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*** sdrd ***elNémo ID: 2503201310413710232Job options:ID = 2503201310413710232 JOBID = sdrd 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 sdrd HEADER CELL ADHESION 25-FEB-13 4JDZ TITLE STRUCTURES OF SDRD FROM STAPHYLOCOCCUS AUREUS REVEAL THE MOLECULAR TITLE 2 MECHANISM OF HOW THE CELL SURFACE RECEPTORS RECOGNIZE THEIR LIGANDS COMPND MOL_ID: 1; COMPND 2 MOLECULE: SER-ASP RICH FIBRINOGEN/BONE SIALOPROTEIN-BINDING PROTEIN COMPND 3 SDRD; COMPND 4 CHAIN: B; COMPND 5 FRAGMENT: UNP RESIDUES 235-678; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: SER-ASP RICH FIBRINOGEN/BONE SIALOPROTEIN-BINDING PROTEIN COMPND 10 SDRD; COMPND 11 CHAIN: A; COMPND 12 FRAGMENT: UNP RESIDUES 235-673; COMPND 13 ENGINEERED: YES; COMPND 14 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS; SOURCE 3 ORGANISM_TAXID: 548473; SOURCE 4 STRAIN: TCH60; SOURCE 5 GENE: SDRD, HMPREF0772_12627; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS; SOURCE 10 ORGANISM_TAXID: 548473; SOURCE 11 STRAIN: TCH60; SOURCE 12 GENE: SDRD, HMPREF0772_12627; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS RECEPTOR, SURFACE, MSCRAMM, STAPHYLOCOCCUS AUREUS, CELL ADHESION EXPDTA X-RAY DIFFRACTION AUTHOR X.WANG,J.GE,M.YANG REVDAT 3 20-MAR-24 4JDZ 1 REMARK LINK REVDAT 2 04-DEC-19 4JDZ 1 REMARK SEQADV REVDAT 1 19-JUN-13 4JDZ 0 JRNL AUTH X.WANG,J.GE,B.LIU,Y.HU,M.YANG JRNL TITL STRUCTURES OF SDRD FROM STAPHYLOCOCCUS AUREUS REVEAL THE JRNL TITL 2 MOLECULAR MECHANISM OF HOW THE CELL SURFACE RECEPTORS JRNL TITL 3 RECOGNIZE THEIR LIGANDS JRNL REF PROTEIN CELL V. 4 277 2013 JRNL REFN ISSN 1674-800X JRNL PMID 23549613 JRNL DOI 10.1007/S13238-013-3009-X REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 55836 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 2753 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 29.4706 - 5.6760 0.00 0 0 0.0000 0.0000 REMARK 3 2 5.6760 - 4.5105 0.00 0 0 0.0000 0.0000 REMARK 3 3 4.5105 - 3.9418 0.00 0 0 0.0000 0.0000 REMARK 3 4 3.9418 - 3.5821 0.00 0 0 0.0000 0.0000 REMARK 3 5 3.5821 - 3.3257 0.00 0 0 0.0000 0.0000 REMARK 3 6 3.3257 - 3.1299 0.00 0 0 0.0000 0.0000 REMARK 3 7 3.1299 - 2.9733 0.00 0 0 0.0000 0.0000 REMARK 3 8 2.9733 - 2.8440 0.00 0 0 0.0000 0.0000 REMARK 3 9 2.8440 - 2.7346 0.00 0 0 0.0000 0.0000 REMARK 3 10 2.7346 - 2.6403 0.00 0 0 0.0000 0.0000 REMARK 3 11 2.6403 - 2.5577 0.00 0 0 0.0000 0.0000 REMARK 3 12 2.5577 - 2.4847 0.00 0 0 0.0000 0.0000 REMARK 3 13 2.4847 - 2.4193 0.00 0 0 0.0000 0.0000 REMARK 3 14 2.4193 - 2.3603 0.00 0 0 0.0000 0.0000 REMARK 3 15 2.3603 - 2.3067 0.00 0 0 0.0000 0.0000 REMARK 3 16 2.3067 - 2.2576 0.00 0 0 0.0000 0.0000 REMARK 3 17 2.2576 - 2.2124 0.00 0 0 0.0000 0.0000 REMARK 3 18 2.2124 - 2.1707 0.00 0 0 0.0000 0.0000 REMARK 3 19 2.1707 - 2.1320 0.00 0 0 0.0000 0.0000 REMARK 3 20 2.1320 - 2.1000 0.00 0 0 0.0000 0.0000 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 24 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 236:271) REMARK 3 ORIGIN FOR THE GROUP (A): 23.6487 0.6385 16.9717 REMARK 3 T TENSOR REMARK 3 T11: 0.6858 T22: 0.5672 REMARK 3 T33: 0.3027 T12: 0.2400 REMARK 3 T13: -0.0377 T23: 0.1008 REMARK 3 L TENSOR REMARK 3 L11: 1.2509 L22: 0.4477 REMARK 3 L33: 1.6433 L12: -0.5254 REMARK 3 L13: -0.3014 L23: 0.9027 REMARK 3 S TENSOR REMARK 3 S11: 0.5140 S12: 0.4622 S13: 0.1545 REMARK 3 S21: -0.5931 S22: -0.6189 S23: 0.2217 REMARK 3 S31: -0.8938 S32: -0.1148 S33: 0.1338 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 272:302) REMARK 3 ORIGIN FOR THE GROUP (A): 35.0275 6.3110 17.1894 REMARK 3 T TENSOR REMARK 3 T11: 1.0414 T22: 0.3934 REMARK 3 T33: 0.4008 T12: -0.1401 REMARK 3 T13: 0.0396 T23: 0.1811 REMARK 3 L TENSOR REMARK 3 L11: 0.9042 L22: 1.2903 REMARK 3 L33: 0.4291 L12: 0.0581 REMARK 3 L13: -0.5964 L23: -0.2402 REMARK 3 S TENSOR REMARK 3 S11: 0.1022 S12: 0.0221 S13: 0.3443 REMARK 3 S21: -0.7585 S22: -0.3391 S23: -0.5051 REMARK 3 S31: -1.0087 S32: 0.6937 S33: 0.0685 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 303:343) REMARK 3 ORIGIN FOR THE GROUP (A): 40.5904 5.5569 10.1787 REMARK 3 T TENSOR REMARK 3 T11: 1.1255 T22: 0.8018 REMARK 3 T33: 0.5537 T12: -0.2573 REMARK 3 T13: 0.1515 T23: 0.3030 REMARK 3 L TENSOR REMARK 3 L11: 0.6912 L22: 0.8196 REMARK 3 L33: 1.0434 L12: 0.1627 REMARK 3 L13: -0.9798 L23: 0.1630 REMARK 3 S TENSOR REMARK 3 S11: 0.4448 S12: 0.1784 S13: 0.0960 REMARK 3 S21: 0.1178 S22: -0.6827 S23: -0.9141 REMARK 3 S31: -1.6352 S32: 1.2020 S33: -0.0784 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 344:400) REMARK 3 ORIGIN FOR THE GROUP (A): 21.4019 -2.1218 28.4149 REMARK 3 T TENSOR REMARK 3 T11: 0.4076 T22: 0.3975 REMARK 3 T33: 0.2123 T12: 0.2103 REMARK 3 T13: -0.0425 T23: 0.0338 REMARK 3 L TENSOR REMARK 3 L11: 1.1569 L22: 1.3059 REMARK 3 L33: 1.8926 L12: -0.2144 REMARK 3 L13: -0.1297 L23: 1.2779 REMARK 3 S TENSOR REMARK 3 S11: 0.1563 S12: 0.5590 S13: 0.0137 REMARK 3 S21: -0.3553 S22: -0.3261 S23: 0.2005 REMARK 3 S31: -0.8085 S32: -0.4187 S33: 0.1494 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 401:434) REMARK 3 ORIGIN FOR THE GROUP (A): 31.3386 -16.2928 40.6312 REMARK 3 T TENSOR REMARK 3 T11: 0.1622 T22: 0.1584 REMARK 3 T33: 0.2425 T12: 0.0142 REMARK 3 T13: 0.0640 T23: 0.0245 REMARK 3 L TENSOR REMARK 3 L11: 0.4544 L22: 2.4792 REMARK 3 L33: 0.3891 L12: -0.0190 REMARK 3 L13: -0.0238 L23: 0.1558 REMARK 3 S TENSOR REMARK 3 S11: -0.0023 S12: 0.0071 S13: 0.0090 REMARK 3 S21: -0.0462 S22: -0.0636 S23: -0.1602 REMARK 3 S31: 0.0308 S32: 0.1018 S33: 0.0871 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN A AND RESID 435:498) REMARK 3 ORIGIN FOR THE GROUP (A): 31.7774 -16.0098 44.7886 REMARK 3 T TENSOR REMARK 3 T11: 0.1133 T22: 0.1341 REMARK 3 T33: 0.2055 T12: 0.0085 REMARK 3 T13: 0.0146 T23: -0.0121 REMARK 3 L TENSOR REMARK 3 L11: 0.3844 L22: 1.5337 REMARK 3 L33: 0.8815 L12: -0.1870 REMARK 3 L13: -0.2149 L23: -0.1598 REMARK 3 S TENSOR REMARK 3 S11: -0.0225 S12: -0.0277 S13: -0.0422 REMARK 3 S21: -0.0090 S22: 0.0026 S23: -0.1620 REMARK 3 S31: -0.0280 S32: 0.0645 S33: 0.0143 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN A AND RESID 499:517) REMARK 3 ORIGIN FOR THE GROUP (A): 30.6772 -15.1852 47.1250 REMARK 3 T TENSOR REMARK 3 T11: 0.1966 T22: 0.1598 REMARK 3 T33: 0.2431 T12: -0.0139 REMARK 3 T13: 0.0116 T23: -0.0300 REMARK 3 L TENSOR REMARK 3 L11: 0.1868 L22: 1.6102 REMARK 3 L33: 0.3629 L12: 0.0569 REMARK 3 L13: 0.1487 L23: -0.4978 REMARK 3 S TENSOR REMARK 3 S11: -0.1330 S12: 0.0433 S13: -0.1602 REMARK 3 S21: 0.3251 S22: 0.0988 S23: -0.2141 REMARK 3 S31: 0.1672 S32: 0.1491 S33: 0.0067 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN A AND RESID 518:523) REMARK 3 ORIGIN FOR THE GROUP (A): 39.1354 -27.2943 23.3484 REMARK 3 T TENSOR REMARK 3 T11: 0.5402 T22: 0.8463 REMARK 3 T33: 0.4849 T12: 0.0817 REMARK 3 T13: 0.3261 T23: -0.2829 REMARK 3 L TENSOR REMARK 3 L11: 0.0723 L22: 0.2938 REMARK 3 L33: 0.6015 L12: -0.0381 REMARK 3 L13: -0.1336 L23: 0.3183 REMARK 3 S TENSOR REMARK 3 S11: 0.1381 S12: 0.7219 S13: -0.1698 REMARK 3 S21: -0.1078 S22: -0.2647 S23: 0.0803 REMARK 3 S31: 0.2800 S32: -0.2015 S33: 0.0669 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN A AND RESID 524:550) REMARK 3 ORIGIN FOR THE GROUP (A): 24.5793 -21.9764 38.8107 REMARK 3 T TENSOR REMARK 3 T11: 0.1919 T22: 0.1763 REMARK 3 T33: 0.3386 T12: -0.0105 REMARK 3 T13: 0.0106 T23: -0.0042 REMARK 3 L TENSOR REMARK 3 L11: 0.2703 L22: 0.9086 REMARK 3 L33: 0.9862 L12: -0.2677 REMARK 3 L13: 0.4874 L23: 0.0634 REMARK 3 S TENSOR REMARK 3 S11: -0.0193 S12: 0.1522 S13: -0.1536 REMARK 3 S21: -0.0635 S22: -0.0030 S23: 0.3964 REMARK 3 S31: -0.0407 S32: -0.2982 S33: 0.0138 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN A AND RESID 558:587) REMARK 3 ORIGIN FOR THE GROUP (A): 49.9478 3.0273 -8.1561 REMARK 3 T TENSOR REMARK 3 T11: 0.7426 T22: 0.8239 REMARK 3 T33: 0.4716 T12: -0.2124 REMARK 3 T13: 0.0433 T23: 0.1420 REMARK 3 L TENSOR REMARK 3 L11: 0.5346 L22: 0.4267 REMARK 3 L33: 0.5991 L12: -0.1106 REMARK 3 L13: -0.1181 L23: 0.3687 REMARK 3 S TENSOR REMARK 3 S11: -0.1379 S12: 0.3920 S13: 0.4355 REMARK 3 S21: 0.3125 S22: 0.4563 S23: 0.3175 REMARK 3 S31: -0.9898 S32: 0.3198 S33: -0.1645 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN A AND RESID 588:593) REMARK 3 ORIGIN FOR THE GROUP (A): 52.7174 -13.9108 -7.8565 REMARK 3 T TENSOR REMARK 3 T11: 0.6680 T22: 1.3369 REMARK 3 T33: 1.4267 T12: 0.1793 REMARK 3 T13: -0.1137 T23: -0.4547 REMARK 3 L TENSOR REMARK 3 L11: 0.1568 L22: 0.9347 REMARK 3 L33: 0.8495 L12: -0.3748 REMARK 3 L13: 0.1542 L23: -0.2152 REMARK 3 S TENSOR REMARK 3 S11: 0.3576 S12: 0.5150 S13: 0.2749 REMARK 3 S21: 0.3154 S22: 0.1290 S23: 0.0501 REMARK 3 S31: 0.2560 S32: 0.2391 S33: -0.3042 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN A AND RESID 594:673) REMARK 3 ORIGIN FOR THE GROUP (A): 52.8779 -3.9031 -8.1868 REMARK 3 T TENSOR REMARK 3 T11: 0.6066 T22: 0.9881 REMARK 3 T33: 0.6146 T12: 0.0457 REMARK 3 T13: -0.0054 T23: 0.1316 REMARK 3 L TENSOR REMARK 3 L11: 1.5360 L22: 1.0078 REMARK 3 L33: 0.6698 L12: 0.8912 REMARK 3 L13: 0.5073 L23: 0.5937 REMARK 3 S TENSOR REMARK 3 S11: -0.4392 S12: 0.7132 S13: -0.3195 REMARK 3 S21: -0.1320 S22: 0.6285 S23: -0.0412 REMARK 3 S31: -0.1096 S32: 0.3538 S33: -0.1377 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN B AND RESID 235:382) REMARK 3 ORIGIN FOR THE GROUP (A): -3.8097 0.7409 17.2345 REMARK 3 T TENSOR REMARK 3 T11: 0.2333 T22: 0.1953 REMARK 3 T33: 0.1481 T12: -0.0204 REMARK 3 T13: -0.0082 T23: 0.0463 REMARK 3 L TENSOR REMARK 3 L11: 2.3474 L22: 0.7362 REMARK 3 L33: 2.0335 L12: 0.2094 REMARK 3 L13: -1.4205 L23: 0.0058 REMARK 3 S TENSOR REMARK 3 S11: 0.0141 S12: 0.1999 S13: 0.1606 REMARK 3 S21: -0.1915 S22: 0.0156 S23: 0.0473 REMARK 3 S31: -0.1693 S32: -0.0412 S33: -0.0129 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN B AND RESID 383:393) REMARK 3 ORIGIN FOR THE GROUP (A): -22.3149 -18.0159 42.3310 REMARK 3 T TENSOR REMARK 3 T11: 0.0294 T22: 0.1586 REMARK 3 T33: 0.2135 T12: -0.0101 REMARK 3 T13: -0.0176 T23: 0.0278 REMARK 3 L TENSOR REMARK 3 L11: 0.2524 L22: 1.9562 REMARK 3 L33: 1.9696 L12: 0.3389 REMARK 3 L13: -0.6021 L23: -1.1079 REMARK 3 S TENSOR REMARK 3 S11: -0.0024 S12: 0.3384 S13: -0.1186 REMARK 3 S21: 0.1749 S22: 0.2333 S23: 0.5525 REMARK 3 S31: -0.2585 S32: -0.4264 S33: -0.2199 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN B AND RESID 394:436) REMARK 3 ORIGIN FOR THE GROUP (A): -6.4117 -20.1639 40.5344 REMARK 3 T TENSOR REMARK 3 T11: 0.0919 T22: 0.1347 REMARK 3 T33: 0.1940 T12: 0.0121 REMARK 3 T13: -0.0101 T23: -0.0264 REMARK 3 L TENSOR REMARK 3 L11: 0.8026 L22: 1.5313 REMARK 3 L33: 0.7176 L12: -0.2712 REMARK 3 L13: 0.2076 L23: -0.1750 REMARK 3 S TENSOR REMARK 3 S11: 0.1237 S12: 0.1478 S13: -0.0354 REMARK 3 S21: -0.0343 S22: -0.0244 S23: -0.0531 REMARK 3 S31: 0.0228 S32: 0.0997 S33: -0.0843 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN B AND RESID 437:516) REMARK 3 ORIGIN FOR THE GROUP (A): -5.3846 -19.1088 45.6463 REMARK 3 T TENSOR REMARK 3 T11: 0.0933 T22: 0.1407 REMARK 3 T33: 0.1568 T12: -0.0012 REMARK 3 T13: -0.0213 T23: -0.0036 REMARK 3 L TENSOR REMARK 3 L11: 0.5370 L22: 2.0143 REMARK 3 L33: 1.2105 L12: -0.1963 REMARK 3 L13: -0.0243 L23: -0.4534 REMARK 3 S TENSOR REMARK 3 S11: -0.0497 S12: -0.0644 S13: 0.0254 REMARK 3 S21: 0.1149 S22: 0.0604 S23: -0.1422 REMARK 3 S31: -0.0208 S32: 0.1343 S33: 0.0003 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN B AND RESID 517:523) REMARK 3 ORIGIN FOR THE GROUP (A): 2.3099 -31.4894 25.3286 REMARK 3 T TENSOR REMARK 3 T11: 0.5682 T22: 0.6849 REMARK 3 T33: 0.4555 T12: 0.3462 REMARK 3 T13: 0.0675 T23: -0.2897 REMARK 3 L TENSOR REMARK 3 L11: 0.2540 L22: 1.0540 REMARK 3 L33: 0.0693 L12: 0.0891 REMARK 3 L13: 0.0538 L23: 0.1322 REMARK 3 S TENSOR REMARK 3 S11: -0.1475 S12: 0.7405 S13: -0.2712 REMARK 3 S21: 0.7115 S22: -0.3476 S23: 0.2286 REMARK 3 S31: 0.1723 S32: 0.1085 S33: 0.2147 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN B AND RESID 524:544) REMARK 3 ORIGIN FOR THE GROUP (A): -14.4342 -25.8948 42.8034 REMARK 3 T TENSOR REMARK 3 T11: 0.1202 T22: 0.1231 REMARK 3 T33: 0.2456 T12: 0.0135 REMARK 3 T13: -0.0032 T23: 0.0201 REMARK 3 L TENSOR REMARK 3 L11: 0.6733 L22: 0.2617 REMARK 3 L33: 0.3320 L12: 0.0795 REMARK 3 L13: -0.3133 L23: 0.0901 REMARK 3 S TENSOR REMARK 3 S11: -0.0484 S12: 0.0894 S13: -0.1798 REMARK 3 S21: -0.0476 S22: 0.1018 S23: 0.2631 REMARK 3 S31: 0.1726 S32: -0.1695 S33: -0.0040 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN B AND RESID 545:550) REMARK 3 ORIGIN FOR THE GROUP (A): -4.0365 -24.1324 24.0907 REMARK 3 T TENSOR REMARK 3 T11: 0.4767 T22: 0.4265 REMARK 3 T33: 0.2693 T12: 0.1326 REMARK 3 T13: -0.0019 T23: -0.0595 REMARK 3 L TENSOR REMARK 3 L11: 2.0917 L22: 1.8820 REMARK 3 L33: 0.9519 L12: -0.3193 REMARK 3 L13: -0.5947 L23: 1.1180 REMARK 3 S TENSOR REMARK 3 S11: 0.2697 S12: 0.7921 S13: -0.2244 REMARK 3 S21: -0.6583 S22: 0.1543 S23: 0.0775 REMARK 3 S31: 0.3516 S32: 0.4107 S33: -0.2176 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN B AND RESID 551:560) REMARK 3 ORIGIN FOR THE GROUP (A): 7.0674 -23.8930 10.7586 REMARK 3 T TENSOR REMARK 3 T11: 0.9493 T22: 0.9993 REMARK 3 T33: 0.9472 T12: -0.4385 REMARK 3 T13: 0.0626 T23: 0.1957 REMARK 3 L TENSOR REMARK 3 L11: 6.5862 L22: 3.6031 REMARK 3 L33: 4.1085 L12: -1.3814 REMARK 3 L13: 5.0791 L23: -0.4130 REMARK 3 S TENSOR REMARK 3 S11: 0.2312 S12: -0.3006 S13: -0.0044 REMARK 3 S21: 0.5143 S22: -0.0624 S23: 0.0691 REMARK 3 S31: -0.0582 S32: 0.5917 S33: 0.1992 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: (CHAIN B AND RESID 561:627) REMARK 3 ORIGIN FOR THE GROUP (A): 13.8811 -6.8342 -8.9013 REMARK 3 T TENSOR REMARK 3 T11: 0.3615 T22: 0.4085 REMARK 3 T33: 0.1525 T12: -0.1624 REMARK 3 T13: -0.0434 T23: 0.0646 REMARK 3 L TENSOR REMARK 3 L11: 1.5467 L22: 0.6884 REMARK 3 L33: 1.3542 L12: 0.0449 REMARK 3 L13: -0.6951 L23: -0.7583 REMARK 3 S TENSOR REMARK 3 S11: -0.0428 S12: 0.0949 S13: -0.0444 REMARK 3 S21: -0.1867 S22: 0.2251 S23: 0.1285 REMARK 3 S31: -0.0023 S32: -0.2647 S33: -0.1502 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: (CHAIN B AND RESID 628:645) REMARK 3 ORIGIN FOR THE GROUP (A): 21.6220 0.2097 -12.7608 REMARK 3 T TENSOR REMARK 3 T11: 0.3815 T22: 0.6546 REMARK 3 T33: 0.2912 T12: -0.0514 REMARK 3 T13: 0.0327 T23: 0.0800 REMARK 3 L TENSOR REMARK 3 L11: 0.3668 L22: 0.8368 REMARK 3 L33: 0.5742 L12: -0.0136 REMARK 3 L13: -0.2572 L23: -0.2312 REMARK 3 S TENSOR REMARK 3 S11: -0.1345 S12: -0.1952 S13: 0.3382 REMARK 3 S21: -0.2655 S22: -0.1949 S23: -0.3186 REMARK 3 S31: -0.2696 S32: 0.2059 S33: 0.0896 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: (CHAIN B AND RESID 646:672) REMARK 3 ORIGIN FOR THE GROUP (A): 19.3236 -5.6087 -7.3481 REMARK 3 T TENSOR REMARK 3 T11: 0.3553 T22: 0.5748 REMARK 3 T33: 0.2235 T12: -0.0325 REMARK 3 T13: -0.0688 T23: 0.0584 REMARK 3 L TENSOR REMARK 3 L11: 0.6497 L22: 0.2179 REMARK 3 L33: 0.3699 L12: -0.0079 REMARK 3 L13: -0.2694 L23: 0.2823 REMARK 3 S TENSOR REMARK 3 S11: 0.0773 S12: 0.1586 S13: -0.1118 REMARK 3 S21: -0.0389 S22: 0.1414 S23: 0.1263 REMARK 3 S31: 0.2838 S32: 0.5869 S33: -0.1157 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: (CHAIN B AND RESID 673:679) REMARK 3 ORIGIN FOR THE GROUP (A): 19.2818 11.1372 -32.8165 REMARK 3 T TENSOR REMARK 3 T11: 0.5492 T22: 0.9637 REMARK 3 T33: 0.1280 T12: -0.0507 REMARK 3 T13: 0.1275 T23: 0.0861 REMARK 3 L TENSOR REMARK 3 L11: 0.0828 L22: 1.2453 REMARK 3 L33: 0.0409 L12: -0.1498 REMARK 3 L13: -0.0485 L23: 0.2179 REMARK 3 S TENSOR REMARK 3 S11: 0.7144 S12: 0.1719 S13: 0.1846 REMARK 3 S21: -0.7476 S22: -0.5534 S23: -0.3180 REMARK 3 S31: 0.2910 S32: -0.0891 S33: -0.1321 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 4JDZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-13. REMARK 100 THE DEPOSITION ID IS D_1000077925. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-JUN-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR225 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55836 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 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 (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.06200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 33.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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: LAUE REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: DM REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM CHLORIDE DIHYDRATE, 0.1M REMARK 280 HEPES SODIUM(7.5), 20%(V/V) 2-PROPANOL, PH 8.0, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 291K 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 36.94000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 ASN A 550A REMARK 465 GLN A 550B REMARK 465 SER A 550C REMARK 465 GLY A 550D REMARK 465 GLY A 550E REMARK 465 ALA A 550F REMARK 465 ALA A 550G REMARK 465 GLN A 550H 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 ASP B 391 -132.02 57.10 REMARK 500 ASP B 391 -132.02 50.45 REMARK 500 HIS B 405 64.40 -114.09 REMARK 500 ASN B 505 -2.99 -144.08 REMARK 500 ALA B 522 -23.86 84.09 REMARK 500 ASN B 550 91.68 -52.93 REMARK 500 ALA B 556 86.80 44.62 REMARK 500 ALA B 557 79.01 15.01 REMARK 500 GLN B 558 -158.79 46.00 REMARK 500 ASN B 565 -33.05 115.50 REMARK 500 ALA B 595 -72.21 -70.98 REMARK 500 ALA B 596 -91.95 -29.98 REMARK 500 ALA B 597 -100.21 -142.53 REMARK 500 ALA B 598 -126.39 -141.67 REMARK 500 LYS B 638 51.68 39.00 REMARK 500 ASN B 658 87.57 -152.81 REMARK 500 VAL A 238 35.21 -90.21 REMARK 500 LYS A 255 60.45 36.04 REMARK 500 ASN A 257 33.25 38.16 REMARK 500 ASP A 335 3.80 -67.86 REMARK 500 ASP A 391 -134.49 51.40 REMARK 500 HIS A 405 71.26 -109.76 REMARK 500 ASN A 564 15.74 -163.24 REMARK 500 THR A 570 40.92 -76.23 REMARK 500 ASN A 571 -17.52 -147.24 REMARK 500 LEU A 578 -88.71 -12.85 REMARK 500 ALA A 595 -52.81 -162.34 REMARK 500 THR A 602 -171.18 -170.28 REMARK 500 ASP A 605 -168.39 -75.95 REMARK 500 ASN A 614 47.77 71.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY B 564 ASN B 565 146.98 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 704 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 252 OD2 REMARK 620 2 ASN B 256 OD1 83.8 REMARK 620 3 LYS B 258 O 90.9 82.2 REMARK 620 4 ASP B 264 OD2 106.3 155.8 75.8 REMARK 620 5 ASP B 264 OD1 78.1 154.3 115.9 49.3 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 701 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN B 565 OD1 REMARK 620 2 LEU B 663 O 90.2 REMARK 620 3 ASP B 666 OD1 78.3 84.8 REMARK 620 4 ASP B 666 OD2 125.4 99.5 49.8 REMARK 620 5 HOH B 808 O 87.6 177.8 95.1 82.1 REMARK 620 6 HOH B 839 O 160.6 84.5 119.6 74.0 97.5 REMARK 620 7 HOH B 885 O 84.8 94.2 163.1 146.3 85.3 77.0 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 703 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 570 OD1 REMARK 620 2 ASN B 574 OD1 86.9 REMARK 620 3 VAL B 576 O 98.9 78.6 REMARK 620 4 ASP B 578 OD2 170.8 90.8 89.4 REMARK 620 5 GLU B 581 OE2 92.6 153.5 127.5 85.4 REMARK 620 6 GLU B 581 OE1 93.9 157.4 79.0 91.6 49.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 702 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 644 O REMARK 620 2 ASP B 647 OD1 87.5 REMARK 620 3 ASN B 649 OD1 172.6 99.7 REMARK 620 4 SER B 664 O 96.1 139.2 79.9 REMARK 620 5 HOH B 801 O 78.6 70.6 105.6 70.4 REMARK 620 6 HOH B 986 O 85.4 142.5 87.6 78.2 142.8 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 701 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 252 OD2 REMARK 620 2 ASN A 256 OD1 80.0 REMARK 620 3 LYS A 258 O 85.7 82.9 REMARK 620 4 ASP A 264 OD1 72.9 151.5 103.4 REMARK 620 5 ASP A 264 OD2 102.6 150.0 67.7 49.0 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 702 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 564 OD1 REMARK 620 2 LEU A 662 O 88.2 REMARK 620 3 ASP A 665 OD2 127.1 98.8 REMARK 620 4 ASP A 665 OD1 78.7 87.1 49.7 REMARK 620 5 HOH A 938 O 85.1 92.5 145.9 163.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 704 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 569 OD1 REMARK 620 2 ASN A 571 OD1 125.9 REMARK 620 3 ASN A 573 OD1 78.3 109.3 REMARK 620 4 VAL A 575 O 78.1 154.6 81.7 REMARK 620 5 ASP A 577 OD2 167.2 66.5 95.3 90.1 REMARK 620 6 GLU A 580 OE2 86.5 59.2 148.9 121.7 104.1 REMARK 620 7 GLU A 580 OE1 77.6 99.8 149.5 75.4 104.4 46.3 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 703 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 643 O REMARK 620 2 ASP A 646 OD1 94.0 REMARK 620 3 ASN A 648 OD1 175.4 90.7 REMARK 620 4 SER A 663 O 106.9 136.6 69.4 REMARK 620 5 HOH A 936 O 95.5 68.8 86.3 142.4 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 701 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 702 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 703 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 704 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 701 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 703 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 704 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4JE0 RELATED DB: PDB REMARK 999 REMARK 999 SEQUENCE REMARK 999 SEQRES CONFLICTS HAVE CAUSED BY REFINEMENT ARTIFACTS. DBREF 4JDZ B 235 679 UNP E5QTK7 E5QTK7_STAAH 235 678 DBREF 4JDZ A 236 673 UNP E5QTK7 E5QTK7_STAAH 236 673 SEQADV 4JDZ ILE B 254 UNP E5QTK7 ASP 254 ENGINEERED MUTATION SEQADV 4JDZ ALA B 522 UNP E5QTK7 GLU 522 SEE REMARK 999 SEQADV 4JDZ ALA B 557 UNP E5QTK7 GLY 557 SEE REMARK 999 SEQADV 4JDZ ALA B 595 UNP E5QTK7 LYS 595 SEE REMARK 999 SEQADV 4JDZ ALA B 596 UNP E5QTK7 THR 596 SEE REMARK 999 SEQADV 4JDZ ALA B 597 UNP E5QTK7 ASN 597 SEE REMARK 999 SEQADV 4JDZ ALA B 598 UNP E5QTK7 LYS 598 SEE REMARK 999 SEQADV 4JDZ ALA B 680 UNP E5QTK7 EXPRESSION TAG SEQADV 4JDZ ALA A 236 UNP E5QTK7 LYS 236 SEE REMARK 999 SEQADV 4JDZ ILE A 254 UNP E5QTK7 ASP 254 ENGINEERED MUTATION SEQADV 4JDZ ALA A 522 UNP E5QTK7 GLU 522 SEE REMARK 999 SEQADV 4JDZ ALA A 550G UNP E5QTK7 GLY 557 SEE REMARK 999 SEQADV 4JDZ ALA A 592 UNP E5QTK7 ASP 593 SEE REMARK 999 SEQADV 4JDZ ALA A 593 UNP E5QTK7 ASN 594 SEE REMARK 999 SEQADV 4JDZ ALA A 594 UNP E5QTK7 LYS 595 SEE REMARK 999 SEQADV 4JDZ ALA A 595 UNP E5QTK7 THR 596 SEE REMARK 999 SEQADV 4JDZ ALA A 596 UNP E5QTK7 ASN 597 SEE REMARK 999 SEQADV 4JDZ ALA A 640 UNP E5QTK7 ASN 641 SEE REMARK 999 SEQADV 4JDZ ALA A 672 UNP E5QTK7 LYS 672 SEE REMARK 999 SEQRES 1 B 445 SER LYS ASN VAL ASN ASP LEU ILE THR SER ASN THR THR SEQRES 2 B 445 LEU THR VAL VAL ASP ALA ILE LYS ASN ASN LYS ILE VAL SEQRES 3 B 445 PRO ALA GLN ASP TYR LEU ALA LEU LYS SER GLN ILE LYS SEQRES 4 B 445 VAL ASP ASP LYS VAL LYS SER GLY ASP TYR PHE THR ILE SEQRES 5 B 445 LYS TYR SER ASP THR VAL GLN VAL TYR GLY LEU ASN PRO SEQRES 6 B 445 GLU ASP ILE LYS ASN ILE GLY ASP ILE LYS ASP PRO ASN SEQRES 7 B 445 ASN GLY GLU THR ILE ALA THR ALA LYS HIS ASP THR ALA SEQRES 8 B 445 ASN ASN LEU ILE THR TYR THR PHE THR ASP TYR VAL ASP SEQRES 9 B 445 ARG PHE ASN SER VAL GLN MET GLY ILE ASN TYR SER ILE SEQRES 10 B 445 TYR MET ASP ALA ASP THR ILE PRO VAL SER LYS ASN ASP SEQRES 11 B 445 VAL GLU PHE ASN VAL THR ILE GLY ASN ASP THR THR LYS SEQRES 12 B 445 THR THR ALA ASN ILE GLN TYR PRO ASP TYR VAL SER ARG SEQRES 13 B 445 ASP ASN ASN SER ILE GLY SER ALA PHE THR GLU THR VAL SEQRES 14 B 445 SER HIS ALA GLY ASN ALA GLU ASP PRO GLY TYR TYR LYS SEQRES 15 B 445 GLN THR VAL TYR VAL ASN PRO SER GLU LYS SER LEU THR SEQRES 16 B 445 ASN ALA LYS LEU LYS VAL GLU ALA TYR HIS LYS ASP TYR SEQRES 17 B 445 PRO ASP ASN VAL GLY GLN ILE ASN LYS ASP VAL THR LYS SEQRES 18 B 445 ILE LYS ILE TYR GLN ALA PRO LYS ASP TYR VAL LEU ASN SEQRES 19 B 445 LYS GLY TYR ASP VAL ASN THR ASN GLN LEU ILE ASP VAL SEQRES 20 B 445 THR GLU GLN PHE LYS ASP LYS ILE THR TYR GLY ALA ASN SEQRES 21 B 445 ASP SER VAL ASN VAL ASP PHE GLY SER ILE ASN ASN SER SEQRES 22 B 445 TYR VAL VAL MET VAL ASP THR LYS PHE GLU TYR THR THR SEQRES 23 B 445 SER ALA SER PRO THR LEU VAL GLN MET ALA THR LEU THR SEQRES 24 B 445 SER ASP GLY ASN ARG SER VAL SER THR GLY ASN ALA LEU SEQRES 25 B 445 GLY PHE THR ASN ASN GLN SER GLY GLY ALA ALA GLN GLU SEQRES 26 B 445 VAL TYR LYS ILE GLY ASN TYR VAL TRP GLU ASP THR ASN SEQRES 27 B 445 LYS ASN GLY VAL GLN ASP LEU GLY GLU VAL GLY VAL LYS SEQRES 28 B 445 GLY VAL THR VAL VAL ALA TYR ASP ASN ALA ALA ALA ALA SEQRES 29 B 445 GLU VAL GLY ARG THR ILE THR ASP ASP LYS GLY GLY TYR SEQRES 30 B 445 LEU ILE PRO ASN LEU PRO ASN GLY ASP TYR ARG VAL GLU SEQRES 31 B 445 PHE SER ASN LEU PRO GLN GLY TYR GLU VAL THR PRO SER SEQRES 32 B 445 LYS GLN GLY ASN ASN GLU GLU LEU ASP SER ASN GLY VAL SEQRES 33 B 445 SER SER VAL ILE THR VAL ASN GLY LYS ASP ASN LEU SER SEQRES 34 B 445 ALA ASP LEU GLY ILE TYR LYS PRO LYS TYR ASN LEU GLY SEQRES 35 B 445 ASP TYR ALA SEQRES 1 A 438 ALA ASN VAL ASN ASP LEU ILE THR SER ASN THR THR LEU SEQRES 2 A 438 THR VAL VAL ASP ALA ILE LYS ASN ASN LYS ILE VAL PRO SEQRES 3 A 438 ALA GLN ASP TYR LEU ALA LEU LYS SER GLN ILE LYS VAL SEQRES 4 A 438 ASP ASP LYS VAL LYS SER GLY ASP TYR PHE THR ILE LYS SEQRES 5 A 438 TYR SER ASP THR VAL GLN VAL TYR GLY LEU ASN PRO GLU SEQRES 6 A 438 ASP ILE LYS ASN ILE GLY ASP ILE LYS ASP PRO ASN ASN SEQRES 7 A 438 GLY GLU THR ILE ALA THR ALA LYS HIS ASP THR ALA ASN SEQRES 8 A 438 ASN LEU ILE THR TYR THR PHE THR ASP TYR VAL ASP ARG SEQRES 9 A 438 PHE ASN SER VAL GLN MET GLY ILE ASN TYR SER ILE TYR SEQRES 10 A 438 MET ASP ALA ASP THR ILE PRO VAL SER LYS ASN ASP VAL SEQRES 11 A 438 GLU PHE ASN VAL THR ILE GLY ASN ASP THR THR LYS THR SEQRES 12 A 438 THR ALA ASN ILE GLN TYR PRO ASP TYR VAL SER ARG ASP SEQRES 13 A 438 ASN ASN SER ILE GLY SER ALA PHE THR GLU THR VAL SER SEQRES 14 A 438 HIS ALA GLY ASN ALA GLU ASP PRO GLY TYR TYR LYS GLN SEQRES 15 A 438 THR VAL TYR VAL ASN PRO SER GLU LYS SER LEU THR ASN SEQRES 16 A 438 ALA LYS LEU LYS VAL GLU ALA TYR HIS LYS ASP TYR PRO SEQRES 17 A 438 ASP ASN VAL GLY GLN ILE ASN LYS ASP VAL THR LYS ILE SEQRES 18 A 438 LYS ILE TYR GLN ALA PRO LYS ASP TYR VAL LEU ASN LYS SEQRES 19 A 438 GLY TYR ASP VAL ASN THR ASN GLN LEU ILE ASP VAL THR SEQRES 20 A 438 GLU GLN PHE LYS ASP LYS ILE THR TYR GLY ALA ASN ASP SEQRES 21 A 438 SER VAL ASN VAL ASP PHE GLY SER ILE ASN ASN SER TYR SEQRES 22 A 438 VAL VAL MET VAL ASP THR LYS PHE GLU TYR THR THR SER SEQRES 23 A 438 ALA SER PRO THR LEU VAL GLN MET ALA THR LEU THR SER SEQRES 24 A 438 ASP GLY ASN ARG SER VAL SER THR GLY ASN ALA LEU GLY SEQRES 25 A 438 PHE THR ASN ASN GLN SER GLY GLY ALA ALA GLN GLU VAL SEQRES 26 A 438 TYR LYS ILE GLY ASN TYR VAL TRP GLU ASP THR ASN LYS SEQRES 27 A 438 ASN GLY VAL GLN ASP LEU GLY GLU VAL GLY VAL LYS GLY SEQRES 28 A 438 VAL THR VAL VAL ALA TYR ALA ALA ALA ALA ALA LYS GLU SEQRES 29 A 438 VAL GLY ARG THR ILE THR ASP ASP LYS GLY GLY TYR LEU SEQRES 30 A 438 ILE PRO ASN LEU PRO ASN GLY ASP TYR ARG VAL GLU PHE SEQRES 31 A 438 SER ASN LEU PRO GLN GLY TYR GLU VAL THR PRO SER LYS SEQRES 32 A 438 GLN GLY ALA ASN GLU GLU LEU ASP SER ASN GLY VAL SER SEQRES 33 A 438 SER VAL ILE THR VAL ASN GLY LYS ASP ASN LEU SER ALA SEQRES 34 A 438 ASP LEU GLY ILE TYR LYS PRO ALA TYR HET CA B 701 1 HET CA B 702 1 HET CA B 703 1 HET CA B 704 1 HET CA A 701 1 HET CA A 702 1 HET CA A 703 1 HET CA A 704 1 HETNAM CA CALCIUM ION FORMUL 3 CA 8(CA 2+) FORMUL 11 HOH *496(H2 O) HELIX 1 1 VAL B 238 ASP B 240 1 3 HELIX 2 2 ASN B 298 ILE B 305 1 8 HELIX 3 3 THR B 324 ASN B 326 1 3 HELIX 4 4 ASP B 335 PHE B 340 1 6 HELIX 5 5 ALA B 355 ILE B 358 1 4 HELIX 6 6 ASN B 474 LEU B 478 1 5 HELIX 7 7 THR B 482 LYS B 486 1 5 SHEET 1 1 1 ILE B 242 VAL B 251 0 SHEET 2 2 1 TYR B 265 VAL B 274 0 SHEET 3 3 1 TYR B 283 TYR B 288 0 SHEET 4 4 1 VAL B 292 GLN B 293 0 SHEET 5 5 1 ILE B 308 LYS B 309 0 SHEET 6 6 1 THR B 316 ASP B 323 0 SHEET 7 7 1 LEU B 328 PHE B 333 0 SHEET 8 8 1 GLN B 344 MET B 353 0 SHEET 9 9 1 LYS B 362 ILE B 371 0 SHEET 10 10 1 ASP B 374 ILE B 382 0 SHEET 11 11 1 VAL B 388 ARG B 390 0 SHEET 12 12 1 ASN B 393 SER B 404 0 SHEET 13 13 1 GLY B 413 VAL B 421 0 SHEET 14 14 1 LEU B 428 GLU B 436 0 SHEET 15 15 1 LYS B 455 GLN B 460 0 SHEET 16 16 1 ILE B 479 ASP B 480 0 SHEET 17 17 1 ILE B 489 GLY B 492 0 SHEET 18 18 1 SER B 496 ILE B 504 0 SHEET 19 19 1 TYR B 508 LYS B 515 0 SHEET 20 20 1 THR B 525 SER B 534 0 SHEET 21 21 1 ASN B 537 GLY B 547 0 SHEET 22 22 1 TYR B 561 GLU B 569 0 SHEET 23 23 1 THR B 588 ASP B 593 0 SHEET 24 24 1 GLU B 599 ILE B 604 0 SHEET 25 25 1 GLY B 610 LEU B 616 0 SHEET 26 26 1 GLY B 619 SER B 626 0 SHEET 27 27 1 GLU B 633 VAL B 634 0 SHEET 28 28 1 SER B 652 VAL B 657 0 SHEET 29 29 1 ASN B 662 TYR B 670 0 LINK OD2 ASP B 252 CA CA B 704 1555 1555 2.39 LINK OD1 ASN B 256 CA CA B 704 1555 1555 2.45 LINK O LYS B 258 CA CA B 704 1555 1555 2.27 LINK OD2 ASP B 264 CA CA B 704 1555 1555 2.62 LINK OD1 ASP B 264 CA CA B 704 1555 1555 2.64 LINK OD1 ASN B 565 CA CA B 701 1555 1555 2.25 LINK OD1 ASP B 570 CA CA B 703 1555 1555 2.29 LINK OD1 ASN B 574 CA CA B 703 1555 1555 2.47 LINK O VAL B 576 CA CA B 703 1555 1555 2.37 LINK OD2 ASP B 578 CA CA B 703 1555 1555 2.39 LINK OE2 GLU B 581 CA CA B 703 1555 1555 2.49 LINK OE1 GLU B 581 CA CA B 703 1555 1555 2.76 LINK O GLU B 644 CA CA B 702 1555 1555 2.45 LINK OD1 ASP B 647 CA CA B 702 1555 1555 2.43 LINK OD1 ASN B 649 CA CA B 702 1555 1555 2.36 LINK O LEU B 663 CA CA B 701 1555 1555 2.29 LINK O SER B 664 CA CA B 702 1555 1555 2.52 LINK OD1 ASP B 666 CA CA B 701 1555 1555 2.62 LINK OD2 ASP B 666 CA CA B 701 1555 1555 2.63 LINK CA CA B 701 O HOH B 808 1555 1555 2.26 LINK CA CA B 701 O HOH B 839 1555 1555 2.48 LINK CA CA B 701 O HOH B 885 1555 1555 2.40 LINK CA CA B 702 O HOH B 801 1555 1555 2.42 LINK CA CA B 702 O HOH B 986 1555 1555 2.84 LINK OD2 ASP A 252 CA CA A 701 1555 1555 2.58 LINK OD1 ASN A 256 CA CA A 701 1555 1555 2.50 LINK O LYS A 258 CA CA A 701 1555 1555 2.38 LINK OD1 ASP A 264 CA CA A 701 1555 1555 2.56 LINK OD2 ASP A 264 CA CA A 701 1555 1555 2.70 LINK OD1 ASN A 564 CA CA A 702 1555 1555 2.41 LINK OD1 ASP A 569 CA CA A 704 1555 1555 2.52 LINK OD1 ASN A 571 CA CA A 704 1555 1555 3.10 LINK OD1 ASN A 573 CA CA A 704 1555 1555 2.60 LINK O VAL A 575 CA CA A 704 1555 1555 2.53 LINK OD2 ASP A 577 CA CA A 704 1555 1555 2.82 LINK OE2 GLU A 580 CA CA A 704 1555 1555 2.78 LINK OE1 GLU A 580 CA CA A 704 1555 1555 2.79 LINK O GLU A 643 CA CA A 703 1555 1555 2.68 LINK OD1 ASP A 646 CA CA A 703 1555 1555 2.61 LINK OD1 ASN A 648 CA CA A 703 1555 1555 2.58 LINK O LEU A 662 CA CA A 702 1555 1555 2.39 LINK O SER A 663 CA CA A 703 1555 1555 2.46 LINK OD2 ASP A 665 CA CA A 702 1555 1555 2.53 LINK OD1 ASP A 665 CA CA A 702 1555 1555 2.68 LINK CA CA A 702 O HOH A 938 1555 1555 2.53 LINK CA CA A 703 O HOH A 936 1555 1555 2.50 CISPEP 1 GLY A 563 ASN A 564 0 5.70 SITE 1 AC1 6 ASN B 565 LEU B 663 ASP B 666 HOH B 808 SITE 2 AC1 6 HOH B 839 HOH B 885 SITE 1 AC2 6 GLU B 644 ASP B 647 ASN B 649 SER B 664 SITE 2 AC2 6 HOH B 801 HOH B 986 SITE 1 AC3 6 ASP B 570 ASN B 572 ASN B 574 VAL B 576 SITE 2 AC3 6 ASP B 578 GLU B 581 SITE 1 AC4 5 ASP B 252 ILE B 254 ASN B 256 LYS B 258 SITE 2 AC4 5 ASP B 264 SITE 1 AC5 5 ASP A 252 ILE A 254 ASN A 256 LYS A 258 SITE 2 AC5 5 ASP A 264 SITE 1 AC6 4 ASN A 564 LEU A 662 ASP A 665 HOH A 938 SITE 1 AC7 5 GLU A 643 ASP A 646 ASN A 648 SER A 663 SITE 2 AC7 5 HOH A 936 SITE 1 AC8 6 ASP A 569 ASN A 571 ASN A 573 VAL A 575 SITE 2 AC8 6 ASP A 577 GLU A 580 CRYST1 74.410 73.880 90.030 90.00 102.42 90.00 P 1 21 1 2 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 0.013439 0.000000 0.002960 0.00000 SCALE2 0.000000 0.013535 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011374 0.00000 ATOM 1 N SER B 235 12.761 13.150 15.302 1.00 80.60 N ANISOU 1 N SER B 235 10761 9902 9960 -1778 1277 76 N ATOM 2 CA SER B 235 12.914 14.013 16.468 1.00 77.55 C ANISOU 2 CA SER B 235 10348 9478 9639 -1934 1361 -85 C ATOM 3 C SER B 235 11.629 14.774 16.805 1.00 76.07 C ANISOU 3 C SER B 235 10289 9059 9557 -1875 1405 -60 C ATOM 4 O SER B 235 11.518 15.378 17.874 1.00 80.22 O ANISOU 4 O SER B 235 10798 9546 10136 -1982 1463 -201 O ATOM 5 CB SER B 235 14.074 14.996 16.254 1.00 73.78 C ANISOU 5 CB SER B 235 9869 8967 9197 -2150 1531 -174 C ATOM 6 OG SER B 235 13.962 15.678 15.013 1.00 64.78 O ANISOU 6 OG SER B 235 8880 7624 8111 -2127 1646 -36 O ATOM 7 N LYS B 236 10.661 14.728 15.895 1.00 68.40 N ANISOU 7 N LYS B 236 9434 7949 8605 -1705 1379 116 N ATOM 8 CA LYS B 236 9.457 15.543 16.004 1.00 60.95 C ANISOU 8 CA LYS B 236 8617 6773 7768 -1629 1441 176 C ATOM 9 C LYS B 236 8.181 14.702 15.962 1.00 46.70 C ANISOU 9 C LYS B 236 6815 4999 5928 -1419 1284 281 C ATOM 10 O LYS B 236 8.068 13.774 15.169 1.00 41.21 O ANISOU 10 O LYS B 236 6099 4413 5144 -1307 1173 386 O ATOM 11 CB LYS B 236 9.437 16.571 14.865 1.00 72.46 C ANISOU 11 CB LYS B 236 10222 8012 9297 -1623 1597 315 C ATOM 12 CG LYS B 236 8.293 17.574 14.914 1.00 78.60 C ANISOU 12 CG LYS B 236 11135 8527 10203 -1538 1700 397 C ATOM 13 CD LYS B 236 8.220 18.383 13.622 1.00 82.30 C ANISOU 13 CD LYS B 236 11742 8811 10716 -1481 1833 592 C ATOM 14 CE LYS B 236 9.516 19.136 13.358 1.00 87.80 C ANISOU 14 CE LYS B 236 12465 9445 11450 -1687 2011 521 C ATOM 15 NZ LYS B 236 9.488 19.888 12.064 1.00 89.12 N ANISOU 15 NZ LYS B 236 12770 9439 11653 -1627 2148 730 N ATOM 16 N ASN B 237 7.227 15.045 16.822 1.00 41.05 N ANISOU 16 N ASN B 237 6124 4189 5285 -1380 1288 240 N ATOM 17 CA ASN B 237 5.904 14.433 16.816 1.00 41.19 C ANISOU 17 CA ASN B 237 6150 4211 5289 -1192 1163 337 C ATOM 18 C ASN B 237 5.063 14.956 15.661 1.00 42.58 C ANISOU 18 C ASN B 237 6446 4229 5502 -1051 1204 537 C ATOM 19 O ASN B 237 4.685 16.125 15.646 1.00 46.47 O ANISOU 19 O ASN B 237 7040 4508 6109 -1050 1348 576 O ATOM 20 CB ASN B 237 5.186 14.713 18.138 1.00 39.36 C ANISOU 20 CB ASN B 237 5901 3930 5125 -1203 1170 224 C ATOM 21 CG ASN B 237 3.776 14.148 18.174 1.00 43.65 C ANISOU 21 CG ASN B 237 6449 4474 5663 -1016 1054 318 C ATOM 22 OD1 ASN B 237 3.031 14.226 17.197 1.00 50.01 O ANISOU 22 OD1 ASN B 237 7321 5206 6473 -878 1038 484 O ATOM 23 ND2 ASN B 237 3.401 13.580 19.311 1.00 43.28 N ANISOU 23 ND2 ASN B 237 6322 4525 5598 -1015 973 213 N ATOM 24 N VAL B 238 4.742 14.084 14.712 1.00 37.74 N ANISOU 24 N VAL B 238 5820 3729 4790 -927 1084 664 N ATOM 25 CA VAL B 238 4.016 14.510 13.523 1.00 39.39 C ANISOU 25 CA VAL B 238 6121 3845 4998 -793 1109 865 C ATOM 26 C VAL B 238 2.580 13.990 13.487 1.00 39.76 C ANISOU 26 C VAL B 238 6152 3933 5022 -617 985 952 C ATOM 27 O VAL B 238 2.017 13.775 12.416 1.00 39.11 O ANISOU 27 O VAL B 238 6092 3898 4869 -498 932 1109 O ATOM 28 CB VAL B 238 4.768 14.108 12.236 1.00 32.26 C ANISOU 28 CB VAL B 238 5225 3044 3987 -800 1094 955 C ATOM 29 CG1 VAL B 238 6.094 14.856 12.150 1.00 37.25 C ANISOU 29 CG1 VAL B 238 5887 3607 4660 -969 1247 894 C ATOM 30 CG2 VAL B 238 5.010 12.592 12.189 1.00 34.68 C ANISOU 30 CG2 VAL B 238 5425 3582 4170 -786 933 894 C ATOM 31 N ASN B 239 1.990 13.791 14.663 1.00 33.58 N ANISOU 31 N ASN B 239 5321 3150 4288 -610 941 847 N ATOM 32 CA ASN B 239 0.578 13.430 14.750 1.00 38.30 C ANISOU 32 CA ASN B 239 5900 3771 4882 -456 843 918 C ATOM 33 C ASN B 239 -0.307 14.331 13.879 1.00 41.69 C ANISOU 33 C ASN B 239 6413 4073 5354 -315 909 1116 C ATOM 34 O ASN B 239 -1.281 13.870 13.281 1.00 40.21 O ANISOU 34 O ASN B 239 6199 3978 5101 -176 806 1233 O ATOM 35 CB ASN B 239 0.095 13.474 16.201 1.00 35.07 C ANISOU 35 CB ASN B 239 5451 3325 4549 -480 840 782 C ATOM 36 CG ASN B 239 0.462 12.220 16.990 1.00 35.23 C ANISOU 36 CG ASN B 239 5362 3530 4492 -539 718 643 C ATOM 37 OD1 ASN B 239 0.788 11.179 16.424 1.00 36.80 O ANISOU 37 OD1 ASN B 239 5514 3879 4588 -526 620 664 O ATOM 38 ND2 ASN B 239 0.401 12.322 18.307 1.00 38.15 N ANISOU 38 ND2 ASN B 239 5694 3889 4912 -601 735 506 N ATOM 39 N ASP B 240 0.036 15.615 13.806 1.00 41.07 N ANISOU 39 N ASP B 240 6431 3789 5385 -353 1087 1156 N ATOM 40 CA ASP B 240 -0.753 16.562 13.025 1.00 50.40 C ANISOU 40 CA ASP B 240 7698 4831 6622 -204 1177 1367 C ATOM 41 C ASP B 240 -0.554 16.410 11.511 1.00 53.89 C ANISOU 41 C ASP B 240 8163 5368 6944 -138 1147 1553 C ATOM 42 O ASP B 240 -1.299 16.997 10.725 1.00 56.99 O ANISOU 42 O ASP B 240 8603 5710 7341 15 1186 1762 O ATOM 43 CB ASP B 240 -0.474 18.003 13.469 1.00 62.05 C ANISOU 43 CB ASP B 240 9280 6024 8271 -264 1408 1352 C ATOM 44 CG ASP B 240 1.011 18.318 13.550 1.00 78.32 C ANISOU 44 CG ASP B 240 11373 8036 10348 -474 1520 1226 C ATOM 45 OD1 ASP B 240 1.363 19.401 14.074 1.00 78.11 O ANISOU 45 OD1 ASP B 240 11424 7790 10464 -573 1715 1155 O ATOM 46 OD2 ASP B 240 1.827 17.482 13.100 1.00 87.01 O ANISOU 46 OD2 ASP B 240 12418 9320 11324 -547 1423 1190 O ATOM 47 N LEU B 241 0.437 15.615 11.111 1.00 46.28 N ANISOU 47 N LEU B 241 7160 4555 5868 -246 1082 1481 N ATOM 48 CA LEU B 241 0.731 15.395 9.696 1.00 45.95 C ANISOU 48 CA LEU B 241 7138 4624 5697 -206 1056 1630 C ATOM 49 C LEU B 241 0.287 14.026 9.179 1.00 49.89 C ANISOU 49 C LEU B 241 7542 5381 6031 -147 861 1628 C ATOM 50 O LEU B 241 0.643 13.630 8.070 1.00 53.66 O ANISOU 50 O LEU B 241 8019 5989 6379 -144 826 1704 O ATOM 51 CB LEU B 241 2.224 15.573 9.419 1.00 43.22 C ANISOU 51 CB LEU B 241 6825 4254 5342 -370 1154 1563 C ATOM 52 CG LEU B 241 2.829 16.948 9.665 1.00 49.73 C ANISOU 52 CG LEU B 241 7752 4828 6314 -458 1374 1567 C ATOM 53 CD1 LEU B 241 4.312 16.920 9.318 1.00 51.96 C ANISOU 53 CD1 LEU B 241 8040 5143 6561 -630 1445 1490 C ATOM 54 CD2 LEU B 241 2.085 18.008 8.863 1.00 52.93 C ANISOU 54 CD2 LEU B 241 8260 5079 6770 -307 1488 1815 C ATOM 55 N ILE B 242 -0.482 13.297 9.975 1.00 42.66 N ANISOU 55 N ILE B 242 6550 4539 5120 -112 744 1534 N ATOM 56 CA ILE B 242 -1.071 12.069 9.474 1.00 45.95 C ANISOU 56 CA ILE B 242 6884 5178 5396 -56 580 1535 C ATOM 57 C ILE B 242 -2.591 12.146 9.535 1.00 46.64 C ANISOU 57 C ILE B 242 6936 5297 5489 96 511 1629 C ATOM 58 O ILE B 242 -3.160 12.805 10.406 1.00 44.79 O ANISOU 58 O ILE B 242 6715 4921 5382 140 563 1623 O ATOM 59 CB ILE B 242 -0.586 10.830 10.256 1.00 47.43 C ANISOU 59 CB ILE B 242 6995 5468 5560 -157 492 1333 C ATOM 60 CG1 ILE B 242 -1.194 10.817 11.650 1.00 37.17 C ANISOU 60 CG1 ILE B 242 5658 4099 4366 -150 473 1229 C ATOM 61 CG2 ILE B 242 0.938 10.802 10.338 1.00 49.99 C ANISOU 61 CG2 ILE B 242 7334 5771 5889 -300 565 1238 C ATOM 62 CD1 ILE B 242 -1.298 9.437 12.248 1.00 42.15 C ANISOU 62 CD1 ILE B 242 6200 4867 4948 -181 355 1094 C ATOM 63 N THR B 243 -3.242 11.471 8.596 1.00 40.74 N ANISOU 63 N THR B 243 6136 4748 4597 170 398 1708 N ATOM 64 CA THR B 243 -4.691 11.365 8.592 1.00 43.07 C ANISOU 64 CA THR B 243 6366 5130 4869 304 311 1785 C ATOM 65 C THR B 243 -5.034 9.905 8.353 1.00 42.24 C ANISOU 65 C THR B 243 6166 5255 4630 268 161 1679 C ATOM 66 O THR B 243 -4.220 9.157 7.815 1.00 43.11 O ANISOU 66 O THR B 243 6275 5459 4645 174 138 1608 O ATOM 67 CB THR B 243 -5.328 12.229 7.485 1.00 48.30 C ANISOU 67 CB THR B 243 7050 5829 5473 453 341 2035 C ATOM 68 OG1 THR B 243 -4.836 11.803 6.210 1.00 54.49 O ANISOU 68 OG1 THR B 243 7833 6785 6084 424 303 2095 O ATOM 69 CG2 THR B 243 -4.980 13.702 7.683 1.00 54.37 C ANISOU 69 CG2 THR B 243 7930 6336 6393 493 522 2150 C ATOM 70 N SER B 244 -6.237 9.499 8.739 1.00 39.66 N ANISOU 70 N SER B 244 5758 5011 4300 337 72 1663 N ATOM 71 CA SER B 244 -6.597 8.090 8.661 1.00 44.48 C ANISOU 71 CA SER B 244 6282 5811 4808 282 -50 1536 C ATOM 72 C SER B 244 -8.093 7.839 8.540 1.00 45.54 C ANISOU 72 C SER B 244 6317 6097 4889 379 -148 1585 C ATOM 73 O SER B 244 -8.911 8.653 8.962 1.00 41.22 O ANISOU 73 O SER B 244 5757 5479 4426 492 -126 1680 O ATOM 74 CB SER B 244 -6.047 7.342 9.883 1.00 39.83 C ANISOU 74 CB SER B 244 5687 5137 4309 175 -47 1338 C ATOM 75 OG SER B 244 -6.479 7.947 11.093 1.00 42.74 O ANISOU 75 OG SER B 244 6060 5358 4823 212 -7 1318 O ATOM 76 N ASN B 245 -8.435 6.698 7.955 1.00 43.31 N ANISOU 76 N ASN B 245 5961 6027 4469 329 -246 1509 N ATOM 77 CA ASN B 245 -9.798 6.207 7.942 1.00 39.45 C ANISOU 77 CA ASN B 245 5358 5709 3922 378 -346 1501 C ATOM 78 C ASN B 245 -9.826 4.937 8.785 1.00 40.93 C ANISOU 78 C ASN B 245 5509 5896 4147 267 -382 1288 C ATOM 79 O ASN B 245 -9.201 3.938 8.428 1.00 39.44 O ANISOU 79 O ASN B 245 5328 5769 3888 156 -391 1170 O ATOM 80 CB ASN B 245 -10.230 5.907 6.511 1.00 50.30 C ANISOU 80 CB ASN B 245 6668 7354 5089 393 -420 1577 C ATOM 81 CG ASN B 245 -11.726 5.809 6.368 1.00 68.06 C ANISOU 81 CG ASN B 245 8786 9803 7272 477 -515 1628 C ATOM 82 OD1 ASN B 245 -12.446 5.656 7.354 1.00 73.70 O ANISOU 82 OD1 ASN B 245 9451 10462 8090 496 -533 1564 O ATOM 83 ND2 ASN B 245 -12.211 5.895 5.131 1.00 83.08 N ANISOU 83 ND2 ASN B 245 10618 11959 8988 525 -577 1746 N ATOM 84 N THR B 246 -10.546 4.976 9.901 1.00 32.17 N ANISOU 84 N THR B 246 4362 4710 3151 301 -389 1246 N ATOM 85 CA THR B 246 -10.392 3.954 10.934 1.00 37.12 C ANISOU 85 CA THR B 246 4978 5278 3848 206 -391 1066 C ATOM 86 C THR B 246 -11.721 3.373 11.397 1.00 38.90 C ANISOU 86 C THR B 246 5099 5606 4076 222 -458 1009 C ATOM 87 O THR B 246 -12.703 4.110 11.526 1.00 35.49 O ANISOU 87 O THR B 246 4615 5199 3671 331 -478 1109 O ATOM 88 CB THR B 246 -9.670 4.552 12.170 1.00 41.36 C ANISOU 88 CB THR B 246 5587 5585 4542 201 -307 1037 C ATOM 89 OG1 THR B 246 -8.405 5.105 11.775 1.00 37.66 O ANISOU 89 OG1 THR B 246 5207 5026 4075 171 -237 1077 O ATOM 90 CG2 THR B 246 -9.469 3.494 13.261 1.00 40.38 C ANISOU 90 CG2 THR B 246 5447 5420 4477 116 -308 875 C ATOM 91 N THR B 247 -11.744 2.063 11.659 1.00 36.48 N ANISOU 91 N THR B 247 4762 5349 3750 116 -480 853 N ATOM 92 CA THR B 247 -12.888 1.424 12.324 1.00 34.69 C ANISOU 92 CA THR B 247 4446 5182 3552 106 -521 774 C ATOM 93 C THR B 247 -12.468 0.580 13.537 1.00 31.80 C ANISOU 93 C THR B 247 4110 4683 3290 30 -474 638 C ATOM 94 O THR B 247 -11.436 -0.085 13.510 1.00 32.51 O ANISOU 94 O THR B 247 4258 4717 3377 -46 -433 567 O ATOM 95 CB THR B 247 -13.691 0.513 11.375 1.00 32.80 C ANISOU 95 CB THR B 247 4112 5179 3171 44 -591 713 C ATOM 96 OG1 THR B 247 -12.869 -0.582 10.960 1.00 44.67 O ANISOU 96 OG1 THR B 247 5660 6690 4624 -82 -561 588 O ATOM 97 CG2 THR B 247 -14.180 1.285 10.150 1.00 45.57 C ANISOU 97 CG2 THR B 247 5677 6981 4657 126 -649 859 C ATOM 98 N LEU B 248 -13.284 0.614 14.588 1.00 30.60 N ANISOU 98 N LEU B 248 3912 4490 3223 61 -477 614 N ATOM 99 CA LEU B 248 -13.072 -0.193 15.786 1.00 28.09 C ANISOU 99 CA LEU B 248 3608 4073 2992 2 -436 504 C ATOM 100 C LEU B 248 -14.388 -0.912 16.072 1.00 32.46 C ANISOU 100 C LEU B 248 4065 4727 3543 -21 -472 438 C ATOM 101 O LEU B 248 -15.435 -0.282 16.230 1.00 39.53 O ANISOU 101 O LEU B 248 4890 5677 4452 53 -508 494 O ATOM 102 CB LEU B 248 -12.672 0.693 16.966 1.00 30.79 C ANISOU 102 CB LEU B 248 3996 4254 3448 55 -386 537 C ATOM 103 CG LEU B 248 -12.375 0.070 18.334 1.00 32.98 C ANISOU 103 CG LEU B 248 4286 4441 3805 11 -342 449 C ATOM 104 CD1 LEU B 248 -11.089 -0.779 18.316 1.00 28.34 C ANISOU 104 CD1 LEU B 248 3752 3814 3201 -62 -301 395 C ATOM 105 CD2 LEU B 248 -12.249 1.178 19.373 1.00 33.30 C ANISOU 105 CD2 LEU B 248 4352 4367 3935 65 -301 481 C ATOM 106 N THR B 249 -14.339 -2.230 16.117 1.00 28.88 N ANISOU 106 N THR B 249 3605 4295 3075 -123 -451 320 N ATOM 107 CA THR B 249 -15.550 -3.034 16.184 1.00 37.58 C ANISOU 107 CA THR B 249 4613 5505 4159 -177 -475 239 C ATOM 108 C THR B 249 -15.377 -4.104 17.252 1.00 33.04 C ANISOU 108 C THR B 249 4064 4818 3670 -244 -403 140 C ATOM 109 O THR B 249 -14.360 -4.796 17.273 1.00 32.87 O ANISOU 109 O THR B 249 4117 4711 3662 -293 -342 99 O ATOM 110 CB THR B 249 -15.769 -3.739 14.832 1.00 49.19 C ANISOU 110 CB THR B 249 6044 7146 5501 -265 -506 175 C ATOM 111 OG1 THR B 249 -15.655 -2.782 13.772 1.00 52.53 O ANISOU 111 OG1 THR B 249 6458 7673 5828 -198 -563 287 O ATOM 112 CG2 THR B 249 -17.137 -4.422 14.774 1.00 49.57 C ANISOU 112 CG2 THR B 249 5974 7347 5515 -332 -536 86 C ATOM 113 N VAL B 250 -16.339 -4.265 18.149 1.00 33.18 N ANISOU 113 N VAL B 250 4023 4838 3748 -239 -399 113 N ATOM 114 CA VAL B 250 -16.182 -5.356 19.104 1.00 37.03 C ANISOU 114 CA VAL B 250 4537 5224 4307 -302 -320 33 C ATOM 115 C VAL B 250 -16.514 -6.668 18.412 1.00 38.83 C ANISOU 115 C VAL B 250 4743 5517 4493 -428 -286 -86 C ATOM 116 O VAL B 250 -17.375 -6.717 17.541 1.00 39.06 O ANISOU 116 O VAL B 250 4692 5706 4443 -474 -340 -126 O ATOM 117 CB VAL B 250 -16.980 -5.172 20.426 1.00 45.23 C ANISOU 117 CB VAL B 250 5532 6225 5428 -265 -306 39 C ATOM 118 CG1 VAL B 250 -17.570 -3.786 20.521 1.00 40.57 C ANISOU 118 CG1 VAL B 250 4894 5677 4843 -158 -368 126 C ATOM 119 CG2 VAL B 250 -18.027 -6.254 20.590 1.00 38.26 C ANISOU 119 CG2 VAL B 250 4581 5399 4556 -356 -278 -59 C ATOM 120 N VAL B 251 -15.797 -7.721 18.772 1.00 33.98 N ANISOU 120 N VAL B 251 4199 4785 3929 -484 -190 -141 N ATOM 121 CA VAL B 251 -16.035 -9.017 18.172 1.00 36.45 C ANISOU 121 CA VAL B 251 4509 5119 4223 -613 -124 -268 C ATOM 122 C VAL B 251 -16.482 -10.007 19.245 1.00 39.63 C ANISOU 122 C VAL B 251 4913 5422 4724 -660 -26 -322 C ATOM 123 O VAL B 251 -15.744 -10.327 20.188 1.00 34.38 O ANISOU 123 O VAL B 251 4314 4611 4137 -613 49 -275 O ATOM 124 CB VAL B 251 -14.800 -9.562 17.443 1.00 40.69 C ANISOU 124 CB VAL B 251 5134 5591 4736 -646 -61 -294 C ATOM 125 CG1 VAL B 251 -15.129 -10.901 16.796 1.00 42.59 C ANISOU 125 CG1 VAL B 251 5374 5844 4963 -792 28 -447 C ATOM 126 CG2 VAL B 251 -14.287 -8.554 16.402 1.00 33.52 C ANISOU 126 CG2 VAL B 251 4231 4777 3727 -599 -149 -228 C ATOM 127 N ASP B 252 -17.715 -10.468 19.101 1.00 31.32 N ANISOU 127 N ASP B 252 3777 4465 3659 -751 -26 -415 N ATOM 128 CA ASP B 252 -18.252 -11.494 19.968 1.00 39.11 C ANISOU 128 CA ASP B 252 4762 5363 4735 -820 82 -481 C ATOM 129 C ASP B 252 -17.655 -12.822 19.519 1.00 43.44 C ANISOU 129 C ASP B 252 5389 5802 5313 -925 221 -580 C ATOM 130 O ASP B 252 -18.264 -13.548 18.736 1.00 52.21 O ANISOU 130 O ASP B 252 6464 6984 6389 -1068 260 -721 O ATOM 131 CB ASP B 252 -19.770 -11.507 19.841 1.00 36.10 C ANISOU 131 CB ASP B 252 4253 5139 4324 -898 38 -560 C ATOM 132 CG ASP B 252 -20.436 -12.438 20.835 1.00 41.09 C ANISOU 132 CG ASP B 252 4876 5683 5054 -968 151 -618 C ATOM 133 OD1 ASP B 252 -21.649 -12.671 20.696 1.00 45.31 O ANISOU 133 OD1 ASP B 252 5304 6343 5570 -1062 139 -709 O ATOM 134 OD2 ASP B 252 -19.755 -12.930 21.757 1.00 42.98 O ANISOU 134 OD2 ASP B 252 5207 5741 5384 -927 253 -567 O ATOM 135 N ALA B 253 -16.454 -13.128 20.005 1.00 34.95 N ANISOU 135 N ALA B 253 4417 4562 4301 -855 302 -508 N ATOM 136 CA ALA B 253 -15.673 -14.266 19.494 1.00 39.27 C ANISOU 136 CA ALA B 253 5050 4989 4881 -921 441 -578 C ATOM 137 C ALA B 253 -16.353 -15.631 19.669 1.00 45.77 C ANISOU 137 C ALA B 253 5884 5722 5783 -1054 600 -703 C ATOM 138 O ALA B 253 -16.317 -16.470 18.773 1.00 55.57 O ANISOU 138 O ALA B 253 7154 6944 7016 -1179 693 -839 O ATOM 139 CB ALA B 253 -14.273 -14.279 20.122 1.00 37.21 C ANISOU 139 CB ALA B 253 4877 4585 4676 -794 496 -451 C ATOM 140 N ILE B 254 -16.957 -15.833 20.833 1.00 38.90 N ANISOU 140 N ILE B 254 4994 4793 4991 -1035 642 -662 N ATOM 141 CA ILE B 254 -17.630 -17.075 21.199 1.00 37.30 C ANISOU 141 CA ILE B 254 4807 4484 4882 -1153 808 -759 C ATOM 142 C ILE B 254 -19.063 -17.089 20.650 1.00 49.03 C ANISOU 142 C ILE B 254 6180 6139 6312 -1310 758 -913 C ATOM 143 O ILE B 254 -19.774 -18.090 20.755 1.00 50.66 O ANISOU 143 O ILE B 254 6381 6287 6581 -1451 893 -1034 O ATOM 144 CB ILE B 254 -17.649 -17.218 22.747 1.00 62.61 C ANISOU 144 CB ILE B 254 8035 7572 8183 -1055 872 -629 C ATOM 145 CG1 ILE B 254 -18.480 -18.419 23.205 1.00 79.53 C ANISOU 145 CG1 ILE B 254 10188 9605 10426 -1177 1047 -715 C ATOM 146 CG2 ILE B 254 -18.179 -15.950 23.400 1.00 38.89 C ANISOU 146 CG2 ILE B 254 4944 4708 5126 -964 704 -541 C ATOM 147 CD1 ILE B 254 -18.563 -18.546 24.727 1.00 83.87 C ANISOU 147 CD1 ILE B 254 10753 10060 11053 -1080 1109 -576 C ATOM 148 N LYS B 255 -19.482 -15.969 20.062 1.00 54.76 N ANISOU 148 N LYS B 255 6809 7079 6919 -1284 572 -904 N ATOM 149 CA LYS B 255 -20.808 -15.862 19.448 1.00 53.99 C ANISOU 149 CA LYS B 255 6577 7195 6742 -1414 500 -1032 C ATOM 150 C LYS B 255 -21.946 -16.219 20.406 1.00 52.35 C ANISOU 150 C LYS B 255 6302 6981 6608 -1469 553 -1063 C ATOM 151 O LYS B 255 -22.939 -16.820 20.001 1.00 47.20 O ANISOU 151 O LYS B 255 5569 6427 5938 -1641 595 -1223 O ATOM 152 CB LYS B 255 -20.895 -16.748 18.197 1.00 53.68 C ANISOU 152 CB LYS B 255 6539 7210 6649 -1604 576 -1228 C ATOM 153 CG LYS B 255 -19.989 -16.316 17.047 1.00 60.75 C ANISOU 153 CG LYS B 255 7469 8176 7436 -1572 504 -1219 C ATOM 154 CD LYS B 255 -19.942 -17.386 15.956 1.00 72.86 C ANISOU 154 CD LYS B 255 9029 9720 8934 -1770 625 -1429 C ATOM 155 CE LYS B 255 -19.231 -16.892 14.696 1.00 80.02 C ANISOU 155 CE LYS B 255 9946 10756 9702 -1757 538 -1435 C ATOM 156 NZ LYS B 255 -17.806 -16.513 14.938 1.00 79.66 N ANISOU 156 NZ LYS B 255 10021 10543 9703 -1585 545 -1275 N ATOM 157 N ASN B 256 -21.819 -15.851 21.676 1.00 49.38 N ANISOU 157 N ASN B 256 5952 6504 6307 -1336 555 -921 N ATOM 158 CA ASN B 256 -22.881 -16.180 22.622 1.00 43.14 C ANISOU 158 CA ASN B 256 5101 5708 5584 -1386 612 -944 C ATOM 159 C ASN B 256 -23.795 -14.999 22.919 1.00 44.79 C ANISOU 159 C ASN B 256 5175 6107 5736 -1309 452 -889 C ATOM 160 O ASN B 256 -24.579 -15.042 23.864 1.00 42.97 O ANISOU 160 O ASN B 256 4893 5874 5559 -1311 483 -875 O ATOM 161 CB ASN B 256 -22.317 -16.760 23.916 1.00 40.35 C ANISOU 161 CB ASN B 256 4855 5124 5351 -1312 754 -839 C ATOM 162 CG ASN B 256 -21.435 -15.775 24.660 1.00 41.16 C ANISOU 162 CG ASN B 256 5000 5195 5443 -1110 665 -654 C ATOM 163 OD1 ASN B 256 -21.032 -14.748 24.111 1.00 33.35 O ANISOU 163 OD1 ASN B 256 3991 4308 4374 -1029 521 -608 O ATOM 164 ND2 ASN B 256 -21.136 -16.080 25.915 1.00 36.19 N ANISOU 164 ND2 ASN B 256 4427 4434 4889 -1035 755 -549 N ATOM 165 N AASN B 257 -23.688 -13.948 22.112 0.50 44.65 N ANISOU 165 N AASN B 257 5103 6249 5614 -1237 292 -849 N ATOM 166 N BASN B 257 -23.681 -13.944 22.111 0.50 44.62 N ANISOU 166 N BASN B 257 5100 6244 5609 -1236 292 -849 N ATOM 167 CA AASN B 257 -24.566 -12.794 22.261 0.50 47.30 C ANISOU 167 CA AASN B 257 5309 6764 5900 -1151 150 -790 C ATOM 168 CA BASN B 257 -24.536 -12.758 22.231 0.50 47.36 C ANISOU 168 CA BASN B 257 5317 6774 5904 -1146 146 -786 C ATOM 169 C AASN B 257 -24.373 -12.082 23.608 0.50 46.86 C ANISOU 169 C AASN B 257 5286 6604 5913 -995 143 -648 C ATOM 170 C BASN B 257 -24.287 -11.946 23.508 0.50 46.66 C ANISOU 170 C BASN B 257 5264 6588 5879 -981 127 -638 C ATOM 171 O AASN B 257 -25.281 -11.416 24.104 0.50 46.58 O ANISOU 171 O AASN B 257 5150 6669 5881 -944 86 -619 O ATOM 172 O BASN B 257 -25.074 -11.068 23.857 0.50 47.72 O ANISOU 172 O BASN B 257 5298 6833 6001 -907 45 -592 O ATOM 173 CB AASN B 257 -26.031 -13.219 22.075 0.50 47.53 C ANISOU 173 CB AASN B 257 5184 6968 5908 -1293 155 -921 C ATOM 174 CB BASN B 257 -26.021 -13.144 22.120 0.50 50.70 C ANISOU 174 CB BASN B 257 5586 7368 6310 -1280 149 -910 C ATOM 175 CG AASN B 257 -26.278 -13.908 20.736 0.50 43.62 C ANISOU 175 CG AASN B 257 4639 6612 5324 -1471 162 -1085 C ATOM 176 CG BASN B 257 -26.930 -11.942 21.875 0.50 56.55 C ANISOU 176 CG BASN B 257 6168 8346 6973 -1188 -9 -853 C ATOM 177 OD1AASN B 257 -25.972 -13.360 19.679 0.50 48.84 O ANISOU 177 OD1AASN B 257 5275 7409 5873 -1441 55 -1072 O ATOM 178 OD1BASN B 257 -26.464 -10.847 21.555 0.50 57.78 O ANISOU 178 OD1BASN B 257 6333 8541 7079 -1040 -119 -733 O ATOM 179 ND2AASN B 257 -26.834 -15.114 20.780 0.50 38.30 N ANISOU 179 ND2AASN B 257 3949 5906 4695 -1664 298 -1247 N ATOM 180 ND2BASN B 257 -28.237 -12.150 22.018 0.50 59.08 N ANISOU 180 ND2BASN B 257 6338 8822 7289 -1274 -10 -935 N ATOM 181 N LYS B 258 -23.191 -12.244 24.201 1.00 43.33 N ANISOU 181 N LYS B 258 4976 5970 5519 -924 207 -567 N ATOM 182 CA LYS B 258 -22.822 -11.499 25.407 1.00 36.83 C ANISOU 182 CA LYS B 258 4187 5070 4736 -782 193 -440 C ATOM 183 C LYS B 258 -21.384 -11.014 25.262 1.00 42.08 C ANISOU 183 C LYS B 258 4957 5650 5381 -682 165 -348 C ATOM 184 O LYS B 258 -20.536 -11.748 24.763 1.00 34.72 O ANISOU 184 O LYS B 258 4107 4635 4451 -723 227 -369 O ATOM 185 CB LYS B 258 -22.946 -12.360 26.661 1.00 40.15 C ANISOU 185 CB LYS B 258 4647 5364 5242 -809 329 -431 C ATOM 186 CG LYS B 258 -24.373 -12.712 27.037 1.00 43.92 C ANISOU 186 CG LYS B 258 5018 5921 5750 -899 365 -509 C ATOM 187 CD LYS B 258 -24.420 -13.400 28.385 1.00 51.87 C ANISOU 187 CD LYS B 258 6072 6800 6836 -900 498 -468 C ATOM 188 CE LYS B 258 -25.771 -14.059 28.622 1.00 54.92 C ANISOU 188 CE LYS B 258 6366 7240 7262 -1030 571 -569 C ATOM 189 NZ LYS B 258 -25.819 -14.696 29.958 1.00 62.06 N ANISOU 189 NZ LYS B 258 7320 8020 8239 -1024 709 -511 N ATOM 190 N ILE B 259 -21.114 -9.780 25.674 1.00 34.99 N ANISOU 190 N ILE B 259 4055 4772 4466 -558 82 -255 N ATOM 191 CA ILE B 259 -19.764 -9.239 25.570 1.00 36.16 C ANISOU 191 CA ILE B 259 4292 4853 4594 -475 56 -176 C ATOM 192 C ILE B 259 -19.058 -9.265 26.918 1.00 34.66 C ANISOU 192 C ILE B 259 4160 4561 4446 -411 117 -103 C ATOM 193 O ILE B 259 -19.509 -8.657 27.884 1.00 29.38 O ANISOU 193 O ILE B 259 3456 3911 3794 -361 105 -73 O ATOM 194 CB ILE B 259 -19.757 -7.822 25.015 1.00 31.99 C ANISOU 194 CB ILE B 259 3732 4406 4017 -391 -61 -126 C ATOM 195 CG1 ILE B 259 -20.482 -7.790 23.667 1.00 32.21 C ANISOU 195 CG1 ILE B 259 3684 4573 3980 -443 -129 -180 C ATOM 196 CG2 ILE B 259 -18.320 -7.308 24.886 1.00 31.98 C ANISOU 196 CG2 ILE B 259 3823 4331 3997 -328 -73 -57 C ATOM 197 CD1 ILE B 259 -19.974 -8.818 22.690 1.00 36.95 C ANISOU 197 CD1 ILE B 259 4330 5165 4546 -546 -88 -252 C ATOM 198 N VAL B 260 -17.945 -9.981 26.962 1.00 24.36 N ANISOU 198 N VAL B 260 2940 3164 3152 -411 186 -73 N ATOM 199 CA VAL B 260 -17.232 -10.253 28.190 1.00 25.48 C ANISOU 199 CA VAL B 260 3127 3237 3320 -356 254 4 C ATOM 200 C VAL B 260 -15.749 -10.058 27.900 1.00 24.33 C ANISOU 200 C VAL B 260 3045 3056 3143 -301 243 63 C ATOM 201 O VAL B 260 -15.225 -10.599 26.931 1.00 27.99 O ANISOU 201 O VAL B 260 3549 3485 3603 -334 267 39 O ATOM 202 CB VAL B 260 -17.446 -11.723 28.607 1.00 32.67 C ANISOU 202 CB VAL B 260 4064 4060 4289 -413 393 -7 C ATOM 203 CG1 VAL B 260 -16.895 -11.967 29.993 1.00 34.80 C ANISOU 203 CG1 VAL B 260 4360 4290 4571 -341 461 96 C ATOM 204 CG2 VAL B 260 -18.932 -12.095 28.522 1.00 30.00 C ANISOU 204 CG2 VAL B 260 3658 3760 3981 -506 414 -99 C ATOM 205 N PRO B 261 -15.057 -9.288 28.733 1.00 25.25 N ANISOU 205 N PRO B 261 3166 3193 3234 -227 214 131 N ATOM 206 CA PRO B 261 -13.644 -9.032 28.390 1.00 28.85 C ANISOU 206 CA PRO B 261 3668 3638 3656 -186 198 179 C ATOM 207 C PRO B 261 -12.764 -10.290 28.246 1.00 34.36 C ANISOU 207 C PRO B 261 4416 4264 4375 -181 297 217 C ATOM 208 O PRO B 261 -11.852 -10.304 27.410 1.00 31.48 O ANISOU 208 O PRO B 261 4085 3884 3991 -175 290 222 O ATOM 209 CB PRO B 261 -13.171 -8.148 29.545 1.00 31.10 C ANISOU 209 CB PRO B 261 3934 3974 3909 -129 171 229 C ATOM 210 CG PRO B 261 -14.438 -7.381 29.941 1.00 25.36 C ANISOU 210 CG PRO B 261 3157 3283 3195 -139 129 184 C ATOM 211 CD PRO B 261 -15.533 -8.428 29.833 1.00 20.84 C ANISOU 211 CD PRO B 261 2565 2685 2667 -190 183 147 C ATOM 212 N ALA B 262 -13.032 -11.333 29.026 1.00 29.98 N ANISOU 212 N ALA B 262 3868 3659 3864 -180 401 249 N ATOM 213 CA ALA B 262 -12.187 -12.542 28.977 1.00 34.99 C ANISOU 213 CA ALA B 262 4553 4206 4534 -153 520 306 C ATOM 214 C ALA B 262 -12.337 -13.370 27.695 1.00 31.97 C ANISOU 214 C ALA B 262 4215 3737 4195 -229 581 221 C ATOM 215 O ALA B 262 -11.443 -14.141 27.349 1.00 39.62 O ANISOU 215 O ALA B 262 5233 4630 5191 -202 670 255 O ATOM 216 CB ALA B 262 -12.417 -13.423 30.211 1.00 30.07 C ANISOU 216 CB ALA B 262 3932 3544 3951 -118 633 387 C ATOM 217 N GLN B 263 -13.458 -13.223 26.998 1.00 35.71 N ANISOU 217 N GLN B 263 4663 4235 4670 -324 540 108 N ATOM 218 CA GLN B 263 -13.722 -14.039 25.803 1.00 34.33 C ANISOU 218 CA GLN B 263 4518 4004 4520 -423 602 1 C ATOM 219 C GLN B 263 -13.677 -13.235 24.513 1.00 35.86 C ANISOU 219 C GLN B 263 4695 4289 4641 -460 485 -68 C ATOM 220 O GLN B 263 -13.326 -13.752 23.460 1.00 40.62 O ANISOU 220 O GLN B 263 5334 4863 5237 -515 527 -133 O ATOM 221 CB GLN B 263 -15.090 -14.715 25.893 1.00 42.53 C ANISOU 221 CB GLN B 263 5528 5024 5606 -530 665 -92 C ATOM 222 CG GLN B 263 -15.161 -15.887 26.846 1.00 50.76 C ANISOU 222 CG GLN B 263 6611 5938 6739 -524 833 -43 C ATOM 223 CD GLN B 263 -15.963 -15.563 28.085 1.00 60.67 C ANISOU 223 CD GLN B 263 7814 7239 7999 -499 813 7 C ATOM 224 OE1 GLN B 263 -17.119 -15.146 28.000 1.00 62.02 O ANISOU 224 OE1 GLN B 263 7917 7492 8155 -569 748 -75 O ATOM 225 NE2 GLN B 263 -15.352 -15.753 29.249 1.00 64.32 N ANISOU 225 NE2 GLN B 263 8299 7666 8476 -395 870 144 N ATOM 226 N ASP B 264 -14.046 -11.965 24.594 1.00 28.16 N ANISOU 226 N ASP B 264 3666 3421 3611 -428 350 -50 N ATOM 227 CA ASP B 264 -14.264 -11.169 23.395 1.00 29.30 C ANISOU 227 CA ASP B 264 3784 3664 3686 -458 242 -100 C ATOM 228 C ASP B 264 -13.100 -10.213 23.120 1.00 30.45 C ANISOU 228 C ASP B 264 3958 3827 3784 -381 175 -27 C ATOM 229 O ASP B 264 -12.225 -10.051 23.960 1.00 37.71 O ANISOU 229 O ASP B 264 4901 4706 4720 -310 196 53 O ATOM 230 CB ASP B 264 -15.593 -10.437 23.557 1.00 25.20 C ANISOU 230 CB ASP B 264 3180 3246 3149 -472 156 -126 C ATOM 231 CG ASP B 264 -16.757 -11.404 23.725 1.00 38.03 C ANISOU 231 CG ASP B 264 4764 4870 4816 -568 225 -214 C ATOM 232 OD1 ASP B 264 -16.850 -12.346 22.910 1.00 34.74 O ANISOU 232 OD1 ASP B 264 4364 4435 4398 -669 292 -307 O ATOM 233 OD2 ASP B 264 -17.566 -11.246 24.666 1.00 32.94 O ANISOU 233 OD2 ASP B 264 4071 4241 4204 -555 225 -200 O ATOM 234 N TYR B 265 -13.067 -9.604 21.939 1.00 30.77 N ANISOU 234 N TYR B 265 3992 3940 3760 -401 100 -52 N ATOM 235 CA TYR B 265 -12.005 -8.646 21.624 1.00 26.52 C ANISOU 235 CA TYR B 265 3483 3414 3180 -339 45 15 C ATOM 236 C TYR B 265 -12.472 -7.554 20.686 1.00 23.01 C ANISOU 236 C TYR B 265 3006 3068 2667 -336 -59 19 C ATOM 237 O TYR B 265 -13.634 -7.488 20.338 1.00 31.37 O ANISOU 237 O TYR B 265 4007 4206 3705 -369 -101 -22 O ATOM 238 CB TYR B 265 -10.778 -9.342 21.035 1.00 33.20 C ANISOU 238 CB TYR B 265 4390 4205 4019 -349 115 12 C ATOM 239 CG TYR B 265 -11.000 -9.973 19.677 1.00 29.38 C ANISOU 239 CG TYR B 265 3918 3752 3493 -436 137 -81 C ATOM 240 CD1 TYR B 265 -10.597 -9.329 18.519 1.00 30.74 C ANISOU 240 CD1 TYR B 265 4099 3997 3584 -444 76 -80 C ATOM 241 CD2 TYR B 265 -11.605 -11.221 19.558 1.00 39.70 C ANISOU 241 CD2 TYR B 265 5229 5019 4838 -520 229 -175 C ATOM 242 CE1 TYR B 265 -10.789 -9.909 17.265 1.00 38.67 C ANISOU 242 CE1 TYR B 265 5108 5055 4528 -533 96 -175 C ATOM 243 CE2 TYR B 265 -11.807 -11.805 18.317 1.00 40.83 C ANISOU 243 CE2 TYR B 265 5379 5203 4932 -621 257 -286 C ATOM 244 CZ TYR B 265 -11.394 -11.146 17.178 1.00 45.04 C ANISOU 244 CZ TYR B 265 5915 5831 5369 -627 186 -286 C ATOM 245 OH TYR B 265 -11.592 -11.724 15.949 1.00 58.38 O ANISOU 245 OH TYR B 265 7606 7585 6991 -735 214 -404 O ATOM 246 N LEU B 266 -11.543 -6.690 20.298 1.00 24.05 N ANISOU 246 N LEU B 266 3171 3201 2766 -292 -93 77 N ATOM 247 CA LEU B 266 -11.840 -5.565 19.432 1.00 24.94 C ANISOU 247 CA LEU B 266 3266 3391 2819 -269 -177 112 C ATOM 248 C LEU B 266 -10.954 -5.660 18.191 1.00 35.04 C ANISOU 248 C LEU B 266 4588 4694 4030 -296 -172 110 C ATOM 249 O LEU B 266 -9.747 -5.915 18.306 1.00 30.54 O ANISOU 249 O LEU B 266 4070 4059 3475 -291 -120 123 O ATOM 250 CB LEU B 266 -11.558 -4.250 20.165 1.00 30.89 C ANISOU 250 CB LEU B 266 4027 4107 3603 -192 -205 190 C ATOM 251 CG LEU B 266 -12.467 -3.859 21.344 1.00 29.39 C ANISOU 251 CG LEU B 266 3793 3904 3471 -156 -213 194 C ATOM 252 CD1 LEU B 266 -11.703 -2.973 22.319 1.00 28.90 C ANISOU 252 CD1 LEU B 266 3759 3777 3445 -113 -194 235 C ATOM 253 CD2 LEU B 266 -13.724 -3.148 20.837 1.00 30.50 C ANISOU 253 CD2 LEU B 266 3873 4123 3593 -125 -276 213 C ATOM 254 N ALA B 267 -11.566 -5.473 17.021 1.00 24.89 N ANISOU 254 N ALA B 267 3273 3520 2664 -324 -226 95 N ATOM 255 CA ALA B 267 -10.870 -5.407 15.747 1.00 24.82 C ANISOU 255 CA ALA B 267 3298 3564 2570 -350 -231 98 C ATOM 256 C ALA B 267 -10.591 -3.957 15.362 1.00 31.24 C ANISOU 256 C ALA B 267 4123 4399 3348 -275 -287 212 C ATOM 257 O ALA B 267 -11.517 -3.188 15.114 1.00 36.03 O ANISOU 257 O ALA B 267 4680 5085 3925 -231 -351 265 O ATOM 258 CB ALA B 267 -11.718 -6.091 14.649 1.00 24.70 C ANISOU 258 CB ALA B 267 3235 3688 2463 -435 -252 11 C ATOM 259 N LEU B 268 -9.316 -3.585 15.316 1.00 32.05 N ANISOU 259 N LEU B 268 4289 4431 3460 -259 -252 253 N ATOM 260 CA LEU B 268 -8.910 -2.252 14.891 1.00 27.00 C ANISOU 260 CA LEU B 268 3675 3788 2794 -204 -278 355 C ATOM 261 C LEU B 268 -8.358 -2.312 13.464 1.00 33.31 C ANISOU 261 C LEU B 268 4501 4667 3487 -237 -279 366 C ATOM 262 O LEU B 268 -7.433 -3.077 13.182 1.00 34.28 O ANISOU 262 O LEU B 268 4660 4769 3598 -288 -226 311 O ATOM 263 CB LEU B 268 -7.837 -1.707 15.820 1.00 25.65 C ANISOU 263 CB LEU B 268 3548 3497 2700 -180 -231 385 C ATOM 264 CG LEU B 268 -7.158 -0.436 15.310 1.00 32.69 C ANISOU 264 CG LEU B 268 4484 4362 3575 -150 -226 473 C ATOM 265 CD1 LEU B 268 -8.152 0.713 15.264 1.00 32.88 C ANISOU 265 CD1 LEU B 268 4491 4390 3612 -80 -263 556 C ATOM 266 CD2 LEU B 268 -5.990 -0.094 16.193 1.00 37.02 C ANISOU 266 CD2 LEU B 268 5063 4816 4186 -161 -171 467 C ATOM 267 N LYS B 269 -8.928 -1.509 12.569 1.00 35.64 N ANISOU 267 N LYS B 269 4777 5062 3705 -200 -334 446 N ATOM 268 CA LYS B 269 -8.473 -1.452 11.178 1.00 34.75 C ANISOU 268 CA LYS B 269 4684 5048 3469 -227 -339 471 C ATOM 269 C LYS B 269 -8.333 -0.006 10.747 1.00 39.69 C ANISOU 269 C LYS B 269 5336 5668 4075 -146 -353 624 C ATOM 270 O LYS B 269 -9.243 0.807 10.965 1.00 40.80 O ANISOU 270 O LYS B 269 5441 5824 4237 -65 -392 710 O ATOM 271 CB LYS B 269 -9.453 -2.167 10.247 1.00 41.79 C ANISOU 271 CB LYS B 269 5509 6128 4241 -280 -389 410 C ATOM 272 CG LYS B 269 -9.331 -3.682 10.228 1.00 55.08 C ANISOU 272 CG LYS B 269 7190 7815 5921 -390 -340 245 C ATOM 273 CD LYS B 269 -10.434 -4.298 9.371 1.00 62.74 C ANISOU 273 CD LYS B 269 8081 8987 6770 -463 -388 165 C ATOM 274 CE LYS B 269 -10.158 -5.758 9.033 1.00 63.69 C ANISOU 274 CE LYS B 269 8219 9109 6872 -593 -311 -11 C ATOM 275 NZ LYS B 269 -10.218 -6.659 10.214 1.00 61.23 N ANISOU 275 NZ LYS B 269 7921 8639 6703 -619 -241 -97 N ATOM 276 N SER B 270 -7.203 0.326 10.126 1.00 29.61 N ANISOU 276 N SER B 270 4123 4364 2763 -162 -309 663 N ATOM 277 CA SER B 270 -6.987 1.707 9.718 1.00 33.23 C ANISOU 277 CA SER B 270 4620 4791 3215 -90 -297 813 C ATOM 278 C SER B 270 -6.093 1.860 8.479 1.00 33.83 C ANISOU 278 C SER B 270 4742 4928 3183 -121 -268 859 C ATOM 279 O SER B 270 -5.137 1.105 8.280 1.00 37.23 O ANISOU 279 O SER B 270 5201 5351 3596 -198 -226 770 O ATOM 280 CB SER B 270 -6.405 2.501 10.895 1.00 33.29 C ANISOU 280 CB SER B 270 4673 4606 3368 -65 -238 833 C ATOM 281 OG SER B 270 -6.209 3.854 10.547 1.00 38.67 O ANISOU 281 OG SER B 270 5402 5225 4064 -4 -201 969 O ATOM 282 N GLN B 271 -6.422 2.838 7.645 1.00 31.10 N ANISOU 282 N GLN B 271 4403 4647 2766 -51 -282 1009 N ATOM 283 CA GLN B 271 -5.546 3.243 6.547 1.00 36.55 C ANISOU 283 CA GLN B 271 5148 5376 3363 -67 -241 1085 C ATOM 284 C GLN B 271 -5.041 4.632 6.863 1.00 41.02 C ANISOU 284 C GLN B 271 5784 5774 4028 -6 -168 1217 C ATOM 285 O GLN B 271 -5.827 5.562 7.014 1.00 39.46 O ANISOU 285 O GLN B 271 5579 5544 3870 95 -174 1341 O ATOM 286 CB GLN B 271 -6.293 3.243 5.212 1.00 48.13 C ANISOU 286 CB GLN B 271 6567 7076 4647 -39 -304 1168 C ATOM 287 CG GLN B 271 -6.340 1.880 4.525 1.00 61.36 C ANISOU 287 CG GLN B 271 8197 8925 6190 -146 -339 1015 C ATOM 288 CD GLN B 271 -4.967 1.404 4.046 1.00 69.94 C ANISOU 288 CD GLN B 271 9350 9977 7248 -236 -262 940 C ATOM 289 OE1 GLN B 271 -4.574 0.261 4.297 1.00 74.36 O ANISOU 289 OE1 GLN B 271 9908 10514 7831 -324 -235 775 O ATOM 290 NE2 GLN B 271 -4.236 2.280 3.356 1.00 69.94 N ANISOU 290 NE2 GLN B 271 9408 9966 7201 -210 -216 1068 N ATOM 291 N ILE B 272 -3.727 4.763 6.989 1.00 44.77 N ANISOU 291 N ILE B 272 6322 6139 4549 -71 -87 1183 N ATOM 292 CA ILE B 272 -3.115 6.002 7.444 1.00 40.68 C ANISOU 292 CA ILE B 272 5873 5441 4144 -50 3 1264 C ATOM 293 C ILE B 272 -2.343 6.665 6.318 1.00 45.99 C ANISOU 293 C ILE B 272 6607 6127 4740 -58 69 1379 C ATOM 294 O ILE B 272 -1.568 6.013 5.625 1.00 46.17 O ANISOU 294 O ILE B 272 6634 6237 4671 -130 77 1324 O ATOM 295 CB ILE B 272 -2.137 5.739 8.602 1.00 42.51 C ANISOU 295 CB ILE B 272 6115 5543 4494 -132 54 1129 C ATOM 296 CG1 ILE B 272 -2.821 4.911 9.709 1.00 41.26 C ANISOU 296 CG1 ILE B 272 5894 5386 4395 -131 -7 1013 C ATOM 297 CG2 ILE B 272 -1.582 7.051 9.124 1.00 44.15 C ANISOU 297 CG2 ILE B 272 6386 5573 4817 -134 154 1186 C ATOM 298 CD1 ILE B 272 -1.941 4.652 10.931 1.00 39.19 C ANISOU 298 CD1 ILE B 272 5628 5028 4235 -197 35 898 C ATOM 299 N LYS B 273 -2.560 7.961 6.134 1.00 46.41 N ANISOU 299 N LYS B 273 6710 6086 4836 20 129 1541 N ATOM 300 CA LYS B 273 -1.792 8.728 5.156 1.00 45.67 C ANISOU 300 CA LYS B 273 6689 5975 4690 15 216 1669 C ATOM 301 C LYS B 273 -0.840 9.674 5.869 1.00 46.20 C ANISOU 301 C LYS B 273 6830 5811 4911 -38 349 1659 C ATOM 302 O LYS B 273 -1.189 10.299 6.873 1.00 48.61 O ANISOU 302 O LYS B 273 7150 5962 5359 -11 387 1649 O ATOM 303 CB LYS B 273 -2.710 9.506 4.222 1.00 45.44 C ANISOU 303 CB LYS B 273 6664 6023 4577 149 206 1890 C ATOM 304 CG LYS B 273 -3.425 8.635 3.212 1.00 55.64 C ANISOU 304 CG LYS B 273 7877 7596 5668 173 87 1903 C ATOM 305 CD LYS B 273 -4.270 9.474 2.268 1.00 68.57 C ANISOU 305 CD LYS B 273 9505 9342 7205 316 77 2147 C ATOM 306 CE LYS B 273 -5.216 8.599 1.463 1.00 78.17 C ANISOU 306 CE LYS B 273 10611 10871 8219 337 -61 2139 C ATOM 307 NZ LYS B 273 -6.173 9.412 0.656 1.00 87.27 N ANISOU 307 NZ LYS B 273 11725 12167 9266 498 -86 2390 N ATOM 308 N VAL B 274 0.370 9.771 5.344 1.00 43.51 N ANISOU 308 N VAL B 274 6534 5458 4539 -126 425 1651 N ATOM 309 CA VAL B 274 1.412 10.543 5.991 1.00 42.59 C ANISOU 309 CA VAL B 274 6474 5154 4554 -212 553 1608 C ATOM 310 C VAL B 274 1.843 11.683 5.073 1.00 44.78 C ANISOU 310 C VAL B 274 6842 5352 4821 -198 679 1780 C ATOM 311 O VAL B 274 2.186 11.457 3.906 1.00 53.32 O ANISOU 311 O VAL B 274 7935 6561 5765 -202 677 1855 O ATOM 312 CB VAL B 274 2.617 9.647 6.320 1.00 37.55 C ANISOU 312 CB VAL B 274 5796 4567 3905 -344 550 1431 C ATOM 313 CG1 VAL B 274 3.708 10.451 6.998 1.00 40.42 C ANISOU 313 CG1 VAL B 274 6195 4773 4390 -449 678 1374 C ATOM 314 CG2 VAL B 274 2.172 8.448 7.178 1.00 39.69 C ANISOU 314 CG2 VAL B 274 5981 4916 4183 -344 437 1282 C ATOM 315 N ASP B 275 1.812 12.908 5.589 1.00 41.63 N ANISOU 315 N ASP B 275 6512 4739 4567 -184 801 1844 N ATOM 316 CA ASP B 275 2.230 14.077 4.795 1.00 43.15 C ANISOU 316 CA ASP B 275 6805 4814 4777 -171 953 2018 C ATOM 317 C ASP B 275 3.666 13.926 4.285 1.00 43.70 C ANISOU 317 C ASP B 275 6894 4914 4797 -314 1024 1959 C ATOM 318 O ASP B 275 4.523 13.380 4.979 1.00 41.84 O ANISOU 318 O ASP B 275 6612 4689 4596 -442 1015 1767 O ATOM 319 CB ASP B 275 2.112 15.342 5.639 1.00 42.26 C ANISOU 319 CB ASP B 275 6766 4428 4862 -167 1102 2043 C ATOM 320 CG ASP B 275 2.166 16.611 4.808 1.00 57.32 C ANISOU 320 CG ASP B 275 8787 6189 6804 -103 1269 2270 C ATOM 321 OD1 ASP B 275 1.135 17.316 4.749 1.00 62.17 O ANISOU 321 OD1 ASP B 275 9436 6715 7473 53 1304 2438 O ATOM 322 OD2 ASP B 275 3.232 16.912 4.219 1.00 59.53 O ANISOU 322 OD2 ASP B 275 9119 6438 7060 -203 1374 2289 O ATOM 323 N ASP B 276 3.934 14.423 3.078 1.00 55.14 N ANISOU 323 N ASP B 276 8405 6387 6159 -286 1099 2131 N ATOM 324 CA ASP B 276 5.284 14.378 2.511 1.00 56.91 C ANISOU 324 CA ASP B 276 8652 6636 6335 -418 1184 2092 C ATOM 325 C ASP B 276 6.319 15.133 3.364 1.00 57.29 C ANISOU 325 C ASP B 276 8739 6477 6552 -568 1339 1979 C ATOM 326 O ASP B 276 7.512 14.828 3.318 1.00 51.74 O ANISOU 326 O ASP B 276 8009 5819 5829 -707 1379 1864 O ATOM 327 CB ASP B 276 5.288 14.924 1.074 1.00 63.13 C ANISOU 327 CB ASP B 276 9509 7475 7002 -352 1253 2324 C ATOM 328 CG ASP B 276 4.474 14.063 0.115 1.00 66.69 C ANISOU 328 CG ASP B 276 9902 8194 7245 -243 1098 2404 C ATOM 329 OD1 ASP B 276 4.114 12.924 0.491 1.00 62.39 O ANISOU 329 OD1 ASP B 276 9266 7791 6650 -251 949 2250 O ATOM 330 OD2 ASP B 276 4.189 14.526 -1.014 1.00 63.93 O ANISOU 330 OD2 ASP B 276 9594 7919 6777 -155 1131 2620 O ATOM 331 N LYS B 277 5.861 16.124 4.127 1.00 55.17 N ANISOU 331 N LYS B 277 8527 5989 6445 -543 1433 2006 N ATOM 332 CA LYS B 277 6.744 16.879 5.019 1.00 50.26 C ANISOU 332 CA LYS B 277 7937 5173 5985 -702 1587 1874 C ATOM 333 C LYS B 277 7.388 15.992 6.088 1.00 50.38 C ANISOU 333 C LYS B 277 7840 5289 6012 -832 1498 1614 C ATOM 334 O LYS B 277 8.450 16.323 6.611 1.00 48.53 O ANISOU 334 O LYS B 277 7594 4996 5849 -998 1600 1479 O ATOM 335 CB LYS B 277 5.984 18.020 5.699 1.00 50.42 C ANISOU 335 CB LYS B 277 8037 4942 6179 -645 1704 1931 C ATOM 336 CG LYS B 277 5.641 19.190 4.787 1.00 63.23 C ANISOU 336 CG LYS B 277 9787 6396 7839 -541 1865 2192 C ATOM 337 CD LYS B 277 4.925 20.297 5.560 1.00 68.84 C ANISOU 337 CD LYS B 277 10578 6833 8747 -483 2004 2231 C ATOM 338 CE LYS B 277 3.523 19.868 5.979 1.00 77.68 C ANISOU 338 CE LYS B 277 11639 8022 9855 -305 1850 2267 C ATOM 339 NZ LYS B 277 2.807 20.911 6.786 1.00 83.75 N ANISOU 339 NZ LYS B 277 12477 8522 10821 -243 1991 2292 N ATOM 340 N VAL B 278 6.733 14.877 6.419 1.00 42.99 N ANISOU 340 N VAL B 278 6816 4513 5007 -755 1315 1550 N ATOM 341 CA VAL B 278 7.242 13.957 7.430 1.00 41.43 C ANISOU 341 CA VAL B 278 6509 4421 4813 -845 1226 1335 C ATOM 342 C VAL B 278 8.587 13.365 6.998 1.00 46.84 C ANISOU 342 C VAL B 278 7139 5240 5417 -961 1239 1256 C ATOM 343 O VAL B 278 8.783 13.048 5.827 1.00 46.15 O ANISOU 343 O VAL B 278 7070 5249 5215 -928 1230 1352 O ATOM 344 CB VAL B 278 6.222 12.823 7.723 1.00 47.26 C ANISOU 344 CB VAL B 278 7174 5296 5487 -729 1042 1306 C ATOM 345 CG1 VAL B 278 6.837 11.754 8.617 1.00 43.19 C ANISOU 345 CG1 VAL B 278 6546 4905 4959 -806 959 1115 C ATOM 346 CG2 VAL B 278 4.961 13.403 8.352 1.00 40.70 C ANISOU 346 CG2 VAL B 278 6376 4339 4750 -627 1033 1357 C ATOM 347 N LYS B 279 9.515 13.231 7.941 1.00 43.45 N ANISOU 347 N LYS B 279 6635 4834 5041 -1096 1264 1082 N ATOM 348 CA LYS B 279 10.850 12.736 7.618 1.00 42.05 C ANISOU 348 CA LYS B 279 6390 4788 4800 -1205 1289 1005 C ATOM 349 C LYS B 279 11.327 11.650 8.572 1.00 49.51 C ANISOU 349 C LYS B 279 7196 5890 5726 -1239 1188 840 C ATOM 350 O LYS B 279 10.727 11.410 9.629 1.00 48.85 O ANISOU 350 O LYS B 279 7071 5801 5690 -1207 1114 768 O ATOM 351 CB LYS B 279 11.871 13.877 7.582 1.00 46.57 C ANISOU 351 CB LYS B 279 7002 5245 5446 -1365 1472 982 C ATOM 352 CG LYS B 279 11.760 14.854 8.739 1.00 59.62 C ANISOU 352 CG LYS B 279 8675 6735 7243 -1455 1562 888 C ATOM 353 CD LYS B 279 10.734 15.946 8.428 1.00 68.17 C ANISOU 353 CD LYS B 279 9903 7587 8411 -1369 1654 1041 C ATOM 354 CE LYS B 279 10.261 16.677 9.684 1.00 67.26 C ANISOU 354 CE LYS B 279 9805 7312 8436 -1414 1712 938 C ATOM 355 NZ LYS B 279 8.767 16.790 9.723 1.00 49.46 N ANISOU 355 NZ LYS B 279 7614 4965 6216 -1228 1652 1060 N ATOM 356 N SER B 280 12.415 10.995 8.181 1.00 46.57 N ANISOU 356 N SER B 280 6748 5662 5283 -1296 1192 792 N ATOM 357 CA SER B 280 13.019 9.944 8.977 1.00 44.24 C ANISOU 357 CA SER B 280 6313 5529 4965 -1314 1115 662 C ATOM 358 C SER B 280 13.211 10.415 10.417 1.00 45.53 C ANISOU 358 C SER B 280 6411 5671 5215 -1405 1131 537 C ATOM 359 O SER B 280 13.626 11.551 10.662 1.00 43.20 O ANISOU 359 O SER B 280 6149 5275 4990 -1533 1250 501 O ATOM 360 CB SER B 280 14.361 9.537 8.360 1.00 53.25 C ANISOU 360 CB SER B 280 7385 6804 6044 -1385 1169 633 C ATOM 361 OG SER B 280 14.776 8.265 8.829 1.00 57.85 O ANISOU 361 OG SER B 280 7841 7554 6586 -1341 1085 556 O ATOM 362 N GLY B 281 12.887 9.551 11.373 1.00 44.82 N ANISOU 362 N GLY B 281 6234 5676 5120 -1347 1020 468 N ATOM 363 CA GLY B 281 13.078 9.889 12.771 1.00 40.41 C ANISOU 363 CA GLY B 281 5598 5139 4617 -1433 1024 344 C ATOM 364 C GLY B 281 11.919 10.637 13.411 1.00 41.45 C ANISOU 364 C GLY B 281 5812 5108 4830 -1409 1025 345 C ATOM 365 O GLY B 281 11.855 10.734 14.643 1.00 38.84 O ANISOU 365 O GLY B 281 5416 4810 4532 -1458 1006 238 O ATOM 366 N ASP B 282 11.027 11.200 12.595 1.00 40.45 N ANISOU 366 N ASP B 282 5821 4817 4732 -1334 1055 468 N ATOM 367 CA ASP B 282 9.750 11.698 13.111 1.00 37.26 C ANISOU 367 CA ASP B 282 5487 4269 4400 -1263 1040 495 C ATOM 368 C ASP B 282 8.953 10.497 13.643 1.00 42.92 C ANISOU 368 C ASP B 282 6140 5095 5075 -1140 884 483 C ATOM 369 O ASP B 282 9.185 9.353 13.232 1.00 35.52 O ANISOU 369 O ASP B 282 5146 4296 4056 -1082 803 499 O ATOM 370 CB ASP B 282 8.929 12.383 12.015 1.00 36.79 C ANISOU 370 CB ASP B 282 5566 4051 4360 -1172 1089 662 C ATOM 371 CG ASP B 282 9.505 13.736 11.583 1.00 49.99 C ANISOU 371 CG ASP B 282 7329 5561 6104 -1281 1272 695 C ATOM 372 OD1 ASP B 282 10.401 14.285 12.268 1.00 49.91 O ANISOU 372 OD1 ASP B 282 7282 5534 6147 -1446 1368 562 O ATOM 373 OD2 ASP B 282 9.043 14.251 10.542 1.00 48.19 O ANISOU 373 OD2 ASP B 282 7207 5228 5874 -1203 1324 858 O ATOM 374 N TYR B 283 8.008 10.748 14.541 1.00 36.56 N ANISOU 374 N TYR B 283 5346 4216 4329 -1103 857 452 N ATOM 375 CA TYR B 283 7.191 9.662 15.061 1.00 34.78 C ANISOU 375 CA TYR B 283 5066 4079 4071 -993 723 445 C ATOM 376 C TYR B 283 5.747 10.102 15.227 1.00 39.56 C ANISOU 376 C TYR B 283 5742 4553 4735 -895 704 504 C ATOM 377 O TYR B 283 5.476 11.290 15.407 1.00 39.21 O ANISOU 377 O TYR B 283 5770 4351 4776 -929 803 511 O ATOM 378 CB TYR B 283 7.740 9.192 16.408 1.00 38.68 C ANISOU 378 CB TYR B 283 5440 4701 4557 -1060 690 309 C ATOM 379 CG TYR B 283 7.721 10.273 17.462 1.00 39.40 C ANISOU 379 CG TYR B 283 5536 4709 4724 -1166 769 206 C ATOM 380 CD1 TYR B 283 6.630 10.425 18.312 1.00 45.51 C ANISOU 380 CD1 TYR B 283 6326 5418 5547 -1114 739 181 C ATOM 381 CD2 TYR B 283 8.784 11.153 17.597 1.00 49.83 C ANISOU 381 CD2 TYR B 283 6846 6019 6070 -1330 885 122 C ATOM 382 CE1 TYR B 283 6.607 11.422 19.275 1.00 51.97 C ANISOU 382 CE1 TYR B 283 7154 6157 6436 -1220 827 70 C ATOM 383 CE2 TYR B 283 8.771 12.152 18.560 1.00 53.18 C ANISOU 383 CE2 TYR B 283 7277 6365 6564 -1449 975 3 C ATOM 384 CZ TYR B 283 7.686 12.281 19.392 1.00 52.76 C ANISOU 384 CZ TYR B 283 7246 6244 6558 -1392 947 -24 C ATOM 385 OH TYR B 283 7.679 13.274 20.348 1.00 65.18 O ANISOU 385 OH TYR B 283 8829 7736 8199 -1519 1051 -159 O ATOM 386 N PHE B 284 4.825 9.143 15.157 1.00 39.46 N ANISOU 386 N PHE B 284 5709 4603 4681 -776 590 544 N ATOM 387 CA PHE B 284 3.432 9.403 15.501 1.00 28.89 C ANISOU 387 CA PHE B 284 4405 3179 3393 -682 556 584 C ATOM 388 C PHE B 284 3.012 8.394 16.553 1.00 34.28 C ANISOU 388 C PHE B 284 5002 3961 4061 -652 460 503 C ATOM 389 O PHE B 284 3.703 7.391 16.783 1.00 25.99 O ANISOU 389 O PHE B 284 3877 3044 2955 -675 414 450 O ATOM 390 CB PHE B 284 2.520 9.354 14.262 1.00 34.93 C ANISOU 390 CB PHE B 284 5229 3925 4118 -563 519 731 C ATOM 391 CG PHE B 284 2.246 7.956 13.746 1.00 29.70 C ANISOU 391 CG PHE B 284 4516 3413 3357 -502 404 741 C ATOM 392 CD1 PHE B 284 1.099 7.264 14.137 1.00 28.06 C ANISOU 392 CD1 PHE B 284 4272 3245 3144 -420 312 734 C ATOM 393 CD2 PHE B 284 3.124 7.337 12.875 1.00 31.06 C ANISOU 393 CD2 PHE B 284 4677 3679 3446 -534 403 748 C ATOM 394 CE1 PHE B 284 0.840 5.988 13.667 1.00 32.27 C ANISOU 394 CE1 PHE B 284 4765 3900 3596 -383 229 727 C ATOM 395 CE2 PHE B 284 2.867 6.053 12.395 1.00 31.52 C ANISOU 395 CE2 PHE B 284 4697 3857 3423 -488 321 740 C ATOM 396 CZ PHE B 284 1.729 5.381 12.792 1.00 28.33 C ANISOU 396 CZ PHE B 284 4263 3481 3020 -418 238 726 C ATOM 397 N THR B 285 1.881 8.649 17.196 1.00 28.39 N ANISOU 397 N THR B 285 4267 3149 3369 -593 440 502 N ATOM 398 CA THR B 285 1.441 7.751 18.237 1.00 28.18 C ANISOU 398 CA THR B 285 4165 3209 3332 -567 361 431 C ATOM 399 C THR B 285 0.076 7.144 17.932 1.00 32.80 C ANISOU 399 C THR B 285 4754 3803 3905 -446 277 498 C ATOM 400 O THR B 285 -0.713 7.695 17.163 1.00 31.30 O ANISOU 400 O THR B 285 4620 3542 3731 -377 284 593 O ATOM 401 CB THR B 285 1.419 8.459 19.614 1.00 34.14 C ANISOU 401 CB THR B 285 4900 3918 4152 -635 414 326 C ATOM 402 OG1 THR B 285 0.530 9.587 19.570 1.00 36.39 O ANISOU 402 OG1 THR B 285 5263 4038 4525 -598 480 364 O ATOM 403 CG2 THR B 285 2.832 8.928 19.993 1.00 31.19 C ANISOU 403 CG2 THR B 285 4497 3584 3772 -780 490 233 C ATOM 404 N ILE B 286 -0.159 5.977 18.510 1.00 28.80 N ANISOU 404 N ILE B 286 4181 3396 3366 -422 203 453 N ATOM 405 CA ILE B 286 -1.496 5.453 18.681 1.00 23.16 C ANISOU 405 CA ILE B 286 3451 2690 2658 -336 136 475 C ATOM 406 C ILE B 286 -1.738 5.280 20.177 1.00 29.33 C ANISOU 406 C ILE B 286 4181 3489 3476 -353 130 390 C ATOM 407 O ILE B 286 -0.961 4.613 20.875 1.00 30.79 O ANISOU 407 O ILE B 286 4308 3760 3630 -397 124 331 O ATOM 408 CB ILE B 286 -1.673 4.128 17.964 1.00 26.93 C ANISOU 408 CB ILE B 286 3903 3263 3065 -298 69 496 C ATOM 409 CG1 ILE B 286 -1.420 4.328 16.466 1.00 27.76 C ANISOU 409 CG1 ILE B 286 4057 3375 3116 -290 77 572 C ATOM 410 CG2 ILE B 286 -3.073 3.539 18.253 1.00 21.72 C ANISOU 410 CG2 ILE B 286 3216 2623 2415 -231 6 497 C ATOM 411 CD1 ILE B 286 -1.820 3.107 15.596 1.00 24.80 C ANISOU 411 CD1 ILE B 286 3664 3095 2664 -260 18 581 C ATOM 412 N LYS B 287 -2.789 5.917 20.687 1.00 24.20 N ANISOU 412 N LYS B 287 3545 2764 2886 -314 140 390 N ATOM 413 CA LYS B 287 -3.098 5.784 22.099 1.00 20.78 C ANISOU 413 CA LYS B 287 3064 2354 2479 -331 139 308 C ATOM 414 C LYS B 287 -4.465 5.147 22.211 1.00 23.54 C ANISOU 414 C LYS B 287 3389 2720 2836 -244 76 336 C ATOM 415 O LYS B 287 -5.201 5.102 21.236 1.00 24.70 O ANISOU 415 O LYS B 287 3556 2851 2976 -179 44 412 O ATOM 416 CB LYS B 287 -3.081 7.144 22.814 1.00 26.61 C ANISOU 416 CB LYS B 287 3834 2987 3289 -381 229 251 C ATOM 417 CG LYS B 287 -1.715 7.822 22.853 1.00 37.41 C ANISOU 417 CG LYS B 287 5216 4345 4652 -497 305 195 C ATOM 418 CD LYS B 287 -1.782 9.152 23.614 1.00 34.67 C ANISOU 418 CD LYS B 287 4906 3881 4387 -565 414 112 C ATOM 419 CE LYS B 287 -0.543 10.002 23.388 1.00 46.52 C ANISOU 419 CE LYS B 287 6437 5341 5899 -690 512 62 C ATOM 420 NZ LYS B 287 -0.639 11.319 24.091 1.00 52.97 N ANISOU 420 NZ LYS B 287 7300 6020 6806 -771 644 -35 N ATOM 421 N TYR B 288 -4.814 4.667 23.399 1.00 22.07 N ANISOU 421 N TYR B 288 3152 2580 2654 -249 61 275 N ATOM 422 CA TYR B 288 -6.056 3.927 23.545 1.00 21.65 C ANISOU 422 CA TYR B 288 3067 2554 2606 -181 8 293 C ATOM 423 C TYR B 288 -6.592 4.099 24.941 1.00 24.16 C ANISOU 423 C TYR B 288 3350 2874 2957 -188 28 228 C ATOM 424 O TYR B 288 -5.832 4.277 25.895 1.00 27.36 O ANISOU 424 O TYR B 288 3735 3315 3347 -253 62 160 O ATOM 425 CB TYR B 288 -5.882 2.423 23.179 1.00 19.78 C ANISOU 425 CB TYR B 288 2799 2408 2311 -174 -43 307 C ATOM 426 CG TYR B 288 -4.641 1.747 23.760 1.00 19.12 C ANISOU 426 CG TYR B 288 2683 2396 2186 -221 -27 275 C ATOM 427 CD1 TYR B 288 -4.669 1.148 25.009 1.00 21.44 C ANISOU 427 CD1 TYR B 288 2924 2752 2471 -224 -26 241 C ATOM 428 CD2 TYR B 288 -3.448 1.714 23.054 1.00 24.11 C ANISOU 428 CD2 TYR B 288 3329 3049 2782 -254 -11 290 C ATOM 429 CE1 TYR B 288 -3.528 0.541 25.555 1.00 24.31 C ANISOU 429 CE1 TYR B 288 3243 3206 2787 -248 -12 234 C ATOM 430 CE2 TYR B 288 -2.301 1.105 23.585 1.00 24.24 C ANISOU 430 CE2 TYR B 288 3300 3151 2760 -283 4 273 C ATOM 431 CZ TYR B 288 -2.353 0.522 24.832 1.00 28.12 C ANISOU 431 CZ TYR B 288 3732 3713 3240 -274 2 251 C ATOM 432 OH TYR B 288 -1.229 -0.079 25.361 1.00 25.90 O ANISOU 432 OH TYR B 288 3391 3540 2911 -284 17 256 O ATOM 433 N SER B 289 -7.912 4.021 25.063 1.00 25.15 N ANISOU 433 N SER B 289 3459 2982 3116 -125 5 244 N ATOM 434 CA SER B 289 -8.566 4.316 26.328 1.00 24.55 C ANISOU 434 CA SER B 289 3353 2897 3077 -124 34 183 C ATOM 435 C SER B 289 -8.206 3.326 27.444 1.00 27.91 C ANISOU 435 C SER B 289 3725 3427 3451 -164 21 133 C ATOM 436 O SER B 289 -7.659 2.244 27.187 1.00 26.69 O ANISOU 436 O SER B 289 3553 3343 3246 -170 -12 160 O ATOM 437 CB SER B 289 -10.080 4.368 26.114 1.00 26.93 C ANISOU 437 CB SER B 289 3636 3173 3424 -40 11 222 C ATOM 438 OG SER B 289 -10.552 3.151 25.561 1.00 26.62 O ANISOU 438 OG SER B 289 3561 3212 3343 -17 -57 257 O ATOM 439 N ASP B 290 -8.512 3.715 28.686 1.00 22.01 N ANISOU 439 N ASP B 290 2954 2692 2718 -186 59 65 N ATOM 440 CA ASP B 290 -8.284 2.871 29.859 1.00 24.31 C ANISOU 440 CA ASP B 290 3187 3098 2951 -213 52 31 C ATOM 441 C ASP B 290 -8.992 1.513 29.786 1.00 22.91 C ANISOU 441 C ASP B 290 2979 2964 2762 -161 9 85 C ATOM 442 O ASP B 290 -8.547 0.554 30.417 1.00 22.49 O ANISOU 442 O ASP B 290 2889 3000 2656 -169 6 98 O ATOM 443 CB ASP B 290 -8.687 3.595 31.151 1.00 25.09 C ANISOU 443 CB ASP B 290 3265 3206 3061 -246 104 -57 C ATOM 444 CG ASP B 290 -7.869 4.842 31.398 1.00 47.24 C ANISOU 444 CG ASP B 290 6097 5978 5873 -328 169 -139 C ATOM 445 OD1 ASP B 290 -6.769 4.960 30.816 1.00 48.58 O ANISOU 445 OD1 ASP B 290 6283 6159 6015 -372 167 -129 O ATOM 446 OD2 ASP B 290 -8.323 5.701 32.184 1.00 56.01 O ANISOU 446 OD2 ASP B 290 7213 7050 7019 -357 233 -224 O ATOM 447 N THR B 291 -10.075 1.438 29.014 1.00 21.75 N ANISOU 447 N THR B 291 2843 2759 2662 -109 -16 119 N ATOM 448 CA THR B 291 -10.818 0.196 28.811 1.00 19.91 C ANISOU 448 CA THR B 291 2581 2558 2425 -81 -46 151 C ATOM 449 C THR B 291 -10.207 -0.737 27.752 1.00 23.18 C ANISOU 449 C THR B 291 3015 2983 2809 -86 -70 194 C ATOM 450 O THR B 291 -10.764 -1.789 27.456 1.00 24.07 O ANISOU 450 O THR B 291 3113 3109 2923 -79 -79 206 O ATOM 451 CB THR B 291 -12.263 0.493 28.386 1.00 23.03 C ANISOU 451 CB THR B 291 2960 2919 2872 -35 -64 158 C ATOM 452 OG1 THR B 291 -12.245 1.462 27.336 1.00 25.43 O ANISOU 452 OG1 THR B 291 3298 3168 3198 -7 -77 190 O ATOM 453 CG2 THR B 291 -13.071 1.055 29.579 1.00 22.97 C ANISOU 453 CG2 THR B 291 2920 2908 2900 -23 -28 111 C ATOM 454 N VAL B 292 -9.063 -0.348 27.197 1.00 21.07 N ANISOU 454 N VAL B 292 2780 2708 2517 -107 -68 206 N ATOM 455 CA VAL B 292 -8.412 -1.107 26.126 1.00 21.74 C ANISOU 455 CA VAL B 292 2887 2799 2573 -112 -80 240 C ATOM 456 C VAL B 292 -6.984 -1.471 26.514 1.00 28.01 C ANISOU 456 C VAL B 292 3675 3642 3326 -134 -54 248 C ATOM 457 O VAL B 292 -6.269 -0.678 27.150 1.00 23.16 O ANISOU 457 O VAL B 292 3050 3056 2696 -163 -39 225 O ATOM 458 CB VAL B 292 -8.377 -0.293 24.790 1.00 23.11 C ANISOU 458 CB VAL B 292 3103 2931 2748 -107 -103 264 C ATOM 459 CG1 VAL B 292 -7.441 -0.935 23.747 1.00 20.95 C ANISOU 459 CG1 VAL B 292 2855 2674 2432 -125 -104 287 C ATOM 460 CG2 VAL B 292 -9.783 -0.101 24.222 1.00 24.36 C ANISOU 460 CG2 VAL B 292 3248 3078 2929 -69 -137 278 C ATOM 461 N GLN B 293 -6.575 -2.679 26.134 1.00 26.29 N ANISOU 461 N GLN B 293 3457 3441 3093 -122 -41 277 N ATOM 462 CA GLN B 293 -5.184 -3.100 26.255 1.00 23.79 C ANISOU 462 CA GLN B 293 3125 3176 2738 -124 -13 304 C ATOM 463 C GLN B 293 -4.801 -3.860 24.984 1.00 24.09 C ANISOU 463 C GLN B 293 3197 3182 2774 -118 0 323 C ATOM 464 O GLN B 293 -5.668 -4.257 24.209 1.00 24.24 O ANISOU 464 O GLN B 293 3242 3155 2811 -121 -10 308 O ATOM 465 CB GLN B 293 -4.962 -3.948 27.515 1.00 14.86 C ANISOU 465 CB GLN B 293 1943 2112 1589 -94 20 334 C ATOM 466 CG GLN B 293 -5.716 -5.287 27.516 1.00 15.93 C ANISOU 466 CG GLN B 293 2088 2205 1761 -59 55 360 C ATOM 467 CD GLN B 293 -5.659 -5.979 28.874 1.00 28.12 C ANISOU 467 CD GLN B 293 3585 3811 3290 -20 95 408 C ATOM 468 OE1 GLN B 293 -6.133 -5.448 29.868 1.00 33.13 O ANISOU 468 OE1 GLN B 293 4189 4493 3908 -30 79 389 O ATOM 469 NE2 GLN B 293 -5.072 -7.167 28.911 1.00 35.82 N ANISOU 469 NE2 GLN B 293 4555 4786 4269 30 157 477 N ATOM 470 N VAL B 294 -3.506 -4.032 24.744 1.00 19.64 N ANISOU 470 N VAL B 294 2625 2655 2180 -117 24 347 N ATOM 471 CA VAL B 294 -3.078 -4.588 23.464 1.00 17.70 C ANISOU 471 CA VAL B 294 2417 2378 1930 -119 45 354 C ATOM 472 C VAL B 294 -2.635 -6.059 23.554 1.00 18.99 C ANISOU 472 C VAL B 294 2571 2538 2109 -76 113 386 C ATOM 473 O VAL B 294 -2.091 -6.598 22.603 1.00 27.05 O ANISOU 473 O VAL B 294 3618 3535 3126 -76 151 385 O ATOM 474 CB VAL B 294 -1.927 -3.771 22.841 1.00 23.93 C ANISOU 474 CB VAL B 294 3212 3195 2684 -148 41 358 C ATOM 475 CG1 VAL B 294 -2.397 -2.402 22.467 1.00 29.71 C ANISOU 475 CG1 VAL B 294 3976 3894 3417 -186 0 337 C ATOM 476 CG2 VAL B 294 -0.766 -3.691 23.804 1.00 23.32 C ANISOU 476 CG2 VAL B 294 3071 3209 2580 -142 61 379 C ATOM 477 N TYR B 295 -2.874 -6.707 24.686 1.00 19.88 N ANISOU 477 N TYR B 295 2649 2666 2239 -35 143 418 N ATOM 478 CA TYR B 295 -2.605 -8.140 24.789 1.00 27.97 C ANISOU 478 CA TYR B 295 3674 3656 3296 19 231 464 C ATOM 479 C TYR B 295 -3.734 -8.699 25.625 1.00 23.37 C ANISOU 479 C TYR B 295 3090 3037 2751 30 251 468 C ATOM 480 O TYR B 295 -4.380 -7.952 26.374 1.00 23.28 O ANISOU 480 O TYR B 295 3055 3066 2726 12 196 451 O ATOM 481 CB TYR B 295 -1.260 -8.384 25.484 1.00 28.49 C ANISOU 481 CB TYR B 295 3679 3814 3332 84 266 545 C ATOM 482 CG TYR B 295 -1.182 -7.685 26.817 1.00 39.15 C ANISOU 482 CG TYR B 295 4961 5281 4634 89 219 569 C ATOM 483 CD1 TYR B 295 -1.459 -8.366 28.001 1.00 37.97 C ANISOU 483 CD1 TYR B 295 4773 5170 4485 147 255 635 C ATOM 484 CD2 TYR B 295 -0.891 -6.325 26.892 1.00 46.53 C ANISOU 484 CD2 TYR B 295 5875 6284 5523 25 150 518 C ATOM 485 CE1 TYR B 295 -1.414 -7.718 29.228 1.00 48.65 C ANISOU 485 CE1 TYR B 295 6059 6652 5775 141 212 644 C ATOM 486 CE2 TYR B 295 -0.847 -5.664 28.114 1.00 52.78 C ANISOU 486 CE2 TYR B 295 6603 7185 6264 9 118 512 C ATOM 487 CZ TYR B 295 -1.108 -6.364 29.281 1.00 57.60 C ANISOU 487 CZ TYR B 295 7168 7857 6859 65 144 572 C ATOM 488 OH TYR B 295 -1.060 -5.709 30.500 1.00 60.62 O ANISOU 488 OH TYR B 295 7485 8373 7175 40 113 556 O ATOM 489 N GLY B 296 -3.989 -9.995 25.484 1.00 26.15 N ANISOU 489 N GLY B 296 3471 3307 3157 54 344 482 N ATOM 490 CA GLY B 296 -4.997 -10.681 26.282 1.00 26.23 C ANISOU 490 CA GLY B 296 3482 3273 3212 62 389 493 C ATOM 491 C GLY B 296 -4.360 -11.446 27.424 1.00 38.39 C ANISOU 491 C GLY B 296 4987 4843 4758 157 467 612 C ATOM 492 O GLY B 296 -3.714 -10.832 28.282 1.00 38.11 O ANISOU 492 O GLY B 296 4888 4932 4659 195 419 668 O ATOM 493 N LEU B 297 -4.529 -12.775 27.437 1.00 31.26 N ANISOU 493 N LEU B 297 4119 3832 3927 193 594 650 N ATOM 494 CA LEU B 297 -3.998 -13.610 28.523 1.00 31.28 C ANISOU 494 CA LEU B 297 4090 3853 3941 304 688 793 C ATOM 495 C LEU B 297 -2.487 -13.730 28.469 1.00 28.85 C ANISOU 495 C LEU B 297 3741 3619 3601 397 713 887 C ATOM 496 O LEU B 297 -1.834 -13.904 29.498 1.00 31.18 O ANISOU 496 O LEU B 297 3968 4026 3854 496 732 1017 O ATOM 497 CB LEU B 297 -4.626 -15.018 28.516 1.00 30.70 C ANISOU 497 CB LEU B 297 4078 3612 3972 318 845 813 C ATOM 498 CG LEU B 297 -6.042 -15.097 29.080 1.00 34.78 C ANISOU 498 CG LEU B 297 4608 4091 4517 254 846 767 C ATOM 499 CD1 LEU B 297 -6.621 -16.492 28.905 1.00 45.42 C ANISOU 499 CD1 LEU B 297 6025 5255 5978 241 1020 764 C ATOM 500 CD2 LEU B 297 -6.056 -14.699 30.538 1.00 33.69 C ANISOU 500 CD2 LEU B 297 4402 4085 4314 315 803 868 C ATOM 501 N ASN B 298 -1.937 -13.653 27.262 1.00 27.39 N ANISOU 501 N ASN B 298 3588 3391 3428 367 715 825 N ATOM 502 CA ASN B 298 -0.499 -13.813 27.066 1.00 27.73 C ANISOU 502 CA ASN B 298 3589 3498 3450 453 750 906 C ATOM 503 C ASN B 298 0.182 -12.490 26.788 1.00 23.40 C ANISOU 503 C ASN B 298 2989 3092 2810 402 619 858 C ATOM 504 O ASN B 298 0.121 -11.997 25.669 1.00 24.84 O ANISOU 504 O ASN B 298 3216 3230 2992 321 580 757 O ATOM 505 CB ASN B 298 -0.225 -14.783 25.912 1.00 29.46 C ANISOU 505 CB ASN B 298 3881 3561 3753 461 877 873 C ATOM 506 CG ASN B 298 1.237 -15.205 25.834 1.00 40.11 C ANISOU 506 CG ASN B 298 5180 4960 5099 580 950 982 C ATOM 507 OD1 ASN B 298 2.122 -14.541 26.371 1.00 42.88 O ANISOU 507 OD1 ASN B 298 5435 5491 5368 627 873 1051 O ATOM 508 ND2 ASN B 298 1.492 -16.317 25.165 1.00 47.17 N ANISOU 508 ND2 ASN B 298 6134 5701 6086 625 1107 988 N ATOM 509 N PRO B 299 0.850 -11.913 27.800 1.00 27.39 N ANISOU 509 N PRO B 299 3396 3777 3233 443 560 930 N ATOM 510 CA PRO B 299 1.447 -10.579 27.620 1.00 36.18 C ANISOU 510 CA PRO B 299 4462 5019 4266 371 449 868 C ATOM 511 C PRO B 299 2.529 -10.562 26.537 1.00 35.37 C ANISOU 511 C PRO B 299 4359 4917 4164 374 472 856 C ATOM 512 O PRO B 299 2.890 -9.494 26.054 1.00 33.45 O ANISOU 512 O PRO B 299 4107 4728 3875 293 398 785 O ATOM 513 CB PRO B 299 2.073 -10.272 28.992 1.00 38.13 C ANISOU 513 CB PRO B 299 4590 5477 4422 421 413 952 C ATOM 514 CG PRO B 299 1.489 -11.287 29.934 1.00 40.13 C ANISOU 514 CG PRO B 299 4841 5704 4702 510 484 1056 C ATOM 515 CD PRO B 299 1.187 -12.498 29.108 1.00 30.85 C ANISOU 515 CD PRO B 299 3758 4322 3643 557 606 1076 C ATOM 516 N GLU B 300 3.049 -11.728 26.174 1.00 35.75 N ANISOU 516 N GLU B 300 4418 4897 4268 468 588 928 N ATOM 517 CA GLU B 300 4.048 -11.806 25.112 1.00 39.28 C ANISOU 517 CA GLU B 300 4867 5336 4722 476 627 914 C ATOM 518 C GLU B 300 3.407 -11.513 23.757 1.00 40.42 C ANISOU 518 C GLU B 300 5118 5345 4895 364 611 779 C ATOM 519 O GLU B 300 4.093 -11.163 22.801 1.00 35.28 O ANISOU 519 O GLU B 300 4475 4707 4224 329 608 737 O ATOM 520 CB GLU B 300 4.709 -13.190 25.073 1.00 44.94 C ANISOU 520 CB GLU B 300 5575 5995 5506 616 779 1025 C ATOM 521 CG GLU B 300 5.460 -13.572 26.338 1.00 53.19 C ANISOU 521 CG GLU B 300 6498 7199 6512 756 805 1193 C ATOM 522 CD GLU B 300 6.231 -14.882 26.190 1.00 64.97 C ANISOU 522 CD GLU B 300 7977 8629 8080 917 970 1322 C ATOM 523 OE1 GLU B 300 6.005 -15.603 25.192 1.00 64.42 O ANISOU 523 OE1 GLU B 300 8011 8356 8108 908 1082 1264 O ATOM 524 OE2 GLU B 300 7.062 -15.189 27.076 1.00 68.09 O ANISOU 524 OE2 GLU B 300 8253 9184 8433 1054 996 1482 O ATOM 525 N ASP B 301 2.087 -11.657 23.680 1.00 36.68 N ANISOU 525 N ASP B 301 4719 4760 4460 307 601 714 N ATOM 526 CA ASP B 301 1.358 -11.389 22.440 1.00 36.60 C ANISOU 526 CA ASP B 301 4792 4656 4457 202 576 592 C ATOM 527 C ASP B 301 1.504 -9.956 21.977 1.00 27.49 C ANISOU 527 C ASP B 301 3629 3583 3231 121 458 539 C ATOM 528 O ASP B 301 1.099 -9.617 20.877 1.00 30.15 O ANISOU 528 O ASP B 301 4023 3876 3555 47 432 461 O ATOM 529 CB ASP B 301 -0.133 -11.713 22.591 1.00 38.35 C ANISOU 529 CB ASP B 301 5067 4785 4720 154 573 537 C ATOM 530 CG ASP B 301 -0.427 -13.179 22.368 1.00 50.11 C ANISOU 530 CG ASP B 301 6609 6135 6296 182 720 532 C ATOM 531 OD1 ASP B 301 0.549 -13.947 22.202 1.00 53.32 O ANISOU 531 OD1 ASP B 301 7012 6510 6737 260 830 589 O ATOM 532 OD2 ASP B 301 -1.622 -13.558 22.349 1.00 53.34 O ANISOU 532 OD2 ASP B 301 7060 6464 6742 124 736 469 O ATOM 533 N ILE B 302 2.048 -9.098 22.826 1.00 30.32 N ANISOU 533 N ILE B 302 3915 4063 3540 129 394 580 N ATOM 534 CA ILE B 302 2.270 -7.704 22.439 1.00 26.83 C ANISOU 534 CA ILE B 302 3470 3678 3045 49 308 530 C ATOM 535 C ILE B 302 3.153 -7.603 21.184 1.00 28.58 C ANISOU 535 C ILE B 302 3714 3897 3249 24 337 510 C ATOM 536 O ILE B 302 3.075 -6.644 20.414 1.00 26.51 O ANISOU 536 O ILE B 302 3487 3628 2956 -49 289 463 O ATOM 537 CB ILE B 302 2.901 -6.955 23.603 1.00 29.50 C ANISOU 537 CB ILE B 302 3717 4156 3334 51 264 563 C ATOM 538 CG1 ILE B 302 2.909 -5.450 23.364 1.00 34.50 C ANISOU 538 CG1 ILE B 302 4362 4814 3932 -47 194 499 C ATOM 539 CG2 ILE B 302 4.300 -7.488 23.900 1.00 33.25 C ANISOU 539 CG2 ILE B 302 4104 4745 3784 122 317 639 C ATOM 540 CD1 ILE B 302 3.306 -4.702 24.632 1.00 33.92 C ANISOU 540 CD1 ILE B 302 4204 4874 3812 -71 159 498 C ATOM 541 N LYS B 303 3.968 -8.619 20.960 1.00 31.12 N ANISOU 541 N LYS B 303 4016 4215 3592 93 428 552 N ATOM 542 CA LYS B 303 4.794 -8.667 19.763 1.00 32.08 C ANISOU 542 CA LYS B 303 4159 4332 3700 75 472 529 C ATOM 543 C LYS B 303 3.963 -8.746 18.490 1.00 31.87 C ANISOU 543 C LYS B 303 4231 4204 3675 6 474 445 C ATOM 544 O LYS B 303 4.470 -8.469 17.403 1.00 35.21 O ANISOU 544 O LYS B 303 4680 4636 4063 -36 487 412 O ATOM 545 CB LYS B 303 5.758 -9.860 19.821 1.00 34.23 C ANISOU 545 CB LYS B 303 4389 4606 4009 181 590 594 C ATOM 546 CG LYS B 303 5.087 -11.199 19.535 1.00 43.91 C ANISOU 546 CG LYS B 303 5685 5685 5312 222 695 579 C ATOM 547 CD LYS B 303 6.070 -12.353 19.723 1.00 53.79 C ANISOU 547 CD LYS B 303 6895 6923 6618 349 832 665 C ATOM 548 CE LYS B 303 5.360 -13.698 19.704 1.00 66.67 C ANISOU 548 CE LYS B 303 8599 8386 8346 393 961 658 C ATOM 549 NZ LYS B 303 6.295 -14.827 20.022 1.00 77.51 N ANISOU 549 NZ LYS B 303 9932 9729 9788 544 1115 769 N ATOM 550 N ASN B 304 2.700 -9.147 18.596 1.00 30.63 N ANISOU 550 N ASN B 304 4121 3969 3548 -11 465 408 N ATOM 551 CA ASN B 304 1.863 -9.232 17.390 1.00 32.71 C ANISOU 551 CA ASN B 304 4459 4176 3792 -86 459 322 C ATOM 552 C ASN B 304 1.554 -7.847 16.812 1.00 36.51 C ANISOU 552 C ASN B 304 4956 4710 4207 -155 354 304 C ATOM 553 O ASN B 304 1.123 -7.720 15.675 1.00 34.05 O ANISOU 553 O ASN B 304 4691 4397 3850 -211 340 253 O ATOM 554 CB ASN B 304 0.548 -9.951 17.681 1.00 33.52 C ANISOU 554 CB ASN B 304 4591 4206 3940 -100 472 279 C ATOM 555 CG ASN B 304 0.746 -11.398 18.037 1.00 48.29 C ANISOU 555 CG ASN B 304 6470 5989 5889 -41 606 292 C ATOM 556 OD1 ASN B 304 -0.119 -12.017 18.660 1.00 51.56 O ANISOU 556 OD1 ASN B 304 6894 6341 6355 -35 636 285 O ATOM 557 ND2 ASN B 304 1.889 -11.954 17.647 1.00 53.49 N ANISOU 557 ND2 ASN B 304 7125 6636 6563 7 702 315 N ATOM 558 N ILE B 305 1.706 -6.811 17.629 1.00 29.13 N ANISOU 558 N ILE B 305 3982 3822 3264 -150 287 347 N ATOM 559 CA ILE B 305 1.531 -5.453 17.129 1.00 28.01 C ANISOU 559 CA ILE B 305 3862 3705 3076 -204 215 345 C ATOM 560 C ILE B 305 2.911 -4.832 16.991 1.00 34.06 C ANISOU 560 C ILE B 305 4600 4527 3816 -217 236 373 C ATOM 561 O ILE B 305 3.515 -4.409 17.975 1.00 31.53 O ANISOU 561 O ILE B 305 4221 4255 3505 -207 229 398 O ATOM 562 CB ILE B 305 0.634 -4.632 18.053 1.00 25.41 C ANISOU 562 CB ILE B 305 3520 3369 2766 -207 146 354 C ATOM 563 CG1 ILE B 305 -0.806 -5.100 17.876 1.00 30.35 C ANISOU 563 CG1 ILE B 305 4172 3955 3405 -210 120 321 C ATOM 564 CG2 ILE B 305 0.769 -3.156 17.729 1.00 32.08 C ANISOU 564 CG2 ILE B 305 4383 4222 3584 -248 104 369 C ATOM 565 CD1 ILE B 305 -1.689 -4.871 19.074 1.00 33.98 C ANISOU 565 CD1 ILE B 305 4604 4402 3904 -190 82 326 C ATOM 566 N GLY B 306 3.420 -4.820 15.763 1.00 33.40 N ANISOU 566 N GLY B 306 4550 4450 3690 -246 267 361 N ATOM 567 CA GLY B 306 4.798 -4.453 15.526 1.00 32.84 C ANISOU 567 CA GLY B 306 4446 4433 3596 -260 306 381 C ATOM 568 C GLY B 306 5.010 -3.406 14.448 1.00 31.67 C ANISOU 568 C GLY B 306 4345 4292 3394 -324 294 385 C ATOM 569 O GLY B 306 4.168 -2.530 14.213 1.00 28.78 O ANISOU 569 O GLY B 306 4025 3896 3015 -351 241 396 O ATOM 570 N ASP B 307 6.166 -3.493 13.807 1.00 31.07 N ANISOU 570 N ASP B 307 4255 4259 3290 -339 354 388 N ATOM 571 CA ASP B 307 6.564 -2.527 12.794 1.00 27.45 C ANISOU 571 CA ASP B 307 3838 3813 2778 -401 361 403 C ATOM 572 C ASP B 307 5.546 -2.480 11.659 1.00 24.28 C ANISOU 572 C ASP B 307 3516 3388 2322 -417 333 400 C ATOM 573 O ASP B 307 4.931 -3.490 11.305 1.00 27.78 O ANISOU 573 O ASP B 307 3976 3825 2753 -397 338 359 O ATOM 574 CB ASP B 307 7.947 -2.883 12.258 1.00 35.38 C ANISOU 574 CB ASP B 307 4806 4876 3760 -410 441 399 C ATOM 575 CG ASP B 307 9.010 -2.875 13.345 1.00 47.66 C ANISOU 575 CG ASP B 307 6259 6499 5352 -394 463 410 C ATOM 576 OD1 ASP B 307 8.749 -2.315 14.444 1.00 42.46 O ANISOU 576 OD1 ASP B 307 5564 5846 4721 -402 415 415 O ATOM 577 OD2 ASP B 307 10.108 -3.427 13.099 1.00 47.50 O ANISOU 577 OD2 ASP B 307 6183 6540 5325 -373 531 411 O ATOM 578 N ILE B 308 5.352 -1.295 11.106 1.00 28.93 N ANISOU 578 N ILE B 308 4149 3968 2874 -454 310 445 N ATOM 579 CA ILE B 308 4.468 -1.139 9.961 1.00 27.03 C ANISOU 579 CA ILE B 308 3969 3743 2558 -461 279 466 C ATOM 580 C ILE B 308 5.304 -1.307 8.707 1.00 31.98 C ANISOU 580 C ILE B 308 4619 4427 3104 -498 340 463 C ATOM 581 O ILE B 308 6.349 -0.671 8.559 1.00 32.91 O ANISOU 581 O ILE B 308 4734 4550 3221 -530 389 493 O ATOM 582 CB ILE B 308 3.788 0.244 9.973 1.00 35.25 C ANISOU 582 CB ILE B 308 5047 4745 3601 -461 235 543 C ATOM 583 CG1 ILE B 308 2.957 0.406 11.250 1.00 32.47 C ANISOU 583 CG1 ILE B 308 4669 4337 3331 -426 185 534 C ATOM 584 CG2 ILE B 308 2.925 0.424 8.757 1.00 33.23 C ANISOU 584 CG2 ILE B 308 4836 4541 3250 -453 201 589 C ATOM 585 CD1 ILE B 308 2.360 1.791 11.395 1.00 35.08 C ANISOU 585 CD1 ILE B 308 5035 4605 3689 -416 166 607 C ATOM 586 N LYS B 309 4.854 -2.188 7.819 1.00 29.15 N ANISOU 586 N LYS B 309 4281 4118 2676 -504 345 415 N ATOM 587 CA LYS B 309 5.607 -2.534 6.630 1.00 35.17 C ANISOU 587 CA LYS B 309 5065 4945 3355 -541 412 391 C ATOM 588 C LYS B 309 4.789 -2.308 5.368 1.00 33.91 C ANISOU 588 C LYS B 309 4949 4870 3064 -569 376 410 C ATOM 589 O LYS B 309 3.553 -2.280 5.406 1.00 30.19 O ANISOU 589 O LYS B 309 4479 4420 2570 -554 301 415 O ATOM 590 CB LYS B 309 6.041 -4.000 6.686 1.00 43.12 C ANISOU 590 CB LYS B 309 6047 5946 4392 -532 485 292 C ATOM 591 CG LYS B 309 6.882 -4.350 7.900 1.00 50.26 C ANISOU 591 CG LYS B 309 6890 6797 5409 -485 525 292 C ATOM 592 CD LYS B 309 7.873 -5.443 7.571 1.00 51.99 C ANISOU 592 CD LYS B 309 7088 7025 5643 -469 637 237 C ATOM 593 CE LYS B 309 8.627 -5.875 8.813 1.00 63.68 C ANISOU 593 CE LYS B 309 8491 8478 7227 -400 672 258 C ATOM 594 NZ LYS B 309 9.716 -6.831 8.468 1.00 73.53 N ANISOU 594 NZ LYS B 309 9707 9737 8494 -364 794 227 N ATOM 595 N ASP B 310 5.498 -2.152 4.255 1.00 35.76 N ANISOU 595 N ASP B 310 5210 5172 3205 -608 430 422 N ATOM 596 CA ASP B 310 4.887 -2.000 2.939 1.00 37.38 C ANISOU 596 CA ASP B 310 5449 5498 3256 -639 406 442 C ATOM 597 C ASP B 310 4.730 -3.386 2.303 1.00 38.13 C ANISOU 597 C ASP B 310 5538 5662 3286 -683 447 299 C ATOM 598 O ASP B 310 5.727 -4.032 1.970 1.00 40.81 O ANISOU 598 O ASP B 310 5880 5998 3628 -708 545 230 O ATOM 599 CB ASP B 310 5.780 -1.114 2.068 1.00 37.30 C ANISOU 599 CB ASP B 310 5473 5529 3172 -665 458 529 C ATOM 600 CG ASP B 310 5.173 -0.824 0.699 1.00 41.13 C ANISOU 600 CG ASP B 310 5989 6162 3477 -687 430 580 C ATOM 601 OD1 ASP B 310 4.302 -1.587 0.244 1.00 45.33 O ANISOU 601 OD1 ASP B 310 6505 6795 3921 -705 389 504 O ATOM 602 OD2 ASP B 310 5.577 0.181 0.076 1.00 49.01 O ANISOU 602 OD2 ASP B 310 7022 7185 4414 -689 454 700 O ATOM 603 N PRO B 311 3.480 -3.851 2.136 1.00 40.87 N ANISOU 603 N PRO B 311 5875 6072 3580 -696 384 246 N ATOM 604 CA PRO B 311 3.211 -5.185 1.582 1.00 41.17 C ANISOU 604 CA PRO B 311 5910 6167 3564 -760 435 85 C ATOM 605 C PRO B 311 3.646 -5.299 0.115 1.00 42.28 C ANISOU 605 C PRO B 311 6076 6452 3538 -830 489 46 C ATOM 606 O PRO B 311 3.755 -6.409 -0.412 1.00 49.59 O ANISOU 606 O PRO B 311 7008 7408 4425 -895 571 -106 O ATOM 607 CB PRO B 311 1.684 -5.301 1.649 1.00 38.16 C ANISOU 607 CB PRO B 311 5501 5860 3138 -772 336 61 C ATOM 608 CG PRO B 311 1.225 -4.154 2.455 1.00 46.15 C ANISOU 608 CG PRO B 311 6500 6819 4215 -693 243 208 C ATOM 609 CD PRO B 311 2.245 -3.089 2.354 1.00 44.46 C ANISOU 609 CD PRO B 311 6317 6564 4012 -660 270 333 C ATOM 610 N ASN B 312 3.876 -4.163 -0.535 1.00 35.98 N ANISOU 610 N ASN B 312 5296 5735 2642 -818 456 181 N ATOM 611 CA ASN B 312 4.221 -4.154 -1.958 1.00 46.22 C ANISOU 611 CA ASN B 312 6613 7192 3755 -882 499 165 C ATOM 612 C ASN B 312 5.709 -4.267 -2.231 1.00 46.42 C ANISOU 612 C ASN B 312 6664 7165 3810 -898 623 148 C ATOM 613 O ASN B 312 6.109 -4.760 -3.280 1.00 44.55 O ANISOU 613 O ASN B 312 6442 7035 3450 -964 696 65 O ATOM 614 CB ASN B 312 3.680 -2.895 -2.632 1.00 56.08 C ANISOU 614 CB ASN B 312 7869 8572 4867 -855 413 339 C ATOM 615 CG ASN B 312 2.171 -2.841 -2.626 1.00 66.43 C ANISOU 615 CG ASN B 312 9138 9994 6108 -840 293 355 C ATOM 616 OD1 ASN B 312 1.508 -3.864 -2.456 1.00 69.18 O ANISOU 616 OD1 ASN B 312 9454 10371 6460 -889 282 202 O ATOM 617 ND2 ASN B 312 1.617 -1.647 -2.812 1.00 68.51 N ANISOU 617 ND2 ASN B 312 9398 10319 6312 -772 215 543 N ATOM 618 N ASN B 313 6.539 -3.795 -1.305 1.00 40.20 N ANISOU 618 N ASN B 313 5871 6230 3174 -843 648 220 N ATOM 619 CA ASN B 313 7.970 -3.846 -1.548 1.00 37.92 C ANISOU 619 CA ASN B 313 5587 5912 2910 -857 763 210 C ATOM 620 C ASN B 313 8.792 -4.409 -0.394 1.00 38.61 C ANISOU 620 C ASN B 313 5634 5854 3182 -811 824 165 C ATOM 621 O ASN B 313 10.023 -4.446 -0.474 1.00 37.18 O ANISOU 621 O ASN B 313 5436 5656 3033 -812 918 163 O ATOM 622 CB ASN B 313 8.510 -2.480 -2.001 1.00 38.24 C ANISOU 622 CB ASN B 313 5652 5985 2894 -859 762 367 C ATOM 623 CG ASN B 313 8.691 -1.505 -0.854 1.00 43.92 C ANISOU 623 CG ASN B 313 6359 6572 3756 -809 724 477 C ATOM 624 OD1 ASN B 313 8.370 -1.802 0.297 1.00 39.61 O ANISOU 624 OD1 ASN B 313 5781 5928 3339 -768 683 445 O ATOM 625 ND2 ASN B 313 9.212 -0.324 -1.168 1.00 50.58 N ANISOU 625 ND2 ASN B 313 7230 7411 4576 -820 748 603 N ATOM 626 N GLY B 314 8.113 -4.838 0.671 1.00 38.54 N ANISOU 626 N GLY B 314 5603 5758 3284 -767 772 137 N ATOM 627 CA GLY B 314 8.762 -5.495 1.791 1.00 34.84 C ANISOU 627 CA GLY B 314 5089 5174 2976 -711 827 103 C ATOM 628 C GLY B 314 9.431 -4.580 2.810 1.00 41.29 C ANISOU 628 C GLY B 314 5865 5933 3892 -669 799 208 C ATOM 629 O GLY B 314 9.967 -5.046 3.812 1.00 40.38 O ANISOU 629 O GLY B 314 5695 5753 3893 -617 831 197 O ATOM 630 N GLU B 315 9.407 -3.276 2.573 1.00 37.31 N ANISOU 630 N GLU B 315 5383 5455 3339 -694 749 311 N ATOM 631 CA GLU B 315 10.160 -2.367 3.431 1.00 27.70 C ANISOU 631 CA GLU B 315 4128 4187 2208 -684 748 386 C ATOM 632 C GLU B 315 9.393 -1.954 4.674 1.00 33.86 C ANISOU 632 C GLU B 315 4892 4892 3080 -646 659 420 C ATOM 633 O GLU B 315 8.163 -1.853 4.663 1.00 38.00 O ANISOU 633 O GLU B 315 5450 5408 3581 -632 581 433 O ATOM 634 CB GLU B 315 10.641 -1.138 2.640 1.00 33.43 C ANISOU 634 CB GLU B 315 4892 4950 2861 -738 771 475 C ATOM 635 CG GLU B 315 11.855 -1.434 1.764 1.00 33.77 C ANISOU 635 CG GLU B 315 4923 5061 2847 -778 882 445 C ATOM 636 CD GLU B 315 12.196 -0.292 0.822 1.00 42.80 C ANISOU 636 CD GLU B 315 6118 6246 3900 -836 914 539 C ATOM 637 OE1 GLU B 315 11.568 0.781 0.962 1.00 44.11 O ANISOU 637 OE1 GLU B 315 6325 6368 4066 -836 859 637 O ATOM 638 OE2 GLU B 315 13.085 -0.473 -0.055 1.00 41.26 O ANISOU 638 OE2 GLU B 315 5921 6119 3636 -876 1005 519 O ATOM 639 N THR B 316 10.141 -1.736 5.749 1.00 27.59 N ANISOU 639 N THR B 316 4035 4064 2384 -633 674 429 N ATOM 640 CA THR B 316 9.604 -1.183 6.981 1.00 33.29 C ANISOU 640 CA THR B 316 4736 4724 3187 -612 604 457 C ATOM 641 C THR B 316 9.393 0.323 6.862 1.00 32.45 C ANISOU 641 C THR B 316 4676 4582 3070 -655 581 537 C ATOM 642 O THR B 316 10.303 1.061 6.501 1.00 40.05 O ANISOU 642 O THR B 316 5641 5558 4020 -711 642 568 O ATOM 643 CB THR B 316 10.569 -1.436 8.141 1.00 35.93 C ANISOU 643 CB THR B 316 4974 5069 3607 -594 633 435 C ATOM 644 OG1 THR B 316 10.763 -2.846 8.289 1.00 42.19 O ANISOU 644 OG1 THR B 316 5728 5878 4425 -531 671 383 O ATOM 645 CG2 THR B 316 10.023 -0.841 9.437 1.00 25.24 C ANISOU 645 CG2 THR B 316 3598 3670 2324 -585 564 451 C ATOM 646 N ILE B 317 8.186 0.775 7.180 1.00 28.20 N ANISOU 646 N ILE B 317 4174 3993 2547 -628 507 572 N ATOM 647 CA ILE B 317 7.849 2.182 7.066 1.00 32.47 C ANISOU 647 CA ILE B 317 4769 4476 3093 -649 501 660 C ATOM 648 C ILE B 317 8.066 2.887 8.399 1.00 34.89 C ANISOU 648 C ILE B 317 5040 4708 3507 -669 502 647 C ATOM 649 O ILE B 317 8.540 4.014 8.433 1.00 31.42 O ANISOU 649 O ILE B 317 4625 4216 3096 -725 556 685 O ATOM 650 CB ILE B 317 6.400 2.381 6.609 1.00 33.34 C ANISOU 650 CB ILE B 317 4930 4581 3155 -599 428 718 C ATOM 651 CG1 ILE B 317 6.228 1.897 5.166 1.00 30.76 C ANISOU 651 CG1 ILE B 317 4636 4360 2693 -602 431 733 C ATOM 652 CG2 ILE B 317 6.013 3.852 6.708 1.00 33.58 C ANISOU 652 CG2 ILE B 317 5013 4524 3223 -595 437 823 C ATOM 653 CD1 ILE B 317 4.774 1.731 4.746 1.00 29.91 C ANISOU 653 CD1 ILE B 317 4543 4305 2516 -554 346 762 C ATOM 654 N ALA B 318 7.711 2.213 9.490 1.00 30.90 N ANISOU 654 N ALA B 318 4481 4201 3059 -631 453 589 N ATOM 655 CA ALA B 318 7.877 2.774 10.829 1.00 29.61 C ANISOU 655 CA ALA B 318 4273 3996 2980 -655 449 561 C ATOM 656 C ALA B 318 8.054 1.663 11.842 1.00 26.23 C ANISOU 656 C ALA B 318 3758 3624 2584 -615 421 497 C ATOM 657 O ALA B 318 7.384 0.622 11.776 1.00 30.64 O ANISOU 657 O ALA B 318 4318 4193 3132 -552 384 483 O ATOM 658 CB ALA B 318 6.697 3.661 11.197 1.00 25.54 C ANISOU 658 CB ALA B 318 3811 3385 2507 -633 410 602 C ATOM 659 N THR B 319 8.972 1.861 12.775 1.00 29.37 N ANISOU 659 N THR B 319 4077 4067 3016 -655 447 460 N ATOM 660 CA THR B 319 9.196 0.847 13.798 1.00 34.46 C ANISOU 660 CA THR B 319 4629 4784 3682 -604 425 425 C ATOM 661 C THR B 319 8.345 1.154 15.025 1.00 34.46 C ANISOU 661 C THR B 319 4616 4749 3728 -591 370 408 C ATOM 662 O THR B 319 8.197 2.310 15.412 1.00 31.27 O ANISOU 662 O THR B 319 4234 4298 3351 -655 375 396 O ATOM 663 CB THR B 319 10.667 0.779 14.210 1.00 36.58 C ANISOU 663 CB THR B 319 4787 5169 3942 -642 475 401 C ATOM 664 OG1 THR B 319 11.063 2.059 14.708 1.00 39.69 O ANISOU 664 OG1 THR B 319 5164 5565 4352 -746 494 373 O ATOM 665 CG2 THR B 319 11.545 0.413 12.997 1.00 43.52 C ANISOU 665 CG2 THR B 319 5671 6086 4778 -648 541 415 C ATOM 666 N ALA B 320 7.803 0.113 15.645 1.00 25.51 N ANISOU 666 N ALA B 320 3451 3631 2609 -513 332 404 N ATOM 667 CA ALA B 320 6.855 0.309 16.730 1.00 32.25 C ANISOU 667 CA ALA B 320 4301 4453 3501 -495 280 391 C ATOM 668 C ALA B 320 7.531 0.099 18.081 1.00 34.36 C ANISOU 668 C ALA B 320 4456 4828 3771 -496 279 366 C ATOM 669 O ALA B 320 8.432 -0.734 18.206 1.00 32.55 O ANISOU 669 O ALA B 320 4148 4698 3522 -458 305 381 O ATOM 670 CB ALA B 320 5.689 -0.626 16.570 1.00 29.80 C ANISOU 670 CB ALA B 320 4031 4091 3201 -418 242 403 C ATOM 671 N LYS B 321 7.113 0.873 19.076 1.00 24.99 N ANISOU 671 N LYS B 321 3256 3634 2604 -537 255 332 N ATOM 672 CA LYS B 321 7.556 0.660 20.454 1.00 31.15 C ANISOU 672 CA LYS B 321 3925 4544 3368 -539 242 307 C ATOM 673 C LYS B 321 6.392 0.858 21.417 1.00 33.80 C ANISOU 673 C LYS B 321 4279 4832 3730 -523 199 286 C ATOM 674 O LYS B 321 5.731 1.897 21.382 1.00 24.53 O ANISOU 674 O LYS B 321 3173 3557 2590 -576 200 253 O ATOM 675 CB LYS B 321 8.691 1.607 20.823 1.00 40.04 C ANISOU 675 CB LYS B 321 4977 5770 4465 -654 277 250 C ATOM 676 CG LYS B 321 9.221 1.348 22.216 1.00 54.89 C ANISOU 676 CG LYS B 321 6721 7836 6300 -660 257 224 C ATOM 677 CD LYS B 321 10.395 2.226 22.571 1.00 66.56 C ANISOU 677 CD LYS B 321 8105 9449 7735 -793 293 150 C ATOM 678 CE LYS B 321 10.821 1.973 24.007 1.00 67.97 C ANISOU 678 CE LYS B 321 8133 9849 7844 -801 262 122 C ATOM 679 NZ LYS B 321 11.103 0.533 24.226 1.00 73.37 N ANISOU 679 NZ LYS B 321 8733 10649 8496 -648 238 228 N ATOM 680 N HIS B 322 6.148 -0.137 22.270 1.00 23.90 N ANISOU 680 N HIS B 322 2967 3648 2467 -445 174 312 N ATOM 681 CA HIS B 322 5.010 -0.093 23.191 1.00 30.87 C ANISOU 681 CA HIS B 322 3863 4494 3371 -424 138 297 C ATOM 682 C HIS B 322 5.372 0.538 24.523 1.00 36.68 C ANISOU 682 C HIS B 322 4514 5354 4070 -490 133 239 C ATOM 683 O HIS B 322 6.479 0.341 25.041 1.00 33.57 O ANISOU 683 O HIS B 322 4009 5130 3616 -507 142 238 O ATOM 684 CB HIS B 322 4.486 -1.495 23.474 1.00 32.27 C ANISOU 684 CB HIS B 322 4028 4676 3558 -312 126 356 C ATOM 685 CG HIS B 322 3.746 -2.096 22.329 1.00 27.44 C ANISOU 685 CG HIS B 322 3507 3934 2983 -267 130 381 C ATOM 686 ND1 HIS B 322 2.403 -1.876 22.120 1.00 25.98 N ANISOU 686 ND1 HIS B 322 3395 3641 2834 -264 99 366 N ATOM 687 CD2 HIS B 322 4.160 -2.906 21.324 1.00 25.07 C ANISOU 687 CD2 HIS B 322 3230 3613 2684 -230 165 410 C ATOM 688 CE1 HIS B 322 2.022 -2.517 21.028 1.00 27.43 C ANISOU 688 CE1 HIS B 322 3635 3759 3028 -236 107 381 C ATOM 689 NE2 HIS B 322 3.069 -3.146 20.525 1.00 26.60 N ANISOU 689 NE2 HIS B 322 3508 3697 2904 -220 151 401 N ATOM 690 N ASP B 323 4.423 1.280 25.083 1.00 31.26 N ANISOU 690 N ASP B 323 3870 4595 3413 -525 121 187 N ATOM 691 CA ASP B 323 4.515 1.714 26.480 1.00 28.25 C ANISOU 691 CA ASP B 323 3410 4334 2990 -583 117 120 C ATOM 692 C ASP B 323 3.129 1.503 27.062 1.00 31.01 C ANISOU 692 C ASP B 323 3801 4606 3374 -526 91 125 C ATOM 693 O ASP B 323 2.320 2.444 27.132 1.00 27.42 O ANISOU 693 O ASP B 323 3413 4035 2970 -569 105 69 O ATOM 694 CB ASP B 323 4.943 3.190 26.553 1.00 23.53 C ANISOU 694 CB ASP B 323 2824 3716 2399 -728 164 13 C ATOM 695 CG ASP B 323 5.155 3.685 27.988 1.00 41.93 C ANISOU 695 CG ASP B 323 5065 6197 4671 -817 171 -87 C ATOM 696 OD1 ASP B 323 4.815 2.967 28.952 1.00 43.00 O ANISOU 696 OD1 ASP B 323 5135 6444 4757 -757 132 -62 O ATOM 697 OD2 ASP B 323 5.676 4.812 28.150 1.00 52.87 O ANISOU 697 OD2 ASP B 323 6444 7591 6055 -958 225 -196 O ATOM 698 N THR B 324 2.840 0.258 27.438 1.00 22.21 N ANISOU 698 N THR B 324 2652 3545 2243 -425 66 199 N ATOM 699 CA THR B 324 1.497 -0.117 27.882 1.00 26.87 C ANISOU 699 CA THR B 324 3281 4058 2870 -368 47 213 C ATOM 700 C THR B 324 1.100 0.628 29.154 1.00 31.13 C ANISOU 700 C THR B 324 3785 4658 3385 -427 48 135 C ATOM 701 O THR B 324 -0.079 0.826 29.409 1.00 33.06 O ANISOU 701 O THR B 324 4077 4809 3676 -411 43 115 O ATOM 702 CB THR B 324 1.389 -1.625 28.188 1.00 33.35 C ANISOU 702 CB THR B 324 4064 4930 3677 -259 44 307 C ATOM 703 OG1 THR B 324 2.324 -1.958 29.227 1.00 30.73 O ANISOU 703 OG1 THR B 324 3615 4800 3261 -249 47 333 O ATOM 704 CG2 THR B 324 1.692 -2.442 26.950 1.00 31.84 C ANISOU 704 CG2 THR B 324 3915 4665 3518 -204 62 366 C ATOM 705 N ALA B 325 2.083 1.026 29.957 1.00 27.55 N ANISOU 705 N ALA B 325 3239 4378 2852 -501 57 84 N ATOM 706 CA ALA B 325 1.771 1.756 31.191 1.00 37.29 C ANISOU 706 CA ALA B 325 4433 5689 4046 -577 66 -14 C ATOM 707 C ALA B 325 1.136 3.100 30.856 1.00 37.51 C ANISOU 707 C ALA B 325 4557 5537 4156 -658 108 -113 C ATOM 708 O ALA B 325 0.366 3.645 31.650 1.00 41.01 O ANISOU 708 O ALA B 325 5012 5956 4613 -690 127 -187 O ATOM 709 CB ALA B 325 3.024 1.955 32.044 1.00 39.03 C ANISOU 709 CB ALA B 325 4522 6161 4148 -661 69 -65 C ATOM 710 N ASN B 326 1.456 3.622 29.672 1.00 24.49 N ANISOU 710 N ASN B 326 2977 3761 2565 -682 131 -107 N ATOM 711 CA ASN B 326 0.881 4.881 29.197 1.00 26.76 C ANISOU 711 CA ASN B 326 3366 3858 2945 -735 185 -168 C ATOM 712 C ASN B 326 -0.116 4.675 28.083 1.00 26.79 C ANISOU 712 C ASN B 326 3466 3682 3030 -631 166 -76 C ATOM 713 O ASN B 326 -0.455 5.623 27.365 1.00 25.02 O ANISOU 713 O ASN B 326 3326 3301 2880 -646 210 -80 O ATOM 714 CB ASN B 326 1.979 5.844 28.725 1.00 24.52 C ANISOU 714 CB ASN B 326 3090 3563 2663 -855 247 -232 C ATOM 715 CG ASN B 326 2.651 6.528 29.880 1.00 42.65 C ANISOU 715 CG ASN B 326 5307 6000 4898 -999 292 -374 C ATOM 716 OD1 ASN B 326 1.978 7.126 30.719 1.00 40.03 O ANISOU 716 OD1 ASN B 326 4989 5634 4585 -1042 329 -464 O ATOM 717 ND2 ASN B 326 3.979 6.426 29.958 1.00 48.75 N ANISOU 717 ND2 ASN B 326 5985 6949 5587 -1079 291 -404 N ATOM 718 N ASN B 327 -0.569 3.437 27.925 1.00 25.60 N ANISOU 718 N ASN B 327 3299 3563 2864 -529 108 10 N ATOM 719 CA ASN B 327 -1.583 3.126 26.919 1.00 22.24 C ANISOU 719 CA ASN B 327 2946 3008 2498 -442 82 83 C ATOM 720 C ASN B 327 -1.184 3.721 25.590 1.00 28.34 C ANISOU 720 C ASN B 327 3784 3686 3296 -458 103 114 C ATOM 721 O ASN B 327 -1.971 4.413 24.932 1.00 29.58 O ANISOU 721 O ASN B 327 4011 3717 3512 -432 116 138 O ATOM 722 CB ASN B 327 -2.943 3.652 27.373 1.00 24.23 C ANISOU 722 CB ASN B 327 3229 3168 2808 -415 89 57 C ATOM 723 CG ASN B 327 -3.563 2.786 28.467 1.00 31.29 C ANISOU 723 CG ASN B 327 4066 4147 3676 -377 61 53 C ATOM 724 OD1 ASN B 327 -4.739 2.448 28.415 1.00 36.98 O ANISOU 724 OD1 ASN B 327 4802 4813 4434 -314 40 80 O ATOM 725 ND2 ASN B 327 -2.764 2.406 29.440 1.00 30.45 N ANISOU 725 ND2 ASN B 327 3886 4188 3497 -413 63 26 N ATOM 726 N LEU B 328 0.053 3.427 25.197 1.00 26.27 N ANISOU 726 N LEU B 328 3493 3501 2987 -493 109 124 N ATOM 727 CA LEU B 328 0.712 4.101 24.087 1.00 22.80 C ANISOU 727 CA LEU B 328 3105 2997 2559 -535 146 141 C ATOM 728 C LEU B 328 1.496 3.134 23.198 1.00 23.59 C ANISOU 728 C LEU B 328 3189 3161 2613 -505 126 200 C ATOM 729 O LEU B 328 2.129 2.186 23.684 1.00 24.31 O ANISOU 729 O LEU B 328 3204 3375 2658 -487 110 206 O ATOM 730 CB LEU B 328 1.670 5.159 24.661 1.00 27.17 C ANISOU 730 CB LEU B 328 3634 3581 3107 -659 211 52 C ATOM 731 CG LEU B 328 2.709 5.835 23.759 1.00 35.13 C ANISOU 731 CG LEU B 328 4673 4559 4117 -734 267 51 C ATOM 732 CD1 LEU B 328 2.063 6.611 22.619 1.00 35.71 C ANISOU 732 CD1 LEU B 328 4862 4451 4257 -702 303 115 C ATOM 733 CD2 LEU B 328 3.624 6.765 24.591 1.00 37.27 C ANISOU 733 CD2 LEU B 328 4896 4889 4377 -881 337 -69 C ATOM 734 N ILE B 329 1.429 3.377 21.896 1.00 25.11 N ANISOU 734 N ILE B 329 3451 3271 2818 -491 135 250 N ATOM 735 CA ILE B 329 2.313 2.750 20.922 1.00 22.51 C ANISOU 735 CA ILE B 329 3118 2989 2447 -486 140 289 C ATOM 736 C ILE B 329 2.898 3.908 20.129 1.00 26.00 C ANISOU 736 C ILE B 329 3613 3367 2899 -555 196 293 C ATOM 737 O ILE B 329 2.149 4.759 19.624 1.00 25.76 O ANISOU 737 O ILE B 329 3659 3220 2908 -544 212 325 O ATOM 738 CB ILE B 329 1.548 1.870 19.919 1.00 21.97 C ANISOU 738 CB ILE B 329 3091 2889 2368 -408 103 346 C ATOM 739 CG1 ILE B 329 0.547 0.960 20.632 1.00 24.57 C ANISOU 739 CG1 ILE B 329 3394 3230 2712 -346 61 341 C ATOM 740 CG2 ILE B 329 2.521 1.046 19.074 1.00 23.80 C ANISOU 740 CG2 ILE B 329 3309 3179 2554 -405 122 366 C ATOM 741 CD1 ILE B 329 -0.463 0.347 19.683 1.00 29.48 C ANISOU 741 CD1 ILE B 329 4058 3814 3328 -296 29 372 C ATOM 742 N THR B 330 4.223 3.945 20.034 1.00 25.61 N ANISOU 742 N THR B 330 3519 3395 2816 -620 234 270 N ATOM 743 CA THR B 330 4.918 4.991 19.295 1.00 22.08 C ANISOU 743 CA THR B 330 3119 2893 2379 -701 303 271 C ATOM 744 C THR B 330 5.554 4.396 18.049 1.00 29.62 C ANISOU 744 C THR B 330 4086 3882 3287 -679 309 328 C ATOM 745 O THR B 330 6.205 3.353 18.112 1.00 30.74 O ANISOU 745 O THR B 330 4158 4135 3387 -653 292 325 O ATOM 746 CB THR B 330 6.019 5.639 20.165 1.00 26.98 C ANISOU 746 CB THR B 330 3668 3589 2994 -824 357 180 C ATOM 747 OG1 THR B 330 5.433 6.148 21.372 1.00 26.44 O ANISOU 747 OG1 THR B 330 3585 3504 2958 -854 358 109 O ATOM 748 CG2 THR B 330 6.731 6.764 19.412 1.00 32.12 C ANISOU 748 CG2 THR B 330 4374 4165 3667 -924 449 173 C ATOM 749 N TYR B 331 5.345 5.047 16.913 1.00 25.83 N ANISOU 749 N TYR B 331 3694 3308 2811 -682 341 386 N ATOM 750 CA TYR B 331 5.896 4.567 15.656 1.00 28.71 C ANISOU 750 CA TYR B 331 4079 3709 3121 -669 353 435 C ATOM 751 C TYR B 331 6.888 5.586 15.114 1.00 29.01 C ANISOU 751 C TYR B 331 4144 3718 3161 -766 442 440 C ATOM 752 O TYR B 331 6.527 6.734 14.872 1.00 32.50 O ANISOU 752 O TYR B 331 4662 4041 3645 -793 492 472 O ATOM 753 CB TYR B 331 4.789 4.369 14.637 1.00 20.42 C ANISOU 753 CB TYR B 331 3103 2608 2047 -590 313 511 C ATOM 754 CG TYR B 331 3.794 3.318 15.037 1.00 28.88 C ANISOU 754 CG TYR B 331 4148 3708 3116 -511 237 498 C ATOM 755 CD1 TYR B 331 3.901 2.014 14.559 1.00 27.84 C ANISOU 755 CD1 TYR B 331 3992 3648 2936 -474 215 489 C ATOM 756 CD2 TYR B 331 2.738 3.624 15.900 1.00 32.04 C ANISOU 756 CD2 TYR B 331 4550 4056 3567 -479 201 489 C ATOM 757 CE1 TYR B 331 2.978 1.041 14.928 1.00 31.92 C ANISOU 757 CE1 TYR B 331 4491 4178 3461 -416 163 470 C ATOM 758 CE2 TYR B 331 1.812 2.660 16.267 1.00 39.47 C ANISOU 758 CE2 TYR B 331 5465 5023 4508 -416 140 475 C ATOM 759 CZ TYR B 331 1.939 1.375 15.780 1.00 35.39 C ANISOU 759 CZ TYR B 331 4928 4572 3946 -390 123 465 C ATOM 760 OH TYR B 331 1.020 0.430 16.146 1.00 37.00 O ANISOU 760 OH TYR B 331 5112 4787 4159 -342 81 445 O ATOM 761 N THR B 332 8.127 5.160 14.911 1.00 29.05 N ANISOU 761 N THR B 332 4085 3826 3125 -812 473 413 N ATOM 762 CA THR B 332 9.170 6.050 14.406 1.00 32.19 C ANISOU 762 CA THR B 332 4496 4213 3522 -918 565 408 C ATOM 763 C THR B 332 9.478 5.733 12.938 1.00 31.06 C ANISOU 763 C THR B 332 4401 4082 3320 -893 588 479 C ATOM 764 O THR B 332 9.906 4.630 12.616 1.00 29.99 O ANISOU 764 O THR B 332 4214 4047 3134 -850 565 474 O ATOM 765 CB THR B 332 10.444 5.912 15.259 1.00 34.49 C ANISOU 765 CB THR B 332 4660 4642 3802 -1004 591 319 C ATOM 766 OG1 THR B 332 10.121 6.171 16.631 1.00 34.86 O ANISOU 766 OG1 THR B 332 4656 4704 3883 -1031 566 246 O ATOM 767 CG2 THR B 332 11.528 6.880 14.790 1.00 40.17 C ANISOU 767 CG2 THR B 332 5384 5355 4526 -1136 697 296 C ATOM 768 N PHE B 333 9.258 6.700 12.050 1.00 28.60 N ANISOU 768 N PHE B 333 4188 3665 3012 -916 645 551 N ATOM 769 CA PHE B 333 9.504 6.487 10.621 1.00 32.70 C ANISOU 769 CA PHE B 333 4757 4210 3458 -897 670 625 C ATOM 770 C PHE B 333 10.966 6.216 10.278 1.00 35.37 C ANISOU 770 C PHE B 333 5032 4649 3759 -972 734 585 C ATOM 771 O PHE B 333 11.875 6.830 10.832 1.00 34.54 O ANISOU 771 O PHE B 333 4877 4555 3691 -1076 798 528 O ATOM 772 CB PHE B 333 9.005 7.673 9.796 1.00 36.29 C ANISOU 772 CB PHE B 333 5327 4539 3920 -899 728 733 C ATOM 773 CG PHE B 333 7.531 7.884 9.896 1.00 36.35 C ANISOU 773 CG PHE B 333 5391 4470 3951 -800 667 797 C ATOM 774 CD1 PHE B 333 6.661 7.102 9.159 1.00 31.97 C ANISOU 774 CD1 PHE B 333 4850 3982 3317 -703 583 852 C ATOM 775 CD2 PHE B 333 7.013 8.850 10.740 1.00 34.48 C ANISOU 775 CD2 PHE B 333 5185 4104 3813 -811 698 792 C ATOM 776 CE1 PHE B 333 5.297 7.291 9.251 1.00 35.07 C ANISOU 776 CE1 PHE B 333 5274 4328 3723 -613 523 911 C ATOM 777 CE2 PHE B 333 5.652 9.037 10.841 1.00 32.35 C ANISOU 777 CE2 PHE B 333 4955 3771 3567 -709 646 856 C ATOM 778 CZ PHE B 333 4.792 8.260 10.094 1.00 32.06 C ANISOU 778 CZ PHE B 333 4920 3817 3446 -608 553 921 C ATOM 779 N THR B 334 11.163 5.284 9.355 1.00 36.93 N ANISOU 779 N THR B 334 5225 4927 3880 -924 720 606 N ATOM 780 CA THR B 334 12.468 4.961 8.798 1.00 38.47 C ANISOU 780 CA THR B 334 5366 5218 4031 -976 788 583 C ATOM 781 C THR B 334 12.732 5.916 7.643 1.00 40.67 C ANISOU 781 C THR B 334 5735 5444 4274 -1035 873 660 C ATOM 782 O THR B 334 11.911 6.789 7.377 1.00 44.35 O ANISOU 782 O THR B 334 6297 5800 4756 -1023 878 738 O ATOM 783 CB THR B 334 12.463 3.529 8.246 1.00 34.82 C ANISOU 783 CB THR B 334 4877 4846 3508 -894 756 568 C ATOM 784 OG1 THR B 334 11.582 3.468 7.121 1.00 36.22 O ANISOU 784 OG1 THR B 334 5152 4994 3616 -850 734 632 O ATOM 785 CG2 THR B 334 11.982 2.540 9.320 1.00 25.11 C ANISOU 785 CG2 THR B 334 3581 3641 2319 -816 680 517 C ATOM 786 N ASP B 335 13.854 5.762 6.939 1.00 37.68 N ANISOU 786 N ASP B 335 5324 5144 3848 -1089 947 651 N ATOM 787 CA ASP B 335 14.099 6.644 5.794 1.00 38.10 C ANISOU 787 CA ASP B 335 5466 5151 3857 -1143 1036 737 C ATOM 788 C ASP B 335 13.133 6.373 4.627 1.00 44.37 C ANISOU 788 C ASP B 335 6356 5947 4557 -1056 996 832 C ATOM 789 O ASP B 335 13.154 7.071 3.620 1.00 44.00 O ANISOU 789 O ASP B 335 6389 5873 4455 -1078 1059 931 O ATOM 790 CB ASP B 335 15.563 6.599 5.339 1.00 40.73 C ANISOU 790 CB ASP B 335 5737 5577 4162 -1233 1135 701 C ATOM 791 CG ASP B 335 15.999 5.214 4.874 1.00 52.97 C ANISOU 791 CG ASP B 335 7221 7263 5643 -1172 1114 658 C ATOM 792 OD1 ASP B 335 15.131 4.354 4.620 1.00 48.04 O ANISOU 792 OD1 ASP B 335 6625 6649 4977 -1073 1039 664 O ATOM 793 OD2 ASP B 335 17.221 4.988 4.753 1.00 63.13 O ANISOU 793 OD2 ASP B 335 8423 8645 6920 -1226 1185 612 O ATOM 794 N TYR B 336 12.274 5.366 4.775 1.00 43.15 N ANISOU 794 N TYR B 336 6185 5832 4376 -963 895 804 N ATOM 795 CA TYR B 336 11.232 5.105 3.789 1.00 39.01 C ANISOU 795 CA TYR B 336 5733 5336 3754 -892 843 876 C ATOM 796 C TYR B 336 10.532 6.402 3.402 1.00 36.33 C ANISOU 796 C TYR B 336 5487 4902 3413 -880 862 1013 C ATOM 797 O TYR B 336 10.213 6.630 2.237 1.00 35.69 O ANISOU 797 O TYR B 336 5469 4867 3226 -856 875 1115 O ATOM 798 CB TYR B 336 10.209 4.138 4.371 1.00 44.36 C ANISOU 798 CB TYR B 336 6380 6031 4445 -812 734 819 C ATOM 799 CG TYR B 336 9.089 3.741 3.428 1.00 41.78 C ANISOU 799 CG TYR B 336 6101 5766 4007 -752 671 865 C ATOM 800 CD1 TYR B 336 9.093 2.504 2.796 1.00 32.93 C ANISOU 800 CD1 TYR B 336 4958 4753 2801 -743 659 789 C ATOM 801 CD2 TYR B 336 8.019 4.591 3.190 1.00 33.59 C ANISOU 801 CD2 TYR B 336 5122 4689 2950 -706 630 979 C ATOM 802 CE1 TYR B 336 8.060 2.122 1.958 1.00 37.22 C ANISOU 802 CE1 TYR B 336 5531 5380 3230 -711 601 807 C ATOM 803 CE2 TYR B 336 6.982 4.218 2.357 1.00 35.53 C ANISOU 803 CE2 TYR B 336 5388 5032 3079 -654 563 1019 C ATOM 804 CZ TYR B 336 7.006 2.988 1.739 1.00 39.67 C ANISOU 804 CZ TYR B 336 5885 5682 3508 -667 545 925 C ATOM 805 OH TYR B 336 5.975 2.631 0.898 1.00 37.60 O ANISOU 805 OH TYR B 336 5631 5542 3114 -638 479 947 O ATOM 806 N VAL B 337 10.302 7.261 4.388 1.00 32.88 N ANISOU 806 N VAL B 337 5061 4339 3094 -893 872 1021 N ATOM 807 CA VAL B 337 9.558 8.491 4.157 1.00 37.44 C ANISOU 807 CA VAL B 337 5731 4797 3699 -862 905 1156 C ATOM 808 C VAL B 337 10.409 9.587 3.517 1.00 43.52 C ANISOU 808 C VAL B 337 6564 5496 4475 -941 1049 1239 C ATOM 809 O VAL B 337 9.886 10.620 3.106 1.00 43.29 O ANISOU 809 O VAL B 337 6625 5362 4461 -906 1104 1381 O ATOM 810 CB VAL B 337 8.937 9.029 5.456 1.00 41.59 C ANISOU 810 CB VAL B 337 6252 5192 4358 -847 884 1124 C ATOM 811 CG1 VAL B 337 8.057 7.961 6.096 1.00 39.90 C ANISOU 811 CG1 VAL B 337 5978 5044 4138 -770 750 1051 C ATOM 812 CG2 VAL B 337 10.032 9.493 6.413 1.00 26.70 C ANISOU 812 CG2 VAL B 337 4324 3246 2575 -971 967 1016 C ATOM 813 N ASP B 338 11.717 9.365 3.448 1.00 42.64 N ANISOU 813 N ASP B 338 6403 5439 4357 -1044 1118 1158 N ATOM 814 CA ASP B 338 12.607 10.266 2.723 1.00 42.90 C ANISOU 814 CA ASP B 338 6490 5428 4382 -1133 1261 1227 C ATOM 815 C ASP B 338 12.683 9.807 1.276 1.00 47.92 C ANISOU 815 C ASP B 338 7156 6193 4859 -1097 1263 1311 C ATOM 816 O ASP B 338 12.846 10.608 0.364 1.00 54.53 O ANISOU 816 O ASP B 338 8074 6995 5650 -1114 1359 1444 O ATOM 817 CB ASP B 338 14.012 10.227 3.325 1.00 47.26 C ANISOU 817 CB ASP B 338 6955 6008 4994 -1270 1336 1091 C ATOM 818 CG ASP B 338 14.048 10.668 4.786 1.00 52.31 C ANISOU 818 CG ASP B 338 7548 6558 5770 -1329 1337 986 C ATOM 819 OD1 ASP B 338 13.279 11.575 5.178 1.00 47.80 O ANISOU 819 OD1 ASP B 338 7053 5829 5280 -1312 1362 1040 O ATOM 820 OD2 ASP B 338 14.871 10.111 5.538 1.00 54.29 O ANISOU 820 OD2 ASP B 338 7681 6906 6042 -1393 1321 851 O ATOM 821 N ARG B 339 12.566 8.498 1.079 1.00 45.44 N ANISOU 821 N ARG B 339 6779 6027 4460 -1052 1167 1230 N ATOM 822 CA ARG B 339 12.771 7.894 -0.225 1.00 44.11 C ANISOU 822 CA ARG B 339 6623 6005 4134 -1041 1176 1261 C ATOM 823 C ARG B 339 11.488 7.758 -1.055 1.00 46.90 C ANISOU 823 C ARG B 339 7029 6428 4361 -938 1093 1370 C ATOM 824 O ARG B 339 11.546 7.572 -2.271 1.00 45.67 O ANISOU 824 O ARG B 339 6902 6397 4053 -935 1113 1430 O ATOM 825 CB ARG B 339 13.482 6.554 -0.062 1.00 43.80 C ANISOU 825 CB ARG B 339 6486 6083 4074 -1061 1152 1102 C ATOM 826 CG ARG B 339 14.878 6.702 0.530 1.00 48.89 C ANISOU 826 CG ARG B 339 7057 6712 4807 -1160 1243 1016 C ATOM 827 CD ARG B 339 15.478 5.358 0.882 1.00 58.77 C ANISOU 827 CD ARG B 339 8199 8069 6060 -1146 1216 877 C ATOM 828 NE ARG B 339 14.748 4.303 0.205 1.00 66.72 N ANISOU 828 NE ARG B 339 9226 9159 6966 -1069 1151 858 N ATOM 829 CZ ARG B 339 13.970 3.416 0.813 1.00 59.11 C ANISOU 829 CZ ARG B 339 8234 8197 6031 -996 1056 792 C ATOM 830 NH1 ARG B 339 13.337 2.509 0.083 1.00 41.15 N ANISOU 830 NH1 ARG B 339 5981 5999 3656 -952 1017 763 N ATOM 831 NH2 ARG B 339 13.833 3.426 2.136 1.00 63.89 N ANISOU 831 NH2 ARG B 339 8786 8733 6757 -978 1007 750 N ATOM 832 N PHE B 340 10.333 7.874 -0.405 1.00 41.41 N ANISOU 832 N PHE B 340 6341 5675 3720 -858 1001 1395 N ATOM 833 CA PHE B 340 9.066 7.882 -1.126 1.00 45.41 C ANISOU 833 CA PHE B 340 6882 6263 4110 -759 920 1511 C ATOM 834 C PHE B 340 8.178 9.036 -0.696 1.00 45.73 C ANISOU 834 C PHE B 340 6976 6163 4237 -684 921 1654 C ATOM 835 O PHE B 340 8.212 9.465 0.464 1.00 40.14 O ANISOU 835 O PHE B 340 6263 5297 3691 -700 938 1604 O ATOM 836 CB PHE B 340 8.305 6.564 -0.938 1.00 48.96 C ANISOU 836 CB PHE B 340 7265 6830 4507 -718 792 1388 C ATOM 837 CG PHE B 340 9.046 5.355 -1.438 1.00 49.18 C ANISOU 837 CG PHE B 340 7248 6988 4452 -777 805 1249 C ATOM 838 CD1 PHE B 340 9.299 5.189 -2.793 1.00 48.21 C ANISOU 838 CD1 PHE B 340 7149 7012 4155 -801 843 1290 C ATOM 839 CD2 PHE B 340 9.477 4.372 -0.549 1.00 41.24 C ANISOU 839 CD2 PHE B 340 6174 5957 3537 -800 790 1082 C ATOM 840 CE1 PHE B 340 9.980 4.070 -3.259 1.00 47.10 C ANISOU 840 CE1 PHE B 340 6972 6979 3946 -855 874 1150 C ATOM 841 CE2 PHE B 340 10.166 3.257 -1.009 1.00 36.16 C ANISOU 841 CE2 PHE B 340 5493 5413 2834 -839 824 962 C ATOM 842 CZ PHE B 340 10.410 3.103 -2.357 1.00 41.94 C ANISOU 842 CZ PHE B 340 6254 6276 3404 -870 870 986 C ATOM 843 N ASN B 341 7.393 9.535 -1.648 1.00 50.38 N ANISOU 843 N ASN B 341 7612 6818 4710 -599 909 1835 N ATOM 844 CA ASN B 341 6.297 10.460 -1.370 1.00 50.50 C ANISOU 844 CA ASN B 341 7667 6734 4786 -488 893 1990 C ATOM 845 C ASN B 341 4.970 9.708 -1.347 1.00 52.97 C ANISOU 845 C ASN B 341 7916 7191 5019 -393 736 1973 C ATOM 846 O ASN B 341 4.919 8.528 -1.710 1.00 49.46 O ANISOU 846 O ASN B 341 7412 6923 4457 -425 653 1851 O ATOM 847 CB ASN B 341 6.235 11.564 -2.429 1.00 48.94 C ANISOU 847 CB ASN B 341 7554 6527 4513 -431 990 2236 C ATOM 848 CG ASN B 341 7.319 12.601 -2.250 1.00 54.32 C ANISOU 848 CG ASN B 341 8313 7004 5323 -516 1170 2276 C ATOM 849 OD1 ASN B 341 7.683 12.948 -1.125 1.00 57.26 O ANISOU 849 OD1 ASN B 341 8688 7190 5877 -578 1222 2171 O ATOM 850 ND2 ASN B 341 7.851 13.100 -3.361 1.00 57.81 N ANISOU 850 ND2 ASN B 341 8815 7488 5663 -531 1272 2420 N ATOM 851 N SER B 342 3.902 10.394 -0.941 1.00 45.23 N ANISOU 851 N SER B 342 6948 6133 4105 -282 707 2090 N ATOM 852 CA SER B 342 2.570 9.790 -0.909 1.00 53.82 C ANISOU 852 CA SER B 342 7966 7365 5120 -191 561 2087 C ATOM 853 C SER B 342 2.554 8.543 -0.033 1.00 50.34 C ANISOU 853 C SER B 342 7450 6949 4727 -257 473 1847 C ATOM 854 O SER B 342 1.928 7.539 -0.364 1.00 48.22 O ANISOU 854 O SER B 342 7117 6864 4342 -252 367 1770 O ATOM 855 CB SER B 342 2.098 9.450 -2.325 1.00 56.68 C ANISOU 855 CB SER B 342 8301 7996 5238 -149 500 2190 C ATOM 856 OG SER B 342 1.904 10.635 -3.075 1.00 65.13 O ANISOU 856 OG SER B 342 9432 9054 6261 -53 574 2450 O ATOM 857 N VAL B 343 3.248 8.625 1.093 1.00 46.91 N ANISOU 857 N VAL B 343 7024 6336 4464 -322 525 1730 N ATOM 858 CA VAL B 343 3.359 7.499 2.001 1.00 45.48 C ANISOU 858 CA VAL B 343 6777 6164 4340 -376 461 1525 C ATOM 859 C VAL B 343 2.000 7.117 2.595 1.00 42.37 C ANISOU 859 C VAL B 343 6329 5801 3967 -297 348 1502 C ATOM 860 O VAL B 343 1.254 7.972 3.061 1.00 46.30 O ANISOU 860 O VAL B 343 6844 6201 4545 -218 348 1601 O ATOM 861 CB VAL B 343 4.369 7.808 3.119 1.00 40.50 C ANISOU 861 CB VAL B 343 6153 5359 3875 -454 541 1429 C ATOM 862 CG1 VAL B 343 4.341 6.717 4.211 1.00 35.34 C ANISOU 862 CG1 VAL B 343 5425 4714 3287 -480 472 1249 C ATOM 863 CG2 VAL B 343 5.757 7.971 2.528 1.00 35.86 C ANISOU 863 CG2 VAL B 343 5593 4774 3256 -547 647 1422 C ATOM 864 N GLN B 344 1.688 5.826 2.557 1.00 37.38 N ANISOU 864 N GLN B 344 5635 5302 3267 -323 265 1369 N ATOM 865 CA GLN B 344 0.476 5.296 3.170 1.00 39.08 C ANISOU 865 CA GLN B 344 5791 5553 3504 -272 164 1317 C ATOM 866 C GLN B 344 0.803 4.023 3.921 1.00 42.09 C ANISOU 866 C GLN B 344 6126 5927 3938 -339 144 1122 C ATOM 867 O GLN B 344 1.735 3.305 3.558 1.00 47.87 O ANISOU 867 O GLN B 344 6859 6698 4630 -410 186 1032 O ATOM 868 CB GLN B 344 -0.597 5.009 2.126 1.00 48.04 C ANISOU 868 CB GLN B 344 6886 6900 4466 -224 80 1381 C ATOM 869 CG GLN B 344 -1.054 6.248 1.368 1.00 64.75 C ANISOU 869 CG GLN B 344 9035 9050 6519 -127 95 1609 C ATOM 870 CD GLN B 344 -2.382 6.045 0.661 1.00 74.52 C ANISOU 870 CD GLN B 344 10200 10513 7603 -54 -12 1682 C ATOM 871 OE1 GLN B 344 -3.272 5.355 1.169 1.00 77.35 O ANISOU 871 OE1 GLN B 344 10485 10931 7972 -50 -97 1584 O ATOM 872 NE2 GLN B 344 -2.528 6.658 -0.511 1.00 73.31 N ANISOU 872 NE2 GLN B 344 10057 10499 7297 2 -5 1860 N ATOM 873 N MET B 345 0.028 3.758 4.968 1.00 35.11 N ANISOU 873 N MET B 345 5204 4990 3147 -307 90 1066 N ATOM 874 CA MET B 345 0.242 2.615 5.840 1.00 40.57 C ANISOU 874 CA MET B 345 5853 5654 3905 -351 79 906 C ATOM 875 C MET B 345 -1.098 2.014 6.191 1.00 44.88 C ANISOU 875 C MET B 345 6347 6259 4447 -317 -7 862 C ATOM 876 O MET B 345 -2.100 2.731 6.282 1.00 42.25 O ANISOU 876 O MET B 345 6003 5932 4120 -247 -55 955 O ATOM 877 CB MET B 345 0.907 3.055 7.146 1.00 38.49 C ANISOU 877 CB MET B 345 5596 5232 3796 -362 125 878 C ATOM 878 CG MET B 345 2.147 3.885 6.958 1.00 42.29 C ANISOU 878 CG MET B 345 6121 5646 4301 -405 216 924 C ATOM 879 SD MET B 345 2.850 4.401 8.522 1.00 41.69 S ANISOU 879 SD MET B 345 6031 5425 4385 -439 265 867 S ATOM 880 CE MET B 345 1.653 5.625 9.056 1.00 38.95 C ANISOU 880 CE MET B 345 5715 4968 4115 -368 249 961 C ATOM 881 N GLY B 346 -1.112 0.706 6.418 1.00 34.72 N ANISOU 881 N GLY B 346 5026 5007 3160 -363 -16 723 N ATOM 882 CA GLY B 346 -2.317 0.048 6.886 1.00 34.85 C ANISOU 882 CA GLY B 346 4989 5062 3189 -349 -82 660 C ATOM 883 C GLY B 346 -2.045 -0.702 8.177 1.00 40.03 C ANISOU 883 C GLY B 346 5629 5606 3975 -362 -56 560 C ATOM 884 O GLY B 346 -0.960 -1.268 8.355 1.00 39.91 O ANISOU 884 O GLY B 346 5627 5544 3993 -397 10 500 O ATOM 885 N ILE B 347 -3.014 -0.692 9.090 1.00 32.34 N ANISOU 885 N ILE B 347 4619 4597 3070 -326 -103 552 N ATOM 886 CA ILE B 347 -2.936 -1.534 10.276 1.00 33.37 C ANISOU 886 CA ILE B 347 4728 4648 3304 -335 -82 463 C ATOM 887 C ILE B 347 -4.185 -2.380 10.406 1.00 37.99 C ANISOU 887 C ILE B 347 5267 5289 3878 -346 -125 393 C ATOM 888 O ILE B 347 -5.296 -1.956 10.054 1.00 36.05 O ANISOU 888 O ILE B 347 4989 5125 3581 -323 -192 433 O ATOM 889 CB ILE B 347 -2.706 -0.751 11.583 1.00 39.99 C ANISOU 889 CB ILE B 347 5565 5371 4257 -296 -74 503 C ATOM 890 CG1 ILE B 347 -3.918 0.104 11.916 1.00 41.66 C ANISOU 890 CG1 ILE B 347 5760 5576 4493 -240 -132 566 C ATOM 891 CG2 ILE B 347 -1.436 0.084 11.509 1.00 44.15 C ANISOU 891 CG2 ILE B 347 6130 5847 4799 -308 -20 553 C ATOM 892 CD1 ILE B 347 -3.810 0.793 13.252 1.00 46.82 C ANISOU 892 CD1 ILE B 347 6413 6119 5259 -214 -115 578 C ATOM 893 N ASN B 348 -3.982 -3.586 10.914 1.00 26.64 N ANISOU 893 N ASN B 348 3822 3809 2491 -380 -77 292 N ATOM 894 CA ASN B 348 -5.054 -4.537 11.121 1.00 26.56 C ANISOU 894 CA ASN B 348 3774 3829 2489 -411 -90 206 C ATOM 895 C ASN B 348 -4.729 -5.294 12.409 1.00 34.38 C ANISOU 895 C ASN B 348 4764 4700 3600 -397 -32 165 C ATOM 896 O ASN B 348 -3.974 -6.266 12.374 1.00 38.03 O ANISOU 896 O ASN B 348 5246 5117 4087 -420 51 108 O ATOM 897 CB ASN B 348 -5.111 -5.472 9.902 1.00 37.20 C ANISOU 897 CB ASN B 348 5127 5273 3736 -493 -59 107 C ATOM 898 CG ASN B 348 -6.267 -6.440 9.952 1.00 45.97 C ANISOU 898 CG ASN B 348 6195 6431 4841 -554 -62 -3 C ATOM 899 OD1 ASN B 348 -7.025 -6.477 10.917 1.00 43.87 O ANISOU 899 OD1 ASN B 348 5896 6121 4651 -529 -87 0 O ATOM 900 ND2 ASN B 348 -6.407 -7.241 8.900 1.00 50.56 N ANISOU 900 ND2 ASN B 348 6776 7107 5330 -647 -29 -113 N ATOM 901 N TYR B 349 -5.266 -4.823 13.546 1.00 28.75 N ANISOU 901 N TYR B 349 4024 3939 2960 -349 -69 205 N ATOM 902 CA TYR B 349 -4.901 -5.365 14.858 1.00 26.06 C ANISOU 902 CA TYR B 349 3677 3507 2720 -324 -20 194 C ATOM 903 C TYR B 349 -6.085 -5.954 15.614 1.00 29.66 C ANISOU 903 C TYR B 349 4096 3949 3223 -328 -30 151 C ATOM 904 O TYR B 349 -7.200 -5.427 15.569 1.00 29.29 O ANISOU 904 O TYR B 349 4018 3954 3158 -324 -97 161 O ATOM 905 CB TYR B 349 -4.330 -4.273 15.779 1.00 21.93 C ANISOU 905 CB TYR B 349 3150 2940 2241 -274 -38 270 C ATOM 906 CG TYR B 349 -3.068 -3.561 15.344 1.00 28.31 C ANISOU 906 CG TYR B 349 3985 3749 3023 -275 -17 315 C ATOM 907 CD1 TYR B 349 -2.176 -4.132 14.444 1.00 38.91 C ANISOU 907 CD1 TYR B 349 5350 5111 4321 -303 34 292 C ATOM 908 CD2 TYR B 349 -2.758 -2.309 15.871 1.00 29.43 C ANISOU 908 CD2 TYR B 349 4130 3864 3189 -257 -35 370 C ATOM 909 CE1 TYR B 349 -1.006 -3.455 14.068 1.00 30.68 C ANISOU 909 CE1 TYR B 349 4326 4075 3256 -309 58 333 C ATOM 910 CE2 TYR B 349 -1.609 -1.639 15.512 1.00 29.98 C ANISOU 910 CE2 TYR B 349 4220 3931 3240 -274 -5 402 C ATOM 911 CZ TYR B 349 -0.736 -2.208 14.616 1.00 31.15 C ANISOU 911 CZ TYR B 349 4384 4110 3341 -298 37 388 C ATOM 912 OH TYR B 349 0.414 -1.511 14.287 1.00 34.29 O ANISOU 912 OH TYR B 349 4796 4511 3722 -321 72 419 O ATOM 913 N SER B 350 -5.824 -7.015 16.362 1.00 26.72 N ANISOU 913 N SER B 350 3726 3507 2917 -327 45 118 N ATOM 914 CA SER B 350 -6.776 -7.503 17.356 1.00 36.59 C ANISOU 914 CA SER B 350 4947 4727 4230 -323 51 96 C ATOM 915 C SER B 350 -6.363 -6.945 18.723 1.00 31.82 C ANISOU 915 C SER B 350 4326 4084 3679 -257 43 168 C ATOM 916 O SER B 350 -5.278 -7.262 19.214 1.00 31.51 O ANISOU 916 O SER B 350 4295 4013 3666 -224 98 200 O ATOM 917 CB SER B 350 -6.792 -9.042 17.381 1.00 30.45 C ANISOU 917 CB SER B 350 4187 3886 3497 -361 159 25 C ATOM 918 OG SER B 350 -7.385 -9.563 16.197 1.00 35.56 O ANISOU 918 OG SER B 350 4840 4582 4089 -448 170 -73 O ATOM 919 N ILE B 351 -7.198 -6.092 19.318 1.00 24.33 N ANISOU 919 N ILE B 351 3347 3155 2741 -237 -21 190 N ATOM 920 CA ILE B 351 -6.901 -5.571 20.655 1.00 20.63 C ANISOU 920 CA ILE B 351 2860 2665 2314 -192 -23 234 C ATOM 921 C ILE B 351 -7.988 -6.019 21.646 1.00 27.01 C ANISOU 921 C ILE B 351 3634 3460 3168 -187 -16 215 C ATOM 922 O ILE B 351 -8.983 -6.635 21.248 1.00 29.85 O ANISOU 922 O ILE B 351 3983 3828 3532 -222 -14 167 O ATOM 923 CB ILE B 351 -6.663 -4.031 20.672 1.00 33.02 C ANISOU 923 CB ILE B 351 4432 4246 3866 -174 -75 275 C ATOM 924 CG1 ILE B 351 -7.929 -3.262 20.273 1.00 29.56 C ANISOU 924 CG1 ILE B 351 3980 3829 3422 -166 -135 278 C ATOM 925 CG2 ILE B 351 -5.487 -3.658 19.772 1.00 36.28 C ANISOU 925 CG2 ILE B 351 4880 4668 4239 -187 -64 297 C ATOM 926 CD1 ILE B 351 -7.686 -1.738 20.051 1.00 25.14 C ANISOU 926 CD1 ILE B 351 3441 3254 2858 -141 -161 329 C ATOM 927 N TYR B 352 -7.787 -5.729 22.928 1.00 23.59 N ANISOU 927 N TYR B 352 3180 3023 2762 -153 -9 246 N ATOM 928 CA TYR B 352 -8.561 -6.390 23.977 1.00 24.64 C ANISOU 928 CA TYR B 352 3284 3143 2935 -145 22 239 C ATOM 929 C TYR B 352 -9.194 -5.414 24.950 1.00 26.70 C ANISOU 929 C TYR B 352 3513 3426 3207 -126 -18 244 C ATOM 930 O TYR B 352 -8.789 -4.268 25.041 1.00 22.93 O ANISOU 930 O TYR B 352 3037 2961 2714 -116 -51 255 O ATOM 931 CB TYR B 352 -7.668 -7.382 24.728 1.00 24.46 C ANISOU 931 CB TYR B 352 3262 3102 2928 -114 101 281 C ATOM 932 CG TYR B 352 -7.133 -8.449 23.796 1.00 26.49 C ANISOU 932 CG TYR B 352 3557 3314 3194 -126 167 269 C ATOM 933 CD1 TYR B 352 -7.835 -9.642 23.590 1.00 26.95 C ANISOU 933 CD1 TYR B 352 3632 3311 3295 -158 239 229 C ATOM 934 CD2 TYR B 352 -5.959 -8.243 23.082 1.00 23.77 C ANISOU 934 CD2 TYR B 352 3231 2981 2817 -118 170 286 C ATOM 935 CE1 TYR B 352 -7.355 -10.615 22.705 1.00 31.47 C ANISOU 935 CE1 TYR B 352 4246 3827 3883 -180 320 199 C ATOM 936 CE2 TYR B 352 -5.472 -9.204 22.203 1.00 37.44 C ANISOU 936 CE2 TYR B 352 4999 4668 4559 -130 243 266 C ATOM 937 CZ TYR B 352 -6.174 -10.387 22.019 1.00 41.32 C ANISOU 937 CZ TYR B 352 5513 5090 5097 -160 321 219 C ATOM 938 OH TYR B 352 -5.679 -11.329 21.140 1.00 48.88 O ANISOU 938 OH TYR B 352 6512 5989 6070 -180 413 182 O ATOM 939 N MET B 353 -10.192 -5.875 25.686 1.00 28.36 N ANISOU 939 N MET B 353 3693 3634 3448 -127 -1 228 N ATOM 940 CA MET B 353 -10.797 -5.044 26.708 1.00 33.96 C ANISOU 940 CA MET B 353 4369 4364 4170 -108 -23 225 C ATOM 941 C MET B 353 -10.045 -5.214 28.018 1.00 35.49 C ANISOU 941 C MET B 353 4549 4586 4349 -87 17 257 C ATOM 942 O MET B 353 -9.683 -6.328 28.387 1.00 34.95 O ANISOU 942 O MET B 353 4481 4515 4283 -75 73 292 O ATOM 943 CB MET B 353 -12.259 -5.427 26.867 1.00 35.65 C ANISOU 943 CB MET B 353 4547 4580 4417 -123 -22 191 C ATOM 944 CG MET B 353 -12.957 -5.490 25.527 1.00 30.55 C ANISOU 944 CG MET B 353 3896 3948 3764 -151 -61 158 C ATOM 945 SD MET B 353 -14.668 -6.023 25.673 1.00 40.25 S ANISOU 945 SD MET B 353 5059 5212 5024 -185 -59 106 S ATOM 946 CE MET B 353 -15.025 -6.275 23.945 1.00 27.95 C ANISOU 946 CE MET B 353 3491 3710 3420 -235 -102 65 C ATOM 947 N ASP B 354 -9.772 -4.100 28.694 1.00 24.33 N ANISOU 947 N ASP B 354 3122 3206 2917 -83 -4 247 N ATOM 948 CA ASP B 354 -9.075 -4.114 29.982 1.00 23.99 C ANISOU 948 CA ASP B 354 3048 3233 2835 -75 24 266 C ATOM 949 C ASP B 354 -10.156 -3.943 31.031 1.00 23.67 C ANISOU 949 C ASP B 354 2976 3211 2809 -74 34 240 C ATOM 950 O ASP B 354 -10.853 -2.940 31.021 1.00 23.73 O ANISOU 950 O ASP B 354 2982 3194 2842 -83 13 192 O ATOM 951 CB ASP B 354 -8.100 -2.935 30.034 1.00 25.83 C ANISOU 951 CB ASP B 354 3281 3500 3032 -100 4 243 C ATOM 952 CG ASP B 354 -7.205 -2.949 31.266 1.00 32.02 C ANISOU 952 CG ASP B 354 4016 4400 3748 -107 25 253 C ATOM 953 OD1 ASP B 354 -7.528 -3.625 32.284 1.00 29.72 O ANISOU 953 OD1 ASP B 354 3689 4169 3436 -83 51 282 O ATOM 954 OD2 ASP B 354 -6.157 -2.273 31.206 1.00 37.42 O ANISOU 954 OD2 ASP B 354 4692 5133 4394 -139 18 234 O ATOM 955 N ALA B 355 -10.332 -4.929 31.905 1.00 21.04 N ANISOU 955 N ALA B 355 2617 2912 2464 -56 79 278 N ATOM 956 CA ALA B 355 -11.417 -4.884 32.888 1.00 22.65 C ANISOU 956 CA ALA B 355 2790 3137 2679 -58 98 255 C ATOM 957 C ALA B 355 -11.102 -4.026 34.118 1.00 26.13 C ANISOU 957 C ALA B 355 3195 3671 3061 -70 101 226 C ATOM 958 O ALA B 355 -11.930 -3.917 35.018 1.00 24.89 O ANISOU 958 O ALA B 355 3011 3544 2904 -73 123 201 O ATOM 959 CB ALA B 355 -11.784 -6.291 33.331 1.00 27.13 C ANISOU 959 CB ALA B 355 3351 3698 3261 -40 161 313 C ATOM 960 N ASP B 356 -9.899 -3.454 34.160 1.00 25.53 N ANISOU 960 N ASP B 356 3116 3654 2931 -86 85 221 N ATOM 961 CA ASP B 356 -9.439 -2.642 35.289 1.00 22.93 C ANISOU 961 CA ASP B 356 2747 3438 2529 -121 92 172 C ATOM 962 C ASP B 356 -10.494 -1.627 35.744 1.00 24.65 C ANISOU 962 C ASP B 356 2965 3618 2783 -148 103 79 C ATOM 963 O ASP B 356 -10.760 -1.483 36.919 1.00 23.55 O ANISOU 963 O ASP B 356 2787 3565 2595 -166 132 46 O ATOM 964 CB ASP B 356 -8.153 -1.879 34.906 1.00 32.35 C ANISOU 964 CB ASP B 356 3942 4668 3683 -161 71 143 C ATOM 965 CG ASP B 356 -7.721 -0.869 35.983 1.00 51.37 C ANISOU 965 CG ASP B 356 6308 7192 6018 -229 86 54 C ATOM 966 OD1 ASP B 356 -7.043 0.136 35.656 1.00 52.97 O ANISOU 966 OD1 ASP B 356 6524 7384 6218 -290 85 -16 O ATOM 967 OD2 ASP B 356 -8.070 -1.078 37.164 1.00 51.59 O ANISOU 967 OD2 ASP B 356 6290 7325 5988 -232 108 46 O ATOM 968 N THR B 357 -11.086 -0.916 34.801 1.00 20.49 N ANISOU 968 N THR B 357 2479 2968 2339 -144 87 44 N ATOM 969 CA THR B 357 -12.093 0.074 35.144 1.00 21.68 C ANISOU 969 CA THR B 357 2630 3068 2541 -149 111 -31 C ATOM 970 C THR B 357 -13.498 -0.436 34.816 1.00 27.21 C ANISOU 970 C THR B 357 3319 3711 3309 -103 105 -6 C ATOM 971 O THR B 357 -14.444 0.336 34.779 1.00 23.85 O ANISOU 971 O THR B 357 2888 3229 2943 -84 119 -48 O ATOM 972 CB THR B 357 -11.802 1.421 34.411 1.00 32.63 C ANISOU 972 CB THR B 357 4061 4359 3977 -166 115 -80 C ATOM 973 OG1 THR B 357 -11.907 1.242 32.989 1.00 27.60 O ANISOU 973 OG1 THR B 357 3459 3638 3388 -127 73 -19 O ATOM 974 CG2 THR B 357 -10.375 1.900 34.743 1.00 28.28 C ANISOU 974 CG2 THR B 357 3513 3876 3357 -235 128 -122 C ATOM 975 N ILE B 358 -13.643 -1.744 34.606 1.00 19.32 N ANISOU 975 N ILE B 358 2310 2728 2302 -87 96 59 N ATOM 976 CA ILE B 358 -14.971 -2.328 34.365 1.00 22.80 C ANISOU 976 CA ILE B 358 2728 3136 2799 -67 99 67 C ATOM 977 C ILE B 358 -15.242 -3.394 35.445 1.00 26.66 C ANISOU 977 C ILE B 358 3186 3688 3255 -74 148 97 C ATOM 978 O ILE B 358 -15.272 -4.586 35.159 1.00 20.80 O ANISOU 978 O ILE B 358 2451 2931 2522 -73 166 150 O ATOM 979 CB ILE B 358 -15.072 -2.971 32.944 1.00 23.88 C ANISOU 979 CB ILE B 358 2886 3219 2970 -61 63 103 C ATOM 980 CG1 ILE B 358 -14.418 -2.083 31.894 1.00 22.84 C ANISOU 980 CG1 ILE B 358 2792 3044 2842 -53 20 102 C ATOM 981 CG2 ILE B 358 -16.540 -3.238 32.538 1.00 22.44 C ANISOU 981 CG2 ILE B 358 2663 3023 2842 -56 56 85 C ATOM 982 CD1 ILE B 358 -14.400 -2.714 30.491 1.00 24.75 C ANISOU 982 CD1 ILE B 358 3053 3257 3093 -56 -15 132 C ATOM 983 N PRO B 359 -15.423 -2.951 36.695 1.00 24.52 N ANISOU 983 N PRO B 359 2886 3485 2946 -83 183 62 N ATOM 984 CA PRO B 359 -15.564 -3.827 37.862 1.00 23.90 C ANISOU 984 CA PRO B 359 2777 3488 2815 -85 235 103 C ATOM 985 C PRO B 359 -16.839 -4.659 37.787 1.00 23.09 C ANISOU 985 C PRO B 359 2655 3344 2776 -82 268 117 C ATOM 986 O PRO B 359 -16.840 -5.793 38.264 1.00 21.32 O ANISOU 986 O PRO B 359 2428 3141 2532 -80 319 185 O ATOM 987 CB PRO B 359 -15.684 -2.850 39.045 1.00 29.73 C ANISOU 987 CB PRO B 359 3485 4308 3502 -107 261 28 C ATOM 988 CG PRO B 359 -15.403 -1.497 38.515 1.00 32.68 C ANISOU 988 CG PRO B 359 3883 4627 3908 -120 234 -52 C ATOM 989 CD PRO B 359 -15.531 -1.516 37.037 1.00 26.87 C ANISOU 989 CD PRO B 359 3180 3778 3251 -94 187 -24 C ATOM 990 N VAL B 360 -17.902 -4.104 37.209 1.00 19.66 N ANISOU 990 N VAL B 360 2201 2855 2414 -81 247 59 N ATOM 991 CA VAL B 360 -19.209 -4.788 37.196 1.00 21.44 C ANISOU 991 CA VAL B 360 2385 3066 2693 -93 278 53 C ATOM 992 C VAL B 360 -19.892 -4.648 35.843 1.00 24.00 C ANISOU 992 C VAL B 360 2695 3339 3086 -92 227 27 C ATOM 993 O VAL B 360 -19.456 -3.869 35.002 1.00 17.99 O ANISOU 993 O VAL B 360 1957 2548 2332 -69 171 20 O ATOM 994 CB VAL B 360 -20.188 -4.252 38.281 1.00 31.93 C ANISOU 994 CB VAL B 360 3662 4444 4026 -91 321 1 C ATOM 995 CG1 VAL B 360 -19.687 -4.568 39.684 1.00 34.36 C ANISOU 995 CG1 VAL B 360 3970 4838 4247 -102 379 29 C ATOM 996 CG2 VAL B 360 -20.443 -2.738 38.097 1.00 27.71 C ANISOU 996 CG2 VAL B 360 3116 3889 3523 -60 293 -70 C ATOM 997 N SER B 361 -20.963 -5.407 35.647 1.00 23.04 N ANISOU 997 N SER B 361 2529 3220 3007 -122 251 14 N ATOM 998 CA SER B 361 -21.686 -5.375 34.390 1.00 19.64 C ANISOU 998 CA SER B 361 2061 2783 2618 -132 200 -14 C ATOM 999 C SER B 361 -22.203 -3.963 34.199 1.00 24.85 C ANISOU 999 C SER B 361 2680 3460 3301 -70 153 -40 C ATOM 1000 O SER B 361 -22.592 -3.316 35.164 1.00 24.15 O ANISOU 1000 O SER B 361 2566 3387 3221 -42 188 -63 O ATOM 1001 CB SER B 361 -22.836 -6.379 34.409 1.00 24.77 C ANISOU 1001 CB SER B 361 2650 3458 3303 -193 246 -43 C ATOM 1002 OG SER B 361 -22.321 -7.706 34.376 1.00 29.05 O ANISOU 1002 OG SER B 361 3244 3950 3842 -249 307 -16 O ATOM 1003 N LYS B 362 -22.168 -3.476 32.961 1.00 24.38 N ANISOU 1003 N LYS B 362 2618 3395 3250 -43 85 -31 N ATOM 1004 CA LYS B 362 -22.486 -2.075 32.693 1.00 32.01 C ANISOU 1004 CA LYS B 362 3562 4356 4245 37 55 -28 C ATOM 1005 C LYS B 362 -22.785 -1.911 31.214 1.00 32.89 C ANISOU 1005 C LYS B 362 3641 4499 4355 60 -19 0 C ATOM 1006 O LYS B 362 -22.073 -2.446 30.370 1.00 33.66 O ANISOU 1006 O LYS B 362 3784 4588 4416 22 -52 16 O ATOM 1007 CB LYS B 362 -21.311 -1.163 33.078 1.00 25.64 C ANISOU 1007 CB LYS B 362 2838 3481 3423 63 68 -20 C ATOM 1008 CG LYS B 362 -21.600 0.345 32.896 1.00 27.37 C ANISOU 1008 CG LYS B 362 3052 3657 3692 145 71 -19 C ATOM 1009 CD LYS B 362 -20.350 1.185 33.208 1.00 35.19 C ANISOU 1009 CD LYS B 362 4130 4574 4668 139 98 -31 C ATOM 1010 CE LYS B 362 -20.588 2.673 32.956 1.00 50.18 C ANISOU 1010 CE LYS B 362 6040 6393 6633 217 128 -28 C ATOM 1011 NZ LYS B 362 -19.475 3.524 33.482 1.00 50.03 N ANISOU 1011 NZ LYS B 362 6101 6301 6608 185 182 -73 N ATOM 1012 N ASN B 363 -23.838 -1.172 30.898 1.00 28.83 N ANISOU 1012 N ASN B 363 3043 4033 3876 129 -40 11 N ATOM 1013 CA ASN B 363 -24.174 -0.911 29.503 1.00 31.73 C ANISOU 1013 CA ASN B 363 3365 4467 4225 168 -114 55 C ATOM 1014 C ASN B 363 -23.368 0.249 28.941 1.00 33.19 C ANISOU 1014 C ASN B 363 3621 4575 4413 247 -132 119 C ATOM 1015 O ASN B 363 -22.950 1.142 29.683 1.00 30.29 O ANISOU 1015 O ASN B 363 3310 4112 4089 290 -78 118 O ATOM 1016 CB ASN B 363 -25.666 -0.599 29.356 1.00 38.18 C ANISOU 1016 CB ASN B 363 4041 5395 5070 226 -131 61 C ATOM 1017 CG ASN B 363 -26.533 -1.816 29.563 1.00 40.68 C ANISOU 1017 CG ASN B 363 4271 5811 5374 127 -122 -6 C ATOM 1018 OD1 ASN B 363 -26.076 -2.948 29.413 1.00 43.56 O ANISOU 1018 OD1 ASN B 363 4678 6167 5705 17 -114 -47 O ATOM 1019 ND2 ASN B 363 -27.789 -1.593 29.910 1.00 41.98 N ANISOU 1019 ND2 ASN B 363 4314 6064 5574 164 -109 -19 N ATOM 1020 N ASP B 364 -23.160 0.230 27.631 1.00 26.46 N ANISOU 1020 N ASP B 364 2767 3772 3516 256 -198 167 N ATOM 1021 CA ASP B 364 -22.538 1.344 26.936 1.00 35.91 C ANISOU 1021 CA ASP B 364 4022 4907 4716 338 -211 245 C ATOM 1022 C ASP B 364 -21.157 1.719 27.481 1.00 38.64 C ANISOU 1022 C ASP B 364 4495 5112 5074 310 -161 230 C ATOM 1023 O ASP B 364 -20.831 2.896 27.633 1.00 34.16 O ANISOU 1023 O ASP B 364 3976 4449 4553 375 -118 262 O ATOM 1024 CB ASP B 364 -23.484 2.548 26.964 1.00 52.57 C ANISOU 1024 CB ASP B 364 6066 7019 6888 473 -192 308 C ATOM 1025 CG ASP B 364 -24.849 2.220 26.374 1.00 60.61 C ANISOU 1025 CG ASP B 364 6932 8215 7881 508 -250 332 C ATOM 1026 OD1 ASP B 364 -24.906 1.481 25.359 1.00 54.03 O ANISOU 1026 OD1 ASP B 364 6057 7507 6965 452 -324 335 O ATOM 1027 OD2 ASP B 364 -25.862 2.694 26.930 1.00 67.55 O ANISOU 1027 OD2 ASP B 364 7727 9120 8820 585 -217 340 O ATOM 1028 N VAL B 365 -20.344 0.713 27.779 1.00 31.46 N ANISOU 1028 N VAL B 365 3636 4194 4125 211 -157 181 N ATOM 1029 CA VAL B 365 -18.952 0.977 28.080 1.00 25.98 C ANISOU 1029 CA VAL B 365 3041 3409 3419 181 -127 175 C ATOM 1030 C VAL B 365 -18.261 1.455 26.806 1.00 31.55 C ANISOU 1030 C VAL B 365 3795 4096 4096 204 -164 238 C ATOM 1031 O VAL B 365 -18.463 0.892 25.735 1.00 27.49 O ANISOU 1031 O VAL B 365 3254 3658 3534 192 -220 263 O ATOM 1032 CB VAL B 365 -18.257 -0.264 28.609 1.00 25.90 C ANISOU 1032 CB VAL B 365 3060 3413 3370 93 -113 134 C ATOM 1033 CG1 VAL B 365 -16.771 0.014 28.778 1.00 27.92 C ANISOU 1033 CG1 VAL B 365 3398 3610 3600 67 -93 137 C ATOM 1034 CG2 VAL B 365 -18.910 -0.689 29.939 1.00 25.48 C ANISOU 1034 CG2 VAL B 365 2965 3380 3338 74 -65 86 C ATOM 1035 N GLU B 366 -17.473 2.514 26.904 1.00 27.43 N ANISOU 1035 N GLU B 366 3343 3479 3600 229 -125 256 N ATOM 1036 CA GLU B 366 -16.820 3.025 25.711 1.00 24.78 C ANISOU 1036 CA GLU B 366 3057 3119 3241 252 -148 325 C ATOM 1037 C GLU B 366 -15.386 2.522 25.560 1.00 29.51 C ANISOU 1037 C GLU B 366 3724 3698 3789 171 -148 302 C ATOM 1038 O GLU B 366 -14.607 2.489 26.521 1.00 27.64 O ANISOU 1038 O GLU B 366 3521 3425 3558 120 -105 249 O ATOM 1039 CB GLU B 366 -16.816 4.552 25.699 1.00 29.26 C ANISOU 1039 CB GLU B 366 3663 3577 3876 330 -88 372 C ATOM 1040 CG GLU B 366 -16.194 5.135 24.431 1.00 38.91 C ANISOU 1040 CG GLU B 366 4939 4770 5076 361 -100 462 C ATOM 1041 CD GLU B 366 -16.169 6.658 24.440 1.00 48.47 C ANISOU 1041 CD GLU B 366 6202 5844 6372 439 -13 517 C ATOM 1042 OE1 GLU B 366 -17.254 7.269 24.319 1.00 51.65 O ANISOU 1042 OE1 GLU B 366 6556 6242 6827 552 3 583 O ATOM 1043 OE2 GLU B 366 -15.067 7.238 24.570 1.00 44.53 O ANISOU 1043 OE2 GLU B 366 5788 5239 5891 388 49 494 O ATOM 1044 N PHE B 367 -15.041 2.146 24.338 1.00 24.74 N ANISOU 1044 N PHE B 367 3134 3138 3129 161 -195 345 N ATOM 1045 CA PHE B 367 -13.676 1.785 24.005 1.00 26.51 C ANISOU 1045 CA PHE B 367 3420 3343 3310 100 -189 337 C ATOM 1046 C PHE B 367 -13.236 2.726 22.897 1.00 31.42 C ANISOU 1046 C PHE B 367 4088 3932 3920 136 -192 413 C ATOM 1047 O PHE B 367 -13.985 2.968 21.948 1.00 25.43 O ANISOU 1047 O PHE B 367 3299 3225 3140 194 -231 479 O ATOM 1048 CB PHE B 367 -13.622 0.336 23.541 1.00 25.00 C ANISOU 1048 CB PHE B 367 3207 3229 3062 45 -223 309 C ATOM 1049 CG PHE B 367 -14.185 -0.635 24.544 1.00 26.53 C ANISOU 1049 CG PHE B 367 3358 3447 3274 14 -207 252 C ATOM 1050 CD1 PHE B 367 -13.360 -1.253 25.475 1.00 21.91 C ANISOU 1050 CD1 PHE B 367 2796 2839 2690 -26 -165 221 C ATOM 1051 CD2 PHE B 367 -15.537 -0.927 24.561 1.00 30.55 C ANISOU 1051 CD2 PHE B 367 3796 4016 3797 28 -229 238 C ATOM 1052 CE1 PHE B 367 -13.881 -2.149 26.404 1.00 28.64 C ANISOU 1052 CE1 PHE B 367 3614 3711 3558 -46 -138 187 C ATOM 1053 CE2 PHE B 367 -16.061 -1.818 25.478 1.00 31.11 C ANISOU 1053 CE2 PHE B 367 3830 4101 3888 -6 -201 187 C ATOM 1054 CZ PHE B 367 -15.234 -2.433 26.404 1.00 23.90 C ANISOU 1054 CZ PHE B 367 2953 3149 2979 -41 -152 167 C ATOM 1055 N ASN B 368 -12.049 3.312 23.022 1.00 27.76 N ANISOU 1055 N ASN B 368 3691 3392 3465 104 -145 409 N ATOM 1056 CA ASN B 368 -11.597 4.181 21.950 1.00 26.19 C ANISOU 1056 CA ASN B 368 3544 3152 3257 133 -134 488 C ATOM 1057 C ASN B 368 -10.100 4.076 21.714 1.00 31.44 C ANISOU 1057 C ASN B 368 4264 3795 3886 59 -109 469 C ATOM 1058 O ASN B 368 -9.345 3.622 22.592 1.00 23.75 O ANISOU 1058 O ASN B 368 3288 2825 2910 -5 -89 396 O ATOM 1059 CB ASN B 368 -12.075 5.649 22.134 1.00 28.73 C ANISOU 1059 CB ASN B 368 3889 3365 3661 208 -71 539 C ATOM 1060 CG ASN B 368 -11.438 6.343 23.329 1.00 36.51 C ANISOU 1060 CG ASN B 368 4916 4244 4713 156 17 458 C ATOM 1061 OD1 ASN B 368 -10.211 6.470 23.422 1.00 35.08 O ANISOU 1061 OD1 ASN B 368 4780 4032 4516 77 52 419 O ATOM 1062 ND2 ASN B 368 -12.271 6.811 24.243 1.00 33.70 N ANISOU 1062 ND2 ASN B 368 4536 3843 4426 193 58 424 N ATOM 1063 N VAL B 369 -9.701 4.482 20.512 1.00 27.23 N ANISOU 1063 N VAL B 369 3770 3258 3318 74 -112 543 N ATOM 1064 CA VAL B 369 -8.317 4.446 20.071 1.00 26.99 C ANISOU 1064 CA VAL B 369 3788 3216 3251 9 -86 537 C ATOM 1065 C VAL B 369 -8.011 5.757 19.354 1.00 32.33 C ANISOU 1065 C VAL B 369 4528 3804 3953 38 -31 621 C ATOM 1066 O VAL B 369 -8.823 6.245 18.572 1.00 26.72 O ANISOU 1066 O VAL B 369 3817 3099 3237 122 -46 719 O ATOM 1067 CB VAL B 369 -8.098 3.274 19.084 1.00 28.18 C ANISOU 1067 CB VAL B 369 3923 3472 3311 -14 -142 541 C ATOM 1068 CG1 VAL B 369 -6.769 3.419 18.366 1.00 33.06 C ANISOU 1068 CG1 VAL B 369 4592 4080 3890 -62 -111 558 C ATOM 1069 CG2 VAL B 369 -8.177 1.936 19.808 1.00 24.35 C ANISOU 1069 CG2 VAL B 369 3393 3042 2817 -51 -164 460 C ATOM 1070 N THR B 370 -6.839 6.325 19.608 1.00 27.53 N ANISOU 1070 N THR B 370 3969 3125 3368 -30 38 589 N ATOM 1071 CA THR B 370 -6.498 7.594 19.006 1.00 28.38 C ANISOU 1071 CA THR B 370 4146 3123 3514 -15 116 663 C ATOM 1072 C THR B 370 -5.269 7.424 18.138 1.00 33.30 C ANISOU 1072 C THR B 370 4803 3775 4073 -79 128 681 C ATOM 1073 O THR B 370 -4.176 7.134 18.632 1.00 32.36 O ANISOU 1073 O THR B 370 4677 3673 3943 -172 150 596 O ATOM 1074 CB THR B 370 -6.296 8.693 20.068 1.00 33.37 C ANISOU 1074 CB THR B 370 4813 3616 4249 -53 223 600 C ATOM 1075 OG1 THR B 370 -7.500 8.828 20.825 1.00 32.76 O ANISOU 1075 OG1 THR B 370 4703 3516 4230 15 217 586 O ATOM 1076 CG2 THR B 370 -5.997 10.036 19.398 1.00 31.48 C ANISOU 1076 CG2 THR B 370 4659 3232 4069 -36 331 685 C ATOM 1077 N ILE B 371 -5.482 7.575 16.832 1.00 31.26 N ANISOU 1077 N ILE B 371 4569 3545 3762 -23 110 795 N ATOM 1078 CA ILE B 371 -4.441 7.422 15.830 1.00 30.04 C ANISOU 1078 CA ILE B 371 4448 3429 3536 -72 122 826 C ATOM 1079 C ILE B 371 -3.982 8.813 15.402 1.00 32.28 C ANISOU 1079 C ILE B 371 4813 3579 3873 -71 231 909 C ATOM 1080 O ILE B 371 -4.742 9.577 14.799 1.00 33.39 O ANISOU 1080 O ILE B 371 4984 3672 4031 27 253 1038 O ATOM 1081 CB ILE B 371 -4.951 6.608 14.627 1.00 31.08 C ANISOU 1081 CB ILE B 371 4551 3702 3554 -25 36 890 C ATOM 1082 CG1 ILE B 371 -5.285 5.184 15.097 1.00 34.42 C ANISOU 1082 CG1 ILE B 371 4905 4230 3942 -50 -43 788 C ATOM 1083 CG2 ILE B 371 -3.916 6.621 13.492 1.00 31.04 C ANISOU 1083 CG2 ILE B 371 4590 3732 3473 -69 63 934 C ATOM 1084 CD1 ILE B 371 -5.720 4.242 14.007 1.00 42.39 C ANISOU 1084 CD1 ILE B 371 5883 5383 4841 -39 -114 804 C ATOM 1085 N GLY B 372 -2.744 9.150 15.744 1.00 27.86 N ANISOU 1085 N GLY B 372 4283 2960 3341 -178 307 840 N ATOM 1086 CA GLY B 372 -2.299 10.521 15.596 1.00 34.53 C ANISOU 1086 CA GLY B 372 5209 3647 4264 -203 439 887 C ATOM 1087 C GLY B 372 -3.144 11.361 16.523 1.00 37.93 C ANISOU 1087 C GLY B 372 5657 3943 4812 -159 500 871 C ATOM 1088 O GLY B 372 -3.112 11.167 17.738 1.00 36.47 O ANISOU 1088 O GLY B 372 5433 3759 4666 -217 498 738 O ATOM 1089 N ASN B 373 -3.928 12.274 15.963 1.00 38.45 N ANISOU 1089 N ASN B 373 5775 3904 4930 -47 558 1013 N ATOM 1090 CA ASN B 373 -4.843 13.066 16.780 1.00 42.93 C ANISOU 1090 CA ASN B 373 6358 4336 5618 18 626 1009 C ATOM 1091 C ASN B 373 -6.312 12.680 16.601 1.00 44.87 C ANISOU 1091 C ASN B 373 6542 4665 5840 173 528 1101 C ATOM 1092 O ASN B 373 -7.189 13.264 17.241 1.00 43.34 O ANISOU 1092 O ASN B 373 6349 4376 5744 248 579 1109 O ATOM 1093 CB ASN B 373 -4.667 14.569 16.516 1.00 49.18 C ANISOU 1093 CB ASN B 373 7257 4902 6527 37 809 1095 C ATOM 1094 CG ASN B 373 -3.330 15.107 17.015 1.00 47.19 C ANISOU 1094 CG ASN B 373 7058 4544 6328 -144 934 959 C ATOM 1095 OD1 ASN B 373 -2.894 14.807 18.132 1.00 39.38 O ANISOU 1095 OD1 ASN B 373 6025 3589 5349 -265 926 776 O ATOM 1096 ND2 ASN B 373 -2.680 15.927 16.188 1.00 42.32 N ANISOU 1096 ND2 ASN B 373 6529 3812 5740 -166 1054 1052 N ATOM 1097 N ASP B 374 -6.585 11.696 15.746 1.00 41.62 N ANISOU 1097 N ASP B 374 6073 4440 5300 214 396 1160 N ATOM 1098 CA ASP B 374 -7.970 11.328 15.443 1.00 40.17 C ANISOU 1098 CA ASP B 374 5817 4369 5076 348 301 1246 C ATOM 1099 C ASP B 374 -8.487 10.130 16.254 1.00 37.32 C ANISOU 1099 C ASP B 374 5365 4133 4682 313 190 1113 C ATOM 1100 O ASP B 374 -7.950 9.022 16.162 1.00 34.15 O ANISOU 1100 O ASP B 374 4931 3850 4196 228 115 1029 O ATOM 1101 CB ASP B 374 -8.128 11.084 13.945 1.00 50.89 C ANISOU 1101 CB ASP B 374 7161 5869 6304 415 234 1396 C ATOM 1102 CG ASP B 374 -7.774 12.316 13.120 1.00 62.46 C ANISOU 1102 CG ASP B 374 8718 7213 7803 475 352 1563 C ATOM 1103 OD1 ASP B 374 -8.391 13.383 13.347 1.00 64.92 O ANISOU 1103 OD1 ASP B 374 9062 7378 8225 583 449 1662 O ATOM 1104 OD2 ASP B 374 -6.872 12.220 12.259 1.00 59.78 O ANISOU 1104 OD2 ASP B 374 8419 6912 7384 417 361 1597 O ATOM 1105 N THR B 375 -9.541 10.363 17.036 1.00 33.09 N ANISOU 1105 N THR B 375 4788 3562 4221 384 194 1102 N ATOM 1106 CA THR B 375 -10.072 9.353 17.937 1.00 40.83 C ANISOU 1106 CA THR B 375 5689 4636 5188 351 114 980 C ATOM 1107 C THR B 375 -11.239 8.592 17.321 1.00 45.83 C ANISOU 1107 C THR B 375 6229 5446 5738 430 -2 1039 C ATOM 1108 O THR B 375 -12.108 9.177 16.683 1.00 40.45 O ANISOU 1108 O THR B 375 5522 4791 5056 555 -6 1176 O ATOM 1109 CB THR B 375 -10.534 9.963 19.269 1.00 40.70 C ANISOU 1109 CB THR B 375 5674 4496 5294 362 190 905 C ATOM 1110 OG1 THR B 375 -9.405 10.518 19.961 1.00 44.04 O ANISOU 1110 OG1 THR B 375 6168 4789 5776 251 292 808 O ATOM 1111 CG2 THR B 375 -11.191 8.886 20.150 1.00 33.56 C ANISOU 1111 CG2 THR B 375 4683 3702 4367 337 107 799 C ATOM 1112 N THR B 376 -11.251 7.279 17.515 1.00 32.30 N ANISOU 1112 N THR B 376 4459 3859 3955 356 -88 937 N ATOM 1113 CA THR B 376 -12.357 6.456 17.045 1.00 34.34 C ANISOU 1113 CA THR B 376 4621 4290 4137 397 -189 954 C ATOM 1114 C THR B 376 -12.925 5.720 18.248 1.00 34.64 C ANISOU 1114 C THR B 376 4601 4341 4218 360 -210 833 C ATOM 1115 O THR B 376 -12.167 5.181 19.061 1.00 33.15 O ANISOU 1115 O THR B 376 4440 4107 4050 268 -188 724 O ATOM 1116 CB THR B 376 -11.901 5.448 15.966 1.00 32.04 C ANISOU 1116 CB THR B 376 4318 4144 3713 330 -259 940 C ATOM 1117 OG1 THR B 376 -11.314 6.159 14.876 1.00 46.82 O ANISOU 1117 OG1 THR B 376 6245 6007 5536 360 -232 1055 O ATOM 1118 CG2 THR B 376 -13.082 4.653 15.435 1.00 33.43 C ANISOU 1118 CG2 THR B 376 4387 4512 3802 351 -353 940 C ATOM 1119 N LYS B 377 -14.248 5.715 18.378 1.00 29.76 N ANISOU 1119 N LYS B 377 3899 3797 3612 436 -247 861 N ATOM 1120 CA LYS B 377 -14.899 5.152 19.562 1.00 34.54 C ANISOU 1120 CA LYS B 377 4449 4406 4267 411 -252 759 C ATOM 1121 C LYS B 377 -15.885 4.069 19.167 1.00 41.05 C ANISOU 1121 C LYS B 377 5169 5411 5016 396 -341 731 C ATOM 1122 O LYS B 377 -16.440 4.077 18.065 1.00 39.94 O ANISOU 1122 O LYS B 377 4974 5407 4796 442 -399 809 O ATOM 1123 CB LYS B 377 -15.687 6.221 20.332 1.00 41.57 C ANISOU 1123 CB LYS B 377 5326 5200 5267 510 -189 796 C ATOM 1124 CG LYS B 377 -14.953 7.511 20.636 1.00 52.97 C ANISOU 1124 CG LYS B 377 6870 6455 6802 535 -78 827 C ATOM 1125 CD LYS B 377 -15.924 8.570 21.183 1.00 60.97 C ANISOU 1125 CD LYS B 377 7863 7376 7926 654 -4 877 C ATOM 1126 CE LYS B 377 -15.218 9.913 21.435 1.00 64.40 C ANISOU 1126 CE LYS B 377 8408 7596 8465 670 136 900 C ATOM 1127 NZ LYS B 377 -16.160 11.009 21.825 1.00 59.53 N ANISOU 1127 NZ LYS B 377 7782 6866 7969 803 233 963 N ATOM 1128 N THR B 378 -16.115 3.144 20.086 1.00 30.88 N ANISOU 1128 N THR B 378 3850 4135 3749 325 -344 618 N ATOM 1129 CA THR B 378 -17.227 2.228 19.963 1.00 38.42 C ANISOU 1129 CA THR B 378 4699 5237 4661 304 -403 575 C ATOM 1130 C THR B 378 -17.661 1.880 21.376 1.00 33.16 C ANISOU 1130 C THR B 378 4010 4518 4073 280 -365 491 C ATOM 1131 O THR B 378 -16.936 2.145 22.332 1.00 31.33 O ANISOU 1131 O THR B 378 3845 4159 3900 261 -305 456 O ATOM 1132 CB THR B 378 -16.878 0.956 19.144 1.00 33.82 C ANISOU 1132 CB THR B 378 4111 4760 3980 197 -445 510 C ATOM 1133 OG1 THR B 378 -18.054 0.149 18.991 1.00 42.82 O ANISOU 1133 OG1 THR B 378 5141 6049 5081 163 -491 457 O ATOM 1134 CG2 THR B 378 -15.793 0.131 19.832 1.00 32.46 C ANISOU 1134 CG2 THR B 378 4015 4486 3834 103 -395 421 C ATOM 1135 N THR B 379 -18.849 1.310 21.518 1.00 31.43 N ANISOU 1135 N THR B 379 3688 4409 3846 275 -398 456 N ATOM 1136 CA THR B 379 -19.342 0.973 22.837 1.00 36.25 C ANISOU 1136 CA THR B 379 4271 4979 4525 253 -357 383 C ATOM 1137 C THR B 379 -19.895 -0.445 22.837 1.00 37.73 C ANISOU 1137 C THR B 379 4395 5268 4673 153 -378 295 C ATOM 1138 O THR B 379 -20.236 -0.992 21.791 1.00 42.39 O ANISOU 1138 O THR B 379 4934 5986 5188 113 -430 285 O ATOM 1139 CB THR B 379 -20.435 1.949 23.303 1.00 46.20 C ANISOU 1139 CB THR B 379 5461 6242 5850 365 -342 432 C ATOM 1140 OG1 THR B 379 -21.600 1.788 22.487 1.00 53.26 O ANISOU 1140 OG1 THR B 379 6231 7310 6694 403 -408 469 O ATOM 1141 CG2 THR B 379 -19.950 3.399 23.214 1.00 49.44 C ANISOU 1141 CG2 THR B 379 5941 6529 6313 466 -295 521 C ATOM 1142 N ALA B 380 -19.973 -1.042 24.014 1.00 29.09 N ANISOU 1142 N ALA B 380 3306 4119 3628 105 -328 226 N ATOM 1143 CA ALA B 380 -20.602 -2.355 24.145 1.00 31.83 C ANISOU 1143 CA ALA B 380 3597 4537 3960 10 -321 143 C ATOM 1144 C ALA B 380 -21.241 -2.483 25.513 1.00 30.12 C ANISOU 1144 C ALA B 380 3346 4287 3810 11 -268 106 C ATOM 1145 O ALA B 380 -20.845 -1.796 26.461 1.00 35.16 O ANISOU 1145 O ALA B 380 4031 4834 4495 60 -229 125 O ATOM 1146 CB ALA B 380 -19.587 -3.465 23.925 1.00 28.71 C ANISOU 1146 CB ALA B 380 3280 4093 3537 -86 -290 96 C ATOM 1147 N ASN B 381 -22.245 -3.346 25.614 1.00 28.09 N ANISOU 1147 N ASN B 381 3005 4115 3553 -53 -262 45 N ATOM 1148 CA ASN B 381 -22.801 -3.682 26.911 1.00 29.98 C ANISOU 1148 CA ASN B 381 3218 4324 3848 -70 -200 6 C ATOM 1149 C ASN B 381 -22.003 -4.848 27.508 1.00 27.31 C ANISOU 1149 C ASN B 381 2961 3898 3516 -156 -129 -31 C ATOM 1150 O ASN B 381 -22.002 -5.953 26.968 1.00 31.43 O ANISOU 1150 O ASN B 381 3486 4437 4019 -248 -109 -80 O ATOM 1151 CB ASN B 381 -24.286 -4.039 26.781 1.00 33.82 C ANISOU 1151 CB ASN B 381 3567 4946 4337 -101 -214 -39 C ATOM 1152 CG ASN B 381 -25.130 -2.869 26.271 1.00 43.43 C ANISOU 1152 CG ASN B 381 4686 6267 5550 11 -279 21 C ATOM 1153 OD1 ASN B 381 -24.800 -1.700 26.482 1.00 35.24 O ANISOU 1153 OD1 ASN B 381 3688 5158 4543 123 -278 92 O ATOM 1154 ND2 ASN B 381 -26.222 -3.188 25.593 1.00 49.56 N ANISOU 1154 ND2 ASN B 381 5328 7214 6287 -19 -325 -6 N ATOM 1155 N ILE B 382 -21.301 -4.598 28.605 1.00 24.17 N ANISOU 1155 N ILE B 382 2629 3412 3143 -124 -81 -6 N ATOM 1156 CA ILE B 382 -20.513 -5.651 29.247 1.00 23.64 C ANISOU 1156 CA ILE B 382 2629 3276 3077 -178 -10 -11 C ATOM 1157 C ILE B 382 -21.377 -6.421 30.257 1.00 29.39 C ANISOU 1157 C ILE B 382 3313 4013 3840 -221 61 -42 C ATOM 1158 O ILE B 382 -22.021 -5.839 31.132 1.00 25.21 O ANISOU 1158 O ILE B 382 2738 3508 3331 -184 72 -44 O ATOM 1159 CB ILE B 382 -19.277 -5.108 29.967 1.00 28.28 C ANISOU 1159 CB ILE B 382 3292 3802 3652 -131 5 35 C ATOM 1160 CG1 ILE B 382 -18.408 -4.276 29.002 1.00 25.56 C ANISOU 1160 CG1 ILE B 382 2993 3440 3280 -95 -53 65 C ATOM 1161 CG2 ILE B 382 -18.478 -6.265 30.584 1.00 25.88 C ANISOU 1161 CG2 ILE B 382 3041 3452 3340 -167 78 56 C ATOM 1162 CD1 ILE B 382 -17.905 -5.038 27.786 1.00 28.14 C ANISOU 1162 CD1 ILE B 382 3351 3765 3576 -141 -70 62 C ATOM 1163 N GLN B 383 -21.400 -7.736 30.113 1.00 24.35 N ANISOU 1163 N GLN B 383 2328 4148 2776 177 -873 629 N ATOM 1164 CA GLN B 383 -22.188 -8.569 30.997 1.00 27.31 C ANISOU 1164 CA GLN B 383 2552 4518 3305 191 -838 670 C ATOM 1165 C GLN B 383 -21.346 -9.708 31.498 1.00 28.48 C ANISOU 1165 C GLN B 383 2725 4615 3483 58 -850 513 C ATOM 1166 O GLN B 383 -20.964 -10.602 30.743 1.00 34.92 O ANISOU 1166 O GLN B 383 3489 5494 4284 -76 -967 404 O ATOM 1167 CB GLN B 383 -23.435 -9.094 30.272 1.00 39.48 C ANISOU 1167 CB GLN B 383 3848 6213 4938 179 -960 765 C ATOM 1168 CG GLN B 383 -24.115 -10.231 30.998 1.00 62.02 C ANISOU 1168 CG GLN B 383 6533 9081 7950 137 -957 775 C ATOM 1169 CD GLN B 383 -25.615 -10.280 30.756 1.00 76.78 C ANISOU 1169 CD GLN B 383 8160 11074 9937 197 -1007 954 C ATOM 1170 OE1 GLN B 383 -26.298 -11.186 31.241 1.00 83.35 O ANISOU 1170 OE1 GLN B 383 8830 11936 10902 156 -1015 982 O ATOM 1171 NE2 GLN B 383 -26.136 -9.304 30.011 1.00 75.06 N ANISOU 1171 NE2 GLN B 383 7911 10935 9674 293 -1039 1089 N ATOM 1172 N TYR B 384 -21.049 -9.668 32.788 1.00 22.66 N ANISOU 1172 N TYR B 384 2079 3751 2778 100 -720 506 N ATOM 1173 CA TYR B 384 -20.295 -10.721 33.425 1.00 20.08 C ANISOU 1173 CA TYR B 384 1772 3367 2489 -6 -717 379 C ATOM 1174 C TYR B 384 -21.233 -11.810 33.979 1.00 23.67 C ANISOU 1174 C TYR B 384 2048 3846 3100 -19 -718 406 C ATOM 1175 O TYR B 384 -22.374 -11.534 34.313 1.00 25.46 O ANISOU 1175 O TYR B 384 2172 4091 3410 83 -667 541 O ATOM 1176 CB TYR B 384 -19.521 -10.150 34.599 1.00 20.44 C ANISOU 1176 CB TYR B 384 2016 3264 2487 31 -588 367 C ATOM 1177 CG TYR B 384 -18.408 -9.196 34.248 1.00 27.35 C ANISOU 1177 CG TYR B 384 3084 4098 3210 9 -582 326 C ATOM 1178 CD1 TYR B 384 -17.222 -9.662 33.706 1.00 22.61 C ANISOU 1178 CD1 TYR B 384 2520 3521 2551 -116 -658 200 C ATOM 1179 CD2 TYR B 384 -18.530 -7.834 34.503 1.00 24.51 C ANISOU 1179 CD2 TYR B 384 2880 3667 2765 115 -486 419 C ATOM 1180 CE1 TYR B 384 -16.190 -8.807 33.416 1.00 27.02 C ANISOU 1180 CE1 TYR B 384 3242 4047 2979 -145 -649 171 C ATOM 1181 CE2 TYR B 384 -17.504 -6.966 34.221 1.00 19.22 C ANISOU 1181 CE2 TYR B 384 2396 2954 1952 79 -480 382 C ATOM 1182 CZ TYR B 384 -16.329 -7.463 33.672 1.00 24.64 C ANISOU 1182 CZ TYR B 384 3093 3678 2591 -56 -567 259 C ATOM 1183 OH TYR B 384 -15.283 -6.618 33.385 1.00 18.63 O ANISOU 1183 OH TYR B 384 2502 2881 1694 -103 -561 230 O ATOM 1184 N PRO B 385 -20.722 -13.039 34.112 1.00 22.89 N ANISOU 1184 N PRO B 385 1917 3739 3040 -139 -764 285 N ATOM 1185 CA PRO B 385 -21.459 -14.154 34.725 1.00 34.89 C ANISOU 1185 CA PRO B 385 3294 5262 4699 -169 -757 292 C ATOM 1186 C PRO B 385 -21.557 -13.956 36.240 1.00 34.06 C ANISOU 1186 C PRO B 385 3262 5028 4651 -80 -602 341 C ATOM 1187 O PRO B 385 -20.707 -13.281 36.831 1.00 29.05 O ANISOU 1187 O PRO B 385 2813 4291 3934 -47 -525 319 O ATOM 1188 CB PRO B 385 -20.562 -15.376 34.450 1.00 37.19 C ANISOU 1188 CB PRO B 385 3644 5522 4967 -308 -794 136 C ATOM 1189 CG PRO B 385 -19.322 -14.870 33.750 1.00 35.55 C ANISOU 1189 CG PRO B 385 3594 5293 4620 -337 -803 59 C ATOM 1190 CD PRO B 385 -19.315 -13.375 33.833 1.00 30.48 C ANISOU 1190 CD PRO B 385 2996 4668 3915 -241 -798 142 C ATOM 1191 N ASP B 386 -22.561 -14.553 36.868 1.00 26.54 N ANISOU 1191 N ASP B 386 2176 4077 3831 -53 -560 407 N ATOM 1192 CA ASP B 386 -22.639 -14.551 38.330 1.00 29.60 C ANISOU 1192 CA ASP B 386 2643 4331 4273 18 -410 440 C ATOM 1193 C ASP B 386 -21.529 -15.412 38.913 1.00 21.61 C ANISOU 1193 C ASP B 386 1732 3237 3242 -83 -413 300 C ATOM 1194 O ASP B 386 -20.994 -16.295 38.239 1.00 26.12 O ANISOU 1194 O ASP B 386 2257 3864 3805 -201 -519 190 O ATOM 1195 CB ASP B 386 -23.987 -15.108 38.801 1.00 36.64 C ANISOU 1195 CB ASP B 386 3348 5251 5322 60 -363 544 C ATOM 1196 CG ASP B 386 -25.167 -14.269 38.339 1.00 56.46 C ANISOU 1196 CG ASP B 386 5730 7848 7875 179 -346 718 C ATOM 1197 OD1 ASP B 386 -25.010 -13.039 38.191 1.00 50.41 O ANISOU 1197 OD1 ASP B 386 5081 7053 7018 283 -291 781 O ATOM 1198 OD2 ASP B 386 -26.261 -14.848 38.139 1.00 69.46 O ANISOU 1198 OD2 ASP B 386 7154 9591 9646 165 -385 801 O ATOM 1199 N TYR B 387 -21.167 -15.150 40.158 1.00 17.24 N ANISOU 1199 N TYR B 387 1328 2546 2675 -34 -294 310 N ATOM 1200 CA TYR B 387 -20.334 -16.080 40.905 1.00 20.90 C ANISOU 1200 CA TYR B 387 1857 2933 3151 -116 -289 208 C ATOM 1201 C TYR B 387 -21.121 -17.364 41.086 1.00 25.60 C ANISOU 1201 C TYR B 387 2283 3559 3885 -158 -300 196 C ATOM 1202 O TYR B 387 -22.315 -17.392 40.840 1.00 21.51 O ANISOU 1202 O TYR B 387 1612 3107 3453 -117 -295 285 O ATOM 1203 CB TYR B 387 -19.980 -15.494 42.273 1.00 26.06 C ANISOU 1203 CB TYR B 387 2710 3432 3760 -56 -160 244 C ATOM 1204 CG TYR B 387 -19.132 -14.255 42.146 1.00 27.41 C ANISOU 1204 CG TYR B 387 3072 3562 3782 -41 -152 251 C ATOM 1205 CD1 TYR B 387 -17.943 -14.288 41.427 1.00 22.31 C ANISOU 1205 CD1 TYR B 387 2462 2964 3050 -138 -257 158 C ATOM 1206 CD2 TYR B 387 -19.524 -13.053 42.718 1.00 23.24 C ANISOU 1206 CD2 TYR B 387 2693 2942 3195 67 -32 353 C ATOM 1207 CE1 TYR B 387 -17.158 -13.149 41.284 1.00 19.03 C ANISOU 1207 CE1 TYR B 387 2217 2516 2497 -139 -254 168 C ATOM 1208 CE2 TYR B 387 -18.734 -11.904 42.588 1.00 25.31 C ANISOU 1208 CE2 TYR B 387 3151 3158 3307 65 -26 357 C ATOM 1209 CZ TYR B 387 -17.548 -11.969 41.870 1.00 23.01 C ANISOU 1209 CZ TYR B 387 2880 2926 2936 -46 -145 263 C ATOM 1210 OH TYR B 387 -16.758 -10.850 41.711 1.00 24.25 O ANISOU 1210 OH TYR B 387 3223 3045 2948 -64 -144 269 O ATOM 1211 N VAL B 388 -20.467 -18.429 41.517 1.00 26.88 N ANISOU 1211 N VAL B 388 2468 3676 4071 -241 -315 98 N ATOM 1212 CA VAL B 388 -21.166 -19.692 41.667 1.00 26.19 C ANISOU 1212 CA VAL B 388 2237 3607 4105 -294 -324 78 C ATOM 1213 C VAL B 388 -21.436 -19.913 43.142 1.00 24.04 C ANISOU 1213 C VAL B 388 2029 3209 3897 -239 -194 119 C ATOM 1214 O VAL B 388 -20.575 -19.661 43.970 1.00 21.34 O ANISOU 1214 O VAL B 388 1856 2761 3491 -225 -142 94 O ATOM 1215 CB VAL B 388 -20.327 -20.864 41.138 1.00 26.61 C ANISOU 1215 CB VAL B 388 2367 3642 4102 -381 -385 -50 C ATOM 1216 CG1 VAL B 388 -21.140 -22.159 41.231 1.00 25.46 C ANISOU 1216 CG1 VAL B 388 2128 3495 4053 -428 -384 -65 C ATOM 1217 CG2 VAL B 388 -19.913 -20.592 39.706 1.00 24.29 C ANISOU 1217 CG2 VAL B 388 2097 3428 3703 -412 -470 -88 C ATOM 1218 N SER B 389 -22.631 -20.370 43.487 1.00 21.25 N ANISOU 1218 N SER B 389 1543 2865 3665 -214 -141 189 N ATOM 1219 CA SER B 389 -22.932 -20.574 44.894 1.00 29.47 C ANISOU 1219 CA SER B 389 2655 3778 4765 -157 -2 232 C ATOM 1220 C SER B 389 -23.813 -21.775 45.177 1.00 28.71 C ANISOU 1220 C SER B 389 2406 3693 4809 -205 16 237 C ATOM 1221 O SER B 389 -24.650 -22.179 44.360 1.00 22.90 O ANISOU 1221 O SER B 389 1477 3076 4148 -254 -56 265 O ATOM 1222 CB SER B 389 -23.551 -19.315 45.510 1.00 35.56 C ANISOU 1222 CB SER B 389 3502 4485 5523 -11 134 368 C ATOM 1223 OG SER B 389 -24.779 -19.006 44.888 1.00 48.38 O ANISOU 1223 OG SER B 389 4936 6216 7231 46 135 483 O ATOM 1224 N AARG B 390 -23.613 -22.356 46.350 0.46 23.70 N ANISOU 1224 N AARG B 390 1866 2934 4205 -201 107 213 N ATOM 1225 N BARG B 390 -23.598 -22.341 46.353 0.54 23.31 N ANISOU 1225 N BARG B 390 1820 2884 4154 -201 107 213 N ATOM 1226 CA AARG B 390 -24.488 -23.408 46.847 0.46 24.18 C ANISOU 1226 CA AARG B 390 1810 2979 4399 -232 158 232 C ATOM 1227 CA BARG B 390 -24.414 -23.421 46.874 0.54 23.89 C ANISOU 1227 CA BARG B 390 1784 2936 4357 -234 158 226 C ATOM 1228 C AARG B 390 -24.587 -23.203 48.353 0.46 22.82 C ANISOU 1228 C AARG B 390 1785 2646 4240 -142 327 286 C ATOM 1229 C BARG B 390 -24.569 -23.070 48.345 0.54 22.62 C ANISOU 1229 C BARG B 390 1769 2619 4205 -133 329 292 C ATOM 1230 O AARG B 390 -23.578 -23.210 49.052 0.46 21.97 O ANISOU 1230 O AARG B 390 1869 2431 4048 -148 346 224 O ATOM 1231 O BARG B 390 -23.570 -22.827 49.012 0.54 22.72 O ANISOU 1231 O BARG B 390 1986 2527 4121 -123 354 244 O ATOM 1232 CB AARG B 390 -23.928 -24.799 46.495 0.46 22.94 C ANISOU 1232 CB AARG B 390 1625 2838 4255 -371 63 98 C ATOM 1233 CB BARG B 390 -23.672 -24.760 46.697 0.54 15.52 C ANISOU 1233 CB BARG B 390 732 1868 3295 -363 75 86 C ATOM 1234 CG AARG B 390 -24.881 -25.651 45.640 0.46 29.66 C ANISOU 1234 CG AARG B 390 2312 3785 5175 -450 -18 100 C ATOM 1235 CG BARG B 390 -23.508 -25.195 45.238 0.54 11.29 C ANISOU 1235 CG BARG B 390 148 1440 2702 -442 -78 13 C ATOM 1236 CD AARG B 390 -24.140 -26.461 44.570 0.46 30.57 C ANISOU 1236 CD AARG B 390 2497 3931 5188 -541 -147 -30 C ATOM 1237 CD BARG B 390 -24.885 -25.512 44.627 0.54 28.61 C ANISOU 1237 CD BARG B 390 2145 3736 4991 -483 -115 86 C ATOM 1238 NE AARG B 390 -23.261 -27.484 45.142 0.46 36.77 N ANISOU 1238 NE AARG B 390 3414 4611 5947 -565 -117 -137 N ATOM 1239 NE BARG B 390 -24.828 -26.158 43.315 0.54 24.15 N ANISOU 1239 NE BARG B 390 1559 3254 4364 -583 -251 14 N ATOM 1240 CZ AARG B 390 -23.472 -28.794 45.062 0.46 24.26 C ANISOU 1240 CZ AARG B 390 1812 3008 4397 -641 -128 -199 C ATOM 1241 CZ BARG B 390 -24.810 -25.506 42.156 0.54 30.68 C ANISOU 1241 CZ BARG B 390 2357 4183 5116 -594 -347 29 C ATOM 1242 NH1AARG B 390 -24.542 -29.267 44.425 0.46 22.87 N ANISOU 1242 NH1AARG B 390 1496 2911 4281 -725 -180 -169 N ATOM 1243 NH1BARG B 390 -24.771 -26.182 41.016 0.54 38.18 N ANISOU 1243 NH1BARG B 390 3302 5198 6008 -697 -454 -37 N ATOM 1244 NH2AARG B 390 -22.611 -29.634 45.625 0.46 12.11 N ANISOU 1244 NH2AARG B 390 393 1376 2834 -640 -88 -283 N ATOM 1245 NH2BARG B 390 -24.824 -24.182 42.131 0.54 15.50 N ANISOU 1245 NH2BARG B 390 419 2296 3173 -505 -328 110 N ATOM 1246 N ASP B 391 -25.807 -22.994 48.839 1.00 22.77 N ANISOU 1246 N ASP B 391 1690 2625 4336 -59 449 412 N ATOM 1247 CA ASP B 391 -26.050 -22.628 50.233 1.00 20.50 C ANISOU 1247 CA ASP B 391 1558 2176 4055 48 636 485 C ATOM 1248 C ASP B 391 -25.267 -21.344 50.538 1.00 28.27 C ANISOU 1248 C ASP B 391 2782 3074 4886 125 676 498 C ATOM 1249 O ASP B 391 -25.323 -20.414 49.746 1.00 25.13 O ANISOU 1249 O ASP B 391 2354 2754 4440 169 636 541 O ATOM 1250 CB ASP B 391 -25.731 -23.792 51.177 1.00 21.49 C ANISOU 1250 CB ASP B 391 1760 2194 4213 -17 673 408 C ATOM 1251 CG ASP B 391 -26.534 -25.061 50.831 1.00 32.31 C ANISOU 1251 CG ASP B 391 2905 3644 5727 -108 635 394 C ATOM 1252 OD1 ASP B 391 -27.716 -24.929 50.441 1.00 27.53 O ANISOU 1252 OD1 ASP B 391 2099 3130 5230 -80 660 503 O ATOM 1253 OD2 ASP B 391 -25.987 -26.187 50.928 1.00 31.58 O ANISOU 1253 OD2 ASP B 391 2835 3525 5638 -211 576 282 O ATOM 1254 N ASN B 392 -24.523 -21.281 51.638 1.00 23.79 N ANISOU 1254 N ASN B 392 2457 2350 4233 130 745 462 N ATOM 1255 CA ASN B 392 -23.778 -20.051 51.928 1.00 23.84 C ANISOU 1255 CA ASN B 392 2707 2271 4080 178 774 477 C ATOM 1256 C ASN B 392 -22.367 -20.023 51.317 1.00 28.67 C ANISOU 1256 C ASN B 392 3387 2934 4573 72 604 363 C ATOM 1257 O ASN B 392 -21.619 -19.071 51.530 1.00 22.37 O ANISOU 1257 O ASN B 392 2791 2072 3635 80 604 367 O ATOM 1258 CB ASN B 392 -23.698 -19.791 53.435 1.00 23.59 C ANISOU 1258 CB ASN B 392 2938 2036 3990 232 935 516 C ATOM 1259 CG ASN B 392 -25.041 -19.394 54.026 1.00 36.10 C ANISOU 1259 CG ASN B 392 4507 3549 5662 374 1144 657 C ATOM 1260 OD1 ASN B 392 -25.766 -18.597 53.446 1.00 29.67 O ANISOU 1260 OD1 ASN B 392 3600 2797 4877 470 1194 755 O ATOM 1261 ND2 ASN B 392 -25.378 -19.962 55.173 1.00 40.57 N ANISOU 1261 ND2 ASN B 392 5159 3983 6273 393 1274 676 N ATOM 1262 N ASN B 393 -22.014 -21.061 50.565 1.00 21.12 N ANISOU 1262 N ASN B 393 2268 2086 3669 -30 467 268 N ATOM 1263 CA ASN B 393 -20.717 -21.105 49.874 1.00 22.90 C ANISOU 1263 CA ASN B 393 2528 2373 3801 -120 318 170 C ATOM 1264 C ASN B 393 -20.736 -20.406 48.509 1.00 20.18 C ANISOU 1264 C ASN B 393 2081 2165 3420 -119 226 173 C ATOM 1265 O ASN B 393 -21.607 -20.673 47.672 1.00 21.64 O ANISOU 1265 O ASN B 393 2070 2461 3694 -116 194 194 O ATOM 1266 CB ASN B 393 -20.246 -22.560 49.682 1.00 22.39 C ANISOU 1266 CB ASN B 393 2365 2344 3797 -220 233 67 C ATOM 1267 CG ASN B 393 -19.687 -23.181 50.967 1.00 25.55 C ANISOU 1267 CG ASN B 393 2913 2611 4186 -239 284 45 C ATOM 1268 OD1 ASN B 393 -19.229 -22.476 51.877 1.00 21.55 O ANISOU 1268 OD1 ASN B 393 2609 1994 3585 -213 336 83 O ATOM 1269 ND2 ASN B 393 -19.715 -24.505 51.038 1.00 21.79 N ANISOU 1269 ND2 ASN B 393 2348 2137 3794 -293 267 -15 N ATOM 1270 N SER B 394 -19.770 -19.526 48.265 1.00 16.93 N ANISOU 1270 N SER B 394 1664 1708 3062 -17 254 138 N ATOM 1271 CA SER B 394 -19.711 -18.867 46.965 1.00 12.35 C ANISOU 1271 CA SER B 394 1046 1158 2488 2 210 117 C ATOM 1272 C SER B 394 -18.282 -18.810 46.474 1.00 19.77 C ANISOU 1272 C SER B 394 2031 2128 3355 3 155 66 C ATOM 1273 O SER B 394 -17.352 -18.768 47.272 1.00 15.67 O ANISOU 1273 O SER B 394 1572 1603 2777 -5 168 49 O ATOM 1274 CB SER B 394 -20.350 -17.466 47.023 1.00 26.18 C ANISOU 1274 CB SER B 394 2790 2909 4250 27 283 140 C ATOM 1275 OG SER B 394 -19.802 -16.634 48.048 1.00 20.05 O ANISOU 1275 OG SER B 394 2090 2121 3407 32 351 133 O ATOM 1276 N ILE B 395 -18.100 -18.796 45.160 1.00 15.50 N ANISOU 1276 N ILE B 395 1458 1616 2817 16 93 45 N ATOM 1277 CA ILE B 395 -16.758 -18.846 44.604 1.00 20.75 C ANISOU 1277 CA ILE B 395 2153 2312 3420 21 48 1 C ATOM 1278 C ILE B 395 -16.773 -18.331 43.159 1.00 20.50 C ANISOU 1278 C ILE B 395 2095 2314 3381 45 14 -9 C ATOM 1279 O ILE B 395 -17.816 -18.333 42.502 1.00 26.91 O ANISOU 1279 O ILE B 395 2862 3123 4239 56 -6 10 O ATOM 1280 CB ILE B 395 -16.199 -20.312 44.657 1.00 12.25 C ANISOU 1280 CB ILE B 395 1083 1229 2344 10 -16 -27 C ATOM 1281 CG1 ILE B 395 -14.689 -20.351 44.392 1.00 16.98 C ANISOU 1281 CG1 ILE B 395 1713 1857 2882 17 -45 -71 C ATOM 1282 CG2 ILE B 395 -16.947 -21.182 43.659 1.00 15.15 C ANISOU 1282 CG2 ILE B 395 1401 1594 2763 16 -83 -32 C ATOM 1283 CD1 ILE B 395 -14.037 -21.699 44.829 1.00 15.58 C ANISOU 1283 CD1 ILE B 395 1552 1662 2703 9 -96 -96 C ATOM 1284 N GLY B 396 -15.616 -17.889 42.680 1.00 19.35 N ANISOU 1284 N GLY B 396 1975 2200 3177 52 8 -35 N ATOM 1285 CA GLY B 396 -15.431 -17.488 41.288 1.00 19.49 C ANISOU 1285 CA GLY B 396 1981 2255 3170 77 -20 -43 C ATOM 1286 C GLY B 396 -13.971 -17.686 40.909 1.00 16.34 C ANISOU 1286 C GLY B 396 1604 1888 2715 81 -35 -80 C ATOM 1287 O GLY B 396 -13.104 -17.685 41.774 1.00 15.91 O ANISOU 1287 O GLY B 396 1572 1826 2646 63 -15 -92 O ATOM 1288 N SER B 397 -13.672 -17.881 39.635 1.00 12.63 N ANISOU 1288 N SER B 397 1129 1454 2214 107 -71 -98 N ATOM 1289 CA SER B 397 -12.269 -18.036 39.250 1.00 16.91 C ANISOU 1289 CA SER B 397 1684 2031 2708 116 -71 -129 C ATOM 1290 C SER B 397 -12.053 -17.720 37.787 1.00 21.36 C ANISOU 1290 C SER B 397 2251 2639 3224 151 -78 -132 C ATOM 1291 O SER B 397 -12.972 -17.832 36.975 1.00 17.32 O ANISOU 1291 O SER B 397 1738 2131 2712 172 -114 -126 O ATOM 1292 CB SER B 397 -11.798 -19.479 39.486 1.00 22.48 C ANISOU 1292 CB SER B 397 2390 2731 3421 120 -121 -172 C ATOM 1293 OG SER B 397 -12.488 -20.370 38.615 1.00 17.44 O ANISOU 1293 OG SER B 397 1744 2093 2788 144 -184 -192 O ATOM 1294 N ALA B 398 -10.809 -17.393 37.452 1.00 17.14 N ANISOU 1294 N ALA B 398 1723 2139 2651 157 -46 -142 N ATOM 1295 CA ALA B 398 -10.425 -17.167 36.078 1.00 13.53 C ANISOU 1295 CA ALA B 398 1276 1728 2136 192 -39 -143 C ATOM 1296 C ALA B 398 -8.912 -17.248 35.947 1.00 14.72 C ANISOU 1296 C ALA B 398 1418 1913 2261 197 -4 -162 C ATOM 1297 O ALA B 398 -8.172 -16.915 36.887 1.00 13.87 O ANISOU 1297 O ALA B 398 1295 1791 2184 164 24 -158 O ATOM 1298 CB ALA B 398 -10.927 -15.767 35.614 1.00 19.62 C ANISOU 1298 CB ALA B 398 2057 2502 2895 191 1 -89 C ATOM 1299 N PHE B 399 -8.448 -17.719 34.795 1.00 12.56 N ANISOU 1299 N PHE B 399 1156 1683 1934 241 -9 -186 N ATOM 1300 CA PHE B 399 -7.040 -17.566 34.441 1.00 17.51 C ANISOU 1300 CA PHE B 399 1767 2351 2537 253 44 -192 C ATOM 1301 C PHE B 399 -6.825 -16.092 34.102 1.00 23.87 C ANISOU 1301 C PHE B 399 2572 3170 3328 234 114 -132 C ATOM 1302 O PHE B 399 -7.649 -15.484 33.440 1.00 16.64 O ANISOU 1302 O PHE B 399 1684 2255 2381 246 115 -100 O ATOM 1303 CB PHE B 399 -6.688 -18.417 33.229 1.00 20.02 C ANISOU 1303 CB PHE B 399 2104 2712 2790 314 32 -231 C ATOM 1304 CG PHE B 399 -6.803 -19.907 33.476 1.00 23.21 C ANISOU 1304 CG PHE B 399 2512 3096 3211 336 -40 -294 C ATOM 1305 CD1 PHE B 399 -6.205 -20.486 34.571 1.00 20.89 C ANISOU 1305 CD1 PHE B 399 2187 2777 2975 313 -53 -315 C ATOM 1306 CD2 PHE B 399 -7.509 -20.718 32.601 1.00 22.60 C ANISOU 1306 CD2 PHE B 399 2474 3021 3091 380 -101 -330 C ATOM 1307 CE1 PHE B 399 -6.308 -21.870 34.794 1.00 23.65 C ANISOU 1307 CE1 PHE B 399 2543 3100 3342 333 -121 -368 C ATOM 1308 CE2 PHE B 399 -7.608 -22.096 32.817 1.00 23.79 C ANISOU 1308 CE2 PHE B 399 2631 3143 3265 398 -171 -388 C ATOM 1309 CZ PHE B 399 -7.006 -22.662 33.911 1.00 22.58 C ANISOU 1309 CZ PHE B 399 2445 2962 3171 374 -178 -404 C ATOM 1310 N THR B 400 -5.733 -15.516 34.572 1.00 18.97 N ANISOU 1310 N THR B 400 1918 2553 2737 204 165 -116 N ATOM 1311 CA THR B 400 -5.490 -14.111 34.326 1.00 25.23 C ANISOU 1311 CA THR B 400 2709 3347 3530 178 229 -58 C ATOM 1312 C THR B 400 -4.269 -13.949 33.459 1.00 26.48 C ANISOU 1312 C THR B 400 2845 3558 3661 196 294 -44 C ATOM 1313 O THR B 400 -4.107 -12.924 32.810 1.00 23.36 O ANISOU 1313 O THR B 400 2457 3175 3244 190 353 10 O ATOM 1314 CB THR B 400 -5.303 -13.335 35.639 1.00 36.35 C ANISOU 1314 CB THR B 400 4100 4705 5008 118 236 -41 C ATOM 1315 OG1 THR B 400 -4.196 -13.880 36.363 1.00 34.78 O ANISOU 1315 OG1 THR B 400 3861 4507 4849 100 227 -73 O ATOM 1316 CG2 THR B 400 -6.562 -13.441 36.493 1.00 33.55 C ANISOU 1316 CG2 THR B 400 3771 4300 4675 106 188 -48 C ATOM 1317 N GLU B 401 -3.433 -14.982 33.403 1.00 26.09 N ANISOU 1317 N GLU B 401 2767 3536 3611 223 288 -91 N ATOM 1318 CA GLU B 401 -2.213 -14.919 32.613 1.00 24.95 C ANISOU 1318 CA GLU B 401 2589 3444 3448 246 361 -80 C ATOM 1319 C GLU B 401 -1.827 -16.336 32.186 1.00 31.64 C ANISOU 1319 C GLU B 401 3434 4325 4264 307 339 -145 C ATOM 1320 O GLU B 401 -1.848 -17.258 33.001 1.00 28.06 O ANISOU 1320 O GLU B 401 2968 3844 3851 305 275 -194 O ATOM 1321 CB GLU B 401 -1.104 -14.263 33.445 1.00 31.09 C ANISOU 1321 CB GLU B 401 3298 4205 4310 189 397 -57 C ATOM 1322 CG GLU B 401 0.111 -13.777 32.670 1.00 34.96 C ANISOU 1322 CG GLU B 401 3739 4741 4802 194 492 -19 C ATOM 1323 CD GLU B 401 0.998 -12.843 33.500 1.00 44.49 C ANISOU 1323 CD GLU B 401 4881 5918 6107 122 516 17 C ATOM 1324 OE1 GLU B 401 2.243 -12.917 33.373 1.00 46.08 O ANISOU 1324 OE1 GLU B 401 5007 6147 6354 120 564 23 O ATOM 1325 OE2 GLU B 401 0.452 -12.031 34.278 1.00 49.10 O ANISOU 1325 OE2 GLU B 401 5485 6445 6724 69 485 38 O ATOM 1326 N THR B 402 -1.511 -16.515 30.904 1.00 27.28 N ANISOU 1326 N THR B 402 2903 3827 3634 366 390 -144 N ATOM 1327 CA THR B 402 -1.076 -17.817 30.381 1.00 26.63 C ANISOU 1327 CA THR B 402 2827 3777 3515 435 378 -210 C ATOM 1328 C THR B 402 0.022 -17.619 29.342 1.00 36.45 C ANISOU 1328 C THR B 402 4050 5086 4714 479 486 -190 C ATOM 1329 O THR B 402 -0.174 -16.936 28.334 1.00 38.60 O ANISOU 1329 O THR B 402 4366 5391 4908 499 545 -145 O ATOM 1330 CB THR B 402 -2.222 -18.636 29.715 1.00 30.44 C ANISOU 1330 CB THR B 402 3391 4254 3919 487 303 -255 C ATOM 1331 OG1 THR B 402 -2.792 -17.897 28.624 1.00 41.99 O ANISOU 1331 OG1 THR B 402 4915 5745 5295 509 334 -212 O ATOM 1332 CG2 THR B 402 -3.310 -19.003 30.709 1.00 25.07 C ANISOU 1332 CG2 THR B 402 2722 3511 3292 448 202 -275 C ATOM 1333 N VAL B 403 1.182 -18.204 29.598 1.00 26.18 N ANISOU 1333 N VAL B 403 2681 3802 3463 496 516 -219 N ATOM 1334 CA VAL B 403 2.258 -18.174 28.629 1.00 32.64 C ANISOU 1334 CA VAL B 403 3471 4685 4246 548 627 -205 C ATOM 1335 C VAL B 403 2.683 -19.604 28.395 1.00 30.25 C ANISOU 1335 C VAL B 403 3169 4398 3925 626 605 -288 C ATOM 1336 O VAL B 403 3.437 -20.179 29.190 1.00 32.32 O ANISOU 1336 O VAL B 403 3357 4645 4277 620 583 -320 O ATOM 1337 CB VAL B 403 3.443 -17.325 29.117 1.00 40.25 C ANISOU 1337 CB VAL B 403 4328 5656 5311 492 705 -148 C ATOM 1338 CG1 VAL B 403 4.541 -17.315 28.075 1.00 43.96 C ANISOU 1338 CG1 VAL B 403 4759 6195 5749 547 834 -127 C ATOM 1339 CG2 VAL B 403 2.983 -15.903 29.418 1.00 44.61 C ANISOU 1339 CG2 VAL B 403 4886 6177 5887 411 717 -71 C ATOM 1340 N SER B 404 2.154 -20.191 27.327 1.00 34.61 N ANISOU 1340 N SER B 404 3812 4977 4362 702 599 -327 N ATOM 1341 CA SER B 404 2.439 -21.583 26.988 1.00 37.50 C ANISOU 1341 CA SER B 404 4200 5352 4698 786 571 -414 C ATOM 1342 C SER B 404 3.575 -21.652 25.983 1.00 46.95 C ANISOU 1342 C SER B 404 5375 6620 5845 861 702 -412 C ATOM 1343 O SER B 404 3.496 -21.028 24.922 1.00 47.54 O ANISOU 1343 O SER B 404 5503 6741 5818 890 783 -370 O ATOM 1344 CB SER B 404 1.201 -22.240 26.388 1.00 38.64 C ANISOU 1344 CB SER B 404 4461 5476 4744 828 478 -466 C ATOM 1345 OG SER B 404 1.497 -23.535 25.898 1.00 47.67 O ANISOU 1345 OG SER B 404 5639 6626 5846 917 456 -553 O ATOM 1346 N HIS B 405 4.630 -22.393 26.325 1.00 42.27 N ANISOU 1346 N HIS B 405 4703 6033 5323 895 725 -452 N ATOM 1347 CA HIS B 405 5.712 -22.686 25.383 1.00 45.16 C ANISOU 1347 CA HIS B 405 5047 6466 5648 983 851 -464 C ATOM 1348 C HIS B 405 5.723 -24.179 25.086 1.00 45.85 C ANISOU 1348 C HIS B 405 5184 6543 5694 1081 797 -571 C ATOM 1349 O HIS B 405 6.673 -24.878 25.429 1.00 41.65 O ANISOU 1349 O HIS B 405 4573 6011 5239 1119 815 -608 O ATOM 1350 CB HIS B 405 7.072 -22.273 25.947 1.00 40.65 C ANISOU 1350 CB HIS B 405 4324 5914 5207 950 937 -418 C ATOM 1351 CG HIS B 405 7.188 -20.809 26.245 1.00 50.24 C ANISOU 1351 CG HIS B 405 5483 7131 6474 852 990 -316 C ATOM 1352 ND1 HIS B 405 7.659 -20.330 27.450 1.00 50.22 N ANISOU 1352 ND1 HIS B 405 5373 7091 6618 764 956 -282 N ATOM 1353 CD2 HIS B 405 6.894 -19.720 25.496 1.00 51.47 C ANISOU 1353 CD2 HIS B 405 5683 7318 6557 831 1070 -239 C ATOM 1354 CE1 HIS B 405 7.659 -19.009 27.426 1.00 52.00 C ANISOU 1354 CE1 HIS B 405 5575 7319 6861 690 1012 -194 C ATOM 1355 NE2 HIS B 405 7.197 -18.614 26.253 1.00 56.26 N ANISOU 1355 NE2 HIS B 405 6204 7900 7272 729 1085 -163 N ATOM 1356 N ALA B 406 4.651 -24.661 24.464 1.00 52.74 N ANISOU 1356 N ALA B 406 6187 7399 6453 1121 722 -620 N ATOM 1357 CA ALA B 406 4.470 -26.090 24.236 1.00 64.04 C ANISOU 1357 CA ALA B 406 7682 8801 7849 1204 644 -727 C ATOM 1358 C ALA B 406 5.538 -26.624 23.295 1.00 69.84 C ANISOU 1358 C ALA B 406 8416 9594 8525 1321 762 -768 C ATOM 1359 O ALA B 406 6.003 -25.912 22.405 1.00 69.94 O ANISOU 1359 O ALA B 406 8436 9677 8461 1352 898 -718 O ATOM 1360 CB ALA B 406 3.081 -26.367 23.681 1.00 67.62 C ANISOU 1360 CB ALA B 406 8275 9225 8194 1217 537 -765 C ATOM 1361 N GLY B 407 5.928 -27.878 23.493 1.00 71.81 N ANISOU 1361 N GLY B 407 8659 9814 8813 1387 715 -856 N ATOM 1362 CA GLY B 407 6.986 -28.456 22.688 1.00 78.75 C ANISOU 1362 CA GLY B 407 9528 10743 9649 1506 830 -902 C ATOM 1363 C GLY B 407 8.353 -28.114 23.249 1.00 81.96 C ANISOU 1363 C GLY B 407 9768 11183 10190 1491 937 -852 C ATOM 1364 O GLY B 407 9.346 -28.753 22.901 1.00 89.59 O ANISOU 1364 O GLY B 407 10690 12178 11172 1585 1018 -894 O ATOM 1365 N ASN B 408 8.410 -27.101 24.110 1.00 71.13 N ANISOU 1365 N ASN B 408 8303 9805 8920 1374 935 -763 N ATOM 1366 CA ASN B 408 9.640 -26.794 24.833 1.00 62.96 C ANISOU 1366 CA ASN B 408 7101 8784 8037 1342 1001 -718 C ATOM 1367 C ASN B 408 9.679 -27.507 26.191 1.00 65.41 C ANISOU 1367 C ASN B 408 7350 9019 8485 1301 860 -756 C ATOM 1368 O ASN B 408 8.777 -27.342 27.019 1.00 62.94 O ANISOU 1368 O ASN B 408 7070 8648 8197 1215 738 -745 O ATOM 1369 CB ASN B 408 9.812 -25.287 25.009 1.00 52.93 C ANISOU 1369 CB ASN B 408 5760 7544 6807 1241 1077 -603 C ATOM 1370 CG ASN B 408 10.942 -24.941 25.964 1.00 68.44 C ANISOU 1370 CG ASN B 408 7551 9505 8950 1185 1103 -557 C ATOM 1371 OD1 ASN B 408 11.684 -25.819 26.413 1.00 68.21 O ANISOU 1371 OD1 ASN B 408 7447 9460 9011 1231 1078 -608 O ATOM 1372 ND2 ASN B 408 11.079 -23.656 26.280 1.00 74.13 N ANISOU 1372 ND2 ASN B 408 8207 10234 9726 1085 1146 -462 N ATOM 1373 N ALA B 409 10.729 -28.291 26.417 1.00 59.28 N ANISOU 1373 N ALA B 409 6484 8243 7795 1366 882 -797 N ATOM 1374 CA ALA B 409 10.794 -29.165 27.588 1.00 54.22 C ANISOU 1374 CA ALA B 409 5804 7528 7269 1350 745 -842 C ATOM 1375 C ALA B 409 11.483 -28.535 28.790 1.00 52.24 C ANISOU 1375 C ALA B 409 5411 7262 7176 1257 723 -777 C ATOM 1376 O ALA B 409 11.225 -28.921 29.931 1.00 54.06 O ANISOU 1376 O ALA B 409 5631 7424 7483 1206 591 -790 O ATOM 1377 CB ALA B 409 11.477 -30.483 27.226 1.00 57.13 C ANISOU 1377 CB ALA B 409 6167 7891 7648 1479 755 -931 C ATOM 1378 N GLU B 410 12.364 -27.576 28.530 1.00 50.46 N ANISOU 1378 N GLU B 410 5078 7097 6998 1234 851 -706 N ATOM 1379 CA GLU B 410 13.144 -26.948 29.588 1.00 58.92 C ANISOU 1379 CA GLU B 410 6006 8155 8227 1149 832 -647 C ATOM 1380 C GLU B 410 12.344 -25.864 30.320 1.00 61.93 C ANISOU 1380 C GLU B 410 6416 8503 8612 1017 766 -583 C ATOM 1381 O GLU B 410 12.372 -25.790 31.550 1.00 56.91 O ANISOU 1381 O GLU B 410 5737 7813 8073 945 657 -573 O ATOM 1382 CB GLU B 410 14.442 -26.370 29.020 1.00 72.71 C ANISOU 1382 CB GLU B 410 7613 9973 10041 1175 994 -594 C ATOM 1383 CG GLU B 410 15.284 -27.371 28.211 1.00 87.91 C ANISOU 1383 CG GLU B 410 9504 11940 11960 1317 1086 -654 C ATOM 1384 CD GLU B 410 15.899 -28.491 29.057 1.00 96.90 C ANISOU 1384 CD GLU B 410 10569 13028 13220 1363 985 -716 C ATOM 1385 OE1 GLU B 410 17.028 -28.924 28.734 1.00101.51 O ANISOU 1385 OE1 GLU B 410 11043 13648 13880 1448 1073 -730 O ATOM 1386 OE2 GLU B 410 15.265 -28.944 30.036 1.00 96.74 O ANISOU 1386 OE2 GLU B 410 10602 12934 13223 1318 822 -746 O ATOM 1387 N ASP B 411 11.648 -25.024 29.554 1.00 60.91 N ANISOU 1387 N ASP B 411 6364 8405 8373 992 832 -541 N ATOM 1388 CA ASP B 411 10.709 -24.050 30.110 1.00 57.85 C ANISOU 1388 CA ASP B 411 6028 7983 7970 882 771 -490 C ATOM 1389 C ASP B 411 9.381 -24.105 29.356 1.00 44.28 C ANISOU 1389 C ASP B 411 4465 6264 6097 902 754 -509 C ATOM 1390 O ASP B 411 9.177 -23.386 28.370 1.00 43.29 O ANISOU 1390 O ASP B 411 4381 6185 5881 911 851 -467 O ATOM 1391 CB ASP B 411 11.293 -22.634 30.056 1.00 64.53 C ANISOU 1391 CB ASP B 411 6786 8861 8873 806 869 -394 C ATOM 1392 CG ASP B 411 10.287 -21.568 30.473 1.00 71.29 C ANISOU 1392 CG ASP B 411 7707 9682 9699 705 820 -342 C ATOM 1393 OD1 ASP B 411 9.338 -21.896 31.229 1.00 67.07 O ANISOU 1393 OD1 ASP B 411 7247 9089 9148 673 695 -375 O ATOM 1394 OD2 ASP B 411 10.446 -20.401 30.038 1.00 74.95 O ANISOU 1394 OD2 ASP B 411 8147 10173 10158 659 913 -266 O ATOM 1395 N PRO B 412 8.470 -24.971 29.808 1.00 34.32 N ANISOU 1395 N PRO B 412 3287 4945 4806 910 625 -570 N ATOM 1396 CA PRO B 412 7.182 -25.094 29.118 1.00 31.55 C ANISOU 1396 CA PRO B 412 3076 4588 4324 928 592 -593 C ATOM 1397 C PRO B 412 6.302 -23.840 29.299 1.00 30.19 C ANISOU 1397 C PRO B 412 2939 4406 4125 834 584 -521 C ATOM 1398 O PRO B 412 5.268 -23.717 28.631 1.00 32.01 O ANISOU 1398 O PRO B 412 3274 4638 4250 845 568 -524 O ATOM 1399 CB PRO B 412 6.533 -26.308 29.792 1.00 31.21 C ANISOU 1399 CB PRO B 412 3086 4474 4297 942 449 -665 C ATOM 1400 CG PRO B 412 7.648 -26.979 30.569 1.00 40.44 C ANISOU 1400 CG PRO B 412 4153 5625 5585 962 429 -691 C ATOM 1401 CD PRO B 412 8.584 -25.892 30.949 1.00 39.70 C ANISOU 1401 CD PRO B 412 3940 5564 5579 903 504 -617 C ATOM 1402 N GLY B 413 6.703 -22.928 30.182 1.00 30.30 N ANISOU 1402 N GLY B 413 2870 4405 4236 747 589 -460 N ATOM 1403 CA GLY B 413 5.919 -21.718 30.435 1.00 19.70 C ANISOU 1403 CA GLY B 413 1559 3045 2881 660 582 -394 C ATOM 1404 C GLY B 413 5.099 -21.769 31.722 1.00 24.02 C ANISOU 1404 C GLY B 413 2130 3520 3477 590 456 -402 C ATOM 1405 O GLY B 413 5.221 -22.717 32.497 1.00 29.68 O ANISOU 1405 O GLY B 413 2833 4199 4246 600 374 -451 O ATOM 1406 N TYR B 414 4.246 -20.762 31.947 1.00 20.66 N ANISOU 1406 N TYR B 414 1744 3072 3032 522 444 -352 N ATOM 1407 CA TYR B 414 3.537 -20.634 33.229 1.00 19.74 C ANISOU 1407 CA TYR B 414 1644 2890 2966 452 346 -350 C ATOM 1408 C TYR B 414 2.131 -20.071 33.047 1.00 27.48 C ANISOU 1408 C TYR B 414 2711 3850 3882 425 321 -325 C ATOM 1409 O TYR B 414 1.782 -19.556 31.977 1.00 28.46 O ANISOU 1409 O TYR B 414 2875 4010 3929 447 379 -299 O ATOM 1410 CB TYR B 414 4.303 -19.696 34.165 1.00 22.00 C ANISOU 1410 CB TYR B 414 1851 3158 3350 377 358 -303 C ATOM 1411 CG TYR B 414 4.206 -18.263 33.707 1.00 36.48 C ANISOU 1411 CG TYR B 414 3684 5008 5169 331 435 -231 C ATOM 1412 CD1 TYR B 414 3.281 -17.396 34.272 1.00 37.95 C ANISOU 1412 CD1 TYR B 414 3918 5150 5352 268 401 -198 C ATOM 1413 CD2 TYR B 414 5.004 -17.790 32.675 1.00 47.97 C ANISOU 1413 CD2 TYR B 414 5097 6521 6611 356 548 -194 C ATOM 1414 CE1 TYR B 414 3.173 -16.083 33.842 1.00 41.54 C ANISOU 1414 CE1 TYR B 414 4377 5611 5796 229 467 -132 C ATOM 1415 CE2 TYR B 414 4.902 -16.479 32.235 1.00 51.49 C ANISOU 1415 CE2 TYR B 414 5546 6974 7042 312 619 -121 C ATOM 1416 CZ TYR B 414 3.987 -15.634 32.824 1.00 45.49 C ANISOU 1416 CZ TYR B 414 4835 6164 6284 249 573 -92 C ATOM 1417 OH TYR B 414 3.881 -14.341 32.388 1.00 46.94 O ANISOU 1417 OH TYR B 414 5028 6350 6460 209 639 -19 O ATOM 1418 N TYR B 415 1.325 -20.160 34.099 1.00 19.59 N ANISOU 1418 N TYR B 415 1738 2792 2912 378 237 -332 N ATOM 1419 CA TYR B 415 -0.016 -19.603 34.062 1.00 20.19 C ANISOU 1419 CA TYR B 415 1881 2845 2947 350 213 -306 C ATOM 1420 C TYR B 415 -0.490 -19.262 35.465 1.00 16.96 C ANISOU 1420 C TYR B 415 1473 2375 2597 282 156 -291 C ATOM 1421 O TYR B 415 0.002 -19.813 36.458 1.00 18.84 O ANISOU 1421 O TYR B 415 1682 2585 2892 267 110 -315 O ATOM 1422 CB TYR B 415 -0.999 -20.565 33.381 1.00 22.37 C ANISOU 1422 CB TYR B 415 2226 3118 3155 404 161 -350 C ATOM 1423 CG TYR B 415 -1.256 -21.883 34.134 1.00 22.24 C ANISOU 1423 CG TYR B 415 2219 3057 3174 414 69 -406 C ATOM 1424 CD1 TYR B 415 -2.316 -21.999 35.032 1.00 22.37 C ANISOU 1424 CD1 TYR B 415 2264 3018 3218 371 1 -401 C ATOM 1425 CD2 TYR B 415 -0.453 -22.996 33.923 1.00 22.43 C ANISOU 1425 CD2 TYR B 415 2224 3092 3206 470 57 -461 C ATOM 1426 CE1 TYR B 415 -2.569 -23.179 35.701 1.00 16.39 C ANISOU 1426 CE1 TYR B 415 1518 2216 2494 377 -76 -441 C ATOM 1427 CE2 TYR B 415 -0.689 -24.201 34.588 1.00 23.91 C ANISOU 1427 CE2 TYR B 415 2425 3231 3428 480 -28 -507 C ATOM 1428 CZ TYR B 415 -1.756 -24.285 35.468 1.00 24.13 C ANISOU 1428 CZ TYR B 415 2485 3203 3482 431 -95 -494 C ATOM 1429 OH TYR B 415 -1.981 -25.459 36.139 1.00 22.65 O ANISOU 1429 OH TYR B 415 2312 2965 3331 436 -174 -531 O ATOM 1430 N LYS B 416 -1.464 -18.367 35.537 1.00 18.03 N ANISOU 1430 N LYS B 416 1646 2490 2714 247 160 -252 N ATOM 1431 CA LYS B 416 -1.943 -17.858 36.811 1.00 17.94 C ANISOU 1431 CA LYS B 416 1643 2424 2748 187 125 -234 C ATOM 1432 C LYS B 416 -3.450 -17.931 36.852 1.00 17.89 C ANISOU 1432 C LYS B 416 1694 2390 2715 186 88 -230 C ATOM 1433 O LYS B 416 -4.126 -17.652 35.863 1.00 20.02 O ANISOU 1433 O LYS B 416 1992 2680 2936 211 106 -214 O ATOM 1434 CB LYS B 416 -1.488 -16.404 37.005 1.00 20.87 C ANISOU 1434 CB LYS B 416 1991 2791 3149 137 180 -182 C ATOM 1435 CG LYS B 416 0.033 -16.254 36.924 1.00 25.96 C ANISOU 1435 CG LYS B 416 2563 3463 3837 131 220 -178 C ATOM 1436 CD LYS B 416 0.481 -14.828 37.183 1.00 40.52 C ANISOU 1436 CD LYS B 416 4381 5290 5724 72 263 -126 C ATOM 1437 CE LYS B 416 2.013 -14.740 37.103 1.00 44.62 C ANISOU 1437 CE LYS B 416 4813 5835 6305 62 299 -119 C ATOM 1438 NZ LYS B 416 2.505 -13.364 37.391 1.00 45.40 N ANISOU 1438 NZ LYS B 416 4881 5907 6460 -4 332 -68 N ATOM 1439 N GLN B 417 -3.976 -18.305 38.004 1.00 16.73 N ANISOU 1439 N GLN B 417 1561 2193 2601 159 37 -241 N ATOM 1440 CA GLN B 417 -5.417 -18.371 38.165 1.00 18.46 C ANISOU 1440 CA GLN B 417 1820 2381 2811 154 8 -231 C ATOM 1441 C GLN B 417 -5.726 -17.609 39.426 1.00 18.73 C ANISOU 1441 C GLN B 417 1866 2371 2880 103 13 -205 C ATOM 1442 O GLN B 417 -4.995 -17.705 40.415 1.00 16.10 O ANISOU 1442 O GLN B 417 1524 2018 2577 79 -1 -216 O ATOM 1443 CB GLN B 417 -5.909 -19.826 38.306 1.00 15.00 C ANISOU 1443 CB GLN B 417 1396 1924 2378 178 -59 -272 C ATOM 1444 CG GLN B 417 -7.440 -19.934 38.245 1.00 12.87 C ANISOU 1444 CG GLN B 417 1154 1628 2109 175 -88 -259 C ATOM 1445 CD GLN B 417 -7.966 -21.366 38.449 1.00 20.87 C ANISOU 1445 CD GLN B 417 2177 2610 3142 189 -157 -294 C ATOM 1446 OE1 GLN B 417 -8.990 -21.754 37.872 1.00 20.42 O ANISOU 1446 OE1 GLN B 417 2132 2543 3082 203 -193 -297 O ATOM 1447 NE2 GLN B 417 -7.266 -22.146 39.268 1.00 14.76 N ANISOU 1447 NE2 GLN B 417 1397 1816 2394 183 -183 -317 N ATOM 1448 N THR B 418 -6.817 -16.865 39.394 1.00 14.66 N ANISOU 1448 N THR B 418 1374 1837 2360 93 30 -172 N ATOM 1449 CA THR B 418 -7.245 -16.129 40.553 1.00 17.64 C ANISOU 1449 CA THR B 418 1772 2169 2763 54 42 -151 C ATOM 1450 C THR B 418 -8.551 -16.692 41.016 1.00 12.21 C ANISOU 1450 C THR B 418 1104 1449 2086 57 16 -149 C ATOM 1451 O THR B 418 -9.442 -16.908 40.210 1.00 19.42 O ANISOU 1451 O THR B 418 2014 2372 2991 81 5 -142 O ATOM 1452 CB THR B 418 -7.462 -14.659 40.182 1.00 24.82 C ANISOU 1452 CB THR B 418 2688 3075 3667 41 93 -109 C ATOM 1453 OG1 THR B 418 -6.193 -14.091 39.899 1.00 20.62 O ANISOU 1453 OG1 THR B 418 2133 2565 3138 27 122 -104 O ATOM 1454 CG2 THR B 418 -8.113 -13.903 41.324 1.00 22.16 C ANISOU 1454 CG2 THR B 418 2383 2686 3353 12 108 -91 C ATOM 1455 N VAL B 419 -8.666 -16.929 42.317 1.00 16.59 N ANISOU 1455 N VAL B 419 1679 1964 2659 34 6 -153 N ATOM 1456 CA VAL B 419 -9.908 -17.460 42.870 1.00 16.06 C ANISOU 1456 CA VAL B 419 1626 1864 2610 33 -6 -142 C ATOM 1457 C VAL B 419 -10.499 -16.472 43.859 1.00 20.35 C ANISOU 1457 C VAL B 419 2201 2370 3162 12 40 -114 C ATOM 1458 O VAL B 419 -9.805 -15.986 44.755 1.00 15.65 O ANISOU 1458 O VAL B 419 1633 1756 2557 -10 50 -120 O ATOM 1459 CB VAL B 419 -9.682 -18.821 43.559 1.00 19.67 C ANISOU 1459 CB VAL B 419 2092 2304 3079 31 -53 -167 C ATOM 1460 CG1 VAL B 419 -10.976 -19.339 44.163 1.00 17.48 C ANISOU 1460 CG1 VAL B 419 1824 1989 2828 24 -54 -145 C ATOM 1461 CG2 VAL B 419 -9.091 -19.850 42.556 1.00 17.21 C ANISOU 1461 CG2 VAL B 419 1754 2024 2761 61 -99 -202 C ATOM 1462 N TYR B 420 -11.771 -16.145 43.689 1.00 16.14 N ANISOU 1462 N TYR B 420 1662 1824 2647 20 63 -86 N ATOM 1463 CA TYR B 420 -12.463 -15.359 44.710 1.00 15.54 C ANISOU 1463 CA TYR B 420 1616 1708 2580 9 113 -62 C ATOM 1464 C TYR B 420 -13.180 -16.304 45.673 1.00 17.73 C ANISOU 1464 C TYR B 420 1904 1956 2875 4 111 -56 C ATOM 1465 O TYR B 420 -14.088 -17.018 45.269 1.00 19.67 O ANISOU 1465 O TYR B 420 2117 2203 3156 13 95 -43 O ATOM 1466 CB TYR B 420 -13.480 -14.416 44.078 1.00 13.32 C ANISOU 1466 CB TYR B 420 1318 1424 2320 27 148 -29 C ATOM 1467 CG TYR B 420 -12.912 -13.237 43.291 1.00 12.72 C ANISOU 1467 CG TYR B 420 1243 1364 2226 30 165 -21 C ATOM 1468 CD1 TYR B 420 -11.549 -12.923 43.313 1.00 12.53 C ANISOU 1468 CD1 TYR B 420 1232 1351 2177 11 160 -40 C ATOM 1469 CD2 TYR B 420 -13.768 -12.405 42.566 1.00 22.53 C ANISOU 1469 CD2 TYR B 420 2471 2605 3485 50 187 12 C ATOM 1470 CE1 TYR B 420 -11.054 -11.794 42.602 1.00 15.42 C ANISOU 1470 CE1 TYR B 420 1597 1727 2537 8 184 -22 C ATOM 1471 CE2 TYR B 420 -13.301 -11.318 41.868 1.00 19.17 C ANISOU 1471 CE2 TYR B 420 2053 2187 3045 52 205 28 C ATOM 1472 CZ TYR B 420 -11.951 -11.009 41.893 1.00 18.53 C ANISOU 1472 CZ TYR B 420 1985 2116 2940 29 208 13 C ATOM 1473 OH TYR B 420 -11.542 -9.925 41.174 1.00 21.41 O ANISOU 1473 OH TYR B 420 2353 2483 3297 27 232 39 O ATOM 1474 N VAL B 421 -12.784 -16.287 46.944 1.00 17.14 N ANISOU 1474 N VAL B 421 1881 1854 2779 -12 125 -62 N ATOM 1475 CA VAL B 421 -13.431 -17.104 47.984 1.00 15.49 C ANISOU 1475 CA VAL B 421 1695 1614 2576 -18 137 -47 C ATOM 1476 C VAL B 421 -14.430 -16.268 48.789 1.00 17.79 C ANISOU 1476 C VAL B 421 2015 1873 2870 -12 215 -17 C ATOM 1477 O VAL B 421 -14.069 -15.203 49.300 1.00 19.08 O ANISOU 1477 O VAL B 421 2226 2022 3001 -13 246 -25 O ATOM 1478 CB VAL B 421 -12.371 -17.656 48.971 1.00 21.95 C ANISOU 1478 CB VAL B 421 2565 2419 3355 -33 103 -70 C ATOM 1479 CG1 VAL B 421 -13.031 -18.373 50.152 1.00 22.17 C ANISOU 1479 CG1 VAL B 421 2635 2412 3377 -38 127 -45 C ATOM 1480 CG2 VAL B 421 -11.376 -18.573 48.249 1.00 13.53 C ANISOU 1480 CG2 VAL B 421 1467 1381 2294 -31 30 -100 C ATOM 1481 N ASN B 422 -15.680 -16.731 48.886 1.00 14.45 N ANISOU 1481 N ASN B 422 1561 1437 2491 -5 246 17 N ATOM 1482 CA ASN B 422 -16.687 -16.051 49.707 1.00 17.15 C ANISOU 1482 CA ASN B 422 1925 1751 2842 7 332 48 C ATOM 1483 C ASN B 422 -16.977 -14.614 49.248 1.00 21.12 C ANISOU 1483 C ASN B 422 2420 2253 3352 28 372 52 C ATOM 1484 O ASN B 422 -17.097 -13.708 50.075 1.00 19.31 O ANISOU 1484 O ASN B 422 2246 1996 3095 39 432 52 O ATOM 1485 CB ASN B 422 -16.232 -16.029 51.174 1.00 12.12 C ANISOU 1485 CB ASN B 422 1380 1085 2141 1 364 41 C ATOM 1486 CG ASN B 422 -17.343 -15.658 52.123 1.00 18.58 C ANISOU 1486 CG ASN B 422 2225 1873 2962 19 462 76 C ATOM 1487 OD1 ASN B 422 -18.522 -15.868 51.835 1.00 21.09 O ANISOU 1487 OD1 ASN B 422 2478 2189 3347 29 503 115 O ATOM 1488 ND2 ASN B 422 -16.975 -15.103 53.269 1.00 18.05 N ANISOU 1488 ND2 ASN B 422 2255 1781 2825 25 501 63 N ATOM 1489 N PRO B 423 -17.123 -14.403 47.928 1.00 16.75 N ANISOU 1489 N PRO B 423 1805 1726 2833 36 336 54 N ATOM 1490 CA PRO B 423 -17.513 -13.072 47.447 1.00 13.72 C ANISOU 1490 CA PRO B 423 1413 1336 2463 58 372 66 C ATOM 1491 C PRO B 423 -18.845 -12.607 48.038 1.00 20.61 C ANISOU 1491 C PRO B 423 2273 2178 3379 83 451 101 C ATOM 1492 O PRO B 423 -19.084 -11.411 48.121 1.00 22.12 O ANISOU 1492 O PRO B 423 2485 2348 3571 105 497 107 O ATOM 1493 CB PRO B 423 -17.644 -13.276 45.921 1.00 18.00 C ANISOU 1493 CB PRO B 423 1890 1913 3035 66 312 72 C ATOM 1494 CG PRO B 423 -17.967 -14.780 45.777 1.00 17.92 C ANISOU 1494 CG PRO B 423 1839 1915 3055 55 264 71 C ATOM 1495 CD PRO B 423 -17.034 -15.382 46.823 1.00 15.88 C ANISOU 1495 CD PRO B 423 1638 1647 2749 31 262 47 C ATOM 1496 N SER B 424 -19.702 -13.532 48.457 1.00 20.74 N ANISOU 1496 N SER B 424 2255 2188 3437 82 471 127 N ATOM 1497 CA SER B 424 -20.968 -13.157 49.100 1.00 24.38 C ANISOU 1497 CA SER B 424 2696 2621 3946 108 560 165 C ATOM 1498 C SER B 424 -20.772 -12.654 50.536 1.00 23.09 C ANISOU 1498 C SER B 424 2626 2425 3720 117 642 156 C ATOM 1499 O SER B 424 -21.703 -12.186 51.155 1.00 22.59 O ANISOU 1499 O SER B 424 2563 2338 3682 147 731 182 O ATOM 1500 CB SER B 424 -21.943 -14.343 49.115 1.00 30.23 C ANISOU 1500 CB SER B 424 3362 3362 4761 97 560 202 C ATOM 1501 OG SER B 424 -22.396 -14.657 47.814 1.00 34.79 O ANISOU 1501 OG SER B 424 3853 3960 5406 97 487 211 O ATOM 1502 N GLU B 425 -19.571 -12.804 51.074 1.00 22.66 N ANISOU 1502 N GLU B 425 2653 2371 3586 95 609 119 N ATOM 1503 CA GLU B 425 -19.278 -12.359 52.428 1.00 20.68 C ANISOU 1503 CA GLU B 425 2507 2088 3262 103 667 103 C ATOM 1504 C GLU B 425 -20.189 -12.968 53.482 1.00 25.67 C ANISOU 1504 C GLU B 425 3154 2703 3897 116 751 140 C ATOM 1505 O GLU B 425 -20.671 -12.278 54.373 1.00 24.71 O ANISOU 1505 O GLU B 425 3089 2552 3747 148 843 145 O ATOM 1506 CB GLU B 425 -19.331 -10.822 52.489 1.00 22.30 C ANISOU 1506 CB GLU B 425 2754 2266 3454 133 711 87 C ATOM 1507 CG GLU B 425 -18.230 -10.199 51.628 1.00 21.53 C ANISOU 1507 CG GLU B 425 2660 2180 3342 113 633 54 C ATOM 1508 CD GLU B 425 -18.184 -8.652 51.711 1.00 34.76 C ANISOU 1508 CD GLU B 425 4383 3816 5007 136 668 38 C ATOM 1509 OE1 GLU B 425 -19.127 -8.034 52.216 1.00 39.90 O ANISOU 1509 OE1 GLU B 425 5050 4436 5673 176 751 52 O ATOM 1510 OE2 GLU B 425 -17.190 -8.060 51.249 1.00 41.37 O ANISOU 1510 OE2 GLU B 425 5240 4651 5827 114 614 13 O ATOM 1511 N LYS B 426 -20.434 -14.262 53.369 1.00 22.07 N ANISOU 1511 N LYS B 426 2647 2261 3477 92 724 167 N ATOM 1512 CA LYS B 426 -21.159 -14.995 54.397 1.00 22.25 C ANISOU 1512 CA LYS B 426 2686 2266 3500 94 801 209 C ATOM 1513 C LYS B 426 -20.228 -15.297 55.576 1.00 28.98 C ANISOU 1513 C LYS B 426 3665 3104 4242 84 796 187 C ATOM 1514 O LYS B 426 -19.010 -15.235 55.430 1.00 29.95 O ANISOU 1514 O LYS B 426 3835 3234 4311 66 709 141 O ATOM 1515 CB LYS B 426 -21.689 -16.287 53.795 1.00 25.25 C ANISOU 1515 CB LYS B 426 2967 2658 3968 65 760 246 C ATOM 1516 CG LYS B 426 -22.612 -16.044 52.597 1.00 25.39 C ANISOU 1516 CG LYS B 426 2862 2690 4097 75 745 266 C ATOM 1517 CD LYS B 426 -23.946 -15.461 53.042 1.00 36.23 C ANISOU 1517 CD LYS B 426 4193 4044 5530 110 865 313 C ATOM 1518 CE LYS B 426 -24.810 -15.127 51.833 1.00 43.34 C ANISOU 1518 CE LYS B 426 4971 4955 6541 123 836 331 C ATOM 1519 NZ LYS B 426 -26.242 -14.994 52.215 1.00 54.90 N ANISOU 1519 NZ LYS B 426 6357 6401 8100 149 941 389 N ATOM 1520 N SER B 427 -20.789 -15.583 56.747 1.00 25.68 N ANISOU 1520 N SER B 427 3304 2664 3789 97 888 222 N ATOM 1521 CA SER B 427 -19.988 -16.129 57.847 1.00 29.10 C ANISOU 1521 CA SER B 427 3857 3084 4117 86 872 212 C ATOM 1522 C SER B 427 -19.842 -17.630 57.691 1.00 30.40 C ANISOU 1522 C SER B 427 3981 3254 4315 48 811 242 C ATOM 1523 O SER B 427 -20.818 -18.363 57.843 1.00 29.53 O ANISOU 1523 O SER B 427 3817 3136 4266 42 871 302 O ATOM 1524 CB SER B 427 -20.653 -15.861 59.197 1.00 31.49 C ANISOU 1524 CB SER B 427 4251 3359 4353 121 1002 241 C ATOM 1525 OG SER B 427 -20.478 -14.511 59.559 1.00 42.19 O ANISOU 1525 OG SER B 427 5685 4698 5646 159 1040 197 O ATOM 1526 N LEU B 428 -18.629 -18.098 57.415 1.00 24.20 N ANISOU 1526 N LEU B 428 3219 2478 3497 23 693 202 N ATOM 1527 CA LEU B 428 -18.402 -19.538 57.257 1.00 22.43 C ANISOU 1527 CA LEU B 428 2965 2254 3305 -9 627 224 C ATOM 1528 C LEU B 428 -17.514 -20.054 58.375 1.00 23.67 C ANISOU 1528 C LEU B 428 3243 2390 3358 -14 594 218 C ATOM 1529 O LEU B 428 -16.676 -19.325 58.900 1.00 25.36 O ANISOU 1529 O LEU B 428 3549 2601 3484 -1 570 174 O ATOM 1530 CB LEU B 428 -17.714 -19.826 55.910 1.00 17.91 C ANISOU 1530 CB LEU B 428 2311 1708 2787 -28 510 184 C ATOM 1531 CG LEU B 428 -18.336 -19.168 54.670 1.00 24.02 C ANISOU 1531 CG LEU B 428 2979 2504 3642 -19 515 178 C ATOM 1532 CD1 LEU B 428 -17.488 -19.442 53.444 1.00 19.11 C ANISOU 1532 CD1 LEU B 428 2305 1910 3045 -32 404 135 C ATOM 1533 CD2 LEU B 428 -19.779 -19.624 54.437 1.00 22.00 C ANISOU 1533 CD2 LEU B 428 2635 2240 3485 -22 575 237 C ATOM 1534 N THR B 429 -17.669 -21.322 58.725 1.00 22.79 N ANISOU 1534 N THR B 429 3134 2262 3262 -33 582 262 N ATOM 1535 CA THR B 429 -16.716 -21.925 59.634 1.00 26.26 C ANISOU 1535 CA THR B 429 3684 2683 3611 -38 526 256 C ATOM 1536 C THR B 429 -16.094 -23.144 58.980 1.00 23.89 C ANISOU 1536 C THR B 429 3331 2382 3366 -64 411 250 C ATOM 1537 O THR B 429 -16.706 -23.799 58.127 1.00 23.12 O ANISOU 1537 O THR B 429 3129 2286 3371 -81 402 272 O ATOM 1538 CB THR B 429 -17.335 -22.257 60.999 1.00 38.40 C ANISOU 1538 CB THR B 429 5319 4190 5080 -27 625 319 C ATOM 1539 OG1 THR B 429 -18.365 -23.224 60.823 1.00 29.94 O ANISOU 1539 OG1 THR B 429 4169 3104 4101 -48 677 390 O ATOM 1540 CG2 THR B 429 -17.929 -20.980 61.652 1.00 43.31 C ANISOU 1540 CG2 THR B 429 6003 4812 5640 10 746 316 C ATOM 1541 N ASN B 430 -14.855 -23.418 59.353 1.00 20.07 N ANISOU 1541 N ASN B 430 2916 1892 2815 -64 318 215 N ATOM 1542 CA ASN B 430 -14.102 -24.497 58.740 1.00 22.47 C ANISOU 1542 CA ASN B 430 3176 2195 3166 -79 204 198 C ATOM 1543 C ASN B 430 -14.126 -24.446 57.211 1.00 21.56 C ANISOU 1543 C ASN B 430 2934 2111 3147 -85 161 163 C ATOM 1544 O ASN B 430 -14.302 -25.469 56.534 1.00 20.36 O ANISOU 1544 O ASN B 430 2717 1951 3070 -98 116 173 O ATOM 1545 CB ASN B 430 -14.656 -25.832 59.208 1.00 32.16 C ANISOU 1545 CB ASN B 430 4414 3383 4421 -95 216 265 C ATOM 1546 CG ASN B 430 -13.581 -26.871 59.348 1.00 52.46 C ANISOU 1546 CG ASN B 430 7020 5933 6978 -98 100 251 C ATOM 1547 OD1 ASN B 430 -12.547 -26.619 59.969 1.00 65.76 O ANISOU 1547 OD1 ASN B 430 8787 7618 8580 -84 43 220 O ATOM 1548 ND2 ASN B 430 -13.811 -28.050 58.777 1.00 59.54 N ANISOU 1548 ND2 ASN B 430 7854 6808 7960 -114 56 271 N ATOM 1549 N ALA B 431 -13.990 -23.247 56.673 1.00 21.10 N ANISOU 1549 N ALA B 431 2849 2084 3084 -75 177 123 N ATOM 1550 CA ALA B 431 -13.998 -23.046 55.231 1.00 18.65 C ANISOU 1550 CA ALA B 431 2432 1806 2846 -76 143 92 C ATOM 1551 C ALA B 431 -12.664 -23.546 54.671 1.00 24.19 C ANISOU 1551 C ALA B 431 3119 2523 3548 -75 32 42 C ATOM 1552 O ALA B 431 -11.598 -23.231 55.220 1.00 21.84 O ANISOU 1552 O ALA B 431 2881 2226 3192 -70 -10 13 O ATOM 1553 CB ALA B 431 -14.189 -21.526 54.909 1.00 13.26 C ANISOU 1553 CB ALA B 431 1738 1147 2151 -63 197 71 C ATOM 1554 N LYS B 432 -12.716 -24.350 53.612 1.00 19.49 N ANISOU 1554 N LYS B 432 2447 1936 3021 -76 -19 31 N ATOM 1555 CA LYS B 432 -11.497 -24.796 52.950 1.00 22.60 C ANISOU 1555 CA LYS B 432 2817 2348 3421 -67 -111 -19 C ATOM 1556 C LYS B 432 -11.589 -24.622 51.442 1.00 17.99 C ANISOU 1556 C LYS B 432 2147 1802 2888 -57 -128 -49 C ATOM 1557 O LYS B 432 -12.611 -24.920 50.835 1.00 20.48 O ANISOU 1557 O LYS B 432 2413 2112 3255 -61 -111 -30 O ATOM 1558 CB LYS B 432 -11.221 -26.274 53.270 1.00 29.93 C ANISOU 1558 CB LYS B 432 3764 3241 4368 -68 -175 -8 C ATOM 1559 CG LYS B 432 -11.027 -26.543 54.759 1.00 39.18 C ANISOU 1559 CG LYS B 432 5034 4375 5479 -74 -169 26 C ATOM 1560 CD LYS B 432 -11.051 -28.029 55.074 1.00 54.68 C ANISOU 1560 CD LYS B 432 7013 6291 7470 -78 -219 54 C ATOM 1561 CE LYS B 432 -11.051 -28.257 56.578 1.00 63.32 C ANISOU 1561 CE LYS B 432 8216 7347 8496 -83 -200 101 C ATOM 1562 NZ LYS B 432 -9.908 -27.535 57.210 1.00 65.93 N ANISOU 1562 NZ LYS B 432 8611 7694 8747 -69 -238 66 N ATOM 1563 N LEU B 433 -10.499 -24.174 50.841 1.00 16.92 N ANISOU 1563 N LEU B 433 1992 1701 2737 -44 -166 -95 N ATOM 1564 CA LEU B 433 -10.409 -24.057 49.394 1.00 22.61 C ANISOU 1564 CA LEU B 433 2643 2459 3488 -28 -183 -125 C ATOM 1565 C LEU B 433 -9.522 -25.181 48.849 1.00 18.32 C ANISOU 1565 C LEU B 433 2078 1918 2963 -9 -261 -163 C ATOM 1566 O LEU B 433 -8.421 -25.405 49.354 1.00 20.90 O ANISOU 1566 O LEU B 433 2428 2243 3270 -2 -301 -182 O ATOM 1567 CB LEU B 433 -9.822 -22.680 49.012 1.00 17.06 C ANISOU 1567 CB LEU B 433 1929 1794 2758 -26 -154 -144 C ATOM 1568 CG LEU B 433 -9.461 -22.584 47.523 1.00 15.32 C ANISOU 1568 CG LEU B 433 1648 1618 2555 -5 -173 -175 C ATOM 1569 CD1 LEU B 433 -10.742 -22.641 46.680 1.00 15.13 C ANISOU 1569 CD1 LEU B 433 1590 1598 2562 0 -154 -157 C ATOM 1570 CD2 LEU B 433 -8.638 -21.348 47.206 1.00 16.57 C ANISOU 1570 CD2 LEU B 433 1796 1809 2690 -6 -149 -188 C ATOM 1571 N LYS B 434 -10.003 -25.901 47.834 1.00 19.70 N ANISOU 1571 N LYS B 434 2212 2096 3178 4 -289 -176 N ATOM 1572 CA LYS B 434 -9.162 -26.869 47.128 1.00 20.66 C ANISOU 1572 CA LYS B 434 2313 2222 3313 33 -357 -221 C ATOM 1573 C LYS B 434 -8.991 -26.458 45.674 1.00 16.41 C ANISOU 1573 C LYS B 434 1729 1734 2771 60 -355 -257 C ATOM 1574 O LYS B 434 -9.964 -26.212 44.961 1.00 21.43 O ANISOU 1574 O LYS B 434 2344 2378 3420 58 -338 -247 O ATOM 1575 CB LYS B 434 -9.752 -28.288 47.209 1.00 24.34 C ANISOU 1575 CB LYS B 434 2786 2636 3825 31 -407 -214 C ATOM 1576 CG LYS B 434 -8.874 -29.348 46.517 1.00 21.95 C ANISOU 1576 CG LYS B 434 2471 2330 3538 69 -480 -268 C ATOM 1577 CD LYS B 434 -9.456 -30.760 46.722 1.00 34.06 C ANISOU 1577 CD LYS B 434 4021 3797 5124 63 -535 -258 C ATOM 1578 CE LYS B 434 -8.396 -31.831 46.485 1.00 47.16 C ANISOU 1578 CE LYS B 434 5686 5438 6794 103 -608 -306 C ATOM 1579 NZ LYS B 434 -8.908 -33.252 46.598 1.00 53.60 N ANISOU 1579 NZ LYS B 434 6520 6178 7666 99 -671 -301 N ATOM 1580 N VAL B 435 -7.754 -26.341 45.220 1.00 14.08 N ANISOU 1580 N VAL B 435 1418 1475 2458 87 -369 -295 N ATOM 1581 CA VAL B 435 -7.549 -26.004 43.805 1.00 13.08 C ANISOU 1581 CA VAL B 435 1255 1397 2317 118 -358 -325 C ATOM 1582 C VAL B 435 -6.860 -27.202 43.157 1.00 16.97 C ANISOU 1582 C VAL B 435 1738 1889 2821 161 -415 -375 C ATOM 1583 O VAL B 435 -5.919 -27.727 43.711 1.00 19.93 O ANISOU 1583 O VAL B 435 2115 2251 3205 173 -444 -391 O ATOM 1584 CB VAL B 435 -6.698 -24.726 43.627 1.00 15.72 C ANISOU 1584 CB VAL B 435 1571 1780 2622 116 -307 -323 C ATOM 1585 CG1 VAL B 435 -6.272 -24.559 42.164 1.00 17.58 C ANISOU 1585 CG1 VAL B 435 1775 2067 2837 155 -294 -352 C ATOM 1586 CG2 VAL B 435 -7.484 -23.481 44.088 1.00 14.18 C ANISOU 1586 CG2 VAL B 435 1389 1581 2416 80 -251 -279 C ATOM 1587 N GLU B 436 -7.342 -27.646 42.003 1.00 18.76 N ANISOU 1587 N GLU B 436 1958 2124 3044 190 -435 -403 N ATOM 1588 CA GLU B 436 -6.749 -28.834 41.394 1.00 17.52 C ANISOU 1588 CA GLU B 436 1803 1959 2896 238 -490 -457 C ATOM 1589 C GLU B 436 -6.653 -28.786 39.880 1.00 15.05 C ANISOU 1589 C GLU B 436 1483 1691 2545 286 -486 -500 C ATOM 1590 O GLU B 436 -7.615 -28.432 39.192 1.00 16.87 O ANISOU 1590 O GLU B 436 1720 1930 2760 280 -483 -491 O ATOM 1591 CB GLU B 436 -7.494 -30.107 41.840 1.00 27.83 C ANISOU 1591 CB GLU B 436 3133 3191 4249 226 -558 -458 C ATOM 1592 CG GLU B 436 -8.980 -30.087 41.539 1.00 32.66 C ANISOU 1592 CG GLU B 436 3748 3779 4882 197 -568 -434 C ATOM 1593 CD GLU B 436 -9.723 -31.183 42.273 1.00 47.67 C ANISOU 1593 CD GLU B 436 5666 5602 6844 168 -620 -414 C ATOM 1594 OE1 GLU B 436 -10.846 -30.921 42.762 1.00 46.48 O ANISOU 1594 OE1 GLU B 436 5509 5426 6725 123 -600 -362 O ATOM 1595 OE2 GLU B 436 -9.182 -32.311 42.361 1.00 46.04 O ANISOU 1595 OE2 GLU B 436 5476 5356 6660 192 -677 -446 O ATOM 1596 N ALA B 437 -5.487 -29.167 39.362 1.00 16.92 N ANISOU 1596 N ALA B 437 2086 2014 2328 118 -22 2 N ATOM 1597 CA ALA B 437 -5.330 -29.295 37.930 1.00 21.28 C ANISOU 1597 CA ALA B 437 2711 2530 2846 111 11 -16 C ATOM 1598 C ALA B 437 -5.681 -30.749 37.608 1.00 25.69 C ANISOU 1598 C ALA B 437 3376 3014 3371 123 7 -21 C ATOM 1599 O ALA B 437 -4.827 -31.545 37.211 1.00 21.10 O ANISOU 1599 O ALA B 437 2843 2402 2773 182 57 -34 O ATOM 1600 CB ALA B 437 -3.918 -28.980 37.507 1.00 21.92 C ANISOU 1600 CB ALA B 437 2752 2637 2938 161 80 -28 C ATOM 1601 N TYR B 438 -6.948 -31.081 37.788 1.00 18.48 N ANISOU 1601 N TYR B 438 2497 2069 2455 67 -52 -7 N ATOM 1602 CA TYR B 438 -7.444 -32.427 37.536 1.00 17.23 C ANISOU 1602 CA TYR B 438 2443 1830 2272 59 -71 -8 C ATOM 1603 C TYR B 438 -8.897 -32.353 37.144 1.00 21.61 C ANISOU 1603 C TYR B 438 3030 2353 2827 -30 -143 5 C ATOM 1604 O TYR B 438 -9.685 -31.693 37.813 1.00 21.55 O ANISOU 1604 O TYR B 438 2941 2384 2861 -69 -175 33 O ATOM 1605 CB TYR B 438 -7.343 -33.284 38.808 1.00 15.96 C ANISOU 1605 CB TYR B 438 2260 1664 2139 96 -71 14 C ATOM 1606 CG TYR B 438 -7.848 -34.670 38.570 1.00 22.41 C ANISOU 1606 CG TYR B 438 3190 2389 2935 82 -90 16 C ATOM 1607 CD1 TYR B 438 -6.982 -35.664 38.140 1.00 19.85 C ANISOU 1607 CD1 TYR B 438 2954 2010 2580 148 -46 -6 C ATOM 1608 CD2 TYR B 438 -9.198 -34.989 38.734 1.00 23.77 C ANISOU 1608 CD2 TYR B 438 3381 2523 3126 2 -149 40 C ATOM 1609 CE1 TYR B 438 -7.421 -36.934 37.887 1.00 24.55 C ANISOU 1609 CE1 TYR B 438 3669 2508 3151 134 -64 -9 C ATOM 1610 CE2 TYR B 438 -9.660 -36.286 38.472 1.00 21.42 C ANISOU 1610 CE2 TYR B 438 3194 2131 2815 -23 -173 41 C ATOM 1611 CZ TYR B 438 -8.745 -37.248 38.052 1.00 23.88 C ANISOU 1611 CZ TYR B 438 3608 2382 3084 44 -132 13 C ATOM 1612 OH TYR B 438 -9.139 -38.530 37.772 1.00 23.66 O ANISOU 1612 OH TYR B 438 3706 2249 3036 22 -155 10 O ATOM 1613 N HIS B 439 -9.265 -33.043 36.074 1.00 22.22 N ANISOU 1613 N HIS B 439 3228 2355 2859 -61 -170 -13 N ATOM 1614 CA HIS B 439 -10.679 -33.213 35.726 1.00 19.71 C ANISOU 1614 CA HIS B 439 2942 1994 2552 -152 -259 5 C ATOM 1615 C HIS B 439 -10.849 -34.549 35.000 1.00 23.15 C ANISOU 1615 C HIS B 439 3530 2324 2941 -171 -288 -16 C ATOM 1616 O HIS B 439 -10.125 -34.841 34.048 1.00 22.58 O ANISOU 1616 O HIS B 439 3570 2210 2799 -133 -254 -55 O ATOM 1617 CB HIS B 439 -11.173 -32.080 34.849 1.00 21.01 C ANISOU 1617 CB HIS B 439 3096 2185 2704 -198 -299 3 C ATOM 1618 CG HIS B 439 -12.658 -32.031 34.693 1.00 27.34 C ANISOU 1618 CG HIS B 439 3883 2964 3542 -288 -398 35 C ATOM 1619 ND1 HIS B 439 -13.359 -32.951 33.945 1.00 29.09 N ANISOU 1619 ND1 HIS B 439 4214 3100 3741 -349 -476 29 N ATOM 1620 CD2 HIS B 439 -13.577 -31.151 35.166 1.00 28.37 C ANISOU 1620 CD2 HIS B 439 3899 3144 3737 -327 -434 75 C ATOM 1621 CE1 HIS B 439 -14.647 -32.653 33.973 1.00 34.39 C ANISOU 1621 CE1 HIS B 439 4822 3773 4471 -427 -563 69 C ATOM 1622 NE2 HIS B 439 -14.807 -31.572 34.717 1.00 32.90 N ANISOU 1622 NE2 HIS B 439 4496 3668 4338 -410 -532 99 N ATOM 1623 N LYS B 440 -11.812 -35.348 35.453 1.00 19.23 N ANISOU 1623 N LYS B 440 3043 1779 2484 -229 -346 11 N ATOM 1624 CA LYS B 440 -12.008 -36.696 34.916 1.00 30.04 C ANISOU 1624 CA LYS B 440 4562 3035 3816 -255 -381 -8 C ATOM 1625 C LYS B 440 -12.292 -36.669 33.417 1.00 31.44 C ANISOU 1625 C LYS B 440 4873 3152 3921 -301 -443 -44 C ATOM 1626 O LYS B 440 -12.104 -37.667 32.736 1.00 34.33 O ANISOU 1626 O LYS B 440 5400 3419 4224 -298 -453 -78 O ATOM 1627 CB LYS B 440 -13.162 -37.387 35.640 1.00 33.28 C ANISOU 1627 CB LYS B 440 4941 3406 4297 -333 -442 37 C ATOM 1628 CG LYS B 440 -14.524 -36.809 35.283 1.00 35.52 C ANISOU 1628 CG LYS B 440 5166 3700 4631 -440 -543 69 C ATOM 1629 CD LYS B 440 -15.637 -37.354 36.174 1.00 41.78 C ANISOU 1629 CD LYS B 440 5885 4471 5519 -512 -581 128 C ATOM 1630 CE LYS B 440 -15.721 -38.859 36.128 1.00 37.44 C ANISOU 1630 CE LYS B 440 5462 3806 4957 -543 -604 122 C ATOM 1631 NZ LYS B 440 -16.929 -39.348 36.860 1.00 39.66 N ANISOU 1631 NZ LYS B 440 5668 4061 5341 -633 -646 188 N ATOM 1632 N ASP B 441 -12.762 -35.537 32.895 1.00 24.38 N ANISOU 1632 N ASP B 441 3926 2308 3029 -340 -486 -36 N ATOM 1633 CA ASP B 441 -13.113 -35.487 31.476 1.00 26.66 C ANISOU 1633 CA ASP B 441 4352 2536 3240 -387 -560 -65 C ATOM 1634 C ASP B 441 -11.951 -34.987 30.639 1.00 25.31 C ANISOU 1634 C ASP B 441 4260 2379 2977 -308 -473 -107 C ATOM 1635 O ASP B 441 -12.022 -34.970 29.423 1.00 24.01 O ANISOU 1635 O ASP B 441 4239 2159 2724 -326 -510 -136 O ATOM 1636 CB ASP B 441 -14.347 -34.616 31.221 1.00 40.83 C ANISOU 1636 CB ASP B 441 6068 4363 5082 -476 -671 -29 C ATOM 1637 CG ASP B 441 -15.627 -35.227 31.779 1.00 47.55 C ANISOU 1637 CG ASP B 441 6859 5182 6026 -570 -767 16 C ATOM 1638 OD1 ASP B 441 -15.700 -36.465 31.915 1.00 48.12 O ANISOU 1638 OD1 ASP B 441 7016 5171 6095 -592 -783 7 O ATOM 1639 OD2 ASP B 441 -16.557 -34.455 32.096 1.00 51.04 O ANISOU 1639 OD2 ASP B 441 7164 5679 6549 -619 -820 64 O ATOM 1640 N TYR B 442 -10.875 -34.572 31.292 1.00 20.80 N ANISOU 1640 N TYR B 442 3596 1879 2427 -221 -357 -106 N ATOM 1641 CA TYR B 442 -9.727 -34.071 30.551 1.00 25.46 C ANISOU 1641 CA TYR B 442 4236 2487 2949 -146 -259 -135 C ATOM 1642 C TYR B 442 -8.456 -34.730 31.036 1.00 26.69 C ANISOU 1642 C TYR B 442 4390 2642 3107 -44 -142 -148 C ATOM 1643 O TYR B 442 -7.659 -34.094 31.710 1.00 28.53 O ANISOU 1643 O TYR B 442 4491 2958 3390 11 -69 -134 O ATOM 1644 CB TYR B 442 -9.661 -32.546 30.645 1.00 25.30 C ANISOU 1644 CB TYR B 442 4087 2565 2962 -151 -243 -113 C ATOM 1645 CG TYR B 442 -10.863 -31.929 29.976 1.00 31.70 C ANISOU 1645 CG TYR B 442 4920 3364 3759 -238 -358 -98 C ATOM 1646 CD1 TYR B 442 -10.844 -31.627 28.620 1.00 34.84 C ANISOU 1646 CD1 TYR B 442 5458 3720 4060 -249 -376 -120 C ATOM 1647 CD2 TYR B 442 -12.039 -31.710 30.680 1.00 31.69 C ANISOU 1647 CD2 TYR B 442 4808 3389 3843 -307 -450 -59 C ATOM 1648 CE1 TYR B 442 -11.954 -31.089 27.994 1.00 43.49 C ANISOU 1648 CE1 TYR B 442 6578 4803 5144 -326 -497 -103 C ATOM 1649 CE2 TYR B 442 -13.160 -31.157 30.061 1.00 37.32 C ANISOU 1649 CE2 TYR B 442 5528 4094 4558 -382 -562 -38 C ATOM 1650 CZ TYR B 442 -13.109 -30.855 28.717 1.00 46.03 C ANISOU 1650 CZ TYR B 442 6769 5157 5564 -392 -594 -61 C ATOM 1651 OH TYR B 442 -14.212 -30.312 28.086 1.00 49.11 O ANISOU 1651 OH TYR B 442 7169 5537 5955 -464 -720 -37 O ATOM 1652 N PRO B 443 -8.291 -36.025 30.701 1.00 31.18 N ANISOU 1652 N PRO B 443 5109 3112 3626 -19 -133 -175 N ATOM 1653 CA PRO B 443 -7.096 -36.839 30.967 1.00 42.52 C ANISOU 1653 CA PRO B 443 6577 4525 5055 91 -22 -190 C ATOM 1654 C PRO B 443 -5.815 -36.134 30.515 1.00 34.96 C ANISOU 1654 C PRO B 443 5585 3621 4076 180 105 -198 C ATOM 1655 O PRO B 443 -4.832 -36.148 31.247 1.00 35.47 O ANISOU 1655 O PRO B 443 5541 3737 4198 260 186 -183 O ATOM 1656 CB PRO B 443 -7.303 -38.085 30.092 1.00 39.78 C ANISOU 1656 CB PRO B 443 6457 4040 4617 88 -42 -228 C ATOM 1657 CG PRO B 443 -8.744 -38.142 29.794 1.00 43.19 C ANISOU 1657 CG PRO B 443 6942 4426 5042 -40 -191 -225 C ATOM 1658 CD PRO B 443 -9.317 -36.762 29.940 1.00 34.45 C ANISOU 1658 CD PRO B 443 5685 3421 3985 -100 -241 -194 C ATOM 1659 N ASP B 444 -5.819 -35.561 29.314 1.00 28.62 N ANISOU 1659 N ASP B 444 4878 2801 3196 165 119 -218 N ATOM 1660 CA ASP B 444 -4.644 -34.858 28.808 1.00 33.43 C ANISOU 1660 CA ASP B 444 5459 3456 3789 241 250 -218 C ATOM 1661 C ASP B 444 -4.718 -33.376 29.218 1.00 30.15 C ANISOU 1661 C ASP B 444 4865 3152 3439 199 234 -187 C ATOM 1662 O ASP B 444 -5.386 -32.579 28.568 1.00 31.53 O ANISOU 1662 O ASP B 444 5075 3331 3575 133 179 -185 O ATOM 1663 CB ASP B 444 -4.538 -35.023 27.292 1.00 43.08 C ANISOU 1663 CB ASP B 444 6897 4594 4879 256 292 -253 C ATOM 1664 CG ASP B 444 -4.800 -36.464 26.844 1.00 67.14 C ANISOU 1664 CG ASP B 444 10154 7511 7846 271 269 -291 C ATOM 1665 OD1 ASP B 444 -4.060 -37.369 27.296 1.00 68.75 O ANISOU 1665 OD1 ASP B 444 10361 7686 8074 358 347 -295 O ATOM 1666 OD2 ASP B 444 -5.752 -36.692 26.055 1.00 71.57 O ANISOU 1666 OD2 ASP B 444 10880 7993 8321 195 165 -315 O ATOM 1667 N ASN B 445 -4.031 -33.038 30.307 1.00 25.48 N ANISOU 1667 N ASN B 445 4094 2643 2945 238 276 -162 N ATOM 1668 CA ASN B 445 -4.143 -31.739 30.972 1.00 26.54 C ANISOU 1668 CA ASN B 445 4057 2874 3152 196 247 -134 C ATOM 1669 C ASN B 445 -2.747 -31.208 31.275 1.00 26.89 C ANISOU 1669 C ASN B 445 3975 2985 3254 267 357 -119 C ATOM 1670 O ASN B 445 -1.982 -31.863 31.977 1.00 27.42 O ANISOU 1670 O ASN B 445 3983 3065 3372 335 398 -113 O ATOM 1671 CB ASN B 445 -4.923 -31.920 32.280 1.00 21.67 C ANISOU 1671 CB ASN B 445 3344 2286 2605 154 153 -114 C ATOM 1672 CG ASN B 445 -5.272 -30.606 32.957 1.00 24.15 C ANISOU 1672 CG ASN B 445 3512 2684 2979 105 111 -90 C ATOM 1673 OD1 ASN B 445 -4.777 -29.549 32.572 1.00 22.67 O ANISOU 1673 OD1 ASN B 445 3278 2540 2796 106 155 -86 O ATOM 1674 ND2 ASN B 445 -6.141 -30.671 33.974 1.00 15.77 N ANISOU 1674 ND2 ASN B 445 2386 1640 1964 65 34 -71 N ATOM 1675 N VAL B 446 -2.405 -30.032 30.752 1.00 23.10 N ANISOU 1675 N VAL B 446 3453 2548 2776 249 400 -109 N ATOM 1676 CA VAL B 446 -1.068 -29.469 30.981 1.00 22.92 C ANISOU 1676 CA VAL B 446 3300 2587 2822 303 503 -90 C ATOM 1677 C VAL B 446 -0.960 -28.670 32.293 1.00 25.31 C ANISOU 1677 C VAL B 446 3416 2974 3226 274 446 -68 C ATOM 1678 O VAL B 446 0.090 -28.118 32.613 1.00 22.30 O ANISOU 1678 O VAL B 446 2909 2648 2916 302 504 -49 O ATOM 1679 CB VAL B 446 -0.625 -28.561 29.807 1.00 29.28 C ANISOU 1679 CB VAL B 446 4147 3393 3587 297 591 -84 C ATOM 1680 CG1 VAL B 446 -0.327 -29.392 28.551 1.00 27.62 C ANISOU 1680 CG1 VAL B 446 4120 3099 3274 355 685 -104 C ATOM 1681 CG2 VAL B 446 -1.702 -27.521 29.518 1.00 29.97 C ANISOU 1681 CG2 VAL B 446 4260 3488 3641 204 502 -81 C ATOM 1682 N GLY B 447 -2.041 -28.602 33.061 1.00 21.39 N ANISOU 1682 N GLY B 447 2903 2485 2737 218 335 -68 N ATOM 1683 CA GLY B 447 -1.971 -27.876 34.315 1.00 14.68 C ANISOU 1683 CA GLY B 447 1906 1705 1966 197 285 -51 C ATOM 1684 C GLY B 447 -1.159 -28.715 35.290 1.00 25.65 C ANISOU 1684 C GLY B 447 3225 3111 3408 266 297 -44 C ATOM 1685 O GLY B 447 -0.997 -29.921 35.104 1.00 20.31 O ANISOU 1685 O GLY B 447 2624 2386 2706 320 324 -51 O ATOM 1686 N GLN B 448 -0.641 -28.075 36.328 1.00 22.55 N ANISOU 1686 N GLN B 448 2699 2783 3087 265 270 -29 N ATOM 1687 CA GLN B 448 0.239 -28.741 37.271 1.00 22.11 C ANISOU 1687 CA GLN B 448 2565 2750 3085 333 270 -17 C ATOM 1688 C GLN B 448 0.208 -27.947 38.564 1.00 23.03 C ANISOU 1688 C GLN B 448 2576 2924 3249 301 191 -7 C ATOM 1689 O GLN B 448 0.333 -26.722 38.549 1.00 19.55 O ANISOU 1689 O GLN B 448 2073 2520 2835 252 182 -6 O ATOM 1690 CB GLN B 448 1.661 -28.779 36.699 1.00 26.39 C ANISOU 1690 CB GLN B 448 3045 3307 3674 397 370 -5 C ATOM 1691 CG GLN B 448 2.665 -29.467 37.560 1.00 32.43 C ANISOU 1691 CG GLN B 448 3719 4096 4506 476 369 14 C ATOM 1692 CD GLN B 448 4.077 -29.365 36.999 1.00 37.63 C ANISOU 1692 CD GLN B 448 4285 4779 5234 537 473 35 C ATOM 1693 OE1 GLN B 448 4.967 -30.070 37.453 1.00 41.07 O ANISOU 1693 OE1 GLN B 448 4652 5225 5727 619 490 55 O ATOM 1694 NE2 GLN B 448 4.288 -28.473 36.011 1.00 28.17 N ANISOU 1694 NE2 GLN B 448 3081 3588 4034 499 546 36 N ATOM 1695 N ILE B 449 0.022 -28.640 39.679 1.00 18.82 N ANISOU 1695 N ILE B 449 2038 2391 2721 329 134 1 N ATOM 1696 CA ILE B 449 -0.034 -27.997 40.979 1.00 16.59 C ANISOU 1696 CA ILE B 449 1684 2154 2465 307 56 8 C ATOM 1697 C ILE B 449 0.760 -28.888 41.932 1.00 29.67 C ANISOU 1697 C ILE B 449 3300 3820 4152 382 31 25 C ATOM 1698 O ILE B 449 0.391 -30.042 42.180 1.00 24.39 O ANISOU 1698 O ILE B 449 2704 3110 3452 421 28 31 O ATOM 1699 CB ILE B 449 -1.507 -27.905 41.521 1.00 21.19 C ANISOU 1699 CB ILE B 449 2333 2717 3000 256 1 6 C ATOM 1700 CG1 ILE B 449 -2.402 -26.971 40.687 1.00 16.25 C ANISOU 1700 CG1 ILE B 449 1741 2084 2351 185 8 -4 C ATOM 1701 CG2 ILE B 449 -1.510 -27.461 42.966 1.00 15.55 C ANISOU 1701 CG2 ILE B 449 1572 2039 2298 254 -67 14 C ATOM 1702 CD1 ILE B 449 -2.116 -25.476 40.867 1.00 23.20 C ANISOU 1702 CD1 ILE B 449 2549 3007 3260 143 -7 -8 C ATOM 1703 N ASN B 450 1.856 -28.368 42.462 1.00 20.08 N ANISOU 1703 N ASN B 450 1972 2656 3001 400 7 35 N ATOM 1704 CA ASN B 450 2.589 -29.085 43.491 1.00 18.86 C ANISOU 1704 CA ASN B 450 1773 2516 2876 470 -41 55 C ATOM 1705 C ASN B 450 3.555 -28.135 44.143 1.00 22.04 C ANISOU 1705 C ASN B 450 2048 2978 3347 455 -101 63 C ATOM 1706 O ASN B 450 3.738 -27.017 43.654 1.00 20.32 O ANISOU 1706 O ASN B 450 1777 2784 3160 394 -86 54 O ATOM 1707 CB ASN B 450 3.292 -30.317 42.913 1.00 25.69 C ANISOU 1707 CB ASN B 450 2648 3351 3762 560 28 70 C ATOM 1708 CG ASN B 450 4.361 -29.953 41.914 1.00 33.28 C ANISOU 1708 CG ASN B 450 3522 4334 4790 580 112 76 C ATOM 1709 OD1 ASN B 450 5.277 -29.210 42.231 1.00 30.30 O ANISOU 1709 OD1 ASN B 450 3013 4010 4490 572 86 91 O ATOM 1710 ND2 ASN B 450 4.250 -30.478 40.699 1.00 32.13 N ANISOU 1710 ND2 ASN B 450 3453 4142 4614 605 214 67 N ATOM 1711 N LYS B 451 4.172 -28.562 45.241 1.00 23.77 N ANISOU 1711 N LYS B 451 2223 3217 3591 505 -177 82 N ATOM 1712 CA LYS B 451 4.861 -27.617 46.115 1.00 30.92 C ANISOU 1712 CA LYS B 451 3032 4171 4544 474 -273 85 C ATOM 1713 C LYS B 451 6.086 -27.110 45.410 1.00 31.88 C ANISOU 1713 C LYS B 451 3011 4328 4772 471 -235 100 C ATOM 1714 O LYS B 451 6.554 -26.005 45.650 1.00 30.03 O ANISOU 1714 O LYS B 451 2694 4128 4588 410 -288 96 O ATOM 1715 CB LYS B 451 5.262 -28.277 47.433 1.00 37.97 C ANISOU 1715 CB LYS B 451 3922 5073 5431 535 -374 106 C ATOM 1716 CG LYS B 451 5.692 -27.269 48.495 1.00 36.38 C ANISOU 1716 CG LYS B 451 3667 4909 5247 490 -500 101 C ATOM 1717 CD LYS B 451 6.281 -27.955 49.724 1.00 52.85 C ANISOU 1717 CD LYS B 451 5746 7005 7331 559 -610 127 C ATOM 1718 CE LYS B 451 6.678 -26.933 50.778 1.00 61.55 C ANISOU 1718 CE LYS B 451 6816 8134 8435 507 -750 116 C ATOM 1719 NZ LYS B 451 7.631 -27.528 51.754 1.00 75.38 N ANISOU 1719 NZ LYS B 451 8518 9905 10217 576 -868 149 N ATOM 1720 N ASP B 452 6.593 -27.945 44.518 1.00 27.46 N ANISOU 1720 N ASP B 452 2430 3756 4248 539 -136 117 N ATOM 1721 CA ASP B 452 7.767 -27.622 43.749 1.00 29.98 C ANISOU 1721 CA ASP B 452 2612 4104 4674 551 -68 141 C ATOM 1722 C ASP B 452 7.560 -26.439 42.818 1.00 32.81 C ANISOU 1722 C ASP B 452 2961 4466 5038 462 -5 125 C ATOM 1723 O ASP B 452 8.439 -25.590 42.698 1.00 32.28 O ANISOU 1723 O ASP B 452 2763 4436 5065 423 -7 142 O ATOM 1724 CB ASP B 452 8.222 -28.850 42.935 1.00 40.86 C ANISOU 1724 CB ASP B 452 4002 5454 6070 657 49 161 C ATOM 1725 CG ASP B 452 9.592 -28.660 42.311 1.00 60.35 C ANISOU 1725 CG ASP B 452 6308 7958 8666 694 126 198 C ATOM 1726 OD1 ASP B 452 10.428 -27.988 42.948 1.00 66.92 O ANISOU 1726 OD1 ASP B 452 6989 8842 9596 666 45 222 O ATOM 1727 OD2 ASP B 452 9.839 -29.179 41.194 1.00 62.85 O ANISOU 1727 OD2 ASP B 452 6648 8246 8986 751 269 207 O ATOM 1728 N VAL B 453 6.418 -26.387 42.139 1.00 26.55 N ANISOU 1728 N VAL B 453 2304 3632 4150 428 48 97 N ATOM 1729 CA VAL B 453 6.264 -25.408 41.052 1.00 26.13 C ANISOU 1729 CA VAL B 453 2256 3575 4097 360 126 88 C ATOM 1730 C VAL B 453 5.215 -24.322 41.295 1.00 25.68 C ANISOU 1730 C VAL B 453 2265 3511 3981 265 66 60 C ATOM 1731 O VAL B 453 5.123 -23.362 40.537 1.00 26.21 O ANISOU 1731 O VAL B 453 2331 3574 4052 204 112 56 O ATOM 1732 CB VAL B 453 5.967 -26.105 39.727 1.00 25.94 C ANISOU 1732 CB VAL B 453 2331 3505 4021 400 255 84 C ATOM 1733 CG1 VAL B 453 7.117 -27.060 39.368 1.00 38.79 C ANISOU 1733 CG1 VAL B 453 3889 5135 5714 503 340 115 C ATOM 1734 CG2 VAL B 453 4.677 -26.871 39.816 1.00 28.39 C ANISOU 1734 CG2 VAL B 453 2797 3766 4223 407 228 59 C ATOM 1735 N THR B 454 4.433 -24.465 42.357 1.00 22.76 N ANISOU 1735 N THR B 454 1956 3135 3556 258 -29 44 N ATOM 1736 CA THR B 454 3.290 -23.573 42.578 1.00 17.86 C ANISOU 1736 CA THR B 454 1413 2501 2873 186 -70 20 C ATOM 1737 C THR B 454 3.608 -22.562 43.665 1.00 20.18 C ANISOU 1737 C THR B 454 1650 2821 3197 139 -171 13 C ATOM 1738 O THR B 454 4.261 -22.895 44.653 1.00 24.17 O ANISOU 1738 O THR B 454 2103 3348 3731 171 -248 22 O ATOM 1739 CB THR B 454 2.045 -24.400 42.966 1.00 20.25 C ANISOU 1739 CB THR B 454 1836 2770 3090 209 -89 11 C ATOM 1740 OG1 THR B 454 1.834 -25.395 41.965 1.00 18.55 O ANISOU 1740 OG1 THR B 454 1680 2521 2848 249 -9 15 O ATOM 1741 CG2 THR B 454 0.778 -23.531 43.058 1.00 13.82 C ANISOU 1741 CG2 THR B 454 1094 1938 2218 145 -112 -6 C ATOM 1742 N LYS B 455 3.168 -21.323 43.461 1.00 21.74 N ANISOU 1742 N LYS B 455 1867 3010 3383 65 -177 -2 N ATOM 1743 CA LYS B 455 3.299 -20.267 44.451 1.00 22.22 C ANISOU 1743 CA LYS B 455 1908 3081 3455 13 -273 -17 C ATOM 1744 C LYS B 455 1.913 -19.654 44.677 1.00 24.16 C ANISOU 1744 C LYS B 455 2269 3295 3618 -20 -283 -39 C ATOM 1745 O LYS B 455 1.156 -19.455 43.739 1.00 21.60 O ANISOU 1745 O LYS B 455 1993 2948 3264 -37 -215 -39 O ATOM 1746 CB LYS B 455 4.272 -19.193 43.954 1.00 32.05 C ANISOU 1746 CB LYS B 455 3053 4338 4787 -51 -263 -9 C ATOM 1747 CG LYS B 455 5.746 -19.643 43.837 1.00 47.51 C ANISOU 1747 CG LYS B 455 4865 6332 6854 -23 -256 22 C ATOM 1748 CD LYS B 455 6.463 -19.717 45.200 1.00 64.64 C ANISOU 1748 CD LYS B 455 6971 8527 9061 -16 -393 23 C ATOM 1749 CE LYS B 455 7.998 -19.969 45.083 1.00 59.55 C ANISOU 1749 CE LYS B 455 6152 7923 8552 2 -399 62 C ATOM 1750 NZ LYS B 455 8.749 -19.941 46.403 1.00 32.84 N ANISOU 1750 NZ LYS B 455 2701 4565 5214 -1 -558 66 N ATOM 1751 N ILE B 456 1.573 -19.363 45.922 1.00 20.26 N ANISOU 1751 N ILE B 456 1819 2795 3082 -22 -367 -55 N ATOM 1752 CA ILE B 456 0.229 -18.902 46.220 1.00 20.91 C ANISOU 1752 CA ILE B 456 2007 2848 3090 -35 -362 -69 C ATOM 1753 C ILE B 456 0.255 -17.569 46.970 1.00 26.13 C ANISOU 1753 C ILE B 456 2694 3494 3742 -85 -428 -94 C ATOM 1754 O ILE B 456 1.015 -17.407 47.921 1.00 19.49 O ANISOU 1754 O ILE B 456 1832 2662 2912 -89 -516 -104 O ATOM 1755 CB ILE B 456 -0.537 -19.966 47.027 1.00 17.95 C ANISOU 1755 CB ILE B 456 1703 2466 2651 24 -373 -62 C ATOM 1756 CG1 ILE B 456 -0.807 -21.182 46.113 1.00 19.72 C ANISOU 1756 CG1 ILE B 456 1928 2687 2877 61 -301 -42 C ATOM 1757 CG2 ILE B 456 -1.853 -19.406 47.516 1.00 18.41 C ANISOU 1757 CG2 ILE B 456 1854 2496 2644 15 -367 -71 C ATOM 1758 CD1 ILE B 456 -1.588 -22.317 46.757 1.00 23.68 C ANISOU 1758 CD1 ILE B 456 2498 3174 3326 111 -301 -28 C ATOM 1759 N LYS B 457 -0.549 -16.604 46.531 1.00 17.46 N ANISOU 1759 N LYS B 457 1645 2366 2622 -122 -393 -103 N ATOM 1760 CA LYS B 457 -0.718 -15.386 47.334 1.00 21.88 C ANISOU 1760 CA LYS B 457 2261 2897 3157 -158 -449 -130 C ATOM 1761 C LYS B 457 -2.169 -15.240 47.732 1.00 23.74 C ANISOU 1761 C LYS B 457 2601 3103 3316 -128 -417 -133 C ATOM 1762 O LYS B 457 -3.056 -15.591 46.973 1.00 20.30 O ANISOU 1762 O LYS B 457 2176 2664 2872 -111 -348 -113 O ATOM 1763 CB LYS B 457 -0.266 -14.147 46.574 1.00 32.05 C ANISOU 1763 CB LYS B 457 3515 4166 4497 -229 -437 -136 C ATOM 1764 CG LYS B 457 1.234 -14.084 46.378 1.00 42.33 C ANISOU 1764 CG LYS B 457 4703 5494 5888 -269 -474 -129 C ATOM 1765 CD LYS B 457 1.666 -12.693 45.976 1.00 53.61 C ANISOU 1765 CD LYS B 457 6114 6892 7364 -352 -481 -137 C ATOM 1766 CE LYS B 457 1.490 -11.720 47.139 1.00 61.63 C ANISOU 1766 CE LYS B 457 7215 7865 8337 -383 -574 -174 C ATOM 1767 NZ LYS B 457 2.258 -12.095 48.367 1.00 58.18 N ANISOU 1767 NZ LYS B 457 6761 7446 7901 -375 -691 -189 N ATOM 1768 N ILE B 458 -2.414 -14.733 48.931 1.00 23.68 N ANISOU 1768 N ILE B 458 2672 3071 3253 -118 -469 -155 N ATOM 1769 CA ILE B 458 -3.777 -14.581 49.414 1.00 23.01 C ANISOU 1769 CA ILE B 458 2683 2957 3102 -80 -425 -152 C ATOM 1770 C ILE B 458 -3.992 -13.150 49.913 1.00 24.37 C ANISOU 1770 C ILE B 458 2935 3081 3244 -105 -448 -182 C ATOM 1771 O ILE B 458 -3.159 -12.619 50.638 1.00 19.50 O ANISOU 1771 O ILE B 458 2343 2450 2617 -133 -530 -213 O ATOM 1772 CB ILE B 458 -4.068 -15.579 50.541 1.00 27.44 C ANISOU 1772 CB ILE B 458 3297 3527 3602 -19 -440 -144 C ATOM 1773 CG1 ILE B 458 -3.874 -17.017 50.033 1.00 27.02 C ANISOU 1773 CG1 ILE B 458 3177 3511 3580 8 -416 -114 C ATOM 1774 CG2 ILE B 458 -5.492 -15.368 51.099 1.00 23.41 C ANISOU 1774 CG2 ILE B 458 2881 2985 3030 24 -378 -134 C ATOM 1775 CD1 ILE B 458 -3.967 -18.091 51.126 1.00 26.01 C ANISOU 1775 CD1 ILE B 458 3097 3388 3396 66 -437 -101 C ATOM 1776 N TYR B 459 -5.087 -12.520 49.496 1.00 19.40 N ANISOU 1776 N TYR B 459 2346 2422 2604 -96 -381 -173 N ATOM 1777 CA TYR B 459 -5.416 -11.160 49.943 1.00 19.45 C ANISOU 1777 CA TYR B 459 2442 2371 2578 -106 -387 -200 C ATOM 1778 C TYR B 459 -6.777 -11.160 50.594 1.00 21.45 C ANISOU 1778 C TYR B 459 2780 2599 2770 -36 -323 -187 C ATOM 1779 O TYR B 459 -7.673 -11.858 50.139 1.00 19.56 O ANISOU 1779 O TYR B 459 2504 2382 2547 -2 -257 -148 O ATOM 1780 CB TYR B 459 -5.453 -10.183 48.760 1.00 13.90 C ANISOU 1780 CB TYR B 459 1708 1645 1928 -155 -358 -195 C ATOM 1781 CG TYR B 459 -4.134 -10.046 48.029 1.00 24.13 C ANISOU 1781 CG TYR B 459 2917 2960 3292 -227 -399 -200 C ATOM 1782 CD1 TYR B 459 -3.224 -9.055 48.383 1.00 29.72 C ANISOU 1782 CD1 TYR B 459 3643 3633 4016 -289 -468 -232 C ATOM 1783 CD2 TYR B 459 -3.799 -10.911 46.996 1.00 22.86 C ANISOU 1783 CD2 TYR B 459 2658 2846 3182 -235 -367 -171 C ATOM 1784 CE1 TYR B 459 -2.019 -8.919 47.708 1.00 34.03 C ANISOU 1784 CE1 TYR B 459 4093 4197 4641 -359 -496 -227 C ATOM 1785 CE2 TYR B 459 -2.593 -10.791 46.310 1.00 26.49 C ANISOU 1785 CE2 TYR B 459 3033 3323 3709 -293 -383 -168 C ATOM 1786 CZ TYR B 459 -1.709 -9.790 46.677 1.00 37.66 C ANISOU 1786 CZ TYR B 459 4449 4709 5153 -356 -445 -193 C ATOM 1787 OH TYR B 459 -0.513 -9.665 46.020 1.00 36.38 O ANISOU 1787 OH TYR B 459 4187 4563 5071 -416 -454 -182 O ATOM 1788 N GLN B 460 -6.932 -10.370 51.652 1.00 19.95 N ANISOU 1788 N GLN B 460 2707 2358 2514 -16 -340 -218 N ATOM 1789 CA GLN B 460 -8.234 -10.212 52.282 1.00 22.50 C ANISOU 1789 CA GLN B 460 3118 2650 2783 59 -259 -202 C ATOM 1790 C GLN B 460 -8.888 -8.897 51.866 1.00 25.17 C ANISOU 1790 C GLN B 460 3498 2932 3132 61 -214 -206 C ATOM 1791 O GLN B 460 -8.244 -7.842 51.888 1.00 23.35 O ANISOU 1791 O GLN B 460 3318 2656 2896 16 -266 -246 O ATOM 1792 CB GLN B 460 -8.112 -10.272 53.808 1.00 19.64 C ANISOU 1792 CB GLN B 460 2884 2259 2318 102 -288 -230 C ATOM 1793 CG GLN B 460 -9.456 -10.084 54.524 1.00 24.88 C ANISOU 1793 CG GLN B 460 3645 2886 2922 188 -182 -210 C ATOM 1794 CD GLN B 460 -9.294 -9.848 56.016 1.00 38.42 C ANISOU 1794 CD GLN B 460 5528 4554 4517 231 -207 -247 C ATOM 1795 OE1 GLN B 460 -9.354 -10.776 56.815 1.00 35.41 O ANISOU 1795 OE1 GLN B 460 5184 4192 4080 272 -200 -232 O ATOM 1796 NE2 GLN B 460 -9.074 -8.602 56.390 1.00 42.09 N ANISOU 1796 NE2 GLN B 460 6107 4949 4935 220 -240 -295 N ATOM 1797 N ALA B 461 -10.161 -8.961 51.482 1.00 24.95 N ANISOU 1797 N ALA B 461 3448 2905 3126 113 -121 -162 N ATOM 1798 CA ALA B 461 -10.899 -7.762 51.085 1.00 18.40 C ANISOU 1798 CA ALA B 461 2656 2023 2313 132 -71 -156 C ATOM 1799 C ALA B 461 -11.737 -7.282 52.247 1.00 21.49 C ANISOU 1799 C ALA B 461 3171 2360 2633 216 -5 -161 C ATOM 1800 O ALA B 461 -12.264 -8.086 53.007 1.00 29.52 O ANISOU 1800 O ALA B 461 4205 3398 3614 272 43 -139 O ATOM 1801 CB ALA B 461 -11.782 -8.022 49.849 1.00 19.11 C ANISOU 1801 CB ALA B 461 2638 2143 2481 138 -20 -98 C ATOM 1802 N PRO B 462 -11.841 -5.959 52.413 1.00 23.00 N ANISOU 1802 N PRO B 462 3463 2478 2800 227 4 -190 N ATOM 1803 CA PRO B 462 -12.627 -5.408 53.526 1.00 22.58 C ANISOU 1803 CA PRO B 462 3550 2361 2670 318 80 -198 C ATOM 1804 C PRO B 462 -14.122 -5.636 53.308 1.00 19.59 C ANISOU 1804 C PRO B 462 3111 1996 2337 405 206 -128 C ATOM 1805 O PRO B 462 -14.557 -5.901 52.193 1.00 22.05 O ANISOU 1805 O PRO B 462 3290 2349 2740 386 216 -80 O ATOM 1806 CB PRO B 462 -12.325 -3.898 53.472 1.00 31.10 C ANISOU 1806 CB PRO B 462 4738 3350 3729 299 54 -244 C ATOM 1807 CG PRO B 462 -11.125 -3.761 52.619 1.00 36.94 C ANISOU 1807 CG PRO B 462 5406 4109 4520 184 -55 -268 C ATOM 1808 CD PRO B 462 -11.106 -4.924 51.670 1.00 30.06 C ANISOU 1808 CD PRO B 462 4362 3333 3726 154 -57 -219 C ATOM 1809 N LYS B 463 -14.906 -5.516 54.366 1.00 20.63 N ANISOU 1809 N LYS B 463 3343 2089 2406 500 300 -119 N ATOM 1810 CA LYS B 463 -16.352 -5.666 54.246 1.00 28.17 C ANISOU 1810 CA LYS B 463 4232 3054 3417 587 429 -45 C ATOM 1811 C LYS B 463 -16.933 -4.758 53.152 1.00 26.19 C ANISOU 1811 C LYS B 463 3917 2781 3255 594 446 -16 C ATOM 1812 O LYS B 463 -16.532 -3.608 53.016 1.00 26.07 O ANISOU 1812 O LYS B 463 3991 2700 3215 581 415 -58 O ATOM 1813 CB LYS B 463 -17.023 -5.351 55.589 1.00 33.30 C ANISOU 1813 CB LYS B 463 5030 3645 3977 698 544 -46 C ATOM 1814 CG LYS B 463 -18.500 -5.676 55.622 1.00 44.46 C ANISOU 1814 CG LYS B 463 6359 5076 5458 792 690 41 C ATOM 1815 CD LYS B 463 -19.149 -5.221 56.924 1.00 61.38 C ANISOU 1815 CD LYS B 463 8663 7151 7509 913 826 41 C ATOM 1816 CE LYS B 463 -20.620 -5.627 56.975 1.00 72.32 C ANISOU 1816 CE LYS B 463 9938 8561 8980 1006 985 140 C ATOM 1817 NZ LYS B 463 -21.414 -5.062 55.842 1.00 72.74 N ANISOU 1817 NZ LYS B 463 9848 8621 9169 1020 1003 194 N ATOM 1818 N ASP B 464 -17.900 -5.284 52.407 1.00 20.30 N ANISOU 1818 N ASP B 464 3021 2085 2609 614 493 60 N ATOM 1819 CA ASP B 464 -18.604 -4.557 51.365 1.00 22.62 C ANISOU 1819 CA ASP B 464 3241 2364 2991 632 507 103 C ATOM 1820 C ASP B 464 -17.734 -4.194 50.155 1.00 26.11 C ANISOU 1820 C ASP B 464 3647 2811 3461 533 394 77 C ATOM 1821 O ASP B 464 -18.213 -3.550 49.229 1.00 22.19 O ANISOU 1821 O ASP B 464 3106 2298 3027 542 392 110 O ATOM 1822 CB ASP B 464 -19.246 -3.289 51.940 1.00 32.51 C ANISOU 1822 CB ASP B 464 4610 3528 4215 734 598 101 C ATOM 1823 CG ASP B 464 -20.248 -3.606 53.046 1.00 50.44 C ANISOU 1823 CG ASP B 464 6907 5790 6466 846 738 141 C ATOM 1824 OD1 ASP B 464 -21.064 -4.537 52.847 1.00 43.78 O ANISOU 1824 OD1 ASP B 464 5921 5011 5703 863 785 215 O ATOM 1825 OD2 ASP B 464 -20.220 -2.929 54.106 1.00 58.49 O ANISOU 1825 OD2 ASP B 464 8097 6737 7391 916 804 101 O ATOM 1826 N TYR B 465 -16.468 -4.595 50.153 1.00 21.71 N ANISOU 1826 N TYR B 465 3110 2277 2861 444 304 23 N ATOM 1827 CA TYR B 465 -15.615 -4.309 48.997 1.00 20.48 C ANISOU 1827 CA TYR B 465 2915 2129 2737 351 214 5 C ATOM 1828 C TYR B 465 -16.185 -4.947 47.720 1.00 25.38 C ANISOU 1828 C TYR B 465 3392 2807 3444 330 202 67 C ATOM 1829 O TYR B 465 -16.554 -6.130 47.718 1.00 23.96 O ANISOU 1829 O TYR B 465 3126 2687 3289 331 210 100 O ATOM 1830 CB TYR B 465 -14.194 -4.826 49.249 1.00 23.42 C ANISOU 1830 CB TYR B 465 3305 2528 3066 266 130 -52 C ATOM 1831 CG TYR B 465 -13.206 -4.443 48.165 1.00 21.24 C ANISOU 1831 CG TYR B 465 2996 2252 2821 172 55 -71 C ATOM 1832 CD1 TYR B 465 -12.573 -3.194 48.167 1.00 26.35 C ANISOU 1832 CD1 TYR B 465 3736 2828 3449 137 24 -112 C ATOM 1833 CD2 TYR B 465 -12.897 -5.332 47.140 1.00 20.97 C ANISOU 1833 CD2 TYR B 465 2848 2283 2835 118 21 -46 C ATOM 1834 CE1 TYR B 465 -11.663 -2.854 47.174 1.00 25.74 C ANISOU 1834 CE1 TYR B 465 3624 2750 3407 48 -31 -121 C ATOM 1835 CE2 TYR B 465 -12.006 -4.993 46.149 1.00 24.74 C ANISOU 1835 CE2 TYR B 465 3302 2760 3337 40 -29 -57 C ATOM 1836 CZ TYR B 465 -11.389 -3.764 46.167 1.00 26.02 C ANISOU 1836 CZ TYR B 465 3543 2856 3488 4 -51 -91 C ATOM 1837 OH TYR B 465 -10.504 -3.461 45.161 1.00 27.18 O ANISOU 1837 OH TYR B 465 3658 3001 3666 -77 -87 -93 O ATOM 1838 N VAL B 466 -16.252 -4.172 46.639 1.00 23.19 N ANISOU 1838 N VAL B 466 3100 2505 3206 309 177 84 N ATOM 1839 CA VAL B 466 -16.761 -4.673 45.359 1.00 14.23 C ANISOU 1839 CA VAL B 466 1854 1415 2140 287 149 140 C ATOM 1840 C VAL B 466 -15.595 -5.233 44.570 1.00 24.61 C ANISOU 1840 C VAL B 466 3140 2766 3443 188 76 112 C ATOM 1841 O VAL B 466 -14.723 -4.478 44.143 1.00 16.11 O ANISOU 1841 O VAL B 466 2115 1656 2349 137 44 80 O ATOM 1842 CB VAL B 466 -17.431 -3.552 44.536 1.00 21.19 C ANISOU 1842 CB VAL B 466 2744 2247 3060 320 155 178 C ATOM 1843 CG1 VAL B 466 -17.814 -4.057 43.147 1.00 23.48 C ANISOU 1843 CG1 VAL B 466 2937 2578 3404 286 103 230 C ATOM 1844 CG2 VAL B 466 -18.676 -2.995 45.291 1.00 29.75 C ANISOU 1844 CG2 VAL B 466 3842 3292 4167 435 242 215 C ATOM 1845 N LEU B 467 -15.576 -6.557 44.402 1.00 19.34 N ANISOU 1845 N LEU B 467 2396 2163 2790 163 57 126 N ATOM 1846 CA LEU B 467 -14.505 -7.247 43.706 1.00 20.41 C ANISOU 1846 CA LEU B 467 2504 2336 2915 84 3 102 C ATOM 1847 C LEU B 467 -14.676 -7.034 42.221 1.00 17.97 C ANISOU 1847 C LEU B 467 2167 2025 2636 53 -28 135 C ATOM 1848 O LEU B 467 -15.799 -6.969 41.728 1.00 18.81 O ANISOU 1848 O LEU B 467 2237 2129 2781 88 -26 186 O ATOM 1849 CB LEU B 467 -14.538 -8.769 44.008 1.00 17.17 C ANISOU 1849 CB LEU B 467 2033 1984 2508 78 -2 110 C ATOM 1850 CG LEU B 467 -14.142 -9.174 45.438 1.00 22.79 C ANISOU 1850 CG LEU B 467 2782 2702 3176 101 18 76 C ATOM 1851 CD1 LEU B 467 -14.429 -10.665 45.703 1.00 23.49 C ANISOU 1851 CD1 LEU B 467 2814 2839 3274 106 23 99 C ATOM 1852 CD2 LEU B 467 -12.695 -8.874 45.718 1.00 21.75 C ANISOU 1852 CD2 LEU B 467 2698 2562 3004 52 -24 18 C ATOM 1853 N ASN B 468 -13.567 -6.942 41.504 1.00 15.93 N ANISOU 1853 N ASN B 468 1924 1767 2360 -13 -58 109 N ATOM 1854 CA ASN B 468 -13.608 -6.745 40.046 1.00 25.04 C ANISOU 1854 CA ASN B 468 3075 2916 3525 -44 -82 138 C ATOM 1855 C ASN B 468 -14.048 -8.036 39.308 1.00 25.22 C ANISOU 1855 C ASN B 468 3039 2984 3557 -55 -111 168 C ATOM 1856 O ASN B 468 -13.367 -9.053 39.374 1.00 20.29 O ANISOU 1856 O ASN B 468 2393 2397 2920 -84 -117 145 O ATOM 1857 CB ASN B 468 -12.219 -6.262 39.576 1.00 22.07 C ANISOU 1857 CB ASN B 468 2736 2523 3128 -111 -87 105 C ATOM 1858 CG ASN B 468 -12.168 -5.932 38.092 1.00 26.76 C ANISOU 1858 CG ASN B 468 3351 3100 3717 -141 -98 136 C ATOM 1859 OD1 ASN B 468 -12.211 -6.832 37.243 1.00 22.28 O ANISOU 1859 OD1 ASN B 468 2759 2564 3140 -157 -114 153 O ATOM 1860 ND2 ASN B 468 -12.025 -4.636 37.771 1.00 21.50 N ANISOU 1860 ND2 ASN B 468 2745 2375 3049 -151 -87 142 N ATOM 1861 N LYS B 469 -15.186 -7.993 38.621 1.00 20.73 N ANISOU 1861 N LYS B 469 2449 2410 3016 -30 -134 219 N ATOM 1862 CA LYS B 469 -15.729 -9.181 37.955 1.00 20.05 C ANISOU 1862 CA LYS B 469 2317 2358 2942 -45 -175 247 C ATOM 1863 C LYS B 469 -14.870 -9.689 36.791 1.00 29.01 C ANISOU 1863 C LYS B 469 3488 3499 4034 -102 -202 232 C ATOM 1864 O LYS B 469 -15.073 -10.800 36.320 1.00 21.94 O ANISOU 1864 O LYS B 469 2575 2627 3135 -121 -235 240 O ATOM 1865 CB LYS B 469 -17.158 -8.929 37.465 1.00 27.40 C ANISOU 1865 CB LYS B 469 3212 3277 3921 -10 -211 311 C ATOM 1866 CG LYS B 469 -18.190 -8.840 38.579 1.00 23.95 C ANISOU 1866 CG LYS B 469 2716 2845 3541 53 -173 339 C ATOM 1867 CD LYS B 469 -18.419 -10.215 39.202 1.00 37.36 C ANISOU 1867 CD LYS B 469 4353 4584 5259 43 -167 341 C ATOM 1868 CE LYS B 469 -19.600 -10.923 38.549 1.00 45.90 C ANISOU 1868 CE LYS B 469 5359 5680 6401 35 -226 402 C ATOM 1869 NZ LYS B 469 -19.819 -12.274 39.137 1.00 47.52 N ANISOU 1869 NZ LYS B 469 5511 5916 6629 18 -218 407 N ATOM 1870 N GLY B 470 -13.925 -8.879 36.326 1.00 25.35 N ANISOU 1870 N GLY B 470 3081 3012 3540 -129 -183 212 N ATOM 1871 CA GLY B 470 -13.010 -9.318 35.286 1.00 20.36 C ANISOU 1871 CA GLY B 470 2486 2385 2866 -175 -183 199 C ATOM 1872 C GLY B 470 -11.750 -9.970 35.836 1.00 26.09 C ANISOU 1872 C GLY B 470 3192 3139 3583 -199 -147 153 C ATOM 1873 O GLY B 470 -10.851 -10.308 35.071 1.00 22.70 O ANISOU 1873 O GLY B 470 2785 2713 3125 -230 -127 142 O ATOM 1874 N TYR B 471 -11.698 -10.159 37.158 1.00 16.39 N ANISOU 1874 N TYR B 471 1920 1929 2377 -179 -136 131 N ATOM 1875 CA TYR B 471 -10.535 -10.719 37.835 1.00 23.54 C ANISOU 1875 CA TYR B 471 2802 2862 3281 -195 -116 91 C ATOM 1876 C TYR B 471 -9.266 -9.877 37.632 1.00 31.21 C ANISOU 1876 C TYR B 471 3789 3817 4252 -235 -90 70 C ATOM 1877 O TYR B 471 -8.142 -10.388 37.655 1.00 28.47 O ANISOU 1877 O TYR B 471 3415 3493 3909 -258 -73 49 O ATOM 1878 CB TYR B 471 -10.352 -12.210 37.489 1.00 21.70 C ANISOU 1878 CB TYR B 471 2549 2661 3035 -198 -122 89 C ATOM 1879 CG TYR B 471 -11.555 -12.995 37.960 1.00 23.57 C ANISOU 1879 CG TYR B 471 2760 2909 3285 -168 -148 110 C ATOM 1880 CD1 TYR B 471 -11.609 -13.538 39.245 1.00 20.11 C ANISOU 1880 CD1 TYR B 471 2289 2493 2860 -143 -140 97 C ATOM 1881 CD2 TYR B 471 -12.668 -13.119 37.153 1.00 20.99 C ANISOU 1881 CD2 TYR B 471 2443 2570 2964 -167 -183 147 C ATOM 1882 CE1 TYR B 471 -12.739 -14.230 39.686 1.00 19.93 C ANISOU 1882 CE1 TYR B 471 2238 2476 2857 -119 -151 125 C ATOM 1883 CE2 TYR B 471 -13.793 -13.796 37.587 1.00 23.86 C ANISOU 1883 CE2 TYR B 471 2766 2942 3357 -148 -207 175 C ATOM 1884 CZ TYR B 471 -13.822 -14.344 38.853 1.00 16.66 C ANISOU 1884 CZ TYR B 471 1817 2050 2462 -125 -183 165 C ATOM 1885 OH TYR B 471 -14.959 -15.007 39.254 1.00 21.56 O ANISOU 1885 OH TYR B 471 2395 2677 3120 -110 -194 201 O ATOM 1886 N ASP B 472 -9.469 -8.570 37.488 1.00 21.93 N ANISOU 1886 N ASP B 472 2653 2598 3081 -242 -86 79 N ATOM 1887 CA ASP B 472 -8.367 -7.629 37.371 1.00 21.84 C ANISOU 1887 CA ASP B 472 2658 2560 3080 -289 -63 64 C ATOM 1888 C ASP B 472 -8.267 -6.937 38.719 1.00 28.49 C ANISOU 1888 C ASP B 472 3505 3382 3938 -283 -79 34 C ATOM 1889 O ASP B 472 -8.950 -5.949 38.976 1.00 31.20 O ANISOU 1889 O ASP B 472 3896 3679 4279 -262 -81 40 O ATOM 1890 CB ASP B 472 -8.667 -6.621 36.267 1.00 29.64 C ANISOU 1890 CB ASP B 472 3707 3499 4056 -303 -50 97 C ATOM 1891 CG ASP B 472 -7.447 -5.816 35.870 1.00 49.55 C ANISOU 1891 CG ASP B 472 6243 5992 6592 -364 -14 92 C ATOM 1892 OD1 ASP B 472 -6.753 -5.293 36.771 1.00 51.32 O ANISOU 1892 OD1 ASP B 472 6449 6205 6847 -392 -20 62 O ATOM 1893 OD2 ASP B 472 -7.182 -5.706 34.656 1.00 56.96 O ANISOU 1893 OD2 ASP B 472 7215 6917 7511 -386 18 120 O ATOM 1894 N VAL B 473 -7.421 -7.465 39.588 1.00 22.69 N ANISOU 1894 N VAL B 473 2730 2678 3214 -296 -92 1 N ATOM 1895 CA VAL B 473 -7.504 -7.133 41.010 1.00 23.71 C ANISOU 1895 CA VAL B 473 2878 2794 3337 -277 -118 -31 C ATOM 1896 C VAL B 473 -6.564 -5.993 41.380 1.00 32.51 C ANISOU 1896 C VAL B 473 4020 3863 4468 -332 -136 -58 C ATOM 1897 O VAL B 473 -5.379 -6.023 41.048 1.00 28.01 O ANISOU 1897 O VAL B 473 3406 3306 3931 -390 -139 -64 O ATOM 1898 CB VAL B 473 -7.122 -8.364 41.826 1.00 30.96 C ANISOU 1898 CB VAL B 473 3748 3764 4250 -260 -138 -50 C ATOM 1899 CG1 VAL B 473 -5.908 -8.998 41.185 1.00 45.89 C ANISOU 1899 CG1 VAL B 473 5576 5691 6168 -301 -133 -50 C ATOM 1900 CG2 VAL B 473 -6.870 -8.009 43.284 1.00 22.44 C ANISOU 1900 CG2 VAL B 473 2703 2670 3155 -251 -174 -87 C ATOM 1901 N ASN B 474 -7.092 -4.985 42.061 1.00 31.15 N ANISOU 1901 N ASN B 474 3922 3635 4279 -314 -145 -73 N ATOM 1902 CA ASN B 474 -6.249 -3.891 42.529 1.00 26.52 C ANISOU 1902 CA ASN B 474 3378 2993 3705 -371 -175 -105 C ATOM 1903 C ASN B 474 -5.735 -4.271 43.890 1.00 24.57 C ANISOU 1903 C ASN B 474 3133 2761 3440 -370 -228 -148 C ATOM 1904 O ASN B 474 -6.336 -3.917 44.885 1.00 21.38 O ANISOU 1904 O ASN B 474 2808 2322 2993 -326 -239 -171 O ATOM 1905 CB ASN B 474 -7.032 -2.577 42.615 1.00 34.39 C ANISOU 1905 CB ASN B 474 4477 3908 4684 -349 -160 -103 C ATOM 1906 CG ASN B 474 -6.159 -1.397 43.062 1.00 39.93 C ANISOU 1906 CG ASN B 474 5239 4536 5397 -419 -196 -139 C ATOM 1907 OD1 ASN B 474 -5.053 -1.580 43.570 1.00 42.56 O ANISOU 1907 OD1 ASN B 474 5537 4885 5751 -479 -247 -168 O ATOM 1908 ND2 ASN B 474 -6.664 -0.186 42.877 1.00 35.77 N ANISOU 1908 ND2 ASN B 474 4804 3926 4860 -411 -178 -133 N ATOM 1909 N THR B 475 -4.612 -4.983 43.935 1.00 26.32 N ANISOU 1909 N THR B 475 3274 3032 3694 -414 -260 -157 N ATOM 1910 CA THR B 475 -4.137 -5.546 45.186 1.00 27.73 C ANISOU 1910 CA THR B 475 3448 3234 3853 -404 -321 -191 C ATOM 1911 C THR B 475 -3.699 -4.492 46.187 1.00 27.51 C ANISOU 1911 C THR B 475 3504 3141 3809 -443 -388 -235 C ATOM 1912 O THR B 475 -3.651 -4.765 47.386 1.00 26.30 O ANISOU 1912 O THR B 475 3396 2987 3609 -417 -441 -267 O ATOM 1913 CB THR B 475 -2.984 -6.537 44.982 1.00 33.94 C ANISOU 1913 CB THR B 475 4121 4087 4689 -437 -345 -184 C ATOM 1914 OG1 THR B 475 -1.915 -5.891 44.278 1.00 37.23 O ANISOU 1914 OG1 THR B 475 4483 4489 5175 -521 -349 -176 O ATOM 1915 CG2 THR B 475 -3.467 -7.756 44.211 1.00 35.15 C ANISOU 1915 CG2 THR B 475 4218 4298 4840 -387 -287 -149 C ATOM 1916 N ASN B 476 -3.378 -3.301 45.696 1.00 28.92 N ANISOU 1916 N ASN B 476 3713 3257 4019 -506 -388 -237 N ATOM 1917 CA ASN B 476 -2.990 -2.204 46.571 1.00 34.02 C ANISOU 1917 CA ASN B 476 4456 3823 4648 -552 -457 -282 C ATOM 1918 C ASN B 476 -4.118 -1.839 47.512 1.00 32.51 C ANISOU 1918 C ASN B 476 4404 3581 4368 -470 -444 -308 C ATOM 1919 O ASN B 476 -3.873 -1.348 48.612 1.00 36.16 O ANISOU 1919 O ASN B 476 4965 3989 4784 -481 -510 -355 O ATOM 1920 CB ASN B 476 -2.587 -0.979 45.755 1.00 47.27 C ANISOU 1920 CB ASN B 476 6150 5433 6377 -633 -444 -271 C ATOM 1921 CG ASN B 476 -1.300 -1.194 44.980 1.00 64.90 C ANISOU 1921 CG ASN B 476 8249 7705 8703 -725 -454 -246 C ATOM 1922 OD1 ASN B 476 -0.990 -0.453 44.042 1.00 71.43 O ANISOU 1922 OD1 ASN B 476 9064 8495 9581 -785 -414 -219 O ATOM 1923 ND2 ASN B 476 -0.542 -2.212 45.369 1.00 65.17 N ANISOU 1923 ND2 ASN B 476 8183 7813 8765 -731 -499 -250 N ATOM 1924 N GLN B 477 -5.352 -2.096 47.071 1.00 28.59 N ANISOU 1924 N GLN B 477 3916 3099 3849 -386 -359 -274 N ATOM 1925 CA GLN B 477 -6.547 -1.824 47.865 1.00 33.74 C ANISOU 1925 CA GLN B 477 4680 3710 4431 -293 -319 -284 C ATOM 1926 C GLN B 477 -6.866 -2.924 48.881 1.00 32.60 C ANISOU 1926 C GLN B 477 4537 3616 4232 -227 -323 -292 C ATOM 1927 O GLN B 477 -7.709 -2.748 49.762 1.00 25.64 O ANISOU 1927 O GLN B 477 3757 2700 3286 -150 -289 -304 O ATOM 1928 CB GLN B 477 -7.757 -1.643 46.949 1.00 33.55 C ANISOU 1928 CB GLN B 477 4644 3682 4423 -232 -231 -233 C ATOM 1929 CG GLN B 477 -7.886 -0.267 46.281 1.00 30.46 C ANISOU 1929 CG GLN B 477 4318 3205 4051 -257 -213 -226 C ATOM 1930 CD GLN B 477 -9.279 -0.090 45.672 1.00 40.65 C ANISOU 1930 CD GLN B 477 5613 4487 5345 -170 -135 -176 C ATOM 1931 OE1 GLN B 477 -9.809 -1.010 45.035 1.00 36.25 O ANISOU 1931 OE1 GLN B 477 4962 4001 4811 -139 -107 -132 O ATOM 1932 NE2 GLN B 477 -9.887 1.079 45.889 1.00 33.32 N ANISOU 1932 NE2 GLN B 477 4797 3467 4396 -128 -107 -181 N ATOM 1933 N LEU B 478 -6.208 -4.067 48.758 1.00 30.48 N ANISOU 1933 N LEU B 478 4162 3428 3991 -250 -354 -282 N ATOM 1934 CA LEU B 478 -6.518 -5.194 49.634 1.00 24.58 C ANISOU 1934 CA LEU B 478 3414 2729 3196 -188 -353 -281 C ATOM 1935 C LEU B 478 -5.407 -5.377 50.638 1.00 25.51 C ANISOU 1935 C LEU B 478 3560 2848 3285 -227 -456 -324 C ATOM 1936 O LEU B 478 -4.368 -4.707 50.563 1.00 24.06 O ANISOU 1936 O LEU B 478 3370 2636 3135 -311 -531 -351 O ATOM 1937 CB LEU B 478 -6.661 -6.464 48.804 1.00 20.38 C ANISOU 1937 CB LEU B 478 2754 2281 2710 -175 -317 -236 C ATOM 1938 CG LEU B 478 -7.610 -6.312 47.630 1.00 18.65 C ANISOU 1938 CG LEU B 478 2496 2064 2528 -154 -241 -191 C ATOM 1939 CD1 LEU B 478 -7.766 -7.638 46.904 1.00 21.48 C ANISOU 1939 CD1 LEU B 478 2750 2496 2917 -143 -217 -153 C ATOM 1940 CD2 LEU B 478 -8.953 -5.827 48.138 1.00 23.91 C ANISOU 1940 CD2 LEU B 478 3244 2687 3153 -74 -180 -180 C ATOM 1941 N ILE B 479 -5.609 -6.278 51.588 1.00 20.09 N ANISOU 1941 N ILE B 479 2902 2191 2539 -170 -464 -328 N ATOM 1942 CA ILE B 479 -4.545 -6.585 52.550 1.00 24.17 C ANISOU 1942 CA ILE B 479 3443 2715 3026 -201 -576 -363 C ATOM 1943 C ILE B 479 -3.903 -7.940 52.258 1.00 27.81 C ANISOU 1943 C ILE B 479 3769 3263 3535 -206 -601 -334 C ATOM 1944 O ILE B 479 -4.590 -8.965 52.224 1.00 23.90 O ANISOU 1944 O ILE B 479 3245 2811 3024 -142 -537 -301 O ATOM 1945 CB ILE B 479 -5.061 -6.590 53.989 1.00 30.92 C ANISOU 1945 CB ILE B 479 4458 3530 3762 -131 -585 -390 C ATOM 1946 CG1 ILE B 479 -5.774 -5.267 54.295 1.00 44.71 C ANISOU 1946 CG1 ILE B 479 6352 5181 5454 -109 -543 -418 C ATOM 1947 CG2 ILE B 479 -3.890 -6.848 54.971 1.00 27.77 C ANISOU 1947 CG2 ILE B 479 4093 3132 3325 -169 -726 -427 C ATOM 1948 CD1 ILE B 479 -6.298 -5.178 55.702 1.00 53.07 C ANISOU 1948 CD1 ILE B 479 7592 6189 6385 -33 -534 -448 C ATOM 1949 N ASP B 480 -2.588 -7.939 52.064 1.00 23.78 N ANISOU 1949 N ASP B 480 3175 2774 3088 -282 -691 -344 N ATOM 1950 CA ASP B 480 -1.850 -9.168 51.761 1.00 28.52 C ANISOU 1950 CA ASP B 480 3643 3451 3742 -282 -713 -317 C ATOM 1951 C ASP B 480 -1.688 -9.992 53.033 1.00 29.69 C ANISOU 1951 C ASP B 480 3848 3615 3817 -232 -781 -327 C ATOM 1952 O ASP B 480 -0.933 -9.612 53.923 1.00 30.01 O ANISOU 1952 O ASP B 480 3942 3630 3830 -264 -897 -361 O ATOM 1953 CB ASP B 480 -0.470 -8.826 51.185 1.00 29.86 C ANISOU 1953 CB ASP B 480 3695 3635 4014 -374 -782 -317 C ATOM 1954 CG ASP B 480 0.345 -10.074 50.820 1.00 34.74 C ANISOU 1954 CG ASP B 480 4170 4331 4699 -365 -793 -284 C ATOM 1955 OD1 ASP B 480 -0.070 -11.188 51.193 1.00 27.56 O ANISOU 1955 OD1 ASP B 480 3271 3456 3744 -291 -772 -269 O ATOM 1956 OD2 ASP B 480 1.400 -9.943 50.157 1.00 39.62 O ANISOU 1956 OD2 ASP B 480 4666 4971 5417 -428 -815 -270 O ATOM 1957 N VAL B 481 -2.386 -11.122 53.124 1.00 27.19 N ANISOU 1957 N VAL B 481 3526 3336 3468 -157 -715 -297 N ATOM 1958 CA VAL B 481 -2.321 -11.936 54.341 1.00 24.97 C ANISOU 1958 CA VAL B 481 3316 3065 3108 -102 -766 -300 C ATOM 1959 C VAL B 481 -1.613 -13.261 54.065 1.00 21.47 C ANISOU 1959 C VAL B 481 2752 2688 2718 -88 -789 -267 C ATOM 1960 O VAL B 481 -1.759 -14.229 54.810 1.00 24.12 O ANISOU 1960 O VAL B 481 3128 3039 2997 -28 -799 -253 O ATOM 1961 CB VAL B 481 -3.726 -12.206 54.920 1.00 27.93 C ANISOU 1961 CB VAL B 481 3805 3416 3389 -19 -668 -286 C ATOM 1962 CG1 VAL B 481 -4.385 -10.910 55.357 1.00 29.46 C ANISOU 1962 CG1 VAL B 481 4135 3538 3522 -15 -643 -319 C ATOM 1963 CG2 VAL B 481 -4.583 -12.907 53.886 1.00 21.44 C ANISOU 1963 CG2 VAL B 481 2894 2630 2621 7 -551 -239 C ATOM 1964 N THR B 482 -0.852 -13.305 52.982 1.00 25.52 N ANISOU 1964 N THR B 482 3123 3235 3339 -138 -789 -253 N ATOM 1965 CA THR B 482 -0.182 -14.537 52.578 1.00 26.85 C ANISOU 1965 CA THR B 482 3174 3461 3565 -116 -792 -221 C ATOM 1966 C THR B 482 0.577 -15.169 53.743 1.00 29.68 C ANISOU 1966 C THR B 482 3554 3834 3890 -87 -907 -224 C ATOM 1967 O THR B 482 0.511 -16.377 53.949 1.00 25.00 O ANISOU 1967 O THR B 482 2950 3270 3280 -26 -891 -196 O ATOM 1968 CB THR B 482 0.773 -14.282 51.408 1.00 29.21 C ANISOU 1968 CB THR B 482 3328 3787 3985 -178 -786 -209 C ATOM 1969 OG1 THR B 482 0.022 -13.719 50.336 1.00 28.69 O ANISOU 1969 OG1 THR B 482 3262 3703 3935 -199 -683 -203 O ATOM 1970 CG2 THR B 482 1.450 -15.592 50.936 1.00 28.51 C ANISOU 1970 CG2 THR B 482 3123 3753 3957 -141 -770 -173 C ATOM 1971 N GLU B 483 1.277 -14.357 54.524 1.00 29.84 N ANISOU 1971 N GLU B 483 3615 3828 3896 -132 -1029 -257 N ATOM 1972 CA GLU B 483 2.076 -14.905 55.616 1.00 32.13 C ANISOU 1972 CA GLU B 483 3924 4130 4153 -108 -1162 -259 C ATOM 1973 C GLU B 483 1.273 -15.543 56.752 1.00 31.70 C ANISOU 1973 C GLU B 483 4027 4055 3961 -25 -1155 -258 C ATOM 1974 O GLU B 483 1.791 -16.400 57.460 1.00 37.04 O ANISOU 1974 O GLU B 483 4710 4752 4611 17 -1234 -241 O ATOM 1975 CB GLU B 483 3.081 -13.871 56.140 1.00 44.10 C ANISOU 1975 CB GLU B 483 5443 5620 5694 -189 -1316 -294 C ATOM 1976 CG GLU B 483 4.222 -13.626 55.149 1.00 67.11 C ANISOU 1976 CG GLU B 483 8160 8570 8769 -263 -1340 -275 C ATOM 1977 CD GLU B 483 5.314 -12.702 55.683 1.00 87.93 C ANISOU 1977 CD GLU B 483 10775 11183 11453 -354 -1509 -302 C ATOM 1978 OE1 GLU B 483 6.411 -12.667 55.078 1.00 93.97 O ANISOU 1978 OE1 GLU B 483 11362 11984 12360 -410 -1548 -276 O ATOM 1979 OE2 GLU B 483 5.083 -12.014 56.702 1.00 92.66 O ANISOU 1979 OE2 GLU B 483 11535 11722 11948 -371 -1601 -346 O ATOM 1980 N GLN B 484 0.013 -15.156 56.925 1.00 29.13 N ANISOU 1980 N GLN B 484 3827 3690 3552 2 -1056 -268 N ATOM 1981 CA GLN B 484 -0.809 -15.781 57.971 1.00 26.22 C ANISOU 1981 CA GLN B 484 3605 3300 3057 84 -1024 -258 C ATOM 1982 C GLN B 484 -1.279 -17.173 57.550 1.00 29.13 C ANISOU 1982 C GLN B 484 3912 3709 3448 142 -928 -206 C ATOM 1983 O GLN B 484 -1.849 -17.910 58.354 1.00 29.74 O ANISOU 1983 O GLN B 484 4088 3774 3436 209 -898 -185 O ATOM 1984 CB GLN B 484 -2.036 -14.922 58.284 1.00 25.12 C ANISOU 1984 CB GLN B 484 3608 3104 2832 102 -931 -278 C ATOM 1985 CG GLN B 484 -1.706 -13.470 58.588 1.00 44.24 C ANISOU 1985 CG GLN B 484 6109 5471 5230 43 -1008 -333 C ATOM 1986 CD GLN B 484 -2.934 -12.585 58.568 1.00 50.04 C ANISOU 1986 CD GLN B 484 6952 6151 5912 65 -891 -347 C ATOM 1987 OE1 GLN B 484 -4.071 -13.066 58.700 1.00 48.61 O ANISOU 1987 OE1 GLN B 484 6817 5968 5685 135 -765 -316 O ATOM 1988 NE2 GLN B 484 -2.715 -11.280 58.400 1.00 40.53 N ANISOU 1988 NE2 GLN B 484 5782 4897 4720 5 -929 -389 N ATOM 1989 N PHE B 485 -1.065 -17.518 56.283 1.00 30.35 N ANISOU 1989 N PHE B 485 3914 3902 3716 117 -876 -185 N ATOM 1990 CA PHE B 485 -1.497 -18.819 55.759 1.00 32.12 C ANISOU 1990 CA PHE B 485 4085 4154 3966 164 -788 -140 C ATOM 1991 C PHE B 485 -0.357 -19.804 55.546 1.00 33.33 C ANISOU 1991 C PHE B 485 4132 4349 4185 179 -851 -118 C ATOM 1992 O PHE B 485 -0.559 -20.893 54.988 1.00 34.61 O ANISOU 1992 O PHE B 485 4245 4528 4378 214 -784 -84 O ATOM 1993 CB PHE B 485 -2.263 -18.627 54.447 1.00 28.76 C ANISOU 1993 CB PHE B 485 3591 3732 3603 137 -670 -129 C ATOM 1994 CG PHE B 485 -3.635 -18.082 54.650 1.00 27.46 C ANISOU 1994 CG PHE B 485 3523 3532 3380 150 -583 -130 C ATOM 1995 CD1 PHE B 485 -4.742 -18.914 54.595 1.00 29.22 C ANISOU 1995 CD1 PHE B 485 3768 3751 3583 192 -486 -92 C ATOM 1996 CD2 PHE B 485 -3.818 -16.740 54.944 1.00 20.18 C ANISOU 1996 CD2 PHE B 485 2667 2574 2427 121 -598 -165 C ATOM 1997 CE1 PHE B 485 -6.024 -18.408 54.819 1.00 29.71 C ANISOU 1997 CE1 PHE B 485 3902 3782 3605 210 -400 -83 C ATOM 1998 CE2 PHE B 485 -5.091 -16.227 55.167 1.00 26.54 C ANISOU 1998 CE2 PHE B 485 3558 3344 3183 147 -509 -161 C ATOM 1999 CZ PHE B 485 -6.194 -17.072 55.118 1.00 25.18 C ANISOU 1999 CZ PHE B 485 3392 3175 2999 194 -407 -117 C ATOM 2000 N LYS B 486 0.838 -19.437 55.988 1.00 29.37 N ANISOU 2000 N LYS B 486 3592 3858 3709 154 -982 -135 N ATOM 2001 CA LYS B 486 2.005 -20.269 55.699 1.00 38.68 C ANISOU 2001 CA LYS B 486 4643 5079 4973 172 -1039 -109 C ATOM 2002 C LYS B 486 1.820 -21.716 56.154 1.00 39.79 C ANISOU 2002 C LYS B 486 4823 5225 5070 257 -1022 -70 C ATOM 2003 O LYS B 486 2.271 -22.647 55.490 1.00 41.91 O ANISOU 2003 O LYS B 486 4993 5520 5411 288 -990 -40 O ATOM 2004 CB LYS B 486 3.290 -19.664 56.274 1.00 45.42 C ANISOU 2004 CB LYS B 486 5449 5944 5865 132 -1202 -126 C ATOM 2005 CG LYS B 486 3.132 -18.969 57.623 1.00 66.12 C ANISOU 2005 CG LYS B 486 8230 8523 8368 124 -1310 -160 C ATOM 2006 CD LYS B 486 3.438 -19.894 58.793 1.00 76.52 C ANISOU 2006 CD LYS B 486 9627 9841 9607 196 -1406 -140 C ATOM 2007 CE LYS B 486 3.729 -19.108 60.067 1.00 78.03 C ANISOU 2007 CE LYS B 486 9957 9994 9699 174 -1560 -177 C ATOM 2008 NZ LYS B 486 3.976 -20.005 61.233 1.00 77.73 N ANISOU 2008 NZ LYS B 486 10018 9950 9565 250 -1656 -154 N ATOM 2009 N ASP B 487 1.148 -21.905 57.280 1.00 34.03 N ANISOU 2009 N ASP B 487 4247 4463 4218 299 -1035 -69 N ATOM 2010 CA ASP B 487 0.933 -23.242 57.809 1.00 33.24 C ANISOU 2010 CA ASP B 487 4204 4359 4068 378 -1017 -29 C ATOM 2011 C ASP B 487 -0.492 -23.724 57.522 1.00 32.34 C ANISOU 2011 C ASP B 487 4156 4219 3912 398 -865 -8 C ATOM 2012 O ASP B 487 -0.964 -24.683 58.119 1.00 35.23 O ANISOU 2012 O ASP B 487 4605 4565 4214 455 -833 26 O ATOM 2013 CB ASP B 487 1.228 -23.267 59.308 1.00 49.61 C ANISOU 2013 CB ASP B 487 6410 6411 6030 416 -1137 -31 C ATOM 2014 CG ASP B 487 2.695 -22.995 59.618 1.00 76.46 C ANISOU 2014 CG ASP B 487 9730 9838 9484 399 -1311 -41 C ATOM 2015 OD1 ASP B 487 3.555 -23.295 58.754 1.00 80.37 O ANISOU 2015 OD1 ASP B 487 10055 10374 10108 388 -1322 -25 O ATOM 2016 OD2 ASP B 487 2.991 -22.485 60.725 1.00 84.80 O ANISOU 2016 OD2 ASP B 487 10895 10873 10454 396 -1437 -62 O ATOM 2017 N LYS B 488 -1.169 -23.057 56.596 1.00 22.63 N ANISOU 2017 N LYS B 488 2886 2988 2725 348 -775 -24 N ATOM 2018 CA LYS B 488 -2.549 -23.415 56.251 1.00 19.52 C ANISOU 2018 CA LYS B 488 2534 2571 2310 356 -643 -1 C ATOM 2019 C LYS B 488 -2.654 -23.938 54.843 1.00 25.23 C ANISOU 2019 C LYS B 488 3149 3311 3128 336 -570 12 C ATOM 2020 O LYS B 488 -3.742 -24.264 54.360 1.00 22.98 O ANISOU 2020 O LYS B 488 2877 3009 2846 330 -474 32 O ATOM 2021 CB LYS B 488 -3.435 -22.182 56.395 1.00 29.47 C ANISOU 2021 CB LYS B 488 3857 3808 3531 324 -598 -26 C ATOM 2022 CG LYS B 488 -3.413 -21.593 57.796 1.00 31.76 C ANISOU 2022 CG LYS B 488 4286 4070 3710 348 -659 -46 C ATOM 2023 CD LYS B 488 -4.240 -22.434 58.743 1.00 38.77 C ANISOU 2023 CD LYS B 488 5295 4931 4504 412 -598 -7 C ATOM 2024 CE LYS B 488 -4.330 -21.792 60.129 1.00 43.84 C ANISOU 2024 CE LYS B 488 6106 5537 5016 443 -641 -27 C ATOM 2025 NZ LYS B 488 -5.115 -22.675 61.043 1.00 48.92 N ANISOU 2025 NZ LYS B 488 6870 6150 5565 510 -566 20 N ATOM 2026 N ILE B 489 -1.517 -24.023 54.171 1.00 27.87 N ANISOU 2026 N ILE B 489 3374 3675 3540 324 -618 4 N ATOM 2027 CA ILE B 489 -1.510 -24.480 52.792 1.00 27.14 C ANISOU 2027 CA ILE B 489 3193 3592 3526 309 -547 13 C ATOM 2028 C ILE B 489 -0.943 -25.889 52.683 1.00 29.26 C ANISOU 2028 C ILE B 489 3437 3861 3818 367 -549 43 C ATOM 2029 O ILE B 489 0.181 -26.148 53.090 1.00 26.18 O ANISOU 2029 O ILE B 489 3004 3492 3452 400 -626 47 O ATOM 2030 CB ILE B 489 -0.715 -23.530 51.906 1.00 25.62 C ANISOU 2030 CB ILE B 489 2898 3426 3412 256 -564 -13 C ATOM 2031 CG1 ILE B 489 -1.411 -22.166 51.871 1.00 27.77 C ANISOU 2031 CG1 ILE B 489 3206 3685 3662 200 -549 -40 C ATOM 2032 CG2 ILE B 489 -0.576 -24.114 50.494 1.00 23.38 C ANISOU 2032 CG2 ILE B 489 2540 3148 3195 253 -489 -2 C ATOM 2033 CD1 ILE B 489 -0.570 -21.070 51.246 1.00 27.88 C ANISOU 2033 CD1 ILE B 489 3136 3715 3742 141 -580 -64 C ATOM 2034 N THR B 490 -1.719 -26.802 52.117 1.00 29.91 N ANISOU 2034 N THR B 490 3547 3919 3900 379 -467 64 N ATOM 2035 CA THR B 490 -1.268 -28.189 52.031 1.00 35.70 C ANISOU 2035 CA THR B 490 4279 4639 4648 439 -461 92 C ATOM 2036 C THR B 490 -1.377 -28.690 50.600 1.00 23.07 C ANISOU 2036 C THR B 490 2638 3027 3102 425 -384 91 C ATOM 2037 O THR B 490 -2.453 -28.655 50.019 1.00 25.51 O ANISOU 2037 O THR B 490 2981 3312 3400 385 -323 90 O ATOM 2038 CB THR B 490 -2.130 -29.107 52.922 1.00 37.85 C ANISOU 2038 CB THR B 490 4663 4871 4848 474 -440 125 C ATOM 2039 OG1 THR B 490 -2.093 -28.632 54.269 1.00 44.38 O ANISOU 2039 OG1 THR B 490 5555 5703 5606 492 -503 126 O ATOM 2040 CG2 THR B 490 -1.608 -30.542 52.884 1.00 41.25 C ANISOU 2040 CG2 THR B 490 5104 5278 5292 540 -439 155 C ATOM 2041 N TYR B 491 -0.276 -29.148 50.028 1.00 20.35 N ANISOU 2041 N TYR B 491 2223 2695 2815 462 -388 92 N ATOM 2042 CA TYR B 491 -0.351 -29.803 48.710 1.00 22.43 C ANISOU 2042 CA TYR B 491 2478 2934 3112 464 -309 91 C ATOM 2043 C TYR B 491 -0.812 -31.256 48.847 1.00 26.18 C ANISOU 2043 C TYR B 491 3037 3354 3555 511 -280 117 C ATOM 2044 O TYR B 491 -0.420 -31.950 49.772 1.00 29.13 O ANISOU 2044 O TYR B 491 3436 3720 3910 571 -321 141 O ATOM 2045 CB TYR B 491 0.977 -29.682 47.941 1.00 20.75 C ANISOU 2045 CB TYR B 491 2160 2751 2974 489 -299 85 C ATOM 2046 CG TYR B 491 1.206 -28.252 47.504 1.00 23.79 C ANISOU 2046 CG TYR B 491 2472 3174 3393 423 -304 62 C ATOM 2047 CD1 TYR B 491 0.705 -27.787 46.291 1.00 21.71 C ANISOU 2047 CD1 TYR B 491 2214 2899 3134 372 -234 45 C ATOM 2048 CD2 TYR B 491 1.873 -27.350 48.327 1.00 28.59 C ANISOU 2048 CD2 TYR B 491 3019 3821 4022 406 -387 56 C ATOM 2049 CE1 TYR B 491 0.884 -26.477 45.897 1.00 26.06 C ANISOU 2049 CE1 TYR B 491 2711 3478 3714 311 -235 28 C ATOM 2050 CE2 TYR B 491 2.048 -26.027 47.944 1.00 23.82 C ANISOU 2050 CE2 TYR B 491 2360 3242 3451 338 -392 35 C ATOM 2051 CZ TYR B 491 1.545 -25.598 46.737 1.00 23.28 C ANISOU 2051 CZ TYR B 491 2297 3161 3388 292 -312 23 C ATOM 2052 OH TYR B 491 1.713 -24.295 46.339 1.00 28.40 O ANISOU 2052 OH TYR B 491 2899 3826 4067 226 -312 6 O ATOM 2053 N GLY B 492 -1.685 -31.697 47.950 1.00 20.52 N ANISOU 2053 N GLY B 492 2372 2594 2828 479 -217 114 N ATOM 2054 CA GLY B 492 -2.184 -33.065 47.996 1.00 26.20 C ANISOU 2054 CA GLY B 492 3180 3251 3524 509 -191 137 C ATOM 2055 C GLY B 492 -2.007 -33.817 46.687 1.00 29.45 C ANISOU 2055 C GLY B 492 3616 3619 3955 520 -134 125 C ATOM 2056 O GLY B 492 -1.368 -33.320 45.752 1.00 25.88 O ANISOU 2056 O GLY B 492 3108 3191 3536 518 -107 102 O ATOM 2057 N ALA B 493 -2.616 -35.000 46.610 1.00 24.01 N ANISOU 2057 N ALA B 493 3022 2860 3242 529 -112 141 N ATOM 2058 CA ALA B 493 -2.444 -35.899 45.476 1.00 25.38 C ANISOU 2058 CA ALA B 493 3251 2973 3419 550 -63 128 C ATOM 2059 C ALA B 493 -3.165 -35.421 44.225 1.00 22.89 C ANISOU 2059 C ALA B 493 2958 2643 3098 472 -36 99 C ATOM 2060 O ALA B 493 -4.159 -34.704 44.304 1.00 25.19 O ANISOU 2060 O ALA B 493 3239 2950 3381 396 -56 100 O ATOM 2061 CB ALA B 493 -2.928 -37.326 45.846 1.00 25.71 C ANISOU 2061 CB ALA B 493 3404 2931 3436 574 -57 154 C ATOM 2062 N ASN B 494 -2.684 -35.859 43.065 1.00 14.33 N ANISOU 2062 N ASN B 494 1912 1522 2012 498 11 77 N ATOM 2063 CA ASN B 494 -3.399 -35.589 41.822 1.00 17.66 C ANISOU 2063 CA ASN B 494 2386 1913 2410 429 29 51 C ATOM 2064 C ASN B 494 -3.551 -34.085 41.583 1.00 24.89 C ANISOU 2064 C ASN B 494 3218 2900 3341 371 17 39 C ATOM 2065 O ASN B 494 -4.635 -33.595 41.254 1.00 19.92 O ANISOU 2065 O ASN B 494 2607 2264 2697 292 -7 36 O ATOM 2066 CB ASN B 494 -4.754 -36.309 41.855 1.00 16.20 C ANISOU 2066 CB ASN B 494 2297 1658 2202 363 -2 62 C ATOM 2067 CG ASN B 494 -4.593 -37.853 41.997 1.00 19.77 C ANISOU 2067 CG ASN B 494 2852 2021 2637 416 13 73 C ATOM 2068 OD1 ASN B 494 -5.136 -38.501 42.908 1.00 24.19 O ANISOU 2068 OD1 ASN B 494 3442 2550 3198 408 -11 105 O ATOM 2069 ND2 ASN B 494 -3.835 -38.417 41.103 1.00 15.43 N ANISOU 2069 ND2 ASN B 494 2363 1428 2071 473 60 48 N ATOM 2070 N ASP B 495 -2.453 -33.367 41.807 1.00 19.97 N ANISOU 2070 N ASP B 495 2496 2342 2751 412 30 37 N ATOM 2071 CA ASP B 495 -2.300 -31.964 41.409 1.00 23.46 C ANISOU 2071 CA ASP B 495 2862 2842 3210 368 33 24 C ATOM 2072 C ASP B 495 -3.271 -31.058 42.140 1.00 17.33 C ANISOU 2072 C ASP B 495 2057 2097 2431 301 -21 31 C ATOM 2073 O ASP B 495 -3.948 -30.248 41.525 1.00 22.16 O ANISOU 2073 O ASP B 495 2672 2714 3033 239 -23 22 O ATOM 2074 CB ASP B 495 -2.450 -31.805 39.883 1.00 22.72 C ANISOU 2074 CB ASP B 495 2827 2716 3089 339 81 1 C ATOM 2075 CG ASP B 495 -1.241 -32.317 39.139 1.00 28.44 C ANISOU 2075 CG ASP B 495 3557 3425 3822 415 158 -7 C ATOM 2076 OD1 ASP B 495 -0.187 -31.638 39.171 1.00 29.86 O ANISOU 2076 OD1 ASP B 495 3634 3660 4050 444 189 -2 O ATOM 2077 OD2 ASP B 495 -1.333 -33.415 38.548 1.00 34.78 O ANISOU 2077 OD2 ASP B 495 4470 4157 4589 448 191 -16 O ATOM 2078 N SER B 496 -3.337 -31.221 43.457 1.00 21.06 N ANISOU 2078 N SER B 496 2510 2586 2907 321 -60 51 N ATOM 2079 CA SER B 496 -4.270 -30.463 44.271 1.00 21.14 C ANISOU 2079 CA SER B 496 2507 2618 2907 272 -97 62 C ATOM 2080 C SER B 496 -3.489 -29.708 45.323 1.00 18.73 C ANISOU 2080 C SER B 496 2134 2368 2616 298 -133 62 C ATOM 2081 O SER B 496 -2.393 -30.118 45.722 1.00 18.82 O ANISOU 2081 O SER B 496 2113 2395 2644 358 -146 66 O ATOM 2082 CB SER B 496 -5.278 -31.405 44.944 1.00 18.80 C ANISOU 2082 CB SER B 496 2279 2277 2589 267 -105 90 C ATOM 2083 OG SER B 496 -4.618 -32.243 45.870 1.00 27.87 O ANISOU 2083 OG SER B 496 3442 3417 3730 334 -117 107 O ATOM 2084 N VAL B 497 -4.049 -28.581 45.735 1.00 19.77 N ANISOU 2084 N VAL B 497 2245 2527 2741 253 -153 58 N ATOM 2085 CA VAL B 497 -3.557 -27.822 46.884 1.00 18.01 C ANISOU 2085 CA VAL B 497 1986 2344 2514 267 -201 56 C ATOM 2086 C VAL B 497 -4.767 -27.343 47.713 1.00 20.54 C ANISOU 2086 C VAL B 497 2350 2656 2797 239 -206 67 C ATOM 2087 O VAL B 497 -5.816 -27.006 47.158 1.00 20.81 O ANISOU 2087 O VAL B 497 2397 2675 2833 194 -177 71 O ATOM 2088 CB VAL B 497 -2.682 -26.638 46.454 1.00 17.67 C ANISOU 2088 CB VAL B 497 1866 2340 2507 243 -213 32 C ATOM 2089 CG1 VAL B 497 -3.478 -25.640 45.618 1.00 23.42 C ANISOU 2089 CG1 VAL B 497 2597 3064 3236 179 -185 19 C ATOM 2090 CG2 VAL B 497 -2.067 -25.959 47.691 1.00 25.56 C ANISOU 2090 CG2 VAL B 497 2838 3370 3502 254 -282 26 C ATOM 2091 N ASN B 498 -4.628 -27.362 49.033 1.00 21.17 N ANISOU 2091 N ASN B 498 2456 2743 2843 272 -241 78 N ATOM 2092 CA ASN B 498 -5.719 -27.038 49.942 1.00 20.15 C ANISOU 2092 CA ASN B 498 2382 2602 2671 263 -228 94 C ATOM 2093 C ASN B 498 -5.331 -25.848 50.799 1.00 30.10 C ANISOU 2093 C ASN B 498 3645 3889 3904 264 -273 73 C ATOM 2094 O ASN B 498 -4.216 -25.787 51.318 1.00 25.69 O ANISOU 2094 O ASN B 498 3071 3350 3340 291 -335 60 O ATOM 2095 CB ASN B 498 -6.022 -28.235 50.843 1.00 22.81 C ANISOU 2095 CB ASN B 498 2787 2909 2970 307 -220 131 C ATOM 2096 CG ASN B 498 -6.347 -29.487 50.044 1.00 35.28 C ANISOU 2096 CG ASN B 498 4379 4450 4577 303 -184 151 C ATOM 2097 OD1 ASN B 498 -7.464 -29.644 49.566 1.00 41.36 O ANISOU 2097 OD1 ASN B 498 5159 5194 5361 260 -144 167 O ATOM 2098 ND2 ASN B 498 -5.361 -30.367 49.866 1.00 35.70 N ANISOU 2098 ND2 ASN B 498 4429 4496 4639 348 -204 149 N ATOM 2099 N VAL B 499 -6.241 -24.889 50.933 1.00 18.03 N ANISOU 2099 N VAL B 499 2134 2355 2360 235 -246 69 N ATOM 2100 CA VAL B 499 -5.965 -23.734 51.778 1.00 14.96 C ANISOU 2100 CA VAL B 499 1773 1977 1935 236 -285 45 C ATOM 2101 C VAL B 499 -7.039 -23.722 52.860 1.00 20.77 C ANISOU 2101 C VAL B 499 2596 2687 2607 262 -243 69 C ATOM 2102 O VAL B 499 -8.230 -23.652 52.569 1.00 19.27 O ANISOU 2102 O VAL B 499 2408 2482 2432 248 -173 93 O ATOM 2103 CB VAL B 499 -6.049 -22.408 50.993 1.00 19.03 C ANISOU 2103 CB VAL B 499 2247 2500 2485 186 -280 17 C ATOM 2104 CG1 VAL B 499 -5.737 -21.242 51.899 1.00 22.74 C ANISOU 2104 CG1 VAL B 499 2761 2968 2913 184 -326 -12 C ATOM 2105 CG2 VAL B 499 -5.109 -22.421 49.782 1.00 18.23 C ANISOU 2105 CG2 VAL B 499 2060 2419 2447 157 -295 1 C ATOM 2106 N ASP B 500 -6.610 -23.762 54.106 1.00 16.46 N ANISOU 2106 N ASP B 500 2124 2136 1992 303 -286 66 N ATOM 2107 CA ASP B 500 -7.532 -23.814 55.229 1.00 20.84 C ANISOU 2107 CA ASP B 500 2781 2664 2473 339 -235 92 C ATOM 2108 C ASP B 500 -7.822 -22.391 55.703 1.00 24.61 C ANISOU 2108 C ASP B 500 3310 3131 2909 334 -231 62 C ATOM 2109 O ASP B 500 -6.946 -21.743 56.285 1.00 22.27 O ANISOU 2109 O ASP B 500 3056 2837 2570 337 -314 24 O ATOM 2110 CB ASP B 500 -6.859 -24.597 56.351 1.00 22.97 C ANISOU 2110 CB ASP B 500 3129 2926 2673 392 -289 104 C ATOM 2111 CG ASP B 500 -7.756 -24.805 57.557 1.00 38.32 C ANISOU 2111 CG ASP B 500 5196 4837 4527 438 -224 139 C ATOM 2112 OD1 ASP B 500 -8.885 -24.258 57.602 1.00 37.98 O ANISOU 2112 OD1 ASP B 500 5172 4777 4481 432 -134 153 O ATOM 2113 OD2 ASP B 500 -7.318 -25.538 58.469 1.00 46.68 O ANISOU 2113 OD2 ASP B 500 6333 5883 5519 485 -261 157 O ATOM 2114 N PHE B 501 -9.035 -21.910 55.450 1.00 23.75 N ANISOU 2114 N PHE B 501 3198 3007 2818 326 -141 81 N ATOM 2115 CA PHE B 501 -9.430 -20.568 55.874 1.00 23.65 C ANISOU 2115 CA PHE B 501 3244 2975 2767 332 -121 56 C ATOM 2116 C PHE B 501 -10.019 -20.504 57.291 1.00 30.30 C ANISOU 2116 C PHE B 501 4222 3783 3506 394 -67 73 C ATOM 2117 O PHE B 501 -10.103 -19.419 57.863 1.00 30.12 O ANISOU 2117 O PHE B 501 4284 3736 3427 411 -65 43 O ATOM 2118 CB PHE B 501 -10.434 -19.961 54.885 1.00 19.61 C ANISOU 2118 CB PHE B 501 2659 2462 2329 304 -50 71 C ATOM 2119 CG PHE B 501 -9.809 -19.500 53.591 1.00 19.79 C ANISOU 2119 CG PHE B 501 2587 2507 2426 246 -103 41 C ATOM 2120 CD1 PHE B 501 -9.351 -18.203 53.459 1.00 21.59 C ANISOU 2120 CD1 PHE B 501 2827 2727 2649 223 -142 -3 C ATOM 2121 CD2 PHE B 501 -9.659 -20.365 52.528 1.00 17.43 C ANISOU 2121 CD2 PHE B 501 2201 2230 2194 215 -111 57 C ATOM 2122 CE1 PHE B 501 -8.771 -17.757 52.294 1.00 21.10 C ANISOU 2122 CE1 PHE B 501 2685 2681 2652 170 -180 -24 C ATOM 2123 CE2 PHE B 501 -9.082 -19.922 51.333 1.00 17.63 C ANISOU 2123 CE2 PHE B 501 2153 2271 2275 167 -147 32 C ATOM 2124 CZ PHE B 501 -8.635 -18.610 51.226 1.00 24.17 C ANISOU 2124 CZ PHE B 501 2987 3094 3101 145 -178 -5 C ATOM 2125 N GLY B 502 -10.459 -21.638 57.844 1.00 31.04 N ANISOU 2125 N GLY B 502 4352 3869 3574 429 -16 123 N ATOM 2126 CA GLY B 502 -11.134 -21.620 59.147 1.00 27.80 C ANISOU 2126 CA GLY B 502 4077 3423 3063 492 62 150 C ATOM 2127 C GLY B 502 -12.426 -20.798 59.137 1.00 28.36 C ANISOU 2127 C GLY B 502 4152 3473 3152 510 185 172 C ATOM 2128 O GLY B 502 -13.260 -20.930 58.234 1.00 28.88 O ANISOU 2128 O GLY B 502 4102 3551 3320 481 248 207 O ATOM 2129 N SER B 503 -12.602 -19.950 60.143 1.00 20.71 N ANISOU 2129 N SER B 503 3319 2467 2082 561 219 152 N ATOM 2130 CA SER B 503 -13.800 -19.123 60.234 1.00 25.13 C ANISOU 2130 CA SER B 503 3893 3002 2654 595 347 175 C ATOM 2131 C SER B 503 -13.563 -17.783 59.553 1.00 28.28 C ANISOU 2131 C SER B 503 4260 3397 3089 565 299 120 C ATOM 2132 O SER B 503 -12.681 -17.034 59.952 1.00 26.49 O ANISOU 2132 O SER B 503 4125 3152 2789 561 208 56 O ATOM 2133 CB SER B 503 -14.201 -18.908 61.704 1.00 33.21 C ANISOU 2133 CB SER B 503 5103 3975 3540 680 433 186 C ATOM 2134 OG SER B 503 -14.501 -20.155 62.316 1.00 42.50 O ANISOU 2134 OG SER B 503 6312 5150 4686 708 493 248 O ATOM 2135 N ILE B 504 -14.342 -17.495 58.514 1.00 25.21 N ANISOU 2135 N ILE B 504 3742 3024 2815 540 352 146 N ATOM 2136 CA ILE B 504 -14.224 -16.222 57.805 1.00 25.51 C ANISOU 2136 CA ILE B 504 3749 3052 2889 514 317 104 C ATOM 2137 C ILE B 504 -15.582 -15.583 57.527 1.00 25.24 C ANISOU 2137 C ILE B 504 3671 3001 2917 552 442 148 C ATOM 2138 O ILE B 504 -16.619 -16.247 57.522 1.00 25.84 O ANISOU 2138 O ILE B 504 3683 3087 3048 574 542 219 O ATOM 2139 CB ILE B 504 -13.467 -16.362 56.461 1.00 30.82 C ANISOU 2139 CB ILE B 504 4290 3767 3653 431 212 81 C ATOM 2140 CG1 ILE B 504 -14.148 -17.389 55.549 1.00 26.72 C ANISOU 2140 CG1 ILE B 504 3634 3281 3237 402 249 140 C ATOM 2141 CG2 ILE B 504 -11.990 -16.710 56.707 1.00 28.38 C ANISOU 2141 CG2 ILE B 504 4016 3473 3296 399 84 31 C ATOM 2142 CD1 ILE B 504 -13.624 -17.368 54.093 1.00 21.39 C ANISOU 2142 CD1 ILE B 504 2843 2637 2648 330 169 121 C ATOM 2143 N ASN B 505 -15.551 -14.285 57.273 1.00 18.47 N ANISOU 2143 N ASN B 505 2844 2116 2059 556 431 109 N ATOM 2144 CA ASN B 505 -16.744 -13.545 56.922 1.00 23.73 C ANISOU 2144 CA ASN B 505 3464 2763 2790 597 535 149 C ATOM 2145 C ASN B 505 -16.387 -12.471 55.892 1.00 23.73 C ANISOU 2145 C ASN B 505 3420 2756 2841 552 464 109 C ATOM 2146 O ASN B 505 -17.263 -11.769 55.407 1.00 31.46 O ANISOU 2146 O ASN B 505 4350 3720 3884 580 526 139 O ATOM 2147 CB ASN B 505 -17.350 -12.922 58.175 1.00 38.06 C ANISOU 2147 CB ASN B 505 5429 4520 4511 695 653 153 C ATOM 2148 CG ASN B 505 -16.343 -12.103 58.945 1.00 49.49 C ANISOU 2148 CG ASN B 505 7057 5919 5827 702 577 68 C ATOM 2149 OD1 ASN B 505 -16.100 -10.942 58.626 1.00 51.54 O ANISOU 2149 OD1 ASN B 505 7354 6143 6085 692 540 22 O ATOM 2150 ND2 ASN B 505 -15.727 -12.712 59.947 1.00 57.94 N ANISOU 2150 ND2 ASN B 505 8244 6984 6788 714 543 48 N ATOM 2151 N ASN B 506 -15.097 -12.364 55.561 1.00 25.62 N ANISOU 2151 N ASN B 506 3672 3006 3057 484 335 48 N ATOM 2152 CA ASN B 506 -14.629 -11.500 54.481 1.00 20.67 C ANISOU 2152 CA ASN B 506 2993 2376 2484 427 264 16 C ATOM 2153 C ASN B 506 -14.529 -12.323 53.197 1.00 22.84 C ANISOU 2153 C ASN B 506 3114 2707 2856 362 219 45 C ATOM 2154 O ASN B 506 -14.455 -13.557 53.239 1.00 18.80 O ANISOU 2154 O ASN B 506 2555 2234 2355 349 212 70 O ATOM 2155 CB ASN B 506 -13.216 -10.942 54.760 1.00 20.62 C ANISOU 2155 CB ASN B 506 3073 2350 2414 378 149 -61 C ATOM 2156 CG ASN B 506 -13.165 -9.912 55.908 1.00 33.50 C ANISOU 2156 CG ASN B 506 4881 3908 3938 428 164 -106 C ATOM 2157 OD1 ASN B 506 -12.790 -8.742 55.711 1.00 36.82 O ANISOU 2157 OD1 ASN B 506 5357 4282 4351 404 124 -150 O ATOM 2158 ND2 ASN B 506 -13.477 -10.358 57.102 1.00 26.28 N ANISOU 2158 ND2 ASN B 506 4071 2978 2936 492 218 -98 N ATOM 2159 N SER B 507 -14.455 -11.633 52.061 1.00 17.77 N ANISOU 2159 N SER B 507 2413 2065 2276 320 185 39 N ATOM 2160 CA SER B 507 -14.071 -12.287 50.821 1.00 18.23 C ANISOU 2160 CA SER B 507 2358 2166 2400 253 127 50 C ATOM 2161 C SER B 507 -12.538 -12.319 50.737 1.00 24.48 C ANISOU 2161 C SER B 507 3169 2970 3162 195 31 -7 C ATOM 2162 O SER B 507 -11.859 -11.469 51.343 1.00 18.25 O ANISOU 2162 O SER B 507 2465 2147 2321 191 -3 -55 O ATOM 2163 CB SER B 507 -14.711 -11.579 49.631 1.00 23.01 C ANISOU 2163 CB SER B 507 2901 2765 3078 239 135 76 C ATOM 2164 OG SER B 507 -14.242 -10.257 49.519 1.00 37.53 O ANISOU 2164 OG SER B 507 4802 4561 4895 230 113 36 O ATOM 2165 N TYR B 508 -11.995 -13.320 50.032 1.00 15.06 N ANISOU 2165 N TYR B 508 1899 1820 2004 151 -10 0 N ATOM 2166 CA TYR B 508 -10.550 -13.465 49.888 1.00 14.15 C ANISOU 2166 CA TYR B 508 1775 1722 1879 103 -90 -41 C ATOM 2167 C TYR B 508 -10.204 -13.683 48.431 1.00 21.71 C ANISOU 2167 C TYR B 508 2646 2704 2900 50 -111 -32 C ATOM 2168 O TYR B 508 -10.982 -14.265 47.680 1.00 20.63 O ANISOU 2168 O TYR B 508 2458 2580 2800 51 -81 6 O ATOM 2169 CB TYR B 508 -10.007 -14.632 50.735 1.00 19.28 C ANISOU 2169 CB TYR B 508 2439 2396 2490 120 -116 -44 C ATOM 2170 CG TYR B 508 -10.037 -14.361 52.217 1.00 22.18 C ANISOU 2170 CG TYR B 508 2918 2735 2774 167 -114 -62 C ATOM 2171 CD1 TYR B 508 -8.876 -14.019 52.903 1.00 17.81 C ANISOU 2171 CD1 TYR B 508 2421 2173 2175 150 -198 -109 C ATOM 2172 CD2 TYR B 508 -11.231 -14.409 52.921 1.00 18.01 C ANISOU 2172 CD2 TYR B 508 2443 2186 2215 228 -28 -30 C ATOM 2173 CE1 TYR B 508 -8.902 -13.751 54.268 1.00 15.68 C ANISOU 2173 CE1 TYR B 508 2278 1869 1811 193 -206 -130 C ATOM 2174 CE2 TYR B 508 -11.272 -14.128 54.280 1.00 20.53 C ANISOU 2174 CE2 TYR B 508 2887 2472 2442 278 -14 -47 C ATOM 2175 CZ TYR B 508 -10.102 -13.809 54.949 1.00 22.11 C ANISOU 2175 CZ TYR B 508 3162 2659 2580 260 -109 -100 C ATOM 2176 OH TYR B 508 -10.146 -13.538 56.304 1.00 27.37 O ANISOU 2176 OH TYR B 508 3976 3286 3139 311 -105 -121 O ATOM 2177 N VAL B 509 -9.041 -13.187 48.030 1.00 13.48 N ANISOU 2177 N VAL B 509 1591 1663 1869 2 -161 -66 N ATOM 2178 CA VAL B 509 -8.590 -13.319 46.654 1.00 11.44 C ANISOU 2178 CA VAL B 509 1265 1423 1659 -44 -168 -58 C ATOM 2179 C VAL B 509 -7.370 -14.229 46.711 1.00 18.09 C ANISOU 2179 C VAL B 509 2066 2300 2509 -60 -208 -72 C ATOM 2180 O VAL B 509 -6.418 -13.950 47.414 1.00 18.98 O ANISOU 2180 O VAL B 509 2189 2412 2611 -72 -256 -101 O ATOM 2181 CB VAL B 509 -8.199 -11.962 46.057 1.00 20.47 C ANISOU 2181 CB VAL B 509 2421 2536 2822 -86 -178 -75 C ATOM 2182 CG1 VAL B 509 -7.632 -12.143 44.652 1.00 18.82 C ANISOU 2182 CG1 VAL B 509 2153 2343 2653 -131 -175 -64 C ATOM 2183 CG2 VAL B 509 -9.412 -11.015 46.028 1.00 17.71 C ANISOU 2183 CG2 VAL B 509 2117 2146 2466 -58 -139 -58 C ATOM 2184 N VAL B 510 -7.416 -15.343 46.004 1.00 15.44 N ANISOU 2184 N VAL B 510 1685 1989 2193 -57 -191 -50 N ATOM 2185 CA VAL B 510 -6.323 -16.296 46.063 1.00 15.28 C ANISOU 2185 CA VAL B 510 1625 1997 2183 -56 -218 -58 C ATOM 2186 C VAL B 510 -5.683 -16.346 44.678 1.00 19.02 C ANISOU 2186 C VAL B 510 2049 2482 2697 -91 -200 -55 C ATOM 2187 O VAL B 510 -6.360 -16.647 43.690 1.00 17.17 O ANISOU 2187 O VAL B 510 1817 2240 2466 -95 -166 -35 O ATOM 2188 CB VAL B 510 -6.832 -17.699 46.437 1.00 14.26 C ANISOU 2188 CB VAL B 510 1503 1879 2035 -15 -204 -36 C ATOM 2189 CG1 VAL B 510 -5.682 -18.726 46.350 1.00 19.14 C ANISOU 2189 CG1 VAL B 510 2080 2522 2669 -6 -226 -40 C ATOM 2190 CG2 VAL B 510 -7.418 -17.693 47.838 1.00 14.84 C ANISOU 2190 CG2 VAL B 510 1634 1941 2062 24 -206 -33 C ATOM 2191 N MET B 511 -4.387 -16.057 44.588 1.00 14.60 N ANISOU 2191 N MET B 511 1444 1935 2168 -116 -222 -71 N ATOM 2192 CA MET B 511 -3.735 -16.072 43.283 1.00 14.01 C ANISOU 2192 CA MET B 511 1325 1867 2131 -144 -186 -63 C ATOM 2193 C MET B 511 -2.787 -17.259 43.201 1.00 18.49 C ANISOU 2193 C MET B 511 1841 2464 2722 -117 -181 -58 C ATOM 2194 O MET B 511 -1.865 -17.357 43.986 1.00 18.55 O ANISOU 2194 O MET B 511 1806 2491 2752 -111 -225 -67 O ATOM 2195 CB MET B 511 -2.963 -14.760 43.055 1.00 18.68 C ANISOU 2195 CB MET B 511 1892 2446 2758 -198 -195 -74 C ATOM 2196 CG MET B 511 -3.882 -13.512 43.198 1.00 24.66 C ANISOU 2196 CG MET B 511 2714 3164 3491 -217 -199 -80 C ATOM 2197 SD MET B 511 -3.034 -12.014 42.628 1.00 44.68 S ANISOU 2197 SD MET B 511 5234 5672 6071 -290 -196 -86 S ATOM 2198 CE MET B 511 -4.291 -10.771 42.876 1.00 42.20 C ANISOU 2198 CE MET B 511 5013 5303 5719 -288 -198 -91 C ATOM 2199 N VAL B 512 -3.032 -18.163 42.260 1.00 15.08 N ANISOU 2199 N VAL B 512 1419 2030 2281 -98 -135 -43 N ATOM 2200 CA VAL B 512 -2.219 -19.368 42.141 1.00 18.23 C ANISOU 2200 CA VAL B 512 1783 2447 2697 -59 -119 -38 C ATOM 2201 C VAL B 512 -1.350 -19.222 40.902 1.00 22.91 C ANISOU 2201 C VAL B 512 2340 3042 3325 -74 -57 -31 C ATOM 2202 O VAL B 512 -1.870 -19.091 39.793 1.00 25.99 O ANISOU 2202 O VAL B 512 2778 3409 3688 -89 -12 -24 O ATOM 2203 CB VAL B 512 -3.087 -20.629 42.014 1.00 21.59 C ANISOU 2203 CB VAL B 512 2264 2856 3083 -23 -105 -28 C ATOM 2204 CG1 VAL B 512 -2.210 -21.910 41.998 1.00 20.80 C ANISOU 2204 CG1 VAL B 512 2140 2766 2999 28 -89 -23 C ATOM 2205 CG2 VAL B 512 -4.083 -20.688 43.166 1.00 21.75 C ANISOU 2205 CG2 VAL B 512 2321 2870 3071 -12 -146 -26 C ATOM 2206 N ASP B 513 -0.032 -19.228 41.102 1.00 14.12 N ANISOU 2206 N ASP B 513 1141 1955 2270 -68 -57 -28 N ATOM 2207 CA ASP B 513 0.924 -19.148 39.998 1.00 17.16 C ANISOU 2207 CA ASP B 513 1477 2344 2698 -73 20 -13 C ATOM 2208 C ASP B 513 1.680 -20.474 39.899 1.00 25.68 C ANISOU 2208 C ASP B 513 2520 3438 3800 -5 55 -2 C ATOM 2209 O ASP B 513 2.243 -20.957 40.892 1.00 22.92 O ANISOU 2209 O ASP B 513 2112 3112 3483 27 2 0 O ATOM 2210 CB ASP B 513 1.925 -18.021 40.265 1.00 26.49 C ANISOU 2210 CB ASP B 513 2566 3543 3955 -125 1 -9 C ATOM 2211 CG ASP B 513 2.905 -17.828 39.122 1.00 60.08 C ANISOU 2211 CG ASP B 513 6761 7801 8264 -136 97 16 C ATOM 2212 OD1 ASP B 513 2.740 -18.493 38.078 1.00 74.06 O ANISOU 2212 OD1 ASP B 513 8585 9557 9999 -100 181 25 O ATOM 2213 OD2 ASP B 513 3.842 -17.010 39.260 1.00 74.59 O ANISOU 2213 OD2 ASP B 513 8506 9652 10181 -182 90 28 O ATOM 2214 N THR B 514 1.714 -21.054 38.707 1.00 24.29 N ANISOU 2214 N THR B 514 2387 3242 3602 21 144 6 N ATOM 2215 CA THR B 514 2.267 -22.396 38.551 1.00 25.11 C ANISOU 2215 CA THR B 514 2485 3344 3713 97 187 14 C ATOM 2216 C THR B 514 2.876 -22.556 37.160 1.00 30.56 C ANISOU 2216 C THR B 514 3189 4018 4406 118 309 28 C ATOM 2217 O THR B 514 2.668 -21.687 36.310 1.00 29.04 O ANISOU 2217 O THR B 514 3030 3810 4193 70 351 31 O ATOM 2218 CB THR B 514 1.173 -23.477 38.831 1.00 21.00 C ANISOU 2218 CB THR B 514 2069 2793 3118 128 152 1 C ATOM 2219 OG1 THR B 514 1.795 -24.745 39.059 1.00 23.97 O ANISOU 2219 OG1 THR B 514 2431 3167 3511 205 171 9 O ATOM 2220 CG2 THR B 514 0.209 -23.606 37.649 1.00 20.72 C ANISOU 2220 CG2 THR B 514 2153 2710 3008 109 193 -7 C ATOM 2221 N LYS B 515 3.642 -23.637 36.939 1.00 21.80 N ANISOU 2221 N LYS B 515 2058 2905 3318 196 370 39 N ATOM 2222 CA LYS B 515 4.263 -23.911 35.633 1.00 23.31 C ANISOU 2222 CA LYS B 515 2278 3075 3505 234 505 54 C ATOM 2223 C LYS B 515 3.465 -24.943 34.830 1.00 21.41 C ANISOU 2223 C LYS B 515 2203 2774 3159 273 541 34 C ATOM 2224 O LYS B 515 2.912 -25.868 35.394 1.00 21.38 O ANISOU 2224 O LYS B 515 2250 2751 3122 301 483 19 O ATOM 2225 CB LYS B 515 5.709 -24.420 35.795 1.00 28.59 C ANISOU 2225 CB LYS B 515 2815 3774 4274 305 568 84 C ATOM 2226 CG LYS B 515 6.657 -23.468 36.551 1.00 36.14 C ANISOU 2226 CG LYS B 515 3592 4789 5353 263 523 109 C ATOM 2227 CD LYS B 515 6.710 -22.081 35.897 1.00 40.85 C ANISOU 2227 CD LYS B 515 4170 5386 5964 176 563 118 C ATOM 2228 CE LYS B 515 7.584 -21.098 36.690 1.00 47.62 C ANISOU 2228 CE LYS B 515 4858 6291 6944 118 501 140 C ATOM 2229 NZ LYS B 515 8.087 -19.976 35.835 1.00 49.02 N ANISOU 2229 NZ LYS B 515 4990 6466 7170 53 589 167 N ATOM 2230 N PHE B 516 3.391 -24.771 33.514 1.00 21.42 N ANISOU 2230 N PHE B 516 2299 2738 3101 269 634 34 N ATOM 2231 CA PHE B 516 2.748 -25.762 32.676 1.00 23.02 C ANISOU 2231 CA PHE B 516 2672 2875 3200 305 665 13 C ATOM 2232 C PHE B 516 3.561 -27.042 32.766 1.00 33.84 C ANISOU 2232 C PHE B 516 4035 4230 4594 406 730 17 C ATOM 2233 O PHE B 516 4.761 -26.990 33.051 1.00 33.24 O ANISOU 2233 O PHE B 516 3822 4195 4614 453 790 45 O ATOM 2234 CB PHE B 516 2.743 -25.315 31.205 1.00 19.59 C ANISOU 2234 CB PHE B 516 2348 2402 2695 293 764 15 C ATOM 2235 CG PHE B 516 1.625 -24.355 30.850 1.00 25.13 C ANISOU 2235 CG PHE B 516 3123 3090 3334 205 692 7 C ATOM 2236 CD1 PHE B 516 0.316 -24.802 30.736 1.00 25.95 C ANISOU 2236 CD1 PHE B 516 3352 3151 3354 178 600 -17 C ATOM 2237 CD2 PHE B 516 1.887 -23.021 30.617 1.00 20.56 C ANISOU 2237 CD2 PHE B 516 2485 2537 2788 151 717 29 C ATOM 2238 CE1 PHE B 516 -0.711 -23.917 30.391 1.00 26.06 C ANISOU 2238 CE1 PHE B 516 3423 3155 3323 106 531 -18 C ATOM 2239 CE2 PHE B 516 0.862 -22.134 30.271 1.00 24.75 C ANISOU 2239 CE2 PHE B 516 3088 3052 3264 81 653 25 C ATOM 2240 CZ PHE B 516 -0.434 -22.591 30.168 1.00 23.17 C ANISOU 2240 CZ PHE B 516 3003 2815 2985 63 559 3 C ATOM 2241 N GLU B 517 2.914 -28.175 32.501 1.00 43.95 N ANISOU 2241 N GLU B 517 7422 5066 4210 3158 505 -2057 N ATOM 2242 CA GLU B 517 3.621 -29.427 32.212 1.00 45.85 C ANISOU 2242 CA GLU B 517 7608 5353 4461 3215 530 -2121 C ATOM 2243 C GLU B 517 4.130 -29.404 30.778 1.00 44.16 C ANISOU 2243 C GLU B 517 7006 5539 4233 3284 404 -2109 C ATOM 2244 O GLU B 517 3.503 -28.826 29.890 1.00 45.89 O ANISOU 2244 O GLU B 517 6972 5989 4475 3286 396 -2170 O ATOM 2245 CB GLU B 517 2.682 -30.625 32.342 1.00 54.39 C ANISOU 2245 CB GLU B 517 8728 6291 5647 3201 804 -2403 C ATOM 2246 CG GLU B 517 2.520 -31.208 33.725 1.00 66.79 C ANISOU 2246 CG GLU B 517 10692 7458 7228 3152 947 -2434 C ATOM 2247 CD GLU B 517 1.640 -32.447 33.707 1.00 78.16 C ANISOU 2247 CD GLU B 517 12129 8791 8778 3145 1215 -2718 C ATOM 2248 OE1 GLU B 517 0.765 -32.583 34.594 1.00 82.45 O ANISOU 2248 OE1 GLU B 517 12912 9047 9368 3082 1402 -2824 O ATOM 2249 OE2 GLU B 517 1.818 -33.277 32.784 1.00 81.96 O ANISOU 2249 OE2 GLU B 517 12363 9479 9298 3202 1242 -2838 O ATOM 2250 N TYR B 518 5.257 -30.053 30.538 1.00 44.32 N ANISOU 2250 N TYR B 518 6980 5641 4220 3341 309 -2036 N ATOM 2251 CA TYR B 518 5.727 -30.232 29.173 1.00 49.09 C ANISOU 2251 CA TYR B 518 7223 6612 4817 3408 223 -2054 C ATOM 2252 C TYR B 518 4.796 -31.186 28.428 1.00 58.10 C ANISOU 2252 C TYR B 518 8169 7854 6053 3423 431 -2347 C ATOM 2253 O TYR B 518 4.305 -32.160 29.002 1.00 51.88 O ANISOU 2253 O TYR B 518 7538 6842 5331 3406 624 -2514 O ATOM 2254 CB TYR B 518 7.161 -30.755 29.150 1.00 53.88 C ANISOU 2254 CB TYR B 518 7835 7259 5376 3464 85 -1914 C ATOM 2255 CG TYR B 518 7.560 -31.324 27.813 1.00 62.64 C ANISOU 2255 CG TYR B 518 8599 8702 6498 3534 62 -1993 C ATOM 2256 CD1 TYR B 518 7.561 -30.533 26.673 1.00 65.89 C ANISOU 2256 CD1 TYR B 518 8708 9451 6877 3557 -52 -1947 C ATOM 2257 CD2 TYR B 518 7.942 -32.652 27.691 1.00 67.77 C ANISOU 2257 CD2 TYR B 518 9230 9329 7192 3576 154 -2115 C ATOM 2258 CE1 TYR B 518 7.924 -31.052 25.441 1.00 68.18 C ANISOU 2258 CE1 TYR B 518 8690 10045 7172 3619 -68 -2022 C ATOM 2259 CE2 TYR B 518 8.308 -33.181 26.468 1.00 71.58 C ANISOU 2259 CE2 TYR B 518 9399 10114 7685 3639 138 -2192 C ATOM 2260 CZ TYR B 518 8.298 -32.379 25.345 1.00 74.53 C ANISOU 2260 CZ TYR B 518 9480 10819 8020 3660 29 -2146 C ATOM 2261 OH TYR B 518 8.667 -32.907 24.125 1.00 76.58 O ANISOU 2261 OH TYR B 518 9436 11378 8282 3721 17 -2223 O ATOM 2262 N THR B 519 4.540 -30.891 27.156 1.00 57.41 N ANISOU 2262 N THR B 519 7745 8098 5971 3455 391 -2407 N ATOM 2263 CA THR B 519 3.614 -31.684 26.357 1.00 59.24 C ANISOU 2263 CA THR B 519 7769 8449 6291 3470 571 -2682 C ATOM 2264 C THR B 519 4.054 -31.785 24.902 1.00 65.24 C ANISOU 2264 C THR B 519 8165 9597 7024 3535 476 -2701 C ATOM 2265 O THR B 519 4.707 -30.886 24.365 1.00 68.53 O ANISOU 2265 O THR B 519 8448 10229 7362 3555 279 -2514 O ATOM 2266 CB THR B 519 2.190 -31.090 26.387 1.00 64.15 C ANISOU 2266 CB THR B 519 8375 9022 6977 3414 687 -2813 C ATOM 2267 OG1 THR B 519 1.289 -31.977 25.716 1.00 67.46 O ANISOU 2267 OG1 THR B 519 8617 9520 7495 3427 873 -3092 O ATOM 2268 CG2 THR B 519 2.154 -29.725 25.703 1.00 52.42 C ANISOU 2268 CG2 THR B 519 6702 7780 5436 3411 511 -2675 C ATOM 2269 N THR B 520 3.679 -32.886 24.267 1.00 65.17 N ANISOU 2269 N THR B 520 8002 9674 7083 3567 623 -2929 N ATOM 2270 CA THR B 520 3.913 -33.065 22.845 1.00 71.23 C ANISOU 2270 CA THR B 520 8424 10805 7834 3625 566 -2988 C ATOM 2271 C THR B 520 2.574 -33.074 22.103 1.00 68.58 C ANISOU 2271 C THR B 520 7894 10589 7574 3611 694 -3220 C ATOM 2272 O THR B 520 2.506 -33.413 20.923 1.00 68.35 O ANISOU 2272 O THR B 520 7585 10836 7550 3654 695 -3332 O ATOM 2273 CB THR B 520 4.692 -34.374 22.579 1.00 74.54 C ANISOU 2273 CB THR B 520 8794 11261 8268 3683 612 -3061 C ATOM 2274 OG1 THR B 520 4.767 -34.617 21.171 1.00 82.01 O ANISOU 2274 OG1 THR B 520 9403 12554 9205 3736 586 -3153 O ATOM 2275 CG2 THR B 520 4.007 -35.552 23.252 1.00 70.51 C ANISOU 2275 CG2 THR B 520 8449 10483 7857 3663 845 -3281 C ATOM 2276 N SER B 521 1.518 -32.656 22.796 1.00 64.85 N ANISOU 2276 N SER B 521 7572 9908 7161 3548 797 -3286 N ATOM 2277 CA SER B 521 0.147 -32.890 22.341 1.00 71.38 C ANISOU 2277 CA SER B 521 8267 10762 8092 3528 962 -3541 C ATOM 2278 C SER B 521 -0.266 -32.266 21.006 1.00 85.37 C ANISOU 2278 C SER B 521 9709 12878 9851 3550 875 -3583 C ATOM 2279 O SER B 521 -0.980 -32.902 20.224 1.00 93.00 O ANISOU 2279 O SER B 521 10482 13965 10889 3568 988 -3810 O ATOM 2280 CB SER B 521 -0.855 -32.488 23.420 1.00 66.20 C ANISOU 2280 CB SER B 521 7850 9797 7505 3454 1086 -3585 C ATOM 2281 OG SER B 521 -2.177 -32.543 22.916 1.00 72.85 O ANISOU 2281 OG SER B 521 8540 10685 8453 3434 1221 -3814 O ATOM 2282 N ALA B 522 0.159 -31.029 20.758 1.00 84.38 N ANISOU 2282 N ALA B 522 9524 12900 9635 3547 675 -3368 N ATOM 2283 CA ALA B 522 -0.243 -30.292 19.552 1.00 88.20 C ANISOU 2283 CA ALA B 522 9717 13697 10098 3561 576 -3385 C ATOM 2284 C ALA B 522 -1.594 -29.593 19.717 1.00 85.78 C ANISOU 2284 C ALA B 522 9416 13303 9873 3505 646 -3485 C ATOM 2285 O ALA B 522 -1.884 -28.612 19.027 1.00 87.20 O ANISOU 2285 O ALA B 522 9426 13683 10024 3501 525 -3428 O ATOM 2286 CB ALA B 522 -0.237 -31.195 18.306 1.00 92.75 C ANISOU 2286 CB ALA B 522 10016 14537 10687 3619 619 -3562 C ATOM 2287 N SER B 523 -2.413 -30.105 20.633 1.00 80.98 N ANISOU 2287 N SER B 523 9004 12394 9372 3461 842 -3634 N ATOM 2288 CA SER B 523 -3.641 -29.427 21.045 1.00 71.98 C ANISOU 2288 CA SER B 523 7923 11106 8320 3400 921 -3711 C ATOM 2289 C SER B 523 -3.742 -29.453 22.560 1.00 67.40 C ANISOU 2289 C SER B 523 7699 10140 7769 3345 1026 -3663 C ATOM 2290 O SER B 523 -4.687 -30.019 23.112 1.00 60.32 O ANISOU 2290 O SER B 523 6913 9017 6989 3308 1235 -3856 O ATOM 2291 CB SER B 523 -4.871 -30.105 20.445 1.00 77.70 C ANISOU 2291 CB SER B 523 8477 11866 9178 3399 1097 -4013 C ATOM 2292 OG SER B 523 -4.947 -31.461 20.855 1.00 84.40 O ANISOU 2292 OG SER B 523 9430 12542 10097 3398 1280 -4175 O ATOM 2293 N PRO B 524 -2.761 -28.839 23.240 1.00 44.90 N ANISOU 2293 N PRO B 524 5895 5546 5620 -289 -641 -953 N ATOM 2294 CA PRO B 524 -2.718 -28.834 24.706 1.00 46.88 C ANISOU 2294 CA PRO B 524 6145 5734 5933 -227 -588 -895 C ATOM 2295 C PRO B 524 -4.003 -28.246 25.284 1.00 43.43 C ANISOU 2295 C PRO B 524 5639 5329 5532 -219 -598 -803 C ATOM 2296 O PRO B 524 -4.511 -27.255 24.746 1.00 41.47 O ANISOU 2296 O PRO B 524 5356 5159 5243 -218 -633 -764 O ATOM 2297 CB PRO B 524 -1.547 -27.892 25.022 1.00 43.48 C ANISOU 2297 CB PRO B 524 5759 5308 5455 -150 -555 -886 C ATOM 2298 CG PRO B 524 -0.760 -27.793 23.758 1.00 50.02 C ANISOU 2298 CG PRO B 524 6625 6172 6207 -176 -582 -960 C ATOM 2299 CD PRO B 524 -1.741 -27.953 22.651 1.00 48.77 C ANISOU 2299 CD PRO B 524 6426 6077 6029 -254 -643 -974 C ATOM 2300 N THR B 525 -4.511 -28.856 26.354 1.00 36.40 N ANISOU 2300 N THR B 525 4731 4380 4720 -212 -566 -768 N ATOM 2301 CA THR B 525 -5.669 -28.346 27.099 1.00 29.32 C ANISOU 2301 CA THR B 525 3770 3502 3867 -198 -564 -680 C ATOM 2302 C THR B 525 -5.274 -28.133 28.567 1.00 29.97 C ANISOU 2302 C THR B 525 3868 3531 3988 -123 -501 -629 C ATOM 2303 O THR B 525 -4.573 -28.969 29.158 1.00 28.94 O ANISOU 2303 O THR B 525 3780 3328 3886 -108 -461 -659 O ATOM 2304 CB THR B 525 -6.859 -29.329 27.039 1.00 35.88 C ANISOU 2304 CB THR B 525 4554 4318 4761 -270 -584 -683 C ATOM 2305 OG1 THR B 525 -7.243 -29.538 25.677 1.00 40.96 O ANISOU 2305 OG1 THR B 525 5178 5019 5364 -343 -643 -735 O ATOM 2306 CG2 THR B 525 -8.069 -28.791 27.826 1.00 34.13 C ANISOU 2306 CG2 THR B 525 4265 4117 4587 -255 -580 -592 C ATOM 2307 N LEU B 526 -5.713 -27.008 29.132 1.00 24.48 N ANISOU 2307 N LEU B 526 3137 2874 3291 -77 -491 -553 N ATOM 2308 CA LEU B 526 -5.507 -26.680 30.540 1.00 22.25 C ANISOU 2308 CA LEU B 526 2856 2555 3042 -10 -434 -499 C ATOM 2309 C LEU B 526 -6.864 -26.665 31.255 1.00 24.28 C ANISOU 2309 C LEU B 526 3047 2814 3364 -22 -429 -428 C ATOM 2310 O LEU B 526 -7.792 -25.976 30.826 1.00 28.57 O ANISOU 2310 O LEU B 526 3537 3416 3904 -39 -464 -389 O ATOM 2311 CB LEU B 526 -4.855 -25.291 30.658 1.00 26.78 C ANISOU 2311 CB LEU B 526 3443 3171 3563 56 -417 -474 C ATOM 2312 CG LEU B 526 -4.819 -24.664 32.051 1.00 17.54 C ANISOU 2312 CG LEU B 526 2260 1984 2419 123 -361 -412 C ATOM 2313 CD1 LEU B 526 -4.016 -25.541 33.008 1.00 15.82 C ANISOU 2313 CD1 LEU B 526 2087 1698 2227 151 -313 -434 C ATOM 2314 CD2 LEU B 526 -4.219 -23.229 32.028 1.00 17.99 C ANISOU 2314 CD2 LEU B 526 2325 2087 2425 180 -345 -394 C ATOM 2315 N VAL B 527 -7.003 -27.441 32.319 1.00 19.56 N ANISOU 2315 N VAL B 527 2451 2153 2826 -14 -388 -410 N ATOM 2316 CA VAL B 527 -8.224 -27.372 33.129 1.00 22.53 C ANISOU 2316 CA VAL B 527 2768 2529 3265 -19 -375 -339 C ATOM 2317 C VAL B 527 -7.808 -27.289 34.579 1.00 23.04 C ANISOU 2317 C VAL B 527 2848 2551 3354 45 -311 -298 C ATOM 2318 O VAL B 527 -6.958 -28.055 35.029 1.00 16.29 O ANISOU 2318 O VAL B 527 2044 1641 2506 62 -279 -327 O ATOM 2319 CB VAL B 527 -9.140 -28.598 32.929 1.00 20.77 C ANISOU 2319 CB VAL B 527 2517 2273 3101 -94 -393 -356 C ATOM 2320 CG1 VAL B 527 -10.426 -28.466 33.779 1.00 21.56 C ANISOU 2320 CG1 VAL B 527 2550 2375 3265 -99 -378 -282 C ATOM 2321 CG2 VAL B 527 -9.483 -28.771 31.458 1.00 21.66 C ANISOU 2321 CG2 VAL B 527 2614 2432 3183 -162 -458 -408 C ATOM 2322 N GLN B 528 -8.377 -26.342 35.307 1.00 18.47 N ANISOU 2322 N GLN B 528 2227 2003 2789 81 -290 -230 N ATOM 2323 CA GLN B 528 -8.030 -26.202 36.714 1.00 16.49 C ANISOU 2323 CA GLN B 528 1986 1722 2557 139 -228 -191 C ATOM 2324 C GLN B 528 -9.259 -25.781 37.495 1.00 21.04 C ANISOU 2324 C GLN B 528 2497 2314 3185 140 -211 -117 C ATOM 2325 O GLN B 528 -9.878 -24.745 37.197 1.00 18.90 O ANISOU 2325 O GLN B 528 2179 2096 2905 145 -229 -84 O ATOM 2326 CB GLN B 528 -6.877 -25.204 36.888 1.00 15.15 C ANISOU 2326 CB GLN B 528 1853 1577 2327 206 -204 -201 C ATOM 2327 CG GLN B 528 -6.333 -25.175 38.298 1.00 16.18 C ANISOU 2327 CG GLN B 528 2001 1680 2466 264 -141 -174 C ATOM 2328 CD GLN B 528 -4.967 -24.578 38.353 1.00 25.20 C ANISOU 2328 CD GLN B 528 3191 2835 3547 319 -119 -209 C ATOM 2329 OE1 GLN B 528 -4.779 -23.440 38.820 1.00 26.38 O ANISOU 2329 OE1 GLN B 528 3327 3021 3673 365 -92 -184 O ATOM 2330 NE2 GLN B 528 -3.990 -25.332 37.875 1.00 13.33 N ANISOU 2330 NE2 GLN B 528 1743 1302 2019 314 -129 -270 N ATOM 2331 N MET B 529 -9.617 -26.608 38.473 1.00 17.94 N ANISOU 2331 N MET B 529 2098 1871 2847 135 -175 -91 N ATOM 2332 CA MET B 529 -10.857 -26.466 39.229 1.00 20.72 C ANISOU 2332 CA MET B 529 2387 2228 3257 125 -157 -26 C ATOM 2333 C MET B 529 -10.607 -25.876 40.621 1.00 20.01 C ANISOU 2333 C MET B 529 2296 2137 3170 190 -94 23 C ATOM 2334 O MET B 529 -9.535 -26.031 41.193 1.00 23.67 O ANISOU 2334 O MET B 529 2811 2578 3606 234 -59 8 O ATOM 2335 CB MET B 529 -11.528 -27.839 39.400 1.00 21.57 C ANISOU 2335 CB MET B 529 2486 2281 3430 69 -155 -28 C ATOM 2336 CG MET B 529 -11.724 -28.618 38.105 1.00 19.10 C ANISOU 2336 CG MET B 529 2177 1961 3118 -1 -210 -86 C ATOM 2337 SD MET B 529 -12.845 -27.688 37.032 1.00 25.41 S ANISOU 2337 SD MET B 529 2904 2845 3907 -39 -274 -72 S ATOM 2338 CE MET B 529 -14.449 -27.996 37.809 1.00 27.25 C ANISOU 2338 CE MET B 529 3059 3068 4227 -75 -257 -9 C ATOM 2339 N ALA B 530 -11.625 -25.235 41.176 1.00 17.08 N ANISOU 2339 N ALA B 530 1863 1791 2834 193 -79 82 N ATOM 2340 CA ALA B 530 -11.513 -24.668 42.498 1.00 18.75 C ANISOU 2340 CA ALA B 530 2066 2007 3050 247 -18 127 C ATOM 2341 C ALA B 530 -12.786 -25.025 43.259 1.00 18.30 C ANISOU 2341 C ALA B 530 1954 1936 3065 220 4 182 C ATOM 2342 O ALA B 530 -13.878 -24.912 42.714 1.00 21.32 O ANISOU 2342 O ALA B 530 2281 2338 3482 178 -30 198 O ATOM 2343 CB ALA B 530 -11.344 -23.147 42.401 1.00 18.60 C ANISOU 2343 CB ALA B 530 2027 2045 2995 291 -12 139 C ATOM 2344 N THR B 531 -12.657 -25.434 44.515 1.00 16.89 N ANISOU 2344 N THR B 531 1787 1727 2905 245 60 212 N ATOM 2345 CA THR B 531 -13.819 -25.911 45.269 1.00 18.21 C ANISOU 2345 CA THR B 531 1906 1873 3140 216 85 262 C ATOM 2346 C THR B 531 -13.797 -25.370 46.701 1.00 20.25 C ANISOU 2346 C THR B 531 2151 2143 3400 266 151 311 C ATOM 2347 O THR B 531 -12.784 -25.432 47.372 1.00 18.00 O ANISOU 2347 O THR B 531 1912 1850 3076 312 187 303 O ATOM 2348 CB THR B 531 -13.814 -27.481 45.325 1.00 26.88 C ANISOU 2348 CB THR B 531 3035 2903 4275 176 87 248 C ATOM 2349 OG1 THR B 531 -13.984 -28.003 44.001 1.00 32.12 O ANISOU 2349 OG1 THR B 531 3703 3559 4944 120 28 200 O ATOM 2350 CG2 THR B 531 -14.956 -28.016 46.194 1.00 22.95 C ANISOU 2350 CG2 THR B 531 2493 2379 3848 148 122 302 C ATOM 2351 N LEU B 532 -14.915 -24.858 47.180 1.00 19.56 N ANISOU 2351 N LEU B 532 1998 2077 3356 257 169 358 N ATOM 2352 CA LEU B 532 -14.972 -24.332 48.537 1.00 19.85 C ANISOU 2352 CA LEU B 532 2019 2129 3396 298 235 402 C ATOM 2353 C LEU B 532 -15.953 -25.178 49.336 1.00 21.62 C ANISOU 2353 C LEU B 532 2212 2318 3684 265 265 447 C ATOM 2354 O LEU B 532 -17.068 -25.449 48.892 1.00 22.18 O ANISOU 2354 O LEU B 532 2236 2383 3810 213 239 460 O ATOM 2355 CB LEU B 532 -15.445 -22.872 48.530 1.00 20.64 C ANISOU 2355 CB LEU B 532 2064 2284 3494 321 242 421 C ATOM 2356 CG LEU B 532 -15.770 -22.219 49.896 1.00 20.34 C ANISOU 2356 CG LEU B 532 1992 2266 3470 354 311 466 C ATOM 2357 CD1 LEU B 532 -14.530 -22.141 50.780 1.00 22.05 C ANISOU 2357 CD1 LEU B 532 2262 2488 3629 408 358 452 C ATOM 2358 CD2 LEU B 532 -16.384 -20.814 49.736 1.00 19.90 C ANISOU 2358 CD2 LEU B 532 1876 2257 3427 369 316 484 C ATOM 2359 N THR B 533 -15.521 -25.612 50.504 1.00 19.23 N ANISOU 2359 N THR B 533 1936 1996 3373 294 320 470 N ATOM 2360 CA THR B 533 -16.362 -26.363 51.415 1.00 26.24 C ANISOU 2360 CA THR B 533 2800 2852 4317 269 360 519 C ATOM 2361 C THR B 533 -16.369 -25.620 52.757 1.00 27.11 C ANISOU 2361 C THR B 533 2890 2998 4413 314 425 560 C ATOM 2362 O THR B 533 -15.422 -24.909 53.071 1.00 22.14 O ANISOU 2362 O THR B 533 2287 2403 3724 366 443 543 O ATOM 2363 CB THR B 533 -15.813 -27.793 51.631 1.00 28.39 C ANISOU 2363 CB THR B 533 3130 3062 4596 259 370 515 C ATOM 2364 OG1 THR B 533 -14.422 -27.726 51.939 1.00 29.42 O ANISOU 2364 OG1 THR B 533 3321 3199 4659 316 385 493 O ATOM 2365 CG2 THR B 533 -15.978 -28.667 50.372 1.00 34.53 C ANISOU 2365 CG2 THR B 533 3921 3798 5401 203 313 473 C ATOM 2366 N SER B 534 -17.441 -25.783 53.528 1.00 23.24 N ANISOU 2366 N SER B 534 2352 2502 3976 291 461 609 N ATOM 2367 CA SER B 534 -17.560 -25.177 54.854 1.00 20.07 C ANISOU 2367 CA SER B 534 1926 2133 3565 326 528 648 C ATOM 2368 C SER B 534 -18.673 -25.896 55.639 1.00 24.06 C ANISOU 2368 C SER B 534 2395 2609 4135 289 565 701 C ATOM 2369 O SER B 534 -19.519 -26.569 55.046 1.00 29.62 O ANISOU 2369 O SER B 534 3077 3279 4899 233 536 704 O ATOM 2370 CB SER B 534 -17.815 -23.658 54.764 1.00 17.37 C ANISOU 2370 CB SER B 534 1536 1850 3213 349 532 643 C ATOM 2371 OG SER B 534 -19.074 -23.321 54.184 1.00 20.72 O ANISOU 2371 OG SER B 534 1894 2280 3700 308 506 657 O ATOM 2372 N ASP B 535 -18.653 -25.789 56.964 1.00 21.83 N ANISOU 2372 N ASP B 535 2109 2344 3841 316 631 740 N ATOM 2373 CA ASP B 535 -19.613 -26.504 57.793 1.00 30.39 C ANISOU 2373 CA ASP B 535 3165 3401 4982 283 674 792 C ATOM 2374 C ASP B 535 -21.028 -26.112 57.438 1.00 27.06 C ANISOU 2374 C ASP B 535 2666 2985 4631 236 661 806 C ATOM 2375 O ASP B 535 -21.327 -24.929 57.333 1.00 23.52 O ANISOU 2375 O ASP B 535 2172 2584 4180 251 661 799 O ATOM 2376 CB ASP B 535 -19.389 -26.177 59.273 1.00 31.57 C ANISOU 2376 CB ASP B 535 3313 3585 5097 324 747 830 C ATOM 2377 CG ASP B 535 -18.127 -26.802 59.823 1.00 42.57 C ANISOU 2377 CG ASP B 535 4777 4970 6427 367 766 831 C ATOM 2378 OD1 ASP B 535 -17.636 -27.797 59.226 1.00 37.40 O ANISOU 2378 OD1 ASP B 535 4171 4264 5775 356 733 817 O ATOM 2379 OD2 ASP B 535 -17.636 -26.305 60.860 1.00 48.66 O ANISOU 2379 OD2 ASP B 535 5554 5789 7147 410 815 846 O ATOM 2380 N GLY B 536 -21.891 -27.109 57.268 1.00 23.67 N ANISOU 2380 N GLY B 536 2220 2508 4267 181 655 824 N ATOM 2381 CA GLY B 536 -23.316 -26.894 57.139 1.00 22.34 C ANISOU 2381 CA GLY B 536 1973 2344 4172 133 653 845 C ATOM 2382 C GLY B 536 -23.724 -26.353 55.779 1.00 33.94 C ANISOU 2382 C GLY B 536 3404 3831 5658 109 582 808 C ATOM 2383 O GLY B 536 -24.872 -25.973 55.593 1.00 30.40 O ANISOU 2383 O GLY B 536 2885 3400 5266 77 575 823 O ATOM 2384 N ASN B 537 -22.796 -26.319 54.823 1.00 25.74 N ANISOU 2384 N ASN B 537 2413 2794 4573 124 530 762 N ATOM 2385 CA ASN B 537 -23.156 -25.967 53.454 1.00 27.74 C ANISOU 2385 CA ASN B 537 2637 3064 4839 96 458 728 C ATOM 2386 C ASN B 537 -22.660 -27.026 52.478 1.00 22.93 C ANISOU 2386 C ASN B 537 2079 2412 4222 63 407 686 C ATOM 2387 O ASN B 537 -21.613 -27.633 52.713 1.00 25.07 O ANISOU 2387 O ASN B 537 2421 2653 4454 87 421 672 O ATOM 2388 CB ASN B 537 -22.525 -24.623 53.071 1.00 26.14 C ANISOU 2388 CB ASN B 537 2435 2915 4582 147 441 708 C ATOM 2389 CG ASN B 537 -22.957 -23.491 53.975 1.00 29.10 C ANISOU 2389 CG ASN B 537 2759 3332 4965 181 494 742 C ATOM 2390 OD1 ASN B 537 -24.084 -23.001 53.884 1.00 27.50 O ANISOU 2390 OD1 ASN B 537 2483 3149 4817 158 492 765 O ATOM 2391 ND2 ASN B 537 -22.053 -23.055 54.843 1.00 35.69 N ANISOU 2391 ND2 ASN B 537 3631 4183 5747 234 543 742 N ATOM 2392 N ARG B 538 -23.393 -27.236 51.387 1.00 23.53 N ANISOU 2392 N ARG B 538 2117 2489 4335 10 350 664 N ATOM 2393 CA ARG B 538 -22.911 -28.091 50.298 1.00 25.98 C ANISOU 2393 CA ARG B 538 2471 2769 4634 -23 296 613 C ATOM 2394 C ARG B 538 -21.711 -27.412 49.659 1.00 25.87 C ANISOU 2394 C ARG B 538 2505 2783 4541 24 263 574 C ATOM 2395 O ARG B 538 -21.607 -26.187 49.691 1.00 20.71 O ANISOU 2395 O ARG B 538 1829 2181 3859 65 264 583 O ATOM 2396 CB ARG B 538 -23.999 -28.315 49.251 1.00 26.28 C ANISOU 2396 CB ARG B 538 2448 2816 4720 -92 240 595 C ATOM 2397 CG ARG B 538 -25.128 -29.250 49.709 1.00 31.17 C ANISOU 2397 CG ARG B 538 3026 3396 5421 -152 267 619 C ATOM 2398 CD ARG B 538 -26.306 -29.137 48.763 1.00 33.18 C ANISOU 2398 CD ARG B 538 3203 3683 5721 -211 212 606 C ATOM 2399 NE ARG B 538 -26.784 -27.761 48.687 1.00 31.04 N ANISOU 2399 NE ARG B 538 2870 3482 5442 -180 199 633 N ATOM 2400 CZ ARG B 538 -27.331 -27.202 47.613 1.00 32.58 C ANISOU 2400 CZ ARG B 538 3012 3729 5638 -200 135 617 C ATOM 2401 NH1 ARG B 538 -27.476 -27.896 46.493 1.00 35.69 N ANISOU 2401 NH1 ARG B 538 3404 4120 6035 -257 75 571 N ATOM 2402 NH2 ARG B 538 -27.735 -25.937 47.658 1.00 29.97 N ANISOU 2402 NH2 ARG B 538 2627 3455 5306 -164 132 649 N ATOM 2403 N SER B 539 -20.795 -28.203 49.104 1.00 20.87 N ANISOU 2403 N SER B 539 1938 2114 3878 18 240 530 N ATOM 2404 CA SER B 539 -19.596 -27.643 48.499 1.00 20.75 C ANISOU 2404 CA SER B 539 1973 2123 3789 61 211 490 C ATOM 2405 C SER B 539 -19.989 -26.950 47.208 1.00 21.92 C ANISOU 2405 C SER B 539 2083 2319 3928 39 144 463 C ATOM 2406 O SER B 539 -21.037 -27.241 46.622 1.00 21.11 O ANISOU 2406 O SER B 539 1927 2220 3873 -19 110 463 O ATOM 2407 CB SER B 539 -18.569 -28.744 48.213 1.00 29.33 C ANISOU 2407 CB SER B 539 3136 3154 4852 57 204 449 C ATOM 2408 OG SER B 539 -19.015 -29.557 47.152 1.00 42.76 O ANISOU 2408 OG SER B 539 4831 4832 6586 -10 156 411 O ATOM 2409 N VAL B 540 -19.164 -26.019 46.759 1.00 21.10 N ANISOU 2409 N VAL B 540 2002 2252 3761 83 125 441 N ATOM 2410 CA VAL B 540 -19.418 -25.387 45.482 1.00 21.53 C ANISOU 2410 CA VAL B 540 2028 2353 3799 66 60 418 C ATOM 2411 C VAL B 540 -18.122 -25.464 44.705 1.00 21.85 C ANISOU 2411 C VAL B 540 2139 2390 3772 84 30 362 C ATOM 2412 O VAL B 540 -17.063 -25.230 45.261 1.00 21.98 O ANISOU 2412 O VAL B 540 2207 2399 3745 136 65 355 O ATOM 2413 CB VAL B 540 -19.878 -23.917 45.639 1.00 21.59 C ANISOU 2413 CB VAL B 540 1980 2419 3806 103 69 456 C ATOM 2414 CG1 VAL B 540 -18.786 -23.062 46.286 1.00 14.43 C ANISOU 2414 CG1 VAL B 540 1114 1524 2844 175 113 455 C ATOM 2415 CG2 VAL B 540 -20.294 -23.337 44.294 1.00 23.02 C ANISOU 2415 CG2 VAL B 540 2123 2649 3976 81 0 442 C ATOM 2416 N SER B 541 -18.208 -25.800 43.424 1.00 14.39 N ANISOU 2416 N SER B 541 1195 1455 2817 40 -33 320 N ATOM 2417 CA SER B 541 -17.024 -25.892 42.583 1.00 20.01 C ANISOU 2417 CA SER B 541 1972 2166 3465 51 -64 263 C ATOM 2418 C SER B 541 -17.184 -25.019 41.363 1.00 20.00 C ANISOU 2418 C SER B 541 1943 2226 3429 44 -124 248 C ATOM 2419 O SER B 541 -18.275 -24.884 40.822 1.00 21.72 O ANISOU 2419 O SER B 541 2098 2477 3680 4 -161 265 O ATOM 2420 CB SER B 541 -16.801 -27.325 42.083 1.00 25.20 C ANISOU 2420 CB SER B 541 2668 2771 4137 -2 -84 214 C ATOM 2421 OG SER B 541 -16.623 -28.213 43.166 1.00 35.73 O ANISOU 2421 OG SER B 541 4030 4042 5503 5 -29 231 O ATOM 2422 N THR B 542 -16.070 -24.477 40.914 1.00 20.11 N ANISOU 2422 N THR B 542 2007 2256 3377 83 -133 216 N ATOM 2423 CA THR B 542 -16.011 -23.806 39.639 1.00 16.27 C ANISOU 2423 CA THR B 542 1511 1822 2848 75 -191 195 C ATOM 2424 C THR B 542 -14.657 -24.160 39.037 1.00 18.60 C ANISOU 2424 C THR B 542 1885 2101 3082 84 -205 130 C ATOM 2425 O THR B 542 -13.908 -24.944 39.623 1.00 21.14 O ANISOU 2425 O THR B 542 2260 2369 3402 95 -171 107 O ATOM 2426 CB THR B 542 -16.183 -22.294 39.806 1.00 20.87 C ANISOU 2426 CB THR B 542 2057 2456 3419 126 -177 239 C ATOM 2427 OG1 THR B 542 -16.431 -21.690 38.528 1.00 26.34 O ANISOU 2427 OG1 THR B 542 2724 3203 4081 110 -238 233 O ATOM 2428 CG2 THR B 542 -14.944 -21.684 40.449 1.00 19.23 C ANISOU 2428 CG2 THR B 542 1903 2237 3164 193 -128 230 C ATOM 2429 N GLY B 543 -14.340 -23.617 37.869 1.00 20.66 N ANISOU 2429 N GLY B 543 2153 2405 3291 80 -253 102 N ATOM 2430 CA GLY B 543 -13.068 -23.909 37.244 1.00 20.62 C ANISOU 2430 CA GLY B 543 2221 2387 3226 87 -266 38 C ATOM 2431 C GLY B 543 -12.957 -23.226 35.893 1.00 26.54 C ANISOU 2431 C GLY B 543 2967 3196 3923 76 -323 17 C ATOM 2432 O GLY B 543 -13.903 -22.610 35.430 1.00 22.18 O ANISOU 2432 O GLY B 543 2353 2693 3381 62 -355 54 O ATOM 2433 N ASN B 544 -11.801 -23.343 35.256 1.00 21.27 N ANISOU 2433 N ASN B 544 2362 2523 3196 84 -335 -41 N ATOM 2434 CA ASN B 544 -11.588 -22.739 33.954 1.00 22.44 C ANISOU 2434 CA ASN B 544 2513 2727 3286 73 -387 -64 C ATOM 2435 C ASN B 544 -10.834 -23.719 33.083 1.00 25.99 C ANISOU 2435 C ASN B 544 3019 3157 3700 32 -417 -144 C ATOM 2436 O ASN B 544 -10.050 -24.517 33.595 1.00 18.59 O ANISOU 2436 O ASN B 544 2134 2161 2769 41 -385 -180 O ATOM 2437 CB ASN B 544 -10.779 -21.444 34.122 1.00 14.38 C ANISOU 2437 CB ASN B 544 1514 1729 2219 142 -357 -48 C ATOM 2438 CG ASN B 544 -11.449 -20.489 35.072 1.00 16.19 C ANISOU 2438 CG ASN B 544 1692 1971 2489 185 -317 24 C ATOM 2439 OD1 ASN B 544 -12.412 -19.825 34.697 1.00 23.38 O ANISOU 2439 OD1 ASN B 544 2542 2927 3416 177 -343 71 O ATOM 2440 ND2 ASN B 544 -10.983 -20.449 36.320 1.00 13.59 N ANISOU 2440 ND2 ASN B 544 1382 1603 2176 228 -254 35 N ATOM 2441 N ALA B 545 -11.082 -23.662 31.776 1.00 23.36 N ANISOU 2441 N ALA B 545 3605 1800 3472 581 -371 349 N ATOM 2442 CA ALA B 545 -10.333 -24.463 30.812 1.00 24.27 C ANISOU 2442 CA ALA B 545 3808 2023 3391 725 -439 175 C ATOM 2443 C ALA B 545 -9.917 -23.573 29.657 1.00 22.81 C ANISOU 2443 C ALA B 545 3586 2071 3011 735 -377 194 C ATOM 2444 O ALA B 545 -10.602 -22.626 29.344 1.00 26.80 O ANISOU 2444 O ALA B 545 4038 2599 3546 633 -359 336 O ATOM 2445 CB ALA B 545 -11.182 -25.609 30.304 1.00 25.90 C ANISOU 2445 CB ALA B 545 4127 2071 3644 740 -631 74 C ATOM 2446 N LEU B 546 -8.783 -23.875 29.042 1.00 23.79 N ANISOU 2446 N LEU B 546 3739 2361 2937 861 -336 54 N ATOM 2447 CA LEU B 546 -8.292 -23.137 27.881 1.00 28.48 C ANISOU 2447 CA LEU B 546 4322 3181 3320 881 -260 58 C ATOM 2448 C LEU B 546 -7.614 -24.147 26.974 1.00 32.66 C ANISOU 2448 C LEU B 546 4949 3802 3659 1022 -333 -156 C ATOM 2449 O LEU B 546 -7.024 -25.114 27.459 1.00 29.38 O ANISOU 2449 O LEU B 546 4564 3327 3273 1119 -362 -302 O ATOM 2450 CB LEU B 546 -7.240 -22.116 28.298 1.00 29.85 C ANISOU 2450 CB LEU B 546 4376 3503 3461 875 -31 108 C ATOM 2451 CG LEU B 546 -7.483 -20.623 28.145 1.00 46.54 C ANISOU 2451 CG LEU B 546 6396 5696 5592 759 113 301 C ATOM 2452 CD1 LEU B 546 -8.965 -20.287 28.195 1.00 51.86 C ANISOU 2452 CD1 LEU B 546 7074 6218 6412 639 -1 466 C ATOM 2453 CD2 LEU B 546 -6.710 -19.894 29.236 1.00 33.51 C ANISOU 2453 CD2 LEU B 546 4603 4081 4049 726 309 333 C ATOM 2454 N GLY B 547 -7.716 -23.931 25.669 1.00 32.17 N ANISOU 2454 N GLY B 547 4940 3883 3400 1038 -365 -175 N ATOM 2455 CA GLY B 547 -6.968 -24.698 24.695 1.00 37.35 C ANISOU 2455 CA GLY B 547 5676 4671 3843 1164 -399 -382 C ATOM 2456 C GLY B 547 -5.796 -23.875 24.200 1.00 39.26 C ANISOU 2456 C GLY B 547 5870 5150 3897 1198 -188 -387 C ATOM 2457 O GLY B 547 -5.819 -22.639 24.246 1.00 38.82 O ANISOU 2457 O GLY B 547 5743 5165 3841 1113 -44 -210 O ATOM 2458 N PHE B 548 -4.761 -24.555 23.728 1.00 34.51 N ANISOU 2458 N PHE B 548 5301 4663 3149 1319 -158 -598 N ATOM 2459 CA PHE B 548 -3.611 -23.877 23.155 1.00 40.29 C ANISOU 2459 CA PHE B 548 5991 5623 3696 1352 52 -638 C ATOM 2460 C PHE B 548 -3.257 -24.532 21.828 1.00 53.99 C ANISOU 2460 C PHE B 548 7832 7502 5179 1446 0 -823 C ATOM 2461 O PHE B 548 -3.601 -25.696 21.596 1.00 58.06 O ANISOU 2461 O PHE B 548 8429 7934 5699 1512 -187 -976 O ATOM 2462 CB PHE B 548 -2.425 -23.940 24.113 1.00 41.87 C ANISOU 2462 CB PHE B 548 6079 5838 3990 1410 191 -740 C ATOM 2463 CG PHE B 548 -2.679 -23.263 25.424 1.00 40.29 C ANISOU 2463 CG PHE B 548 5768 5524 4015 1322 254 -577 C ATOM 2464 CD1 PHE B 548 -2.429 -21.907 25.575 1.00 37.19 C ANISOU 2464 CD1 PHE B 548 5267 5225 3638 1229 460 -430 C ATOM 2465 CD2 PHE B 548 -3.190 -23.974 26.497 1.00 33.33 C ANISOU 2465 CD2 PHE B 548 4896 4438 3332 1329 119 -571 C ATOM 2466 CE1 PHE B 548 -2.673 -21.275 26.772 1.00 34.07 C ANISOU 2466 CE1 PHE B 548 4762 4732 3451 1145 520 -298 C ATOM 2467 CE2 PHE B 548 -3.439 -23.351 27.714 1.00 28.51 C ANISOU 2467 CE2 PHE B 548 4187 3732 2913 1247 181 -427 C ATOM 2468 CZ PHE B 548 -3.176 -22.001 27.856 1.00 36.91 C ANISOU 2468 CZ PHE B 548 5131 4902 3990 1155 377 -300 C ATOM 2469 N THR B 549 -2.580 -23.785 20.959 1.00 60.09 N ANISOU 2469 N THR B 549 8605 8488 5737 1448 178 -813 N ATOM 2470 CA THR B 549 -2.152 -24.313 19.667 1.00 75.25 C ANISOU 2470 CA THR B 549 10626 10576 7389 1534 162 -992 C ATOM 2471 C THR B 549 -0.639 -24.497 19.607 1.00 87.96 C ANISOU 2471 C THR B 549 12173 12325 8921 1619 349 -1196 C ATOM 2472 O THR B 549 0.102 -23.537 19.394 1.00 91.37 O ANISOU 2472 O THR B 549 12547 12903 9266 1585 589 -1140 O ATOM 2473 CB THR B 549 -2.589 -23.404 18.502 1.00 74.75 C ANISOU 2473 CB THR B 549 10645 10668 7088 1482 215 -834 C ATOM 2474 OG1 THR B 549 -4.021 -23.378 18.416 1.00 68.90 O ANISOU 2474 OG1 THR B 549 9963 9810 6405 1426 4 -687 O ATOM 2475 CG2 THR B 549 -2.017 -23.921 17.191 1.00 81.57 C ANISOU 2475 CG2 THR B 549 11613 11731 7650 1574 229 -1032 C ATOM 2476 N ASN B 550 -0.196 -25.737 19.798 1.00 95.47 N ANISOU 2476 N ASN B 550 13134 13220 9920 1730 242 -1439 N ATOM 2477 CA ASN B 550 1.219 -26.095 19.734 1.00101.86 C ANISOU 2477 CA ASN B 550 13879 14149 10675 1832 383 -1675 C ATOM 2478 C ASN B 550 1.857 -25.624 18.428 1.00109.20 C ANISOU 2478 C ASN B 550 14851 15327 11313 1836 559 -1742 C ATOM 2479 O ASN B 550 1.845 -26.340 17.424 1.00109.97 O ANISOU 2479 O ASN B 550 15052 15507 11224 1900 475 -1905 O ATOM 2480 CB ASN B 550 1.361 -27.611 19.882 1.00104.75 C ANISOU 2480 CB ASN B 550 14284 14403 11112 1959 197 -1922 C ATOM 2481 CG ASN B 550 2.769 -28.046 20.248 1.00109.21 C ANISOU 2481 CG ASN B 550 14749 15028 11718 2077 310 -2153 C ATOM 2482 OD1 ASN B 550 2.956 -29.029 20.970 1.00111.20 O ANISOU 2482 OD1 ASN B 550 14985 15134 12132 2175 187 -2281 O ATOM 2483 ND2 ASN B 550 3.764 -27.323 19.749 1.00109.49 N ANISOU 2483 ND2 ASN B 550 14715 15273 11612 2071 547 -2211 N ATOM 2484 N ASN B 551 2.418 -24.418 18.453 1.00160.19 N ANISOU 2484 N ASN B 551 20542 21440 18883 -4476 1502 2373 N ATOM 2485 CA ASN B 551 2.953 -23.777 17.253 1.00160.84 C ANISOU 2485 CA ASN B 551 20634 21217 19261 -4459 1372 2143 C ATOM 2486 C ASN B 551 4.256 -24.388 16.744 1.00160.58 C ANISOU 2486 C ASN B 551 20627 21059 19325 -4503 1107 2201 C ATOM 2487 O ASN B 551 4.656 -24.151 15.604 1.00159.17 O ANISOU 2487 O ASN B 551 20398 20693 19386 -4495 1014 2110 O ATOM 2488 CB ASN B 551 3.143 -22.276 17.493 1.00162.41 C ANISOU 2488 CB ASN B 551 20918 21434 19357 -4385 1384 1764 C ATOM 2489 CG ASN B 551 1.837 -21.559 17.777 1.00163.38 C ANISOU 2489 CG ASN B 551 20987 21652 19438 -4273 1608 1608 C ATOM 2490 OD1 ASN B 551 1.779 -20.660 18.616 1.00163.72 O ANISOU 2490 OD1 ASN B 551 21108 21865 19234 -4148 1630 1327 O ATOM 2491 ND2 ASN B 551 0.780 -21.958 17.080 1.00163.41 N ANISOU 2491 ND2 ASN B 551 20848 21548 19692 -4285 1744 1760 N ATOM 2492 N GLN B 552 4.919 -25.168 17.591 1.00161.91 N ANISOU 2492 N GLN B 552 20860 21370 19288 -4535 981 2353 N ATOM 2493 CA GLN B 552 6.177 -25.803 17.212 1.00160.26 C ANISOU 2493 CA GLN B 552 20653 21078 19161 -4539 706 2377 C ATOM 2494 C GLN B 552 5.961 -26.985 16.269 1.00160.15 C ANISOU 2494 C GLN B 552 20539 20865 19447 -4508 562 2566 C ATOM 2495 O GLN B 552 6.491 -27.003 15.158 1.00159.53 O ANISOU 2495 O GLN B 552 20381 20668 19565 -4433 447 2447 O ATOM 2496 CB GLN B 552 6.958 -26.247 18.453 1.00160.35 C ANISOU 2496 CB GLN B 552 20781 21272 18872 -4568 563 2459 C ATOM 2497 CG GLN B 552 8.025 -25.261 18.911 1.00158.51 C ANISOU 2497 CG GLN B 552 20632 21128 18466 -4557 476 2189 C ATOM 2498 CD GLN B 552 7.463 -23.890 19.234 1.00158.54 C ANISOU 2498 CD GLN B 552 20693 21193 18354 -4525 656 1941 C ATOM 2499 OE1 GLN B 552 7.234 -23.072 18.341 1.00156.20 O ANISOU 2499 OE1 GLN B 552 20327 20738 18283 -4525 709 1788 O ATOM 2500 NE2 GLN B 552 7.242 -23.629 20.518 1.00162.08 N ANISOU 2500 NE2 GLN B 552 21270 21878 18436 -4476 716 1889 N ATOM 2501 N SER B 553 5.182 -27.967 16.717 1.00160.52 N ANISOU 2501 N SER B 553 20577 20894 19521 -4558 541 2867 N ATOM 2502 CA SER B 553 4.924 -29.167 15.925 1.00159.01 C ANISOU 2502 CA SER B 553 20308 20450 19658 -4520 304 3051 C ATOM 2503 C SER B 553 4.385 -28.819 14.540 1.00157.31 C ANISOU 2503 C SER B 553 19999 20039 19734 -4423 366 2898 C ATOM 2504 O SER B 553 3.252 -28.357 14.401 1.00157.86 O ANISOU 2504 O SER B 553 20021 20076 19884 -4463 592 2931 O ATOM 2505 CB SER B 553 3.949 -30.094 16.654 1.00159.78 C ANISOU 2505 CB SER B 553 20383 20542 19784 -4653 280 3467 C ATOM 2506 OG SER B 553 3.771 -31.308 15.944 1.00158.78 O ANISOU 2506 OG SER B 553 20200 20100 20031 -4617 -65 3646 O ATOM 2507 N GLY B 554 5.204 -29.050 13.518 1.00154.36 N ANISOU 2507 N GLY B 554 19583 19571 19496 -4277 159 2724 N ATOM 2508 CA GLY B 554 4.843 -28.710 12.154 1.00150.75 C ANISOU 2508 CA GLY B 554 19046 18982 19248 -4162 196 2572 C ATOM 2509 C GLY B 554 5.403 -27.358 11.758 1.00148.53 C ANISOU 2509 C GLY B 554 18749 18854 18831 -4181 385 2339 C ATOM 2510 O GLY B 554 6.278 -27.266 10.896 1.00148.11 O ANISOU 2510 O GLY B 554 18616 18881 18779 -4076 287 2200 O ATOM 2511 N GLY B 555 4.893 -26.307 12.394 1.00148.08 N ANISOU 2511 N GLY B 555 18748 18856 18659 -4308 631 2306 N ATOM 2512 CA GLY B 555 5.388 -24.959 12.182 1.00148.13 C ANISOU 2512 CA GLY B 555 18758 18944 18581 -4365 732 2117 C ATOM 2513 C GLY B 555 5.359 -24.500 10.737 1.00148.85 C ANISOU 2513 C GLY B 555 18761 18952 18842 -4316 729 2039 C ATOM 2514 O GLY B 555 6.301 -23.860 10.264 1.00149.17 O ANISOU 2514 O GLY B 555 18738 19113 18827 -4354 687 1968 O ATOM 2515 N ALA B 556 4.274 -24.828 10.038 1.00148.91 N ANISOU 2515 N ALA B 556 18751 18774 19054 -4245 761 2085 N ATOM 2516 CA ALA B 556 4.073 -24.406 8.652 1.00147.54 C ANISOU 2516 CA ALA B 556 18518 18519 19021 -4185 754 2024 C ATOM 2517 C ALA B 556 5.322 -24.577 7.788 1.00149.03 C ANISOU 2517 C ALA B 556 18597 18918 19111 -4097 625 1982 C ATOM 2518 O ALA B 556 6.112 -23.644 7.639 1.00147.79 O ANISOU 2518 O ALA B 556 18385 18923 18845 -4213 661 1959 O ATOM 2519 CB ALA B 556 3.582 -22.962 8.601 1.00145.38 C ANISOU 2519 CB ALA B 556 18288 18165 18784 -4315 894 1944 C ATOM 2520 N ALA B 557 5.482 -25.773 7.225 1.00151.43 N ANISOU 2520 N ALA B 557 18845 19229 19463 -3882 446 1974 N ATOM 2521 CA ALA B 557 6.592 -26.103 6.327 1.00153.57 C ANISOU 2521 CA ALA B 557 18967 19774 19609 -3706 319 1889 C ATOM 2522 C ALA B 557 7.753 -25.106 6.354 1.00157.54 C ANISOU 2522 C ALA B 557 19352 20590 19915 -3862 415 1897 C ATOM 2523 O ALA B 557 7.875 -24.262 5.465 1.00158.00 O ANISOU 2523 O ALA B 557 19321 20779 19933 -3926 501 1932 O ATOM 2524 CB ALA B 557 6.082 -26.285 4.900 1.00151.20 C ANISOU 2524 CB ALA B 557 18620 19440 19388 -3503 263 1828 C ATOM 2525 N GLN B 558 8.597 -25.217 7.377 1.00160.16 N ANISOU 2525 N GLN B 558 19679 21033 20142 -3941 369 1899 N ATOM 2526 CA GLN B 558 9.795 -24.385 7.520 1.00162.55 C ANISOU 2526 CA GLN B 558 19845 21615 20304 -4099 396 1923 C ATOM 2527 C GLN B 558 9.562 -22.892 7.267 1.00154.41 C ANISOU 2527 C GLN B 558 18821 20530 19317 -4357 521 2008 C ATOM 2528 O GLN B 558 8.437 -22.402 7.360 1.00155.47 O ANISOU 2528 O GLN B 558 19115 20378 19579 -4428 601 2006 O ATOM 2529 CB GLN B 558 10.931 -24.906 6.628 1.00171.70 C ANISOU 2529 CB GLN B 558 20737 23175 21327 -3902 305 1876 C ATOM 2530 CG GLN B 558 10.689 -24.746 5.133 1.00178.24 C ANISOU 2530 CG GLN B 558 21431 24177 22116 -3773 369 1888 C ATOM 2531 CD GLN B 558 11.832 -25.282 4.294 1.00184.91 C ANISOU 2531 CD GLN B 558 21970 25534 22752 -3522 302 1812 C ATOM 2532 OE1 GLN B 558 12.830 -25.770 4.824 1.00188.18 O ANISOU 2532 OE1 GLN B 558 22258 26150 23090 -3446 193 1738 O ATOM 2533 NE2 GLN B 558 11.690 -25.196 2.975 1.00186.15 N ANISOU 2533 NE2 GLN B 558 21994 25940 22794 -3366 359 1815 N ATOM 2534 N GLU B 559 10.640 -22.177 6.954 1.00144.99 N ANISOU 2534 N GLU B 559 17434 19612 18044 -4503 502 2096 N ATOM 2535 CA GLU B 559 10.583 -20.734 6.745 1.00136.50 C ANISOU 2535 CA GLU B 559 16350 18456 17056 -4790 522 2224 C ATOM 2536 C GLU B 559 10.918 -20.348 5.309 1.00128.75 C ANISOU 2536 C GLU B 559 15137 17763 16020 -4829 562 2401 C ATOM 2537 O GLU B 559 11.834 -20.904 4.703 1.00130.75 O ANISOU 2537 O GLU B 559 15131 18451 16096 -4699 570 2440 O ATOM 2538 CB GLU B 559 11.550 -20.023 7.697 1.00138.90 C ANISOU 2538 CB GLU B 559 16618 18796 17360 -5017 404 2257 C ATOM 2539 CG GLU B 559 11.061 -19.909 9.131 1.00140.87 C ANISOU 2539 CG GLU B 559 17137 18745 17641 -5033 359 2096 C ATOM 2540 CD GLU B 559 10.042 -18.802 9.312 1.00142.20 C ANISOU 2540 CD GLU B 559 17494 18569 17965 -5156 355 2044 C ATOM 2541 OE1 GLU B 559 9.705 -18.134 8.312 1.00143.33 O ANISOU 2541 OE1 GLU B 559 17578 18649 18231 -5256 359 2157 O ATOM 2542 OE2 GLU B 559 9.582 -18.596 10.456 1.00141.23 O ANISOU 2542 OE2 GLU B 559 17572 18262 17825 -5132 330 1881 O ATOM 2543 N VAL B 560 10.172 -19.391 4.768 1.00118.34 N ANISOU 2543 N VAL B 560 13900 16233 14832 -4992 576 2506 N ATOM 2544 CA VAL B 560 10.483 -18.832 3.457 1.00110.55 C ANISOU 2544 CA VAL B 560 12703 15525 13775 -5100 596 2751 C ATOM 2545 C VAL B 560 10.594 -17.317 3.536 1.00103.32 C ANISOU 2545 C VAL B 560 11791 14421 13044 -5503 462 2975 C ATOM 2546 O VAL B 560 10.068 -16.688 4.451 1.00 91.39 O ANISOU 2546 O VAL B 560 10508 12476 11740 -5618 352 2855 O ATOM 2547 CB VAL B 560 9.433 -19.207 2.400 1.00108.44 C ANISOU 2547 CB VAL B 560 12524 15181 13497 -4890 668 2708 C ATOM 2548 CG1 VAL B 560 9.497 -20.694 2.096 1.00108.49 C ANISOU 2548 CG1 VAL B 560 12477 15408 13337 -4479 706 2509 C ATOM 2549 CG2 VAL B 560 8.044 -18.800 2.865 1.00107.13 C ANISOU 2549 CG2 VAL B 560 12666 14446 13593 -4928 645 2582 C ATOM 2550 N TYR B 561 11.281 -16.736 2.562 1.00 51.98 N ANISOU 2550 N TYR B 561 6350 7801 5598 -1359 -307 1247 N ATOM 2551 CA TYR B 561 11.548 -15.305 2.564 1.00 56.52 C ANISOU 2551 CA TYR B 561 6963 8428 6084 -1310 -310 1185 C ATOM 2552 C TYR B 561 11.324 -14.722 1.177 1.00 56.21 C ANISOU 2552 C TYR B 561 7006 8335 6015 -1385 -355 1118 C ATOM 2553 O TYR B 561 11.108 -15.451 0.211 1.00 57.62 O ANISOU 2553 O TYR B 561 7220 8443 6230 -1480 -385 1105 O ATOM 2554 CB TYR B 561 12.985 -15.038 3.008 1.00 58.80 C ANISOU 2554 CB TYR B 561 7281 8725 6334 -1264 -261 1111 C ATOM 2555 CG TYR B 561 13.416 -15.835 4.216 1.00 72.87 C ANISOU 2555 CG TYR B 561 8983 10559 8146 -1203 -215 1178 C ATOM 2556 CD1 TYR B 561 14.043 -17.066 4.070 1.00 75.99 C ANISOU 2556 CD1 TYR B 561 9376 10885 8613 -1230 -184 1195 C ATOM 2557 CD2 TYR B 561 13.203 -15.356 5.501 1.00 78.83 C ANISOU 2557 CD2 TYR B 561 9663 11434 8855 -1114 -196 1230 C ATOM 2558 CE1 TYR B 561 14.442 -17.797 5.167 1.00 82.40 C ANISOU 2558 CE1 TYR B 561 10104 11751 9455 -1166 -136 1275 C ATOM 2559 CE2 TYR B 561 13.597 -16.083 6.609 1.00 84.28 C ANISOU 2559 CE2 TYR B 561 10270 12191 9562 -1056 -156 1303 C ATOM 2560 CZ TYR B 561 14.217 -17.304 6.436 1.00 86.88 C ANISOU 2560 CZ TYR B 561 10588 12454 9967 -1080 -126 1332 C ATOM 2561 OH TYR B 561 14.614 -18.035 7.533 1.00 88.75 O ANISOU 2561 OH TYR B 561 10733 12764 10225 -1014 -80 1423 O ATOM 2562 N LYS B 562 11.381 -13.401 1.075 1.00 52.42 N ANISOU 2562 N LYS B 562 6560 7891 5467 -1345 -355 1077 N ATOM 2563 CA LYS B 562 11.138 -12.753 -0.201 1.00 54.45 C ANISOU 2563 CA LYS B 562 6884 8113 5692 -1403 -393 1033 C ATOM 2564 C LYS B 562 12.334 -11.920 -0.632 1.00 50.12 C ANISOU 2564 C LYS B 562 6423 7527 5093 -1395 -365 921 C ATOM 2565 O LYS B 562 13.068 -11.375 0.190 1.00 51.12 O ANISOU 2565 O LYS B 562 6550 7683 5192 -1331 -322 886 O ATOM 2566 CB LYS B 562 9.852 -11.919 -0.158 1.00 54.78 C ANISOU 2566 CB LYS B 562 6879 8222 5711 -1368 -418 1115 C ATOM 2567 CG LYS B 562 9.533 -11.330 1.201 1.00 61.00 C ANISOU 2567 CG LYS B 562 7605 9089 6483 -1255 -375 1169 C ATOM 2568 CD LYS B 562 8.200 -10.596 1.206 1.00 65.92 C ANISOU 2568 CD LYS B 562 8178 9774 7094 -1212 -388 1266 C ATOM 2569 CE LYS B 562 7.892 -10.042 2.595 1.00 72.55 C ANISOU 2569 CE LYS B 562 8964 10688 7913 -1093 -332 1314 C ATOM 2570 NZ LYS B 562 6.778 -9.042 2.588 1.00 75.64 N ANISOU 2570 NZ LYS B 562 9327 11127 8284 -1027 -320 1395 N ATOM 2571 N ILE B 563 12.543 -11.851 -1.934 1.00 47.19 N ANISOU 2571 N ILE B 563 6125 7098 4707 -1468 -391 865 N ATOM 2572 CA ILE B 563 13.597 -11.023 -2.468 1.00 49.17 C ANISOU 2572 CA ILE B 563 6456 7314 4914 -1466 -366 771 C ATOM 2573 C ILE B 563 12.993 -9.957 -3.333 1.00 44.06 C ANISOU 2573 C ILE B 563 5840 6676 4225 -1475 -392 778 C ATOM 2574 O ILE B 563 11.801 -9.993 -3.639 1.00 41.23 O ANISOU 2574 O ILE B 563 5441 6354 3870 -1494 -434 855 O ATOM 2575 CB ILE B 563 14.546 -11.822 -3.362 1.00 52.25 C ANISOU 2575 CB ILE B 563 6913 7626 5315 -1536 -361 698 C ATOM 2576 CG1 ILE B 563 13.768 -12.479 -4.496 1.00 51.33 C ANISOU 2576 CG1 ILE B 563 6820 7478 5206 -1630 -413 710 C ATOM 2577 CG2 ILE B 563 15.292 -12.859 -2.556 1.00 58.96 C ANISOU 2577 CG2 ILE B 563 7732 8459 6211 -1516 -320 699 C ATOM 2578 CD1 ILE B 563 14.650 -13.244 -5.464 1.00 55.36 C ANISOU 2578 CD1 ILE B 563 7411 7903 5719 -1701 -398 628 C ATOM 2579 N GLY B 564 13.830 -8.999 -3.708 1.00 41.27 N ANISOU 2579 N GLY B 564 5551 6296 3835 -1461 -363 706 N ATOM 2580 CA GLY B 564 13.574 -8.202 -4.878 1.00 51.15 C ANISOU 2580 CA GLY B 564 6850 7534 5051 -1489 -382 701 C ATOM 2581 C GLY B 564 13.712 -6.713 -4.717 1.00 52.78 C ANISOU 2581 C GLY B 564 7082 7742 5231 -1425 -341 690 C ATOM 2582 O GLY B 564 14.752 -6.209 -4.332 1.00 35.39 O ANISOU 2582 O GLY B 564 4916 5511 3019 -1402 -296 617 O ATOM 2583 N ASN B 565 12.674 -6.032 -5.179 1.00 61.27 N ANISOU 2583 N ASN B 565 8139 8846 6294 -1406 -357 764 N ATOM 2584 CA ASN B 565 12.193 -4.790 -4.608 1.00 49.14 C ANISOU 2584 CA ASN B 565 6592 7325 4754 -1318 -310 804 C ATOM 2585 C ASN B 565 12.227 -3.454 -5.383 1.00 38.41 C ANISOU 2585 C ASN B 565 5284 5934 3375 -1293 -276 808 C ATOM 2586 O ASN B 565 11.291 -2.678 -5.221 1.00 37.70 O ANISOU 2586 O ASN B 565 5164 5869 3290 -1227 -251 892 O ATOM 2587 CB ASN B 565 12.518 -4.724 -3.104 1.00 48.58 C ANISOU 2587 CB ASN B 565 6499 7266 4694 -1255 -263 774 C ATOM 2588 CG ASN B 565 12.915 -3.365 -2.646 1.00 40.59 C ANISOU 2588 CG ASN B 565 5534 6222 3666 -1195 -192 727 C ATOM 2589 OD1 ASN B 565 13.866 -2.785 -3.167 1.00 29.25 O ANISOU 2589 OD1 ASN B 565 4166 4729 2218 -1222 -169 649 O ATOM 2590 ND2 ASN B 565 12.210 -2.846 -1.638 1.00 38.38 N ANISOU 2590 ND2 ASN B 565 5222 5974 3388 -1113 -150 769 N ATOM 2591 N TYR B 566 13.208 -3.190 -6.259 1.00 34.30 N ANISOU 2591 N TYR B 566 4834 5362 2837 -1339 -269 735 N ATOM 2592 CA TYR B 566 13.264 -1.851 -6.871 1.00 31.95 C ANISOU 2592 CA TYR B 566 4581 5027 2531 -1305 -224 747 C ATOM 2593 C TYR B 566 13.906 -1.700 -8.261 1.00 36.06 C ANISOU 2593 C TYR B 566 5158 5520 3025 -1365 -238 718 C ATOM 2594 O TYR B 566 15.091 -1.989 -8.438 1.00 33.53 O ANISOU 2594 O TYR B 566 4886 5157 2697 -1409 -231 624 O ATOM 2595 CB TYR B 566 13.982 -0.905 -5.912 1.00 35.11 C ANISOU 2595 CB TYR B 566 5023 5372 2946 -1252 -144 675 C ATOM 2596 CG TYR B 566 13.609 0.548 -6.051 1.00 39.19 C ANISOU 2596 CG TYR B 566 5570 5847 3476 -1185 -75 715 C ATOM 2597 CD1 TYR B 566 12.340 0.925 -6.472 1.00 38.71 C ANISOU 2597 CD1 TYR B 566 5465 5823 3420 -1134 -75 844 C ATOM 2598 CD2 TYR B 566 14.518 1.551 -5.718 1.00 40.86 C ANISOU 2598 CD2 TYR B 566 5849 5979 3698 -1173 -2 628 C ATOM 2599 CE1 TYR B 566 11.991 2.265 -6.582 1.00 33.70 C ANISOU 2599 CE1 TYR B 566 4858 5141 2807 -1059 5 893 C ATOM 2600 CE2 TYR B 566 14.179 2.892 -5.818 1.00 35.49 C ANISOU 2600 CE2 TYR B 566 5205 5239 3040 -1110 77 662 C ATOM 2601 CZ TYR B 566 12.911 3.242 -6.245 1.00 37.37 C ANISOU 2601 CZ TYR B 566 5401 5507 3289 -1046 86 799 C ATOM 2602 OH TYR B 566 12.568 4.571 -6.341 1.00 36.62 O ANISOU 2602 OH TYR B 566 5342 5345 3228 -970 179 845 O ATOM 2603 N VAL B 567 13.125 -1.205 -9.224 1.00 32.51 N ANISOU 2603 N VAL B 567 4696 5102 2556 -1358 -253 809 N ATOM 2604 CA VAL B 567 13.655 -0.742 -10.505 1.00 34.44 C ANISOU 2604 CA VAL B 567 4991 5326 2769 -1393 -249 799 C ATOM 2605 C VAL B 567 13.414 0.770 -10.599 1.00 39.29 C ANISOU 2605 C VAL B 567 5620 5905 3405 -1312 -175 861 C ATOM 2606 O VAL B 567 12.267 1.225 -10.571 1.00 37.09 O ANISOU 2606 O VAL B 567 5288 5671 3134 -1254 -168 978 O ATOM 2607 CB VAL B 567 12.969 -1.445 -11.697 1.00 34.29 C ANISOU 2607 CB VAL B 567 4942 5388 2697 -1460 -330 862 C ATOM 2608 CG1 VAL B 567 13.401 -0.806 -13.018 1.00 30.28 C ANISOU 2608 CG1 VAL B 567 4481 4877 2147 -1481 -319 872 C ATOM 2609 CG2 VAL B 567 13.267 -2.935 -11.699 1.00 31.57 C ANISOU 2609 CG2 VAL B 567 4603 5054 2339 -1547 -389 790 C ATOM 2610 N TRP B 568 14.485 1.550 -10.699 1.00 34.39 N ANISOU 2610 N TRP B 568 5066 5201 2798 -1308 -113 789 N ATOM 2611 CA TRP B 568 14.357 3.004 -10.648 1.00 32.20 C ANISOU 2611 CA TRP B 568 4814 4862 2557 -1233 -25 833 C ATOM 2612 C TRP B 568 14.963 3.722 -11.861 1.00 37.51 C ANISOU 2612 C TRP B 568 5533 5499 3220 -1250 4 846 C ATOM 2613 O TRP B 568 15.847 3.190 -12.549 1.00 42.00 O ANISOU 2613 O TRP B 568 6132 6070 3755 -1322 -30 782 O ATOM 2614 CB TRP B 568 14.941 3.565 -9.326 1.00 34.62 C ANISOU 2614 CB TRP B 568 5159 5087 2907 -1199 48 739 C ATOM 2615 CG TRP B 568 16.440 3.905 -9.324 1.00 36.84 C ANISOU 2615 CG TRP B 568 5510 5289 3197 -1250 84 616 C ATOM 2616 CD1 TRP B 568 17.007 5.157 -9.422 1.00 37.28 C ANISOU 2616 CD1 TRP B 568 5625 5250 3289 -1234 168 590 C ATOM 2617 CD2 TRP B 568 17.540 2.984 -9.189 1.00 35.93 C ANISOU 2617 CD2 TRP B 568 5405 5186 3060 -1325 41 514 C ATOM 2618 NE1 TRP B 568 18.386 5.065 -9.364 1.00 34.39 N ANISOU 2618 NE1 TRP B 568 5301 4847 2920 -1303 172 478 N ATOM 2619 CE2 TRP B 568 18.737 3.745 -9.231 1.00 32.80 C ANISOU 2619 CE2 TRP B 568 5066 4714 2682 -1354 96 435 C ATOM 2620 CE3 TRP B 568 17.629 1.593 -9.048 1.00 33.99 C ANISOU 2620 CE3 TRP B 568 5123 5004 2786 -1370 -32 489 C ATOM 2621 CZ2 TRP B 568 19.996 3.159 -9.132 1.00 32.23 C ANISOU 2621 CZ2 TRP B 568 5007 4644 2596 -1420 76 342 C ATOM 2622 CZ3 TRP B 568 18.883 1.010 -8.952 1.00 28.20 C ANISOU 2622 CZ3 TRP B 568 4410 4260 2044 -1427 -41 396 C ATOM 2623 CH2 TRP B 568 20.051 1.795 -8.992 1.00 34.45 C ANISOU 2623 CH2 TRP B 568 5250 4992 2849 -1449 11 328 C ATOM 2624 N GLU B 569 14.465 4.927 -12.132 1.00 36.35 N ANISOU 2624 N GLU B 569 5389 5318 3105 -1177 75 939 N ATOM 2625 CA GLU B 569 15.066 5.778 -13.150 1.00 29.62 C ANISOU 2625 CA GLU B 569 4580 4418 2257 -1180 122 961 C ATOM 2626 C GLU B 569 16.265 6.513 -12.545 1.00 36.24 C ANISOU 2626 C GLU B 569 5494 5128 3147 -1189 202 843 C ATOM 2627 O GLU B 569 16.116 7.443 -11.735 1.00 36.98 O ANISOU 2627 O GLU B 569 5615 5137 3299 -1131 288 835 O ATOM 2628 CB GLU B 569 14.053 6.759 -13.746 1.00 40.85 C ANISOU 2628 CB GLU B 569 5968 5856 3696 -1094 172 1126 C ATOM 2629 CG GLU B 569 14.669 7.692 -14.799 1.00 45.61 C ANISOU 2629 CG GLU B 569 6611 6407 4310 -1089 231 1165 C ATOM 2630 CD GLU B 569 13.646 8.254 -15.783 1.00 58.17 C ANISOU 2630 CD GLU B 569 8143 8074 5884 -1025 244 1356 C ATOM 2631 OE1 GLU B 569 12.502 7.752 -15.815 1.00 62.31 O ANISOU 2631 OE1 GLU B 569 8588 8714 6372 -1005 184 1455 O ATOM 2632 OE2 GLU B 569 13.992 9.194 -16.535 1.00 62.96 O ANISOU 2632 OE2 GLU B 569 8775 8632 6515 -995 314 1417 O ATOM 2633 N ASP B 570 17.452 6.060 -12.933 1.00 37.12 N ANISOU 2633 N ASP B 570 5640 5229 3235 -1267 175 749 N ATOM 2634 CA ASP B 570 18.708 6.573 -12.407 1.00 38.20 C ANISOU 2634 CA ASP B 570 5835 5269 3410 -1301 231 633 C ATOM 2635 C ASP B 570 19.117 7.796 -13.197 1.00 42.99 C ANISOU 2635 C ASP B 570 6485 5795 4055 -1285 311 677 C ATOM 2636 O ASP B 570 20.014 7.725 -14.047 1.00 48.97 O ANISOU 2636 O ASP B 570 7262 6551 4793 -1335 303 657 O ATOM 2637 CB ASP B 570 19.789 5.500 -12.525 1.00 40.80 C ANISOU 2637 CB ASP B 570 6170 5635 3699 -1385 170 536 C ATOM 2638 CG ASP B 570 21.077 5.892 -11.833 1.00 41.66 C ANISOU 2638 CG ASP B 570 6318 5670 3840 -1428 215 421 C ATOM 2639 OD1 ASP B 570 21.049 6.818 -11.000 1.00 36.10 O ANISOU 2639 OD1 ASP B 570 5640 4893 3183 -1403 281 390 O ATOM 2640 OD2 ASP B 570 22.113 5.257 -12.112 1.00 37.90 O ANISOU 2640 OD2 ASP B 570 5847 5215 3340 -1488 186 361 O ATOM 2641 N THR B 571 18.447 8.912 -12.930 1.00 43.68 N ANISOU 2641 N THR B 571 6585 5813 4200 -1209 397 743 N ATOM 2642 CA THR B 571 18.639 10.127 -13.723 1.00 58.04 C ANISOU 2642 CA THR B 571 8438 7549 6067 -1178 485 814 C ATOM 2643 C THR B 571 20.096 10.585 -13.686 1.00 60.77 C ANISOU 2643 C THR B 571 8845 7800 6447 -1250 529 704 C ATOM 2644 O THR B 571 20.667 10.985 -14.703 1.00 60.81 O ANISOU 2644 O THR B 571 8863 7785 6457 -1269 552 745 O ATOM 2645 CB THR B 571 17.726 11.254 -13.226 1.00 66.43 C ANISOU 2645 CB THR B 571 9514 8527 7201 -1078 591 892 C ATOM 2646 OG1 THR B 571 16.390 10.751 -13.088 1.00 74.64 O ANISOU 2646 OG1 THR B 571 10485 9667 8209 -1013 547 993 O ATOM 2647 CG2 THR B 571 17.731 12.420 -14.207 1.00 67.37 C ANISOU 2647 CG2 THR B 571 9653 8574 7372 -1031 684 1006 C ATOM 2648 N ASN B 572 20.672 10.514 -12.490 1.00 65.17 N ANISOU 2648 N ASN B 572 9431 8311 7021 -1293 537 569 N ATOM 2649 CA ASN B 572 22.085 10.767 -12.231 1.00 62.14 C ANISOU 2649 CA ASN B 572 9088 7863 6657 -1380 559 450 C ATOM 2650 C ASN B 572 23.025 10.037 -13.172 1.00 51.62 C ANISOU 2650 C ASN B 572 7737 6598 5278 -1444 497 442 C ATOM 2651 O ASN B 572 24.097 10.533 -13.497 1.00 51.21 O ANISOU 2651 O ASN B 572 7713 6489 5254 -1498 535 406 O ATOM 2652 CB ASN B 572 22.417 10.280 -10.814 1.00 52.59 C ANISOU 2652 CB ASN B 572 7880 6671 5432 -1423 530 318 C ATOM 2653 CG ASN B 572 22.276 11.355 -9.789 1.00 66.53 C ANISOU 2653 CG ASN B 572 9701 8324 7254 -1407 624 258 C ATOM 2654 OD1 ASN B 572 23.143 11.517 -8.935 1.00 72.66 O ANISOU 2654 OD1 ASN B 572 10505 9070 8032 -1481 635 132 O ATOM 2655 ND2 ASN B 572 21.184 12.111 -9.859 1.00 76.05 N ANISOU 2655 ND2 ASN B 572 10925 9470 8502 -1313 696 347 N ATOM 2656 N LYS B 573 22.625 8.830 -13.558 1.00 47.87 N ANISOU 2656 N LYS B 573 7216 6241 4733 -1441 406 472 N ATOM 2657 CA LYS B 573 23.520 7.863 -14.182 1.00 45.16 C ANISOU 2657 CA LYS B 573 6858 5965 4335 -1502 346 436 C ATOM 2658 C LYS B 573 24.734 7.485 -13.305 1.00 43.19 C ANISOU 2658 C LYS B 573 6613 5708 4091 -1573 336 311 C ATOM 2659 O LYS B 573 25.749 7.029 -13.818 1.00 40.57 O ANISOU 2659 O LYS B 573 6278 5402 3736 -1621 320 283 O ATOM 2660 CB LYS B 573 23.968 8.333 -15.568 1.00 50.16 C ANISOU 2660 CB LYS B 573 7506 6588 4963 -1507 375 506 C ATOM 2661 CG LYS B 573 22.830 8.717 -16.510 1.00 64.24 C ANISOU 2661 CG LYS B 573 9275 8404 6731 -1439 383 646 C ATOM 2662 CD LYS B 573 23.367 8.982 -17.924 1.00 76.96 C ANISOU 2662 CD LYS B 573 10892 10033 8314 -1450 401 714 C ATOM 2663 CE LYS B 573 22.505 9.978 -18.718 1.00 86.41 C ANISOU 2663 CE LYS B 573 12080 11222 9532 -1376 455 866 C ATOM 2664 NZ LYS B 573 21.237 9.404 -19.271 1.00 87.39 N ANISOU 2664 NZ LYS B 573 12154 11471 9581 -1337 388 966 N ATOM 2665 N ASN B 574 24.629 7.634 -11.987 1.00 44.89 N ANISOU 2665 N ASN B 574 6829 5899 4329 -1576 347 240 N ATOM 2666 CA ASN B 574 25.722 7.195 -11.114 1.00 39.27 C ANISOU 2666 CA ASN B 574 6104 5210 3608 -1644 327 134 C ATOM 2667 C ASN B 574 25.613 5.745 -10.624 1.00 45.40 C ANISOU 2667 C ASN B 574 6830 6088 4331 -1645 249 111 C ATOM 2668 O ASN B 574 26.470 5.269 -9.873 1.00 43.30 O ANISOU 2668 O ASN B 574 6539 5860 4053 -1691 231 41 O ATOM 2669 CB ASN B 574 25.880 8.139 -9.927 1.00 45.80 C ANISOU 2669 CB ASN B 574 6960 5968 4474 -1666 382 55 C ATOM 2670 CG ASN B 574 24.651 8.169 -9.043 1.00 41.79 C ANISOU 2670 CG ASN B 574 6451 5463 3965 -1601 385 63 C ATOM 2671 OD1 ASN B 574 23.728 7.360 -9.200 1.00 36.18 O ANISOU 2671 OD1 ASN B 574 5704 4820 3224 -1547 335 126 O ATOM 2672 ND2 ASN B 574 24.634 9.101 -8.104 1.00 38.96 N ANISOU 2672 ND2 ASN B 574 6133 5032 3638 -1609 448 -3 N ATOM 2673 N GLY B 575 24.567 5.040 -11.049 1.00 40.10 N ANISOU 2673 N GLY B 575 6139 5466 3632 -1597 205 178 N ATOM 2674 CA GLY B 575 24.357 3.671 -10.609 1.00 29.47 C ANISOU 2674 CA GLY B 575 4749 4200 2248 -1598 139 164 C ATOM 2675 C GLY B 575 23.952 3.576 -9.139 1.00 38.81 C ANISOU 2675 C GLY B 575 5906 5403 3438 -1580 134 124 C ATOM 2676 O GLY B 575 23.967 2.494 -8.547 1.00 38.77 O ANISOU 2676 O GLY B 575 5859 5462 3411 -1584 89 106 O ATOM 2677 N VAL B 576 23.595 4.707 -8.540 1.00 36.38 N ANISOU 2677 N VAL B 576 5626 5037 3161 -1557 188 110 N ATOM 2678 CA VAL B 576 23.226 4.732 -7.117 1.00 45.16 C ANISOU 2678 CA VAL B 576 6722 6169 4270 -1539 193 64 C ATOM 2679 C VAL B 576 21.810 5.263 -6.910 1.00 44.98 C ANISOU 2679 C VAL B 576 6706 6120 4265 -1459 222 128 C ATOM 2680 O VAL B 576 21.413 6.250 -7.524 1.00 41.07 O ANISOU 2680 O VAL B 576 6249 5551 3803 -1427 276 176 O ATOM 2681 CB VAL B 576 24.210 5.591 -6.278 1.00 47.08 C ANISOU 2681 CB VAL B 576 6994 6370 4523 -1594 242 -38 C ATOM 2682 CG1 VAL B 576 23.724 5.711 -4.831 1.00 48.96 C ANISOU 2682 CG1 VAL B 576 7224 6633 4744 -1571 254 -88 C ATOM 2683 CG2 VAL B 576 25.620 5.002 -6.322 1.00 43.72 C ANISOU 2683 CG2 VAL B 576 6541 5995 4078 -1670 211 -89 C ATOM 2684 N GLN B 577 21.040 4.613 -6.048 1.00 43.63 N ANISOU 2684 N GLN B 577 6492 6011 4074 -1420 192 142 N ATOM 2685 CA GLN B 577 19.692 5.089 -5.756 1.00 25.62 C ANISOU 2685 CA GLN B 577 4209 3716 1810 -1337 224 211 C ATOM 2686 C GLN B 577 19.737 6.378 -4.913 1.00 41.73 C ANISOU 2686 C GLN B 577 6307 5672 3875 -1317 317 149 C ATOM 2687 O GLN B 577 20.084 6.349 -3.734 1.00 38.98 O ANISOU 2687 O GLN B 577 5961 5345 3504 -1335 326 62 O ATOM 2688 CB GLN B 577 18.898 3.996 -5.018 1.00 39.31 C ANISOU 2688 CB GLN B 577 5874 5544 3516 -1305 168 246 C ATOM 2689 CG GLN B 577 18.828 2.683 -5.791 1.00 42.41 C ANISOU 2689 CG GLN B 577 6219 6006 3889 -1335 83 295 C ATOM 2690 CD GLN B 577 18.368 1.515 -4.936 1.00 41.06 C ANISOU 2690 CD GLN B 577 5983 5918 3701 -1323 33 309 C ATOM 2691 OE1 GLN B 577 17.435 1.637 -4.134 1.00 34.45 O ANISOU 2691 OE1 GLN B 577 5117 5105 2866 -1263 47 348 O ATOM 2692 NE2 GLN B 577 19.012 0.366 -5.120 1.00 30.48 N ANISOU 2692 NE2 GLN B 577 4617 4617 2345 -1374 -19 286 N ATOM 2693 N ASP B 578 19.386 7.507 -5.518 1.00 41.33 N ANISOU 2693 N ASP B 578 6306 5526 3871 -1279 391 195 N ATOM 2694 CA ASP B 578 19.453 8.784 -4.817 1.00 44.36 C ANISOU 2694 CA ASP B 578 6763 5804 4289 -1263 496 130 C ATOM 2695 C ASP B 578 18.077 9.275 -4.364 1.00 47.23 C ANISOU 2695 C ASP B 578 7129 6143 4674 -1150 560 205 C ATOM 2696 O ASP B 578 17.074 9.064 -5.046 1.00 45.59 O ANISOU 2696 O ASP B 578 6876 5969 4476 -1080 544 341 O ATOM 2697 CB ASP B 578 20.100 9.853 -5.709 1.00 46.02 C ANISOU 2697 CB ASP B 578 7036 5896 4552 -1295 562 126 C ATOM 2698 CG ASP B 578 21.528 9.504 -6.111 1.00 52.55 C ANISOU 2698 CG ASP B 578 7862 6743 5363 -1404 514 53 C ATOM 2699 OD1 ASP B 578 22.343 9.183 -5.221 1.00 54.54 O ANISOU 2699 OD1 ASP B 578 8108 7034 5580 -1473 487 -57 O ATOM 2700 OD2 ASP B 578 21.839 9.565 -7.320 1.00 43.02 O ANISOU 2700 OD2 ASP B 578 6655 5519 4173 -1419 505 113 O ATOM 2701 N LEU B 579 18.034 9.944 -3.216 1.00 52.26 N ANISOU 2701 N LEU B 579 7818 6727 5313 -1133 636 118 N ATOM 2702 CA LEU B 579 16.824 10.639 -2.798 1.00 53.48 C ANISOU 2702 CA LEU B 579 7993 6830 5496 -1017 729 184 C ATOM 2703 C LEU B 579 16.356 11.491 -3.963 1.00 55.72 C ANISOU 2703 C LEU B 579 8299 7022 5850 -958 796 305 C ATOM 2704 O LEU B 579 17.156 12.202 -4.576 1.00 48.06 O ANISOU 2704 O LEU B 579 7386 5955 4919 -1011 838 268 O ATOM 2705 CB LEU B 579 17.106 11.527 -1.585 1.00 56.15 C ANISOU 2705 CB LEU B 579 8419 7083 5833 -1026 828 46 C ATOM 2706 CG LEU B 579 16.801 10.973 -0.192 1.00 53.32 C ANISOU 2706 CG LEU B 579 8036 6818 5406 -1007 809 -17 C ATOM 2707 CD1 LEU B 579 16.817 9.444 -0.168 1.00 55.73 C ANISOU 2707 CD1 LEU B 579 8230 7289 5655 -1033 670 27 C ATOM 2708 CD2 LEU B 579 17.764 11.549 0.836 1.00 50.05 C ANISOU 2708 CD2 LEU B 579 7701 6359 4956 -1095 854 -205 C ATOM 2709 N GLY B 580 15.068 11.405 -4.285 1.00 54.25 N ANISOU 2709 N GLY B 580 8059 6876 5678 -849 807 461 N ATOM 2710 CA GLY B 580 14.512 12.187 -5.377 1.00 55.19 C ANISOU 2710 CA GLY B 580 8181 6932 5856 -779 872 603 C ATOM 2711 C GLY B 580 14.214 11.387 -6.638 1.00 58.14 C ANISOU 2711 C GLY B 580 8467 7421 6204 -792 764 734 C ATOM 2712 O GLY B 580 13.300 11.728 -7.386 1.00 60.29 O ANISOU 2712 O GLY B 580 8698 7708 6501 -709 793 897 O ATOM 2713 N GLU B 581 14.989 10.332 -6.884 1.00 51.45 N ANISOU 2713 N GLU B 581 7589 6658 5303 -895 645 667 N ATOM 2714 CA GLU B 581 14.756 9.470 -8.042 1.00 49.44 C ANISOU 2714 CA GLU B 581 7261 6512 5010 -922 541 766 C ATOM 2715 C GLU B 581 13.601 8.516 -7.727 1.00 47.09 C ANISOU 2715 C GLU B 581 6874 6343 4677 -880 469 853 C ATOM 2716 O GLU B 581 13.387 8.174 -6.567 1.00 42.72 O ANISOU 2716 O GLU B 581 6310 5808 4111 -863 469 798 O ATOM 2717 CB GLU B 581 16.033 8.707 -8.407 1.00 38.71 C ANISOU 2717 CB GLU B 581 5914 5181 3613 -1041 458 658 C ATOM 2718 CG GLU B 581 17.154 9.629 -8.929 1.00 47.62 C ANISOU 2718 CG GLU B 581 7116 6198 4778 -1087 522 598 C ATOM 2719 CD GLU B 581 18.527 8.968 -8.966 1.00 46.57 C ANISOU 2719 CD GLU B 581 6997 6085 4613 -1199 460 476 C ATOM 2720 OE1 GLU B 581 18.700 7.895 -8.348 1.00 43.61 O ANISOU 2720 OE1 GLU B 581 6585 5791 4193 -1236 385 417 O ATOM 2721 OE2 GLU B 581 19.445 9.536 -9.600 1.00 42.02 O ANISOU 2721 OE2 GLU B 581 6463 5443 4060 -1245 494 448 O ATOM 2722 N VAL B 582 12.852 8.101 -8.749 1.00 46.77 N ANISOU 2722 N VAL B 582 6764 6395 4613 -868 408 992 N ATOM 2723 CA VAL B 582 11.648 7.285 -8.536 1.00 45.29 C ANISOU 2723 CA VAL B 582 6481 6330 4397 -833 343 1095 C ATOM 2724 C VAL B 582 11.599 5.998 -9.375 1.00 47.80 C ANISOU 2724 C VAL B 582 6738 6769 4654 -922 207 1120 C ATOM 2725 O VAL B 582 12.386 5.814 -10.313 1.00 39.35 O ANISOU 2725 O VAL B 582 5697 5696 3558 -995 169 1080 O ATOM 2726 CB VAL B 582 10.371 8.096 -8.808 1.00 48.42 C ANISOU 2726 CB VAL B 582 6832 6741 4826 -715 411 1276 C ATOM 2727 CG1 VAL B 582 10.122 9.100 -7.680 1.00 50.85 C ANISOU 2727 CG1 VAL B 582 7190 6940 5191 -613 547 1254 C ATOM 2728 CG2 VAL B 582 10.484 8.793 -10.153 1.00 43.00 C ANISOU 2728 CG2 VAL B 582 6153 6038 4149 -709 436 1368 C ATOM 2729 N GLY B 583 10.653 5.123 -9.035 1.00 33.55 N ANISOU 2729 N GLY B 583 4852 5069 2827 -915 140 1186 N ATOM 2730 CA GLY B 583 10.572 3.804 -9.627 1.00 38.95 C ANISOU 2730 CA GLY B 583 5486 5856 3457 -1009 16 1188 C ATOM 2731 C GLY B 583 10.088 3.778 -11.063 1.00 38.86 C ANISOU 2731 C GLY B 583 5435 5926 3405 -1039 -37 1302 C ATOM 2732 O GLY B 583 9.550 4.756 -11.575 1.00 47.95 O ANISOU 2732 O GLY B 583 6570 7079 4571 -967 19 1422 O ATOM 2733 N VAL B 584 10.293 2.641 -11.713 1.00 36.75 N ANISOU 2733 N VAL B 584 5154 5727 3083 -1144 -139 1265 N ATOM 2734 CA VAL B 584 9.811 2.418 -13.069 1.00 41.13 C ANISOU 2734 CA VAL B 584 5668 6384 3575 -1195 -207 1358 C ATOM 2735 C VAL B 584 8.813 1.251 -13.100 1.00 40.22 C ANISOU 2735 C VAL B 584 5467 6394 3422 -1256 -313 1416 C ATOM 2736 O VAL B 584 9.110 0.140 -12.651 1.00 40.43 O ANISOU 2736 O VAL B 584 5502 6414 3445 -1326 -365 1320 O ATOM 2737 CB VAL B 584 10.973 2.162 -14.048 1.00 38.73 C ANISOU 2737 CB VAL B 584 5437 6051 3226 -1280 -231 1257 C ATOM 2738 CG1 VAL B 584 10.437 1.708 -15.395 1.00 43.76 C ANISOU 2738 CG1 VAL B 584 6033 6816 3779 -1351 -316 1336 C ATOM 2739 CG2 VAL B 584 11.841 3.423 -14.199 1.00 38.67 C ANISOU 2739 CG2 VAL B 584 5500 5935 3258 -1225 -129 1231 C ATOM 2740 N LYS B 585 7.620 1.518 -13.618 1.00 45.55 N ANISOU 2740 N LYS B 585 6052 7183 4073 -1229 -339 1584 N ATOM 2741 CA LYS B 585 6.538 0.538 -13.616 1.00 48.80 C ANISOU 2741 CA LYS B 585 6367 7722 4453 -1287 -437 1661 C ATOM 2742 C LYS B 585 6.621 -0.419 -14.809 1.00 49.05 C ANISOU 2742 C LYS B 585 6399 7841 4395 -1433 -547 1627 C ATOM 2743 O LYS B 585 7.184 -0.082 -15.833 1.00 40.05 O ANISOU 2743 O LYS B 585 5308 6705 3205 -1462 -546 1606 O ATOM 2744 CB LYS B 585 5.189 1.266 -13.633 1.00 52.84 C ANISOU 2744 CB LYS B 585 6768 8334 4974 -1194 -416 1871 C ATOM 2745 CG LYS B 585 3.994 0.326 -13.690 1.00 65.34 C ANISOU 2745 CG LYS B 585 8234 10070 6524 -1261 -521 1974 C ATOM 2746 CD LYS B 585 2.680 1.074 -13.811 1.00 74.26 C ANISOU 2746 CD LYS B 585 9241 11318 7658 -1167 -500 2203 C ATOM 2747 CE LYS B 585 1.511 0.098 -13.816 1.00 80.00 C ANISOU 2747 CE LYS B 585 9841 12202 8352 -1247 -611 2306 C ATOM 2748 NZ LYS B 585 0.202 0.782 -14.008 1.00 84.12 N ANISOU 2748 NZ LYS B 585 10224 12865 8871 -1159 -597 2551 N ATOM 2749 N GLY B 586 6.064 -1.618 -14.675 1.00 56.41 N ANISOU 2749 N GLY B 586 7282 8843 5307 -1527 -638 1619 N ATOM 2750 CA GLY B 586 5.928 -2.511 -15.814 1.00 50.44 C ANISOU 2750 CA GLY B 586 6523 8183 4460 -1673 -743 1597 C ATOM 2751 C GLY B 586 7.159 -3.289 -16.252 1.00 49.08 C ANISOU 2751 C GLY B 586 6467 7925 4257 -1770 -757 1410 C ATOM 2752 O GLY B 586 7.176 -3.869 -17.340 1.00 43.19 O ANISOU 2752 O GLY B 586 5740 7248 3424 -1885 -827 1378 O ATOM 2753 N VAL B 587 8.194 -3.316 -15.419 1.00 50.08 N ANISOU 2753 N VAL B 587 6669 7909 4449 -1725 -688 1288 N ATOM 2754 CA VAL B 587 9.372 -4.108 -15.745 1.00 43.51 C ANISOU 2754 CA VAL B 587 5938 6996 3598 -1804 -691 1124 C ATOM 2755 C VAL B 587 9.194 -5.527 -15.235 1.00 39.78 C ANISOU 2755 C VAL B 587 5458 6510 3147 -1889 -742 1058 C ATOM 2756 O VAL B 587 8.828 -5.738 -14.086 1.00 42.40 O ANISOU 2756 O VAL B 587 5741 6819 3548 -1843 -729 1084 O ATOM 2757 CB VAL B 587 10.674 -3.490 -15.184 1.00 42.25 C ANISOU 2757 CB VAL B 587 5858 6702 3493 -1726 -595 1029 C ATOM 2758 CG1 VAL B 587 11.841 -4.428 -15.416 1.00 41.23 C ANISOU 2758 CG1 VAL B 587 5817 6498 3351 -1800 -594 876 C ATOM 2759 CG2 VAL B 587 10.948 -2.156 -15.851 1.00 44.04 C ANISOU 2759 CG2 VAL B 587 6105 6928 3701 -1660 -541 1083 C ATOM 2760 N THR B 588 9.449 -6.503 -16.096 1.00 46.89 N ANISOU 2760 N THR B 588 6409 7420 3988 -2013 -795 975 N ATOM 2761 CA THR B 588 9.350 -7.901 -15.697 1.00 50.50 C ANISOU 2761 CA THR B 588 6873 7843 4473 -2102 -832 905 C ATOM 2762 C THR B 588 10.595 -8.336 -14.934 1.00 49.87 C ANISOU 2762 C THR B 588 6867 7621 4460 -2065 -760 782 C ATOM 2763 O THR B 588 11.716 -8.000 -15.318 1.00 58.34 O ANISOU 2763 O THR B 588 8020 8631 5517 -2041 -708 703 O ATOM 2764 CB THR B 588 9.173 -8.828 -16.915 1.00 56.24 C ANISOU 2764 CB THR B 588 7640 8619 5109 -2258 -906 847 C ATOM 2765 OG1 THR B 588 8.060 -8.385 -17.707 1.00 59.49 O ANISOU 2765 OG1 THR B 588 7974 9188 5441 -2301 -980 968 O ATOM 2766 CG2 THR B 588 8.947 -10.266 -16.455 1.00 54.39 C ANISOU 2766 CG2 THR B 588 7410 8336 4919 -2353 -936 785 C ATOM 2767 N VAL B 589 10.391 -9.084 -13.854 1.00 46.70 N ANISOU 2767 N VAL B 589 6430 7181 4134 -2058 -756 780 N ATOM 2768 CA VAL B 589 11.489 -9.610 -13.048 1.00 43.65 C ANISOU 2768 CA VAL B 589 6093 6679 3811 -2022 -691 684 C ATOM 2769 C VAL B 589 11.299 -11.114 -12.862 1.00 46.51 C ANISOU 2769 C VAL B 589 6460 7003 4208 -2113 -717 641 C ATOM 2770 O VAL B 589 10.203 -11.568 -12.541 1.00 41.93 O ANISOU 2770 O VAL B 589 5805 6478 3650 -2153 -769 716 O ATOM 2771 CB VAL B 589 11.550 -8.951 -11.649 1.00 42.37 C ANISOU 2771 CB VAL B 589 5878 6501 3718 -1898 -638 731 C ATOM 2772 CG1 VAL B 589 12.821 -9.383 -10.915 1.00 42.62 C ANISOU 2772 CG1 VAL B 589 5957 6437 3799 -1863 -572 636 C ATOM 2773 CG2 VAL B 589 11.481 -7.436 -11.748 1.00 37.68 C ANISOU 2773 CG2 VAL B 589 5274 5939 3103 -1811 -607 787 C ATOM 2774 N VAL B 590 12.363 -11.884 -13.066 1.00 53.59 N ANISOU 2774 N VAL B 590 7442 7802 5115 -2145 -674 529 N ATOM 2775 CA VAL B 590 12.288 -13.337 -12.916 1.00 59.16 C ANISOU 2775 CA VAL B 590 8167 8445 5865 -2227 -678 482 C ATOM 2776 C VAL B 590 13.420 -13.887 -12.048 1.00 54.95 C ANISOU 2776 C VAL B 590 7663 7805 5409 -2162 -593 427 C ATOM 2777 O VAL B 590 14.580 -13.516 -12.219 1.00 54.48 O ANISOU 2777 O VAL B 590 7662 7701 5336 -2112 -535 366 O ATOM 2778 CB VAL B 590 12.306 -14.050 -14.289 1.00 56.73 C ANISOU 2778 CB VAL B 590 7946 8122 5485 -2362 -710 396 C ATOM 2779 CG1 VAL B 590 12.188 -15.564 -14.109 1.00 62.71 C ANISOU 2779 CG1 VAL B 590 8732 8794 6301 -2452 -703 343 C ATOM 2780 CG2 VAL B 590 11.182 -13.535 -15.165 1.00 53.66 C ANISOU 2780 CG2 VAL B 590 7516 7865 5009 -2434 -802 461 C ATOM 2781 N ALA B 591 13.077 -14.781 -11.125 1.00 58.28 N ANISOU 2781 N ALA B 591 8035 8196 5911 -2164 -586 459 N ATOM 2782 CA ALA B 591 14.079 -15.411 -10.266 1.00 58.14 C ANISOU 2782 CA ALA B 591 8031 8092 5969 -2102 -505 428 C ATOM 2783 C ALA B 591 14.204 -16.907 -10.550 1.00 64.63 C ANISOU 2783 C ALA B 591 8907 8813 6838 -2188 -480 372 C ATOM 2784 O ALA B 591 13.199 -17.613 -10.657 1.00 61.46 O ANISOU 2784 O ALA B 591 8481 8414 6456 -2278 -529 399 O ATOM 2785 CB ALA B 591 13.758 -15.170 -8.787 1.00 53.49 C ANISOU 2785 CB ALA B 591 7337 7547 5441 -2006 -494 520 C ATOM 2786 N TYR B 592 15.447 -17.369 -10.681 1.00 68.31 N ANISOU 2786 N TYR B 592 9446 9185 7323 -2160 -398 298 N ATOM 2787 CA TYR B 592 15.762 -18.778 -10.888 1.00 66.94 C ANISOU 2787 CA TYR B 592 9337 8890 7207 -2219 -343 242 C ATOM 2788 C TYR B 592 16.708 -19.248 -9.786 1.00 71.10 C ANISOU 2788 C TYR B 592 9831 9360 7823 -2113 -250 273 C ATOM 2789 O TYR B 592 17.529 -18.472 -9.298 1.00 63.77 O ANISOU 2789 O TYR B 592 8875 8474 6882 -2013 -219 289 O ATOM 2790 CB TYR B 592 16.484 -18.975 -12.221 1.00 65.41 C ANISOU 2790 CB TYR B 592 9273 8632 6947 -2278 -310 125 C ATOM 2791 CG TYR B 592 15.818 -18.371 -13.435 1.00 63.39 C ANISOU 2791 CG TYR B 592 9055 8452 6578 -2371 -394 90 C ATOM 2792 CD1 TYR B 592 15.998 -17.033 -13.755 1.00 57.39 C ANISOU 2792 CD1 TYR B 592 8278 7784 5742 -2318 -424 110 C ATOM 2793 CD2 TYR B 592 15.038 -19.151 -14.286 1.00 67.06 C ANISOU 2793 CD2 TYR B 592 9574 8897 7010 -2517 -441 38 C ATOM 2794 CE1 TYR B 592 15.404 -16.478 -14.874 1.00 60.85 C ANISOU 2794 CE1 TYR B 592 8743 8303 6075 -2395 -495 95 C ATOM 2795 CE2 TYR B 592 14.438 -18.603 -15.408 1.00 69.42 C ANISOU 2795 CE2 TYR B 592 9897 9288 7191 -2605 -522 14 C ATOM 2796 CZ TYR B 592 14.625 -17.265 -15.696 1.00 67.83 C ANISOU 2796 CZ TYR B 592 9669 9186 6916 -2537 -547 50 C ATOM 2797 OH TYR B 592 14.034 -16.712 -16.808 1.00 74.91 O ANISOU 2797 OH TYR B 592 10581 10187 7696 -2615 -623 45 O ATOM 2798 N ASP B 593 16.622 -20.519 -9.406 1.00 77.02 N ANISOU 2798 N ASP B 593 10584 10017 8664 -2138 -202 284 N ATOM 2799 CA ASP B 593 17.614 -21.073 -8.488 1.00 77.12 C ANISOU 2799 CA ASP B 593 10569 9974 8760 -2036 -102 320 C ATOM 2800 C ASP B 593 18.916 -21.333 -9.249 1.00 77.25 C ANISOU 2800 C ASP B 593 10690 9902 8760 -2018 -12 234 C ATOM 2801 O ASP B 593 18.945 -22.106 -10.209 1.00 75.38 O ANISOU 2801 O ASP B 593 10559 9560 8522 -2101 19 151 O ATOM 2802 CB ASP B 593 17.105 -22.352 -7.816 1.00 78.71 C ANISOU 2802 CB ASP B 593 10733 10098 9074 -2058 -66 378 C ATOM 2803 CG ASP B 593 17.910 -22.724 -6.574 1.00 82.81 C ANISOU 2803 CG ASP B 593 11177 10612 9676 -1931 21 463 C ATOM 2804 OD1 ASP B 593 17.290 -22.995 -5.525 1.00 86.55 O ANISOU 2804 OD1 ASP B 593 11549 11126 10210 -1900 8 564 O ATOM 2805 OD2 ASP B 593 19.158 -22.744 -6.639 1.00 83.49 O ANISOU 2805 OD2 ASP B 593 11297 10665 9762 -1861 101 438 O ATOM 2806 N ASN B 594 19.986 -20.667 -8.823 1.00 78.85 N ANISOU 2806 N ASN B 594 10861 10153 8947 -1912 29 253 N ATOM 2807 CA ASN B 594 21.278 -20.766 -9.494 1.00 78.03 C ANISOU 2807 CA ASN B 594 10839 9987 8823 -1881 114 190 C ATOM 2808 C ASN B 594 21.735 -22.215 -9.674 1.00 86.28 C ANISOU 2808 C ASN B 594 11949 10880 9952 -1887 225 168 C ATOM 2809 O ASN B 594 21.901 -22.692 -10.799 1.00 89.28 O ANISOU 2809 O ASN B 594 12451 11166 10306 -1953 261 72 O ATOM 2810 CB ASN B 594 22.329 -19.962 -8.727 1.00 70.96 C ANISOU 2810 CB ASN B 594 9869 9175 7917 -1767 143 240 C ATOM 2811 CG ASN B 594 23.394 -19.373 -9.635 1.00 69.48 C ANISOU 2811 CG ASN B 594 9753 8985 7663 -1753 179 173 C ATOM 2812 OD1 ASN B 594 24.563 -19.297 -9.262 1.00 70.33 O ANISOU 2812 OD1 ASN B 594 9830 9105 7786 -1673 248 201 O ATOM 2813 ND2 ASN B 594 22.995 -18.950 -10.832 1.00 68.05 N ANISOU 2813 ND2 ASN B 594 9656 8796 7403 -1832 131 95 N ATOM 2814 N ALA B 595 21.931 -22.914 -8.562 1.00 91.41 N ANISOU 2814 N ALA B 595 12521 11509 10702 -1815 285 260 N ATOM 2815 CA ALA B 595 22.300 -24.326 -8.602 1.00 95.66 C ANISOU 2815 CA ALA B 595 13112 11894 11342 -1809 403 260 C ATOM 2816 C ALA B 595 21.130 -25.186 -9.065 1.00 96.34 C ANISOU 2816 C ALA B 595 13260 11879 11464 -1937 375 214 C ATOM 2817 O ALA B 595 21.132 -25.683 -10.188 1.00 93.31 O ANISOU 2817 O ALA B 595 13009 11387 11058 -2024 406 103 O ATOM 2818 CB ALA B 595 22.787 -24.792 -7.238 1.00 96.57 C ANISOU 2818 CB ALA B 595 13110 12030 11553 -1691 474 393 C ATOM 2819 N ALA B 596 20.132 -25.337 -8.194 1.00 97.90 N ANISOU 2819 N ALA B 596 13362 12121 11713 -1954 316 298 N ATOM 2820 CA ALA B 596 18.969 -26.193 -8.446 1.00 96.11 C ANISOU 2820 CA ALA B 596 13169 11811 11537 -2080 286 277 C ATOM 2821 C ALA B 596 18.584 -26.324 -9.919 1.00100.73 C ANISOU 2821 C ALA B 596 13896 12330 12047 -2227 251 132 C ATOM 2822 O ALA B 596 19.078 -27.204 -10.619 1.00106.39 O ANISOU 2822 O ALA B 596 14735 12894 12793 -2265 348 46 O ATOM 2823 CB ALA B 596 17.775 -25.735 -7.620 1.00 89.54 C ANISOU 2823 CB ALA B 596 12210 11103 10707 -2096 174 371 C ATOM 2824 N ALA B 597 17.690 -25.464 -10.389 1.00 98.98 N ANISOU 2824 N ALA B 597 13658 12225 11724 -2309 118 107 N ATOM 2825 CA ALA B 597 17.243 -25.545 -11.777 1.00101.19 C ANISOU 2825 CA ALA B 597 14058 12475 11915 -2458 70 -21 C ATOM 2826 C ALA B 597 17.028 -24.165 -12.387 1.00 95.68 C ANISOU 2826 C ALA B 597 13344 11934 11075 -2468 -38 -40 C ATOM 2827 O ALA B 597 17.976 -23.493 -12.800 1.00 88.92 O ANISOU 2827 O ALA B 597 12526 11103 10155 -2399 -6 -77 O ATOM 2828 CB ALA B 597 15.960 -26.382 -11.876 1.00104.89 C ANISOU 2828 CB ALA B 597 14529 12897 12427 -2610 15 -28 C ATOM 2829 N ALA B 598 15.770 -23.746 -12.440 1.00 95.39 N ANISOU 2829 N ALA B 598 13245 12003 10996 -2553 -162 -3 N ATOM 2830 CA ALA B 598 15.434 -22.471 -13.049 1.00 93.40 C ANISOU 2830 CA ALA B 598 12972 11898 10616 -2566 -261 -5 C ATOM 2831 C ALA B 598 14.328 -21.744 -12.287 1.00 89.57 C ANISOU 2831 C ALA B 598 12346 11553 10134 -2549 -362 117 C ATOM 2832 O ALA B 598 14.416 -21.543 -11.076 1.00 92.51 O ANISOU 2832 O ALA B 598 12621 11952 10577 -2439 -340 214 O ATOM 2833 CB ALA B 598 15.039 -22.669 -14.499 1.00 96.37 C ANISOU 2833 CB ALA B 598 13457 12270 10888 -2719 -308 -119 C ATOM 2834 N GLU B 599 13.279 -21.369 -13.007 1.00 83.36 N ANISOU 2834 N GLU B 599 11547 10861 9264 -2658 -469 118 N ATOM 2835 CA GLU B 599 12.313 -20.398 -12.506 1.00 78.59 C ANISOU 2835 CA GLU B 599 10816 10409 8636 -2625 -561 236 C ATOM 2836 C GLU B 599 11.645 -20.773 -11.182 1.00 77.11 C ANISOU 2836 C GLU B 599 10510 10232 8557 -2582 -564 353 C ATOM 2837 O GLU B 599 10.941 -21.776 -11.090 1.00 79.85 O ANISOU 2837 O GLU B 599 10845 10532 8964 -2682 -580 364 O ATOM 2838 CB GLU B 599 11.262 -20.099 -13.575 1.00 74.72 C ANISOU 2838 CB GLU B 599 10326 10024 8041 -2760 -672 228 C ATOM 2839 CG GLU B 599 10.342 -18.958 -13.207 1.00 70.69 C ANISOU 2839 CG GLU B 599 9688 9674 7495 -2710 -754 358 C ATOM 2840 CD GLU B 599 9.473 -18.516 -14.360 1.00 68.94 C ANISOU 2840 CD GLU B 599 9463 9577 7155 -2825 -856 362 C ATOM 2841 OE1 GLU B 599 9.913 -18.643 -15.528 1.00 74.21 O ANISOU 2841 OE1 GLU B 599 10237 10225 7734 -2904 -857 253 O ATOM 2842 OE2 GLU B 599 8.352 -18.033 -14.093 1.00 63.37 O ANISOU 2842 OE2 GLU B 599 8641 8997 6439 -2831 -933 483 O ATOM 2843 N VAL B 600 11.876 -19.946 -10.163 1.00 76.49 N ANISOU 2843 N VAL B 600 10346 10217 8500 -2438 -546 437 N ATOM 2844 CA VAL B 600 11.256 -20.118 -8.848 1.00 77.16 C ANISOU 2844 CA VAL B 600 10310 10338 8669 -2376 -548 558 C ATOM 2845 C VAL B 600 10.216 -19.024 -8.569 1.00 72.12 C ANISOU 2845 C VAL B 600 9567 9852 7983 -2343 -629 662 C ATOM 2846 O VAL B 600 9.451 -19.103 -7.600 1.00 65.16 O ANISOU 2846 O VAL B 600 8578 9023 7157 -2306 -645 772 O ATOM 2847 CB VAL B 600 12.309 -20.107 -7.715 1.00 76.26 C ANISOU 2847 CB VAL B 600 10171 10187 8618 -2230 -455 582 C ATOM 2848 CG1 VAL B 600 13.325 -21.223 -7.914 1.00 80.31 C ANISOU 2848 CG1 VAL B 600 10773 10551 9190 -2244 -361 505 C ATOM 2849 CG2 VAL B 600 13.001 -18.749 -7.641 1.00 74.84 C ANISOU 2849 CG2 VAL B 600 9992 10080 8366 -2124 -448 571 C ATOM 2850 N GLY B 601 10.200 -18.002 -9.418 1.00 67.79 N ANISOU 2850 N GLY B 601 9049 9375 7335 -2349 -671 636 N ATOM 2851 CA GLY B 601 9.253 -16.910 -9.279 1.00 65.61 C ANISOU 2851 CA GLY B 601 8681 9235 7013 -2310 -734 738 C ATOM 2852 C GLY B 601 9.400 -15.884 -10.384 1.00 64.18 C ANISOU 2852 C GLY B 601 8551 9111 6725 -2321 -766 701 C ATOM 2853 O GLY B 601 10.414 -15.856 -11.087 1.00 68.19 O ANISOU 2853 O GLY B 601 9160 9555 7194 -2331 -729 596 O ATOM 2854 N ARG B 602 8.378 -15.049 -10.548 1.00 56.81 N ANISOU 2854 N ARG B 602 7539 8301 5745 -2315 -829 800 N ATOM 2855 CA ARG B 602 8.426 -13.951 -11.509 1.00 59.19 C ANISOU 2855 CA ARG B 602 7868 8671 5951 -2306 -853 797 C ATOM 2856 C ARG B 602 7.336 -12.932 -11.202 1.00 59.16 C ANISOU 2856 C ARG B 602 7753 8795 5930 -2241 -890 943 C ATOM 2857 O ARG B 602 6.321 -13.267 -10.588 1.00 53.25 O ANISOU 2857 O ARG B 602 6906 8102 5225 -2251 -925 1043 O ATOM 2858 CB ARG B 602 8.267 -14.462 -12.942 1.00 66.39 C ANISOU 2858 CB ARG B 602 8846 9598 6781 -2460 -912 727 C ATOM 2859 CG ARG B 602 6.852 -14.895 -13.301 1.00 66.71 C ANISOU 2859 CG ARG B 602 8806 9744 6798 -2583 -1011 809 C ATOM 2860 CD ARG B 602 6.662 -14.902 -14.814 1.00 66.58 C ANISOU 2860 CD ARG B 602 8842 9794 6660 -2715 -1078 758 C ATOM 2861 NE ARG B 602 7.713 -15.669 -15.475 1.00 66.65 N ANISOU 2861 NE ARG B 602 8994 9682 6648 -2785 -1035 591 N ATOM 2862 CZ ARG B 602 8.169 -15.411 -16.696 1.00 67.18 C ANISOU 2862 CZ ARG B 602 9147 9771 6607 -2838 -1045 512 C ATOM 2863 NH1 ARG B 602 7.662 -14.400 -17.388 1.00 68.51 N ANISOU 2863 NH1 ARG B 602 9266 10084 6680 -2830 -1100 591 N ATOM 2864 NH2 ARG B 602 9.132 -16.161 -17.219 1.00 64.08 N ANISOU 2864 NH2 ARG B 602 8886 9259 6201 -2890 -993 363 N ATOM 2865 N THR B 603 7.539 -11.692 -11.641 1.00 51.97 N ANISOU 2865 N THR B 603 6855 7928 4963 -2171 -876 962 N ATOM 2866 CA THR B 603 6.593 -10.628 -11.334 1.00 49.69 C ANISOU 2866 CA THR B 603 6469 7745 4667 -2086 -888 1105 C ATOM 2867 C THR B 603 6.832 -9.414 -12.228 1.00 51.11 C ANISOU 2867 C THR B 603 6682 7965 4774 -2045 -877 1118 C ATOM 2868 O THR B 603 7.614 -9.474 -13.185 1.00 52.59 O ANISOU 2868 O THR B 603 6960 8117 4906 -2101 -877 1021 O ATOM 2869 CB THR B 603 6.676 -10.228 -9.832 1.00 53.57 C ANISOU 2869 CB THR B 603 6914 8206 5235 -1945 -818 1149 C ATOM 2870 OG1 THR B 603 5.615 -9.323 -9.498 1.00 58.07 O ANISOU 2870 OG1 THR B 603 7387 8875 5803 -1863 -822 1296 O ATOM 2871 CG2 THR B 603 8.015 -9.576 -9.523 1.00 49.89 C ANISOU 2871 CG2 THR B 603 6533 7647 4774 -1856 -734 1051 C ATOM 2872 N ILE B 604 6.158 -8.314 -11.924 1.00 47.17 N ANISOU 2872 N ILE B 604 6109 7537 4277 -1943 -859 1243 N ATOM 2873 CA ILE B 604 6.329 -7.084 -12.699 1.00 51.20 C ANISOU 2873 CA ILE B 604 6642 8079 4732 -1888 -836 1276 C ATOM 2874 C ILE B 604 6.294 -5.897 -11.741 1.00 46.20 C ANISOU 2874 C ILE B 604 5983 7421 4152 -1727 -749 1342 C ATOM 2875 O ILE B 604 5.521 -5.897 -10.785 1.00 44.09 O ANISOU 2875 O ILE B 604 5636 7186 3933 -1667 -739 1430 O ATOM 2876 CB ILE B 604 5.239 -6.949 -13.784 1.00 55.72 C ANISOU 2876 CB ILE B 604 7142 8801 5228 -1960 -918 1394 C ATOM 2877 CG1 ILE B 604 5.252 -5.553 -14.394 1.00 57.45 C ANISOU 2877 CG1 ILE B 604 7359 9062 5407 -1872 -878 1473 C ATOM 2878 CG2 ILE B 604 3.871 -7.214 -13.193 1.00 65.08 C ANISOU 2878 CG2 ILE B 604 8195 10088 6443 -1959 -964 1540 C ATOM 2879 CD1 ILE B 604 3.936 -5.167 -15.030 1.00 67.21 C ANISOU 2879 CD1 ILE B 604 8477 10469 6589 -1886 -940 1653 C ATOM 2880 N THR B 605 7.148 -4.902 -11.968 1.00 39.73 N ANISOU 2880 N THR B 605 5234 6537 3323 -1659 -681 1296 N ATOM 2881 CA THR B 605 7.228 -3.771 -11.042 1.00 40.73 C ANISOU 2881 CA THR B 605 5357 6617 3500 -1516 -588 1331 C ATOM 2882 C THR B 605 5.947 -2.946 -11.043 1.00 45.31 C ANISOU 2882 C THR B 605 5842 7293 4083 -1437 -579 1510 C ATOM 2883 O THR B 605 5.338 -2.726 -12.094 1.00 46.53 O ANISOU 2883 O THR B 605 5954 7542 4184 -1472 -626 1605 O ATOM 2884 CB THR B 605 8.417 -2.847 -11.357 1.00 36.54 C ANISOU 2884 CB THR B 605 4925 5993 2966 -1474 -515 1244 C ATOM 2885 OG1 THR B 605 8.376 -2.450 -12.742 1.00 35.37 O ANISOU 2885 OG1 THR B 605 4791 5895 2754 -1515 -543 1283 O ATOM 2886 CG2 THR B 605 9.737 -3.565 -11.049 1.00 31.84 C ANISOU 2886 CG2 THR B 605 4412 5303 2383 -1522 -503 1081 C ATOM 2887 N ASP B 606 5.554 -2.477 -9.862 1.00 41.75 N ANISOU 2887 N ASP B 606 5353 6822 3687 -1325 -514 1560 N ATOM 2888 CA ASP B 606 4.336 -1.690 -9.709 1.00 47.99 C ANISOU 2888 CA ASP B 606 6050 7692 4490 -1227 -485 1738 C ATOM 2889 C ASP B 606 4.551 -0.219 -10.064 1.00 49.48 C ANISOU 2889 C ASP B 606 6282 7835 4685 -1124 -392 1779 C ATOM 2890 O ASP B 606 5.584 0.146 -10.621 1.00 50.05 O ANISOU 2890 O ASP B 606 6447 7830 4741 -1148 -368 1678 O ATOM 2891 CB ASP B 606 3.801 -1.825 -8.280 1.00 50.52 C ANISOU 2891 CB ASP B 606 6318 8012 4866 -1144 -443 1776 C ATOM 2892 CG ASP B 606 4.756 -1.269 -7.238 1.00 59.47 C ANISOU 2892 CG ASP B 606 7541 9019 6036 -1061 -342 1654 C ATOM 2893 OD1 ASP B 606 5.517 -0.331 -7.560 1.00 60.27 O ANISOU 2893 OD1 ASP B 606 7726 9038 6135 -1026 -278 1593 O ATOM 2894 OD2 ASP B 606 4.734 -1.761 -6.087 1.00 64.14 O ANISOU 2894 OD2 ASP B 606 8114 9600 6655 -1035 -328 1623 O ATOM 2895 N ASP B 607 3.571 0.619 -9.732 1.00 46.98 N ANISOU 2895 N ASP B 607 5895 7561 4395 -1004 -331 1934 N ATOM 2896 CA ASP B 607 3.627 2.051 -10.036 1.00 55.33 C ANISOU 2896 CA ASP B 607 6985 8566 5472 -893 -225 1998 C ATOM 2897 C ASP B 607 4.869 2.730 -9.464 1.00 53.00 C ANISOU 2897 C ASP B 607 6821 8103 5214 -850 -126 1837 C ATOM 2898 O ASP B 607 5.391 3.680 -10.053 1.00 49.85 O ANISOU 2898 O ASP B 607 6483 7635 4821 -818 -62 1829 O ATOM 2899 CB ASP B 607 2.385 2.755 -9.485 1.00 73.13 C ANISOU 2899 CB ASP B 607 9146 10873 7764 -753 -154 2183 C ATOM 2900 CG ASP B 607 1.092 2.165 -10.017 1.00 89.07 C ANISOU 2900 CG ASP B 607 11017 13077 9748 -793 -250 2366 C ATOM 2901 OD1 ASP B 607 0.135 2.013 -9.225 1.00 95.11 O ANISOU 2901 OD1 ASP B 607 11692 13904 10542 -728 -237 2475 O ATOM 2902 OD2 ASP B 607 1.033 1.852 -11.224 1.00 93.64 O ANISOU 2902 OD2 ASP B 607 11567 13747 10264 -893 -341 2402 O ATOM 2903 N LYS B 608 5.321 2.248 -8.307 1.00 48.25 N ANISOU 2903 N LYS B 608 6254 7443 4636 -852 -113 1717 N ATOM 2904 CA LYS B 608 6.446 2.849 -7.581 1.00 52.09 C ANISOU 2904 CA LYS B 608 6852 7789 5152 -820 -24 1564 C ATOM 2905 C LYS B 608 7.796 2.195 -7.910 1.00 44.21 C ANISOU 2905 C LYS B 608 5930 6739 4128 -937 -77 1394 C ATOM 2906 O LYS B 608 8.816 2.495 -7.281 1.00 42.80 O ANISOU 2906 O LYS B 608 5833 6464 3966 -934 -23 1260 O ATOM 2907 CB LYS B 608 6.204 2.767 -6.067 1.00 58.03 C ANISOU 2907 CB LYS B 608 7594 8523 5932 -749 28 1534 C ATOM 2908 CG LYS B 608 5.437 3.940 -5.451 1.00 66.31 C ANISOU 2908 CG LYS B 608 8636 9539 7019 -600 153 1630 C ATOM 2909 CD LYS B 608 5.462 3.839 -3.912 1.00 72.43 C ANISOU 2909 CD LYS B 608 9425 10288 7806 -543 208 1557 C ATOM 2910 CE LYS B 608 4.824 5.052 -3.228 1.00 72.16 C ANISOU 2910 CE LYS B 608 9409 10199 7807 -391 352 1623 C ATOM 2911 NZ LYS B 608 4.813 4.958 -1.723 1.00 58.15 N ANISOU 2911 NZ LYS B 608 7652 8414 6028 -335 408 1550 N ATOM 2912 N GLY B 609 7.802 1.296 -8.886 1.00 37.08 N ANISOU 2912 N GLY B 609 5001 5906 3181 -1042 -179 1402 N ATOM 2913 CA GLY B 609 9.016 0.589 -9.245 1.00 42.75 C ANISOU 2913 CA GLY B 609 5788 6580 3876 -1145 -223 1255 C ATOM 2914 C GLY B 609 9.308 -0.598 -8.340 1.00 42.30 C ANISOU 2914 C GLY B 609 5719 6525 3827 -1192 -264 1170 C ATOM 2915 O GLY B 609 10.349 -1.236 -8.475 1.00 44.55 O ANISOU 2915 O GLY B 609 6057 6769 4101 -1264 -288 1052 O ATOM 2916 N GLY B 610 8.387 -0.896 -7.421 1.00 37.74 N ANISOU 2916 N GLY B 610 5068 5998 3272 -1144 -267 1242 N ATOM 2917 CA GLY B 610 8.582 -1.963 -6.449 1.00 31.00 C ANISOU 2917 CA GLY B 610 4193 5151 2434 -1172 -294 1184 C ATOM 2918 C GLY B 610 8.141 -3.327 -6.954 1.00 35.71 C ANISOU 2918 C GLY B 610 4737 5814 3017 -1275 -395 1212 C ATOM 2919 O GLY B 610 7.242 -3.440 -7.793 1.00 41.29 O ANISOU 2919 O GLY B 610 5391 6597 3702 -1311 -450 1313 O ATOM 2920 N TYR B 611 8.795 -4.372 -6.464 1.00 32.86 N ANISOU 2920 N TYR B 611 4391 5424 2669 -1328 -416 1123 N ATOM 2921 CA TYR B 611 8.373 -5.739 -6.763 1.00 36.77 C ANISOU 2921 CA TYR B 611 4842 5960 3166 -1425 -497 1142 C ATOM 2922 C TYR B 611 8.816 -6.647 -5.626 1.00 38.11 C ANISOU 2922 C TYR B 611 4999 6103 3376 -1421 -484 1091 C ATOM 2923 O TYR B 611 9.734 -6.300 -4.863 1.00 31.50 O ANISOU 2923 O TYR B 611 4204 5218 2548 -1368 -424 1013 O ATOM 2924 CB TYR B 611 8.971 -6.251 -8.082 1.00 33.87 C ANISOU 2924 CB TYR B 611 4539 5569 2761 -1537 -545 1070 C ATOM 2925 CG TYR B 611 10.409 -6.727 -7.946 1.00 42.25 C ANISOU 2925 CG TYR B 611 5682 6541 3831 -1564 -515 930 C ATOM 2926 CD1 TYR B 611 11.463 -5.824 -7.976 1.00 34.91 C ANISOU 2926 CD1 TYR B 611 4822 5553 2892 -1520 -455 856 C ATOM 2927 CD2 TYR B 611 10.705 -8.078 -7.777 1.00 40.98 C ANISOU 2927 CD2 TYR B 611 5523 6353 3693 -1633 -541 881 C ATOM 2928 CE1 TYR B 611 12.763 -6.245 -7.856 1.00 38.29 C ANISOU 2928 CE1 TYR B 611 5309 5914 3325 -1544 -428 744 C ATOM 2929 CE2 TYR B 611 12.008 -8.514 -7.651 1.00 36.57 C ANISOU 2929 CE2 TYR B 611 5028 5720 3146 -1646 -504 772 C ATOM 2930 CZ TYR B 611 13.038 -7.587 -7.688 1.00 40.05 C ANISOU 2930 CZ TYR B 611 5527 6119 3569 -1600 -451 707 C ATOM 2931 OH TYR B 611 14.352 -7.994 -7.555 1.00 35.66 O ANISOU 2931 OH TYR B 611 5022 5503 3023 -1611 -414 613 O ATOM 2932 N LEU B 612 8.158 -7.802 -5.524 1.00 32.25 N ANISOU 2932 N LEU B 612 4196 5398 2658 -1482 -539 1140 N ATOM 2933 CA LEU B 612 8.533 -8.836 -4.563 1.00 39.55 C ANISOU 2933 CA LEU B 612 5101 6298 3626 -1486 -528 1108 C ATOM 2934 C LEU B 612 8.400 -10.230 -5.179 1.00 44.18 C ANISOU 2934 C LEU B 612 5685 6869 4233 -1610 -589 1095 C ATOM 2935 O LEU B 612 7.517 -10.478 -5.999 1.00 47.28 O ANISOU 2935 O LEU B 612 6049 7308 4610 -1686 -653 1152 O ATOM 2936 CB LEU B 612 7.651 -8.752 -3.322 1.00 44.36 C ANISOU 2936 CB LEU B 612 5617 6971 4265 -1400 -507 1210 C ATOM 2937 CG LEU B 612 7.944 -7.610 -2.351 1.00 42.23 C ANISOU 2937 CG LEU B 612 5359 6702 3982 -1276 -428 1196 C ATOM 2938 CD1 LEU B 612 6.824 -7.512 -1.335 1.00 46.07 C ANISOU 2938 CD1 LEU B 612 5750 7266 4488 -1192 -409 1317 C ATOM 2939 CD2 LEU B 612 9.297 -7.807 -1.662 1.00 40.19 C ANISOU 2939 CD2 LEU B 612 5154 6392 3723 -1263 -384 1079 C ATOM 2940 N ILE B 613 9.293 -11.132 -4.794 1.00 46.56 N ANISOU 2940 N ILE B 613 6018 7104 4568 -1632 -565 1020 N ATOM 2941 CA ILE B 613 9.139 -12.535 -5.142 1.00 53.22 C ANISOU 2941 CA ILE B 613 6860 7913 5449 -1737 -602 1011 C ATOM 2942 C ILE B 613 9.136 -13.339 -3.847 1.00 55.56 C ANISOU 2942 C ILE B 613 7094 8205 5814 -1692 -569 1053 C ATOM 2943 O ILE B 613 10.176 -13.535 -3.227 1.00 59.03 O ANISOU 2943 O ILE B 613 7559 8601 6270 -1645 -514 998 O ATOM 2944 CB ILE B 613 10.224 -13.016 -6.121 1.00 51.75 C ANISOU 2944 CB ILE B 613 6781 7638 5245 -1813 -594 888 C ATOM 2945 CG1 ILE B 613 10.163 -12.180 -7.405 1.00 53.49 C ANISOU 2945 CG1 ILE B 613 7056 7880 5390 -1852 -626 860 C ATOM 2946 CG2 ILE B 613 10.041 -14.496 -6.427 1.00 47.06 C ANISOU 2946 CG2 ILE B 613 6196 6988 4697 -1921 -616 871 C ATOM 2947 CD1 ILE B 613 11.034 -12.682 -8.542 1.00 52.32 C ANISOU 2947 CD1 ILE B 613 7011 7658 5209 -1938 -625 747 C ATOM 2948 N PRO B 614 7.945 -13.780 -3.423 1.00 56.60 N ANISOU 2948 N PRO B 614 7130 8393 5981 -1705 -604 1164 N ATOM 2949 CA PRO B 614 7.714 -14.390 -2.107 1.00 55.94 C ANISOU 2949 CA PRO B 614 6965 8331 5959 -1646 -572 1237 C ATOM 2950 C PRO B 614 8.091 -15.866 -2.058 1.00 55.42 C ANISOU 2950 C PRO B 614 6909 8183 5963 -1719 -562 1213 C ATOM 2951 O PRO B 614 8.411 -16.451 -3.094 1.00 54.16 O ANISOU 2951 O PRO B 614 6826 7948 5806 -1825 -583 1137 O ATOM 2952 CB PRO B 614 6.192 -14.264 -1.924 1.00 55.50 C ANISOU 2952 CB PRO B 614 6804 8370 5913 -1647 -618 1376 C ATOM 2953 CG PRO B 614 5.676 -13.502 -3.132 1.00 56.65 C ANISOU 2953 CG PRO B 614 6975 8552 5998 -1699 -672 1378 C ATOM 2954 CD PRO B 614 6.701 -13.666 -4.198 1.00 56.52 C ANISOU 2954 CD PRO B 614 7076 8449 5950 -1776 -677 1242 C ATOM 2955 N ASN B 615 8.051 -16.446 -0.860 1.00 58.52 N ANISOU 2955 N ASN B 615 7231 8592 6414 -1658 -524 1281 N ATOM 2956 CA ASN B 615 8.163 -17.894 -0.671 1.00 62.52 C ANISOU 2956 CA ASN B 615 7724 9023 7008 -1717 -506 1297 C ATOM 2957 C ASN B 615 9.478 -18.530 -1.125 1.00 60.70 C ANISOU 2957 C ASN B 615 7591 8675 6796 -1748 -458 1185 C ATOM 2958 O ASN B 615 9.482 -19.614 -1.704 1.00 61.84 O ANISOU 2958 O ASN B 615 7776 8725 6997 -1847 -457 1157 O ATOM 2959 CB ASN B 615 6.985 -18.602 -1.345 1.00 66.86 C ANISOU 2959 CB ASN B 615 8243 9566 7596 -1846 -573 1350 C ATOM 2960 CG ASN B 615 5.646 -18.074 -0.868 1.00 73.74 C ANISOU 2960 CG ASN B 615 9000 10561 8458 -1811 -616 1484 C ATOM 2961 OD1 ASN B 615 5.407 -17.959 0.335 1.00 75.04 O ANISOU 2961 OD1 ASN B 615 9078 10788 8645 -1705 -579 1575 O ATOM 2962 ND2 ASN B 615 4.765 -17.745 -1.812 1.00 72.42 N ANISOU 2962 ND2 ASN B 615 8824 10439 8252 -1897 -690 1505 N ATOM 2963 N LEU B 616 10.591 -17.866 -0.850 1.00 55.48 N ANISOU 2963 N LEU B 616 6970 8021 6090 -1665 -412 1122 N ATOM 2964 CA LEU B 616 11.896 -18.413 -1.200 1.00 64.42 C ANISOU 2964 CA LEU B 616 8181 9056 7239 -1677 -357 1033 C ATOM 2965 C LEU B 616 12.650 -18.927 0.025 1.00 72.84 C ANISOU 2965 C LEU B 616 9191 10134 8351 -1583 -285 1081 C ATOM 2966 O LEU B 616 12.744 -18.231 1.035 1.00 77.12 O ANISOU 2966 O LEU B 616 9670 10776 8856 -1487 -272 1122 O ATOM 2967 CB LEU B 616 12.741 -17.359 -1.916 1.00 57.27 C ANISOU 2967 CB LEU B 616 7360 8149 6249 -1665 -357 930 C ATOM 2968 CG LEU B 616 12.603 -17.275 -3.432 1.00 61.16 C ANISOU 2968 CG LEU B 616 7945 8587 6704 -1772 -400 850 C ATOM 2969 CD1 LEU B 616 11.277 -17.846 -3.906 1.00 64.34 C ANISOU 2969 CD1 LEU B 616 8321 8993 7132 -1873 -464 900 C ATOM 2970 CD2 LEU B 616 12.779 -15.837 -3.886 1.00 61.77 C ANISOU 2970 CD2 LEU B 616 8058 8719 6694 -1741 -422 808 C ATOM 2971 N PRO B 617 13.189 -20.154 -0.061 1.00 77.40 N ANISOU 2971 N PRO B 617 9790 10610 9007 -1611 -231 1078 N ATOM 2972 CA PRO B 617 14.039 -20.691 1.009 1.00 76.82 C ANISOU 2972 CA PRO B 617 9661 10551 8977 -1518 -154 1134 C ATOM 2973 C PRO B 617 15.400 -20.006 0.984 1.00 73.34 C ANISOU 2973 C PRO B 617 9262 10133 8471 -1461 -119 1059 C ATOM 2974 O PRO B 617 15.644 -19.171 0.114 1.00 73.95 O ANISOU 2974 O PRO B 617 9416 10201 8481 -1496 -151 965 O ATOM 2975 CB PRO B 617 14.206 -22.169 0.625 1.00 76.05 C ANISOU 2975 CB PRO B 617 9597 10310 8987 -1577 -100 1142 C ATOM 2976 CG PRO B 617 13.182 -22.436 -0.442 1.00 77.06 C ANISOU 2976 CG PRO B 617 9782 10370 9129 -1711 -162 1102 C ATOM 2977 CD PRO B 617 12.970 -21.134 -1.138 1.00 77.00 C ANISOU 2977 CD PRO B 617 9816 10431 9010 -1732 -235 1030 C ATOM 2978 N ASN B 618 16.274 -20.346 1.924 1.00 67.94 N ANISOU 2978 N ASN B 618 8519 9488 7806 -1376 -55 1110 N ATOM 2979 CA ASN B 618 17.649 -19.882 1.848 1.00 68.34 C ANISOU 2979 CA ASN B 618 8602 9557 7805 -1335 -18 1048 C ATOM 2980 C ASN B 618 18.283 -20.432 0.581 1.00 74.07 C ANISOU 2980 C ASN B 618 9439 10142 8564 -1399 16 966 C ATOM 2981 O ASN B 618 17.917 -21.515 0.120 1.00 80.28 O ANISOU 2981 O ASN B 618 10258 10813 9432 -1453 41 978 O ATOM 2982 CB ASN B 618 18.433 -20.333 3.073 1.00 69.75 C ANISOU 2982 CB ASN B 618 8684 9814 8003 -1239 46 1138 C ATOM 2983 CG ASN B 618 17.888 -19.746 4.350 1.00 74.39 C ANISOU 2983 CG ASN B 618 9168 10556 8540 -1173 17 1210 C ATOM 2984 OD1 ASN B 618 18.087 -20.292 5.433 1.00 77.84 O ANISOU 2984 OD1 ASN B 618 9507 11069 9001 -1103 59 1313 O ATOM 2985 ND2 ASN B 618 17.187 -18.626 4.231 1.00 72.21 N ANISOU 2985 ND2 ASN B 618 8914 10331 8193 -1191 -46 1160 N ATOM 2986 N GLY B 619 19.218 -19.684 0.006 1.00 70.34 N ANISOU 2986 N GLY B 619 9027 9674 8025 -1399 20 879 N ATOM 2987 CA GLY B 619 19.868 -20.119 -1.217 1.00 70.10 C ANISOU 2987 CA GLY B 619 9104 9519 8011 -1451 57 798 C ATOM 2988 C GLY B 619 20.335 -18.991 -2.117 1.00 65.39 C ANISOU 2988 C GLY B 619 8585 8935 7326 -1480 24 695 C ATOM 2989 O GLY B 619 20.143 -17.813 -1.820 1.00 70.17 O ANISOU 2989 O GLY B 619 9165 9635 7861 -1464 -28 682 O ATOM 2990 N ASP B 620 20.957 -19.365 -3.226 1.00 60.82 N ANISOU 2990 N ASP B 620 8103 8253 6752 -1521 62 623 N ATOM 2991 CA ASP B 620 21.472 -18.397 -4.186 1.00 62.50 C ANISOU 2991 CA ASP B 620 8392 8469 6886 -1549 41 532 C ATOM 2992 C ASP B 620 20.522 -18.281 -5.370 1.00 59.82 C ANISOU 2992 C ASP B 620 8136 8075 6516 -1647 -19 468 C ATOM 2993 O ASP B 620 20.108 -19.291 -5.940 1.00 57.31 O ANISOU 2993 O ASP B 620 7871 7661 6243 -1709 -4 450 O ATOM 2994 CB ASP B 620 22.865 -18.810 -4.663 1.00 63.15 C ANISOU 2994 CB ASP B 620 8522 8492 6980 -1522 128 500 C ATOM 2995 CG ASP B 620 23.916 -18.670 -3.579 1.00 70.76 C ANISOU 2995 CG ASP B 620 9392 9544 7949 -1430 175 566 C ATOM 2996 OD1 ASP B 620 23.545 -18.336 -2.433 1.00 72.46 O ANISOU 2996 OD1 ASP B 620 9512 9863 8157 -1391 142 628 O ATOM 2997 OD2 ASP B 620 25.113 -18.889 -3.873 1.00 77.47 O ANISOU 2997 OD2 ASP B 620 10261 10370 8805 -1397 245 558 O ATOM 2998 N TYR B 621 20.173 -17.050 -5.736 1.00 63.27 N ANISOU 2998 N TYR B 621 8586 8577 6876 -1664 -83 436 N ATOM 2999 CA TYR B 621 19.201 -16.835 -6.807 1.00 57.69 C ANISOU 2999 CA TYR B 621 7938 7851 6129 -1753 -149 396 C ATOM 3000 C TYR B 621 19.702 -15.928 -7.919 1.00 58.92 C ANISOU 3000 C TYR B 621 8172 8009 6206 -1777 -159 322 C ATOM 3001 O TYR B 621 20.342 -14.903 -7.675 1.00 57.90 O ANISOU 3001 O TYR B 621 8027 7933 6041 -1725 -152 317 O ATOM 3002 CB TYR B 621 17.892 -16.289 -6.244 1.00 53.87 C ANISOU 3002 CB TYR B 621 7382 7451 5637 -1754 -223 462 C ATOM 3003 CG TYR B 621 17.224 -17.226 -5.265 1.00 60.06 C ANISOU 3003 CG TYR B 621 8088 8236 6498 -1742 -218 543 C ATOM 3004 CD1 TYR B 621 16.406 -18.256 -5.715 1.00 65.08 C ANISOU 3004 CD1 TYR B 621 8743 8807 7178 -1828 -237 550 C ATOM 3005 CD2 TYR B 621 17.411 -17.086 -3.894 1.00 60.24 C ANISOU 3005 CD2 TYR B 621 8018 8326 6545 -1651 -194 613 C ATOM 3006 CE1 TYR B 621 15.788 -19.120 -4.830 1.00 65.05 C ANISOU 3006 CE1 TYR B 621 8664 8798 7253 -1820 -229 633 C ATOM 3007 CE2 TYR B 621 16.796 -17.949 -2.999 1.00 63.09 C ANISOU 3007 CE2 TYR B 621 8302 8694 6976 -1635 -186 700 C ATOM 3008 CZ TYR B 621 15.987 -18.963 -3.477 1.00 66.79 C ANISOU 3008 CZ TYR B 621 8788 9088 7500 -1717 -201 713 C ATOM 3009 OH TYR B 621 15.365 -19.829 -2.605 1.00 75.17 O ANISOU 3009 OH TYR B 621 9771 10150 8641 -1705 -189 807 O ATOM 3010 N ARG B 622 19.399 -16.317 -9.150 1.00 56.22 N ANISOU 3010 N ARG B 622 7914 7613 5835 -1862 -176 264 N ATOM 3011 CA ARG B 622 19.674 -15.471 -10.292 1.00 59.88 C ANISOU 3011 CA ARG B 622 8446 8089 6214 -1891 -195 206 C ATOM 3012 C ARG B 622 18.419 -14.672 -10.636 1.00 64.09 C ANISOU 3012 C ARG B 622 8956 8701 6697 -1934 -285 238 C ATOM 3013 O ARG B 622 17.399 -15.231 -11.054 1.00 70.34 O ANISOU 3013 O ARG B 622 9752 9491 7482 -2014 -336 245 O ATOM 3014 CB ARG B 622 20.135 -16.304 -11.483 1.00 59.38 C ANISOU 3014 CB ARG B 622 8492 7937 6132 -1956 -155 123 C ATOM 3015 CG ARG B 622 20.611 -15.482 -12.662 1.00 61.54 C ANISOU 3015 CG ARG B 622 8836 8229 6315 -1975 -159 66 C ATOM 3016 CD ARG B 622 21.284 -16.372 -13.685 1.00 65.01 C ANISOU 3016 CD ARG B 622 9387 8577 6737 -2018 -96 -19 C ATOM 3017 NE ARG B 622 20.550 -17.620 -13.866 1.00 73.75 N ANISOU 3017 NE ARG B 622 10531 9615 7876 -2101 -101 -47 N ATOM 3018 CZ ARG B 622 19.545 -17.772 -14.722 1.00 80.22 C ANISOU 3018 CZ ARG B 622 11392 10454 8636 -2212 -172 -83 C ATOM 3019 NH1 ARG B 622 19.153 -16.751 -15.472 1.00 75.97 N ANISOU 3019 NH1 ARG B 622 10855 10009 8000 -2240 -240 -81 N ATOM 3020 NH2 ARG B 622 18.931 -18.945 -14.827 1.00 86.07 N ANISOU 3020 NH2 ARG B 622 12167 11124 9412 -2298 -173 -114 N ATOM 3021 N VAL B 623 18.500 -13.362 -10.427 1.00 51.32 N ANISOU 3021 N VAL B 623 7307 7149 5044 -1880 -301 263 N ATOM 3022 CA VAL B 623 17.415 -12.451 -10.756 1.00 45.19 C ANISOU 3022 CA VAL B 623 6504 6447 4220 -1897 -369 308 C ATOM 3023 C VAL B 623 17.687 -11.860 -12.138 1.00 48.92 C ANISOU 3023 C VAL B 623 7050 6925 4614 -1938 -379 262 C ATOM 3024 O VAL B 623 18.787 -11.389 -12.404 1.00 50.36 O ANISOU 3024 O VAL B 623 7274 7082 4780 -1904 -330 220 O ATOM 3025 CB VAL B 623 17.314 -11.327 -9.708 1.00 42.64 C ANISOU 3025 CB VAL B 623 6112 6181 3911 -1809 -365 363 C ATOM 3026 CG1 VAL B 623 16.218 -10.339 -10.074 1.00 43.14 C ANISOU 3026 CG1 VAL B 623 6148 6312 3933 -1811 -418 423 C ATOM 3027 CG2 VAL B 623 17.061 -11.921 -8.322 1.00 38.53 C ANISOU 3027 CG2 VAL B 623 5514 5670 3456 -1765 -353 412 C ATOM 3028 N GLU B 624 16.691 -11.920 -13.018 1.00 48.48 N ANISOU 3028 N GLU B 624 7004 6911 4506 -2014 -444 278 N ATOM 3029 CA GLU B 624 16.815 -11.397 -14.372 1.00 50.25 C ANISOU 3029 CA GLU B 624 7289 7161 4641 -2057 -460 248 C ATOM 3030 C GLU B 624 15.711 -10.371 -14.633 1.00 49.15 C ANISOU 3030 C GLU B 624 7093 7123 4459 -2053 -523 337 C ATOM 3031 O GLU B 624 14.528 -10.664 -14.438 1.00 47.89 O ANISOU 3031 O GLU B 624 6874 7019 4305 -2091 -583 399 O ATOM 3032 CB GLU B 624 16.710 -12.536 -15.388 1.00 59.04 C ANISOU 3032 CB GLU B 624 8477 8243 5712 -2167 -476 176 C ATOM 3033 CG GLU B 624 17.784 -12.528 -16.462 1.00 75.06 C ANISOU 3033 CG GLU B 624 10606 10233 7680 -2182 -427 91 C ATOM 3034 CD GLU B 624 19.008 -13.336 -16.073 1.00 86.25 C ANISOU 3034 CD GLU B 624 12072 11542 9157 -2145 -336 24 C ATOM 3035 OE1 GLU B 624 19.979 -13.362 -16.859 1.00 91.59 O ANISOU 3035 OE1 GLU B 624 12826 12181 9792 -2143 -282 -39 O ATOM 3036 OE2 GLU B 624 18.997 -13.951 -14.986 1.00 88.67 O ANISOU 3036 OE2 GLU B 624 12334 11806 9551 -2114 -314 46 O ATOM 3037 N PHE B 625 16.102 -9.173 -15.061 1.00 43.44 N ANISOU 3037 N PHE B 625 6382 6424 3698 -2004 -502 354 N ATOM 3038 CA PHE B 625 15.147 -8.128 -15.423 1.00 45.87 C ANISOU 3038 CA PHE B 625 6640 6823 3966 -1987 -545 450 C ATOM 3039 C PHE B 625 14.960 -8.080 -16.941 1.00 51.30 C ANISOU 3039 C PHE B 625 7371 7570 4551 -2063 -584 443 C ATOM 3040 O PHE B 625 15.929 -8.172 -17.690 1.00 52.52 O ANISOU 3040 O PHE B 625 7604 7686 4666 -2080 -547 367 O ATOM 3041 CB PHE B 625 15.627 -6.763 -14.914 1.00 50.42 C ANISOU 3041 CB PHE B 625 7201 7382 4572 -1883 -489 483 C ATOM 3042 CG PHE B 625 15.748 -6.685 -13.418 1.00 51.25 C ANISOU 3042 CG PHE B 625 7262 7450 4759 -1812 -454 490 C ATOM 3043 CD1 PHE B 625 16.887 -7.156 -12.771 1.00 46.42 C ANISOU 3043 CD1 PHE B 625 6679 6769 4189 -1795 -404 412 C ATOM 3044 CD2 PHE B 625 14.722 -6.153 -12.655 1.00 49.87 C ANISOU 3044 CD2 PHE B 625 7014 7322 4614 -1760 -468 580 C ATOM 3045 CE1 PHE B 625 17.000 -7.094 -11.395 1.00 45.68 C ANISOU 3045 CE1 PHE B 625 6539 6662 4156 -1735 -376 420 C ATOM 3046 CE2 PHE B 625 14.831 -6.085 -11.274 1.00 46.11 C ANISOU 3046 CE2 PHE B 625 6501 6821 4200 -1696 -434 581 C ATOM 3047 CZ PHE B 625 15.972 -6.556 -10.644 1.00 43.08 C ANISOU 3047 CZ PHE B 625 6144 6378 3847 -1687 -392 499 C ATOM 3048 N SER B 626 13.717 -7.931 -17.388 1.00 45.58 N ANISOU 3048 N SER B 626 6590 6950 3779 -2105 -656 529 N ATOM 3049 CA SER B 626 13.422 -7.901 -18.815 1.00 51.41 C ANISOU 3049 CA SER B 626 7355 7775 4403 -2185 -704 534 C ATOM 3050 C SER B 626 12.254 -6.978 -19.104 1.00 49.55 C ANISOU 3050 C SER B 626 7028 7669 4129 -2164 -754 681 C ATOM 3051 O SER B 626 11.603 -6.486 -18.184 1.00 52.60 O ANISOU 3051 O SER B 626 7335 8069 4582 -2092 -751 773 O ATOM 3052 CB SER B 626 13.100 -9.305 -19.327 1.00 57.85 C ANISOU 3052 CB SER B 626 8210 8597 5173 -2322 -758 457 C ATOM 3053 OG SER B 626 11.985 -9.848 -18.637 1.00 55.08 O ANISOU 3053 OG SER B 626 7779 8282 4866 -2359 -816 516 O ATOM 3054 N ASN B 627 12.007 -6.742 -20.390 1.00 51.87 N ANISOU 3054 N ASN B 627 7332 8063 4312 -2221 -795 708 N ATOM 3055 CA ASN B 627 10.908 -5.896 -20.829 1.00 52.92 C ANISOU 3055 CA ASN B 627 7371 8340 4395 -2204 -843 864 C ATOM 3056 C ASN B 627 11.064 -4.449 -20.352 1.00 54.71 C ANISOU 3056 C ASN B 627 7562 8538 4686 -2055 -768 963 C ATOM 3057 O ASN B 627 10.095 -3.800 -19.945 1.00 50.76 O ANISOU 3057 O ASN B 627 6968 8103 4216 -1994 -777 1101 O ATOM 3058 CB ASN B 627 9.576 -6.482 -20.363 1.00 63.91 C ANISOU 3058 CB ASN B 627 8668 9815 5801 -2260 -923 941 C ATOM 3059 CG ASN B 627 8.425 -6.104 -21.269 1.00 74.72 C ANISOU 3059 CG ASN B 627 9948 11373 7070 -2308 -1004 1079 C ATOM 3060 OD1 ASN B 627 8.627 -5.563 -22.361 1.00 79.20 O ANISOU 3060 OD1 ASN B 627 10534 12017 7542 -2317 -1008 1104 O ATOM 3061 ND2 ASN B 627 7.207 -6.392 -20.825 1.00 76.61 N ANISOU 3061 ND2 ASN B 627 10081 11701 7327 -2339 -1068 1180 N ATOM 3062 N LEU B 628 12.294 -3.948 -20.395 1.00 49.79 N ANISOU 3062 N LEU B 628 6772 8101 4045 14 459 531 N ATOM 3063 CA LEU B 628 12.536 -2.542 -20.125 1.00 49.65 C ANISOU 3063 CA LEU B 628 6735 8017 4114 -15 355 510 C ATOM 3064 C LEU B 628 11.721 -1.725 -21.112 1.00 44.08 C ANISOU 3064 C LEU B 628 6166 7195 3389 8 267 485 C ATOM 3065 O LEU B 628 11.534 -2.144 -22.252 1.00 42.27 O ANISOU 3065 O LEU B 628 6056 6914 3091 22 321 541 O ATOM 3066 CB LEU B 628 14.018 -2.209 -20.282 1.00 46.97 C ANISOU 3066 CB LEU B 628 6367 7642 3838 -75 434 634 C ATOM 3067 CG LEU B 628 14.983 -3.019 -19.418 1.00 46.83 C ANISOU 3067 CG LEU B 628 6215 7736 3844 -99 531 684 C ATOM 3068 CD1 LEU B 628 16.329 -2.313 -19.343 1.00 49.92 C ANISOU 3068 CD1 LEU B 628 6554 8089 4326 -164 558 779 C ATOM 3069 CD2 LEU B 628 14.406 -3.261 -18.025 1.00 42.18 C ANISOU 3069 CD2 LEU B 628 5506 7261 3260 -78 461 564 C ATOM 3070 N PRO B 629 11.224 -0.561 -20.670 1.00 41.30 N ANISOU 3070 N PRO B 629 5798 6800 3095 12 132 401 N ATOM 3071 CA PRO B 629 10.434 0.367 -21.495 1.00 35.82 C ANISOU 3071 CA PRO B 629 5221 5993 2395 37 34 373 C ATOM 3072 C PRO B 629 11.255 0.880 -22.669 1.00 38.65 C ANISOU 3072 C PRO B 629 5689 6234 2763 3 87 498 C ATOM 3073 O PRO B 629 12.459 1.085 -22.525 1.00 39.26 O ANISOU 3073 O PRO B 629 5721 6301 2896 -50 153 579 O ATOM 3074 CB PRO B 629 10.142 1.528 -20.539 1.00 41.12 C ANISOU 3074 CB PRO B 629 5825 6650 3150 35 -94 276 C ATOM 3075 CG PRO B 629 10.349 0.949 -19.149 1.00 45.83 C ANISOU 3075 CG PRO B 629 6272 7377 3766 26 -77 219 C ATOM 3076 CD PRO B 629 11.441 -0.053 -19.306 1.00 37.38 C ANISOU 3076 CD PRO B 629 5169 6361 2673 -8 69 330 C ATOM 3077 N GLN B 630 10.615 1.070 -23.817 1.00 38.57 N ANISOU 3077 N GLN B 630 5819 6139 2697 33 60 514 N ATOM 3078 CA GLN B 630 11.317 1.554 -24.996 1.00 42.83 C ANISOU 3078 CA GLN B 630 6476 6561 3235 6 112 632 C ATOM 3079 C GLN B 630 12.183 2.786 -24.692 1.00 47.01 C ANISOU 3079 C GLN B 630 6969 7020 3873 -44 81 664 C ATOM 3080 O GLN B 630 11.783 3.677 -23.932 1.00 45.17 O ANISOU 3080 O GLN B 630 6681 6778 3704 -40 -33 574 O ATOM 3081 CB GLN B 630 10.327 1.834 -26.137 1.00 39.51 C ANISOU 3081 CB GLN B 630 6210 6054 2747 50 47 623 C ATOM 3082 CG GLN B 630 9.062 2.573 -25.713 1.00 37.86 C ANISOU 3082 CG GLN B 630 5990 5836 2558 97 -114 496 C ATOM 3083 CD GLN B 630 8.143 2.886 -26.885 1.00 41.80 C ANISOU 3083 CD GLN B 630 6640 6249 2993 140 -181 500 C ATOM 3084 OE1 GLN B 630 8.026 2.104 -27.840 1.00 36.82 O ANISOU 3084 OE1 GLN B 630 6109 5612 2269 149 -118 555 O ATOM 3085 NE2 GLN B 630 7.485 4.037 -26.817 1.00 40.11 N ANISOU 3085 NE2 GLN B 630 6446 5968 2827 167 -311 441 N ATOM 3086 N GLY B 631 13.383 2.812 -25.265 1.00 43.22 N ANISOU 3086 N GLY B 631 6517 6490 3415 -91 189 792 N ATOM 3087 CA GLY B 631 14.261 3.964 -25.146 1.00 43.52 C ANISOU 3087 CA GLY B 631 6533 6447 3554 -145 171 837 C ATOM 3088 C GLY B 631 15.094 3.997 -23.875 1.00 47.07 C ANISOU 3088 C GLY B 631 6816 6978 4089 -196 181 823 C ATOM 3089 O GLY B 631 15.908 4.901 -23.686 1.00 58.03 O ANISOU 3089 O GLY B 631 8171 8310 5567 -251 169 861 O ATOM 3090 N TYR B 632 14.893 3.022 -22.994 1.00 37.03 N ANISOU 3090 N TYR B 632 5440 5840 2789 -179 202 768 N ATOM 3091 CA TYR B 632 15.659 2.977 -21.751 1.00 45.85 C ANISOU 3091 CA TYR B 632 6398 7046 3978 -224 209 754 C ATOM 3092 C TYR B 632 16.924 2.127 -21.836 1.00 48.30 C ANISOU 3092 C TYR B 632 6648 7407 4295 -264 360 881 C ATOM 3093 O TYR B 632 16.982 1.117 -22.546 1.00 44.55 O ANISOU 3093 O TYR B 632 6229 6950 3747 -239 471 948 O ATOM 3094 CB TYR B 632 14.784 2.546 -20.565 1.00 45.09 C ANISOU 3094 CB TYR B 632 6207 7065 3860 -187 135 619 C ATOM 3095 CG TYR B 632 14.055 3.711 -19.939 1.00 54.93 C ANISOU 3095 CG TYR B 632 7443 8271 5157 -179 -17 499 C ATOM 3096 CD1 TYR B 632 12.898 4.220 -20.515 1.00 60.50 C ANISOU 3096 CD1 TYR B 632 8255 8902 5830 -126 -105 436 C ATOM 3097 CD2 TYR B 632 14.535 4.318 -18.784 1.00 55.24 C ANISOU 3097 CD2 TYR B 632 7369 8343 5275 -223 -73 451 C ATOM 3098 CE1 TYR B 632 12.231 5.292 -19.955 1.00 64.53 C ANISOU 3098 CE1 TYR B 632 8758 9370 6389 -113 -236 330 C ATOM 3099 CE2 TYR B 632 13.875 5.394 -18.216 1.00 56.51 C ANISOU 3099 CE2 TYR B 632 7530 8459 5480 -215 -205 340 C ATOM 3100 CZ TYR B 632 12.724 5.877 -18.805 1.00 63.52 C ANISOU 3100 CZ TYR B 632 8524 9271 6339 -157 -283 281 C ATOM 3101 OH TYR B 632 12.061 6.949 -18.248 1.00 66.19 O ANISOU 3101 OH TYR B 632 8864 9562 6725 -143 -408 173 O ATOM 3102 N GLU B 633 17.931 2.558 -21.086 1.00 48.65 N ANISOU 3102 N GLU B 633 6579 7474 4431 -326 362 910 N ATOM 3103 CA GLU B 633 19.241 1.935 -21.073 1.00 50.51 C ANISOU 3103 CA GLU B 633 6738 7755 4697 -369 495 1036 C ATOM 3104 C GLU B 633 19.560 1.588 -19.634 1.00 48.02 C ANISOU 3104 C GLU B 633 6254 7573 4420 -390 470 985 C ATOM 3105 O GLU B 633 19.167 2.310 -18.725 1.00 40.96 O ANISOU 3105 O GLU B 633 5305 6694 3565 -401 345 877 O ATOM 3106 CB GLU B 633 20.289 2.926 -21.581 1.00 57.90 C ANISOU 3106 CB GLU B 633 7692 8583 5723 -436 515 1136 C ATOM 3107 CG GLU B 633 21.352 2.317 -22.475 1.00 70.04 C ANISOU 3107 CG GLU B 633 9256 10097 7259 -456 682 1300 C ATOM 3108 CD GLU B 633 20.816 1.962 -23.848 1.00 73.66 C ANISOU 3108 CD GLU B 633 9889 10474 7624 -406 746 1344 C ATOM 3109 OE1 GLU B 633 20.260 0.852 -24.000 1.00 70.27 O ANISOU 3109 OE1 GLU B 633 9489 10109 7101 -353 799 1326 O ATOM 3110 OE2 GLU B 633 20.955 2.795 -24.773 1.00 77.30 O ANISOU 3110 OE2 GLU B 633 10461 10807 8105 -422 742 1396 O ATOM 3111 N VAL B 634 20.278 0.487 -19.437 1.00 49.92 N ANISOU 3111 N VAL B 634 6416 7906 4644 -393 591 1065 N ATOM 3112 CA VAL B 634 20.703 0.055 -18.115 1.00 51.71 C ANISOU 3112 CA VAL B 634 6480 8265 4903 -412 582 1036 C ATOM 3113 C VAL B 634 21.864 0.911 -17.603 1.00 53.75 C ANISOU 3113 C VAL B 634 6639 8510 5275 -496 554 1088 C ATOM 3114 O VAL B 634 22.826 1.180 -18.329 1.00 49.92 O ANISOU 3114 O VAL B 634 6172 7955 4841 -539 631 1212 O ATOM 3115 CB VAL B 634 21.108 -1.431 -18.136 1.00 58.08 C ANISOU 3115 CB VAL B 634 7241 9170 5656 -384 729 1116 C ATOM 3116 CG1 VAL B 634 21.459 -1.909 -16.747 1.00 57.27 C ANISOU 3116 CG1 VAL B 634 6973 9209 5576 -396 714 1083 C ATOM 3117 CG2 VAL B 634 19.979 -2.273 -18.721 1.00 58.10 C ANISOU 3117 CG2 VAL B 634 7352 9177 5546 -309 760 1068 C ATOM 3118 N THR B 635 21.756 1.347 -16.351 1.00 36.05 N ANISOU 3118 N THR B 635 4294 6333 3072 -520 443 990 N ATOM 3119 CA THR B 635 22.767 2.194 -15.734 1.00 37.32 C ANISOU 3119 CA THR B 635 4355 6489 3338 -605 395 1018 C ATOM 3120 C THR B 635 23.962 1.345 -15.286 1.00 38.56 C ANISOU 3120 C THR B 635 4374 6753 3525 -637 498 1130 C ATOM 3121 O THR B 635 23.847 0.122 -15.181 1.00 40.08 O ANISOU 3121 O THR B 635 4538 7039 3653 -586 586 1153 O ATOM 3122 CB THR B 635 22.168 2.920 -14.510 1.00 40.05 C ANISOU 3122 CB THR B 635 4647 6869 3702 -617 238 865 C ATOM 3123 OG1 THR B 635 22.782 4.204 -14.343 1.00 39.22 O ANISOU 3123 OG1 THR B 635 4524 6684 3695 -698 160 868 O ATOM 3124 CG2 THR B 635 22.333 2.078 -13.234 1.00 39.57 C ANISOU 3124 CG2 THR B 635 4444 6969 3620 -611 238 829 C ATOM 3125 N PRO B 636 25.115 1.990 -15.022 1.00 46.43 N ANISOU 3125 N PRO B 636 5283 7734 4623 -721 489 1201 N ATOM 3126 CA PRO B 636 26.310 1.292 -14.518 1.00 49.48 C ANISOU 3126 CA PRO B 636 5521 8226 5053 -757 573 1310 C ATOM 3127 C PRO B 636 26.026 0.398 -13.309 1.00 46.38 C ANISOU 3127 C PRO B 636 5021 7991 4609 -722 552 1242 C ATOM 3128 O PRO B 636 25.355 0.822 -12.368 1.00 43.71 O ANISOU 3128 O PRO B 636 4661 7690 4258 -721 424 1105 O ATOM 3129 CB PRO B 636 27.233 2.442 -14.114 1.00 52.93 C ANISOU 3129 CB PRO B 636 5881 8623 5607 -859 496 1333 C ATOM 3130 CG PRO B 636 26.874 3.538 -15.066 1.00 54.94 C ANISOU 3130 CG PRO B 636 6276 8713 5885 -873 457 1318 C ATOM 3131 CD PRO B 636 25.384 3.421 -15.276 1.00 52.30 C ANISOU 3131 CD PRO B 636 6066 8354 5450 -788 405 1193 C ATOM 3132 N SER B 637 26.552 -0.823 -13.340 1.00 42.36 N ANISOU 3132 N SER B 637 4449 7572 4074 -693 683 1341 N ATOM 3133 CA SER B 637 26.283 -1.813 -12.308 1.00 48.97 C ANISOU 3133 CA SER B 637 5194 8558 4855 -650 686 1292 C ATOM 3134 C SER B 637 27.209 -1.703 -11.100 1.00 50.85 C ANISOU 3134 C SER B 637 5260 8902 5160 -711 635 1312 C ATOM 3135 O SER B 637 28.331 -1.199 -11.205 1.00 54.05 O ANISOU 3135 O SER B 637 5596 9282 5658 -785 647 1411 O ATOM 3136 CB SER B 637 26.366 -3.216 -12.902 1.00 51.90 C ANISOU 3136 CB SER B 637 5585 8973 5162 -584 854 1387 C ATOM 3137 OG SER B 637 25.212 -3.493 -13.674 1.00 58.25 O ANISOU 3137 OG SER B 637 6539 9716 5878 -518 872 1324 O ATOM 3138 N LYS B 638 26.716 -2.176 -9.959 1.00 46.48 N ANISOU 3138 N LYS B 638 4639 8466 4555 -681 577 1217 N ATOM 3139 CA LYS B 638 27.489 -2.250 -8.716 1.00 62.60 C ANISOU 3139 CA LYS B 638 6518 10629 6638 -728 528 1227 C ATOM 3140 C LYS B 638 28.415 -1.054 -8.458 1.00 67.84 C ANISOU 3140 C LYS B 638 7115 11249 7412 -835 438 1255 C ATOM 3141 O LYS B 638 29.607 -1.228 -8.190 1.00 70.12 O ANISOU 3141 O LYS B 638 7278 11597 7768 -886 476 1369 O ATOM 3142 CB LYS B 638 28.300 -3.550 -8.663 1.00 69.42 C ANISOU 3142 CB LYS B 638 7282 11599 7493 -699 673 1364 C ATOM 3143 CG LYS B 638 27.477 -4.815 -8.840 1.00 81.10 C ANISOU 3143 CG LYS B 638 8818 13130 8866 -599 770 1344 C ATOM 3144 CD LYS B 638 28.294 -6.040 -8.469 1.00 90.69 C ANISOU 3144 CD LYS B 638 9914 14468 10076 -574 892 1463 C ATOM 3145 CE LYS B 638 28.814 -5.928 -7.041 1.00 97.27 C ANISOU 3145 CE LYS B 638 10590 15427 10940 -615 796 1438 C ATOM 3146 NZ LYS B 638 29.687 -7.073 -6.654 1.00100.91 N ANISOU 3146 NZ LYS B 638 10926 16011 11406 -592 910 1565 N ATOM 3147 N GLN B 639 27.870 0.156 -8.534 1.00 63.97 N ANISOU 3147 N GLN B 639 6707 10656 6943 -868 319 1151 N ATOM 3148 CA GLN B 639 28.638 1.347 -8.184 1.00 58.49 C ANISOU 3148 CA GLN B 639 5957 9917 6350 -973 219 1154 C ATOM 3149 C GLN B 639 28.602 1.536 -6.674 1.00 56.45 C ANISOU 3149 C GLN B 639 5597 9768 6084 -1006 91 1050 C ATOM 3150 O GLN B 639 27.732 0.995 -5.997 1.00 50.25 O ANISOU 3150 O GLN B 639 4821 9060 5213 -941 62 948 O ATOM 3151 CB GLN B 639 28.079 2.580 -8.888 1.00 47.73 C ANISOU 3151 CB GLN B 639 4730 8392 5013 -995 149 1087 C ATOM 3152 CG GLN B 639 28.143 2.496 -10.404 1.00 52.80 C ANISOU 3152 CG GLN B 639 5482 8919 5662 -969 267 1191 C ATOM 3153 CD GLN B 639 29.570 2.436 -10.914 1.00 59.69 C ANISOU 3153 CD GLN B 639 6275 9779 6625 -1032 366 1368 C ATOM 3154 OE1 GLN B 639 30.092 1.359 -11.220 1.00 55.69 O ANISOU 3154 OE1 GLN B 639 5720 9337 6103 -998 502 1485 O ATOM 3155 NE2 GLN B 639 30.212 3.598 -11.006 1.00 61.97 N ANISOU 3155 NE2 GLN B 639 6551 9982 7013 -1125 303 1389 N ATOM 3156 N GLY B 640 29.551 2.296 -6.148 1.00 62.49 N ANISOU 3156 N GLY B 640 6268 10538 6937 -1107 15 1078 N ATOM 3157 CA GLY B 640 29.644 2.481 -4.714 1.00 65.04 C ANISOU 3157 CA GLY B 640 6493 10967 7253 -1147 -107 989 C ATOM 3158 C GLY B 640 30.013 1.183 -4.017 1.00 64.25 C ANISOU 3158 C GLY B 640 6270 11033 7106 -1106 -41 1049 C ATOM 3159 O GLY B 640 30.337 0.186 -4.666 1.00 65.51 O ANISOU 3159 O GLY B 640 6413 11223 7255 -1055 103 1171 O ATOM 3160 N ASN B 641 29.979 1.199 -2.689 1.00 53.18 N ANISOU 3160 N ASN B 641 4788 9739 5677 -1127 -146 964 N ATOM 3161 CA ASN B 641 30.336 0.024 -1.909 1.00 59.86 C ANISOU 3161 CA ASN B 641 5515 10750 6478 -1090 -97 1016 C ATOM 3162 C ASN B 641 29.142 -0.412 -1.088 1.00 57.76 C ANISOU 3162 C ASN B 641 5294 10552 6100 -1011 -143 868 C ATOM 3163 O ASN B 641 29.276 -1.109 -0.083 1.00 68.56 O ANISOU 3163 O ASN B 641 6569 12058 7421 -992 -155 861 O ATOM 3164 CB ASN B 641 31.545 0.309 -1.012 1.00 68.30 C ANISOU 3164 CB ASN B 641 6427 11906 7616 -1188 -172 1073 C ATOM 3165 CG ASN B 641 32.827 0.531 -1.811 1.00 79.21 C ANISOU 3165 CG ASN B 641 7741 13242 9115 -1259 -104 1245 C ATOM 3166 OD1 ASN B 641 33.269 -0.346 -2.554 1.00 78.01 O ANISOU 3166 OD1 ASN B 641 7561 13104 8973 -1214 46 1384 O ATOM 3167 ND2 ASN B 641 33.426 1.709 -1.659 1.00 82.75 N ANISOU 3167 ND2 ASN B 641 8160 13628 9651 -1372 -210 1234 N ATOM 3168 N ASN B 643 27.964 0.018 -1.525 1.00 53.72 N ANISOU 3168 N ASN B 643 4925 9940 5547 -966 -169 752 N ATOM 3169 CA ASN B 643 26.726 -0.343 -0.854 1.00 50.57 C ANISOU 3169 CA ASN B 643 4578 9589 5046 -887 -206 608 C ATOM 3170 C ASN B 643 25.824 -1.140 -1.791 1.00 53.43 C ANISOU 3170 C ASN B 643 5041 9913 5346 -785 -90 614 C ATOM 3171 O ASN B 643 25.177 -0.577 -2.680 1.00 48.72 O ANISOU 3171 O ASN B 643 4565 9189 4756 -770 -93 575 O ATOM 3172 CB ASN B 643 26.011 0.902 -0.329 1.00 48.77 C ANISOU 3172 CB ASN B 643 4423 9287 4819 -921 -358 443 C ATOM 3173 CG ASN B 643 24.841 0.561 0.579 1.00 60.40 C ANISOU 3173 CG ASN B 643 5928 10826 6194 -848 -404 294 C ATOM 3174 OD1 ASN B 643 24.178 1.449 1.109 1.00 70.65 O ANISOU 3174 OD1 ASN B 643 7285 12077 7482 -862 -518 154 O ATOM 3175 ND2 ASN B 643 24.586 -0.731 0.765 1.00 55.22 N ANISOU 3175 ND2 ASN B 643 5238 10277 5468 -769 -310 326 N ATOM 3176 N GLU B 644 25.788 -2.453 -1.588 1.00 54.14 N ANISOU 3176 N GLU B 644 5082 10113 5376 -717 11 665 N ATOM 3177 CA GLU B 644 24.983 -3.333 -2.428 1.00 58.15 C ANISOU 3177 CA GLU B 644 5678 10596 5820 -625 126 675 C ATOM 3178 C GLU B 644 23.483 -3.198 -2.177 1.00 43.24 C ANISOU 3178 C GLU B 644 3889 8683 3858 -561 66 509 C ATOM 3179 O GLU B 644 22.685 -3.848 -2.835 1.00 46.31 O ANISOU 3179 O GLU B 644 4357 9047 4192 -488 144 498 O ATOM 3180 CB GLU B 644 25.434 -4.788 -2.290 1.00 64.81 C ANISOU 3180 CB GLU B 644 6440 11560 6626 -574 260 783 C ATOM 3181 CG GLU B 644 26.740 -5.075 -3.022 1.00 73.90 C ANISOU 3181 CG GLU B 644 7529 12702 7848 -612 367 969 C ATOM 3182 CD GLU B 644 27.176 -6.525 -2.918 1.00 87.42 C ANISOU 3182 CD GLU B 644 9165 14526 9523 -555 508 1079 C ATOM 3183 OE1 GLU B 644 26.624 -7.263 -2.070 1.00 90.32 O ANISOU 3183 OE1 GLU B 644 9506 14997 9817 -499 507 1015 O ATOM 3184 OE2 GLU B 644 28.081 -6.924 -3.684 1.00 94.34 O ANISOU 3184 OE2 GLU B 644 10012 15386 10448 -564 625 1234 O ATOM 3185 N GLU B 645 23.093 -2.347 -1.237 1.00 42.40 N ANISOU 3185 N GLU B 645 3780 8580 3750 -590 -73 378 N ATOM 3186 CA GLU B 645 21.670 -2.062 -1.065 1.00 45.87 C ANISOU 3186 CA GLU B 645 4316 8978 4133 -532 -133 221 C ATOM 3187 C GLU B 645 21.237 -0.846 -1.886 1.00 39.69 C ANISOU 3187 C GLU B 645 3647 8036 3398 -557 -198 172 C ATOM 3188 O GLU B 645 20.056 -0.654 -2.139 1.00 39.26 O ANISOU 3188 O GLU B 645 3688 7924 3306 -501 -224 71 O ATOM 3189 CB GLU B 645 21.316 -1.858 0.410 1.00 56.86 C ANISOU 3189 CB GLU B 645 5660 10457 5487 -534 -238 95 C ATOM 3190 CG GLU B 645 21.374 -3.123 1.253 1.00 77.07 C ANISOU 3190 CG GLU B 645 8133 13172 7979 -485 -175 115 C ATOM 3191 CD GLU B 645 21.206 -2.839 2.742 1.00 95.72 C ANISOU 3191 CD GLU B 645 10444 15621 10306 -499 -282 3 C ATOM 3192 OE1 GLU B 645 21.081 -3.806 3.526 1.00101.85 O ANISOU 3192 OE1 GLU B 645 11161 16520 11017 -452 -242 -2 O ATOM 3193 OE2 GLU B 645 21.202 -1.650 3.132 1.00 99.62 O ANISOU 3193 OE2 GLU B 645 10960 16055 10834 -559 -405 -80 O ATOM 3194 N LEU B 646 22.187 -0.027 -2.318 1.00 35.44 N ANISOU 3194 N LEU B 646 3746 6950 2769 -726 -241 580 N ATOM 3195 CA LEU B 646 21.813 1.216 -2.984 1.00 35.62 C ANISOU 3195 CA LEU B 646 3721 6968 2845 -885 -178 623 C ATOM 3196 C LEU B 646 22.262 1.304 -4.451 1.00 41.83 C ANISOU 3196 C LEU B 646 4479 7855 3562 -886 -197 583 C ATOM 3197 O LEU B 646 22.062 2.330 -5.103 1.00 39.54 O ANISOU 3197 O LEU B 646 4145 7579 3300 -1011 -144 615 O ATOM 3198 CB LEU B 646 22.312 2.412 -2.175 1.00 42.04 C ANISOU 3198 CB LEU B 646 4433 7889 3651 -987 -78 609 C ATOM 3199 CG LEU B 646 21.625 2.553 -0.815 1.00 47.78 C ANISOU 3199 CG LEU B 646 5188 8494 4472 -1024 -48 667 C ATOM 3200 CD1 LEU B 646 22.254 3.663 0.011 1.00 54.14 C ANISOU 3200 CD1 LEU B 646 5886 9429 5257 -1113 51 634 C ATOM 3201 CD2 LEU B 646 20.144 2.807 -1.014 1.00 49.45 C ANISOU 3201 CD2 LEU B 646 5473 8479 4836 -1121 -49 777 C ATOM 3202 N ASP B 647 22.849 0.222 -4.960 1.00 36.08 N ANISOU 3202 N ASP B 647 3775 7191 2742 -748 -271 515 N ATOM 3203 CA ASP B 647 23.349 0.170 -6.334 1.00 42.71 C ANISOU 3203 CA ASP B 647 4588 8137 3503 -733 -296 466 C ATOM 3204 C ASP B 647 22.355 -0.493 -7.299 1.00 38.82 C ANISOU 3204 C ASP B 647 4187 7490 3073 -715 -368 515 C ATOM 3205 O ASP B 647 21.224 -0.813 -6.924 1.00 35.93 O ANISOU 3205 O ASP B 647 3903 6928 2821 -728 -392 591 O ATOM 3206 CB ASP B 647 24.677 -0.591 -6.375 1.00 41.60 C ANISOU 3206 CB ASP B 647 4408 8178 3218 -592 -331 349 C ATOM 3207 CG ASP B 647 24.500 -2.084 -6.107 1.00 50.65 C ANISOU 3207 CG ASP B 647 5645 9234 4363 -434 -422 333 C ATOM 3208 OD1 ASP B 647 23.353 -2.515 -5.859 1.00 39.85 O ANISOU 3208 OD1 ASP B 647 4371 7664 3107 -438 -454 412 O ATOM 3209 OD2 ASP B 647 25.502 -2.829 -6.155 1.00 53.34 O ANISOU 3209 OD2 ASP B 647 5966 9706 4596 -306 -460 242 O ATOM 3210 N SER B 648 22.799 -0.701 -8.536 1.00 37.00 N ANISOU 3210 N SER B 648 3940 7354 2765 -686 -400 465 N ATOM 3211 CA SER B 648 22.052 -1.453 -9.535 1.00 36.36 C ANISOU 3211 CA SER B 648 3936 7163 2718 -650 -475 487 C ATOM 3212 C SER B 648 22.751 -2.784 -9.766 1.00 41.38 C ANISOU 3212 C SER B 648 4597 7861 3264 -483 -552 395 C ATOM 3213 O SER B 648 23.972 -2.827 -9.887 1.00 43.85 O ANISOU 3213 O SER B 648 4842 8363 3456 -426 -544 304 O ATOM 3214 CB SER B 648 22.004 -0.669 -10.843 1.00 37.37 C ANISOU 3214 CB SER B 648 4022 7353 2823 -745 -454 501 C ATOM 3215 OG SER B 648 21.375 -1.415 -11.876 1.00 37.21 O ANISOU 3215 OG SER B 648 4068 7251 2821 -705 -529 510 O ATOM 3216 N ASN B 649 21.985 -3.870 -9.819 1.00 37.87 N ANISOU 3216 N ASN B 649 4249 7259 2881 -406 -624 415 N ATOM 3217 CA ASN B 649 22.562 -5.200 -10.016 1.00 42.98 C ANISOU 3217 CA ASN B 649 4929 7945 3457 -244 -697 332 C ATOM 3218 C ASN B 649 22.893 -5.510 -11.474 1.00 44.90 C ANISOU 3218 C ASN B 649 5156 8277 3627 -216 -740 271 C ATOM 3219 O ASN B 649 23.703 -6.395 -11.760 1.00 57.12 O ANISOU 3219 O ASN B 649 6698 9917 5086 -91 -786 180 O ATOM 3220 CB ASN B 649 21.628 -6.289 -9.482 1.00 41.02 C ANISOU 3220 CB ASN B 649 4792 7487 3306 -168 -753 372 C ATOM 3221 CG ASN B 649 21.730 -6.461 -7.984 1.00 42.33 C ANISOU 3221 CG ASN B 649 4977 7611 3498 -125 -730 392 C ATOM 3222 OD1 ASN B 649 21.724 -5.487 -7.234 1.00 43.17 O ANISOU 3222 OD1 ASN B 649 5038 7739 3627 -217 -663 433 O ATOM 3223 ND2 ASN B 649 21.818 -7.708 -7.538 1.00 44.61 N ANISOU 3223 ND2 ASN B 649 5330 7838 3781 17 -785 363 N ATOM 3224 N GLY B 650 22.261 -4.793 -12.397 1.00 34.97 N ANISOU 3224 N GLY B 650 3890 6990 2406 -331 -725 322 N ATOM 3225 CA GLY B 650 22.337 -5.172 -13.795 1.00 32.98 C ANISOU 3225 CA GLY B 650 3639 6792 2101 -307 -773 278 C ATOM 3226 C GLY B 650 21.239 -6.182 -14.088 1.00 49.67 C ANISOU 3226 C GLY B 650 5853 8714 4304 -258 -846 306 C ATOM 3227 O GLY B 650 20.678 -6.797 -13.169 1.00 45.79 O ANISOU 3227 O GLY B 650 5431 8072 3894 -211 -864 338 O ATOM 3228 N VAL B 651 20.931 -6.366 -15.367 1.00 46.01 N ANISOU 3228 N VAL B 651 5399 8259 3825 -270 -885 292 N ATOM 3229 CA VAL B 651 19.788 -7.189 -15.763 1.00 45.58 C ANISOU 3229 CA VAL B 651 5432 8024 3862 -246 -949 321 C ATOM 3230 C VAL B 651 19.891 -8.639 -15.286 1.00 45.11 C ANISOU 3230 C VAL B 651 5439 7889 3814 -95 -1008 263 C ATOM 3231 O VAL B 651 18.900 -9.370 -15.290 1.00 44.63 O ANISOU 3231 O VAL B 651 5459 7650 3848 -71 -1051 291 O ATOM 3232 CB VAL B 651 19.571 -7.156 -17.285 1.00 52.72 C ANISOU 3232 CB VAL B 651 6323 8980 4729 -277 -983 301 C ATOM 3233 CG1 VAL B 651 19.045 -5.790 -17.710 1.00 57.95 C ANISOU 3233 CG1 VAL B 651 6948 9650 5422 -432 -930 390 C ATOM 3234 CG2 VAL B 651 20.863 -7.486 -18.012 1.00 54.91 C ANISOU 3234 CG2 VAL B 651 6539 9465 4859 -200 -999 188 C ATOM 3235 N SER B 652 21.084 -9.047 -14.867 1.00 44.69 N ANISOU 3235 N SER B 652 5350 7966 3664 6 -1007 183 N ATOM 3236 CA SER B 652 21.289 -10.415 -14.401 1.00 56.24 C ANISOU 3236 CA SER B 652 6871 9367 5129 158 -1060 127 C ATOM 3237 C SER B 652 22.364 -10.485 -13.336 1.00 55.95 C ANISOU 3237 C SER B 652 6799 9434 5024 236 -1033 88 C ATOM 3238 O SER B 652 23.480 -9.998 -13.537 1.00 61.36 O ANISOU 3238 O SER B 652 7398 10321 5597 239 -1007 27 O ATOM 3239 CB SER B 652 21.667 -11.329 -15.567 1.00 64.37 C ANISOU 3239 CB SER B 652 7902 10461 6093 247 -1122 31 C ATOM 3240 OG SER B 652 21.935 -12.645 -15.105 1.00 66.20 O ANISOU 3240 OG SER B 652 8188 10637 6327 399 -1168 -25 O ATOM 3241 N SER B 653 22.026 -11.110 -12.211 1.00 56.80 N ANISOU 3241 N SER B 653 6973 9410 5200 302 -1041 120 N ATOM 3242 CA SER B 653 22.929 -11.198 -11.072 1.00 52.82 C ANISOU 3242 CA SER B 653 6442 8989 4639 379 -1018 94 C ATOM 3243 C SER B 653 22.478 -12.282 -10.091 1.00 57.54 C ANISOU 3243 C SER B 653 7136 9418 5310 486 -1048 120 C ATOM 3244 O SER B 653 21.341 -12.753 -10.142 1.00 55.56 O ANISOU 3244 O SER B 653 6971 8970 5171 471 -1073 174 O ATOM 3245 CB SER B 653 23.000 -9.850 -10.348 1.00 58.87 C ANISOU 3245 CB SER B 653 7147 9811 5411 256 -940 153 C ATOM 3246 OG SER B 653 21.790 -9.579 -9.650 1.00 58.89 O ANISOU 3246 OG SER B 653 7212 9618 5545 177 -919 259 O ATOM 3247 N VAL B 654 23.376 -12.670 -9.193 1.00 55.46 N ANISOU 3247 N VAL B 654 6856 9236 4982 594 -1045 81 N ATOM 3248 CA VAL B 654 23.041 -13.642 -8.158 1.00 59.39 C ANISOU 3248 CA VAL B 654 7441 9586 5539 699 -1067 112 C ATOM 3249 C VAL B 654 23.051 -13.003 -6.786 1.00 64.14 C ANISOU 3249 C VAL B 654 8029 10182 6157 660 -1013 175 C ATOM 3250 O VAL B 654 24.027 -12.355 -6.397 1.00 63.20 O ANISOU 3250 O VAL B 654 7823 10245 5946 655 -977 140 O ATOM 3251 CB VAL B 654 24.021 -14.820 -8.127 1.00 55.49 C ANISOU 3251 CB VAL B 654 6953 9167 4962 883 -1115 21 C ATOM 3252 CG1 VAL B 654 23.719 -15.720 -6.926 1.00 53.41 C ANISOU 3252 CG1 VAL B 654 6779 8758 4757 989 -1127 64 C ATOM 3253 CG2 VAL B 654 23.949 -15.598 -9.432 1.00 56.83 C ANISOU 3253 CG2 VAL B 654 7145 9323 5125 931 -1171 -46 C ATOM 3254 N ILE B 655 21.960 -13.198 -6.055 1.00 62.64 N ANISOU 3254 N ILE B 655 7925 9789 6088 632 -1006 263 N ATOM 3255 CA ILE B 655 21.848 -12.700 -4.696 1.00 61.61 C ANISOU 3255 CA ILE B 655 7793 9631 5984 598 -957 327 C ATOM 3256 C ILE B 655 21.618 -13.869 -3.748 1.00 56.56 C ANISOU 3256 C ILE B 655 7250 8855 5385 729 -985 351 C ATOM 3257 O ILE B 655 21.176 -14.936 -4.168 1.00 60.28 O ANISOU 3257 O ILE B 655 7802 9197 5903 807 -1034 341 O ATOM 3258 CB ILE B 655 20.693 -11.696 -4.558 1.00 64.62 C ANISOU 3258 CB ILE B 655 8185 9889 6478 425 -911 422 C ATOM 3259 CG1 ILE B 655 19.356 -12.395 -4.808 1.00 62.87 C ANISOU 3259 CG1 ILE B 655 8075 9425 6388 415 -945 478 C ATOM 3260 CG2 ILE B 655 20.893 -10.514 -5.513 1.00 63.50 C ANISOU 3260 CG2 ILE B 655 7952 9876 6300 295 -879 407 C ATOM 3261 CD1 ILE B 655 18.155 -11.573 -4.403 1.00 63.19 C ANISOU 3261 CD1 ILE B 655 8140 9319 6551 265 -902 577 C ATOM 3262 N THR B 656 21.910 -13.662 -2.469 1.00 51.84 N ANISOU 3262 N THR B 656 6643 8285 4769 750 -951 382 N ATOM 3263 CA THR B 656 21.820 -14.741 -1.494 1.00 56.31 C ANISOU 3263 CA THR B 656 7295 8742 5358 883 -974 407 C ATOM 3264 C THR B 656 20.769 -14.493 -0.416 1.00 55.51 C ANISOU 3264 C THR B 656 7258 8467 5368 810 -936 513 C ATOM 3265 O THR B 656 20.790 -13.477 0.264 1.00 51.93 O ANISOU 3265 O THR B 656 6749 8072 4910 712 -882 548 O ATOM 3266 CB THR B 656 23.187 -14.998 -0.824 1.00 60.48 C ANISOU 3266 CB THR B 656 7767 9460 5753 1015 -978 346 C ATOM 3267 OG1 THR B 656 24.045 -15.693 -1.739 1.00 59.75 O ANISOU 3267 OG1 THR B 656 7650 9477 5576 1129 -1027 249 O ATOM 3268 CG2 THR B 656 23.025 -15.822 0.451 1.00 61.49 C ANISOU 3268 CG2 THR B 656 7977 9481 5907 1127 -983 397 C ATOM 3269 N VAL B 657 19.855 -15.443 -0.262 1.00 60.59 N ANISOU 3269 N VAL B 657 8017 8895 6111 856 -963 558 N ATOM 3270 CA VAL B 657 18.880 -15.407 0.818 1.00 54.66 C ANISOU 3270 CA VAL B 657 7338 7967 5463 808 -931 654 C ATOM 3271 C VAL B 657 19.360 -16.272 1.979 1.00 59.77 C ANISOU 3271 C VAL B 657 8034 8607 6069 958 -938 665 C ATOM 3272 O VAL B 657 19.718 -17.437 1.790 1.00 55.06 O ANISOU 3272 O VAL B 657 7489 7984 5446 1108 -984 627 O ATOM 3273 CB VAL B 657 17.519 -15.939 0.349 1.00 51.16 C ANISOU 3273 CB VAL B 657 6998 7280 5162 764 -950 701 C ATOM 3274 CG1 VAL B 657 16.553 -16.036 1.524 1.00 55.40 C ANISOU 3274 CG1 VAL B 657 7616 7630 5803 730 -918 796 C ATOM 3275 CG2 VAL B 657 16.960 -15.064 -0.760 1.00 44.81 C ANISOU 3275 CG2 VAL B 657 6148 6477 4401 614 -943 700 C ATOM 3276 N ASN B 658 19.362 -15.701 3.180 1.00 68.86 N ANISOU 3276 N ASN B 658 9168 9781 7216 920 -892 718 N ATOM 3277 CA ASN B 658 19.805 -16.425 4.367 1.00 71.41 C ANISOU 3277 CA ASN B 658 9533 10106 7494 1056 -895 737 C ATOM 3278 C ASN B 658 19.144 -15.904 5.651 1.00 70.69 C ANISOU 3278 C ASN B 658 9466 9930 7463 976 -842 827 C ATOM 3279 O ASN B 658 19.674 -15.019 6.325 1.00 63.76 O ANISOU 3279 O ASN B 658 8504 9200 6521 928 -801 825 O ATOM 3280 CB ASN B 658 21.331 -16.355 4.485 1.00 77.40 C ANISOU 3280 CB ASN B 658 10195 11121 8092 1161 -906 656 C ATOM 3281 CG ASN B 658 21.901 -17.432 5.393 1.00 84.57 C ANISOU 3281 CG ASN B 658 11156 12034 8943 1347 -931 660 C ATOM 3282 OD1 ASN B 658 21.257 -18.450 5.649 1.00 87.49 O ANISOU 3282 OD1 ASN B 658 11641 12213 9387 1423 -951 707 O ATOM 3283 ND2 ASN B 658 23.122 -17.217 5.874 1.00 85.59 N ANISOU 3283 ND2 ASN B 658 11198 12382 8938 1424 -928 608 N ATOM 3284 N GLY B 659 17.974 -16.448 5.975 1.00 73.08 N ANISOU 3284 N GLY B 659 9882 9996 7890 959 -840 901 N ATOM 3285 CA GLY B 659 17.308 -16.143 7.229 1.00 67.78 C ANISOU 3285 CA GLY B 659 9249 9225 7278 900 -793 987 C ATOM 3286 C GLY B 659 16.493 -14.865 7.238 1.00 64.15 C ANISOU 3286 C GLY B 659 8746 8727 6901 698 -741 1030 C ATOM 3287 O GLY B 659 15.795 -14.570 8.212 1.00 56.58 O ANISOU 3287 O GLY B 659 7821 7668 6010 630 -700 1102 O ATOM 3288 N LYS B 660 16.573 -14.102 6.154 1.00 65.15 N ANISOU 3288 N LYS B 660 8798 8933 7024 601 -742 987 N ATOM 3289 CA LYS B 660 15.804 -12.869 6.046 1.00 60.20 C ANISOU 3289 CA LYS B 660 8127 8268 6478 410 -693 1027 C ATOM 3290 C LYS B 660 15.475 -12.549 4.593 1.00 55.87 C ANISOU 3290 C LYS B 660 7555 7707 5967 331 -715 997 C ATOM 3291 O LYS B 660 15.947 -13.216 3.664 1.00 49.01 O ANISOU 3291 O LYS B 660 6691 6883 5048 421 -765 936 O ATOM 3292 CB LYS B 660 16.563 -11.703 6.690 1.00 60.38 C ANISOU 3292 CB LYS B 660 8033 8487 6421 343 -640 1012 C ATOM 3293 CG LYS B 660 18.042 -11.652 6.317 1.00 66.21 C ANISOU 3293 CG LYS B 660 8677 9476 7005 432 -658 920 C ATOM 3294 CD LYS B 660 18.720 -10.404 6.870 1.00 74.90 C ANISOU 3294 CD LYS B 660 9655 10767 8037 346 -598 899 C ATOM 3295 CE LYS B 660 18.185 -9.141 6.198 1.00 82.21 C ANISOU 3295 CE LYS B 660 10519 11686 9030 158 -555 912 C ATOM 3296 NZ LYS B 660 18.983 -7.922 6.531 1.00 82.53 N ANISOU 3296 NZ LYS B 660 10429 11930 8997 77 -495 875 N ATOM 3297 N ASP B 661 14.647 -11.533 4.398 1.00 51.93 N ANISOU 3297 N ASP B 661 7030 7146 5556 164 -677 1040 N ATOM 3298 CA ASP B 661 14.384 -11.051 3.057 1.00 54.38 C ANISOU 3298 CA ASP B 661 7303 7468 5891 79 -691 1017 C ATOM 3299 C ASP B 661 15.660 -10.447 2.484 1.00 47.04 C ANISOU 3299 C ASP B 661 6258 6787 4828 90 -687 941 C ATOM 3300 O ASP B 661 16.457 -9.849 3.205 1.00 40.36 O ANISOU 3300 O ASP B 661 5337 6093 3904 86 -648 925 O ATOM 3301 CB ASP B 661 13.272 -10.009 3.075 1.00 54.60 C ANISOU 3301 CB ASP B 661 7321 7385 6038 -101 -645 1085 C ATOM 3302 CG ASP B 661 11.916 -10.611 3.393 1.00 60.48 C ANISOU 3302 CG ASP B 661 8180 7876 6925 -122 -654 1151 C ATOM 3303 OD1 ASP B 661 10.988 -9.848 3.739 1.00 70.90 O ANISOU 3303 OD1 ASP B 661 9500 9092 8347 -257 -612 1213 O ATOM 3304 OD2 ASP B 661 11.775 -11.848 3.295 1.00 51.86 O ANISOU 3304 OD2 ASP B 661 7175 6685 5844 -5 -700 1139 O ATOM 3305 N ASN B 662 15.862 -10.625 1.189 1.00 53.56 N ANISOU 3305 N ASN B 662 7067 7658 5624 105 -727 890 N ATOM 3306 CA ASN B 662 16.920 -9.904 0.499 1.00 46.86 C ANISOU 3306 CA ASN B 662 6107 7034 4665 86 -716 823 C ATOM 3307 C ASN B 662 16.278 -8.958 -0.500 1.00 41.54 C ANISOU 3307 C ASN B 662 5397 6336 4051 -65 -699 846 C ATOM 3308 O ASN B 662 15.826 -9.368 -1.565 1.00 38.29 O ANISOU 3308 O ASN B 662 5021 5857 3671 -62 -742 834 O ATOM 3309 CB ASN B 662 17.897 -10.865 -0.177 1.00 45.17 C ANISOU 3309 CB ASN B 662 5890 6930 4343 238 -775 735 C ATOM 3310 CG ASN B 662 19.117 -10.152 -0.742 1.00 52.63 C ANISOU 3310 CG ASN B 662 6715 8122 5160 228 -760 658 C ATOM 3311 OD1 ASN B 662 19.009 -9.039 -1.254 1.00 49.83 O ANISOU 3311 OD1 ASN B 662 6293 7826 4815 95 -721 668 O ATOM 3312 ND2 ASN B 662 20.282 -10.792 -0.653 1.00 50.18 N ANISOU 3312 ND2 ASN B 662 6378 7957 4731 369 -788 582 N ATOM 3313 N LEU B 663 16.213 -7.686 -0.133 1.00 38.83 N ANISOU 3313 N LEU B 663 4983 6046 3726 -198 -634 879 N ATOM 3314 CA LEU B 663 15.535 -6.687 -0.949 1.00 42.27 C ANISOU 3314 CA LEU B 663 5385 6447 4228 -349 -608 915 C ATOM 3315 C LEU B 663 16.533 -5.862 -1.772 1.00 41.83 C ANISOU 3315 C LEU B 663 5219 6606 4067 -387 -587 857 C ATOM 3316 O LEU B 663 16.222 -4.763 -2.236 1.00 36.32 O ANISOU 3316 O LEU B 663 4470 5926 3406 -521 -544 887 O ATOM 3317 CB LEU B 663 14.693 -5.774 -0.054 1.00 38.97 C ANISOU 3317 CB LEU B 663 4965 5927 3917 -483 -545 997 C ATOM 3318 CG LEU B 663 13.281 -6.232 0.339 1.00 43.61 C ANISOU 3318 CG LEU B 663 5657 6265 4649 -513 -558 1072 C ATOM 3319 CD1 LEU B 663 13.117 -7.737 0.211 1.00 36.04 C ANISOU 3319 CD1 LEU B 663 4798 5204 3693 -370 -627 1051 C ATOM 3320 CD2 LEU B 663 12.901 -5.746 1.745 1.00 35.40 C ANISOU 3320 CD2 LEU B 663 4619 5162 3670 -575 -499 1129 C ATOM 3321 N SER B 664 17.727 -6.410 -1.972 1.00 37.70 N ANISOU 3321 N SER B 664 4663 6246 3416 -266 -615 772 N ATOM 3322 CA SER B 664 18.808 -5.639 -2.582 1.00 42.72 C ANISOU 3322 CA SER B 664 5188 7101 3941 -295 -587 708 C ATOM 3323 C SER B 664 18.968 -5.903 -4.076 1.00 42.13 C ANISOU 3323 C SER B 664 5108 7075 3824 -275 -633 663 C ATOM 3324 O SER B 664 19.885 -5.374 -4.699 1.00 48.71 O ANISOU 3324 O SER B 664 5856 8091 4560 -290 -615 605 O ATOM 3325 CB SER B 664 20.131 -5.880 -1.844 1.00 43.55 C ANISOU 3325 CB SER B 664 5238 7387 3921 -189 -579 635 C ATOM 3326 OG SER B 664 20.642 -7.175 -2.101 1.00 38.50 O ANISOU 3326 OG SER B 664 4644 6768 3216 -24 -649 576 O ATOM 3327 N ALA B 665 18.073 -6.711 -4.647 1.00 36.20 N ANISOU 3327 N ALA B 665 4446 6162 3146 -245 -690 688 N ATOM 3328 CA ALA B 665 18.107 -7.019 -6.074 1.00 37.06 C ANISOU 3328 CA ALA B 665 4555 6303 3221 -228 -737 647 C ATOM 3329 C ALA B 665 17.414 -5.919 -6.864 1.00 36.48 C ANISOU 3329 C ALA B 665 4450 6205 3206 -383 -706 701 C ATOM 3330 O ALA B 665 16.251 -6.050 -7.227 1.00 37.87 O ANISOU 3330 O ALA B 665 4688 6214 3486 -432 -728 758 O ATOM 3331 CB ALA B 665 17.445 -8.355 -6.345 1.00 37.62 C ANISOU 3331 CB ALA B 665 4731 6216 3348 -130 -809 644 C ATOM 3332 N ASP B 666 18.135 -4.834 -7.131 1.00 34.95 N ANISOU 3332 N ASP B 666 4158 6178 2943 -460 -652 683 N ATOM 3333 CA ASP B 666 17.538 -3.656 -7.754 1.00 35.44 C ANISOU 3333 CA ASP B 666 4184 6223 3060 -612 -609 744 C ATOM 3334 C ASP B 666 18.191 -3.360 -9.119 1.00 39.88 C ANISOU 3334 C ASP B 666 4686 6942 3525 -623 -618 691 C ATOM 3335 O ASP B 666 19.318 -3.771 -9.381 1.00 44.80 O ANISOU 3335 O ASP B 666 5269 7725 4027 -533 -636 603 O ATOM 3336 CB ASP B 666 17.684 -2.430 -6.839 1.00 35.12 C ANISOU 3336 CB ASP B 666 4078 6224 3042 -722 -520 783 C ATOM 3337 CG ASP B 666 17.230 -2.697 -5.402 1.00 42.71 C ANISOU 3337 CG ASP B 666 5086 7062 4078 -706 -505 824 C ATOM 3338 OD1 ASP B 666 16.135 -3.283 -5.204 1.00 35.36 O ANISOU 3338 OD1 ASP B 666 4245 5937 3253 -698 -540 878 O ATOM 3339 OD2 ASP B 666 17.975 -2.307 -4.468 1.00 31.72 O ANISOU 3339 OD2 ASP B 666 3639 5775 2639 -703 -456 799 O ATOM 3340 N LEU B 667 17.471 -2.644 -9.977 1.00 31.66 N ANISOU 3340 N LEU B 667 3638 5855 2535 -732 -606 748 N ATOM 3341 CA LEU B 667 17.947 -2.316 -11.316 1.00 38.07 C ANISOU 3341 CA LEU B 667 4400 6802 3263 -754 -613 712 C ATOM 3342 C LEU B 667 17.741 -0.834 -11.576 1.00 32.68 C ANISOU 3342 C LEU B 667 3655 6152 2610 -908 -537 777 C ATOM 3343 O LEU B 667 16.645 -0.319 -11.402 1.00 32.48 O ANISOU 3343 O LEU B 667 3660 5979 2703 -1001 -519 867 O ATOM 3344 CB LEU B 667 17.189 -3.114 -12.384 1.00 32.92 C ANISOU 3344 CB LEU B 667 3813 6056 2640 -716 -691 714 C ATOM 3345 CG LEU B 667 17.592 -2.730 -13.811 1.00 36.21 C ANISOU 3345 CG LEU B 667 4178 6609 2971 -746 -698 684 C ATOM 3346 CD1 LEU B 667 19.025 -3.187 -14.091 1.00 35.78 C ANISOU 3346 CD1 LEU B 667 4072 6756 2767 -646 -711 571 C ATOM 3347 CD2 LEU B 667 16.624 -3.307 -14.851 1.00 33.99 C ANISOU 3347 CD2 LEU B 667 3957 6221 2736 -738 -767 703 C ATOM 3348 N GLY B 668 18.801 -0.146 -11.975 1.00 36.73 N ANISOU 3348 N GLY B 668 4080 6858 3018 -935 -491 729 N ATOM 3349 CA GLY B 668 18.689 1.255 -12.334 1.00 38.32 C ANISOU 3349 CA GLY B 668 4220 7100 3239 -1078 -414 787 C ATOM 3350 C GLY B 668 18.760 1.396 -13.841 1.00 39.42 C ANISOU 3350 C GLY B 668 4343 7316 3318 -1097 -438 779 C ATOM 3351 O GLY B 668 19.608 0.768 -14.479 1.00 40.98 O ANISOU 3351 O GLY B 668 4524 7646 3402 -1009 -477 692 O ATOM 3352 N ILE B 669 17.859 2.202 -14.402 1.00 37.42 N ANISOU 3352 N ILE B 669 4096 6980 3140 -1208 -416 870 N ATOM 3353 CA ILE B 669 17.814 2.467 -15.847 1.00 38.19 C ANISOU 3353 CA ILE B 669 4178 7145 3186 -1239 -433 880 C ATOM 3354 C ILE B 669 17.675 3.976 -16.131 1.00 37.83 C ANISOU 3354 C ILE B 669 4075 7129 3169 -1385 -344 958 C ATOM 3355 O ILE B 669 17.237 4.745 -15.267 1.00 37.41 O ANISOU 3355 O ILE B 669 4013 6989 3211 -1470 -282 1023 O ATOM 3356 CB ILE B 669 16.646 1.716 -16.544 1.00 40.29 C ANISOU 3356 CB ILE B 669 4525 7265 3517 -1210 -519 918 C ATOM 3357 CG1 ILE B 669 15.304 2.112 -15.930 1.00 40.08 C ANISOU 3357 CG1 ILE B 669 4546 7032 3650 -1290 -505 1024 C ATOM 3358 CG2 ILE B 669 16.835 0.204 -16.462 1.00 40.87 C ANISOU 3358 CG2 ILE B 669 4654 7320 3556 -1064 -604 834 C ATOM 3359 CD1 ILE B 669 14.096 1.444 -16.610 1.00 38.13 C ANISOU 3359 CD1 ILE B 669 4375 6639 3474 -1271 -585 1061 C ATOM 3360 N TYR B 670 18.073 4.400 -17.325 1.00 37.97 N ANISOU 3360 N TYR B 670 4053 7269 3103 -1414 -334 951 N ATOM 3361 CA TYR B 670 17.968 5.806 -17.711 1.00 47.78 C ANISOU 3361 CA TYR B 670 5245 8542 4368 -1548 -249 1027 C ATOM 3362 C TYR B 670 17.532 5.941 -19.168 1.00 47.19 C ANISOU 3362 C TYR B 670 5183 8485 4263 -1572 -284 1069 C ATOM 3363 O TYR B 670 17.676 5.010 -19.954 1.00 43.15 O ANISOU 3363 O TYR B 670 4696 8021 3678 -1484 -362 1012 O ATOM 3364 CB TYR B 670 19.290 6.559 -17.476 1.00 38.37 C ANISOU 3364 CB TYR B 670 3961 7534 3083 -1582 -159 969 C ATOM 3365 CG TYR B 670 20.442 6.087 -18.344 1.00 53.40 C ANISOU 3365 CG TYR B 670 5828 9634 4829 -1507 -184 865 C ATOM 3366 CD1 TYR B 670 20.629 6.589 -19.626 1.00 51.47 C ANISOU 3366 CD1 TYR B 670 5554 9486 4515 -1552 -170 882 C ATOM 3367 CD2 TYR B 670 21.346 5.138 -17.878 1.00 62.18 C ANISOU 3367 CD2 TYR B 670 6931 10836 5860 -1390 -221 752 C ATOM 3368 CE1 TYR B 670 21.681 6.159 -20.418 1.00 57.49 C ANISOU 3368 CE1 TYR B 670 6281 10431 5133 -1487 -191 784 C ATOM 3369 CE2 TYR B 670 22.398 4.699 -18.666 1.00 61.89 C ANISOU 3369 CE2 TYR B 670 6857 10977 5681 -1322 -244 652 C ATOM 3370 CZ TYR B 670 22.562 5.213 -19.933 1.00 64.06 C ANISOU 3370 CZ TYR B 670 7103 11346 5890 -1372 -228 667 C ATOM 3371 OH TYR B 670 23.613 4.776 -20.713 1.00 70.95 O ANISOU 3371 OH TYR B 670 7937 12399 6621 -1307 -249 564 O ATOM 3372 N LYS B 671 16.978 7.097 -19.509 1.00 46.63 N ANISOU 3372 N LYS B 671 5093 8374 4252 -1690 -224 1170 N ATOM 3373 CA LYS B 671 16.586 7.380 -20.876 1.00 49.66 C ANISOU 3373 CA LYS B 671 5481 8784 4603 -1721 -247 1221 C ATOM 3374 C LYS B 671 17.563 8.371 -21.490 1.00 53.98 C ANISOU 3374 C LYS B 671 5950 9507 5051 -1786 -162 1213 C ATOM 3375 O LYS B 671 17.574 9.550 -21.122 1.00 52.14 O ANISOU 3375 O LYS B 671 5677 9265 4870 -1892 -66 1276 O ATOM 3376 CB LYS B 671 15.175 7.961 -20.926 1.00 50.68 C ANISOU 3376 CB LYS B 671 5649 8736 4870 -1804 -245 1350 C ATOM 3377 CG LYS B 671 14.714 8.321 -22.333 1.00 58.47 C ANISOU 3377 CG LYS B 671 6639 9750 5825 -1839 -267 1412 C ATOM 3378 CD LYS B 671 13.570 9.321 -22.302 1.00 65.90 C ANISOU 3378 CD LYS B 671 7592 10550 6896 -1947 -229 1548 C ATOM 3379 CE LYS B 671 12.447 8.858 -21.383 1.00 76.51 C ANISOU 3379 CE LYS B 671 8997 11688 8385 -1938 -270 1583 C ATOM 3380 NZ LYS B 671 11.514 9.975 -21.065 1.00 80.30 N ANISOU 3380 NZ LYS B 671 9475 12037 8999 -2052 -210 1706 N ATOM 3381 N PRO B 672 18.402 7.895 -22.418 1.00 58.33 N ANISOU 3381 N PRO B 672 6479 10220 5462 -1724 -195 1133 N ATOM 3382 CA PRO B 672 19.242 8.822 -23.180 1.00 64.99 C ANISOU 3382 CA PRO B 672 7255 11229 6210 -1788 -118 1132 C ATOM 3383 C PRO B 672 18.348 9.708 -24.042 1.00 64.80 C ANISOU 3383 C PRO B 672 7243 11143 6236 -1881 -97 1260 C ATOM 3384 O PRO B 672 17.242 9.296 -24.405 1.00 55.41 O ANISOU 3384 O PRO B 672 6114 9830 5111 -1864 -170 1318 O ATOM 3385 CB PRO B 672 20.074 7.893 -24.071 1.00 68.41 C ANISOU 3385 CB PRO B 672 7679 11818 6494 -1688 -182 1022 C ATOM 3386 CG PRO B 672 20.000 6.548 -23.413 1.00 66.67 C ANISOU 3386 CG PRO B 672 7507 11536 6290 -1568 -270 944 C ATOM 3387 CD PRO B 672 18.641 6.492 -22.792 1.00 62.15 C ANISOU 3387 CD PRO B 672 6999 10743 5872 -1593 -298 1036 C ATOM 3388 N LYS B 673 18.807 10.913 -24.354 1.00 67.21 N ANISOU 3388 N LYS B 673 7440 13021 5074 -2377 726 551 N ATOM 3389 CA LYS B 673 18.030 11.793 -25.210 1.00 66.78 C ANISOU 3389 CA LYS B 673 7420 12999 4955 -2224 823 552 C ATOM 3390 C LYS B 673 17.813 11.086 -26.542 1.00 58.65 C ANISOU 3390 C LYS B 673 6622 11927 3735 -1959 763 560 C ATOM 3391 O LYS B 673 18.610 10.230 -26.931 1.00 55.20 O ANISOU 3391 O LYS B 673 6294 11420 3257 -1844 740 601 O ATOM 3392 CB LYS B 673 18.754 13.130 -25.397 1.00 77.66 C ANISOU 3392 CB LYS B 673 8673 14352 6481 -2124 1107 644 C ATOM 3393 CG LYS B 673 19.196 13.768 -24.075 1.00 83.06 C ANISOU 3393 CG LYS B 673 9130 15061 7368 -2374 1174 647 C ATOM 3394 CD LYS B 673 19.585 15.236 -24.230 1.00 90.45 C ANISOU 3394 CD LYS B 673 9930 15993 8444 -2298 1442 718 C ATOM 3395 CE LYS B 673 21.006 15.422 -24.764 1.00 95.27 C ANISOU 3395 CE LYS B 673 10540 16504 9153 -2102 1647 830 C ATOM 3396 NZ LYS B 673 21.165 15.060 -26.204 1.00 97.86 N ANISOU 3396 NZ LYS B 673 11074 16770 9339 -1790 1701 879 N ATOM 3397 N TYR B 674 16.729 11.415 -27.239 1.00 60.93 N ANISOU 3397 N TYR B 674 6991 12254 3906 -1862 728 517 N ATOM 3398 CA TYR B 674 16.474 10.786 -28.539 1.00 62.64 C ANISOU 3398 CA TYR B 674 7440 12427 3934 -1601 665 521 C ATOM 3399 C TYR B 674 17.608 11.076 -29.509 1.00 62.31 C ANISOU 3399 C TYR B 674 7479 12295 3903 -1324 885 639 C ATOM 3400 O TYR B 674 18.085 12.214 -29.613 1.00 64.02 O ANISOU 3400 O TYR B 674 7594 12497 4234 -1258 1118 708 O ATOM 3401 CB TYR B 674 15.141 11.234 -29.133 1.00 57.19 C ANISOU 3401 CB TYR B 674 6812 11786 3132 -1535 603 457 C ATOM 3402 CG TYR B 674 13.976 11.003 -28.207 1.00 56.58 C ANISOU 3402 CG TYR B 674 6649 11793 3055 -1805 400 338 C ATOM 3403 CD1 TYR B 674 13.578 11.988 -27.311 1.00 37.93 C ANISOU 3403 CD1 TYR B 674 4086 9496 830 -2009 469 311 C ATOM 3404 CD2 TYR B 674 13.287 9.792 -28.204 1.00 41.51 C ANISOU 3404 CD2 TYR B 674 4860 9895 1018 -1862 145 251 C ATOM 3405 CE1 TYR B 674 12.509 11.791 -26.461 1.00 43.62 C ANISOU 3405 CE1 TYR B 674 4730 10286 1556 -2257 297 201 C ATOM 3406 CE2 TYR B 674 12.213 9.587 -27.349 1.00 45.56 C ANISOU 3406 CE2 TYR B 674 5293 10477 1541 -2112 -29 139 C ATOM 3407 CZ TYR B 674 11.832 10.590 -26.477 1.00 50.83 C ANISOU 3407 CZ TYR B 674 5762 11204 2345 -2310 51 115 C ATOM 3408 OH TYR B 674 10.771 10.398 -25.616 1.00 62.57 O ANISOU 3408 OH TYR B 674 7171 12754 3848 -2561 -109 5 O ATOM 3409 N ASN B 675 18.042 10.036 -30.211 1.00 54.75 N ANISOU 3409 N ASN B 675 6703 11270 2828 -1163 815 660 N ATOM 3410 CA ASN B 675 19.141 10.163 -31.148 1.00 68.28 C ANISOU 3410 CA ASN B 675 8511 12885 4545 -897 1017 769 C ATOM 3411 C ASN B 675 18.659 9.759 -32.536 1.00 70.65 C ANISOU 3411 C ASN B 675 9066 13146 4631 -622 970 768 C ATOM 3412 O ASN B 675 19.047 8.710 -33.049 1.00 79.59 O ANISOU 3412 O ASN B 675 10361 14220 5661 -505 887 779 O ATOM 3413 CB ASN B 675 20.303 9.277 -30.697 1.00 77.39 C ANISOU 3413 CB ASN B 675 9649 13979 5775 -949 999 807 C ATOM 3414 CG ASN B 675 21.577 9.534 -31.483 1.00 88.41 C ANISOU 3414 CG ASN B 675 11096 15267 7228 -707 1243 923 C ATOM 3415 OD1 ASN B 675 21.713 10.559 -32.156 1.00 91.35 O ANISOU 3415 OD1 ASN B 675 11470 15613 7624 -537 1461 985 O ATOM 3416 ND2 ASN B 675 22.523 8.605 -31.394 1.00 88.71 N ANISOU 3416 ND2 ASN B 675 11175 15238 7294 -691 1212 954 N ATOM 3417 N LEU B 676 17.805 10.590 -33.134 1.00 62.68 N ANISOU 3417 N LEU B 676 8095 12167 3554 -520 1015 752 N ATOM 3418 CA LEU B 676 17.092 10.208 -34.357 1.00 62.01 C ANISOU 3418 CA LEU B 676 8251 12056 3254 -289 921 728 C ATOM 3419 C LEU B 676 17.810 10.539 -35.657 1.00 62.37 C ANISOU 3419 C LEU B 676 8466 12001 3231 43 1133 830 C ATOM 3420 O LEU B 676 18.455 11.580 -35.789 1.00 61.74 O ANISOU 3420 O LEU B 676 8303 11890 3264 122 1391 912 O ATOM 3421 CB LEU B 676 15.689 10.817 -34.390 1.00 55.11 C ANISOU 3421 CB LEU B 676 7356 11259 2323 -342 824 645 C ATOM 3422 CG LEU B 676 14.542 9.999 -33.792 1.00 51.56 C ANISOU 3422 CG LEU B 676 6900 10883 1806 -547 523 516 C ATOM 3423 CD1 LEU B 676 15.046 8.939 -32.839 1.00 44.12 C ANISOU 3423 CD1 LEU B 676 5896 9947 920 -752 394 493 C ATOM 3424 CD2 LEU B 676 13.596 10.941 -33.088 1.00 51.35 C ANISOU 3424 CD2 LEU B 676 6694 10946 1871 -738 513 452 C ATOM 3425 N GLY B 677 17.663 9.637 -36.621 1.00 64.09 N ANISOU 3425 N GLY B 677 8928 12165 3260 239 1022 821 N ATOM 3426 CA GLY B 677 18.189 9.830 -37.953 1.00 62.12 C ANISOU 3426 CA GLY B 677 8882 11813 2906 568 1195 907 C ATOM 3427 C GLY B 677 19.687 10.045 -37.985 1.00 64.37 C ANISOU 3427 C GLY B 677 9118 12013 3327 650 1453 1022 C ATOM 3428 O GLY B 677 20.411 9.647 -37.067 1.00 62.31 O ANISOU 3428 O GLY B 677 8709 11757 3210 472 1445 1031 O ATOM 3429 N ASP B 678 20.141 10.679 -39.062 1.00 65.66 N ANISOU 3429 N ASP B 678 9410 12092 3447 925 1683 1109 N ATOM 3430 CA ASP B 678 21.546 10.995 -39.260 1.00 76.82 C ANISOU 3430 CA ASP B 678 10792 13408 4989 1041 1961 1222 C ATOM 3431 C ASP B 678 21.902 12.305 -38.549 1.00 85.86 C ANISOU 3431 C ASP B 678 11682 14584 6355 918 2176 1264 C ATOM 3432 O ASP B 678 21.029 12.974 -38.001 1.00 84.90 O ANISOU 3432 O ASP B 678 11432 14558 6267 765 2113 1207 O ATOM 3433 CB ASP B 678 21.823 11.113 -40.767 1.00 78.95 C ANISOU 3433 CB ASP B 678 11328 13565 5104 1396 2121 1295 C ATOM 3434 CG ASP B 678 21.367 9.881 -41.545 1.00 71.68 C ANISOU 3434 CG ASP B 678 10675 12614 3948 1532 1902 1250 C ATOM 3435 OD1 ASP B 678 20.938 10.021 -42.705 1.00 56.15 O ANISOU 3435 OD1 ASP B 678 8940 10597 1799 1780 1926 1263 O ATOM 3436 OD2 ASP B 678 21.427 8.766 -40.986 1.00 86.74 O ANISOU 3436 OD2 ASP B 678 12564 14544 5851 1389 1701 1201 O ATOM 3437 N TYR B 679 23.181 12.667 -38.543 1.00 99.77 N ANISOU 3437 N TYR B 679 13368 16264 8275 983 2429 1360 N ATOM 3438 CA TYR B 679 23.578 14.004 -38.103 1.00113.99 C ANISOU 3438 CA TYR B 679 14959 18075 10276 924 2670 1412 C ATOM 3439 C TYR B 679 24.549 14.660 -39.091 1.00126.00 C ANISOU 3439 C TYR B 679 16569 19471 11834 1200 2999 1529 C ATOM 3440 O TYR B 679 25.508 14.036 -39.555 1.00124.73 O ANISOU 3440 O TYR B 679 16509 19206 11677 1339 3086 1587 O ATOM 3441 CB TYR B 679 24.161 13.999 -36.685 1.00115.67 C ANISOU 3441 CB TYR B 679 14895 18331 10723 635 2651 1399 C ATOM 3442 CG TYR B 679 24.183 12.647 -36.010 1.00121.14 C ANISOU 3442 CG TYR B 679 15589 19049 11391 466 2390 1336 C ATOM 3443 CD1 TYR B 679 25.365 11.926 -35.899 1.00123.16 C ANISOU 3443 CD1 TYR B 679 15840 19219 11736 488 2436 1384 C ATOM 3444 CD2 TYR B 679 23.025 12.094 -35.475 1.00122.30 C ANISOU 3444 CD2 TYR B 679 15737 19299 11432 283 2099 1227 C ATOM 3445 CE1 TYR B 679 25.395 10.693 -35.280 1.00124.37 C ANISOU 3445 CE1 TYR B 679 15997 19393 11865 335 2197 1328 C ATOM 3446 CE2 TYR B 679 23.044 10.857 -34.856 1.00123.15 C ANISOU 3446 CE2 TYR B 679 15850 19426 11514 128 1865 1170 C ATOM 3447 CZ TYR B 679 24.233 10.161 -34.760 1.00124.24 C ANISOU 3447 CZ TYR B 679 15990 19481 11735 155 1913 1222 C ATOM 3448 OH TYR B 679 24.264 8.930 -34.145 1.00122.13 O ANISOU 3448 OH TYR B 679 15733 19230 11443 3 1679 1166 O ATOM 3449 N ALA B 680 24.277 15.922 -39.411 1.00 82.96 N ATOM 3450 CA ALA B 680 25.106 16.690 -40.335 1.00 70.09 C ATOM 3451 C ALA B 680 24.911 18.185 -40.113 1.00 77.07 C ATOM 3452 O ALA B 680 24.220 18.591 -39.181 1.00 78.05 O ATOM 3453 CB ALA B 680 24.770 16.336 -41.739 1.00 43.24 C TER 3454 ALA B 680 HETATM 3455 CA CA B 701 16.052 -2.531 -2.695 1.00 21.24 Ca HETATM 3456 CA CA B 702 22.225 -4.542 -5.135 1.00 28.51 Ca HETATM 3457 CA CA B 703 21.357 8.033 -9.088 1.00 25.67 Ca HETATM 3458 CA CA B 704 -19.055 -13.297 24.016 1.00 25.70 Ca HETATM 3459 O HOH B 801 20.726 -2.657 -4.897 1.00 42.56 O HETATM 3460 O HOH B 802 -7.712 6.893 22.729 1.00 34.54 O HETATM 3461 O HOH B 803 -12.735 -13.042 57.372 1.00 19.15 O HETATM 3462 O HOH B 804 -9.700 6.609 28.949 1.00 24.51 O HETATM 3463 O HOH B 805 8.942 4.087 18.029 1.00 28.03 O HETATM 3464 O HOH B 806 -11.342 -28.250 43.248 1.00 26.56 O HETATM 3465 O HOH B 807 -19.074 -27.831 52.031 1.00 26.63 O HETATM 3466 O HOH B 808 15.797 -0.333 -3.153 1.00 31.31 O HETATM 3467 O HOH B 809 -16.954 -14.979 37.622 1.00 26.59 O HETATM 3468 O HOH B 810 -15.942 -8.328 48.950 1.00 33.08 O HETATM 3469 O HOH B 811 -2.500 -21.387 38.413 1.00 23.75 O HETATM 3470 O HOH B 812 -5.705 -37.378 34.665 1.00 23.00 O HETATM 3471 O HOH B 813 -18.249 -1.472 35.432 1.00 24.47 O HETATM 3472 O HOH B 814 -10.439 -0.674 32.125 1.00 33.18 O HETATM 3473 O HOH B 815 2.449 -29.420 51.578 1.00 17.12 O HETATM 3474 O HOH B 816 -7.153 -33.733 42.753 1.00 24.16 O HETATM 3475 O HOH B 817 -13.794 -22.418 30.971 1.00 27.52 O HETATM 3476 O HOH B 818 -12.626 -27.513 49.607 1.00 22.09 O HETATM 3477 O HOH B 819 -11.903 7.283 10.646 1.00 44.23 O HETATM 3478 O HOH B 820 -10.922 -8.469 25.618 1.00 27.94 O HETATM 3479 O HOH B 821 1.100 -0.168 23.986 1.00 22.56 O HETATM 3480 O HOH B 822 1.509 -11.460 54.334 1.00 44.52 O HETATM 3481 O HOH B 823 -8.407 -37.214 34.045 1.00 26.07 O HETATM 3482 O HOH B 824 -23.902 -15.305 56.927 1.00 28.77 O HETATM 3483 O HOH B 825 -9.901 -5.122 42.938 1.00 24.76 O HETATM 3484 O HOH B 826 -3.142 -8.051 16.237 1.00 34.71 O HETATM 3485 O HOH B 827 -17.984 -8.567 42.334 1.00 24.23 O HETATM 3486 O HOH B 828 -18.852 -29.003 44.563 1.00 37.91 O HETATM 3487 O HOH B 829 -2.214 9.294 19.496 1.00 30.17 O HETATM 3488 O HOH B 830 -6.994 -33.528 34.335 1.00 23.97 O HETATM 3489 O HOH B 831 8.531 12.651 3.454 1.00 36.91 O HETATM 3490 O HOH B 832 -15.178 -1.903 51.426 1.00 25.82 O HETATM 3491 O HOH B 833 -16.206 -18.862 38.030 1.00 26.69 O HETATM 3492 O HOH B 834 -3.207 -37.456 38.616 1.00 28.06 O HETATM 3493 O HOH B 835 -19.546 -17.843 50.511 1.00 23.15 O HETATM 3494 O HOH B 836 -0.018 -18.900 25.399 1.00 42.82 O HETATM 3495 O HOH B 837 -20.161 -22.459 57.417 1.00 27.56 O HETATM 3496 O HOH B 838 -18.003 -8.007 45.191 1.00 28.40 O HETATM 3497 O HOH B 839 18.162 -2.349 -1.399 1.00 42.97 O HETATM 3498 O HOH B 840 -4.087 -14.949 38.960 1.00 32.25 O HETATM 3499 O HOH B 841 0.774 -16.381 43.365 1.00 28.78 O HETATM 3500 O HOH B 842 -13.637 -22.596 61.706 1.00 23.54 O HETATM 3501 O HOH B 843 -14.301 4.300 28.450 1.00 31.95 O HETATM 3502 O HOH B 844 -11.088 -20.008 30.601 1.00 35.02 O HETATM 3503 O HOH B 845 -24.679 -4.578 30.957 1.00 42.68 O HETATM 3504 O HOH B 846 0.056 -36.622 43.208 1.00 34.33 O HETATM 3505 O HOH B 847 16.689 8.905 -17.394 1.00 40.98 O HETATM 3506 O HOH B 848 -14.529 -16.670 35.344 1.00 36.79 O HETATM 3507 O HOH B 849 6.715 -10.581 23.463 1.00 51.06 O HETATM 3508 O HOH B 850 -7.163 -34.570 45.134 1.00 41.51 O HETATM 3509 O HOH B 851 -2.364 -11.837 36.710 1.00 51.17 O HETATM 3510 O HOH B 852 -4.964 -0.738 29.278 1.00 33.63 O HETATM 3511 O HOH B 853 5.771 -7.805 -7.010 1.00 41.96 O HETATM 3512 O HOH B 854 6.844 -28.183 34.590 1.00 45.75 O HETATM 3513 O HOH B 855 -1.933 -2.475 26.755 1.00 22.88 O HETATM 3514 O HOH B 856 -1.269 -4.556 10.650 1.00 28.98 O HETATM 3515 O HOH B 857 5.685 4.031 23.007 1.00 37.69 O HETATM 3516 O HOH B 858 -16.911 0.447 33.500 1.00 35.77 O HETATM 3517 O HOH B 859 4.408 -8.787 0.904 1.00 57.22 O HETATM 3518 O HOH B 860 -2.298 4.678 30.988 1.00 41.87 O HETATM 3519 O HOH B 861 -11.232 -7.418 42.694 1.00 31.02 O HETATM 3520 O HOH B 862 -15.549 -19.812 35.559 1.00 45.69 O HETATM 3521 O HOH B 863 -10.482 -19.335 62.052 1.00 50.71 O HETATM 3522 O HOH B 864 -13.410 -34.324 37.657 1.00 30.05 O HETATM 3523 O HOH B 865 -9.189 -6.458 54.786 1.00 45.63 O HETATM 3524 O HOH B 866 1.926 -2.720 12.605 1.00 30.00 O HETATM 3525 O HOH B 867 -18.573 -22.784 37.091 1.00 39.63 O HETATM 3526 O HOH B 868 0.066 -31.468 44.586 1.00 24.20 O HETATM 3527 O HOH B 869 -4.295 -18.337 26.472 1.00 32.33 O HETATM 3528 O HOH B 870 -3.850 13.320 13.492 1.00 41.94 O HETATM 3529 O HOH B 871 13.315 5.897 -3.658 1.00 38.29 O HETATM 3530 O HOH B 872 -8.782 -3.109 39.268 1.00 58.75 O HETATM 3531 O HOH B 873 10.951 -0.404 -3.822 1.00 31.65 O HETATM 3532 O HOH B 874 -15.900 7.230 16.410 1.00 40.74 O HETATM 3533 O HOH B 875 13.175 -10.542 6.849 1.00 51.59 O HETATM 3534 O HOH B 876 -4.689 -34.930 35.064 1.00 34.66 O HETATM 3535 O HOH B 877 -13.841 -10.889 31.691 1.00 27.98 O HETATM 3536 O HOH B 878 1.205 -24.810 55.165 1.00 53.36 O HETATM 3537 O HOH B 879 -16.915 -12.729 35.806 1.00 33.27 O HETATM 3538 O HOH B 880 19.879 -8.706 -11.527 1.00 40.12 O HETATM 3539 O HOH B 881 -5.339 10.054 12.172 1.00 43.34 O HETATM 3540 O HOH B 882 -15.604 -14.982 61.076 1.00 45.71 O HETATM 3541 O HOH B 883 -7.586 -40.637 27.067 1.00 47.43 O HETATM 3542 O HOH B 884 -17.302 -17.148 60.521 1.00 31.16 O HETATM 3543 O HOH B 885 15.288 -1.957 -0.494 1.00 25.11 O HETATM 3544 O HOH B 886 2.779 -3.933 8.438 1.00 31.73 O HETATM 3545 O HOH B 887 -18.580 -2.800 17.683 1.00 37.54 O HETATM 3546 O HOH B 888 -14.532 -27.649 54.777 1.00 40.27 O HETATM 3547 O HOH B 889 -6.614 -19.604 58.010 1.00 30.44 O HETATM 3548 O HOH B 890 -8.567 -14.864 57.762 1.00 40.86 O HETATM 3549 O HOH B 891 -3.712 -34.594 37.708 1.00 31.95 O HETATM 3550 O HOH B 892 -3.624 -31.610 26.764 1.00 35.79 O HETATM 3551 O HOH B 893 -22.477 -20.831 56.973 1.00 28.22 O HETATM 3552 O HOH B 894 -13.904 -4.445 56.821 1.00 37.00 O HETATM 3553 O HOH B 895 -21.591 -13.707 45.473 1.00 46.38 O HETATM 3554 O HOH B 896 -6.393 7.869 24.512 1.00 36.33 O HETATM 3555 O HOH B 897 21.671 1.193 3.172 1.00 51.85 O HETATM 3556 O HOH B 898 7.076 -23.266 44.662 1.00 40.15 O HETATM 3557 O HOH B 899 -25.346 -0.163 33.118 1.00 36.97 O HETATM 3558 O HOH B 900 -18.541 -17.342 37.647 1.00 32.51 O HETATM 3559 O HOH B 901 2.840 -3.127 -13.068 1.00 46.61 O HETATM 3560 O HOH B 902 6.911 4.263 -14.416 1.00 45.34 O HETATM 3561 O HOH B 903 -22.382 -12.266 40.996 1.00 41.23 O HETATM 3562 O HOH B 904 -8.587 -6.085 12.888 1.00 45.97 O HETATM 3563 O HOH B 905 -8.856 6.995 14.887 1.00 40.23 O HETATM 3564 O HOH B 906 -2.858 1.092 31.691 1.00 39.78 O HETATM 3565 O HOH B 907 -24.078 -17.000 43.115 1.00 42.02 O HETATM 3566 O HOH B 908 13.024 -1.840 5.379 1.00 45.23 O HETATM 3567 O HOH B 909 23.978 -8.134 -16.020 1.00 50.54 O HETATM 3568 O HOH B 910 13.238 0.642 -2.440 1.00 31.60 O HETATM 3569 O HOH B 911 -6.036 -32.692 48.153 1.00 38.07 O HETATM 3570 O HOH B 912 -1.642 -5.298 49.174 1.00 43.91 O HETATM 3571 O HOH B 913 -12.332 -39.324 30.209 1.00 45.67 O HETATM 3572 O HOH B 914 2.255 -19.010 49.993 1.00 29.03 O HETATM 3573 O HOH B 915 7.850 -2.687 -20.051 1.00 59.57 O HETATM 3574 O HOH B 916 8.819 -26.708 34.740 1.00 58.15 O HETATM 3575 O HOH B 917 -9.877 -22.365 24.546 1.00 43.83 O HETATM 3576 O HOH B 918 -23.298 -8.039 26.354 1.00 29.16 O HETATM 3577 O HOH B 919 10.917 2.342 17.318 1.00 34.65 O HETATM 3578 O HOH B 920 4.873 -5.392 -8.310 1.00 40.53 O HETATM 3579 O HOH B 921 -9.411 -38.980 26.280 1.00 55.98 O HETATM 3580 O HOH B 922 5.993 -5.466 19.167 1.00 40.76 O HETATM 3581 O HOH B 923 1.372 -0.720 5.374 1.00 33.20 O HETATM 3582 O HOH B 924 -2.776 -8.365 18.858 1.00 31.91 O HETATM 3583 O HOH B 925 2.230 -5.544 13.364 1.00 35.16 O HETATM 3584 O HOH B 926 -21.961 -9.975 42.870 1.00 33.25 O HETATM 3585 O HOH B 927 -11.644 -4.761 57.386 1.00 38.89 O HETATM 3586 O HOH B 928 13.015 1.259 5.175 1.00 51.39 O HETATM 3587 O HOH B 929 -16.031 -19.817 64.831 1.00 49.52 O HETATM 3588 O HOH B 930 -17.237 3.078 16.037 1.00 44.04 O HETATM 3589 O HOH B 931 11.155 -4.862 6.281 1.00 44.13 O HETATM 3590 O HOH B 932 -4.568 -17.996 58.827 1.00 37.49 O HETATM 3591 O HOH B 933 -14.977 -38.759 30.666 1.00 58.20 O HETATM 3592 O HOH B 934 18.014 -6.253 2.001 1.00 47.52 O HETATM 3593 O HOH B 935 -23.117 -4.847 23.257 1.00 33.62 O HETATM 3594 O HOH B 936 -21.160 -10.721 45.296 1.00 53.22 O HETATM 3595 O HOH B 937 -11.381 -10.287 32.389 1.00 32.11 O HETATM 3596 O HOH B 938 -13.772 -36.337 27.555 1.00 59.99 O HETATM 3597 O HOH B 939 -16.833 -15.506 31.470 1.00 42.36 O HETATM 3598 O HOH B 940 -8.467 -17.473 57.538 1.00 35.69 O HETATM 3599 O HOH B 941 -23.411 -14.355 43.654 1.00 40.87 O HETATM 3600 O HOH B 942 -19.390 -6.852 48.214 1.00 41.57 O HETATM 3601 O HOH B 943 -10.006 -39.142 33.399 1.00 33.52 O HETATM 3602 O HOH B 944 -10.754 5.627 33.170 1.00 50.01 O HETATM 3603 O HOH B 945 16.676 3.291 -2.231 1.00 38.17 O HETATM 3604 O HOH B 946 1.860 -32.561 40.381 1.00 44.18 O HETATM 3605 O HOH B 947 -8.890 -7.467 31.588 1.00 38.60 O HETATM 3606 O HOH B 948 -4.298 -26.841 54.310 1.00 29.56 O HETATM 3607 O HOH B 949 -21.549 -13.429 30.682 1.00 38.53 O HETATM 3608 O HOH B 950 9.719 4.746 -22.596 1.00 50.15 O HETATM 3609 O HOH B 951 -17.671 -9.484 47.105 1.00 41.02 O HETATM 3610 O HOH B 952 -17.090 3.859 29.354 1.00 42.19 O HETATM 3611 O HOH B 953 7.869 -2.523 22.386 1.00 31.62 O HETATM 3612 O HOH B 954 -29.451 -26.666 50.725 1.00 46.43 O HETATM 3613 O HOH B 955 -23.639 -14.423 31.903 1.00 41.27 O HETATM 3614 O HOH B 956 -23.935 -3.915 37.354 1.00 35.30 O HETATM 3615 O HOH B 957 3.480 4.018 0.904 1.00 39.99 O HETATM 3616 O HOH B 958 5.239 -6.186 11.184 1.00 43.62 O HETATM 3617 O HOH B 959 14.395 -14.116 -17.624 1.00 58.63 O HETATM 3618 O HOH B 960 -8.691 -8.291 14.196 1.00 51.96 O HETATM 3619 O HOH B 961 -5.529 -19.924 24.494 1.00 54.40 O HETATM 3620 O HOH B 962 -27.026 -27.545 53.147 1.00 53.41 O HETATM 3621 O HOH B 963 -1.175 -7.977 14.308 1.00 43.18 O HETATM 3622 O HOH B 964 1.689 -34.255 47.999 1.00 37.03 O HETATM 3623 O HOH B 965 -21.398 -31.231 49.695 1.00 29.94 O HETATM 3624 O HOH B 966 3.880 -31.252 46.224 1.00 28.25 O HETATM 3625 O HOH B 967 -10.997 -25.158 58.558 1.00 54.80 O HETATM 3626 O HOH B 968 0.754 -2.923 9.976 1.00 31.14 O HETATM 3627 O HOH B 969 3.538 -20.319 48.035 1.00 36.47 O HETATM 3628 O HOH B 970 2.453 -22.504 48.213 1.00 34.67 O HETATM 3629 O HOH B 971 -4.936 -35.441 48.927 1.00 28.17 O HETATM 3630 O HOH B 972 -24.333 -7.065 23.789 1.00 40.06 O HETATM 3631 O HOH B 973 -0.147 -6.631 12.195 1.00 40.49 O HETATM 3632 O HOH B 974 17.618 -3.070 1.558 1.00 57.57 O HETATM 3633 O HOH B 975 -7.142 -37.339 44.616 1.00 38.10 O HETATM 3634 O HOH B 976 -13.188 -19.967 32.066 1.00 45.51 O HETATM 3635 O HOH B 977 1.953 0.500 2.822 1.00 46.01 O HETATM 3636 O HOH B 978 13.920 3.507 -2.402 1.00 37.18 O HETATM 3637 O HOH B 979 2.085 16.731 15.680 1.00 48.88 O HETATM 3638 O HOH B 980 6.197 -31.162 44.988 1.00 34.17 O HETATM 3639 O HOH B 981 -11.616 4.392 29.480 1.00 38.30 O HETATM 3640 O HOH B 982 0.110 -33.819 42.974 1.00 32.34 O HETATM 3641 O HOH B 983 1.985 -32.898 45.710 1.00 32.12 O HETATM 3642 O HOH B 984 -20.467 -2.916 19.789 1.00 41.18 O HETATM 3643 O HOH B 985 14.020 9.312 -11.181 1.00 46.04 O HETATM 3644 O HOH B 986 22.711 -7.175 -4.198 1.00 45.68 O HETATM 3645 O HOH B 987 -5.407 2.202 44.273 1.00 47.92 O HETATM 3646 O HOH B 988 22.985 -1.736 -13.870 1.00 48.55 O HETATM 3647 O HOH B 989 -24.249 -2.617 22.190 1.00 47.76 O HETATM 3648 O HOH B 990 -12.556 3.766 32.017 1.00 40.26 O HETATM 3649 O HOH B 991 -26.968 -30.843 45.505 1.00 49.61 O HETATM 3650 O HOH B 992 -8.536 -26.626 60.493 1.00 31.77 O HETATM 3651 O HOH B 993 8.071 -30.894 46.985 1.00 53.13 O HETATM 3652 O HOH B 994 7.237 -7.075 17.212 1.00 42.63 O HETATM 3653 O HOH B 995 -13.918 -21.609 28.491 1.00 64.74 O HETATM 3654 O HOH B 996 7.553 -30.430 37.859 1.00 53.83 O HETATM 3655 O HOH B 997 8.853 0.797 -4.807 1.00 36.04 O HETATM 3656 O HOH B 998 4.230 -31.490 48.962 1.00 42.29 O HETATM 3657 O HOH B 999 -25.456 -8.917 27.484 1.00 39.82 O HETATM 3658 O HOH B1000 13.970 5.647 12.114 1.00 51.42 O HETATM 3659 O HOH B1001 -1.945 -5.240 7.842 1.00 49.23 O HETATM 3660 O HOH B1002 1.538 12.390 21.464 1.00 54.05 O HETATM 3661 O HOH B1003 3.436 -35.000 40.701 1.00 57.12 O HETATM 3662 O HOH B1004 -12.566 -3.829 42.465 1.00 33.78 O HETATM 3663 O HOH B1005 4.547 11.044 2.277 1.00 44.72 O HETATM 3664 O HOH B1006 -10.994 -9.762 13.564 1.00 44.43 O HETATM 3665 O HOH B1007 -3.396 -26.876 56.984 1.00 59.51 O HETATM 3666 O HOH B1008 -12.328 -2.660 40.088 1.00 39.40 O HETATM 3667 O HOH B1009 -21.086 -5.246 20.923 1.00 52.26 O HETATM 3668 O HOH B1010 0.811 5.651 -2.031 1.00 51.22 O HETATM 3669 O HOH B1011 -12.790 -2.771 12.688 1.00 36.55 O HETATM 3670 O HOH B1012 -14.959 -8.745 52.479 1.00 24.32 O HETATM 3671 O HOH B1013 25.266 0.642 -9.649 1.00 36.42 O HETATM 3672 O HOH B1014 -2.767 -32.172 35.136 1.00 37.23 O HETATM 3673 O HOH B1015 -2.919 -12.370 24.604 1.00 50.43 O HETATM 3674 O HOH B1016 6.310 -0.445 -4.329 1.00 44.36 O HETATM 3675 O HOH B1017 1.024 -7.891 10.317 1.00 43.77 O HETATM 3676 O HOH B1018 17.441 6.977 -35.674 1.00 35.48 O HETATM 3677 O HOH B1019 -6.505 -37.130 48.315 1.00 42.24 O HETATM 3678 O HOH B1020 7.007 -30.712 33.079 1.00 55.38 O HETATM 3679 O HOH B1021 -20.723 -9.424 48.989 1.00 41.92 O HETATM 3680 O HOH B1022 -24.023 -16.323 35.289 1.00 49.16 O HETATM 3681 O HOH B1023 0.974 -37.861 45.787 1.00 33.54 O HETATM 3682 O HOH B1024 -0.530 -7.288 20.508 1.00 45.46 O HETATM 3683 O HOH B1025 -26.594 -23.296 54.887 1.00 54.30 O HETATM 3684 O HOH B1026 -15.104 4.082 32.934 1.00 55.29 O HETATM 3685 O HOH B1027 -20.509 -7.979 41.820 1.00 35.91 O HETATM 3686 O HOH B1028 -16.099 -33.885 37.118 1.00 44.96 O HETATM 3687 O HOH B1029 -7.975 -29.096 61.202 1.00 48.26 O HETATM 3688 O HOH B1030 19.155 10.899 -17.131 1.00 54.76 O HETATM 3689 O HOH B1031 -3.421 11.340 21.318 1.00 58.75 O HETATM 3690 O HOH B1032 2.579 -18.679 52.871 1.00 57.83 O HETATM 3691 O HOH B1033 -18.893 -30.489 51.803 1.00 49.52 O HETATM 3692 O HOH B1034 -6.294 7.061 4.801 1.00 42.36 O HETATM 3693 O HOH B1035 18.061 -1.245 -22.951 1.00 51.85 O HETATM 3694 O HOH B1036 10.015 4.921 20.494 1.00 46.20 O HETATM 3695 O HOH B1037 8.407 9.231 -4.526 1.00 44.62 O HETATM 3696 O HOH B1038 -11.457 -13.093 33.428 1.00 38.40 O HETATM 3697 O HOH B1039 15.849 7.075 -3.326 1.00 45.11 O HETATM 3698 O HOH B1040 -6.211 -11.543 39.602 1.00 41.09 O HETATM 3699 O HOH B1041 3.166 -14.728 21.995 1.00 51.15 O HETATM 3700 O HOH B1042 -26.888 -6.131 25.168 1.00 58.52 O HETATM 3701 O HOH B1043 -5.240 -39.788 26.244 1.00 55.67 O HETATM 3702 O HOH B1044 4.321 -32.830 37.836 1.00 49.22 O HETATM 3703 O HOH B1045 -10.241 -18.168 32.482 1.00 25.92 O HETATM 3704 O HOH B1046 2.549 -39.980 45.466 1.00 37.06 O HETATM 3705 O HOH B1047 -9.675 -4.257 56.363 1.00 46.39 O HETATM 3706 O HOH B1048 -15.735 1.915 13.906 1.00 37.34 O HETATM 3707 O HOH B1049 7.205 -15.192 1.315 1.00 46.45 O HETATM 3708 O HOH B1050 -1.219 -34.032 51.799 1.00 35.24 O HETATM 3709 O HOH B1051 -15.635 -18.578 32.185 1.00 54.30 O HETATM 3710 O HOH B1052 -11.941 -21.730 26.585 1.00 60.98 O HETATM 3711 O HOH B1053 -11.220 -17.948 28.542 1.00 56.40 O HETATM 3712 O HOH B1054 27.099 -3.670 0.922 1.00 56.02 O HETATM 3713 O HOH B1055 -25.146 -28.985 54.220 1.00 45.50 O HETATM 3714 O HOH B1056 -21.323 -22.517 60.676 1.00 46.79 O HETATM 3715 O HOH B1057 -19.109 -10.419 16.612 1.00 46.35 O HETATM 3716 O HOH B1058 13.050 3.386 13.167 1.00 55.34 O HETATM 3717 O HOH B1059 -24.079 3.052 31.248 1.00 50.46 O HETATM 3718 O HOH B1060 -23.286 -10.925 53.347 1.00 51.19 O HETATM 3719 O HOH B1061 -19.510 -13.124 61.543 1.00 56.56 O HETATM 3720 O HOH B1062 1.446 -1.760 31.924 1.00 48.55 O HETATM 3721 O HOH B1063 -6.890 -28.262 54.789 1.00 53.03 O HETATM 3722 O HOH B1064 -19.185 -15.709 29.712 1.00 53.46 O HETATM 3723 O HOH B1065 23.256 -10.889 -1.899 1.00 31.34 O HETATM 3724 O HOH B1066 5.324 -23.966 47.019 1.00 45.92 O HETATM 3725 O HOH B1067 -2.257 -1.181 28.863 1.00 41.21 O HETATM 3726 O HOH B1068 9.606 5.096 -6.484 1.00 44.81 O HETATM 3727 O HOH B1069 -17.442 2.716 32.006 1.00 39.57 O HETATM 3728 O HOH B1070 -9.981 -15.224 31.379 1.00 52.37 O HETATM 3729 O HOH B1071 -4.117 -34.665 51.373 1.00 47.36 O HETATM 3730 O HOH B1072 -1.669 7.526 31.848 1.00 66.71 O HETATM 3731 O HOH B1073 17.704 5.738 -1.911 1.00 38.75 O HETATM 3732 O HOH B1074 -0.440 14.788 19.449 1.00 43.91 O HETATM 3733 O HOH B1075 -11.981 -38.145 27.572 1.00 54.07 O HETATM 3734 O HOH B1076 -5.002 -26.142 58.940 1.00 61.74 O HETATM 3735 O HOH B1077 -24.267 -16.180 47.290 1.00 39.72 O HETATM 3736 O HOH B1078 3.175 -35.066 44.912 1.00 51.98 O HETATM 3737 O HOH B1079 -20.508 -6.431 45.786 1.00 48.67 O HETATM 3738 O HOH B1080 18.757 3.974 2.609 1.00 55.00 O HETATM 3739 O HOH B1081 7.904 -5.676 14.400 1.00 44.34 O HETATM 3740 O HOH B1082 -5.127 10.721 23.374 1.00 46.20 O HETATM 3741 O HOH B1083 -10.934 -33.464 44.821 1.00 63.82 O HETATM 3742 O HOH B1084 -9.242 -0.115 41.490 1.00 57.10 O HETATM 3743 O HOH B1085 -31.236 -26.038 52.625 1.00 67.49 O HETATM 3744 O HOH B1086 -24.902 -28.674 40.457 1.00 47.85 O HETATM 3745 O HOH B1087 -1.130 -0.430 32.695 1.00 49.93 O HETATM 3746 O HOH B1088 -5.793 -28.270 57.245 1.00 60.52 O HETATM 3747 O HOH B1089 -23.685 -2.938 39.936 1.00 46.52 O HETATM 3748 O HOH B1090 11.260 8.124 18.364 1.00 50.48 O HETATM 3749 O HOH B1091 -19.457 -37.864 36.093 1.00 52.65 O HETATM 3750 O HOH B1092 9.765 -28.347 37.637 1.00 55.09 O HETATM 3751 O HOH B1093 -4.920 -0.459 33.245 1.00 54.90 O HETATM 3752 O HOH B1094 3.110 -22.004 52.979 1.00 57.12 O HETATM 3753 O HOH B1095 1.064 7.271 33.386 1.00 54.39 O HETATM 3754 O HOH B1096 12.407 -3.328 14.728 1.00 55.19 O HETATM 3755 O HOH B1097 0.141 -36.714 48.191 1.00 41.62 O HETATM 3756 O HOH B1098 -13.718 -30.367 40.847 1.00 57.95 O HETATM 3757 O HOH B1099 -19.410 0.412 36.957 1.00 37.61 O HETATM 3758 O HOH B1100 9.464 -16.193 25.531 1.00 56.32 O HETATM 3759 O HOH B1101 -12.034 -32.237 39.032 1.00 35.97 O HETATM 3760 O HOH B1102 3.083 -23.491 50.834 1.00 39.85 O HETATM 3761 O HOH B1103 -5.179 6.989 26.456 1.00 45.87 O HETATM 3762 O HOH B1104 3.531 -25.674 27.640 1.00 46.04 O HETATM 3763 O HOH B1105 -7.443 2.972 46.446 1.00 47.08 O HETATM 3764 O HOH B1106 -9.771 -17.176 60.369 1.00 60.85 O HETATM 3765 O HOH B1107 -16.835 -29.420 61.272 1.00 49.73 O HETATM 3766 O HOH B1108 -21.325 -19.356 60.897 1.00 52.73 O HETATM 3767 O HOH B1109 0.329 -33.114 30.432 1.00 49.84 O HETATM 3768 O HOH B1110 10.665 -7.594 4.618 1.00 53.41 O HETATM 3769 O HOH B1111 6.068 -19.489 48.013 1.00 71.92 O HETATM 3770 O HOH B1112 -21.662 -5.513 43.516 1.00 56.16 O HETATM 3771 O HOH B1113 -23.297 -0.287 23.300 1.00 55.66 O HETATM 3772 O HOH B1114 -18.324 -18.406 34.896 1.00 56.56 O HETATM 3773 O HOH B1115 -8.720 -8.728 28.468 1.00 51.74 O HETATM 3774 O HOH B1116 -8.022 11.879 9.705 1.00 56.06 O HETATM 3775 O HOH B1117 -24.122 -11.084 49.849 1.00 57.96 O HETATM 3776 O HOH B1118 6.634 -32.138 42.591 1.00 60.42 O HETATM 3777 O HOH B1119 3.952 -16.470 47.472 1.00 50.37 O HETATM 3778 O HOH B1120 3.401 -6.384 9.256 1.00 59.02 O HETATM 3779 O HOH B1121 -15.489 6.646 31.545 1.00 67.74 O HETATM 3780 O HOH B1122 -13.327 -15.139 62.832 1.00 57.55 O CONECT 134 3458 CONECT 163 3458 CONECT 184 3458 CONECT 232 3458 CONECT 233 3458 CONECT 2589 3455 CONECT 2639 3457 CONECT 2671 3457 CONECT 2680 3457 CONECT 2700 3457 CONECT 2720 3457 CONECT 2721 3457 CONECT 3179 3456 CONECT 3208 3456 CONECT 3222 3456 CONECT 3316 3455 CONECT 3324 3456 CONECT 3338 3455 CONECT 3339 3455 CONECT 3455 3316 3543 3338 2589 CONECT 3455 3339 3466 3497 CONECT 3456 3324 3459 3644 3179 CONECT 3456 3208 3222 CONECT 3457 2639 2671 2680 2700 CONECT 3457 2720 2721 CONECT 3458 184 232 134 233 CONECT 3458 163 CONECT 3459 3456 CONECT 3466 3455 CONECT 3497 3455 CONECT 3543 3455 CONECT 3644 3456 END If you find results from this site helpful for your research, please cite one of our papers:
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