 C ANISOU 759 CB PHE A 404 1665 2121 1835 183 340 43 C ATOM 760 CG PHE A 404 60.517 -7.608 58.043 1.00 14.08 C ANISOU 760 CG PHE A 404 1498 2047 1806 185 311 183 C ATOM 761 CD1 PHE A 404 60.372 -6.497 58.862 1.00 12.32 C ANISOU 761 CD1 PHE A 404 1267 1931 1485 97 208 243 C ATOM 762 CD2 PHE A 404 60.546 -8.867 58.622 1.00 13.12 C ANISOU 762 CD2 PHE A 404 1341 1817 1827 269 391 251 C ATOM 763 CE1 PHE A 404 60.284 -6.635 60.235 1.00 12.72 C ANISOU 763 CE1 PHE A 404 1284 1999 1551 86 187 362 C ATOM 764 CE2 PHE A 404 60.457 -9.018 59.996 1.00 16.92 C ANISOU 764 CE2 PHE A 404 1782 2313 2332 263 363 393 C ATOM 765 CZ PHE A 404 60.328 -7.894 60.810 1.00 13.95 C ANISOU 765 CZ PHE A 404 1407 2064 1830 167 260 445 C ATOM 766 N ALA A 405 59.626 -7.680 53.542 1.00 15.30 N ANISOU 766 N ALA A 405 2020 2035 1759 141 353 -326 N ATOM 767 CA ALA A 405 59.738 -7.341 52.129 1.00 15.73 C ANISOU 767 CA ALA A 405 2217 2104 1656 112 357 -442 C ATOM 768 C ALA A 405 59.475 -8.614 51.340 1.00 15.25 C ANISOU 768 C ALA A 405 2267 1884 1642 151 448 -593 C ATOM 769 O ALA A 405 59.546 -9.704 51.911 1.00 18.16 O ANISOU 769 O ALA A 405 2577 2143 2179 221 542 -574 O ATOM 770 CB ALA A 405 61.115 -6.770 51.821 1.00 15.76 C ANISOU 770 CB ALA A 405 2182 2243 1564 135 463 -353 C ATOM 771 N PRO A 406 59.154 -8.499 50.038 1.00 18.23 N ANISOU 771 N PRO A 406 2827 2237 1864 98 414 -742 N ATOM 772 CA PRO A 406 58.898 -9.746 49.308 1.00 20.43 C ANISOU 772 CA PRO A 406 3218 2359 2184 122 479 -885 C ATOM 773 C PRO A 406 60.126 -10.651 49.256 1.00 23.92 C ANISOU 773 C PRO A 406 3628 2758 2703 250 722 -854 C ATOM 774 O PRO A 406 59.979 -11.860 49.082 1.00 26.34 O ANISOU 774 O PRO A 406 3976 2915 3118 290 781 -923 O ATOM 775 CB PRO A 406 58.506 -9.263 47.908 1.00 22.99 C ANISOU 775 CB PRO A 406 3671 2737 2327 57 335 -960 C ATOM 776 CG PRO A 406 58.012 -7.871 48.114 1.00 22.22 C ANISOU 776 CG PRO A 406 3522 2762 2160 -6 154 -878 C ATOM 777 CD PRO A 406 58.874 -7.311 49.213 1.00 19.21 C ANISOU 777 CD PRO A 406 3043 2461 1795 20 265 -751 C ATOM 778 N ASN A 407 61.318 -10.082 49.417 1.00 20.11 N ANISOU 778 N ASN A 407 3049 2409 2183 311 844 -735 N ATOM 779 CA ASN A 407 62.532 -10.889 49.444 1.00 22.45 C ANISOU 779 CA ASN A 407 3248 2687 2596 445 1044 -669 C ATOM 780 C ASN A 407 63.082 -11.020 50.866 1.00 19.65 C ANISOU 780 C ASN A 407 2667 2368 2432 537 1084 -477 C ATOM 781 O ASN A 407 64.243 -11.367 51.066 1.00 21.35 O ANISOU 781 O ASN A 407 2741 2628 2744 636 1191 -365 O ATOM 782 CB ASN A 407 63.590 -10.300 48.506 1.00 23.51 C ANISOU 782 CB ASN A 407 3391 2955 2588 446 1139 -652 C ATOM 783 CG ASN A 407 64.102 -8.945 48.972 1.00 22.70 C ANISOU 783 CG ASN A 407 3166 3049 2412 392 1097 -509 C ATOM 784 OD1 ASN A 407 63.445 -8.249 49.747 1.00 23.00 O ANISOU 784 OD1 ASN A 407 3180 3126 2432 328 965 -458 O ATOM 785 ND2 ASN A 407 65.286 -8.567 48.497 1.00 23.21 N ANISOU 785 ND2 ASN A 407 3151 3231 2436 406 1209 -445 N ATOM 786 N LEU A 408 62.242 -10.730 51.854 1.00 17.77 N ANISOU 786 N LEU A 408 2866 1692 2195 -43 1076 -395 N ATOM 787 CA LEU A 408 62.627 -10.902 53.249 1.00 19.75 C ANISOU 787 CA LEU A 408 3042 1948 2512 15 1079 -316 C ATOM 788 C LEU A 408 61.415 -11.332 54.065 1.00 20.46 C ANISOU 788 C LEU A 408 3168 1879 2726 27 1017 -208 C ATOM 789 O LEU A 408 60.758 -10.516 54.714 1.00 18.29 O ANISOU 789 O LEU A 408 2901 1625 2422 -4 1011 -113 O ATOM 790 CB LEU A 408 63.236 -9.617 53.821 1.00 20.15 C ANISOU 790 CB LEU A 408 3074 2131 2453 -92 1097 -247 C ATOM 791 CG LEU A 408 63.939 -9.739 55.181 1.00 21.89 C ANISOU 791 CG LEU A 408 3211 2397 2710 -34 1100 -180 C ATOM 792 CD1 LEU A 408 65.096 -10.723 55.112 1.00 21.34 C ANISOU 792 CD1 LEU A 408 2994 2466 2649 93 1143 -255 C ATOM 793 CD2 LEU A 408 64.419 -8.373 55.678 1.00 20.09 C ANISOU 793 CD2 LEU A 408 3043 2245 2346 -181 1056 -102 C ATOM 794 N LEU A 409 61.128 -12.627 54.003 1.00 17.79 N ANISOU 794 N LEU A 409 2867 1403 2491 79 948 -217 N ATOM 795 CA LEU A 409 60.000 -13.234 54.699 1.00 23.54 C ANISOU 795 CA LEU A 409 3605 2026 3313 17 862 -69 C ATOM 796 C LEU A 409 60.542 -14.112 55.823 1.00 24.24 C ANISOU 796 C LEU A 409 3684 2051 3476 90 820 -12 C ATOM 797 O LEU A 409 61.126 -15.171 55.574 1.00 24.35 O ANISOU 797 O LEU A 409 3804 1925 3522 184 737 -97 O ATOM 798 CB LEU A 409 59.148 -14.042 53.714 1.00 24.78 C ANISOU 798 CB LEU A 409 3876 2032 3507 -69 740 -79 C ATOM 799 CG LEU A 409 57.904 -14.804 54.170 1.00 27.15 C ANISOU 799 CG LEU A 409 4180 2259 3875 -231 602 115 C ATOM 800 CD1 LEU A 409 56.838 -13.857 54.690 1.00 26.52 C ANISOU 800 CD1 LEU A 409 3923 2416 3738 -297 668 270 C ATOM 801 CD2 LEU A 409 57.369 -15.631 53.010 1.00 27.76 C ANISOU 801 CD2 LEU A 409 4434 2143 3970 -333 438 74 C ATOM 802 N LEU A 410 60.364 -13.661 57.061 1.00 19.96 N ANISOU 802 N LEU A 410 3045 1605 2933 84 862 119 N ATOM 803 CA LEU A 410 61.010 -14.296 58.205 1.00 22.58 C ANISOU 803 CA LEU A 410 3363 1899 3317 159 837 172 C ATOM 804 C LEU A 410 60.011 -14.995 59.122 1.00 25.94 C ANISOU 804 C LEU A 410 3775 2288 3791 50 748 384 C ATOM 805 O LEU A 410 58.930 -14.472 59.365 1.00 23.77 O ANISOU 805 O LEU A 410 3399 2167 3465 -35 775 519 O ATOM 806 CB LEU A 410 61.796 -13.253 59.003 1.00 20.58 C ANISOU 806 CB LEU A 410 3022 1801 2998 233 939 164 C ATOM 807 CG LEU A 410 62.848 -12.457 58.232 1.00 20.79 C ANISOU 807 CG LEU A 410 3030 1934 2937 254 1006 21 C ATOM 808 CD1 LEU A 410 63.452 -11.369 59.105 1.00 22.91 C ANISOU 808 CD1 LEU A 410 3262 2321 3120 247 1039 65 C ATOM 809 CD2 LEU A 410 63.939 -13.376 57.690 1.00 23.20 C ANISOU 809 CD2 LEU A 410 3323 2241 3251 376 994 -111 C ATOM 810 N ASP A 411 60.366 -16.169 59.637 1.00 26.42 N ANISOU 810 N ASP A 411 3938 2181 3920 58 628 426 N ATOM 811 CA ASP A 411 59.546 -16.777 60.684 1.00 28.92 C ANISOU 811 CA ASP A 411 4230 2506 4254 -96 536 674 C ATOM 812 C ASP A 411 60.161 -16.464 62.044 1.00 28.15 C ANISOU 812 C ASP A 411 4042 2516 4138 21 617 727 C ATOM 813 O ASP A 411 61.198 -15.803 62.117 1.00 28.16 O ANISOU 813 O ASP A 411 4012 2565 4122 194 719 575 O ATOM 814 CB ASP A 411 59.367 -18.291 60.476 1.00 33.71 C ANISOU 814 CB ASP A 411 5077 2813 4919 -227 284 740 C ATOM 815 CG ASP A 411 60.673 -19.075 60.527 1.00 38.44 C ANISOU 815 CG ASP A 411 5886 3170 5551 2 189 565 C ATOM 816 OD1 ASP A 411 61.713 -18.544 60.972 1.00 37.84 O ANISOU 816 OD1 ASP A 411 5702 3215 5462 219 330 448 O ATOM 817 OD2 ASP A 411 60.646 -20.258 60.123 1.00 43.19 O ANISOU 817 OD2 ASP A 411 6782 3461 6166 -28 -60 550 O ATOM 818 N ARG A 412 59.525 -16.925 63.115 1.00 27.65 N ANISOU 818 N ARG A 412 3930 2518 4059 -101 559 962 N ATOM 819 CA ARG A 412 59.930 -16.498 64.449 1.00 26.61 C ANISOU 819 CA ARG A 412 3701 2528 3881 14 645 1029 C ATOM 820 C ARG A 412 61.339 -16.981 64.787 1.00 26.30 C ANISOU 820 C ARG A 412 3787 2296 3911 176 602 891 C ATOM 821 O ARG A 412 62.073 -16.301 65.502 1.00 25.48 O ANISOU 821 O ARG A 412 3612 2295 3773 323 697 840 O ATOM 822 CB ARG A 412 58.925 -16.977 65.506 1.00 28.97 C ANISOU 822 CB ARG A 412 3901 2993 4114 -161 590 1335 C ATOM 823 CG ARG A 412 59.230 -18.323 66.128 1.00 25.73 C ANISOU 823 CG ARG A 412 3661 2350 3767 -286 400 1462 C ATOM 824 CD ARG A 412 58.240 -18.649 67.224 1.00 30.92 C ANISOU 824 CD ARG A 412 4176 3261 4312 -501 362 1799 C ATOM 825 NE ARG A 412 58.504 -17.905 68.449 1.00 31.18 N ANISOU 825 NE ARG A 412 4056 3542 4248 -305 516 1827 N ATOM 826 CZ ARG A 412 59.259 -18.357 69.446 1.00 33.35 C ANISOU 826 CZ ARG A 412 4429 3698 4545 -242 464 1853 C ATOM 827 NH1 ARG A 412 59.835 -19.551 69.357 1.00 31.73 N ANISOU 827 NH1 ARG A 412 4486 3126 4445 -331 256 1842 N ATOM 828 NH2 ARG A 412 59.438 -17.618 70.533 1.00 31.35 N ANISOU 828 NH2 ARG A 412 4048 3678 4185 -60 592 1867 N ATOM 829 N ASN A 413 61.724 -18.134 64.245 1.00 25.21 N ANISOU 829 N ASN A 413 3853 1883 3843 175 435 823 N ATOM 830 CA ASN A 413 63.033 -18.704 64.524 1.00 28.03 C ANISOU 830 CA ASN A 413 4327 2092 4230 395 370 682 C ATOM 831 C ASN A 413 64.159 -17.794 64.065 1.00 27.11 C ANISOU 831 C ASN A 413 4078 2142 4080 606 528 460 C ATOM 832 O ASN A 413 65.216 -17.736 64.691 1.00 26.47 O ANISOU 832 O ASN A 413 3949 2123 3985 772 551 399 O ATOM 833 CB ASN A 413 63.173 -20.075 63.864 1.00 31.72 C ANISOU 833 CB ASN A 413 5102 2224 4727 429 122 612 C ATOM 834 CG ASN A 413 62.303 -21.117 64.517 1.00 39.51 C ANISOU 834 CG ASN A 413 6282 3003 5726 170 -112 871 C ATOM 835 OD1 ASN A 413 61.985 -21.016 65.703 1.00 38.57 O ANISOU 835 OD1 ASN A 413 6054 3009 5591 48 -80 1083 O ATOM 836 ND2 ASN A 413 61.913 -22.132 63.751 1.00 47.13 N ANISOU 836 ND2 ASN A 413 7517 3700 6689 67 -355 858 N ATOM 837 N GLN A 414 63.926 -17.079 62.973 1.00 26.39 N ANISOU 837 N GLN A 414 3921 2147 3958 566 622 363 N ATOM 838 CA GLN A 414 64.935 -16.179 62.434 1.00 25.90 C ANISOU 838 CA GLN A 414 3732 2278 3831 680 749 199 C ATOM 839 C GLN A 414 65.036 -14.896 63.249 1.00 23.69 C ANISOU 839 C GLN A 414 3319 2187 3495 623 859 274 C ATOM 840 O GLN A 414 66.046 -14.197 63.194 1.00 29.20 O ANISOU 840 O GLN A 414 3925 3044 4126 666 915 197 O ATOM 841 CB GLN A 414 64.630 -15.874 60.970 1.00 25.12 C ANISOU 841 CB GLN A 414 3646 2201 3698 632 785 87 C ATOM 842 CG GLN A 414 64.817 -17.091 60.081 1.00 30.08 C ANISOU 842 CG GLN A 414 4448 2646 4336 764 653 -42 C ATOM 843 CD GLN A 414 64.209 -16.917 58.710 1.00 34.13 C ANISOU 843 CD GLN A 414 5014 3133 4821 686 660 -118 C ATOM 844 OE1 GLN A 414 62.996 -16.774 58.576 1.00 32.00 O ANISOU 844 OE1 GLN A 414 4780 2785 4592 479 633 1 O ATOM 845 NE2 GLN A 414 65.049 -16.927 57.681 1.00 38.06 N ANISOU 845 NE2 GLN A 414 5493 3745 5223 861 699 -311 N ATOM 846 N GLY A 415 63.997 -14.594 64.015 1.00 23.60 N ANISOU 846 N GLY A 415 3308 2181 3477 531 866 435 N ATOM 847 CA GLY A 415 64.037 -13.462 64.920 1.00 23.99 C ANISOU 847 CA GLY A 415 3310 2369 3438 547 925 495 C ATOM 848 C GLY A 415 65.033 -13.672 66.049 1.00 23.93 C ANISOU 848 C GLY A 415 3285 2371 3437 643 898 514 C ATOM 849 O GLY A 415 65.584 -12.710 66.582 1.00 23.13 O ANISOU 849 O GLY A 415 3172 2363 3252 662 914 507 O ATOM 850 N LYS A 416 65.269 -14.935 66.405 1.00 19.32 N ANISOU 850 N LYS A 416 2738 1665 2939 696 821 542 N ATOM 851 CA LYS A 416 66.205 -15.290 67.473 1.00 19.96 C ANISOU 851 CA LYS A 416 2813 1741 3030 810 777 559 C ATOM 852 C LYS A 416 67.628 -14.865 67.135 1.00 25.23 C ANISOU 852 C LYS A 416 3383 2549 3656 902 800 413 C ATOM 853 O LYS A 416 68.491 -14.821 68.006 1.00 28.96 O ANISOU 853 O LYS A 416 3808 3089 4107 980 772 426 O ATOM 854 CB LYS A 416 66.173 -16.799 67.746 1.00 21.61 C ANISOU 854 CB LYS A 416 3148 1744 3318 860 641 603 C ATOM 855 CG LYS A 416 64.843 -17.329 68.287 1.00 22.20 C ANISOU 855 CG LYS A 416 3294 1736 3405 687 581 822 C ATOM 856 CD LYS A 416 64.913 -18.837 68.494 1.00 33.68 C ANISOU 856 CD LYS A 416 4957 2924 4917 683 375 879 C ATOM 857 CE LYS A 416 63.606 -19.404 69.018 1.00 35.35 C ANISOU 857 CE LYS A 416 5223 3098 5109 416 283 1157 C ATOM 858 NZ LYS A 416 63.688 -20.878 69.226 1.00 39.24 N ANISOU 858 NZ LYS A 416 6006 3267 5636 356 13 1238 N ATOM 859 N CYS A 417 67.861 -14.562 65.862 1.00 25.96 N ANISOU 859 N CYS A 417 3422 2725 3716 875 845 293 N ATOM 860 CA CYS A 417 69.166 -14.126 65.380 1.00 26.54 C ANISOU 860 CA CYS A 417 3341 3040 3702 913 875 191 C ATOM 861 C CYS A 417 69.613 -12.841 66.076 1.00 23.63 C ANISOU 861 C CYS A 417 2922 2814 3242 770 878 271 C ATOM 862 O CYS A 417 70.811 -12.593 66.256 1.00 22.01 O ANISOU 862 O CYS A 417 2572 2831 2961 770 858 260 O ATOM 863 CB CYS A 417 69.115 -13.919 63.866 1.00 29.07 C ANISOU 863 CB CYS A 417 3619 3453 3972 866 930 84 C ATOM 864 SG CYS A 417 70.589 -13.192 63.161 1.00 80.04 S ANISOU 864 SG CYS A 417 9824 10333 10255 821 980 21 S ATOM 865 N VAL A 418 68.632 -12.033 66.461 1.00 20.01 N ANISOU 865 N VAL A 418 2599 2243 2763 662 877 355 N ATOM 866 CA VAL A 418 68.880 -10.768 67.134 1.00 19.27 C ANISOU 866 CA VAL A 418 2578 2195 2550 553 820 420 C ATOM 867 C VAL A 418 68.401 -10.853 68.573 1.00 22.27 C ANISOU 867 C VAL A 418 3058 2467 2935 661 785 516 C ATOM 868 O VAL A 418 67.249 -11.204 68.824 1.00 22.37 O ANISOU 868 O VAL A 418 3127 2391 2980 731 821 569 O ATOM 869 CB VAL A 418 68.172 -9.599 66.422 1.00 18.65 C ANISOU 869 CB VAL A 418 2642 2078 2367 416 806 415 C ATOM 870 CG1 VAL A 418 68.437 -8.285 67.157 1.00 20.13 C ANISOU 870 CG1 VAL A 418 3016 2239 2394 324 672 475 C ATOM 871 CG2 VAL A 418 68.632 -9.508 64.972 1.00 19.05 C ANISOU 871 CG2 VAL A 418 2590 2257 2391 286 845 338 C ATOM 872 N GLU A 419 69.285 -10.537 69.515 1.00 22.32 N ANISOU 872 N GLU A 419 3067 2527 2888 663 708 555 N ATOM 873 CA GLU A 419 68.942 -10.599 70.931 1.00 24.94 C ANISOU 873 CA GLU A 419 3498 2780 3198 783 670 643 C ATOM 874 C GLU A 419 67.701 -9.762 71.234 1.00 22.59 C ANISOU 874 C GLU A 419 3385 2420 2779 836 666 685 C ATOM 875 O GLU A 419 67.620 -8.594 70.855 1.00 22.00 O ANISOU 875 O GLU A 419 3466 2323 2570 767 594 651 O ATOM 876 CB GLU A 419 70.116 -10.128 71.792 1.00 28.45 C ANISOU 876 CB GLU A 419 3952 3288 3568 746 557 672 C ATOM 877 N GLY A 420 66.727 -10.384 71.893 1.00 23.11 N ANISOU 877 N GLY A 420 3435 2483 2860 966 725 769 N ATOM 878 CA GLY A 420 65.525 -9.701 72.338 1.00 25.32 C ANISOU 878 CA GLY A 420 3828 2819 2975 1100 735 821 C ATOM 879 C GLY A 420 64.500 -9.445 71.251 1.00 23.39 C ANISOU 879 C GLY A 420 3569 2612 2708 1078 794 790 C ATOM 880 O GLY A 420 63.470 -8.818 71.487 1.00 24.74 O ANISOU 880 O GLY A 420 3810 2885 2706 1235 800 817 O ATOM 881 N MET A 421 64.778 -9.926 70.050 1.00 21.81 N ANISOU 881 N MET A 421 2542 3345 2400 387 -361 1165 N ATOM 882 CA MET A 421 63.906 -9.647 68.927 1.00 20.41 C ANISOU 882 CA MET A 421 2380 3146 2228 310 -244 997 C ATOM 883 C MET A 421 62.723 -10.615 68.815 1.00 19.56 C ANISOU 883 C MET A 421 2348 2837 2247 390 -83 925 C ATOM 884 O MET A 421 61.643 -10.237 68.349 1.00 17.99 O ANISOU 884 O MET A 421 2233 2580 2021 318 -23 817 O ATOM 885 CB MET A 421 64.712 -9.680 67.636 1.00 20.79 C ANISOU 885 CB MET A 421 2217 3345 2336 290 -201 909 C ATOM 886 CG MET A 421 63.842 -9.708 66.421 1.00 26.38 C ANISOU 886 CG MET A 421 2949 4005 3069 251 -74 730 C ATOM 887 SD MET A 421 63.368 -8.034 66.030 1.00 46.18 S ANISOU 887 SD MET A 421 5584 6595 5368 31 -179 687 S ATOM 888 CE MET A 421 64.864 -7.600 65.182 1.00 16.42 C ANISOU 888 CE MET A 421 1591 3087 1560 -53 -216 720 C ATOM 889 N VAL A 422 62.917 -11.864 69.232 1.00 19.89 N ANISOU 889 N VAL A 422 2356 2763 2439 533 -30 990 N ATOM 890 CA VAL A 422 61.892 -12.875 68.998 1.00 21.51 C ANISOU 890 CA VAL A 422 2612 2764 2798 586 109 928 C ATOM 891 C VAL A 422 60.602 -12.544 69.755 1.00 21.71 C ANISOU 891 C VAL A 422 2809 2692 2748 517 151 972 C ATOM 892 O VAL A 422 59.510 -12.844 69.272 1.00 21.00 O ANISOU 892 O VAL A 422 2743 2488 2749 482 254 879 O ATOM 893 CB VAL A 422 62.388 -14.300 69.365 1.00 24.05 C ANISOU 893 CB VAL A 422 2891 2948 3300 752 131 1008 C ATOM 894 CG1 VAL A 422 62.594 -14.460 70.872 1.00 26.42 C ANISOU 894 CG1 VAL A 422 3302 3201 3534 798 54 1223 C ATOM 895 CG2 VAL A 422 61.413 -15.343 68.833 1.00 25.73 C ANISOU 895 CG2 VAL A 422 3141 2938 3698 781 252 916 C ATOM 896 N GLU A 423 60.725 -11.890 70.909 1.00 20.54 N ANISOU 896 N GLU A 423 2775 2601 2427 500 68 1105 N ATOM 897 CA GLU A 423 59.553 -11.463 71.672 1.00 21.90 C ANISOU 897 CA GLU A 423 3105 2723 2494 449 119 1121 C ATOM 898 C GLU A 423 58.702 -10.498 70.858 1.00 19.21 C ANISOU 898 C GLU A 423 2778 2428 2094 357 143 977 C ATOM 899 O GLU A 423 57.476 -10.573 70.869 1.00 19.04 O ANISOU 899 O GLU A 423 2797 2328 2110 337 252 935 O ATOM 900 CB GLU A 423 59.971 -10.807 72.991 1.00 26.77 C ANISOU 900 CB GLU A 423 3838 3391 2941 397 -18 1123 C ATOM 901 N ILE A 424 59.360 -9.592 70.147 1.00 17.47 N ANISOU 901 N ILE A 424 2512 2337 1789 290 29 896 N ATOM 902 CA ILE A 424 58.659 -8.626 69.311 1.00 18.13 C ANISOU 902 CA ILE A 424 2623 2455 1809 194 13 747 C ATOM 903 C ILE A 424 58.082 -9.296 68.063 1.00 16.03 C ANISOU 903 C ILE A 424 2254 2113 1724 184 121 602 C ATOM 904 O ILE A 424 56.968 -8.977 67.643 1.00 14.71 O ANISOU 904 O ILE A 424 2123 1896 1572 141 158 499 O ATOM 905 CB ILE A 424 59.595 -7.471 68.916 1.00 18.51 C ANISOU 905 CB ILE A 424 2671 2652 1711 100 -153 728 C ATOM 906 CG1 ILE A 424 60.066 -6.750 70.180 1.00 24.77 C ANISOU 906 CG1 ILE A 424 3599 3390 2423 112 -254 700 C ATOM 907 CG2 ILE A 424 58.900 -6.500 67.967 1.00 17.16 C ANISOU 907 CG2 ILE A 424 2547 2490 1485 4 -185 573 C ATOM 908 CD1 ILE A 424 61.296 -5.915 69.991 1.00 28.92 C ANISOU 908 CD1 ILE A 424 4058 4007 2925 68 -365 669 C ATOM 909 N PHE A 425 58.833 -10.226 67.473 1.00 15.21 N ANISOU 909 N PHE A 425 2027 1997 1755 236 157 587 N ATOM 910 CA PHE A 425 58.284 -11.020 66.376 1.00 18.09 C ANISOU 910 CA PHE A 425 2327 2257 2289 248 248 444 C ATOM 911 C PHE A 425 56.994 -11.707 66.837 1.00 16.06 C ANISOU 911 C PHE A 425 2118 1821 2164 258 344 461 C ATOM 912 O PHE A 425 55.975 -11.672 66.139 1.00 15.27 O ANISOU 912 O PHE A 425 2016 1651 2134 204 374 337 O ATOM 913 CB PHE A 425 59.280 -12.075 65.874 1.00 20.75 C ANISOU 913 CB PHE A 425 2547 2584 2754 352 281 428 C ATOM 914 CG PHE A 425 60.200 -11.593 64.779 1.00 22.22 C ANISOU 914 CG PHE A 425 2637 2943 2862 328 251 333 C ATOM 915 CD1 PHE A 425 60.651 -10.282 64.744 1.00 21.23 C ANISOU 915 CD1 PHE A 425 2522 2998 2548 214 155 365 C ATOM 916 CD2 PHE A 425 60.623 -12.469 63.787 1.00 24.37 C ANISOU 916 CD2 PHE A 425 2817 3196 3245 420 319 216 C ATOM 917 CE1 PHE A 425 61.502 -9.853 63.740 1.00 21.91 C ANISOU 917 CE1 PHE A 425 2509 3257 2560 167 143 306 C ATOM 918 CE2 PHE A 425 61.469 -12.048 62.783 1.00 24.76 C ANISOU 918 CE2 PHE A 425 2771 3434 3202 404 324 138 C ATOM 919 CZ PHE A 425 61.915 -10.738 62.757 1.00 25.33 C ANISOU 919 CZ PHE A 425 2833 3701 3088 265 244 196 C ATOM 920 N ASP A 426 57.038 -12.311 68.023 1.00 15.03 N ANISOU 920 N ASP A 426 2026 1621 2063 318 383 626 N ATOM 921 CA ASP A 426 55.886 -13.047 68.542 1.00 18.59 C ANISOU 921 CA ASP A 426 2508 1912 2644 309 491 684 C ATOM 922 C ASP A 426 54.648 -12.156 68.664 1.00 17.06 C ANISOU 922 C ASP A 426 2352 1757 2373 234 524 636 C ATOM 923 O ASP A 426 53.542 -12.580 68.341 1.00 17.71 O ANISOU 923 O ASP A 426 2389 1734 2606 187 600 584 O ATOM 924 CB ASP A 426 56.213 -13.686 69.897 1.00 19.60 C ANISOU 924 CB ASP A 426 2700 1986 2759 376 522 901 C ATOM 925 CG ASP A 426 57.065 -14.944 69.761 1.00 26.32 C ANISOU 925 CG ASP A 426 3508 2717 3775 470 507 946 C ATOM 926 OD1 ASP A 426 57.082 -15.536 68.660 1.00 27.92 O ANISOU 926 OD1 ASP A 426 3637 2834 4137 484 513 803 O ATOM 927 OD2 ASP A 426 57.711 -15.352 70.756 1.00 28.57 O ANISOU 927 OD2 ASP A 426 3847 2984 4025 545 478 1119 O ATOM 928 N MET A 427 54.841 -10.919 69.107 1.00 15.98 N ANISOU 928 N MET A 427 2293 1766 2013 226 452 648 N ATOM 929 CA MET A 427 53.718 -9.995 69.228 1.00 17.97 C ANISOU 929 CA MET A 427 2589 2058 2180 192 469 585 C ATOM 930 C MET A 427 53.183 -9.599 67.854 1.00 15.94 C ANISOU 930 C MET A 427 2270 1791 1994 127 419 389 C ATOM 931 O MET A 427 51.970 -9.559 67.628 1.00 16.90 O ANISOU 931 O MET A 427 2349 1864 2207 102 472 320 O ATOM 932 CB MET A 427 54.134 -8.760 70.024 1.00 19.34 C ANISOU 932 CB MET A 427 2899 2361 2087 217 370 630 C ATOM 933 CG MET A 427 54.454 -9.074 71.470 1.00 23.19 C ANISOU 933 CG MET A 427 3475 2860 2478 283 406 808 C ATOM 934 SD MET A 427 54.646 -7.603 72.479 1.00 33.50 S ANISOU 934 SD MET A 427 4884 4286 3557 260 234 732 S ATOM 935 CE MET A 427 56.009 -6.796 71.648 1.00 22.20 C ANISOU 935 CE MET A 427 3416 2929 2090 164 20 666 C ATOM 936 N LEU A 428 54.094 -9.323 66.929 1.00 12.95 N ANISOU 936 N LEU A 428 1879 1467 1574 100 318 307 N ATOM 937 CA LEU A 428 53.707 -8.961 65.573 1.00 12.78 C ANISOU 937 CA LEU A 428 1829 1441 1586 37 259 129 C ATOM 938 C LEU A 428 52.947 -10.091 64.891 1.00 14.97 C ANISOU 938 C LEU A 428 2018 1567 2102 30 334 48 C ATOM 939 O LEU A 428 51.960 -9.848 64.201 1.00 15.36 O ANISOU 939 O LEU A 428 2050 1573 2215 -16 306 -75 O ATOM 940 CB LEU A 428 54.936 -8.578 64.751 1.00 11.25 C ANISOU 940 CB LEU A 428 1633 1353 1288 6 168 86 C ATOM 941 CG LEU A 428 55.556 -7.240 65.157 1.00 13.75 C ANISOU 941 CG LEU A 428 2044 1806 1376 -38 42 141 C ATOM 942 CD1 LEU A 428 56.979 -7.112 64.626 1.00 12.16 C ANISOU 942 CD1 LEU A 428 1790 1728 1101 -77 -16 167 C ATOM 943 CD2 LEU A 428 54.702 -6.065 64.692 1.00 12.60 C ANISOU 943 CD2 LEU A 428 1991 1664 1130 -98 -57 34 C ATOM 944 N LEU A 429 53.412 -11.320 65.091 1.00 15.46 N ANISOU 944 N LEU A 429 2035 1536 2303 77 405 115 N ATOM 945 CA LEU A 429 52.757 -12.495 64.524 1.00 16.55 C ANISOU 945 CA LEU A 429 2115 1492 2682 65 453 48 C ATOM 946 C LEU A 429 51.352 -12.686 65.093 1.00 20.19 C ANISOU 946 C LEU A 429 2537 1865 3271 13 524 99 C ATOM 947 O LEU A 429 50.427 -13.052 64.366 1.00 20.88 O ANISOU 947 O LEU A 429 2566 1841 3524 -47 508 -9 O ATOM 948 CB LEU A 429 53.596 -13.752 64.771 1.00 16.55 C ANISOU 948 CB LEU A 429 2102 1389 2799 144 496 127 C ATOM 949 CG LEU A 429 54.859 -13.910 63.918 1.00 19.21 C ANISOU 949 CG LEU A 429 2425 1790 3084 217 450 36 C ATOM 950 CD1 LEU A 429 55.712 -15.057 64.427 1.00 21.85 C ANISOU 950 CD1 LEU A 429 2744 2032 3524 332 484 138 C ATOM 951 CD2 LEU A 429 54.496 -14.122 62.459 1.00 18.24 C ANISOU 951 CD2 LEU A 429 2298 1604 3028 193 411 -180 C ATOM 952 N ALA A 430 51.197 -12.441 66.392 1.00 18.93 N ANISOU 952 N ALA A 430 2401 1761 3028 35 602 265 N ATOM 953 CA ALA A 430 49.889 -12.582 67.034 1.00 19.87 C ANISOU 953 CA ALA A 430 2460 1841 3248 -7 708 337 C ATOM 954 C ALA A 430 48.902 -11.543 66.497 1.00 18.14 C ANISOU 954 C ALA A 430 2199 1698 2994 -39 657 194 C ATOM 955 O ALA A 430 47.705 -11.813 66.369 1.00 18.11 O ANISOU 955 O ALA A 430 2082 1634 3163 -95 706 171 O ATOM 956 CB ALA A 430 50.016 -12.463 68.558 1.00 17.84 C ANISOU 956 CB ALA A 430 2266 1660 2853 44 814 543 C ATOM 957 N THR A 431 49.409 -10.352 66.192 1.00 19.88 N ANISOU 957 N THR A 431 2506 2044 3002 -7 546 108 N ATOM 958 CA THR A 431 48.577 -9.278 65.658 1.00 19.55 C ANISOU 958 CA THR A 431 2458 2062 2909 -17 462 -30 C ATOM 959 C THR A 431 48.156 -9.596 64.231 1.00 18.43 C ANISOU 959 C THR A 431 2255 1824 2926 -86 366 -200 C ATOM 960 O THR A 431 47.029 -9.312 63.837 1.00 16.56 O ANISOU 960 O THR A 431 1941 1565 2786 -110 329 -290 O ATOM 961 CB THR A 431 49.306 -7.920 65.690 1.00 18.26 C ANISOU 961 CB THR A 431 2438 2027 2473 19 337 -64 C ATOM 962 OG1 THR A 431 49.712 -7.634 67.031 1.00 22.35 O ANISOU 962 OG1 THR A 431 3039 2622 2832 86 398 82 O ATOM 963 CG2 THR A 431 48.394 -6.804 65.209 1.00 17.21 C ANISOU 963 CG2 THR A 431 2323 1928 2290 26 233 -199 C ATOM 964 N SER A 432 49.068 -10.191 63.462 1.00 14.96 N ANISOU 964 N SER A 432 1849 1331 2504 -102 321 -247 N ATOM 965 CA SER A 432 48.746 -10.642 62.116 1.00 18.88 C ANISOU 965 CA SER A 432 2320 1723 3131 -154 232 -414 C ATOM 966 C SER A 432 47.641 -11.696 62.148 1.00 19.08 C ANISOU 966 C SER A 432 2223 1584 3443 -207 283 -408 C ATOM 967 O SER A 432 46.719 -11.665 61.330 1.00 19.41 O ANISOU 967 O SER A 432 2212 1559 3606 -263 189 -538 O ATOM 968 CB SER A 432 49.992 -11.195 61.426 1.00 23.08 C ANISOU 968 CB SER A 432 2911 2241 3617 -129 212 -458 C ATOM 969 OG SER A 432 49.762 -11.358 60.039 1.00 29.05 O ANISOU 969 OG SER A 432 3691 2931 4414 -163 109 -643 O ATOM 970 N SER A 433 47.736 -12.618 63.104 1.00 19.02 N ANISOU 970 N SER A 433 2174 1506 3546 -202 414 -245 N ATOM 971 CA SER A 433 46.711 -13.637 63.307 1.00 21.35 C ANISOU 971 CA SER A 433 2349 1643 4120 -283 472 -190 C ATOM 972 C SER A 433 45.358 -13.028 63.656 1.00 19.67 C ANISOU 972 C SER A 433 2001 1501 3972 -326 507 -176 C ATOM 973 O SER A 433 44.318 -13.513 63.201 1.00 21.56 O ANISOU 973 O SER A 433 2113 1632 4449 -419 470 -226 O ATOM 974 CB SER A 433 47.132 -14.612 64.408 1.00 27.35 C ANISOU 974 CB SER A 433 3118 2328 4944 -272 610 21 C ATOM 975 OG SER A 433 48.320 -15.296 64.052 1.00 34.69 O ANISOU 975 OG SER A 433 4148 3175 5858 -211 568 -2 O ATOM 976 N ARG A 434 45.374 -11.972 64.466 1.00 18.77 N ANISOU 976 N ARG A 434 1913 1568 3652 -251 569 -114 N ATOM 977 CA ARG A 434 44.145 -11.278 64.854 1.00 19.53 C ANISOU 977 CA ARG A 434 1881 1762 3778 -243 616 -114 C ATOM 978 C ARG A 434 43.492 -10.606 63.640 1.00 17.60 C ANISOU 978 C ARG A 434 1598 1511 3579 -260 430 -326 C ATOM 979 O ARG A 434 42.270 -10.656 63.482 1.00 19.00 O ANISOU 979 O ARG A 434 1597 1673 3949 -304 424 -360 O ATOM 980 CB ARG A 434 44.436 -10.246 65.953 1.00 19.36 C ANISOU 980 CB ARG A 434 1948 1923 3486 -124 700 -30 C ATOM 981 CG ARG A 434 43.274 -9.322 66.317 1.00 24.65 C ANISOU 981 CG ARG A 434 2513 2718 4134 -59 738 -68 C ATOM 982 CD ARG A 434 42.079 -10.075 66.900 1.00 30.51 C ANISOU 982 CD ARG A 434 3023 3458 5113 -118 921 50 C ATOM 983 NE ARG A 434 41.037 -9.156 67.355 1.00 30.79 N ANISOU 983 NE ARG A 434 2941 3652 5106 -17 988 17 N ATOM 984 CZ ARG A 434 39.771 -9.502 67.556 1.00 33.47 C ANISOU 984 CZ ARG A 434 3016 4030 5670 -61 1109 63 C ATOM 985 NH1 ARG A 434 39.381 -10.750 67.338 1.00 36.36 N ANISOU 985 NH1 ARG A 434 3224 4266 6325 -234 1157 154 N ATOM 986 NH2 ARG A 434 38.891 -8.600 67.970 1.00 33.41 N ANISOU 986 NH2 ARG A 434 2898 4189 5607 70 1176 18 N ATOM 987 N PHE A 435 44.283 -10.004 62.760 1.00 16.03 N ANISOU 987 N PHE A 435 1559 1330 3202 -229 276 -454 N ATOM 988 CA PHE A 435 43.795 -9.420 61.547 1.00 18.46 C ANISOU 988 CA PHE A 435 1880 1611 3521 -252 75 -649 C ATOM 989 C PHE A 435 43.127 -10.481 60.671 1.00 18.18 C ANISOU 989 C PHE A 435 1743 1440 3725 -336 7 -707 C ATOM 990 O PHE A 435 42.151 -10.243 60.025 1.00 18.08 O ANISOU 990 O PHE A 435 1648 1441 3779 -338 -104 -778 O ATOM 991 CB PHE A 435 44.930 -8.838 60.722 1.00 20.92 C ANISOU 991 CB PHE A 435 2395 1967 3586 -231 -51 -730 C ATOM 992 CG PHE A 435 45.392 -7.487 61.159 1.00 26.06 C ANISOU 992 CG PHE A 435 3171 2753 3978 -163 -94 -720 C ATOM 993 CD1 PHE A 435 45.248 -7.062 62.426 1.00 25.38 C ANISOU 993 CD1 PHE A 435 3066 2759 3819 -87 22 -602 C ATOM 994 CD2 PHE A 435 46.005 -6.663 60.261 1.00 26.44 C ANISOU 994 CD2 PHE A 435 3380 2897 3767 -159 -225 -716 C ATOM 995 CE1 PHE A 435 45.693 -5.825 62.780 1.00 27.04 C ANISOU 995 CE1 PHE A 435 3423 3071 3779 -20 -50 -600 C ATOM 996 CE2 PHE A 435 46.435 -5.427 60.614 1.00 24.20 C ANISOU 996 CE2 PHE A 435 3221 2710 3265 -127 -273 -676 C ATOM 997 CZ PHE A 435 46.274 -5.015 61.877 1.00 23.90 C ANISOU 997 CZ PHE A 435 3178 2685 3217 -52 -235 -694 C ATOM 998 N ARG A 436 43.756 -11.634 60.635 1.00 18.87 N ANISOU 998 N ARG A 436 1870 1443 3858 -360 60 -640 N ATOM 999 CA ARG A 436 43.236 -12.739 59.841 1.00 23.99 C ANISOU 999 CA ARG A 436 2488 2000 4628 -401 -17 -661 C ATOM 1000 C ARG A 436 41.916 -13.242 60.414 1.00 25.99 C ANISOU 1000 C ARG A 436 2529 2178 5169 -483 42 -592 C ATOM 1001 O ARG A 436 40.967 -13.505 59.675 1.00 26.31 O ANISOU 1001 O ARG A 436 2504 2184 5310 -517 -76 -652 O ATOM 1002 CB ARG A 436 44.262 -13.873 59.780 1.00 28.33 C ANISOU 1002 CB ARG A 436 3139 2462 5165 -394 21 -619 C ATOM 1003 CG ARG A 436 43.995 -14.910 58.701 1.00 34.66 C ANISOU 1003 CG ARG A 436 3985 3166 6018 -419 -96 -688 C ATOM 1004 CD ARG A 436 45.126 -15.930 58.631 1.00 34.52 C ANISOU 1004 CD ARG A 436 4082 3056 5976 -383 -65 -676 C ATOM 1005 NE ARG A 436 46.429 -15.281 58.714 1.00 33.77 N ANISOU 1005 NE ARG A 436 4087 3067 5679 -301 -17 -686 N ATOM 1006 CZ ARG A 436 47.278 -15.425 59.728 1.00 33.57 C ANISOU 1006 CZ ARG A 436 4062 3017 5674 -266 106 -587 C ATOM 1007 NH1 ARG A 436 46.970 -16.216 60.747 1.00 36.32 N ANISOU 1007 NH1 ARG A 436 4340 3246 6214 -303 203 -446 N ATOM 1008 NH2 ARG A 436 48.439 -14.783 59.717 1.00 28.39 N ANISOU 1008 NH2 ARG A 436 3485 2459 4843 -196 133 -607 N ATOM 1009 N MET A 437 41.864 -13.365 61.738 1.00 24.59 N ANISOU 1009 N MET A 437 2248 1995 5100 -517 238 -436 N ATOM 1010 CA MET A 437 40.652 -13.799 62.421 1.00 25.26 C ANISOU 1010 CA MET A 437 2119 2072 5406 -595 342 -313 C ATOM 1011 C MET A 437 39.498 -12.826 62.180 1.00 25.44 C ANISOU 1011 C MET A 437 1976 2198 5492 -583 282 -404 C ATOM 1012 O MET A 437 38.343 -13.240 62.059 1.00 28.18 O ANISOU 1012 O MET A 437 2160 2527 6021 -646 256 -380 O ATOM 1013 CB MET A 437 40.909 -13.947 63.924 1.00 26.35 C ANISOU 1013 CB MET A 437 2215 2270 5526 -596 596 -86 C ATOM 1014 N MET A 438 39.819 -11.537 62.114 1.00 23.80 N ANISOU 1014 N MET A 438 1810 2098 5136 -503 244 -512 N ATOM 1015 CA MET A 438 38.819 -10.495 61.888 1.00 23.89 C ANISOU 1015 CA MET A 438 1681 2220 5176 -447 158 -619 C ATOM 1016 C MET A 438 38.452 -10.309 60.419 1.00 24.79 C ANISOU 1016 C MET A 438 1891 2268 5260 -431 -115 -793 C ATOM 1017 O MET A 438 37.482 -9.608 60.101 1.00 24.15 O ANISOU 1017 O MET A 438 1694 2241 5242 -388 -220 -879 O ATOM 1018 CB MET A 438 39.318 -9.157 62.428 1.00 26.81 C ANISOU 1018 CB MET A 438 2202 2767 5219 -273 191 -631 C ATOM 1019 CG MET A 438 39.501 -9.098 63.920 1.00 31.06 C ANISOU 1019 CG MET A 438 2726 3437 5636 -197 452 -442 C ATOM 1020 SD MET A 438 39.646 -7.379 64.440 1.00 29.78 S ANISOU 1020 SD MET A 438 2711 3462 5143 19 426 -509 S ATOM 1021 CE MET A 438 38.004 -6.795 64.020 1.00 22.68 C ANISOU 1021 CE MET A 438 1544 2624 4451 76 342 -636 C ATOM 1022 N ASN A 439 39.242 -10.910 59.531 1.00 25.66 N ANISOU 1022 N ASN A 439 2620 2570 4558 -949 -93 -151 N ATOM 1023 CA ASN A 439 39.136 -10.660 58.096 1.00 25.56 C ANISOU 1023 CA ASN A 439 2542 2680 4487 -892 -78 -439 C ATOM 1024 C ASN A 439 39.222 -9.161 57.789 1.00 22.14 C ANISOU 1024 C ASN A 439 2132 2530 3749 -761 -45 -427 C ATOM 1025 O ASN A 439 38.369 -8.606 57.094 1.00 22.95 O ANISOU 1025 O ASN A 439 2176 2857 3685 -759 -43 -528 O ATOM 1026 CB ASN A 439 37.835 -11.256 57.543 1.00 29.89 C ANISOU 1026 CB ASN A 439 3014 3305 5037 -1012 -88 -577 C ATOM 1027 CG ASN A 439 37.814 -11.314 56.026 1.00 33.80 C ANISOU 1027 CG ASN A 439 3459 3910 5472 -969 -94 -881 C ATOM 1028 OD1 ASN A 439 38.859 -11.280 55.378 1.00 35.64 O ANISOU 1028 OD1 ASN A 439 3715 4100 5729 -873 -78 -1019 O ATOM 1029 ND2 ASN A 439 36.619 -11.401 55.454 1.00 37.18 N ANISOU 1029 ND2 ASN A 439 3814 4508 5804 -1043 -114 -983 N ATOM 1030 N LEU A 440 40.256 -8.515 58.325 1.00 19.40 N ANISOU 1030 N LEU A 440 1863 2156 3350 -656 -34 -292 N ATOM 1031 CA LEU A 440 40.490 -7.092 58.098 1.00 18.29 C ANISOU 1031 CA LEU A 440 1758 2225 2967 -538 -6 -263 C ATOM 1032 C LEU A 440 40.578 -6.779 56.611 1.00 21.57 C ANISOU 1032 C LEU A 440 2144 2783 3270 -481 1 -468 C ATOM 1033 O LEU A 440 41.336 -7.419 55.884 1.00 23.59 O ANISOU 1033 O LEU A 440 2389 2950 3625 -468 11 -628 O ATOM 1034 CB LEU A 440 41.776 -6.634 58.788 1.00 17.38 C ANISOU 1034 CB LEU A 440 1722 2025 2859 -455 -2 -126 C ATOM 1035 CG LEU A 440 42.036 -5.139 58.596 1.00 17.73 C ANISOU 1035 CG LEU A 440 1807 2249 2682 -352 27 -91 C ATOM 1036 CD1 LEU A 440 41.075 -4.334 59.459 1.00 23.32 C ANISOU 1036 CD1 LEU A 440 2517 3082 3262 -372 41 27 C ATOM 1037 CD2 LEU A 440 43.472 -4.764 58.885 1.00 21.02 C ANISOU 1037 CD2 LEU A 440 2277 2587 3122 -278 31 -27 C ATOM 1038 N GLN A 441 39.799 -5.796 56.171 1.00 20.60 N ANISOU 1038 N GLN A 441 1999 2887 2940 -449 -7 -464 N ATOM 1039 CA GLN A 441 39.770 -5.384 54.768 1.00 21.22 C ANISOU 1039 CA GLN A 441 2057 3150 2856 -414 -22 -608 C ATOM 1040 C GLN A 441 40.749 -4.244 54.504 1.00 18.79 C ANISOU 1040 C GLN A 441 1826 2911 2401 -308 5 -525 C ATOM 1041 O GLN A 441 41.085 -3.487 55.414 1.00 17.54 O ANISOU 1041 O GLN A 441 1724 2702 2238 -252 21 -357 O ATOM 1042 CB GLN A 441 38.359 -4.948 54.367 1.00 19.51 C ANISOU 1042 CB GLN A 441 1760 3141 2512 -437 -80 -619 C ATOM 1043 CG GLN A 441 37.314 -6.018 54.571 1.00 23.40 C ANISOU 1043 CG GLN A 441 2154 3592 3143 -566 -103 -708 C ATOM 1044 CD GLN A 441 37.526 -7.193 53.650 1.00 28.33 C ANISOU 1044 CD GLN A 441 2747 4159 3858 -654 -113 -950 C ATOM 1045 OE1 GLN A 441 37.389 -7.069 52.434 1.00 34.95 O ANISOU 1045 OE1 GLN A 441 3553 5184 4543 -659 -148 -1108 O ATOM 1046 NE2 GLN A 441 37.879 -8.340 54.220 1.00 27.48 N ANISOU 1046 NE2 GLN A 441 2647 3791 4004 -728 -87 -984 N ATOM 1047 N GLY A 442 41.179 -4.120 53.252 1.00 18.19 N ANISOU 1047 N GLY A 442 1750 2967 2194 -302 15 -651 N ATOM 1048 CA GLY A 442 42.115 -3.082 52.861 1.00 18.58 C ANISOU 1048 CA GLY A 442 1866 3097 2097 -237 49 -571 C ATOM 1049 C GLY A 442 41.616 -1.681 53.164 1.00 18.40 C ANISOU 1049 C GLY A 442 1885 3158 1949 -169 4 -364 C ATOM 1050 O GLY A 442 42.381 -0.820 53.591 1.00 17.96 O ANISOU 1050 O GLY A 442 1896 3047 1880 -115 34 -235 O ATOM 1051 N GLU A 443 40.326 -1.450 52.952 1.00 18.89 N ANISOU 1051 N GLU A 443 1891 3339 1946 -171 -73 -347 N ATOM 1052 CA GLU A 443 39.751 -0.135 53.213 1.00 18.32 C ANISOU 1052 CA GLU A 443 1833 3322 1807 -85 -126 -173 C ATOM 1053 C GLU A 443 39.747 0.174 54.710 1.00 14.70 C ANISOU 1053 C GLU A 443 1394 2705 1488 -43 -84 -77 C ATOM 1054 O GLU A 443 39.904 1.331 55.113 1.00 17.07 O ANISOU 1054 O GLU A 443 1741 2974 1770 36 -86 46 O ATOM 1055 CB GLU A 443 38.331 -0.045 52.643 1.00 21.38 C ANISOU 1055 CB GLU A 443 2117 3878 2127 -85 -232 -193 C ATOM 1056 CG GLU A 443 38.246 -0.238 51.135 1.00 29.69 C ANISOU 1056 CG GLU A 443 3151 5144 2986 -140 -298 -278 C ATOM 1057 CD GLU A 443 37.988 -1.683 50.729 1.00 37.76 C ANISOU 1057 CD GLU A 443 4100 6199 4047 -261 -286 -518 C ATOM 1058 OE1 GLU A 443 38.494 -2.605 51.409 1.00 35.56 O ANISOU 1058 OE1 GLU A 443 3833 5731 3947 -303 -198 -610 O ATOM 1059 OE2 GLU A 443 37.267 -1.892 49.729 1.00 44.88 O ANISOU 1059 OE2 GLU A 443 4932 7310 4812 -317 -377 -611 O ATOM 1060 N GLU A 444 39.566 -0.852 55.536 1.00 17.71 N ANISOU 1060 N GLU A 444 1740 2987 2002 -110 -48 -133 N ATOM 1061 CA GLU A 444 39.653 -0.672 56.982 1.00 17.70 C ANISOU 1061 CA GLU A 444 1765 2873 2087 -105 -2 -42 C ATOM 1062 C GLU A 444 41.097 -0.406 57.409 1.00 16.67 C ANISOU 1062 C GLU A 444 1734 2623 1976 -81 38 22 C ATOM 1063 O GLU A 444 41.362 0.428 58.286 1.00 16.48 O ANISOU 1063 O GLU A 444 1756 2560 1945 -43 58 111 O ATOM 1064 CB GLU A 444 39.103 -1.898 57.710 1.00 18.13 C ANISOU 1064 CB GLU A 444 1763 2865 2261 -213 16 -78 C ATOM 1065 CG GLU A 444 37.610 -2.118 57.526 1.00 19.36 C ANISOU 1065 CG GLU A 444 1794 3145 2416 -256 -12 -137 C ATOM 1066 CD GLU A 444 37.136 -3.449 58.082 1.00 21.45 C ANISOU 1066 CD GLU A 444 2005 3334 2811 -402 8 -170 C ATOM 1067 OE1 GLU A 444 37.925 -4.417 58.074 1.00 19.31 O ANISOU 1067 OE1 GLU A 444 1784 2906 2647 -460 12 -191 O ATOM 1068 OE2 GLU A 444 35.975 -3.528 58.531 1.00 21.38 O ANISOU 1068 OE2 GLU A 444 1891 3413 2818 -461 21 -172 O ATOM 1069 N PHE A 445 42.030 -1.116 56.785 1.00 16.46 N ANISOU 1069 N PHE A 445 1723 2546 1985 -108 51 -50 N ATOM 1070 CA PHE A 445 43.443 -0.957 57.102 1.00 14.22 C ANISOU 1070 CA PHE A 445 1498 2163 1743 -87 84 -8 C ATOM 1071 C PHE A 445 43.926 0.481 56.901 1.00 14.98 C ANISOU 1071 C PHE A 445 1653 2311 1727 -27 93 80 C ATOM 1072 O PHE A 445 44.577 1.046 57.782 1.00 12.81 O ANISOU 1072 O PHE A 445 1425 1961 1482 -11 106 162 O ATOM 1073 CB PHE A 445 44.291 -1.921 56.263 1.00 14.86 C ANISOU 1073 CB PHE A 445 1547 2204 1894 -111 109 -145 C ATOM 1074 CG PHE A 445 45.748 -1.542 56.189 1.00 15.96 C ANISOU 1074 CG PHE A 445 1712 2305 2049 -79 151 -128 C ATOM 1075 CD1 PHE A 445 46.590 -1.717 57.285 1.00 12.52 C ANISOU 1075 CD1 PHE A 445 1286 1725 1745 -68 140 -47 C ATOM 1076 CD2 PHE A 445 46.276 -1.010 55.026 1.00 15.81 C ANISOU 1076 CD2 PHE A 445 1694 2415 1899 -75 196 -186 C ATOM 1077 CE1 PHE A 445 47.932 -1.361 57.210 1.00 11.51 C ANISOU 1077 CE1 PHE A 445 1152 1575 1647 -44 171 -42 C ATOM 1078 CE2 PHE A 445 47.618 -0.653 54.944 1.00 16.68 C ANISOU 1078 CE2 PHE A 445 1804 2508 2027 -65 250 -177 C ATOM 1079 CZ PHE A 445 48.447 -0.829 56.039 1.00 15.53 C ANISOU 1079 CZ PHE A 445 1650 2209 2042 -44 237 -115 C ATOM 1080 N VAL A 446 43.603 1.083 55.760 1.00 13.71 N ANISOU 1080 N VAL A 446 1494 2278 1438 -7 76 73 N ATOM 1081 CA VAL A 446 44.096 2.431 55.498 1.00 14.64 C ANISOU 1081 CA VAL A 446 1676 2415 1472 33 77 185 C ATOM 1082 C VAL A 446 43.474 3.442 56.461 1.00 14.19 C ANISOU 1082 C VAL A 446 1642 2295 1453 94 49 279 C ATOM 1083 O VAL A 446 44.137 4.400 56.841 1.00 13.05 O ANISOU 1083 O VAL A 446 1557 2076 1324 115 63 355 O ATOM 1084 CB VAL A 446 43.868 2.890 54.022 1.00 13.86 C ANISOU 1084 CB VAL A 446 1582 2478 1205 25 45 205 C ATOM 1085 CG1 VAL A 446 44.671 2.015 53.071 1.00 14.37 C ANISOU 1085 CG1 VAL A 446 1622 2631 1208 -47 105 71 C ATOM 1086 CG2 VAL A 446 42.392 2.916 53.642 1.00 14.58 C ANISOU 1086 CG2 VAL A 446 1618 2675 1246 54 -44 206 C ATOM 1087 N CYS A 447 42.224 3.227 56.868 1.00 13.52 N ANISOU 1087 N CYS A 447 1497 2243 1398 115 20 251 N ATOM 1088 CA CYS A 447 41.607 4.103 57.866 1.00 14.04 C ANISOU 1088 CA CYS A 447 1557 2263 1515 174 20 287 C ATOM 1089 C CYS A 447 42.356 4.019 59.198 1.00 11.70 C ANISOU 1089 C CYS A 447 1305 1871 1270 134 75 286 C ATOM 1090 O CYS A 447 42.616 5.037 59.841 1.00 11.44 O ANISOU 1090 O CYS A 447 1315 1776 1255 169 89 311 O ATOM 1091 CB CYS A 447 40.135 3.747 58.085 1.00 14.04 C ANISOU 1091 CB CYS A 447 1447 2346 1540 187 0 230 C ATOM 1092 SG CYS A 447 39.011 4.221 56.758 1.00 19.21 S ANISOU 1092 SG CYS A 447 2022 3131 2147 263 -108 251 S ATOM 1093 N LEU A 448 42.693 2.798 59.613 1.00 10.71 N ANISOU 1093 N LEU A 448 1168 1729 1175 56 94 259 N ATOM 1094 CA LEU A 448 43.409 2.586 60.869 1.00 11.91 C ANISOU 1094 CA LEU A 448 1357 1813 1357 4 116 290 C ATOM 1095 C LEU A 448 44.787 3.234 60.856 1.00 13.88 C ANISOU 1095 C LEU A 448 1670 1994 1611 14 115 328 C ATOM 1096 O LEU A 448 45.231 3.808 61.855 1.00 8.63 O ANISOU 1096 O LEU A 448 1043 1298 939 -2 120 349 O ATOM 1097 CB LEU A 448 43.555 1.091 61.156 1.00 13.03 C ANISOU 1097 CB LEU A 448 1471 1918 1563 -77 105 293 C ATOM 1098 CG LEU A 448 42.286 0.341 61.540 1.00 16.09 C ANISOU 1098 CG LEU A 448 1795 2358 1961 -137 114 276 C ATOM 1099 CD1 LEU A 448 42.633 -1.110 61.816 1.00 16.65 C ANISOU 1099 CD1 LEU A 448 1856 2334 2137 -225 89 310 C ATOM 1100 CD2 LEU A 448 41.629 0.997 62.764 1.00 19.62 C ANISOU 1100 CD2 LEU A 448 2237 2879 2339 -158 155 296 C ATOM 1101 N LYS A 449 45.466 3.135 59.718 1.00 12.87 N ANISOU 1101 N LYS A 449 1544 1864 1483 25 115 321 N ATOM 1102 CA LYS A 449 46.806 3.685 59.603 1.00 14.44 C ANISOU 1102 CA LYS A 449 1777 2016 1694 15 129 351 C ATOM 1103 C LYS A 449 46.780 5.210 59.721 1.00 12.56 C ANISOU 1103 C LYS A 449 1597 1750 1426 45 129 400 C ATOM 1104 O LYS A 449 47.657 5.807 60.354 1.00 12.40 O ANISOU 1104 O LYS A 449 1608 1667 1435 17 133 419 O ATOM 1105 CB LYS A 449 47.450 3.251 58.284 1.00 13.80 C ANISOU 1105 CB LYS A 449 1666 1978 1598 4 156 311 C ATOM 1106 CG LYS A 449 48.938 3.530 58.215 1.00 16.47 C ANISOU 1106 CG LYS A 449 2000 2284 1974 -25 187 323 C ATOM 1107 CD LYS A 449 49.608 2.696 57.134 1.00 19.06 C ANISOU 1107 CD LYS A 449 2259 2670 2314 -44 238 227 C ATOM 1108 CE LYS A 449 48.993 2.964 55.783 1.00 20.94 C ANISOU 1108 CE LYS A 449 2511 3042 2401 -54 264 208 C ATOM 1109 NZ LYS A 449 49.955 2.610 54.702 1.00 22.52 N ANISOU 1109 NZ LYS A 449 2652 3342 2561 -101 347 112 N ATOM 1110 N ASER A 450 45.766 5.829 59.124 0.66 10.59 N ANISOU 1110 N ASER A 450 1351 1532 1142 101 112 417 N ATOM 1111 N BSER A 450 45.777 5.851 59.135 0.34 11.16 N ANISOU 1111 N BSER A 450 1424 1602 1214 101 112 418 N ATOM 1112 CA ASER A 450 45.616 7.276 59.202 0.66 12.55 C ANISOU 1112 CA ASER A 450 1646 1706 1415 147 97 467 C ATOM 1113 CA BSER A 450 45.703 7.303 59.234 0.34 12.38 C ANISOU 1113 CA BSER A 450 1628 1679 1395 143 99 468 C ATOM 1114 C ASER A 450 45.234 7.715 60.609 0.66 11.69 C ANISOU 1114 C ASER A 450 1539 1544 1357 163 110 401 C ATOM 1115 C BSER A 450 45.235 7.733 60.625 0.34 11.78 C ANISOU 1115 C BSER A 450 1552 1555 1371 163 110 400 C ATOM 1116 O ASER A 450 45.643 8.782 61.062 0.66 11.81 O ANISOU 1116 O ASER A 450 1601 1461 1426 167 113 396 O ATOM 1117 O BSER A 450 45.592 8.815 61.089 0.34 11.92 O ANISOU 1117 O BSER A 450 1614 1473 1442 170 113 394 O ATOM 1118 CB ASER A 450 44.577 7.771 58.198 0.66 15.95 C ANISOU 1118 CB ASER A 450 2063 2177 1822 219 47 522 C ATOM 1119 CB BSER A 450 44.789 7.883 58.155 0.34 15.42 C ANISOU 1119 CB BSER A 450 2008 2098 1755 211 50 534 C ATOM 1120 OG ASER A 450 45.125 7.827 56.896 0.66 18.08 O ANISOU 1120 OG ASER A 450 2360 2504 2007 182 36 606 O ATOM 1121 OG BSER A 450 43.471 7.388 58.278 0.34 16.71 O ANISOU 1121 OG BSER A 450 2096 2334 1918 264 26 477 O ATOM 1122 N ILE A 451 44.442 6.894 61.290 1.00 11.25 N ANISOU 1122 N ILE A 451 1430 1562 1282 155 125 338 N ATOM 1123 CA ILE A 451 44.054 7.176 62.674 1.00 12.45 C ANISOU 1123 CA ILE A 451 1573 1723 1434 140 159 258 C ATOM 1124 C ILE A 451 45.298 7.188 63.561 1.00 12.16 C ANISOU 1124 C ILE A 451 1590 1655 1375 54 160 261 C ATOM 1125 O ILE A 451 45.478 8.103 64.369 1.00 11.95 O ANISOU 1125 O ILE A 451 1593 1591 1356 45 176 193 O ATOM 1126 CB ILE A 451 43.019 6.159 63.202 1.00 13.72 C ANISOU 1126 CB ILE A 451 1660 2000 1552 107 185 218 C ATOM 1127 CG1 ILE A 451 41.658 6.436 62.557 1.00 16.14 C ANISOU 1127 CG1 ILE A 451 1884 2352 1898 199 180 182 C ATOM 1128 CG2 ILE A 451 42.896 6.242 64.725 1.00 13.71 C ANISOU 1128 CG2 ILE A 451 1658 2059 1491 39 236 149 C ATOM 1129 CD1 ILE A 451 40.615 5.361 62.806 1.00 19.04 C ANISOU 1129 CD1 ILE A 451 2157 2840 2236 148 205 148 C ATOM 1130 N ILE A 452 46.172 6.202 63.377 1.00 11.26 N ANISOU 1130 N ILE A 452 1475 1551 1252 -4 135 324 N ATOM 1131 CA ILE A 452 47.421 6.151 64.135 1.00 11.83 C ANISOU 1131 CA ILE A 452 1573 1602 1321 -77 108 344 C ATOM 1132 C ILE A 452 48.239 7.432 63.933 1.00 11.15 C ANISOU 1132 C ILE A 452 1529 1430 1277 -76 109 330 C ATOM 1133 O ILE A 452 48.713 8.023 64.904 1.00 11.81 O ANISOU 1133 O ILE A 452 1638 1504 1346 -129 98 281 O ATOM 1134 CB ILE A 452 48.275 4.928 63.746 1.00 12.49 C ANISOU 1134 CB ILE A 452 1619 1678 1448 -106 72 409 C ATOM 1135 CG1 ILE A 452 47.641 3.636 64.262 1.00 10.12 C ANISOU 1135 CG1 ILE A 452 1288 1420 1136 -140 52 441 C ATOM 1136 CG2 ILE A 452 49.702 5.059 64.301 1.00 13.19 C ANISOU 1136 CG2 ILE A 452 1706 1739 1567 -161 26 436 C ATOM 1137 CD1 ILE A 452 48.331 2.376 63.728 1.00 15.91 C ANISOU 1137 CD1 ILE A 452 1973 2097 1977 -142 14 481 C ATOM 1138 N LEU A 453 48.384 7.870 62.681 1.00 8.53 N ANISOU 1138 N LEU A 453 1206 1046 989 -35 121 374 N ATOM 1139 CA LEU A 453 49.150 9.081 62.389 1.00 11.52 C ANISOU 1139 CA LEU A 453 1629 1326 1424 -57 123 394 C ATOM 1140 C LEU A 453 48.579 10.284 63.133 1.00 14.03 C ANISOU 1140 C LEU A 453 1987 1557 1787 -30 126 315 C ATOM 1141 O LEU A 453 49.314 11.045 63.764 1.00 13.83 O ANISOU 1141 O LEU A 453 1990 1460 1803 -92 120 264 O ATOM 1142 CB LEU A 453 49.178 9.362 60.881 1.00 9.40 C ANISOU 1142 CB LEU A 453 1371 1043 1159 -33 136 488 C ATOM 1143 CG LEU A 453 49.712 10.732 60.451 1.00 10.95 C ANISOU 1143 CG LEU A 453 1624 1115 1422 -65 137 553 C ATOM 1144 CD1 LEU A 453 51.207 10.855 60.772 1.00 14.88 C ANISOU 1144 CD1 LEU A 453 2107 1596 1953 -177 152 546 C ATOM 1145 CD2 LEU A 453 49.442 10.982 58.960 1.00 11.15 C ANISOU 1145 CD2 LEU A 453 1669 1163 1404 -48 136 685 C ATOM 1146 N LEU A 454 47.260 10.432 63.082 1.00 12.01 N ANISOU 1146 N LEU A 454 1717 1308 1540 60 136 278 N ATOM 1147 CA LEU A 454 46.612 11.607 63.660 1.00 11.62 C ANISOU 1147 CA LEU A 454 1681 1156 1579 116 148 171 C ATOM 1148 C LEU A 454 46.400 11.523 65.177 1.00 13.21 C ANISOU 1148 C LEU A 454 1864 1438 1716 69 187 3 C ATOM 1149 O LEU A 454 46.342 12.554 65.851 1.00 16.60 O ANISOU 1149 O LEU A 454 2310 1781 2216 73 207 -137 O ATOM 1150 CB LEU A 454 45.269 11.847 62.971 1.00 12.17 C ANISOU 1150 CB LEU A 454 1708 1206 1708 248 136 189 C ATOM 1151 CG LEU A 454 45.375 12.256 61.501 1.00 17.42 C ANISOU 1151 CG LEU A 454 2404 1793 2421 289 80 364 C ATOM 1152 CD1 LEU A 454 44.012 12.271 60.859 1.00 20.71 C ANISOU 1152 CD1 LEU A 454 2758 2240 2872 415 37 396 C ATOM 1153 CD2 LEU A 454 46.039 13.619 61.384 1.00 21.14 C ANISOU 1153 CD2 LEU A 454 2948 2052 3031 274 58 407 C ATOM 1154 N ASN A 455 46.284 10.313 65.713 1.00 11.66 N ANISOU 1154 N ASN A 455 1634 1409 1386 12 196 14 N ATOM 1155 CA ASN A 455 45.975 10.148 67.138 1.00 12.43 C ANISOU 1155 CA ASN A 455 1715 1637 1370 -59 235 -115 C ATOM 1156 C ASN A 455 47.175 10.018 68.074 1.00 14.53 C ANISOU 1156 C ASN A 455 2019 1958 1542 -193 194 -120 C ATOM 1157 O ASN A 455 47.147 10.524 69.193 1.00 16.25 O ANISOU 1157 O ASN A 455 2247 2246 1681 -259 220 -269 O ATOM 1158 CB ASN A 455 45.076 8.921 67.349 1.00 17.61 C ANISOU 1158 CB ASN A 455 2313 2453 1923 -76 261 -74 C ATOM 1159 CG ASN A 455 44.783 8.660 68.820 1.00 16.98 C ANISOU 1159 CG ASN A 455 2221 2551 1679 -187 308 -170 C ATOM 1160 OD1 ASN A 455 44.101 9.449 69.476 1.00 18.09 O ANISOU 1160 OD1 ASN A 455 2332 2736 1804 -171 386 -355 O ATOM 1161 ND2 ASN A 455 45.298 7.553 69.344 1.00 14.01 N ANISOU 1161 ND2 ASN A 455 1861 2281 1182 -303 261 -44 N ATOM 1162 N SER A 456 48.218 9.328 67.632 1.00 13.59 N ANISOU 1162 N SER A 456 1907 1827 1431 -234 127 25 N ATOM 1163 CA SER A 456 49.217 8.846 68.575 1.00 18.20 C ANISOU 1163 CA SER A 456 2493 2505 1917 -354 59 57 C ATOM 1164 C SER A 456 49.902 9.973 69.341 1.00 18.48 C ANISOU 1164 C SER A 456 2559 2520 1942 -430 44 -79 C ATOM 1165 O SER A 456 50.179 9.835 70.534 1.00 22.17 O ANISOU 1165 O SER A 456 3031 3131 2261 -540 6 -130 O ATOM 1166 CB SER A 456 50.243 7.975 67.853 1.00 22.34 C ANISOU 1166 CB SER A 456 2985 2991 2512 -356 -9 213 C ATOM 1167 OG SER A 456 49.656 6.721 67.545 1.00 20.90 O ANISOU 1167 OG SER A 456 2773 2851 2318 -324 -11 310 O ATOM 1168 N GLY A 457 50.131 11.099 68.681 1.00 13.54 N ANISOU 1168 N GLY A 457 1957 1721 1466 -386 67 -137 N ATOM 1169 CA GLY A 457 50.787 12.214 69.337 1.00 16.83 C ANISOU 1169 CA GLY A 457 2401 2081 1913 -468 53 -286 C ATOM 1170 C GLY A 457 49.874 13.402 69.582 1.00 19.43 C ANISOU 1170 C GLY A 457 2756 2302 2323 -411 129 -491 C ATOM 1171 O GLY A 457 50.341 14.489 69.927 1.00 22.78 O ANISOU 1171 O GLY A 457 3208 2610 2837 -464 125 -638 O ATOM 1172 N VAL A 458 48.571 13.199 69.419 1.00 21.26 N ANISOU 1172 N VAL A 458 2964 2562 2550 -302 196 -518 N ATOM 1173 CA VAL A 458 47.640 14.323 69.424 1.00 21.69 C ANISOU 1173 CA VAL A 458 3013 2475 2753 -200 263 -702 C ATOM 1174 C VAL A 458 47.411 14.918 70.815 1.00 28.04 C ANISOU 1174 C VAL A 458 3807 3371 3475 -273 322 -1000 C ATOM 1175 O VAL A 458 47.085 16.100 70.930 1.00 31.15 O ANISOU 1175 O VAL A 458 4201 3587 4047 -214 363 -1205 O ATOM 1176 CB VAL A 458 46.271 13.927 68.795 1.00 27.35 C ANISOU 1176 CB VAL A 458 3672 3212 3508 -52 309 -651 C ATOM 1177 CG1 VAL A 458 45.426 13.104 69.759 1.00 25.40 C ANISOU 1177 CG1 VAL A 458 3365 3226 3061 -94 380 -746 C ATOM 1178 CG2 VAL A 458 45.517 15.165 68.332 1.00 30.90 C ANISOU 1178 CG2 VAL A 458 4103 3429 4207 96 331 -758 C ATOM 1179 N TYR A 459 47.558 14.136 71.853 1.00 23.21 N ANISOU 1179 N TYR A 459 3187 3030 2600 -407 323 -1035 N ATOM 1180 CA TYR A 459 47.369 14.708 73.166 1.00 30.41 C ANISOU 1180 CA TYR A 459 4091 4069 3396 -497 389 -1345 C ATOM 1181 C TYR A 459 48.658 15.364 73.655 1.00 34.06 C ANISOU 1181 C TYR A 459 4602 4493 3845 -639 308 -1427 C ATOM 1182 O TYR A 459 48.590 16.273 74.438 1.00 38.64 O ANISOU 1182 O TYR A 459 5186 5085 4412 -706 353 -1732 O ATOM 1183 CB TYR A 459 46.689 13.752 74.152 1.00 33.94 C ANISOU 1183 CB TYR A 459 4502 4861 3532 -596 442 -1358 C ATOM 1184 CG TYR A 459 45.324 13.415 73.647 1.00 39.99 C ANISOU 1184 CG TYR A 459 5197 5636 4362 -459 537 -1330 C ATOM 1185 CD2 TYR A 459 44.834 12.162 73.701 1.00 39.63 C ANISOU 1185 CD2 TYR A 459 5123 5797 4139 -505 545 -1144 C ATOM 1186 CE2 TYR A 459 43.610 11.865 73.193 1.00 41.51 C ANISOU 1186 CE2 TYR A 459 5278 6042 4453 -392 626 -1129 C ATOM 1187 CZ TYR A 459 42.842 12.822 72.583 1.00 46.94 C ANISOU 1187 CZ TYR A 459 5905 6533 5397 -210 681 -1283 C ATOM 1188 N THR A 460 49.813 15.026 73.081 1.00 35.87 N ANISOU 1188 N THR A 460 4855 4668 4105 -681 194 -1180 N ATOM 1189 CA THR A 460 51.041 15.788 73.302 1.00 37.83 C ANISOU 1189 CA THR A 460 5126 4859 4390 -812 104 -1228 C ATOM 1190 C THR A 460 50.970 17.150 72.642 1.00 41.48 C ANISOU 1190 C THR A 460 5616 4979 5164 -756 131 -1344 C ATOM 1191 O THR A 460 50.289 18.049 73.110 1.00 46.83 O ANISOU 1191 O THR A 460 6298 5540 5955 -699 213 -1600 O ATOM 1192 CB THR A 460 52.345 15.112 72.814 1.00 20.00 C ATOM 1193 OG1 THR A 460 52.176 13.737 72.592 1.00 20.00 O ATOM 1194 CG2 THR A 460 53.470 15.242 73.816 1.00 20.00 C ATOM 1195 N ASP A 473 41.301 20.680 67.769 1.00 46.70 N ANISOU 1195 N ASP A 473 5832 4424 7488 859 343 -1360 N ATOM 1196 CA ASP A 473 39.922 20.371 67.405 1.00 46.23 C ANISOU 1196 CA ASP A 473 5633 4466 7465 1014 344 -1332 C ATOM 1197 C ASP A 473 39.833 19.982 65.936 1.00 45.01 C ANISOU 1197 C ASP A 473 5504 4250 7346 1093 215 -982 C ATOM 1198 O ASP A 473 39.052 19.106 65.564 1.00 44.74 O ANISOU 1198 O ASP A 473 5374 4403 7223 1152 215 -911 O ATOM 1199 CB ASP A 473 39.007 21.562 67.694 1.00 49.53 C ANISOU 1199 CB ASP A 473 5959 4736 8125 1146 349 -1496 C ATOM 1200 N HIS A 474 40.633 20.652 65.112 1.00 47.16 N ANISOU 1200 N HIS A 474 6135 3623 8159 -304 668 123 N ATOM 1201 CA HIS A 474 40.754 20.328 63.695 1.00 45.20 C ANISOU 1201 CA HIS A 474 5914 3443 7816 -206 663 548 C ATOM 1202 C HIS A 474 41.110 18.856 63.516 1.00 37.83 C ANISOU 1202 C HIS A 474 4908 2957 6508 -232 606 602 C ATOM 1203 O HIS A 474 40.470 18.140 62.746 1.00 35.16 O ANISOU 1203 O HIS A 474 4572 2814 5974 -62 568 775 O ATOM 1204 CB HIS A 474 41.807 21.228 63.037 1.00 49.50 C ANISOU 1204 CB HIS A 474 6502 3710 8594 -370 742 778 C ATOM 1205 CG HIS A 474 42.260 20.757 61.689 1.00 49.46 C ANISOU 1205 CG HIS A 474 6503 3883 8406 -353 759 1178 C ATOM 1206 ND1 HIS A 474 41.404 20.622 60.617 1.00 48.60 N ANISOU 1206 ND1 HIS A 474 6439 3874 8154 -131 718 1448 N ATOM 1207 CD2 HIS A 474 43.487 20.401 61.237 1.00 51.08 C ANISOU 1207 CD2 HIS A 474 6658 4274 8475 -533 796 1298 C ATOM 1208 CE1 HIS A 474 42.082 20.195 59.566 1.00 49.61 C ANISOU 1208 CE1 HIS A 474 6558 4241 8049 -191 739 1691 C ATOM 1209 NE2 HIS A 474 43.348 20.055 59.915 1.00 50.55 N ANISOU 1209 NE2 HIS A 474 6619 4406 8181 -421 797 1603 N ATOM 1210 N ILE A 475 42.124 18.405 64.248 1.00 35.80 N ANISOU 1210 N ILE A 475 4574 2857 6171 -447 593 445 N ATOM 1211 CA ILE A 475 42.548 17.013 64.182 1.00 32.34 C ANISOU 1211 CA ILE A 475 4045 2794 5449 -470 543 488 C ATOM 1212 C ILE A 475 41.426 16.075 64.620 1.00 26.88 C ANISOU 1212 C ILE A 475 3331 2332 4551 -310 467 364 C ATOM 1213 O ILE A 475 41.210 15.019 64.021 1.00 23.15 O ANISOU 1213 O ILE A 475 2829 2085 3882 -214 439 489 O ATOM 1214 CB ILE A 475 43.788 16.751 65.055 1.00 35.61 C ANISOU 1214 CB ILE A 475 4348 3328 5853 -720 517 345 C ATOM 1215 CG1 ILE A 475 44.930 17.689 64.665 1.00 40.78 C ANISOU 1215 CG1 ILE A 475 4999 3762 6732 -910 597 454 C ATOM 1216 CG2 ILE A 475 44.231 15.305 64.922 1.00 35.10 C ANISOU 1216 CG2 ILE A 475 4172 3604 5562 -711 470 426 C ATOM 1217 CD1 ILE A 475 46.254 17.339 65.311 1.00 42.69 C ANISOU 1217 CD1 ILE A 475 5092 4169 6959 -1155 561 371 C ATOM 1218 N HIS A 476 40.702 16.462 65.660 1.00 29.87 N ANISOU 1218 N HIS A 476 3715 2654 4979 -296 447 102 N ATOM 1219 CA HIS A 476 39.644 15.606 66.179 1.00 31.51 C ANISOU 1219 CA HIS A 476 3883 3094 4995 -175 389 -20 C ATOM 1220 C HIS A 476 38.458 15.528 65.227 1.00 29.72 C ANISOU 1220 C HIS A 476 3697 2843 4753 76 385 139 C ATOM 1221 O HIS A 476 37.743 14.525 65.190 1.00 21.55 O ANISOU 1221 O HIS A 476 2616 2045 3528 172 332 143 O ATOM 1222 CB HIS A 476 39.206 16.091 67.556 1.00 35.42 C ANISOU 1222 CB HIS A 476 4361 3570 5525 -244 395 -362 C ATOM 1223 CG HIS A 476 40.147 15.689 68.646 1.00 40.71 C ANISOU 1223 CG HIS A 476 4956 4445 6068 -491 345 -520 C ATOM 1224 ND1 HIS A 476 40.996 16.579 69.266 1.00 46.16 N ANISOU 1224 ND1 HIS A 476 5648 4997 6894 -703 367 -694 N ATOM 1225 CD2 HIS A 476 40.398 14.479 69.199 1.00 41.72 C ANISOU 1225 CD2 HIS A 476 4989 4908 5953 -566 258 -505 C ATOM 1226 CE1 HIS A 476 41.718 15.938 70.168 1.00 46.64 C ANISOU 1226 CE1 HIS A 476 5611 5340 6769 -901 282 -779 C ATOM 1227 NE2 HIS A 476 41.375 14.662 70.147 1.00 43.60 N ANISOU 1227 NE2 HIS A 476 5167 5236 6163 -812 215 -646 N ATOM 1228 N ARG A 477 38.265 16.579 64.441 1.00 27.19 N ANISOU 1228 N ARG A 477 3451 2240 4641 169 431 291 N ATOM 1229 CA ARG A 477 37.226 16.567 63.424 1.00 30.03 C ANISOU 1229 CA ARG A 477 3831 2599 4978 399 402 500 C ATOM 1230 C ARG A 477 37.565 15.597 62.301 1.00 23.98 C ANISOU 1230 C ARG A 477 3063 2076 3973 406 372 743 C ATOM 1231 O ARG A 477 36.684 14.906 61.799 1.00 23.01 O ANISOU 1231 O ARG A 477 2913 2143 3685 544 312 805 O ATOM 1232 CB ARG A 477 37.004 17.964 62.862 1.00 36.53 C ANISOU 1232 CB ARG A 477 4725 3048 6106 493 446 658 C ATOM 1233 CG ARG A 477 36.301 18.898 63.822 1.00 42.81 C ANISOU 1233 CG ARG A 477 5510 3580 7175 562 487 391 C ATOM 1234 CD ARG A 477 35.983 20.219 63.157 1.00 48.98 C ANISOU 1234 CD ARG A 477 6347 3949 8313 697 523 595 C ATOM 1235 NE ARG A 477 36.139 21.335 64.082 1.00 55.49 N ANISOU 1235 NE ARG A 477 7193 4402 9490 627 616 314 N ATOM 1236 CZ ARG A 477 36.956 22.363 63.879 1.00 60.32 C ANISOU 1236 CZ ARG A 477 7873 4686 10358 498 673 396 C ATOM 1237 NH1 ARG A 477 37.686 22.426 62.773 1.00 60.56 N ANISOU 1237 NH1 ARG A 477 7954 4744 10312 428 650 772 N ATOM 1238 NH2 ARG A 477 37.036 23.334 64.779 1.00 63.22 N ANISOU 1238 NH2 ARG A 477 8249 4805 10967 413 739 78 N ATOM 1239 N VAL A 478 38.838 15.540 61.913 1.00 24.00 N ANISOU 1239 N VAL A 478 3078 2081 3959 247 423 856 N ATOM 1240 CA VAL A 478 39.264 14.587 60.893 1.00 22.95 C ANISOU 1240 CA VAL A 478 2929 2189 3600 239 429 1028 C ATOM 1241 C VAL A 478 39.152 13.174 61.443 1.00 20.77 C ANISOU 1241 C VAL A 478 2568 2186 3138 225 378 856 C ATOM 1242 O VAL A 478 38.685 12.264 60.753 1.00 20.41 O ANISOU 1242 O VAL A 478 2506 2342 2908 309 349 908 O ATOM 1243 CB VAL A 478 40.706 14.850 60.409 1.00 23.77 C ANISOU 1243 CB VAL A 478 3035 2244 3752 67 524 1167 C ATOM 1244 CG1 VAL A 478 41.149 13.748 59.461 1.00 22.71 C ANISOU 1244 CG1 VAL A 478 2862 2388 3381 61 559 1270 C ATOM 1245 CG2 VAL A 478 40.790 16.201 59.715 1.00 26.69 C ANISOU 1245 CG2 VAL A 478 3493 2340 4308 70 579 1403 C ATOM 1246 N LEU A 479 39.564 12.992 62.695 1.00 19.69 N ANISOU 1246 N LEU A 479 2374 2058 3051 108 361 654 N ATOM 1247 CA LEU A 479 39.454 11.684 63.325 1.00 17.68 C ANISOU 1247 CA LEU A 479 2031 2037 2650 87 302 534 C ATOM 1248 C LEU A 479 37.991 11.232 63.356 1.00 20.01 C ANISOU 1248 C LEU A 479 2323 2435 2845 242 243 476 C ATOM 1249 O LEU A 479 37.701 10.060 63.106 1.00 20.14 O ANISOU 1249 O LEU A 479 2292 2637 2725 274 208 481 O ATOM 1250 CB LEU A 479 40.063 11.704 64.736 1.00 17.66 C ANISOU 1250 CB LEU A 479 1964 2053 2695 -75 273 361 C ATOM 1251 CG LEU A 479 41.592 11.547 64.801 1.00 19.16 C ANISOU 1251 CG LEU A 479 2081 2261 2936 -245 294 418 C ATOM 1252 CD1 LEU A 479 42.119 11.862 66.198 1.00 21.19 C ANISOU 1252 CD1 LEU A 479 2278 2540 3234 -423 241 249 C ATOM 1253 CD2 LEU A 479 42.032 10.135 64.370 1.00 17.19 C ANISOU 1253 CD2 LEU A 479 1740 2201 2590 -224 284 508 C ATOM 1254 N ASP A 480 37.074 12.159 63.633 1.00 20.35 N ANISOU 1254 N ASP A 480 2402 2345 2986 336 239 413 N ATOM 1255 CA ASP A 480 35.640 11.852 63.605 1.00 18.48 C ANISOU 1255 CA ASP A 480 2133 2207 2682 492 188 369 C ATOM 1256 C ASP A 480 35.170 11.459 62.203 1.00 20.59 C ANISOU 1256 C ASP A 480 2417 2571 2837 612 153 563 C ATOM 1257 O ASP A 480 34.304 10.600 62.045 1.00 19.85 O ANISOU 1257 O ASP A 480 2266 2660 2615 677 95 532 O ATOM 1258 CB ASP A 480 34.814 13.045 64.100 1.00 21.34 C ANISOU 1258 CB ASP A 480 2506 2376 3226 593 212 266 C ATOM 1259 CG ASP A 480 34.871 13.218 65.608 1.00 25.41 C ANISOU 1259 CG ASP A 480 2983 2897 3775 481 243 -11 C ATOM 1260 OD1 ASP A 480 35.338 12.291 66.304 1.00 23.80 O ANISOU 1260 OD1 ASP A 480 2731 2895 3419 341 216 -85 O ATOM 1261 OD2 ASP A 480 34.432 14.282 66.098 1.00 29.11 O ANISOU 1261 OD2 ASP A 480 3463 3172 4425 533 296 -156 O ATOM 1262 N LYS A 481 35.741 12.100 61.191 1.00 21.09 N ANISOU 1262 N LYS A 481 2552 2526 2934 618 190 764 N ATOM 1263 CA LYS A 481 35.404 11.802 59.804 1.00 21.34 C ANISOU 1263 CA LYS A 481 2606 2697 2807 700 158 959 C ATOM 1264 C LYS A 481 35.868 10.390 59.420 1.00 21.08 C ANISOU 1264 C LYS A 481 2536 2902 2573 618 167 905 C ATOM 1265 O LYS A 481 35.186 9.671 58.686 1.00 18.84 O ANISOU 1265 O LYS A 481 2230 2811 2118 677 115 919 O ATOM 1266 CB LYS A 481 36.023 12.852 58.880 1.00 26.24 C ANISOU 1266 CB LYS A 481 3311 3165 3495 692 211 1212 C ATOM 1267 CG LYS A 481 35.853 12.564 57.400 1.00 32.85 C ANISOU 1267 CG LYS A 481 4175 4203 4103 735 188 1433 C ATOM 1268 CD LYS A 481 34.398 12.639 56.972 1.00 36.69 C ANISOU 1268 CD LYS A 481 4627 4789 4524 911 61 1508 C ATOM 1269 CE LYS A 481 33.874 14.061 57.067 1.00 40.69 C ANISOU 1269 CE LYS A 481 5154 5016 5290 1040 33 1673 C ATOM 1270 NZ LYS A 481 32.491 14.184 56.524 1.00 42.46 N ANISOU 1270 NZ LYS A 481 5319 5352 5463 1164 -102 1706 N ATOM 1271 N ILE A 482 37.022 9.981 59.930 1.00 18.16 N ANISOU 1271 N ILE A 482 2144 2512 2245 482 231 832 N ATOM 1272 CA ILE A 482 37.507 8.632 59.655 1.00 17.47 C ANISOU 1272 CA ILE A 482 2001 2595 2042 422 253 766 C ATOM 1273 C ILE A 482 36.634 7.587 60.359 1.00 17.45 C ANISOU 1273 C ILE A 482 1926 2703 2003 447 175 610 C ATOM 1274 O ILE A 482 36.422 6.493 59.836 1.00 17.48 O ANISOU 1274 O ILE A 482 1894 2843 1904 451 166 561 O ATOM 1275 CB ILE A 482 38.972 8.470 60.076 1.00 15.82 C ANISOU 1275 CB ILE A 482 1749 2329 1933 288 331 752 C ATOM 1276 CG1 ILE A 482 39.850 9.481 59.334 1.00 19.25 C ANISOU 1276 CG1 ILE A 482 2240 2664 2409 237 425 916 C ATOM 1277 CG2 ILE A 482 39.473 7.053 59.778 1.00 15.18 C ANISOU 1277 CG2 ILE A 482 1588 2384 1795 256 366 682 C ATOM 1278 CD1 ILE A 482 41.317 9.389 59.694 1.00 20.74 C ANISOU 1278 CD1 ILE A 482 2356 2812 2713 96 503 909 C ATOM 1279 N THR A 483 36.119 7.927 61.538 1.00 16.40 N ANISOU 1279 N THR A 483 1767 2510 1955 450 129 522 N ATOM 1280 CA THR A 483 35.181 7.046 62.233 1.00 16.15 C ANISOU 1280 CA THR A 483 1660 2595 1880 462 64 404 C ATOM 1281 C THR A 483 33.913 6.845 61.395 1.00 17.99 C ANISOU 1281 C THR A 483 1884 2941 2011 577 7 419 C ATOM 1282 O THR A 483 33.480 5.709 61.196 1.00 19.67 O ANISOU 1282 O THR A 483 2041 3284 2148 559 -28 358 O ATOM 1283 CB THR A 483 34.810 7.594 63.630 1.00 16.32 C ANISOU 1283 CB THR A 483 1653 2574 1975 434 50 297 C ATOM 1284 OG1 THR A 483 35.980 7.628 64.456 1.00 15.46 O ANISOU 1284 OG1 THR A 483 1531 2419 1922 296 74 274 O ATOM 1285 CG2 THR A 483 33.747 6.719 64.298 1.00 16.88 C ANISOU 1285 CG2 THR A 483 1636 2797 1982 437 -1 202 C ATOM 1286 N ASP A 484 33.332 7.937 60.894 1.00 18.66 N ANISOU 1286 N ASP A 484 2009 2967 2113 691 -12 508 N ATOM 1287 CA ASP A 484 32.159 7.841 60.019 1.00 21.78 C ANISOU 1287 CA ASP A 484 2373 3498 2404 804 -93 560 C ATOM 1288 C ASP A 484 32.477 6.949 58.820 1.00 20.43 C ANISOU 1288 C ASP A 484 2221 3490 2051 756 -96 592 C ATOM 1289 O ASP A 484 31.633 6.180 58.346 1.00 20.31 O ANISOU 1289 O ASP A 484 2148 3652 1916 770 -168 534 O ATOM 1290 CB ASP A 484 31.706 9.219 59.505 1.00 21.20 C ANISOU 1290 CB ASP A 484 2336 3315 2404 943 -119 725 C ATOM 1291 CG ASP A 484 31.344 10.192 60.616 0.49 21.59 C ANISOU 1291 CG ASP A 484 2362 3171 2669 1005 -92 646 C ATOM 1292 OD1 ASP A 484 31.052 9.761 61.749 0.79 20.87 O ANISOU 1292 OD1 ASP A 484 2205 3116 2608 958 -76 457 O ATOM 1293 OD2 ASP A 484 31.339 11.410 60.340 0.78 23.31 O ANISOU 1293 OD2 ASP A 484 2626 3197 3033 1098 -80 776 O ATOM 1294 N THR A 485 33.707 7.068 58.338 1.00 19.71 N ANISOU 1294 N THR A 485 2200 3345 1942 687 -8 661 N ATOM 1295 CA THR A 485 34.150 6.321 57.174 1.00 20.36 C ANISOU 1295 CA THR A 485 2302 3586 1848 635 31 660 C ATOM 1296 C THR A 485 34.226 4.823 57.471 1.00 18.85 C ANISOU 1296 C THR A 485 2040 3460 1661 558 45 458 C ATOM 1297 O THR A 485 33.780 4.000 56.666 1.00 21.03 O ANISOU 1297 O THR A 485 2295 3901 1793 541 22 367 O ATOM 1298 CB THR A 485 35.516 6.838 56.686 1.00 21.66 C ANISOU 1298 CB THR A 485 2534 3677 2018 572 155 775 C ATOM 1299 OG1 THR A 485 35.377 8.200 56.262 1.00 22.39 O ANISOU 1299 OG1 THR A 485 2695 3694 2117 635 139 997 O ATOM 1300 CG2 THR A 485 36.016 6.015 55.515 1.00 21.62 C ANISOU 1300 CG2 THR A 485 2534 3861 1818 511 232 727 C ATOM 1301 N LEU A 486 34.780 4.469 58.627 1.00 17.29 N ANISOU 1301 N LEU A 486 1800 3133 1635 502 76 393 N ATOM 1302 CA LEU A 486 34.833 3.066 59.033 1.00 17.98 C ANISOU 1302 CA LEU A 486 1810 3235 1786 437 78 253 C ATOM 1303 C LEU A 486 33.428 2.472 59.153 1.00 19.86 C ANISOU 1303 C LEU A 486 1991 3579 1977 454 -22 165 C ATOM 1304 O LEU A 486 33.171 1.374 58.654 1.00 20.79 O ANISOU 1304 O LEU A 486 2069 3765 2064 410 -25 44 O ATOM 1305 CB LEU A 486 35.591 2.919 60.351 1.00 16.85 C ANISOU 1305 CB LEU A 486 1618 2961 1822 375 95 264 C ATOM 1306 CG LEU A 486 37.114 2.904 60.227 1.00 17.26 C ANISOU 1306 CG LEU A 486 1664 2931 1965 325 193 307 C ATOM 1307 CD1 LEU A 486 37.760 3.039 61.597 1.00 14.84 C ANISOU 1307 CD1 LEU A 486 1301 2536 1803 259 167 352 C ATOM 1308 CD2 LEU A 486 37.577 1.624 59.529 1.00 19.75 C ANISOU 1308 CD2 LEU A 486 1925 3264 2316 305 264 207 C ATOM 1309 N ILE A 487 32.516 3.205 59.790 1.00 17.24 N ANISOU 1309 N ILE A 487 1641 3255 1656 513 -92 206 N ATOM 1310 CA ILE A 487 31.141 2.735 59.939 1.00 16.65 C ANISOU 1310 CA ILE A 487 1480 3299 1547 527 -181 133 C ATOM 1311 C ILE A 487 30.456 2.585 58.570 1.00 19.54 C ANISOU 1311 C ILE A 487 1846 3839 1741 562 -243 116 C ATOM 1312 O ILE A 487 29.750 1.606 58.322 1.00 18.56 O ANISOU 1312 O ILE A 487 1661 3801 1589 497 -282 -6 O ATOM 1313 CB ILE A 487 30.308 3.686 60.839 1.00 19.42 C ANISOU 1313 CB ILE A 487 1821 3594 1963 580 -199 157 C ATOM 1314 CG1 ILE A 487 30.826 3.654 62.279 1.00 20.46 C ANISOU 1314 CG1 ILE A 487 1935 3638 2202 510 -156 134 C ATOM 1315 CG2 ILE A 487 28.827 3.303 60.819 1.00 17.07 C ANISOU 1315 CG2 ILE A 487 1467 3369 1649 567 -247 87 C ATOM 1316 CD1 ILE A 487 30.699 2.297 62.952 1.00 19.41 C ANISOU 1316 CD1 ILE A 487 1760 3505 2110 377 -153 73 C ATOM 1317 N HIS A 488 30.678 3.551 57.684 1.00 19.54 N ANISOU 1317 N HIS A 488 1922 3871 1632 635 -244 244 N ATOM 1318 CA HIS A 488 30.156 3.484 56.322 1.00 21.54 C ANISOU 1318 CA HIS A 488 2191 4283 1710 628 -287 250 C ATOM 1319 C HIS A 488 30.615 2.203 55.610 1.00 23.51 C ANISOU 1319 C HIS A 488 2435 4672 1824 523 -254 78 C ATOM 1320 O HIS A 488 29.810 1.506 54.984 1.00 25.25 O ANISOU 1320 O HIS A 488 2607 5019 1969 464 -309 -46 O ATOM 1321 CB HIS A 488 30.597 4.730 55.543 1.00 25.36 C ANISOU 1321 CB HIS A 488 2766 4750 2120 692 -271 458 C ATOM 1322 CG HIS A 488 30.114 4.782 54.124 1.00 28.39 C ANISOU 1322 CG HIS A 488 3163 5311 2312 668 -325 503 C ATOM 1323 ND1 HIS A 488 28.812 5.086 53.791 0.74 31.15 N ANISOU 1323 ND1 HIS A 488 3455 5730 2653 709 -441 546 N ATOM 1324 CD2 HIS A 488 30.769 4.599 52.953 0.84 31.87 C ANISOU 1324 CD2 HIS A 488 3664 5888 2556 598 -277 515 C ATOM 1325 CE1 HIS A 488 28.682 5.074 52.476 0.71 34.80 C ANISOU 1325 CE1 HIS A 488 3940 6374 2911 664 -483 597 C ATOM 1326 NE2 HIS A 488 29.855 4.782 51.944 1.00 35.53 N ANISOU 1326 NE2 HIS A 488 4109 6513 2880 591 -380 570 N ATOM 1327 N LEU A 489 31.906 1.894 55.710 1.00 19.12 N ANISOU 1327 N LEU A 489 1930 3997 1336 472 -121 41 N ATOM 1328 CA LEU A 489 32.453 0.704 55.064 1.00 19.63 C ANISOU 1328 CA LEU A 489 1989 4105 1365 374 -33 -163 C ATOM 1329 C LEU A 489 31.793 -0.563 55.601 1.00 19.39 C ANISOU 1329 C LEU A 489 1865 4029 1475 304 -76 -354 C ATOM 1330 O LEU A 489 31.469 -1.482 54.841 1.00 22.41 O ANISOU 1330 O LEU A 489 2220 4520 1774 225 -77 -558 O ATOM 1331 CB LEU A 489 33.970 0.631 55.257 1.00 20.22 C ANISOU 1331 CB LEU A 489 2094 4014 1573 352 128 -153 C ATOM 1332 CG LEU A 489 34.779 1.678 54.498 1.00 20.99 C ANISOU 1332 CG LEU A 489 2277 4173 1526 376 210 7 C ATOM 1333 CD1 LEU A 489 36.198 1.761 55.051 1.00 20.58 C ANISOU 1333 CD1 LEU A 489 2216 3930 1674 356 345 49 C ATOM 1334 CD2 LEU A 489 34.786 1.336 53.014 1.00 24.83 C ANISOU 1334 CD2 LEU A 489 2795 4916 1725 323 263 -99 C ATOM 1335 N MET A 490 31.579 -0.595 56.910 1.00 17.30 N ANISOU 1335 N MET A 490 1548 3612 1415 315 -109 -290 N ATOM 1336 CA MET A 490 30.968 -1.750 57.554 1.00 17.81 C ANISOU 1336 CA MET A 490 1517 3615 1636 233 -145 -411 C ATOM 1337 C MET A 490 29.501 -1.915 57.191 1.00 21.94 C ANISOU 1337 C MET A 490 1969 4329 2039 210 -272 -485 C ATOM 1338 O MET A 490 29.035 -3.033 56.950 1.00 22.69 O ANISOU 1338 O MET A 490 2000 4438 2183 104 -290 -664 O ATOM 1339 CB MET A 490 31.123 -1.644 59.065 1.00 15.42 C ANISOU 1339 CB MET A 490 1174 3159 1526 234 -147 -287 C ATOM 1340 CG MET A 490 32.571 -1.692 59.511 1.00 20.55 C ANISOU 1340 CG MET A 490 1854 3634 2321 231 -48 -219 C ATOM 1341 SD MET A 490 32.702 -1.546 61.300 1.00 22.74 S ANISOU 1341 SD MET A 490 2077 3812 2752 201 -80 -67 S ATOM 1342 CE MET A 490 34.394 -1.009 61.479 1.00 24.64 C ANISOU 1342 CE MET A 490 2360 3932 3070 221 3 36 C ATOM 1343 N ALA A 491 28.778 -0.800 57.152 1.00 20.83 N ANISOU 1343 N ALA A 491 1826 4312 1778 307 -356 -348 N ATOM 1344 CA ALA A 491 27.382 -0.816 56.736 1.00 23.13 C ANISOU 1344 CA ALA A 491 2077 4688 2023 292 -423 -366 C ATOM 1345 C ALA A 491 27.268 -1.258 55.282 1.00 24.16 C ANISOU 1345 C ALA A 491 2217 5000 1962 231 -454 -488 C ATOM 1346 O ALA A 491 26.397 -2.055 54.932 1.00 25.62 O ANISOU 1346 O ALA A 491 2334 5262 2137 138 -505 -623 O ATOM 1347 CB ALA A 491 26.751 0.559 56.931 1.00 21.40 C ANISOU 1347 CB ALA A 491 1884 4440 1809 411 -448 -181 C ATOM 1348 N LYS A 492 28.166 -0.751 54.440 1.00 23.56 N ANISOU 1348 N LYS A 492 2233 4988 1732 264 -409 -440 N ATOM 1349 CA LYS A 492 28.153 -1.079 53.020 1.00 26.99 C ANISOU 1349 CA LYS A 492 2696 5600 1959 189 -411 -545 C ATOM 1350 C LYS A 492 28.456 -2.556 52.810 1.00 27.04 C ANISOU 1350 C LYS A 492 2673 5607 1996 47 -350 -863 C ATOM 1351 O LYS A 492 28.024 -3.149 51.824 1.00 31.79 O ANISOU 1351 O LYS A 492 3258 6341 2480 -52 -368 -1023 O ATOM 1352 CB LYS A 492 29.157 -0.214 52.251 1.00 27.98 C ANISOU 1352 CB LYS A 492 2933 5768 1929 235 -340 -406 C ATOM 1353 N ALA A 493 29.185 -3.150 53.750 1.00 25.77 N ANISOU 1353 N ALA A 493 2496 5281 2014 32 -279 -968 N ATOM 1354 CA ALA A 493 29.526 -4.565 53.677 1.00 29.02 C ANISOU 1354 CA ALA A 493 2878 5548 2601 -92 -183 -1256 C ATOM 1355 C ALA A 493 28.426 -5.456 54.262 1.00 31.90 C ANISOU 1355 C ALA A 493 3123 5856 3142 -195 -281 -1363 C ATOM 1356 O ALA A 493 28.554 -6.679 54.272 1.00 35.10 O ANISOU 1356 O ALA A 493 3490 6091 3755 -309 -215 -1590 O ATOM 1357 CB ALA A 493 30.837 -4.821 54.387 1.00 25.70 C ANISOU 1357 CB ALA A 493 2486 4819 2459 -50 -25 -1205 C ATOM 1358 N GLY A 494 27.358 -4.847 54.767 1.00 29.54 N ANISOU 1358 N GLY A 494 2764 5647 2813 -149 -408 -1177 N ATOM 1359 CA GLY A 494 26.212 -5.611 55.223 1.00 27.34 C ANISOU 1359 CA GLY A 494 2384 5318 2686 -246 -467 -1228 C ATOM 1360 C GLY A 494 26.176 -5.978 56.698 1.00 24.43 C ANISOU 1360 C GLY A 494 1945 4739 2598 -269 -454 -1126 C ATOM 1361 O GLY A 494 25.334 -6.767 57.117 1.00 25.01 O ANISOU 1361 O GLY A 494 1946 4740 2817 -374 -477 -1162 O ATOM 1362 N ALEU A 495 27.081 -5.408 57.486 0.67 21.86 N ANISOU 1362 N ALEU A 495 1652 4305 2348 -177 -403 -963 N ATOM 1363 N BLEU A 495 27.088 -5.417 57.486 0.33 22.17 N ANISOU 1363 N BLEU A 495 1691 4343 2388 -177 -402 -964 N ATOM 1364 CA ALEU A 495 27.080 -5.646 58.926 0.67 21.06 C ANISOU 1364 CA ALEU A 495 1501 4027 2475 -198 -378 -805 C ATOM 1365 CA BLEU A 495 27.076 -5.651 58.926 0.33 21.39 C ANISOU 1365 CA BLEU A 495 1541 4068 2516 -198 -378 -805 C ATOM 1366 C ALEU A 495 25.855 -4.998 59.562 0.67 21.67 C ANISOU 1366 C ALEU A 495 1593 4155 2487 -153 -416 -643 C ATOM 1367 C BLEU A 495 25.850 -5.002 59.558 0.33 21.42 C ANISOU 1367 C BLEU A 495 1561 4123 2454 -154 -416 -643 C ATOM 1368 O ALEU A 495 25.443 -3.909 59.159 0.67 20.81 O ANISOU 1368 O ALEU A 495 1534 4163 2210 -41 -440 -575 O ATOM 1369 O BLEU A 495 25.439 -3.914 59.154 0.33 21.07 O ANISOU 1369 O BLEU A 495 1566 4196 2243 -41 -441 -576 O ATOM 1370 CB ALEU A 495 28.362 -5.110 59.572 0.67 21.45 C ANISOU 1370 CB ALEU A 495 1633 3924 2594 -105 -292 -639 C ATOM 1371 CB BLEU A 495 28.349 -5.111 59.584 0.33 21.25 C ANISOU 1371 CB BLEU A 495 1606 3899 2569 -106 -293 -638 C ATOM 1372 CG ALEU A 495 29.612 -5.997 59.581 0.67 22.51 C ANISOU 1372 CG ALEU A 495 1799 3805 2949 -139 -184 -681 C ATOM 1373 CG BLEU A 495 29.666 -5.845 59.332 0.33 22.26 C ANISOU 1373 CG BLEU A 495 1785 3804 2868 -122 -180 -701 C ATOM 1374 CD1ALEU A 495 30.066 -6.363 58.172 0.67 22.80 C ANISOU 1374 CD1ALEU A 495 1891 3861 2913 -144 -118 -916 C ATOM 1375 CD1BLEU A 495 30.781 -5.218 60.157 0.33 21.47 C ANISOU 1375 CD1BLEU A 495 1729 3594 2834 -42 -128 -497 C ATOM 1376 CD2ALEU A 495 30.740 -5.315 60.349 0.67 21.78 C ANISOU 1376 CD2ALEU A 495 1756 3616 2904 -54 -132 -480 C ATOM 1377 CD2BLEU A 495 29.534 -7.328 59.646 0.33 23.66 C ANISOU 1377 CD2BLEU A 495 1880 3776 3334 -253 -160 -792 C ATOM 1378 N THR A 496 25.263 -5.676 60.542 1.00 19.07 N ANISOU 1378 N THR A 496 1203 3727 2315 -247 -412 -583 N ATOM 1379 CA THR A 496 24.131 -5.112 61.280 1.00 21.09 C ANISOU 1379 CA THR A 496 1445 4036 2532 -216 -423 -468 C ATOM 1380 C THR A 496 24.594 -3.926 62.123 1.00 18.81 C ANISOU 1380 C THR A 496 1239 3715 2194 -100 -370 -326 C ATOM 1381 O THR A 496 25.789 -3.762 62.358 1.00 16.95 O ANISOU 1381 O THR A 496 1062 3391 1986 -73 -332 -276 O ATOM 1382 CB THR A 496 23.474 -6.141 62.199 1.00 20.74 C ANISOU 1382 CB THR A 496 1307 3916 2658 -358 -420 -429 C ATOM 1383 OG1 THR A 496 24.395 -6.503 63.236 1.00 19.68 O ANISOU 1383 OG1 THR A 496 1185 3630 2663 -397 -370 -303 O ATOM 1384 CG2 THR A 496 23.065 -7.379 61.413 1.00 24.30 C ANISOU 1384 CG2 THR A 496 1676 4353 3205 -505 -465 -592 C ATOM 1385 N LEU A 497 23.652 -3.104 62.578 1.00 16.91 N ANISOU 1385 N LEU A 497 1604 2357 2466 -235 43 -617 N ATOM 1386 CA LEU A 497 24.008 -1.944 63.389 1.00 17.53 C ANISOU 1386 CA LEU A 497 1790 2388 2484 -212 38 -438 C ATOM 1387 C LEU A 497 24.835 -2.318 64.631 1.00 14.20 C ANISOU 1387 C LEU A 497 1447 1837 2112 -197 119 -376 C ATOM 1388 O LEU A 497 25.806 -1.639 64.958 1.00 15.55 O ANISOU 1388 O LEU A 497 1688 2022 2196 -183 109 -288 O ATOM 1389 CB LEU A 497 22.752 -1.186 63.818 1.00 18.96 C ANISOU 1389 CB LEU A 497 1963 2520 2721 -201 22 -387 C ATOM 1390 CG LEU A 497 23.054 0.176 64.444 1.00 20.03 C ANISOU 1390 CG LEU A 497 2164 2624 2823 -179 1 -250 C ATOM 1391 CD1 LEU A 497 23.924 1.007 63.501 1.00 21.02 C ANISOU 1391 CD1 LEU A 497 2283 2872 2831 -179 -70 -167 C ATOM 1392 CD2 LEU A 497 21.761 0.909 64.780 1.00 20.74 C ANISOU 1392 CD2 LEU A 497 2219 2664 2997 -169 -17 -227 C ATOM 1393 N GLN A 498 24.455 -3.397 65.310 1.00 17.21 N ANISOU 1393 N GLN A 498 1796 2099 2641 -196 199 -410 N ATOM 1394 CA GLN A 498 25.199 -3.827 66.495 1.00 16.35 C ANISOU 1394 CA GLN A 498 1735 1907 2571 -174 278 -315 C ATOM 1395 C GLN A 498 26.589 -4.332 66.106 1.00 15.94 C ANISOU 1395 C GLN A 498 1696 1877 2484 -178 281 -334 C ATOM 1396 O GLN A 498 27.578 -4.010 66.759 1.00 14.54 O ANISOU 1396 O GLN A 498 1587 1708 2228 -157 295 -240 O ATOM 1397 CB GLN A 498 24.418 -4.903 67.259 1.00 17.69 C ANISOU 1397 CB GLN A 498 1833 1952 2936 -169 371 -297 C ATOM 1398 CG GLN A 498 23.179 -4.350 67.937 1.00 22.58 C ANISOU 1398 CG GLN A 498 2447 2558 3572 -157 385 -252 C ATOM 1399 CD GLN A 498 22.240 -5.420 68.461 1.00 30.09 C ANISOU 1399 CD GLN A 498 3301 3394 4737 -158 475 -234 C ATOM 1400 OE1 GLN A 498 22.247 -6.559 67.989 1.00 32.91 O ANISOU 1400 OE1 GLN A 498 3567 3660 5277 -178 509 -305 O ATOM 1401 NE2 GLN A 498 21.419 -5.054 69.447 1.00 27.14 N ANISOU 1401 NE2 GLN A 498 2924 3024 4364 -136 519 -147 N ATOM 1402 N GLN A 499 26.658 -5.102 65.024 1.00 14.09 N ANISOU 1402 N GLN A 499 1381 1667 2306 -206 266 -479 N ATOM 1403 CA GLN A 499 27.935 -5.580 64.506 1.00 15.70 C ANISOU 1403 CA GLN A 499 1578 1906 2481 -213 266 -532 C ATOM 1404 C GLN A 499 28.861 -4.428 64.130 1.00 14.37 C ANISOU 1404 C GLN A 499 1495 1873 2092 -208 200 -462 C ATOM 1405 O GLN A 499 30.082 -4.561 64.215 1.00 15.20 O ANISOU 1405 O GLN A 499 1635 1984 2155 -202 213 -434 O ATOM 1406 CB GLN A 499 27.722 -6.491 63.299 1.00 15.82 C ANISOU 1406 CB GLN A 499 1459 1969 2585 -244 252 -756 C ATOM 1407 CG GLN A 499 27.257 -7.889 63.666 1.00 19.05 C ANISOU 1407 CG GLN A 499 1750 2190 3300 -252 336 -842 C ATOM 1408 CD GLN A 499 26.906 -8.711 62.449 1.00 25.35 C ANISOU 1408 CD GLN A 499 2380 3042 4211 -284 315 -1127 C ATOM 1409 OE1 GLN A 499 26.705 -8.171 61.365 1.00 25.61 O ANISOU 1409 OE1 GLN A 499 2384 3295 4053 -297 232 -1247 O ATOM 1410 NE2 GLN A 499 26.834 -10.026 62.618 1.00 29.28 N ANISOU 1410 NE2 GLN A 499 2740 3353 5034 -294 392 -1237 N ATOM 1411 N GLN A 500 28.288 -3.293 63.735 1.00 17.08 N ANISOU 1411 N GLN A 500 1857 2311 2322 -208 133 -419 N ATOM 1412 CA GLN A 500 29.098 -2.142 63.352 1.00 17.20 C ANISOU 1412 CA GLN A 500 1922 2432 2182 -203 76 -324 C ATOM 1413 C GLN A 500 29.859 -1.549 64.539 1.00 16.85 C ANISOU 1413 C GLN A 500 1970 2299 2133 -178 102 -206 C ATOM 1414 O GLN A 500 31.075 -1.326 64.439 1.00 14.88 O ANISOU 1414 O GLN A 500 1755 2083 1814 -176 95 -170 O ATOM 1415 CB GLN A 500 28.231 -1.067 62.689 1.00 15.80 C ANISOU 1415 CB GLN A 500 1709 2354 1941 -204 3 -271 C ATOM 1416 CG GLN A 500 27.698 -1.452 61.303 1.00 16.42 C ANISOU 1416 CG GLN A 500 1673 2615 1950 -223 -45 -379 C ATOM 1417 CD GLN A 500 26.592 -0.520 60.827 1.00 18.63 C ANISOU 1417 CD GLN A 500 1900 2980 2198 -217 -110 -304 C ATOM 1418 OE1 GLN A 500 26.581 0.663 61.164 1.00 20.57 O ANISOU 1418 OE1 GLN A 500 2183 3181 2452 -201 -136 -143 O ATOM 1419 NE2 GLN A 500 25.647 -1.055 60.055 1.00 18.08 N ANISOU 1419 NE2 GLN A 500 1724 3027 2119 -228 -138 -431 N ATOM 1420 N HIS A 501 29.177 -1.295 65.656 1.00 12.83 N ANISOU 1420 N HIS A 501 1486 1700 1688 -158 132 -163 N ATOM 1421 CA HIS A 501 29.894 -0.706 66.781 1.00 13.71 C ANISOU 1421 CA HIS A 501 1656 1781 1773 -131 151 -92 C ATOM 1422 C HIS A 501 30.809 -1.741 67.447 1.00 12.54 C ANISOU 1422 C HIS A 501 1524 1603 1636 -116 215 -76 C ATOM 1423 O HIS A 501 31.864 -1.382 67.983 1.00 11.83 O ANISOU 1423 O HIS A 501 1474 1536 1487 -97 216 -35 O ATOM 1424 CB HIS A 501 28.939 -0.032 67.800 1.00 14.14 C ANISOU 1424 CB HIS A 501 1706 1799 1868 -109 163 -74 C ATOM 1425 CG HIS A 501 28.028 -0.960 68.553 1.00 14.55 C ANISOU 1425 CG HIS A 501 1728 1807 1992 -98 234 -78 C ATOM 1426 ND1 HIS A 501 26.654 -0.846 68.502 1.00 15.53 N ANISOU 1426 ND1 HIS A 501 1812 1904 2184 -105 233 -106 N ATOM 1427 CD2 HIS A 501 28.286 -1.950 69.443 1.00 14.97 C ANISOU 1427 CD2 HIS A 501 1771 1844 2074 -77 312 -30 C ATOM 1428 CE1 HIS A 501 26.106 -1.759 69.287 1.00 17.19 C ANISOU 1428 CE1 HIS A 501 1990 2077 2466 -92 311 -82 C ATOM 1429 NE2 HIS A 501 27.075 -2.438 69.873 1.00 16.95 N ANISOU 1429 NE2 HIS A 501 1970 2054 2416 -74 361 -20 N ATOM 1430 N GLN A 502 30.447 -3.019 67.372 1.00 12.42 N ANISOU 1430 N GLN A 502 1461 1534 1725 -123 268 -109 N ATOM 1431 CA GLN A 502 31.301 -4.062 67.937 1.00 12.58 C ANISOU 1431 CA GLN A 502 1467 1505 1806 -107 332 -65 C ATOM 1432 C GLN A 502 32.610 -4.176 67.166 1.00 12.70 C ANISOU 1432 C GLN A 502 1500 1557 1769 -120 305 -106 C ATOM 1433 O GLN A 502 33.683 -4.254 67.768 1.00 12.51 O ANISOU 1433 O GLN A 502 1504 1537 1711 -98 324 -39 O ATOM 1434 CB GLN A 502 30.583 -5.413 67.961 1.00 13.76 C ANISOU 1434 CB GLN A 502 1524 1548 2155 -114 400 -86 C ATOM 1435 CG GLN A 502 29.451 -5.476 68.973 1.00 16.73 C ANISOU 1435 CG GLN A 502 1873 1889 2595 -92 452 0 C ATOM 1436 CD GLN A 502 28.633 -6.746 68.861 1.00 22.37 C ANISOU 1436 CD GLN A 502 2473 2474 3554 -105 519 -21 C ATOM 1437 OE1 GLN A 502 28.860 -7.571 67.976 1.00 22.62 O ANISOU 1437 OE1 GLN A 502 2435 2437 3724 -133 521 -140 O ATOM 1438 NE2 GLN A 502 27.671 -6.909 69.766 1.00 24.30 N ANISOU 1438 NE2 GLN A 502 2675 2688 3871 -86 579 80 N ATOM 1439 N ARG A 503 32.523 -4.159 65.839 1.00 12.45 N ANISOU 1439 N ARG A 503 1436 1581 1713 -154 259 -217 N ATOM 1440 CA ARG A 503 33.722 -4.252 65.018 1.00 11.66 C ANISOU 1440 CA ARG A 503 1334 1550 1546 -168 237 -266 C ATOM 1441 C ARG A 503 34.569 -2.992 65.125 1.00 16.26 C ANISOU 1441 C ARG A 503 1993 2203 1984 -158 190 -175 C ATOM 1442 O ARG A 503 35.794 -3.078 65.146 1.00 12.27 O ANISOU 1442 O ARG A 503 1509 1711 1444 -153 197 -158 O ATOM 1443 CB ARG A 503 33.372 -4.515 63.552 1.00 13.21 C ANISOU 1443 CB ARG A 503 1447 1856 1715 -201 199 -416 C ATOM 1444 CG ARG A 503 34.600 -4.780 62.677 1.00 14.51 C ANISOU 1444 CG ARG A 503 1582 2124 1809 -215 189 -492 C ATOM 1445 CD ARG A 503 34.205 -5.222 61.282 1.00 17.65 C ANISOU 1445 CD ARG A 503 1857 2680 2169 -243 160 -681 C ATOM 1446 NE ARG A 503 35.356 -5.486 60.420 1.00 18.37 N ANISOU 1446 NE ARG A 503 1898 2908 2175 -254 154 -775 N ATOM 1447 CZ ARG A 503 36.001 -6.647 60.367 1.00 21.09 C ANISOU 1447 CZ ARG A 503 2172 3180 2663 -260 205 -922 C ATOM 1448 NH1 ARG A 503 35.622 -7.657 61.140 1.00 17.32 N ANISOU 1448 NH1 ARG A 503 1659 2479 2443 -254 266 -959 N ATOM 1449 NH2 ARG A 503 37.030 -6.798 59.541 1.00 22.10 N ANISOU 1449 NH2 ARG A 503 2246 3455 2696 -271 198 -1020 N ATOM 1450 N LEU A 504 33.920 -1.827 65.181 1.00 12.90 N ANISOU 1450 N LEU A 504 1589 1805 1509 -156 146 -121 N ATOM 1451 CA LEU A 504 34.642 -0.565 65.340 1.00 12.67 C ANISOU 1451 CA LEU A 504 1598 1802 1413 -147 107 -41 C ATOM 1452 C LEU A 504 35.519 -0.643 66.588 1.00 13.13 C ANISOU 1452 C LEU A 504 1701 1810 1478 -117 142 -10 C ATOM 1453 O LEU A 504 36.703 -0.310 66.556 1.00 12.26 O ANISOU 1453 O LEU A 504 1611 1722 1326 -114 130 12 O ATOM 1454 CB LEU A 504 33.676 0.625 65.435 1.00 13.05 C ANISOU 1454 CB LEU A 504 1634 1839 1485 -144 66 4 C ATOM 1455 CG LEU A 504 34.313 1.998 65.693 1.00 16.22 C ANISOU 1455 CG LEU A 504 2039 2223 1903 -134 30 72 C ATOM 1456 CD1 LEU A 504 35.186 2.440 64.513 1.00 16.49 C ANISOU 1456 CD1 LEU A 504 2044 2338 1884 -154 -5 143 C ATOM 1457 CD2 LEU A 504 33.263 3.063 66.004 1.00 17.08 C ANISOU 1457 CD2 LEU A 504 2110 2277 2103 -127 2 93 C ATOM 1458 N ALA A 505 34.925 -1.106 67.681 1.00 12.18 N ANISOU 1458 N ALA A 505 1581 1645 1402 -92 187 -1 N ATOM 1459 CA ALA A 505 35.650 -1.307 68.931 1.00 12.81 C ANISOU 1459 CA ALA A 505 1674 1735 1459 -54 223 43 C ATOM 1460 C ALA A 505 36.800 -2.312 68.801 1.00 12.92 C ANISOU 1460 C ALA A 505 1686 1738 1483 -50 254 63 C ATOM 1461 O ALA A 505 37.908 -2.056 69.276 1.00 14.10 O ANISOU 1461 O ALA A 505 1854 1925 1578 -30 248 89 O ATOM 1462 CB ALA A 505 34.683 -1.752 70.030 1.00 11.99 C ANISOU 1462 CB ALA A 505 1540 1629 1386 -25 276 81 C ATOM 1463 N GLN A 506 36.538 -3.459 68.178 1.00 12.37 N ANISOU 1463 N GLN A 506 1578 1614 1510 -69 288 34 N ATOM 1464 CA GLN A 506 37.579 -4.471 67.994 1.00 12.55 C ANISOU 1464 CA GLN A 506 1573 1602 1594 -67 322 33 C ATOM 1465 C GLN A 506 38.762 -3.896 67.226 1.00 15.66 C ANISOU 1465 C GLN A 506 2001 2057 1894 -85 276 -9 C ATOM 1466 O GLN A 506 39.916 -4.125 67.587 1.00 12.71 O ANISOU 1466 O GLN A 506 1635 1684 1511 -67 288 27 O ATOM 1467 CB GLN A 506 37.033 -5.700 67.263 1.00 13.81 C ANISOU 1467 CB GLN A 506 1649 1678 1918 -92 360 -52 C ATOM 1468 CG GLN A 506 35.968 -6.462 68.028 1.00 20.51 C ANISOU 1468 CG GLN A 506 2438 2435 2918 -75 422 12 C ATOM 1469 CD GLN A 506 35.123 -7.345 67.124 1.00 26.50 C ANISOU 1469 CD GLN A 506 3102 3113 3854 -109 441 -125 C ATOM 1470 OE1 GLN A 506 35.401 -7.477 65.930 1.00 23.30 O ANISOU 1470 OE1 GLN A 506 2663 2748 3440 -143 409 -286 O ATOM 1471 NE2 GLN A 506 34.069 -7.940 67.688 1.00 29.22 N ANISOU 1471 NE2 GLN A 506 3382 3364 4357 -100 495 -74 N ATOM 1472 N LEU A 507 38.470 -3.148 66.167 1.00 13.26 N ANISOU 1472 N LEU A 507 1702 1816 1521 -117 225 -64 N ATOM 1473 CA LEU A 507 39.526 -2.569 65.343 1.00 15.67 C ANISOU 1473 CA LEU A 507 2018 2199 1739 -134 188 -74 C ATOM 1474 C LEU A 507 40.342 -1.538 66.114 1.00 16.00 C ANISOU 1474 C LEU A 507 2107 2241 1732 -113 165 2 C ATOM 1475 O LEU A 507 41.565 -1.499 66.007 1.00 14.49 O ANISOU 1475 O LEU A 507 1922 2068 1513 -112 164 10 O ATOM 1476 CB LEU A 507 38.942 -1.925 64.083 1.00 15.20 C ANISOU 1476 CB LEU A 507 1924 2244 1609 -165 142 -98 C ATOM 1477 CG LEU A 507 38.361 -2.883 63.040 1.00 18.98 C ANISOU 1477 CG LEU A 507 2323 2788 2100 -190 151 -226 C ATOM 1478 CD1 LEU A 507 37.804 -2.120 61.862 1.00 21.22 C ANISOU 1478 CD1 LEU A 507 2556 3237 2268 -210 97 -217 C ATOM 1479 CD2 LEU A 507 39.416 -3.869 62.586 1.00 21.75 C ANISOU 1479 CD2 LEU A 507 2629 3159 2475 -198 183 -327 C ATOM 1480 N LEU A 508 39.669 -0.690 66.881 1.00 12.91 N ANISOU 1480 N LEU A 508 1730 1829 1345 -96 148 34 N ATOM 1481 CA LEU A 508 40.371 0.376 67.584 1.00 14.34 C ANISOU 1481 CA LEU A 508 1923 2014 1512 -78 122 54 C ATOM 1482 C LEU A 508 41.162 -0.156 68.777 1.00 11.53 C ANISOU 1482 C LEU A 508 1574 1674 1134 -38 151 60 C ATOM 1483 O LEU A 508 42.176 0.427 69.162 1.00 13.91 O ANISOU 1483 O LEU A 508 1872 1998 1414 -25 131 50 O ATOM 1484 CB LEU A 508 39.389 1.457 68.030 1.00 16.64 C ANISOU 1484 CB LEU A 508 2195 2284 1844 -71 94 46 C ATOM 1485 CG LEU A 508 38.729 2.184 66.855 1.00 18.96 C ANISOU 1485 CG LEU A 508 2460 2571 2173 -104 56 82 C ATOM 1486 CD1 LEU A 508 37.767 3.237 67.354 1.00 18.53 C ANISOU 1486 CD1 LEU A 508 2370 2466 2204 -95 32 72 C ATOM 1487 CD2 LEU A 508 39.772 2.803 65.927 1.00 16.52 C ANISOU 1487 CD2 LEU A 508 2128 2289 1861 -125 29 142 C ATOM 1488 N LEU A 509 40.713 -1.261 69.360 1.00 10.53 N ANISOU 1488 N LEU A 509 1437 1541 1022 -16 201 89 N ATOM 1489 CA LEU A 509 41.458 -1.866 70.453 1.00 14.63 C ANISOU 1489 CA LEU A 509 1938 2105 1514 29 232 144 C ATOM 1490 C LEU A 509 42.770 -2.469 69.946 1.00 15.79 C ANISOU 1490 C LEU A 509 2088 2231 1680 23 239 153 C ATOM 1491 O LEU A 509 43.720 -2.596 70.711 1.00 15.57 O ANISOU 1491 O LEU A 509 2046 2256 1615 58 243 193 O ATOM 1492 CB LEU A 509 40.621 -2.924 71.173 1.00 15.09 C ANISOU 1492 CB LEU A 509 1956 2158 1618 58 294 227 C ATOM 1493 CG LEU A 509 39.517 -2.363 72.070 1.00 16.91 C ANISOU 1493 CG LEU A 509 2168 2459 1799 81 298 230 C ATOM 1494 CD1 LEU A 509 38.772 -3.495 72.737 1.00 20.07 C ANISOU 1494 CD1 LEU A 509 2510 2858 2256 110 371 350 C ATOM 1495 CD2 LEU A 509 40.092 -1.413 73.106 1.00 19.10 C ANISOU 1495 CD2 LEU A 509 2424 2876 1955 120 267 190 C ATOM 1496 N ILE A 510 42.805 -2.853 68.679 1.00 12.29 N ANISOU 1496 N ILE A 510 1648 1737 1285 -20 239 105 N ATOM 1497 CA ILE A 510 44.072 -3.263 68.068 1.00 12.96 C ANISOU 1497 CA ILE A 510 1725 1815 1383 -32 243 82 C ATOM 1498 C ILE A 510 45.131 -2.174 68.180 1.00 13.46 C ANISOU 1498 C ILE A 510 1814 1930 1372 -29 200 83 C ATOM 1499 O ILE A 510 46.245 -2.445 68.311 1.00 13.59 O ANISOU 1499 O ILE A 510 1822 1953 1388 -15 206 94 O ATOM 1500 CB ILE A 510 43.922 -3.552 66.574 1.00 27.42 C ANISOU 1500 CB ILE A 510 3532 3650 3235 -81 241 -7 C ATOM 1501 CG1 ILE A 510 43.079 -4.764 66.361 1.00 33.50 C ANISOU 1501 CG1 ILE A 510 4252 4362 4116 -89 280 -56 C ATOM 1502 CG2 ILE A 510 45.249 -3.865 65.899 1.00 28.20 C ANISOU 1502 CG2 ILE A 510 3608 3766 3340 -91 250 -50 C ATOM 1503 CD1 ILE A 510 42.741 -4.906 64.905 1.00 35.55 C ANISOU 1503 CD1 ILE A 510 4455 4672 4380 -132 275 -192 C ATOM 1504 N LEU A 511 44.719 -0.931 68.083 1.00 13.81 N ANISOU 1504 N LEU A 511 1871 1992 1384 -41 158 70 N ATOM 1505 CA LEU A 511 45.649 0.194 68.135 1.00 16.13 C ANISOU 1505 CA LEU A 511 2159 2301 1668 -44 120 61 C ATOM 1506 C LEU A 511 46.385 0.287 69.475 1.00 15.89 C ANISOU 1506 C LEU A 511 2113 2311 1612 3 115 46 C ATOM 1507 O LEU A 511 47.504 0.795 69.529 1.00 16.97 O ANISOU 1507 O LEU A 511 2234 2459 1754 5 93 23 O ATOM 1508 CB LEU A 511 44.913 1.504 67.835 1.00 15.50 C ANISOU 1508 CB LEU A 511 2061 2199 1629 -63 82 60 C ATOM 1509 CG LEU A 511 44.313 1.586 66.427 1.00 19.11 C ANISOU 1509 CG LEU A 511 2508 2667 2084 -104 77 102 C ATOM 1510 CD1 LEU A 511 43.862 3.003 66.108 1.00 21.20 C ANISOU 1510 CD1 LEU A 511 2728 2900 2426 -119 38 150 C ATOM 1511 CD2 LEU A 511 45.292 1.082 65.368 1.00 18.30 C ANISOU 1511 CD2 LEU A 511 2397 2621 1936 -128 90 115 C ATOM 1512 N SER A 512 45.778 -0.207 70.549 1.00 13.05 N ANISOU 1512 N SER A 512 1741 2000 1217 44 136 64 N ATOM 1513 CA ASER A 512 46.450 -0.275 71.845 0.75 12.90 C ANISOU 1513 CA ASER A 512 1681 2090 1130 99 133 65 C ATOM 1514 CA BSER A 512 46.468 -0.250 71.832 0.25 13.01 C ANISOU 1514 CA BSER A 512 1695 2103 1145 98 132 63 C ATOM 1515 C SER A 512 47.601 -1.274 71.796 1.00 13.27 C ANISOU 1515 C SER A 512 1724 2139 1178 114 156 132 C ATOM 1516 O SER A 512 48.668 -1.053 72.370 1.00 12.14 O ANISOU 1516 O SER A 512 1549 2071 992 143 134 115 O ATOM 1517 CB ASER A 512 45.467 -0.669 72.950 0.75 12.24 C ANISOU 1517 CB ASER A 512 1563 2102 986 143 161 107 C ATOM 1518 CB BSER A 512 45.491 -0.570 72.962 0.25 12.59 C ANISOU 1518 CB BSER A 512 1606 2149 1028 143 157 98 C ATOM 1519 OG ASER A 512 46.158 -1.019 74.138 0.75 13.82 O ANISOU 1519 OG ASER A 512 1702 2462 1089 205 167 152 O ATOM 1520 OG BSER A 512 44.583 0.499 73.159 0.25 11.72 O ANISOU 1520 OG BSER A 512 1481 2049 923 134 131 2 O ATOM 1521 N HIS A 513 47.369 -2.386 71.114 1.00 11.94 N ANISOU 1521 N HIS A 513 1569 1887 1082 96 199 191 N ATOM 1522 CA HIS A 513 48.392 -3.409 70.968 1.00 10.90 C ANISOU 1522 CA HIS A 513 1412 1724 1004 108 227 243 C ATOM 1523 C HIS A 513 49.514 -2.924 70.056 1.00 12.01 C ANISOU 1523 C HIS A 513 1576 1839 1150 73 200 169 C ATOM 1524 O HIS A 513 50.686 -3.182 70.320 1.00 13.74 O ANISOU 1524 O HIS A 513 1772 2079 1371 94 198 187 O ATOM 1525 CB HIS A 513 47.771 -4.696 70.439 1.00 15.04 C ANISOU 1525 CB HIS A 513 1912 2143 1661 95 285 283 C ATOM 1526 CG HIS A 513 46.754 -5.282 71.365 1.00 20.26 C ANISOU 1526 CG HIS A 513 2530 2818 2351 133 324 393 C ATOM 1527 ND1 HIS A 513 47.098 -6.053 72.453 1.00 23.74 N ANISOU 1527 ND1 HIS A 513 2896 3312 2813 194 360 553 N ATOM 1528 CD2 HIS A 513 45.403 -5.176 71.388 1.00 22.61 C ANISOU 1528 CD2 HIS A 513 2834 3100 2656 121 337 389 C ATOM 1529 CE1 HIS A 513 46.001 -6.414 73.096 1.00 23.40 C ANISOU 1529 CE1 HIS A 513 2811 3290 2789 218 398 653 C ATOM 1530 NE2 HIS A 513 44.960 -5.896 72.468 1.00 22.93 N ANISOU 1530 NE2 HIS A 513 2806 3180 2726 173 385 543 N ATOM 1531 N ILE A 514 49.158 -2.210 68.994 1.00 10.43 N ANISOU 1531 N ILE A 514 1406 1608 949 21 181 106 N ATOM 1532 CA ILE A 514 50.176 -1.675 68.094 1.00 11.60 C ANISOU 1532 CA ILE A 514 1556 1756 1095 -12 163 68 C ATOM 1533 C ILE A 514 51.049 -0.655 68.835 1.00 11.18 C ANISOU 1533 C ILE A 514 1489 1738 1022 9 122 52 C ATOM 1534 O ILE A 514 52.270 -0.633 68.657 1.00 10.12 O ANISOU 1534 O ILE A 514 1339 1608 899 7 118 42 O ATOM 1535 CB ILE A 514 49.529 -1.052 66.841 1.00 14.42 C ANISOU 1535 CB ILE A 514 1919 2116 1443 -62 153 51 C ATOM 1536 CG1 ILE A 514 48.996 -2.169 65.942 1.00 19.76 C ANISOU 1536 CG1 ILE A 514 2579 2793 2136 -84 190 13 C ATOM 1537 CG2 ILE A 514 50.537 -0.187 66.072 1.00 13.02 C ANISOU 1537 CG2 ILE A 514 1722 1964 1260 -90 134 60 C ATOM 1538 CD1 ILE A 514 48.026 -1.708 64.891 1.00 22.29 C ANISOU 1538 CD1 ILE A 514 2890 3165 2416 -121 177 1 C ATOM 1539 N ARG A 515 50.435 0.166 69.685 1.00 11.52 N ANISOU 1539 N ARG A 515 1520 1810 1048 29 94 25 N ATOM 1540 CA ARG A 515 51.200 1.102 70.502 1.00 12.61 C ANISOU 1540 CA ARG A 515 1611 1993 1189 53 53 -43 C ATOM 1541 C ARG A 515 52.203 0.381 71.402 1.00 11.42 C ANISOU 1541 C ARG A 515 1431 1931 977 103 55 -30 C ATOM 1542 O ARG A 515 53.364 0.791 71.505 1.00 10.64 O ANISOU 1542 O ARG A 515 1298 1848 896 107 30 -77 O ATOM 1543 CB ARG A 515 50.283 1.959 71.370 1.00 13.40 C ANISOU 1543 CB ARG A 515 1673 2133 1285 72 27 -118 C ATOM 1544 CG ARG A 515 51.050 2.941 72.244 1.00 15.90 C ANISOU 1544 CG ARG A 515 1904 2511 1628 98 -18 -248 C ATOM 1545 CD ARG A 515 51.420 4.199 71.455 1.00 17.06 C ANISOU 1545 CD ARG A 515 2011 2526 1947 51 -42 -296 C ATOM 1546 NE ARG A 515 50.299 5.132 71.440 1.00 20.65 N ANISOU 1546 NE ARG A 515 2427 2916 2505 35 -55 -344 N ATOM 1547 CZ ARG A 515 50.415 6.457 71.468 1.00 22.78 C ANISOU 1547 CZ ARG A 515 2593 3093 2968 20 -85 -443 C ATOM 1548 NH1 ARG A 515 51.614 7.025 71.480 1.00 24.97 N ANISOU 1548 NH1 ARG A 515 2798 3332 3359 14 -104 -505 N ATOM 1549 NH2 ARG A 515 49.326 7.214 71.475 1.00 24.30 N ANISOU 1549 NH2 ARG A 515 2739 3215 3277 9 -94 -481 N ATOM 1550 N HIS A 516 51.742 -0.682 72.060 1.00 11.17 N ANISOU 1550 N HIS A 516 1396 1959 889 144 86 52 N ATOM 1551 CA HIS A 516 52.589 -1.492 72.939 1.00 14.81 C ANISOU 1551 CA HIS A 516 1808 2522 1299 201 93 123 C ATOM 1552 C HIS A 516 53.809 -2.053 72.200 1.00 13.50 C ANISOU 1552 C HIS A 516 1650 2276 1204 184 106 146 C ATOM 1553 O HIS A 516 54.944 -1.960 72.681 1.00 12.76 O ANISOU 1553 O HIS A 516 1512 2251 1084 213 81 133 O ATOM 1554 CB HIS A 516 51.772 -2.640 73.552 1.00 13.95 C ANISOU 1554 CB HIS A 516 1675 2455 1171 243 142 266 C ATOM 1555 CG HIS A 516 52.543 -3.488 74.518 1.00 17.26 C ANISOU 1555 CG HIS A 516 2013 2996 1547 312 153 398 C ATOM 1556 ND1 HIS A 516 52.836 -3.075 75.801 1.00 21.73 N ANISOU 1556 ND1 HIS A 516 2498 3801 1958 377 118 395 N ATOM 1557 CD2 HIS A 516 53.083 -4.723 74.389 1.00 16.32 C ANISOU 1557 CD2 HIS A 516 1859 2810 1532 331 195 538 C ATOM 1558 CE1 HIS A 516 53.525 -4.018 76.419 1.00 21.00 C ANISOU 1558 CE1 HIS A 516 2328 3801 1850 436 137 561 C ATOM 1559 NE2 HIS A 516 53.690 -5.028 75.584 1.00 19.14 N ANISOU 1559 NE2 HIS A 516 2119 3359 1793 409 185 658 N ATOM 1560 N MET A 517 53.568 -2.642 71.033 1.00 11.78 N ANISOU 1560 N MET A 517 1472 1932 1072 137 144 161 N ATOM 1561 CA MET A 517 54.643 -3.223 70.226 1.00 12.71 C ANISOU 1561 CA MET A 517 1582 1984 1262 117 164 154 C ATOM 1562 C MET A 517 55.627 -2.154 69.781 1.00 11.66 C ANISOU 1562 C MET A 517 1454 1860 1116 88 128 75 C ATOM 1563 O MET A 517 56.833 -2.377 69.768 1.00 10.86 O ANISOU 1563 O MET A 517 1325 1763 1039 98 126 71 O ATOM 1564 CB MET A 517 54.068 -3.954 69.010 1.00 13.88 C ANISOU 1564 CB MET A 517 1744 2037 1492 70 209 130 C ATOM 1565 CG MET A 517 53.263 -5.192 69.361 1.00 14.48 C ANISOU 1565 CG MET A 517 1785 2059 1659 96 256 202 C ATOM 1566 SD MET A 517 52.836 -6.147 67.891 1.00 19.30 S ANISOU 1566 SD MET A 517 2365 2564 2404 42 307 99 S ATOM 1567 CE MET A 517 51.817 -4.986 66.984 1.00 15.38 C ANISOU 1567 CE MET A 517 1932 2129 1783 -12 275 21 C ATOM 1568 N SER A 518 55.108 -0.987 69.422 1.00 10.09 N ANISOU 1568 N SER A 518 1275 1653 906 54 102 26 N ATOM 1569 CA SER A 518 55.966 0.125 69.051 1.00 13.12 C ANISOU 1569 CA SER A 518 1635 2023 1328 28 74 -23 C ATOM 1570 C SER A 518 56.856 0.545 70.210 1.00 10.86 C ANISOU 1570 C SER A 518 1293 1800 1032 72 33 -79 C ATOM 1571 O SER A 518 58.052 0.768 70.021 1.00 11.65 O ANISOU 1571 O SER A 518 1361 1890 1174 66 23 -105 O ATOM 1572 CB SER A 518 55.142 1.312 68.578 1.00 16.39 C ANISOU 1572 CB SER A 518 2047 2397 1783 -9 57 -34 C ATOM 1573 OG SER A 518 55.969 2.451 68.393 1.00 18.87 O ANISOU 1573 OG SER A 518 2305 2674 2190 -29 33 -64 O ATOM 1574 N ASN A 519 56.285 0.653 71.409 1.00 11.40 N ANISOU 1574 N ASN A 519 1335 1961 1035 120 8 -108 N ATOM 1575 CA ASN A 519 57.081 1.023 72.577 1.00 13.64 C ANISOU 1575 CA ASN A 519 1538 2371 1275 170 -37 -189 C ATOM 1576 C ASN A 519 58.194 0.007 72.834 1.00 13.69 C ANISOU 1576 C ASN A 519 1525 2431 1246 207 -28 -117 C ATOM 1577 O ASN A 519 59.321 0.373 73.151 1.00 12.34 O ANISOU 1577 O ASN A 519 1295 2307 1087 223 -62 -185 O ATOM 1578 CB ASN A 519 56.210 1.154 73.834 1.00 16.35 C ANISOU 1578 CB ASN A 519 1833 2871 1508 223 -58 -230 C ATOM 1579 CG ASN A 519 55.208 2.300 73.750 1.00 23.40 C ANISOU 1579 CG ASN A 519 2715 3712 2464 193 -75 -340 C ATOM 1580 OD1 ASN A 519 54.093 2.197 74.262 1.00 27.23 O ANISOU 1580 OD1 ASN A 519 3201 4266 2880 213 -66 -333 O ATOM 1581 ND2 ASN A 519 55.601 3.391 73.108 1.00 26.67 N ANISOU 1581 ND2 ASN A 519 3101 3998 3033 146 -95 -426 N ATOM 1582 N LYS A 520 57.878 -1.275 72.698 1.00 11.70 N ANISOU 1582 N LYS A 520 1304 2158 981 223 18 19 N ATOM 1583 CA LYS A 520 58.884 -2.309 72.924 1.00 13.40 C ANISOU 1583 CA LYS A 520 1481 2398 1212 261 33 109 C ATOM 1584 C LYS A 520 59.907 -2.330 71.794 1.00 12.11 C ANISOU 1584 C LYS A 520 1339 2110 1151 211 48 68 C ATOM 1585 O LYS A 520 61.100 -2.538 72.023 1.00 12.21 O ANISOU 1585 O LYS A 520 1304 2153 1182 235 34 68 O ATOM 1586 CB LYS A 520 58.222 -3.680 73.074 1.00 14.64 C ANISOU 1586 CB LYS A 520 1633 2529 1402 289 86 269 C ATOM 1587 CG LYS A 520 57.252 -3.754 74.248 1.00 20.30 C ANISOU 1587 CG LYS A 520 2308 3399 2005 345 82 350 C ATOM 1588 CD LYS A 520 57.972 -3.724 75.591 1.00 30.18 C ANISOU 1588 CD LYS A 520 3453 4891 3124 427 41 398 C ATOM 1589 CE LYS A 520 58.012 -5.114 76.214 1.00 37.16 C ANISOU 1589 CE LYS A 520 4253 5829 4035 494 84 649 C ATOM 1590 NZ LYS A 520 58.126 -5.057 77.699 1.00 40.44 N ANISOU 1590 NZ LYS A 520 4545 6569 4252 587 50 742 N ATOM 1591 N GLY A 521 59.439 -2.111 70.571 1.00 13.33 N ANISOU 1591 N GLY A 521 1551 2153 1360 145 77 35 N ATOM 1592 CA GLY A 521 60.332 -2.025 69.429 1.00 13.96 C ANISOU 1592 CA GLY A 521 1635 2163 1507 97 98 -3 C ATOM 1593 C GLY A 521 61.290 -0.853 69.539 1.00 14.89 C ANISOU 1593 C GLY A 521 1716 2298 1643 87 57 -73 C ATOM 1594 O GLY A 521 62.458 -0.944 69.141 1.00 13.91 O ANISOU 1594 O GLY A 521 1564 2155 1567 76 65 -89 O ATOM 1595 N MET A 522 60.802 0.254 70.087 1.00 12.04 N ANISOU 1595 N MET A 522 1339 1963 1273 89 16 -129 N ATOM 1596 CA MET A 522 61.632 1.439 70.250 1.00 14.12 C ANISOU 1596 CA MET A 522 1536 2217 1614 78 -23 -221 C ATOM 1597 C MET A 522 62.712 1.196 71.296 1.00 13.93 C ANISOU 1597 C MET A 522 1443 2293 1556 135 -62 -276 C ATOM 1598 O MET A 522 63.859 1.607 71.115 1.00 13.40 O ANISOU 1598 O MET A 522 1325 2199 1569 123 -75 -327 O ATOM 1599 CB MET A 522 60.788 2.649 70.647 1.00 14.63 C ANISOU 1599 CB MET A 522 1565 2268 1725 70 -56 -301 C ATOM 1600 CG MET A 522 61.458 3.977 70.326 1.00 17.66 C ANISOU 1600 CG MET A 522 1862 2560 2287 34 -75 -376 C ATOM 1601 SD MET A 522 61.393 4.288 68.554 1.00 20.01 S ANISOU 1601 SD MET A 522 2188 2734 2679 -42 -16 -225 S ATOM 1602 CE MET A 522 59.632 4.512 68.324 1.00 24.93 C ANISOU 1602 CE MET A 522 2860 3338 3274 -56 -9 -172 C ATOM 1603 N GLU A 523 62.342 0.536 72.394 1.00 13.93 N ANISOU 1603 N GLU A 523 1428 2427 1437 199 -81 -249 N ATOM 1604 CA GLU A 523 63.313 0.147 73.416 1.00 15.22 C ANISOU 1604 CA GLU A 523 1510 2739 1534 266 -119 -260 C ATOM 1605 C GLU A 523 64.367 -0.797 72.845 1.00 15.56 C ANISOU 1605 C GLU A 523 1563 2715 1634 263 -87 -172 C ATOM 1606 O GLU A 523 65.550 -0.687 73.168 1.00 16.02 O ANISOU 1606 O GLU A 523 1554 2824 1711 286 -118 -219 O ATOM 1607 CB GLU A 523 62.619 -0.523 74.604 1.00 17.60 C ANISOU 1607 CB GLU A 523 1777 3230 1681 340 -131 -181 C ATOM 1608 CG GLU A 523 61.768 0.416 75.445 1.00 25.30 C ANISOU 1608 CG GLU A 523 2701 4339 2571 359 -171 -311 C ATOM 1609 CD GLU A 523 60.874 -0.326 76.425 0.21 29.46 C ANISOU 1609 CD GLU A 523 3202 5058 2934 426 -162 -191 C ATOM 1610 OE1 GLU A 523 61.353 -1.284 77.067 0.62 31.49 O ANISOU 1610 OE1 GLU A 523 3401 5458 3106 491 -160 -42 O ATOM 1611 OE2 GLU A 523 59.687 0.042 76.549 0.66 32.22 O ANISOU 1611 OE2 GLU A 523 3574 5417 3250 415 -153 -224 O ATOM 1612 N HIS A 524 63.932 -1.734 72.007 1.00 14.59 N ANISOU 1612 N HIS A 524 1509 2483 1554 237 -25 -66 N ATOM 1613 CA HIS A 524 64.860 -2.677 71.396 1.00 14.81 C ANISOU 1613 CA HIS A 524 1526 2434 1665 232 13 -13 C ATOM 1614 C HIS A 524 65.846 -1.965 70.474 1.00 15.72 C ANISOU 1614 C HIS A 524 1637 2477 1858 177 18 -103 C ATOM 1615 O HIS A 524 67.047 -2.227 70.513 1.00 13.83 O ANISOU 1615 O HIS A 524 1347 2241 1665 192 13 -114 O ATOM 1616 CB HIS A 524 64.116 -3.760 70.610 1.00 13.63 C ANISOU 1616 CB HIS A 524 1421 2181 1579 210 81 60 C ATOM 1617 CG HIS A 524 65.035 -4.737 69.942 1.00 14.98 C ANISOU 1617 CG HIS A 524 1554 2267 1870 202 124 70 C ATOM 1618 ND1 HIS A 524 65.483 -4.576 68.647 1.00 14.47 N ANISOU 1618 ND1 HIS A 524 1504 2136 1856 139 161 -18 N ATOM 1619 CD2 HIS A 524 65.616 -5.871 70.402 1.00 19.56 C ANISOU 1619 CD2 HIS A 524 2062 2828 2543 254 139 160 C ATOM 1620 CE1 HIS A 524 66.293 -5.575 68.336 1.00 18.69 C ANISOU 1620 CE1 HIS A 524 1981 2614 2506 149 197 -19 C ATOM 1621 NE2 HIS A 524 66.390 -6.374 69.384 1.00 21.18 N ANISOU 1621 NE2 HIS A 524 2242 2935 2869 218 184 92 N ATOM 1622 N LEU A 525 65.334 -1.063 69.645 1.00 12.45 N ANISOU 1622 N LEU A 525 1262 2004 1463 115 32 -147 N ATOM 1623 CA LEU A 525 66.180 -0.351 68.695 1.00 14.65 C ANISOU 1623 CA LEU A 525 1517 2225 1823 61 49 -186 C ATOM 1624 C LEU A 525 67.201 0.504 69.434 1.00 14.27 C ANISOU 1624 C LEU A 525 1389 2202 1829 81 -5 -269 C ATOM 1625 O LEU A 525 68.369 0.569 69.048 1.00 13.42 O ANISOU 1625 O LEU A 525 1237 2068 1793 67 6 -289 O ATOM 1626 CB LEU A 525 65.335 0.520 67.757 1.00 14.52 C ANISOU 1626 CB LEU A 525 1530 2163 1825 2 73 -166 C ATOM 1627 CG LEU A 525 66.108 1.296 66.682 1.00 16.42 C ANISOU 1627 CG LEU A 525 1723 2366 2152 -54 104 -148 C ATOM 1628 CD1 LEU A 525 66.906 0.355 65.795 1.00 14.57 C ANISOU 1628 CD1 LEU A 525 1482 2156 1897 -69 159 -134 C ATOM 1629 CD2 LEU A 525 65.157 2.151 65.848 1.00 17.66 C ANISOU 1629 CD2 LEU A 525 1884 2502 2325 -101 125 -76 C ATOM 1630 N TYR A 526 66.756 1.155 70.505 1.00 14.53 N ANISOU 1630 N TYR A 526 1387 2302 1833 116 -63 -340 N ATOM 1631 CA TYR A 526 67.644 1.975 71.321 1.00 14.98 C ANISOU 1631 CA TYR A 526 1337 2409 1946 140 -123 -473 C ATOM 1632 C TYR A 526 68.772 1.131 71.890 1.00 16.92 C ANISOU 1632 C TYR A 526 1538 2748 2144 194 -144 -463 C ATOM 1633 O TYR A 526 69.920 1.577 71.968 1.00 17.16 O ANISOU 1633 O TYR A 526 1488 2773 2259 192 -169 -546 O ATOM 1634 CB TYR A 526 66.858 2.648 72.452 1.00 15.43 C ANISOU 1634 CB TYR A 526 1341 2572 1951 177 -181 -588 C ATOM 1635 CG TYR A 526 67.643 3.690 73.219 1.00 18.80 C ANISOU 1635 CG TYR A 526 1622 3051 2470 194 -246 -790 C ATOM 1636 CD1 TYR A 526 67.945 4.919 72.644 1.00 21.95 C ANISOU 1636 CD1 TYR A 526 1952 3288 3102 136 -241 -880 C ATOM 1637 CD2 TYR A 526 68.063 3.455 74.519 1.00 24.65 C ANISOU 1637 CD2 TYR A 526 2269 4017 3079 271 -311 -891 C ATOM 1638 CE1 TYR A 526 68.656 5.875 73.334 1.00 27.75 C ANISOU 1638 CE1 TYR A 526 2526 4045 3974 148 -298 -1097 C ATOM 1639 CE2 TYR A 526 68.775 4.407 75.220 1.00 31.06 C ANISOU 1639 CE2 TYR A 526 2922 4901 3977 287 -376 -1124 C ATOM 1640 CZ TYR A 526 69.067 5.617 74.621 1.00 33.29 C ANISOU 1640 CZ TYR A 526 3137 4982 4530 223 -369 -1244 C ATOM 1641 OH TYR A 526 69.774 6.574 75.309 1.00 41.67 O ANISOU 1641 OH TYR A 526 4021 6085 5727 236 -427 -1503 O ATOM 1642 N ASER A 527 68.465 -0.102 72.280 0.41 16.33 N ANISOU 1642 N ASER A 527 1497 2747 1960 242 -132 -347 N ATOM 1643 N BSER A 527 68.419 -0.088 72.286 0.59 16.12 N ANISOU 1643 N BSER A 527 1472 2720 1931 242 -132 -347 N ATOM 1644 CA ASER A 527 69.488 -0.961 72.865 0.41 18.04 C ANISOU 1644 CA ASER A 527 1652 3052 2151 302 -152 -298 C ATOM 1645 CA BSER A 527 69.369 -1.042 72.835 0.59 18.31 C ANISOU 1645 CA BSER A 527 1694 3082 2181 302 -147 -285 C ATOM 1646 C ASER A 527 70.488 -1.431 71.807 0.41 18.04 C ANISOU 1646 C ASER A 527 1664 2916 2273 262 -102 -270 C ATOM 1647 C BSER A 527 70.446 -1.385 71.812 0.59 17.90 C ANISOU 1647 C BSER A 527 1649 2900 2254 261 -103 -273 C ATOM 1648 O ASER A 527 71.672 -1.583 72.103 0.41 19.82 O ANISOU 1648 O ASER A 527 1816 3179 2534 290 -127 -293 O ATOM 1649 O BSER A 527 71.633 -1.393 72.133 0.59 19.94 O ANISOU 1649 O BSER A 527 1830 3198 2548 287 -133 -311 O ATOM 1650 CB ASER A 527 68.855 -2.160 73.574 0.41 19.25 C ANISOU 1650 CB ASER A 527 1806 3304 2204 369 -144 -138 C ATOM 1651 CB BSER A 527 68.644 -2.309 73.293 0.59 19.49 C ANISOU 1651 CB BSER A 527 1864 3289 2252 355 -124 -117 C ATOM 1652 OG ASER A 527 68.317 -3.083 72.649 0.41 19.09 O ANISOU 1652 OG ASER A 527 1863 3132 2258 335 -69 -32 O ATOM 1653 OG BSER A 527 69.543 -3.223 73.892 0.59 20.40 O ANISOU 1653 OG BSER A 527 1898 3485 2368 421 -139 -18 O ATOM 1654 N MET A 528 70.023 -1.654 70.579 1.00 16.37 N ANISOU 1654 N MET A 528 1530 2575 2114 200 -32 -233 N ATOM 1655 CA MET A 528 70.937 -1.989 69.483 1.00 17.31 C ANISOU 1655 CA MET A 528 1642 2604 2330 157 23 -238 C ATOM 1656 C MET A 528 71.883 -0.833 69.195 1.00 17.98 C ANISOU 1656 C MET A 528 1674 2666 2492 120 7 -325 C ATOM 1657 O MET A 528 73.089 -1.030 69.025 1.00 20.14 O ANISOU 1657 O MET A 528 1892 2925 2834 122 14 -348 O ATOM 1658 CB MET A 528 70.162 -2.354 68.212 1.00 18.35 C ANISOU 1658 CB MET A 528 1839 2665 2467 99 97 -211 C ATOM 1659 CG MET A 528 69.289 -3.600 68.330 1.00 23.47 C ANISOU 1659 CG MET A 528 2516 3297 3103 127 125 -146 C ATOM 1660 SD MET A 528 70.234 -5.123 68.569 1.00 27.75 S ANISOU 1660 SD MET A 528 2979 3796 3768 178 149 -102 S ATOM 1661 CE MET A 528 70.122 -5.345 70.344 1.00 30.69 C ANISOU 1661 CE MET A 528 3306 4277 4079 276 77 20 C ATOM 1662 N LYS A 529 71.328 0.373 69.142 1.00 16.20 N ANISOU 1662 N LYS A 529 1450 2420 2286 87 -9 -367 N ATOM 1663 CA LYS A 529 72.126 1.581 68.942 1.00 15.90 C ANISOU 1663 CA LYS A 529 1331 2330 2382 51 -22 -440 C ATOM 1664 C LYS A 529 73.179 1.752 70.041 1.00 20.17 C ANISOU 1664 C LYS A 529 1771 2937 2955 103 -92 -552 C ATOM 1665 O LYS A 529 74.343 2.049 69.761 1.00 18.28 O ANISOU 1665 O LYS A 529 1462 2656 2830 86 -86 -593 O ATOM 1666 CB LYS A 529 71.228 2.822 68.901 1.00 20.38 C ANISOU 1666 CB LYS A 529 1884 2843 3015 18 -33 -466 C ATOM 1667 CG LYS A 529 71.986 4.146 68.882 1.00 23.02 C ANISOU 1667 CG LYS A 529 2093 3092 3561 -12 -50 -549 C ATOM 1668 CD LYS A 529 71.072 5.298 69.263 1.00 29.87 C ANISOU 1668 CD LYS A 529 2911 3904 4534 -24 -81 -617 C ATOM 1669 CE LYS A 529 71.332 5.790 70.679 1.00 31.70 C ANISOU 1669 CE LYS A 529 3033 4210 4803 28 -169 -838 C ATOM 1670 NZ LYS A 529 72.229 6.987 70.671 1.00 35.39 N ANISOU 1670 NZ LYS A 529 3333 4556 5556 -2 -183 -962 N ATOM 1671 N CYS A 530 72.763 1.564 71.290 1.00 19.30 N ANISOU 1671 N CYS A 530 1642 2959 2734 170 -159 -601 N ATOM 1672 CA CYS A 530 73.647 1.798 72.433 1.00 18.71 C ANISOU 1672 CA CYS A 530 1445 3015 2650 228 -239 -728 C ATOM 1673 C CYS A 530 74.719 0.719 72.563 1.00 19.35 C ANISOU 1673 C CYS A 530 1503 3148 2701 271 -239 -656 C ATOM 1674 O CYS A 530 75.700 0.892 73.286 1.00 23.25 O ANISOU 1674 O CYS A 530 1885 3742 3205 313 -300 -750 O ATOM 1675 CB CYS A 530 72.833 1.892 73.722 1.00 22.09 C ANISOU 1675 CB CYS A 530 1835 3635 2924 293 -306 -793 C ATOM 1676 SG CYS A 530 71.819 3.372 73.789 1.00 30.14 S ANISOU 1676 SG CYS A 530 2820 4594 4037 250 -323 -952 S ATOM 1677 N LYS A 531 74.536 -0.384 71.849 1.00 16.49 N ANISOU 1677 N LYS A 531 957 2603 2706 -162 -188 370 N ATOM 1678 CA LYS A 531 75.529 -1.445 71.824 1.00 23.49 C ANISOU 1678 CA LYS A 531 1900 3380 3646 -145 -352 266 C ATOM 1679 C LYS A 531 76.335 -1.447 70.523 1.00 20.83 C ANISOU 1679 C LYS A 531 1651 2907 3358 -160 -397 0 C ATOM 1680 O LYS A 531 77.137 -2.350 70.293 1.00 19.43 O ANISOU 1680 O LYS A 531 1533 2648 3204 -105 -557 -119 O ATOM 1681 CB LYS A 531 74.857 -2.806 72.036 1.00 25.77 C ANISOU 1681 CB LYS A 531 2164 3545 4080 -212 -553 588 C ATOM 1682 CG LYS A 531 74.291 -2.988 73.435 1.00 29.48 C ANISOU 1682 CG LYS A 531 2501 4228 4470 -139 -478 939 C ATOM 1683 CD LYS A 531 73.991 -4.447 73.740 1.00 36.39 C ANISOU 1683 CD LYS A 531 3328 4937 5561 -213 -691 1297 C ATOM 1684 CE LYS A 531 72.667 -4.894 73.154 1.00 40.52 C ANISOU 1684 CE LYS A 531 3757 5272 6365 -422 -809 1630 C ATOM 1685 NZ LYS A 531 72.444 -6.359 73.382 1.00 47.10 N ANISOU 1685 NZ LYS A 531 4562 5820 7514 -538 -1059 1962 N ATOM 1686 N ASN A 532 76.133 -0.421 69.696 1.00 16.30 N ANISOU 1686 N ASN A 532 1076 2344 2772 -190 -247 -71 N ATOM 1687 CA ASN A 532 76.835 -0.286 68.415 1.00 19.09 C ANISOU 1687 CA ASN A 532 1471 2663 3120 -145 -226 -243 C ATOM 1688 C ASN A 532 76.697 -1.528 67.539 1.00 20.51 C ANISOU 1688 C ASN A 532 1747 2722 3323 -76 -483 -266 C ATOM 1689 O ASN A 532 77.643 -1.933 66.866 1.00 18.79 O ANISOU 1689 O ASN A 532 1568 2534 3039 67 -550 -449 O ATOM 1690 CB ASN A 532 78.325 0.026 68.628 1.00 18.66 C ANISOU 1690 CB ASN A 532 1353 2690 3047 -86 -145 -451 C ATOM 1691 CG ASN A 532 78.567 1.459 69.069 1.00 16.47 C ANISOU 1691 CG ASN A 532 970 2454 2833 -143 52 -498 C ATOM 1692 OD1 ASN A 532 77.878 1.969 69.954 1.00 19.18 O ANISOU 1692 OD1 ASN A 532 1304 2812 3170 -160 74 -445 O ATOM 1693 ND2 ASN A 532 79.547 2.122 68.448 1.00 15.82 N ANISOU 1693 ND2 ASN A 532 826 2381 2805 -144 172 -566 N ATOM 1694 N VAL A 533 75.514 -2.130 67.557 1.00 18.45 N ANISOU 1694 N VAL A 533 1504 2332 3174 -153 -657 -86 N ATOM 1695 CA VAL A 533 75.227 -3.288 66.720 1.00 22.58 C ANISOU 1695 CA VAL A 533 2115 2661 3805 -87 -1000 -142 C ATOM 1696 C VAL A 533 75.079 -2.885 65.253 1.00 19.07 C ANISOU 1696 C VAL A 533 1730 2268 3247 69 -996 -295 C ATOM 1697 O VAL A 533 75.540 -3.585 64.352 1.00 21.07 O ANISOU 1697 O VAL A 533 2079 2485 3442 289 -1225 -512 O ATOM 1698 CB VAL A 533 73.943 -4.007 67.189 1.00 26.32 C ANISOU 1698 CB VAL A 533 2536 2944 4522 -253 -1204 144 C ATOM 1699 CG1 VAL A 533 73.577 -5.138 66.242 1.00 27.05 C ANISOU 1699 CG1 VAL A 533 2776 2754 4748 -171 -1538 42 C ATOM 1700 CG2 VAL A 533 74.126 -4.530 68.606 1.00 27.01 C ANISOU 1700 CG2 VAL A 533 2561 3028 4675 -334 -1191 362 C ATOM 1701 N VAL A 534 74.441 -1.747 65.020 1.00 20.25 N ANISOU 1701 N VAL A 534 1828 2530 3335 11 -743 -187 N ATOM 1702 CA VAL A 534 74.127 -1.319 63.666 1.00 21.37 C ANISOU 1702 CA VAL A 534 2019 2749 3351 183 -718 -267 C ATOM 1703 C VAL A 534 74.277 0.191 63.557 1.00 19.90 C ANISOU 1703 C VAL A 534 1775 2737 3050 160 -314 -174 C ATOM 1704 O VAL A 534 73.890 0.920 64.471 1.00 17.85 O ANISOU 1704 O VAL A 534 1450 2473 2860 -17 -147 -37 O ATOM 1705 CB VAL A 534 72.687 -1.745 63.261 1.00 33.08 C ANISOU 1705 CB VAL A 534 3508 4085 4976 142 -979 -193 C ATOM 1706 CG1 VAL A 534 71.688 -1.334 64.332 1.00 29.00 C ANISOU 1706 CG1 VAL A 534 2868 3548 4603 -123 -858 96 C ATOM 1707 CG2 VAL A 534 72.295 -1.167 61.908 1.00 36.21 C ANISOU 1707 CG2 VAL A 534 3956 4609 5191 369 -933 -281 C ATOM 1708 N PRO A 535 74.865 0.668 62.450 1.00 24.16 N ANISOU 1708 N PRO A 535 2326 3438 3417 375 -167 -233 N ATOM 1709 CA PRO A 535 74.866 2.113 62.222 1.00 25.72 C ANISOU 1709 CA PRO A 535 2456 3734 3581 339 187 -77 C ATOM 1710 C PRO A 535 73.488 2.565 61.749 1.00 24.01 C ANISOU 1710 C PRO A 535 2288 3498 3338 351 184 27 C ATOM 1711 O PRO A 535 72.953 2.024 60.782 1.00 27.06 O ANISOU 1711 O PRO A 535 2745 3924 3612 556 -3 -49 O ATOM 1712 CB PRO A 535 75.933 2.296 61.141 1.00 27.59 C ANISOU 1712 CB PRO A 535 2649 4190 3644 597 342 -86 C ATOM 1713 CG PRO A 535 75.909 1.011 60.384 1.00 31.15 C ANISOU 1713 CG PRO A 535 3209 4698 3930 886 16 -293 C ATOM 1714 CD PRO A 535 75.597 -0.061 61.397 1.00 29.26 C ANISOU 1714 CD PRO A 535 3027 4209 3880 699 -311 -413 C ATOM 1715 N LEU A 536 72.901 3.525 62.449 1.00 22.16 N ANISOU 1715 N LEU A 536 2014 3208 3197 174 348 162 N ATOM 1716 CA LEU A 536 71.605 4.049 62.063 1.00 20.40 C ANISOU 1716 CA LEU A 536 1822 2995 2935 199 367 266 C ATOM 1717 C LEU A 536 71.775 5.347 61.282 1.00 21.78 C ANISOU 1717 C LEU A 536 2001 3243 3030 310 660 390 C ATOM 1718 O LEU A 536 72.699 6.119 61.547 1.00 22.30 O ANISOU 1718 O LEU A 536 2003 3278 3191 240 867 450 O ATOM 1719 CB LEU A 536 70.735 4.276 63.296 1.00 21.63 C ANISOU 1719 CB LEU A 536 1926 3093 3200 8 351 357 C ATOM 1720 CG LEU A 536 70.419 3.045 64.148 1.00 23.26 C ANISOU 1720 CG LEU A 536 2080 3242 3517 -113 99 367 C ATOM 1721 CD1 LEU A 536 69.555 3.432 65.348 1.00 25.61 C ANISOU 1721 CD1 LEU A 536 2282 3600 3847 -220 160 535 C ATOM 1722 CD2 LEU A 536 69.733 1.974 63.307 1.00 19.97 C ANISOU 1722 CD2 LEU A 536 1681 2757 3151 -54 -208 331 C ATOM 1723 N SER A 537 70.891 5.581 60.319 1.00 19.03 N ANISOU 1723 N SER A 537 1710 2977 2543 484 658 444 N ATOM 1724 CA SER A 537 70.908 6.831 59.567 1.00 23.28 C ANISOU 1724 CA SER A 537 2258 3581 3008 610 942 627 C ATOM 1725 C SER A 537 70.614 7.992 60.506 1.00 21.60 C ANISOU 1725 C SER A 537 2073 3172 2962 385 1013 684 C ATOM 1726 O SER A 537 70.035 7.794 61.575 1.00 20.93 O ANISOU 1726 O SER A 537 1959 3037 2956 248 918 626 O ATOM 1727 CB SER A 537 69.886 6.797 58.431 1.00 25.95 C ANISOU 1727 CB SER A 537 2673 4058 3127 880 874 639 C ATOM 1728 OG SER A 537 68.565 6.821 58.942 1.00 24.24 O ANISOU 1728 OG SER A 537 2469 3772 2970 767 733 618 O ATOM 1729 N ASP A 538 71.022 9.195 60.118 1.00 25.85 N ANISOU 1729 N ASP A 538 2054 3054 4714 -224 439 808 N ATOM 1730 CA ASP A 538 70.760 10.369 60.938 1.00 25.85 C ANISOU 1730 CA ASP A 538 2158 2814 4851 -439 412 744 C ATOM 1731 C ASP A 538 69.261 10.537 61.168 1.00 24.69 C ANISOU 1731 C ASP A 538 2257 2536 4588 -335 412 662 C ATOM 1732 O ASP A 538 68.831 10.882 62.272 1.00 22.98 O ANISOU 1732 O ASP A 538 2161 2197 4375 -424 312 509 O ATOM 1733 CB ASP A 538 71.345 11.624 60.290 1.00 28.76 C ANISOU 1733 CB ASP A 538 2442 3042 5442 -586 591 928 C ATOM 1734 CG ASP A 538 72.861 11.571 60.169 1.00 37.51 C ANISOU 1734 CG ASP A 538 3307 4329 6614 -707 569 972 C ATOM 1735 OD1 ASP A 538 73.514 10.929 61.022 1.00 38.60 O ANISOU 1735 OD1 ASP A 538 3307 4630 6730 -780 391 831 O ATOM 1736 OD2 ASP A 538 73.400 12.175 59.216 1.00 40.07 O ANISOU 1736 OD2 ASP A 538 3564 4666 6996 -702 738 1172 O ATOM 1737 N LEU A 539 68.469 10.273 60.132 1.00 21.31 N ANISOU 1737 N LEU A 539 1871 2203 4024 -123 517 745 N ATOM 1738 CA LEU A 539 67.019 10.357 60.259 1.00 20.67 C ANISOU 1738 CA LEU A 539 1951 2092 3810 -8 516 675 C ATOM 1739 C LEU A 539 66.527 9.410 61.346 1.00 18.95 C ANISOU 1739 C LEU A 539 1784 1897 3522 -44 360 499 C ATOM 1740 O LEU A 539 65.796 9.826 62.244 1.00 19.25 O ANISOU 1740 O LEU A 539 1941 1846 3528 -72 322 423 O ATOM 1741 CB LEU A 539 66.323 10.046 58.931 1.00 21.41 C ANISOU 1741 CB LEU A 539 2004 2407 3725 233 611 745 C ATOM 1742 CG LEU A 539 64.788 10.020 58.996 1.00 22.50 C ANISOU 1742 CG LEU A 539 2226 2620 3703 356 592 657 C ATOM 1743 CD1 LEU A 539 64.222 11.336 59.513 1.00 21.76 C ANISOU 1743 CD1 LEU A 539 2286 2326 3655 371 670 735 C ATOM 1744 CD2 LEU A 539 64.173 9.675 57.647 1.00 22.67 C ANISOU 1744 CD2 LEU A 539 2143 2963 3508 597 645 666 C ATOM 1745 N LEU A 540 66.945 8.146 61.284 1.00 17.82 N ANISOU 1745 N LEU A 540 1554 1861 3356 -17 298 458 N ATOM 1746 CA LEU A 540 66.539 7.175 62.292 1.00 18.07 C ANISOU 1746 CA LEU A 540 1632 1876 3356 -35 204 373 C ATOM 1747 C LEU A 540 67.008 7.561 63.691 1.00 20.20 C ANISOU 1747 C LEU A 540 1929 2109 3637 -136 108 352 C ATOM 1748 O LEU A 540 66.257 7.417 64.652 1.00 21.15 O ANISOU 1748 O LEU A 540 2133 2226 3676 -126 71 316 O ATOM 1749 CB LEU A 540 67.052 5.778 61.947 1.00 19.74 C ANISOU 1749 CB LEU A 540 1776 2129 3596 40 191 358 C ATOM 1750 CG LEU A 540 66.100 4.871 61.163 1.00 21.16 C ANISOU 1750 CG LEU A 540 1971 2317 3753 110 227 245 C ATOM 1751 CD1 LEU A 540 66.705 3.474 61.009 1.00 20.41 C ANISOU 1751 CD1 LEU A 540 1859 2152 3743 185 224 197 C ATOM 1752 CD2 LEU A 540 64.728 4.806 61.827 1.00 21.84 C ANISOU 1752 CD2 LEU A 540 2124 2358 3817 37 221 202 C ATOM 1753 N LEU A 541 68.242 8.045 63.803 1.00 17.80 N ANISOU 1753 N LEU A 541 1521 1829 3415 -226 66 364 N ATOM 1754 CA LEU A 541 68.770 8.477 65.096 1.00 19.60 C ANISOU 1754 CA LEU A 541 1726 2095 3624 -328 -66 268 C ATOM 1755 C LEU A 541 67.874 9.532 65.723 1.00 21.19 C ANISOU 1755 C LEU A 541 2093 2169 3789 -371 -70 144 C ATOM 1756 O LEU A 541 67.600 9.501 66.920 1.00 22.21 O ANISOU 1756 O LEU A 541 2275 2381 3781 -342 -168 41 O ATOM 1757 CB LEU A 541 70.192 9.025 64.953 1.00 22.33 C ANISOU 1757 CB LEU A 541 1877 2503 4106 -480 -109 258 C ATOM 1758 CG LEU A 541 71.246 7.966 64.650 1.00 25.49 C ANISOU 1758 CG LEU A 541 2077 3114 4492 -384 -130 368 C ATOM 1759 CD1 LEU A 541 72.590 8.625 64.368 1.00 26.22 C ANISOU 1759 CD1 LEU A 541 1914 3314 4734 -558 -144 383 C ATOM 1760 CD2 LEU A 541 71.356 6.994 65.807 1.00 28.62 C ANISOU 1760 CD2 LEU A 541 2464 3682 4728 -247 -252 362 C ATOM 1761 N GLU A 542 67.419 10.463 64.896 1.00 19.47 N ANISOU 1761 N GLU A 542 1958 1773 3667 -388 55 175 N ATOM 1762 CA GLU A 542 66.567 11.545 65.363 1.00 20.32 C ANISOU 1762 CA GLU A 542 2247 1713 3759 -373 87 69 C ATOM 1763 C GLU A 542 65.146 11.074 65.675 1.00 19.34 C ANISOU 1763 C GLU A 542 2225 1690 3434 -190 114 82 C ATOM 1764 O GLU A 542 64.571 11.503 66.675 1.00 20.64 O ANISOU 1764 O GLU A 542 2500 1857 3486 -136 74 -43 O ATOM 1765 CB GLU A 542 66.555 12.684 64.338 1.00 21.53 C ANISOU 1765 CB GLU A 542 2462 1624 4093 -394 257 171 C ATOM 1766 CG GLU A 542 67.865 13.468 64.333 1.00 26.87 C ANISOU 1766 CG GLU A 542 3045 2129 5036 -649 252 130 C ATOM 1767 CD GLU A 542 67.853 14.669 63.409 1.00 31.38 C ANISOU 1767 CD GLU A 542 3699 2383 5841 -675 477 296 C ATOM 1768 OE1 GLU A 542 66.805 14.946 62.795 1.00 30.39 O ANISOU 1768 OE1 GLU A 542 3717 2208 5622 -437 626 444 O ATOM 1769 OE2 GLU A 542 68.902 15.342 63.302 1.00 35.08 O ANISOU 1769 OE2 GLU A 542 4080 2723 6527 -901 502 292 O ATOM 1770 N MET A 543 64.590 10.195 64.839 1.00 17.27 N ANISOU 1770 N MET A 543 1900 1537 3124 -98 179 206 N ATOM 1771 CA MET A 543 63.257 9.631 65.088 1.00 21.61 C ANISOU 1771 CA MET A 543 2472 2211 3528 13 207 219 C ATOM 1772 C MET A 543 63.262 8.849 66.395 1.00 25.31 C ANISOU 1772 C MET A 543 2931 2780 3905 0 127 203 C ATOM 1773 O MET A 543 62.298 8.876 67.167 1.00 25.97 O ANISOU 1773 O MET A 543 3058 2958 3850 82 151 202 O ATOM 1774 CB MET A 543 62.808 8.707 63.942 1.00 23.76 C ANISOU 1774 CB MET A 543 2634 2588 3804 51 258 277 C ATOM 1775 CG MET A 543 62.761 9.359 62.568 1.00 28.66 C ANISOU 1775 CG MET A 543 3230 3231 4429 144 347 332 C ATOM 1776 SD MET A 543 61.524 10.660 62.429 1.00 34.82 S ANISOU 1776 SD MET A 543 4108 4032 5091 335 455 379 S ATOM 1777 CE MET A 543 60.045 9.718 62.074 1.00 27.72 C ANISOU 1777 CE MET A 543 3050 3456 4027 416 444 326 C ATOM 1778 N LEU A 544 64.366 8.148 66.626 1.00 22.12 N ANISOU 1778 N LEU A 544 2452 2396 3555 -61 52 230 N ATOM 1779 CA LEU A 544 64.550 7.355 67.828 1.00 22.70 C ANISOU 1779 CA LEU A 544 2504 2600 3522 -13 -5 284 C ATOM 1780 C LEU A 544 64.744 8.271 69.028 1.00 24.57 C ANISOU 1780 C LEU A 544 2795 2941 3599 18 -105 142 C ATOM 1781 O LEU A 544 64.199 8.028 70.106 1.00 25.82 O ANISOU 1781 O LEU A 544 2981 3269 3560 138 -107 176 O ATOM 1782 CB LEU A 544 65.748 6.417 67.651 1.00 20.89 C ANISOU 1782 CB LEU A 544 2170 2390 3376 -17 -48 368 C ATOM 1783 CG LEU A 544 66.213 5.517 68.793 1.00 23.79 C ANISOU 1783 CG LEU A 544 2497 2915 3628 101 -91 497 C ATOM 1784 CD1 LEU A 544 65.108 4.569 69.223 1.00 21.21 C ANISOU 1784 CD1 LEU A 544 2223 2556 3278 175 40 675 C ATOM 1785 CD2 LEU A 544 67.445 4.740 68.351 1.00 23.84 C ANISOU 1785 CD2 LEU A 544 2396 2930 3734 143 -115 579 C ATOM 1786 N ASP A 545 65.507 9.341 68.823 1.00 22.57 N ANISOU 1786 N ASP A 545 2549 2587 3438 -94 -176 -28 N ATOM 1787 CA ASP A 545 65.807 10.299 69.884 1.00 27.11 C ANISOU 1787 CA ASP A 545 3173 3221 3908 -110 -301 -275 C ATOM 1788 C ASP A 545 64.581 11.072 70.368 1.00 26.25 C ANISOU 1788 C ASP A 545 3241 3071 3663 21 -239 -384 C ATOM 1789 O ASP A 545 64.547 11.543 71.509 1.00 25.54 O ANISOU 1789 O ASP A 545 3205 3123 3376 104 -337 -595 O ATOM 1790 CB ASP A 545 66.864 11.295 69.412 1.00 35.27 C ANISOU 1790 CB ASP A 545 4160 4065 5175 -332 -358 -445 C ATOM 1791 CG ASP A 545 67.333 12.210 70.521 1.00 44.94 C ANISOU 1791 CG ASP A 545 5401 5341 6334 -409 -526 -796 C ATOM 1792 OD1 ASP A 545 67.659 11.697 71.612 1.00 46.57 O ANISOU 1792 OD1 ASP A 545 5511 5899 6284 -310 -679 -878 O ATOM 1793 OD2 ASP A 545 67.364 13.442 70.309 1.00 52.09 O ANISOU 1793 OD2 ASP A 545 6416 5935 7439 -550 -498 -998 O ATOM 1794 N ALA A 546 63.584 11.217 69.498 1.00 25.83 N ANISOU 1794 N ALA A 546 3259 2877 3677 79 -81 -260 N ATOM 1795 CA ALA A 546 62.353 11.917 69.858 1.00 26.83 C ANISOU 1795 CA ALA A 546 3528 3006 3662 260 4 -321 C ATOM 1796 C ALA A 546 61.618 11.166 70.963 1.00 26.13 C ANISOU 1796 C ALA A 546 3396 3244 3288 428 8 -243 C ATOM 1797 O ALA A 546 60.782 11.735 71.672 1.00 27.65 O ANISOU 1797 O ALA A 546 3682 3545 3279 619 47 -335 O ATOM 1798 CB ALA A 546 61.451 12.088 68.636 1.00 24.52 C ANISOU 1798 CB ALA A 546 3249 2609 3460 325 164 -164 C ATOM 1799 N HIS A 547 61.949 9.886 71.104 1.00 22.24 N ANISOU 1799 N HIS A 547 2765 2900 2784 383 -6 -48 N ATOM 1800 CA HIS A 547 61.339 9.034 72.113 1.00 26.71 C ANISOU 1800 CA HIS A 547 3270 3753 3124 533 49 130 C ATOM 1801 C HIS A 547 62.195 8.948 73.369 1.00 27.08 C ANISOU 1801 C HIS A 547 3297 4053 2937 636 -90 54 C ATOM 1802 O HIS A 547 61.711 8.536 74.420 1.00 28.38 O ANISOU 1802 O HIS A 547 3434 4524 2826 839 -40 186 O ATOM 1803 CB HIS A 547 61.091 7.637 71.540 1.00 24.30 C ANISOU 1803 CB HIS A 547 2844 3407 2983 442 161 421 C ATOM 1804 CG HIS A 547 59.929 7.580 70.598 1.00 21.28 C ANISOU 1804 CG HIS A 547 2417 2948 2720 387 288 476 C ATOM 1805 ND1 HIS A 547 58.686 7.121 70.980 1.00 24.28 N ANISOU 1805 ND1 HIS A 547 2706 3501 3017 445 429 641 N ATOM 1806 CD2 HIS A 547 59.810 7.957 69.303 1.00 20.14 C ANISOU 1806 CD2 HIS A 547 2270 2643 2740 300 295 391 C ATOM 1807 CE1 HIS A 547 57.854 7.205 69.956 1.00 24.79 C ANISOU 1807 CE1 HIS A 547 2693 3532 3195 375 489 614 C ATOM 1808 NE2 HIS A 547 58.510 7.712 68.927 1.00 22.25 N ANISOU 1808 NE2 HIS A 547 2433 3022 2998 314 407 466 N TER 3976 NH2 F 12 HETATM 3977 C1 EST A 601 61.406 -2.429 59.753 1.00 14.56 C HETATM 3978 C2 EST A 601 60.596 -2.223 58.672 1.00 13.87 C HETATM 3979 C3 EST A 601 59.230 -2.382 58.724 1.00 17.60 C HETATM 3980 O3 EST A 601 58.497 -2.144 57.640 1.00 21.53 O HETATM 3981 C4 EST A 601 58.638 -2.781 59.887 1.00 16.79 C HETATM 3982 C5 EST A 601 59.400 -2.996 61.016 1.00 15.80 C HETATM 3983 C6 EST A 601 58.761 -3.426 62.315 1.00 16.72 C HETATM 3984 C7 EST A 601 59.757 -3.957 63.313 1.00 16.54 C HETATM 3985 C8 EST A 601 61.001 -3.109 63.447 1.00 15.55 C HETATM 3986 C9 EST A 601 61.747 -3.070 62.132 1.00 14.53 C HETATM 3987 C10 EST A 601 60.872 -2.820 60.947 1.00 16.40 C HETATM 3988 C11 EST A 601 62.914 -2.105 62.269 1.00 12.31 C HETATM 3989 C12 EST A 601 63.882 -2.660 63.297 1.00 12.61 C HETATM 3990 C13 EST A 601 63.216 -2.824 64.665 1.00 13.27 C HETATM 3991 C14 EST A 601 61.988 -3.669 64.468 1.00 14.94 C HETATM 3992 C15 EST A 601 61.543 -3.989 65.881 1.00 16.58 C HETATM 3993 C16 EST A 601 62.795 -4.029 66.701 1.00 19.59 C HETATM 3994 C17 EST A 601 63.930 -3.563 65.802 1.00 16.78 C HETATM 3995 O17 EST A 601 64.900 -2.840 66.499 1.00 17.27 O HETATM 3996 C18 EST A 601 62.805 -1.487 65.169 1.00 14.15 C HETATM 4017 O HOH A 701 62.121 -3.303 76.438 1.00 38.46 O HETATM 4018 O HOH A 702 70.216 -1.046 47.245 1.00 41.70 O HETATM 4019 O HOH A 703 55.631 15.150 49.273 1.00 36.09 O HETATM 4020 O HOH A 704 49.139 22.879 63.676 1.00 24.32 O HETATM 4021 O HOH A 705 33.757 3.285 49.452 1.00 46.38 O HETATM 4022 O HOH A 706 30.056 8.130 63.187 1.00 25.07 O HETATM 4023 O HOH A 707 73.137 -7.436 71.312 1.00 35.90 O HETATM 4024 O HOH A 708 70.764 -15.893 54.200 1.00 33.64 O HETATM 4025 O HOH A 709 58.326 5.003 72.284 1.00 31.29 O HETATM 4026 O HOH A 710 64.381 14.329 62.312 1.00 21.48 O HETATM 4027 O HOH A 711 69.623 17.571 62.294 1.00 35.30 O HETATM 4028 O HOH A 712 29.886 7.869 50.251 1.00 42.18 O HETATM 4029 O HOH A 713 48.008 3.518 68.801 1.00 23.06 O HETATM 4030 O HOH A 714 46.069 5.599 55.649 1.00 22.97 O HETATM 4031 O HOH A 715 62.874 -7.570 73.655 1.00 33.30 O HETATM 4032 O HOH A 716 56.943 -18.087 63.186 1.00 28.70 O HETATM 4033 O HOH A 717 35.579 9.709 66.408 1.00 16.90 O HETATM 4034 O HOH A 718 36.348 -4.891 51.463 1.00 39.70 O HETATM 4035 O HOH A 719 24.341 -8.056 68.394 1.00 41.54 O HETATM 4036 O HOH A 720 69.157 8.696 68.852 1.00 35.20 O HETATM 4037 O HOH A 721 43.027 1.760 71.477 1.00 18.82 O HETATM 4038 O HOH A 722 48.131 -0.993 50.490 1.00 42.70 O HETATM 4039 O HOH A 723 58.672 2.458 76.539 1.00 35.63 O HETATM 4040 O HOH A 724 59.881 -21.457 67.208 1.00 33.24 O HETATM 4041 O HOH A 725 62.654 13.443 64.007 1.00 27.60 O HETATM 4042 O HOH A 726 58.610 27.743 65.960 1.00 34.28 O HETATM 4043 O HOH A 727 78.220 0.937 72.523 1.00 18.36 O HETATM 4044 O HOH A 728 58.383 -4.019 52.274 1.00 20.24 O HETATM 4045 O HOH A 729 40.740 -6.352 68.741 1.00 25.80 O HETATM 4046 O HOH A 730 47.241 16.575 54.126 1.00 24.85 O HETATM 4047 O HOH A 731 72.969 -6.393 52.089 1.00 37.17 O HETATM 4048 O HOH A 732 77.471 -10.432 59.337 1.00 35.97 O HETATM 4049 O HOH A 733 75.166 2.712 67.328 1.00 22.48 O HETATM 4050 O HOH A 734 46.689 5.304 52.964 1.00 19.17 O HETATM 4051 O HOH A 735 54.284 19.262 54.825 1.00 24.32 O HETATM 4052 O HOH A 736 23.841 -8.201 65.205 1.00 31.76 O HETATM 4053 O HOH A 737 76.034 -8.232 67.010 1.00 30.64 O HETATM 4054 O HOH A 738 25.280 2.874 60.446 1.00 30.47 O HETATM 4055 O HOH A 739 55.789 4.332 70.271 1.00 19.51 O HETATM 4056 O HOH A 740 31.915 13.977 60.765 1.00 33.46 O HETATM 4057 O HOH A 741 25.671 0.799 66.647 1.00 16.65 O HETATM 4058 O HOH A 742 39.801 18.079 55.846 1.00 52.91 O HETATM 4059 O HOH A 743 35.389 15.935 67.968 1.00 39.38 O HETATM 4060 O HOH A 744 34.115 15.618 61.593 1.00 29.99 O HETATM 4061 O HOH A 745 55.806 4.969 66.831 1.00 12.72 O HETATM 4062 O HOH A 746 64.539 -13.648 49.687 1.00 34.74 O HETATM 4063 O HOH A 747 48.832 4.338 45.987 1.00 39.98 O HETATM 4064 O HOH A 748 53.639 5.917 69.709 1.00 21.61 O HETATM 4065 O HOH A 749 58.944 17.251 68.183 1.00 36.97 O HETATM 4066 O HOH A 750 32.548 -1.838 52.400 1.00 32.18 O HETATM 4067 O HOH A 751 52.014 8.466 49.109 1.00 29.57 O HETATM 4068 O HOH A 752 41.792 -8.908 53.678 1.00 35.28 O HETATM 4069 O HOH A 753 52.757 -15.166 68.466 1.00 24.24 O HETATM 4070 O HOH A 754 65.544 -13.047 69.842 1.00 22.42 O HETATM 4071 O HOH A 755 57.466 -14.421 73.289 1.00 35.92 O HETATM 4072 O HOH A 756 38.663 7.997 64.616 1.00 21.82 O HETATM 4073 O HOH A 757 64.747 14.139 67.297 1.00 32.15 O HETATM 4074 O HOH A 758 59.589 -10.870 44.668 1.00 33.86 O HETATM 4075 O HOH A 759 24.392 -3.192 56.749 1.00 29.75 O HETATM 4076 O HOH A 760 68.998 -7.304 47.978 1.00 38.57 O HETATM 4077 O HOH A 761 76.587 4.342 69.475 1.00 24.71 O HETATM 4078 O HOH A 762 74.354 8.232 60.976 1.00 32.24 O HETATM 4079 O HOH A 763 54.062 -17.934 53.294 1.00 37.03 O HETATM 4080 O HOH A 764 28.985 6.510 59.032 1.00 31.49 O HETATM 4081 O HOH A 765 33.359 16.057 64.283 1.00 35.27 O HETATM 4082 O HOH A 766 59.363 2.921 74.204 1.00 30.39 O HETATM 4083 O HOH A 767 74.091 -11.476 56.342 1.00 33.54 O HETATM 4084 O HOH A 768 62.436 4.319 47.646 1.00 18.45 O HETATM 4085 O HOH A 769 68.914 -5.909 73.783 1.00 35.84 O HETATM 4086 O HOH A 770 51.635 0.455 55.111 1.00 20.08 O HETATM 4087 O HOH A 771 60.801 -14.370 49.919 1.00 42.80 O HETATM 4088 O HOH A 772 52.879 13.652 48.925 1.00 25.84 O HETATM 4089 O HOH A 773 75.391 -12.626 65.319 1.00 34.34 O HETATM 4090 O HOH A 774 67.600 -17.975 57.365 1.00 37.66 O HETATM 4091 O HOH A 775 49.895 12.155 72.487 1.00 26.68 O HETATM 4092 O HOH A 776 67.041 -3.702 53.632 1.00 19.24 O HETATM 4093 O HOH A 777 37.790 12.848 67.502 1.00 34.09 O HETATM 4094 O HOH A 778 26.028 -9.634 59.091 1.00 37.01 O HETATM 4095 O HOH A 779 60.157 14.437 71.333 1.00 33.94 O HETATM 4096 O HOH A 780 41.936 11.174 69.858 1.00 36.69 O HETATM 4097 O HOH A 781 34.446 -3.716 56.196 1.00 37.11 O HETATM 4098 O HOH A 782 71.383 1.262 55.582 1.00 42.12 O HETATM 4099 O HOH A 783 67.463 -10.466 47.848 1.00 35.14 O HETATM 4100 O HOH A 784 52.811 -19.137 55.776 1.00 35.98 O HETATM 4101 O HOH A 785 21.022 -3.379 61.637 1.00 24.61 O HETATM 4102 O HOH A 786 54.887 -0.620 52.190 1.00 24.10 O HETATM 4103 O HOH A 787 66.561 0.057 75.682 1.00 24.95 O HETATM 4104 O HOH A 788 55.785 -0.951 56.816 1.00 14.31 O HETATM 4105 O HOH A 789 74.931 6.354 70.218 1.00 29.77 O HETATM 4106 O HOH A 790 50.964 10.581 65.994 1.00 12.96 O HETATM 4107 O HOH A 791 51.731 -13.518 59.911 1.00 20.23 O HETATM 4108 O HOH A 792 47.021 5.793 67.896 1.00 20.05 O HETATM 4109 O HOH A 793 57.888 19.333 66.620 1.00 32.78 O HETATM 4110 O HOH A 794 51.852 4.673 55.036 1.00 18.49 O HETATM 4111 O HOH A 795 39.023 11.810 47.269 1.00 39.03 O HETATM 4112 O HOH A 796 30.838 -8.739 66.328 1.00 31.37 O HETATM 4113 O HOH A 797 66.025 -12.906 72.974 1.00 39.82 O HETATM 4114 O HOH A 798 61.936 -4.337 74.051 1.00 25.70 O HETATM 4115 O HOH A 799 54.751 -16.754 67.595 1.00 27.03 O HETATM 4116 O HOH A 800 72.843 -5.914 56.459 1.00 22.15 O HETATM 4117 O HOH A 801 52.198 22.222 55.194 1.00 34.53 O HETATM 4118 O HOH A 802 29.729 10.429 53.497 1.00 38.78 O HETATM 4119 O HOH A 803 63.152 5.617 49.997 1.00 20.63 O HETATM 4120 O HOH A 804 45.834 1.167 47.719 1.00 29.45 O HETATM 4121 O HOH A 805 49.770 17.392 50.137 1.00 40.81 O HETATM 4122 O HOH A 806 48.910 -18.053 63.457 1.00 41.96 O HETATM 4123 O HOH A 807 57.277 -1.592 52.380 1.00 20.54 O HETATM 4124 O HOH A 808 79.424 -12.748 49.257 1.00 41.01 O HETATM 4125 O HOH A 809 34.391 -10.332 56.954 1.00 46.34 O HETATM 4126 O HOH A 810 79.735 -3.134 71.291 1.00 25.29 O HETATM 4127 O HOH A 811 54.176 -1.507 45.643 1.00 36.85 O HETATM 4128 O HOH A 812 55.184 -7.490 75.943 1.00 38.24 O HETATM 4129 O HOH A 813 23.322 0.415 59.126 1.00 32.10 O HETATM 4130 O HOH A 814 56.246 -11.635 73.275 1.00 32.54 O HETATM 4131 O HOH A 815 75.307 5.623 62.733 1.00 34.94 O HETATM 4132 O HOH A 816 72.598 -12.022 54.516 1.00 37.94 O HETATM 4133 O HOH A 817 67.640 14.942 67.829 1.00 44.14 O HETATM 4134 O HOH A 818 77.991 -5.014 65.010 1.00 13.72 O HETATM 4135 O HOH A 819 33.816 -8.088 63.392 1.00 26.57 O HETATM 4136 O HOH A 820 69.604 3.297 59.035 1.00 28.79 O HETATM 4137 O HOH A 821 27.309 -10.904 65.365 1.00 38.33 O HETATM 4138 O HOH A 822 56.084 3.884 53.899 1.00 18.44 O HETATM 4139 O HOH A 823 57.624 13.815 69.353 1.00 36.76 O HETATM 4140 O HOH A 824 53.777 1.167 56.751 1.00 19.32 O HETATM 4141 O HOH A 825 63.011 -14.254 52.426 1.00 30.04 O HETATM 4142 O HOH A 826 56.317 -4.118 45.285 1.00 34.88 O HETATM 4143 O HOH A 827 69.347 10.238 57.314 1.00 24.50 O HETATM 4144 O HOH A 828 55.762 7.593 47.776 1.00 35.78 O HETATM 4145 O HOH A 829 40.941 -6.307 51.254 1.00 31.87 O HETATM 4146 O HOH A 830 54.347 7.419 49.513 1.00 33.03 O HETATM 4147 O HOH A 831 68.251 3.109 53.986 1.00 33.79 O HETATM 4148 O HOH A 832 47.281 -8.751 53.057 1.00 36.41 O HETATM 4149 O HOH A 833 36.367 -10.200 68.162 1.00 40.30 O HETATM 4150 O HOH A 834 72.310 9.344 57.418 1.00 31.86 O HETATM 4151 O HOH A 835 67.804 8.739 55.360 1.00 39.32 O HETATM 4152 O HOH A 836 65.474 -9.420 45.624 1.00 40.03 O HETATM 4153 O HOH A 837 19.858 -7.029 71.084 1.00 39.35 O HETATM 4154 O HOH A 838 61.748 -23.175 69.040 1.00 43.73 O HETATM 4155 O HOH A 839 72.395 7.763 74.346 1.00 44.47 O HETATM 4156 O HOH A 840 76.509 -9.749 64.863 1.00 21.20 O HETATM 4157 O HOH A 841 62.768 10.842 76.151 1.00 39.37 O HETATM 4158 O HOH A 842 31.202 -7.427 64.141 1.00 24.07 O HETATM 4159 O HOH A 843 77.465 -9.954 47.836 1.00 51.62 O HETATM 4160 O HOH A 844 71.460 -9.770 54.095 1.00 34.29 O HETATM 4161 O HOH A 845 57.038 -12.188 48.146 1.00 43.64 O HETATM 4162 O HOH A 846 26.218 -8.873 66.956 1.00 34.02 O HETATM 4163 O HOH A 847 63.507 1.494 47.550 1.00 11.63 O HETATM 4164 O HOH A 848 51.777 -11.519 49.526 1.00 45.96 O HETATM 4165 O HOH A 849 37.349 -11.022 52.433 1.00 44.25 O HETATM 4166 O HOH A 850 31.854 16.109 45.331 1.00 57.31 O HETATM 4167 O HOH A 851 62.923 -11.806 73.154 1.00 27.97 O HETATM 4168 O HOH A 852 54.091 20.628 68.563 1.00 41.45 O HETATM 4169 O HOH A 853 57.847 8.569 73.648 1.00 38.95 O HETATM 4170 O HOH A 854 52.448 10.273 46.992 1.00 47.18 O HETATM 4171 O HOH A 855 51.608 -9.042 50.864 1.00 39.42 O HETATM 4172 O HOH A 856 77.451 -13.253 58.738 1.00 38.06 O HETATM 4173 O HOH A 857 64.016 -15.936 54.546 1.00 39.56 O HETATM 4174 O HOH A 858 75.270 -4.120 59.855 1.00 40.23 O HETATM 4175 O HOH A 859 50.767 -15.076 61.950 1.00 28.96 O HETATM 4176 O HOH A 860 67.314 -6.576 46.394 1.00 43.09 O HETATM 4177 O HOH A 861 75.395 12.114 63.317 1.00 52.18 O HETATM 4178 O HOH A 862 42.880 23.206 66.604 1.00 48.61 O HETATM 4179 O HOH A 863 34.411 21.459 55.365 1.00 58.13 O HETATM 4180 O HOH A 864 52.486 -1.856 53.436 1.00 31.99 O HETATM 4181 O HOH A 865 57.912 11.565 70.133 1.00 34.72 O HETATM 4182 O HOH A 866 61.591 -12.261 46.272 1.00 37.75 O HETATM 4183 O HOH A 867 60.402 20.618 64.250 1.00 22.89 O HETATM 4184 O HOH A 868 60.991 -1.198 80.338 1.00 43.90 O HETATM 4185 O HOH A 869 44.024 20.824 65.867 1.00 42.55 O HETATM 4186 O HOH A 870 25.801 -11.744 59.941 1.00 41.42 O HETATM 4187 O HOH A 871 37.271 21.174 54.580 1.00 56.88 O HETATM 4188 O HOH A 872 45.639 19.059 71.770 1.00 46.31 O HETATM 4189 O HOH A 873 72.643 5.950 77.038 1.00 41.02 O HETATM 4190 O HOH A 874 43.740 25.464 55.723 1.00 56.55 O HETATM 4191 O HOH A 875 35.082 -10.671 62.701 1.00 38.67 O HETATM 4192 O HOH A 876 74.635 4.179 65.387 1.00 34.34 O HETATM 4193 O HOH A 877 72.400 9.976 68.860 1.00 46.79 O HETATM 4194 O HOH A 878 55.707 -8.515 44.616 1.00 50.65 O HETATM 4195 O HOH A 879 72.073 -3.594 55.031 1.00 35.48 O HETATM 4196 O HOH A 880 51.482 -16.918 64.069 1.00 39.61 O HETATM 4197 O HOH A 881 23.096 -9.827 63.654 1.00 39.06 O HETATM 4198 O HOH A 882 38.208 9.089 66.915 1.00 20.95 O HETATM 4199 O HOH A 883 32.912 15.889 68.988 1.00 44.00 O HETATM 4200 O HOH A 884 68.276 17.512 66.179 1.00 53.30 O HETATM 4201 O HOH A 885 23.704 -11.033 61.012 1.00 38.78 O HETATM 4202 O HOH A 886 66.661 -3.969 46.205 1.00 27.95 O HETATM 4203 O HOH A 887 37.868 -6.686 71.019 1.00 30.48 O HETATM 4204 O HOH A 888 66.391 7.392 76.853 1.00 48.13 O HETATM 4205 O HOH A 889 27.030 4.859 57.805 1.00 35.62 O HETATM 4206 O HOH A 890 61.313 27.232 66.822 1.00 33.59 O HETATM 4207 O HOH A 891 38.159 19.221 69.998 1.00 54.84 O HETATM 4208 O HOH A 892 70.266 3.200 56.168 1.00 40.21 O HETATM 4209 O HOH A 893 74.759 7.570 67.674 1.00 36.41 O HETATM 4210 O HOH A 894 35.210 -2.723 53.791 1.00 34.19 O HETATM 4211 O HOH A 895 21.870 -1.959 58.815 1.00 38.25 O HETATM 4212 O HOH A 896 50.857 -2.562 52.099 1.00 40.54 O HETATM 4213 O HOH A 897 21.589 -5.939 73.433 1.00 42.30 O HETATM 4214 O HOH A 898 56.119 -19.141 52.728 1.00 49.38 O HETATM 4215 O HOH A 899 34.033 -6.281 56.096 1.00 36.32 O HETATM 4216 O HOH A 900 79.353 -13.219 46.314 1.00 46.35 O HETATM 4217 O HOH A 901 71.433 -9.890 45.402 1.00 43.65 O HETATM 4218 O HOH A 902 70.795 -16.490 63.168 1.00 44.71 O HETATM 4219 O HOH A 903 53.345 12.332 46.766 1.00 35.92 O HETATM 4220 O HOH A 904 55.966 10.823 71.154 1.00 34.38 O HETATM 4221 O HOH A 905 51.285 15.876 48.431 1.00 35.72 O HETATM 4222 O HOH A 906 57.651 -21.841 65.579 1.00 40.71 O HETATM 4223 O HOH A 907 73.406 -7.869 54.496 1.00 32.40 O HETATM 4224 O HOH A 908 55.919 -21.121 66.733 1.00 43.18 O HETATM 4225 O HOH A 909 54.774 -18.261 65.156 1.00 35.12 O HETATM 4226 O HOH A 910 76.917 -14.637 64.028 1.00 39.38 O HETATM 4227 O HOH A 911 54.387 3.732 55.742 1.00 18.88 O HETATM 4228 O HOH A 912 61.640 10.339 78.811 1.00 47.99 O HETATM 4229 O HOH A 913 63.279 -11.204 45.064 1.00 39.50 O HETATM 4230 O HOH A 914 55.049 -10.940 48.310 1.00 33.55 O HETATM 4231 O HOH A 915 54.616 -7.378 46.349 1.00 42.94 O HETATM 4232 O HOH A 916 50.139 19.771 49.758 1.00 50.26 O HETATM 4233 O HOH A 917 53.912 -7.858 48.442 1.00 41.53 O CONECT 3977 3978 3987 CONECT 3987 3982 3986 3977 CONECT 3988 3986 3989 CONECT 3989 3990 3988 CONECT 3990 3996 3991 3994 3989 CONECT 3991 3990 3985 3992 CONECT 3992 3993 3991 CONECT 3993 3992 3994 CONECT 3994 3990 3993 3995 CONECT 3996 3990 CONECT 3978 3977 3979 CONECT 3979 3978 3980 3981 CONECT 3981 3982 3979 CONECT 3982 3987 3981 3983 CONECT 3983 3984 3982 CONECT 3984 3985 3983 CONECT 3985 3984 3991 3986 CONECT 3986 3985 3988 3987 CONECT 3995 3994 CONECT 3980 3979 END If you find results from this site helpful for your research, please cite one of our papers:
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