HEADER SIGNALING PROTEIN/ANTAGONIST 15-JUN-15 5C1M TITLE CRYSTAL STRUCTURE OF ACTIVE MU-OPIOID RECEPTOR BOUND TO THE AGONIST TITLE 2 BU72 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MU-TYPE OPIOID RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MOR-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY 39; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: OPRM1, MOR, OPRM; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LIGANDS, MICE, AGONISTS, MORPHINANS, ACTIVATION, RECEPTORS, OPIOID, KEYWDS 2 MU, NANOBODY, SIGNALING PROTEIN-ANTAGONIST COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.J.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS,E.N.FEINBERG, AUTHOR 2 A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON,T.S.THORSEN,R.KLING,S.GRANIER, AUTHOR 3 P.GMEINER,S.M.HUSBANDS,J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR, AUTHOR 4 B.K.KOBILKA REVDAT 7 10-FEB-21 5C1M 1 COMPND REMARK HET HETNAM REVDAT 7 2 1 HETSYN FORMUL HELIX SHEET REVDAT 7 3 1 SSBOND LINK SITE CRYST1 REVDAT 7 4 1 ATOM REVDAT 6 11-DEC-19 5C1M 1 REMARK REVDAT 5 06-SEP-17 5C1M 1 JRNL REMARK REVDAT 4 02-SEP-15 5C1M 1 JRNL REVDAT 3 26-AUG-15 5C1M 1 REMARK REVDAT 2 19-AUG-15 5C1M 1 JRNL REVDAT 1 05-AUG-15 5C1M 0 JRNL AUTH W.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS, JRNL AUTH 2 E.N.FEINBERG,A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON, JRNL AUTH 3 T.S.THORSEN,R.C.KLING,S.GRANIER,P.GMEINER,S.M.HUSBANDS, JRNL AUTH 4 J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR,B.K.KOBILKA JRNL TITL STRUCTURAL INSIGHTS INTO MU-OPIOID RECEPTOR ACTIVATION. JRNL REF NATURE V. 524 315 2015 JRNL REFN ESSN 1476-4687 JRNL PMID 26245379 JRNL DOI 10.1038/NATURE14886 REMARK 2 REMARK 2 RESOLUTION. 2.07 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1_3660 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 41704 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2086 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 43.4700 - 5.1000 0.99 2808 148 0.2027 0.2347 REMARK 3 2 5.1000 - 4.0500 0.99 2680 141 0.1858 0.2210 REMARK 3 3 4.0500 - 3.5400 1.00 2688 142 0.1911 0.1991 REMARK 3 4 3.5400 - 3.2200 1.00 2641 139 0.1999 0.2371 REMARK 3 5 3.2200 - 2.9900 1.00 2645 139 0.1945 0.2277 REMARK 3 6 2.9900 - 2.8100 1.00 2623 138 0.1883 0.2252 REMARK 3 7 2.8100 - 2.6700 1.00 2650 140 0.1776 0.2023 REMARK 3 8 2.6700 - 2.5500 1.00 2619 138 0.1863 0.2225 REMARK 3 9 2.5500 - 2.4500 1.00 2599 136 0.1966 0.2425 REMARK 3 10 2.4500 - 2.3700 1.00 2634 139 0.2115 0.2623 REMARK 3 11 2.3700 - 2.3000 1.00 2617 138 0.2230 0.2516 REMARK 3 12 2.3000 - 2.2300 1.00 2571 135 0.2318 0.2856 REMARK 3 13 2.2300 - 2.1700 1.00 2621 138 0.2509 0.2729 REMARK 3 14 2.1700 - 2.1200 1.00 2569 135 0.2599 0.2585 REMARK 3 15 2.1200 - 2.0700 1.00 2653 140 0.2931 0.3353 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.253 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.048 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.71 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 3513 REMARK 3 ANGLE : 0.690 4790 REMARK 3 CHIRALITY : 0.047 560 REMARK 3 PLANARITY : 0.004 571 REMARK 3 DIHEDRAL : 14.260 1400 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 16 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 64 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.5891 22.6057 -71.1536 REMARK 3 T TENSOR REMARK 3 T11: 1.4149 T22: 0.9370 REMARK 3 T33: 1.0244 T12: 0.1781 REMARK 3 T13: -0.2471 T23: 0.1495 REMARK 3 L TENSOR REMARK 3 L11: 0.0060 L22: 0.0117 REMARK 3 L33: -0.0034 L12: -0.0149 REMARK 3 L13: 0.0054 L23: -0.0002 REMARK 3 S TENSOR REMARK 3 S11: 0.3028 S12: 0.3913 S13: 0.4062 REMARK 3 S21: -1.5315 S22: -0.8949 S23: 0.5507 REMARK 3 S31: -0.8561 S32: 0.0878 S33: 0.5554 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 95 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.2398 30.2151 -48.4470 REMARK 3 T TENSOR REMARK 3 T11: 0.5628 T22: 0.2601 REMARK 3 T33: 0.5140 T12: -0.0099 REMARK 3 T13: -0.0596 T23: -0.0198 REMARK 3 L TENSOR REMARK 3 L11: 3.1013 L22: 3.2198 REMARK 3 L33: 8.0669 L12: 0.3273 REMARK 3 L13: 2.9077 L23: -0.5687 REMARK 3 S TENSOR REMARK 3 S11: -0.5399 S12: 0.1773 S13: 0.4895 REMARK 3 S21: -0.0861 S22: -0.0706 S23: -0.0475 REMARK 3 S31: -1.3043 S32: 0.2895 S33: 0.6762 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 96 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.0657 16.6333 -44.1704 REMARK 3 T TENSOR REMARK 3 T11: 0.3192 T22: 0.2630 REMARK 3 T33: 0.3367 T12: -0.0254 REMARK 3 T13: -0.0213 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 1.3828 L22: 2.6820 REMARK 3 L33: 4.0029 L12: 0.8204 REMARK 3 L13: -0.9788 L23: -1.0480 REMARK 3 S TENSOR REMARK 3 S11: -0.0634 S12: -0.0164 S13: 0.1631 REMARK 3 S21: -0.0691 S22: 0.0875 S23: -0.1017 REMARK 3 S31: -0.4743 S32: 0.0467 S33: 0.0059 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 211 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.8718 11.2197 -49.9976 REMARK 3 T TENSOR REMARK 3 T11: 0.2869 T22: 0.3015 REMARK 3 T33: 0.4301 T12: -0.0028 REMARK 3 T13: 0.0533 T23: -0.0456 REMARK 3 L TENSOR REMARK 3 L11: 2.7531 L22: 1.8425 REMARK 3 L33: 8.9793 L12: 0.1796 REMARK 3 L13: -1.1970 L23: 0.0508 REMARK 3 S TENSOR REMARK 3 S11: 0.1032 S12: 0.0509 S13: -0.0446 REMARK 3 S21: -0.1784 S22: -0.0122 S23: -0.2427 REMARK 3 S31: -0.4123 S32: 0.1724 S33: -0.0400 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 241 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.8969 7.5274 -63.8304 REMARK 3 T TENSOR REMARK 3 T11: 0.5378 T22: 0.3389 REMARK 3 T33: 0.2828 T12: -0.0556 REMARK 3 T13: -0.0062 T23: 0.0046 REMARK 3 L TENSOR REMARK 3 L11: 3.7710 L22: 2.6801 REMARK 3 L33: 1.8496 L12: -0.1972 REMARK 3 L13: -0.3744 L23: 0.7723 REMARK 3 S TENSOR REMARK 3 S11: -0.0020 S12: 0.1045 S13: 0.0363 REMARK 3 S21: -0.1801 S22: -0.1025 S23: 0.0251 REMARK 3 S31: -1.0530 S32: 0.2528 S33: 0.0930 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 242 THROUGH 267 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.7318 3.1503 -33.5235 REMARK 3 T TENSOR REMARK 3 T11: 0.3483 T22: 0.4357 REMARK 3 T33: 0.4408 T12: 0.0253 REMARK 3 T13: 0.0048 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 2.3875 L22: 4.4261 REMARK 3 L33: 7.5216 L12: 0.4843 REMARK 3 L13: 0.4549 L23: -0.1986 REMARK 3 S TENSOR REMARK 3 S11: -0.2308 S12: -0.3768 S13: -0.2054 REMARK 3 S21: 0.1917 S22: -0.0009 S23: 0.2801 REMARK 3 S31: 0.2651 S32: -0.8508 S33: 0.1903 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 268 THROUGH 311 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.3365 12.7969 -48.9402 REMARK 3 T TENSOR REMARK 3 T11: 0.2376 T22: 0.2754 REMARK 3 T33: 0.3915 T12: 0.0346 REMARK 3 T13: -0.0663 T23: -0.0207 REMARK 3 L TENSOR REMARK 3 L11: 3.1989 L22: 3.2274 REMARK 3 L33: 4.7548 L12: -0.1670 REMARK 3 L13: -0.4240 L23: 0.9065 REMARK 3 S TENSOR REMARK 3 S11: 0.0121 S12: -0.2381 S13: -0.0726 REMARK 3 S21: -0.2136 S22: -0.1219 S23: 0.2198 REMARK 3 S31: -1.1015 S32: -0.1917 S33: 0.0825 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 312 THROUGH 347 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.3435 22.0563 -46.4059 REMARK 3 T TENSOR REMARK 3 T11: 0.4761 T22: 0.2846 REMARK 3 T33: 0.4341 T12: 0.0369 REMARK 3 T13: -0.0269 T23: 0.0023 REMARK 3 L TENSOR REMARK 3 L11: 3.4697 L22: 2.6680 REMARK 3 L33: 2.0100 L12: 0.0381 REMARK 3 L13: -0.0602 L23: -1.4810 REMARK 3 S TENSOR REMARK 3 S11: 0.0284 S12: -0.1886 S13: 0.1845 REMARK 3 S21: 0.0969 S22: 0.3256 S23: 0.0630 REMARK 3 S31: -0.6201 S32: -0.0427 S33: -0.2463 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.4486 3.9078 -5.1278 REMARK 3 T TENSOR REMARK 3 T11: 0.6782 T22: 1.0219 REMARK 3 T33: 0.4988 T12: -0.0879 REMARK 3 T13: 0.1389 T23: -0.0516 REMARK 3 L TENSOR REMARK 3 L11: 4.6372 L22: 8.0480 REMARK 3 L33: 4.5779 L12: -5.7587 REMARK 3 L13: -3.1603 L23: 2.4421 REMARK 3 S TENSOR REMARK 3 S11: -0.7480 S12: -1.6370 S13: -0.8629 REMARK 3 S21: 0.8400 S22: 0.0511 S23: 0.9206 REMARK 3 S31: 0.3766 S32: -1.0408 S33: 0.6809 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 19 ) REMARK 3 ORIGIN FOR THE GROUP (A): 10.4005 2.6080 -8.6559 REMARK 3 T TENSOR REMARK 3 T11: 0.5308 T22: 1.2515 REMARK 3 T33: 0.5907 T12: 0.1796 REMARK 3 T13: -0.0319 T23: -0.0104 REMARK 3 L TENSOR REMARK 3 L11: 4.5026 L22: 5.8531 REMARK 3 L33: 1.9206 L12: 5.1320 REMARK 3 L13: -1.2400 L23: -1.3171 REMARK 3 S TENSOR REMARK 3 S11: 0.2846 S12: -0.0241 S13: -1.6935 REMARK 3 S21: -0.0163 S22: -0.1807 S23: -0.6660 REMARK 3 S31: 0.6751 S32: 1.9366 S33: -0.2132 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 30 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.2361 1.9030 -11.6962 REMARK 3 T TENSOR REMARK 3 T11: 0.4557 T22: 0.7102 REMARK 3 T33: 0.7206 T12: -0.0006 REMARK 3 T13: 0.0638 T23: 0.0848 REMARK 3 L TENSOR REMARK 3 L11: 9.8419 L22: 4.7221 REMARK 3 L33: 4.9911 L12: -0.8418 REMARK 3 L13: -2.4360 L23: 0.4217 REMARK 3 S TENSOR REMARK 3 S11: 0.5188 S12: -0.0506 S13: -0.8622 REMARK 3 S21: 0.6608 S22: -0.1890 S23: 1.2019 REMARK 3 S31: 0.2478 S32: -0.8319 S33: -0.2978 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.4457 11.4887 -10.7871 REMARK 3 T TENSOR REMARK 3 T11: 0.3459 T22: 0.6991 REMARK 3 T33: 0.2118 T12: 0.0475 REMARK 3 T13: -0.0002 T23: -0.0944 REMARK 3 L TENSOR REMARK 3 L11: 2.5958 L22: 4.2995 REMARK 3 L33: 2.3041 L12: 0.3775 REMARK 3 L13: -0.8360 L23: -0.5040 REMARK 3 S TENSOR REMARK 3 S11: 0.2115 S12: -1.6132 S13: 0.3036 REMARK 3 S21: 0.2319 S22: -0.4213 S23: 0.1600 REMARK 3 S31: -0.6267 S32: -0.9913 S33: 0.2115 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 40 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.9366 17.4698 -8.0685 REMARK 3 T TENSOR REMARK 3 T11: 0.7108 T22: 0.7285 REMARK 3 T33: 0.5553 T12: -0.0264 REMARK 3 T13: -0.0924 T23: -0.1922 REMARK 3 L TENSOR REMARK 3 L11: 7.9923 L22: 3.8306 REMARK 3 L33: 4.1181 L12: 1.9293 REMARK 3 L13: 5.5580 L23: 2.2469 REMARK 3 S TENSOR REMARK 3 S11: -0.4369 S12: -1.4584 S13: 1.6318 REMARK 3 S21: 0.8269 S22: -0.3606 S23: -0.0019 REMARK 3 S31: -0.4863 S32: -0.5620 S33: 0.7491 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 73 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.0909 11.6223 -20.5209 REMARK 3 T TENSOR REMARK 3 T11: 0.4543 T22: 0.5188 REMARK 3 T33: 0.3366 T12: 0.0161 REMARK 3 T13: 0.0409 T23: -0.0111 REMARK 3 L TENSOR REMARK 3 L11: 3.2477 L22: 3.9858 REMARK 3 L33: 5.8077 L12: -0.6185 REMARK 3 L13: 2.0907 L23: 1.3572 REMARK 3 S TENSOR REMARK 3 S11: -0.2209 S12: 0.0845 S13: 0.2728 REMARK 3 S21: -0.1136 S22: -0.1570 S23: 0.0891 REMARK 3 S31: -0.4519 S32: 0.0330 S33: 0.3518 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 74 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.2438 3.1689 -16.7487 REMARK 3 T TENSOR REMARK 3 T11: 0.3699 T22: 0.5660 REMARK 3 T33: 0.3249 T12: -0.0754 REMARK 3 T13: 0.0545 T23: -0.0120 REMARK 3 L TENSOR REMARK 3 L11: 4.9126 L22: 2.9980 REMARK 3 L33: 4.3866 L12: -0.3547 REMARK 3 L13: 0.7290 L23: 0.0016 REMARK 3 S TENSOR REMARK 3 S11: 0.1583 S12: -1.2029 S13: -0.1933 REMARK 3 S21: 0.0645 S22: -0.3439 S23: -0.0090 REMARK 3 S31: 0.4944 S32: -0.3991 S33: 0.1944 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 127 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.2932 10.2307 -7.4414 REMARK 3 T TENSOR REMARK 3 T11: 0.3739 T22: 0.7268 REMARK 3 T33: 0.3089 T12: -0.0017 REMARK 3 T13: -0.0189 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 8.3032 L22: 3.2579 REMARK 3 L33: 4.5278 L12: 0.3011 REMARK 3 L13: 0.2393 L23: 0.5296 REMARK 3 S TENSOR REMARK 3 S11: -0.1699 S12: -0.1189 S13: 0.5013 REMARK 3 S21: 0.1838 S22: -0.0583 S23: -0.0232 REMARK 3 S31: -0.5458 S32: 0.1071 S33: 0.1972 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 5C1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-15. REMARK 100 THE DEPOSITION ID IS D_1000210873. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 7.0-7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41704 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070 REMARK 200 RESOLUTION RANGE LOW (A) : 43.470 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 8.600 REMARK 200 R MERGE (I) : 0.11200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.53600 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4DKL, 3P0G REMARK 200 REMARK 200 REMARK: CUBIC REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: RECONSTITUTED IN 10:1 REMARK 280 MONOOLEIN:CHOLESTEROL MIX. PRECIPITANT SOLUTION:15-25% PEG300, REMARK 280 100 MM HEPES PH 7.0-7.5, 1% 1,2,3-HEPTANETRIOL, 0.5-1.0% REMARK 280 POLYPROPYLENE GLYCOL P 400, 100-300 MM (NH4)2HPO4, PH 7.5, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y,-Z REMARK 290 8555 X,-Y,-Z+1/2 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 22.21500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 104.95000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 104.95000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLY B 103 REMARK 465 GLN B 104 REMARK 465 SER B 105 REMARK 465 SER B 106 REMARK 465 SER B 107 REMARK 465 PRO B 108 REMARK 465 TYR B 109 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 269 CG CD CE NZ REMARK 470 GLU A 270 CG CD OE1 OE2 REMARK 470 ARG A 273 CG CD NE CZ NH1 NH2 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 HIS A 54 -88.98 -131.93 REMARK 500 PRO A 58 97.19 -60.26 REMARK 500 THR A 60 128.41 -37.40 REMARK 500 ARG A 179 44.86 -92.61 REMARK 500 PHE A 241 -60.00 -126.81 REMARK 500 LEU A 265 -12.61 -43.91 REMARK 500 SER A 266 -76.91 -122.79 REMARK 500 ARG B 29 16.27 57.12 REMARK 500 MET B 34 -9.39 -141.20 REMARK 500 VAL B 48 -60.89 -109.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 401 REMARK 610 OLC A 402 REMARK 610 P6G A 406 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4DKL RELATED DB: PDB REMARK 900 4DKL CONTAINS THE SAME PROTEIN BOUND TO A MORPHINAN ANTAGONIST DBREF 5C1M A 52 347 UNP P42866 OPRM_MOUSE 52 347 DBREF 5C1M B 3 127 PDB 5C1M 5C1M 3 127 SEQRES 1 A 296 GLY SER HIS SER LEU YCM PRO GLN THR GLY SER PRO SER SEQRES 2 A 296 MET VAL THR ALA ILE THR ILE MET ALA LEU TYR SER ILE SEQRES 3 A 296 VAL CYS VAL VAL GLY LEU PHE GLY ASN PHE LEU VAL MET SEQRES 4 A 296 TYR VAL ILE VAL ARG TYR THR LYS MET LYS THR ALA THR SEQRES 5 A 296 ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU SEQRES 6 A 296 ALA THR SER THR LEU PRO PHE GLN SER VAL ASN TYR LEU SEQRES 7 A 296 MET GLY THR TRP PRO PHE GLY ASN ILE LEU CYS LYS ILE SEQRES 8 A 296 VAL ILE SER ILE ASP TYR TYR ASN MET PHE THR SER ILE SEQRES 9 A 296 PHE THR LEU CYS THR MET SER VAL ASP ARG TYR ILE ALA SEQRES 10 A 296 VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO SEQRES 11 A 296 ARG ASN ALA LYS ILE VAL ASN VAL CYS ASN TRP ILE LEU SEQRES 12 A 296 SER SER ALA ILE GLY LEU PRO VAL MET PHE MET ALA THR SEQRES 13 A 296 THR LYS TYR ARG GLN GLY SER ILE ASP CYS THR LEU THR SEQRES 14 A 296 PHE SER HIS PRO THR TRP TYR TRP GLU ASN LEU LEU LYS SEQRES 15 A 296 ILE CYS VAL PHE ILE PHE ALA PHE ILE MET PRO VAL LEU SEQRES 16 A 296 ILE ILE THR VAL CYS TYR GLY LEU MET ILE LEU ARG LEU SEQRES 17 A 296 LYS SER VAL ARG MET LEU SER GLY SER LYS GLU LYS ASP SEQRES 18 A 296 ARG ASN LEU ARG ARG ILE THR ARG MET VAL LEU VAL VAL SEQRES 19 A 296 VAL ALA VAL PHE ILE VAL CYS TRP THR PRO ILE HIS ILE SEQRES 20 A 296 TYR VAL ILE ILE LYS ALA LEU ILE THR ILE PRO GLU THR SEQRES 21 A 296 THR PHE GLN THR VAL SER TRP HIS PHE CYS ILE ALA LEU SEQRES 22 A 296 GLY TYR THR ASN SER CYS LEU ASN PRO VAL LEU TYR ALA SEQRES 23 A 296 PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE SEQRES 1 B 125 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL ARG SEQRES 2 B 125 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP SER GLU SEQRES 3 B 125 ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG ALA PRO SEQRES 4 B 125 GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR TRP SER SEQRES 5 B 125 GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA ASP ARG SEQRES 6 B 125 PHE THR THR SER ARG ASP VAL ALA ASN ASN THR LEU TYR SEQRES 7 B 125 LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR ALA VAL SEQRES 8 B 125 TYR TYR CYS ALA ALA ARG ALA PRO VAL GLY GLN SER SER SEQRES 9 B 125 SER PRO TYR ASP TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 B 125 VAL THR VAL SER SER ALA ALA ALA MODRES 5C1M YCM A 57 CYS MODIFIED RESIDUE HET YCM A 57 10 HET OLC A 401 16 HET OLC A 402 18 HET CLR A 403 28 HET PO4 A 404 5 HET P6G A 405 19 HET P6G A 406 13 HET VF1 A 407 32 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CLR CHOLESTEROL HETNAM PO4 PHOSPHATE ION HETNAM P6G HEXAETHYLENE GLYCOL HETNAM VF1 (2R,3S,3AR,5AR,6R,11BR,11CS)-3A-METHOXY-3,14-DIMETHYL- HETNAM 2 VF1 2-PHENYL-2,3,3A,6,7,11C-HEXAHYDRO-1H-6,11B- HETNAM 3 VF1 (EPIMINOETHANO)-3,5A-METHANONAPHTHO[2,1-G]INDOL-10-OL HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN P6G POLYETHYLENE GLYCOL PEG400 HETSYN VF1 BU72 FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 3 OLC 2(C21 H40 O4) FORMUL 5 CLR C27 H46 O FORMUL 6 PO4 O4 P 3- FORMUL 7 P6G 2(C12 H26 O7) FORMUL 9 VF1 C28 H32 N2 O2 FORMUL 10 HOH *94(H2 O) HELIX 1 AA1 SER A 64 TYR A 96 1 33 HELIX 2 AA2 THR A 101 SER A 119 1 19 HELIX 3 AA3 THR A 120 MET A 130 1 11 HELIX 4 AA4 PHE A 135 HIS A 171 1 37 HELIX 5 AA5 HIS A 171 ARG A 179 1 9 HELIX 6 AA6 THR A 180 MET A 205 1 26 HELIX 7 AA7 PRO A 224 PHE A 241 1 18 HELIX 8 AA8 PHE A 241 VAL A 262 1 22 HELIX 9 AA9 GLY A 267 ILE A 306 1 40 HELIX 10 AB1 THR A 311 ALA A 337 1 27 HELIX 11 AB2 ASP A 340 PHE A 347 1 8 HELIX 12 AB3 LYS B 87 THR B 91 5 5 SHEET 1 AA1 2 ALA A 206 ARG A 211 0 SHEET 2 AA1 2 SER A 214 LEU A 219 -1 O SER A 214 N ARG A 211 SHEET 1 AA2 4 VAL B 7 SER B 9 0 SHEET 2 AA2 4 LEU B 20 VAL B 25 -1 O SER B 23 N SER B 9 SHEET 3 AA2 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 20 SHEET 4 AA2 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA3 6 GLY B 12 VAL B 14 0 SHEET 2 AA3 6 THR B 118 VAL B 122 1 O THR B 121 N GLY B 12 SHEET 3 AA3 6 ALA B 92 ARG B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AA3 6 TYR B 32 ARG B 39 -1 N PHE B 37 O TYR B 95 SHEET 5 AA3 6 ARG B 45 ILE B 51 -1 O ALA B 49 N TRP B 36 SHEET 6 AA3 6 PRO B 58 TYR B 60 -1 O THR B 59 N SER B 50 SHEET 1 AA4 4 GLY B 12 VAL B 14 0 SHEET 2 AA4 4 THR B 118 VAL B 122 1 O THR B 121 N GLY B 12 SHEET 3 AA4 4 ALA B 92 ARG B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AA4 4 TYR B 113 TRP B 114 -1 O TYR B 113 N ALA B 98 SSBOND 1 CYS A 140 CYS A 217 1555 1555 2.04 SSBOND 2 CYS B 24 CYS B 96 1555 1555 2.04 LINK C LEU A 56 N YCM A 57 1555 1555 1.33 LINK C YCM A 57 N PRO A 58 1555 1555 1.34 CISPEP 1 HIS A 223 PRO A 224 0 -6.96 CRYST1 44.430 144.000 209.900 90.00 90.00 90.00 I 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.022507 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006944 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004764 0.00000 ATOM 1 N GLY A 52 5.641 11.638 -72.150 1.00110.27 N ANISOU 1 N GLY A 52 15893 14217 11786 1077 -83 2692 N ATOM 2 CA GLY A 52 4.612 11.828 -71.143 1.00107.88 C ANISOU 2 CA GLY A 52 15251 13888 11852 1017 -270 2367 C ATOM 3 C GLY A 52 4.546 13.235 -70.580 1.00106.83 C ANISOU 3 C GLY A 52 15153 13592 11847 887 -304 2406 C ATOM 4 O GLY A 52 5.549 13.777 -70.112 1.00102.57 O ANISOU 4 O GLY A 52 14605 13098 11270 631 -18 2670 O ATOM 5 N SER A 53 3.355 13.827 -70.628 1.00107.33 N ANISOU 5 N SER A 53 15257 13463 12061 1066 -657 2141 N ATOM 6 CA SER A 53 3.135 15.162 -70.092 1.00107.30 C ANISOU 6 CA SER A 53 15277 13290 12201 967 -731 2137 C ATOM 7 C SER A 53 2.948 15.108 -68.582 1.00 97.40 C ANISOU 7 C SER A 53 13536 12160 11311 680 -633 1978 C ATOM 8 O SER A 53 2.361 14.167 -68.040 1.00101.33 O ANISOU 8 O SER A 53 13690 12794 12016 669 -691 1723 O ATOM 9 CB SER A 53 1.909 15.811 -70.737 1.00110.90 C ANISOU 9 CB SER A 53 15967 13492 12679 1275 -1154 1909 C ATOM 10 OG SER A 53 1.500 16.956 -70.006 1.00113.32 O ANISOU 10 OG SER A 53 16198 13659 13200 1166 -1250 1829 O ATOM 11 N HIS A 54 3.451 16.137 -67.902 1.00 90.90 N ANISOU 11 N HIS A 54 12685 11287 10565 447 -485 2130 N ATOM 12 CA HIS A 54 3.338 16.212 -66.450 1.00 84.22 C ANISOU 12 CA HIS A 54 11393 10548 10059 160 -380 2003 C ATOM 13 C HIS A 54 2.840 17.587 -66.021 1.00 72.09 C ANISOU 13 C HIS A 54 9906 8804 8681 124 -541 1937 C ATOM 14 O HIS A 54 1.631 17.799 -65.885 1.00 72.61 O ANISOU 14 O HIS A 54 9896 8749 8943 273 -861 1629 O ATOM 15 CB HIS A 54 4.683 15.896 -65.790 1.00 68.93 C ANISOU 15 CB HIS A 54 9277 8829 8086 -174 59 2283 C ATOM 16 CG HIS A 54 4.575 15.537 -64.341 1.00 69.90 C ANISOU 16 CG HIS A 54 8888 9120 8548 -455 188 2128 C ATOM 17 ND1 HIS A 54 4.056 14.335 -63.909 1.00 64.07 N ANISOU 17 ND1 HIS A 54 7805 8553 7985 -449 152 1880 N ATOM 18 CD2 HIS A 54 4.914 16.223 -63.225 1.00 64.69 C ANISOU 18 CD2 HIS A 54 8004 8486 8088 -749 351 2183 C ATOM 19 CE1 HIS A 54 4.081 14.296 -62.590 1.00 61.68 C ANISOU 19 CE1 HIS A 54 7089 8374 7974 -727 287 1790 C ATOM 20 NE2 HIS A 54 4.601 15.427 -62.150 1.00 66.20 N ANISOU 20 NE2 HIS A 54 7724 8861 8567 -914 411 1971 N ATOM 21 N SER A 55 3.764 18.526 -65.803 1.00 72.40 N ANISOU 21 N SER A 55 10070 8803 8636 -74 -320 2225 N ATOM 22 CA SER A 55 3.367 19.877 -65.424 1.00 79.19 C ANISOU 22 CA SER A 55 10996 9463 9629 -114 -458 2188 C ATOM 23 C SER A 55 2.828 20.654 -66.618 1.00 85.33 C ANISOU 23 C SER A 55 12234 9978 10210 204 -756 2186 C ATOM 24 O SER A 55 1.866 21.419 -66.481 1.00 86.66 O ANISOU 24 O SER A 55 12424 9965 10539 307 -1039 1979 O ATOM 25 CB SER A 55 4.548 20.619 -64.796 1.00 81.52 C ANISOU 25 CB SER A 55 11272 9804 9898 -433 -120 2500 C ATOM 26 OG SER A 55 5.516 20.960 -65.776 1.00 87.70 O ANISOU 26 OG SER A 55 12463 10532 10326 -378 27 2844 O ATOM 27 N LEU A 56 3.432 20.473 -67.787 1.00 84.34 N ANISOU 27 N LEU A 56 12477 9828 9741 360 -698 2413 N ATOM 28 CA LEU A 56 2.998 21.175 -68.987 1.00 84.78 C ANISOU 28 CA LEU A 56 12988 9639 9585 665 -965 2434 C ATOM 29 C LEU A 56 1.677 20.625 -69.503 1.00 85.67 C ANISOU 29 C LEU A 56 13106 9676 9767 978 -1340 2090 C ATOM 30 O LEU A 56 1.599 19.481 -69.951 1.00 83.26 O ANISOU 30 O LEU A 56 12762 9493 9378 1101 -1346 2024 O ATOM 31 CB LEU A 56 4.061 21.083 -70.081 1.00 85.66 C ANISOU 31 CB LEU A 56 13483 9758 9305 736 -781 2781 C ATOM 32 CG LEU A 56 3.731 21.780 -71.404 1.00 87.52 C ANISOU 32 CG LEU A 56 14218 9750 9288 1051 -1032 2837 C ATOM 33 CD1 LEU A 56 3.492 23.265 -71.184 1.00 87.52 C ANISOU 33 CD1 LEU A 56 14362 9530 9362 1018 -1149 2861 C ATOM 34 CD2 LEU A 56 4.838 21.561 -72.420 1.00 90.95 C ANISOU 34 CD2 LEU A 56 14994 10220 9342 1102 -822 3182 C HETATM 35 N YCM A 57 0.642 21.453 -69.436 1.00 90.27 N ANISOU 35 N YCM A 57 13739 10056 10504 1106 -1652 1874 N HETATM 36 CA YCM A 57 -0.660 21.086 -69.924 1.00100.97 C ANISOU 36 CA YCM A 57 15119 11312 11932 1408 -2028 1545 C HETATM 37 CB YCM A 57 -1.759 21.738 -69.089 1.00107.03 C ANISOU 37 CB YCM A 57 15667 11964 13035 1388 -2274 1246 C HETATM 38 SG YCM A 57 -2.624 20.721 -67.928 1.00111.58 S ANISOU 38 SG YCM A 57 15682 12718 13996 1291 -2342 870 S HETATM 39 CD YCM A 57 -1.613 19.298 -67.683 1.00103.81 C ANISOU 39 CD YCM A 57 14459 12049 12934 1110 -1977 1017 C HETATM 40 CE YCM A 57 -2.320 18.010 -68.041 1.00100.60 C ANISOU 40 CE YCM A 57 13930 11742 12553 1310 -2135 771 C HETATM 41 OZ1 YCM A 57 -1.686 16.939 -68.166 1.00 97.43 O ANISOU 41 OZ1 YCM A 57 13439 11540 12041 1258 -1924 872 O HETATM 42 NZ2 YCM A 57 -3.677 18.045 -68.229 1.00 98.31 N ANISOU 42 NZ2 YCM A 57 13630 11315 12408 1552 -2518 435 N HETATM 43 C YCM A 57 -0.870 21.460 -71.386 1.00113.61 C ANISOU 43 C YCM A 57 17220 12713 13233 1740 -2244 1620 C HETATM 44 O YCM A 57 -0.693 22.610 -71.800 1.00110.96 O ANISOU 44 O YCM A 57 17197 12187 12774 1782 -2294 1774 O ATOM 45 N PRO A 58 -1.243 20.464 -72.205 1.00124.15 N ANISOU 45 N PRO A 58 18638 14091 14441 1982 -2372 1513 N ATOM 46 CA PRO A 58 -1.641 20.732 -73.590 1.00135.47 C ANISOU 46 CA PRO A 58 20522 15332 15619 2327 -2625 1526 C ATOM 47 C PRO A 58 -2.849 21.662 -73.630 1.00143.48 C ANISOU 47 C PRO A 58 21624 16103 16786 2502 -2999 1279 C ATOM 48 O PRO A 58 -3.984 21.211 -73.479 1.00143.53 O ANISOU 48 O PRO A 58 21455 16094 16987 2647 -3265 943 O ATOM 49 CB PRO A 58 -1.985 19.342 -74.136 1.00134.79 C ANISOU 49 CB PRO A 58 20376 15373 15466 2514 -2700 1381 C ATOM 50 CG PRO A 58 -1.220 18.397 -73.270 1.00129.71 C ANISOU 50 CG PRO A 58 19361 15009 14915 2233 -2364 1453 C ATOM 51 CD PRO A 58 -1.214 19.021 -71.907 1.00126.49 C ANISOU 51 CD PRO A 58 18624 14628 14808 1938 -2263 1401 C ATOM 52 N GLN A 59 -2.596 22.956 -73.821 1.00149.23 N ANISOU 52 N GLN A 59 22623 16647 17430 2484 -3015 1447 N ATOM 53 CA GLN A 59 -3.615 23.983 -73.663 1.00155.25 C ANISOU 53 CA GLN A 59 23438 17186 18365 2588 -3324 1241 C ATOM 54 C GLN A 59 -4.064 24.617 -74.970 1.00153.72 C ANISOU 54 C GLN A 59 23722 16747 17936 2918 -3601 1260 C ATOM 55 O GLN A 59 -4.914 25.514 -74.933 1.00158.07 O ANISOU 55 O GLN A 59 24353 17098 18610 3024 -3870 1098 O ATOM 56 CB GLN A 59 -3.109 25.086 -72.725 1.00160.56 C ANISOU 56 CB GLN A 59 24013 17820 19170 2299 -3154 1381 C ATOM 57 CG GLN A 59 -3.068 24.683 -71.268 1.00162.34 C ANISOU 57 CG GLN A 59 23727 18237 19719 1994 -2983 1261 C ATOM 58 CD GLN A 59 -4.431 24.290 -70.751 1.00164.87 C ANISOU 58 CD GLN A 59 23753 18544 20345 2096 -3277 844 C ATOM 59 OE1 GLN A 59 -5.456 24.767 -71.243 1.00168.22 O ANISOU 59 OE1 GLN A 59 24348 18769 20800 2344 -3623 645 O ATOM 60 NE2 GLN A 59 -4.455 23.411 -69.758 1.00163.04 N ANISOU 60 NE2 GLN A 59 23078 18526 20344 1905 -3144 708 N ATOM 61 N THR A 60 -3.526 24.173 -76.110 1.00149.99 N ANISOU 61 N THR A 60 23566 16286 17137 3084 -3545 1451 N ATOM 62 CA THR A 60 -3.749 24.778 -77.423 1.00148.17 C ANISOU 62 CA THR A 60 23824 15834 16640 3383 -3761 1527 C ATOM 63 C THR A 60 -5.177 25.279 -77.601 1.00148.90 C ANISOU 63 C THR A 60 23972 15716 16888 3626 -4185 1203 C ATOM 64 O THR A 60 -6.143 24.544 -77.371 1.00148.23 O ANISOU 64 O THR A 60 23651 15677 16992 3733 -4384 885 O ATOM 65 CB THR A 60 -3.399 23.784 -78.533 1.00146.14 C ANISOU 65 CB THR A 60 23780 15655 16091 3578 -3724 1628 C ATOM 66 OG1 THR A 60 -2.220 23.059 -78.165 1.00142.32 O ANISOU 66 OG1 THR A 60 23135 15410 15530 3336 -3337 1859 O ATOM 67 CG2 THR A 60 -3.132 24.522 -79.837 1.00147.10 C ANISOU 67 CG2 THR A 60 24434 15578 15880 3801 -3815 1841 C ATOM 68 N GLY A 61 -5.310 26.535 -78.012 1.00149.88 N ANISOU 68 N GLY A 61 24408 15609 16933 3712 -4323 1283 N ATOM 69 CA GLY A 61 -6.559 27.252 -77.869 1.00150.23 C ANISOU 69 CA GLY A 61 24449 15455 17178 3858 -4680 997 C ATOM 70 C GLY A 61 -6.469 28.159 -76.659 1.00148.79 C ANISOU 70 C GLY A 61 24033 15252 17249 3577 -4585 997 C ATOM 71 O GLY A 61 -7.088 27.891 -75.625 1.00147.77 O ANISOU 71 O GLY A 61 23508 15200 17438 3457 -4638 745 O ATOM 72 N SER A 62 -5.682 29.236 -76.790 1.00147.63 N ANISOU 72 N SER A 62 24132 15003 16958 3470 -4442 1284 N ATOM 73 CA SER A 62 -5.277 30.147 -75.721 1.00142.05 C ANISOU 73 CA SER A 62 23253 14290 16430 3171 -4277 1376 C ATOM 74 C SER A 62 -6.404 30.450 -74.741 1.00135.94 C ANISOU 74 C SER A 62 22160 13462 16030 3130 -4500 1035 C ATOM 75 O SER A 62 -7.563 30.616 -75.147 1.00137.86 O ANISOU 75 O SER A 62 22492 13546 16341 3385 -4857 774 O ATOM 76 CB SER A 62 -4.742 31.451 -76.317 1.00144.61 C ANISOU 76 CB SER A 62 23989 14415 16540 3196 -4257 1647 C ATOM 77 OG SER A 62 -5.694 32.049 -77.178 1.00148.40 O ANISOU 77 OG SER A 62 24777 14652 16956 3509 -4624 1501 O ATOM 78 N PRO A 63 -6.098 30.545 -73.450 1.00128.05 N ANISOU 78 N PRO A 63 20791 12587 15277 2813 -4299 1029 N ATOM 79 CA PRO A 63 -7.155 30.699 -72.446 1.00118.94 C ANISOU 79 CA PRO A 63 19291 11408 14493 2758 -4493 694 C ATOM 80 C PRO A 63 -7.864 32.039 -72.573 1.00113.02 C ANISOU 80 C PRO A 63 18746 10391 13805 2870 -4762 610 C ATOM 81 O PRO A 63 -7.345 33.006 -73.134 1.00114.91 O ANISOU 81 O PRO A 63 19335 10484 13843 2895 -4727 851 O ATOM 82 CB PRO A 63 -6.397 30.598 -71.119 1.00115.15 C ANISOU 82 CB PRO A 63 18423 11123 14205 2369 -4158 790 C ATOM 83 CG PRO A 63 -5.015 31.064 -71.451 1.00117.95 C ANISOU 83 CG PRO A 63 19027 11498 14293 2225 -3844 1204 C ATOM 84 CD PRO A 63 -4.753 30.575 -72.848 1.00123.25 C ANISOU 84 CD PRO A 63 20071 12140 14617 2486 -3883 1338 C ATOM 85 N SER A 64 -9.079 32.079 -72.036 1.00107.37 N ANISOU 85 N SER A 64 17804 9614 13378 2939 -5038 260 N ATOM 86 CA SER A 64 -9.865 33.300 -72.012 1.00106.28 C ANISOU 86 CA SER A 64 17802 9233 13348 3032 -5308 137 C ATOM 87 C SER A 64 -9.489 34.146 -70.796 1.00122.18 C ANISOU 87 C SER A 64 19586 11260 15577 2709 -5134 206 C ATOM 88 O SER A 64 -8.639 33.777 -69.981 1.00114.78 O ANISOU 88 O SER A 64 18385 10519 14706 2418 -4809 344 O ATOM 89 CB SER A 64 -11.357 32.975 -72.013 1.00106.54 C ANISOU 89 CB SER A 64 17706 9187 13588 3260 -5690 -273 C ATOM 90 OG SER A 64 -11.723 32.270 -70.841 1.00103.81 O ANISOU 90 OG SER A 64 16869 9016 13559 3081 -5640 -498 O ATOM 91 N MET A 65 -10.142 35.302 -70.672 1.00 86.88 N ANISOU 91 N MET A 65 15777 8343 8891 -1189 -3547 1914 N ATOM 92 CA MET A 65 -9.847 36.213 -69.572 1.00 87.64 C ANISOU 92 CA MET A 65 15987 8102 9209 -1126 -3682 1941 C ATOM 93 C MET A 65 -10.326 35.647 -68.241 1.00 82.86 C ANISOU 93 C MET A 65 14947 7537 8998 -696 -3507 1599 C ATOM 94 O MET A 65 -9.552 35.550 -67.281 1.00 79.45 O ANISOU 94 O MET A 65 14346 7146 8695 -771 -3257 1540 O ATOM 95 CB MET A 65 -10.492 37.573 -69.839 1.00 96.03 C ANISOU 95 CB MET A 65 17497 8704 10286 -1010 -4221 2054 C ATOM 96 CG MET A 65 -10.392 38.547 -68.679 1.00105.14 C ANISOU 96 CG MET A 65 18720 9527 11701 -848 -4357 1935 C ATOM 97 SD MET A 65 -8.705 39.117 -68.427 1.00112.18 S ANISOU 97 SD MET A 65 19747 10437 12440 -1472 -4175 2161 S ATOM 98 CE MET A 65 -8.374 39.884 -70.011 1.00103.68 C ANISOU 98 CE MET A 65 19041 9361 10990 -1969 -4376 2460 C ATOM 99 N VAL A 66 -11.603 35.264 -68.168 1.00 83.31 N ANISOU 99 N VAL A 66 14803 7620 9230 -267 -3642 1388 N ATOM 100 CA VAL A 66 -12.193 34.856 -66.897 1.00 87.12 C ANISOU 100 CA VAL A 66 14889 8156 10057 140 -3522 1093 C ATOM 101 C VAL A 66 -11.557 33.571 -66.381 1.00 81.04 C ANISOU 101 C VAL A 66 13689 7752 9351 8 -3006 939 C ATOM 102 O VAL A 66 -11.418 33.385 -65.165 1.00 78.67 O ANISOU 102 O VAL A 66 13146 7468 9276 161 -2829 779 O ATOM 103 CB VAL A 66 -13.719 34.713 -67.051 1.00 91.74 C ANISOU 103 CB VAL A 66 15303 8782 10771 575 -3786 940 C ATOM 104 CG1 VAL A 66 -14.376 34.472 -65.700 1.00 89.29 C ANISOU 104 CG1 VAL A 66 14589 8558 10779 994 -3688 665 C ATOM 105 CG2 VAL A 66 -14.301 35.949 -67.720 1.00 98.00 C ANISOU 105 CG2 VAL A 66 16558 9212 11467 725 -4331 1107 C ATOM 106 N THR A 67 -11.152 32.671 -67.279 1.00 80.92 N ANISOU 106 N THR A 67 13605 8021 9118 -254 -2775 975 N ATOM 107 CA THR A 67 -10.598 31.394 -66.838 1.00 73.47 C ANISOU 107 CA THR A 67 12299 7388 8226 -316 -2331 808 C ATOM 108 C THR A 67 -9.184 31.556 -66.292 1.00 64.70 C ANISOU 108 C THR A 67 11179 6321 7082 -564 -2061 893 C ATOM 109 O THR A 67 -8.847 30.976 -65.253 1.00 57.65 O ANISOU 109 O THR A 67 9997 5524 6382 -474 -1808 738 O ATOM 110 CB THR A 67 -10.617 30.382 -67.985 1.00 72.78 C ANISOU 110 CB THR A 67 12195 7565 7892 -460 -2200 783 C ATOM 111 OG1 THR A 67 -9.875 30.899 -69.096 1.00 85.80 O ANISOU 111 OG1 THR A 67 14173 9243 9185 -782 -2233 1025 O ATOM 112 CG2 THR A 67 -12.048 30.098 -68.417 1.00 57.52 C ANISOU 112 CG2 THR A 67 10213 5625 6017 -241 -2476 688 C ATOM 113 N ALA A 68 -8.344 32.337 -66.976 1.00 65.22 N ANISOU 113 N ALA A 68 11548 6342 6891 -903 -2127 1159 N ATOM 114 CA ALA A 68 -6.972 32.525 -66.513 1.00 65.95 C ANISOU 114 CA ALA A 68 11591 6540 6928 -1193 -1890 1276 C ATOM 115 C ALA A 68 -6.937 33.226 -65.160 1.00 66.66 C ANISOU 115 C ALA A 68 11684 6345 7301 -1064 -2009 1231 C ATOM 116 O ALA A 68 -6.132 32.873 -64.290 1.00 62.13 O ANISOU 116 O ALA A 68 10870 5906 6832 -1121 -1749 1169 O ATOM 117 CB ALA A 68 -6.169 33.310 -67.549 1.00 70.78 C ANISOU 117 CB ALA A 68 12528 7190 7177 -1645 -1978 1615 C ATOM 118 N ILE A 69 -7.807 34.219 -64.962 1.00 69.34 N ANISOU 118 N ILE A 69 12306 6288 7750 -856 -2418 1247 N ATOM 119 CA ILE A 69 -7.883 34.889 -63.667 1.00 67.41 C ANISOU 119 CA ILE A 69 12109 5755 7750 -660 -2555 1155 C ATOM 120 C ILE A 69 -8.378 33.925 -62.598 1.00 64.05 C ANISOU 120 C ILE A 69 11236 5509 7591 -304 -2303 842 C ATOM 121 O ILE A 69 -7.874 33.919 -61.467 1.00 61.98 O ANISOU 121 O ILE A 69 10849 5229 7472 -281 -2170 758 O ATOM 122 CB ILE A 69 -8.780 36.137 -63.758 1.00 66.30 C ANISOU 122 CB ILE A 69 12401 5149 7642 -423 -3073 1203 C ATOM 123 CG1 ILE A 69 -8.198 37.145 -64.747 1.00 66.14 C ANISOU 123 CG1 ILE A 69 12895 4897 7337 -848 -3361 1560 C ATOM 124 CG2 ILE A 69 -8.948 36.778 -62.388 1.00 66.51 C ANISOU 124 CG2 ILE A 69 12494 4882 7897 -130 -3213 1044 C ATOM 125 CD1 ILE A 69 -9.021 38.408 -64.871 1.00 71.79 C ANISOU 125 CD1 ILE A 69 14021 5180 8077 -607 -3867 1556 C ATOM 126 N THR A 70 -9.367 33.095 -62.936 1.00 59.61 N ANISOU 126 N THR A 70 10442 5128 7080 -63 -2254 685 N ATOM 127 CA THR A 70 -9.900 32.141 -61.968 1.00 62.79 C ANISOU 127 CA THR A 70 10430 5722 7706 210 -2035 426 C ATOM 128 C THR A 70 -8.822 31.165 -61.510 1.00 53.25 C ANISOU 128 C THR A 70 8969 4760 6502 5 -1631 387 C ATOM 129 O THR A 70 -8.626 30.958 -60.308 1.00 54.69 O ANISOU 129 O THR A 70 8966 4959 6856 112 -1492 266 O ATOM 130 CB THR A 70 -11.089 31.389 -62.570 1.00 66.88 C ANISOU 130 CB THR A 70 10760 6416 8236 392 -2085 318 C ATOM 131 OG1 THR A 70 -12.114 32.323 -62.929 1.00 74.48 O ANISOU 131 OG1 THR A 70 11916 7176 9209 640 -2484 346 O ATOM 132 CG2 THR A 70 -11.650 30.389 -61.571 1.00 63.88 C ANISOU 132 CG2 THR A 70 9959 6253 8061 593 -1875 93 C ATOM 133 N ILE A 71 -8.106 30.562 -62.462 1.00 53.94 N ANISOU 133 N ILE A 71 9056 5056 6381 -261 -1447 482 N ATOM 134 CA ILE A 71 -7.037 29.630 -62.114 1.00 58.39 C ANISOU 134 CA ILE A 71 9384 5874 6928 -395 -1081 436 C ATOM 135 C ILE A 71 -5.945 30.344 -61.329 1.00 59.04 C ANISOU 135 C ILE A 71 9502 5889 7042 -569 -1040 549 C ATOM 136 O ILE A 71 -5.357 29.781 -60.395 1.00 54.06 O ANISOU 136 O ILE A 71 8634 5374 6530 -541 -821 455 O ATOM 137 CB ILE A 71 -6.485 28.959 -63.385 1.00 57.59 C ANISOU 137 CB ILE A 71 9306 6032 6544 -590 -911 499 C ATOM 138 CG1 ILE A 71 -7.592 28.165 -64.083 1.00 51.97 C ANISOU 138 CG1 ILE A 71 8581 5362 5804 -433 -981 365 C ATOM 139 CG2 ILE A 71 -5.301 28.062 -63.053 1.00 51.59 C ANISOU 139 CG2 ILE A 71 8304 5551 5746 -664 -549 441 C ATOM 140 CD1 ILE A 71 -7.160 27.516 -65.384 1.00 53.42 C ANISOU 140 CD1 ILE A 71 8853 5774 5670 -582 -848 391 C ATOM 141 N MET A 72 -5.667 31.600 -61.683 1.00 52.90 N ANISOU 141 N MET A 72 9047 4902 6151 -773 -1288 765 N ATOM 142 CA MET A 72 -4.676 32.377 -60.947 1.00 57.12 C ANISOU 142 CA MET A 72 9665 5334 6705 -997 -1322 896 C ATOM 143 C MET A 72 -5.130 32.638 -59.518 1.00 55.10 C ANISOU 143 C MET A 72 9374 4846 6714 -714 -1415 717 C ATOM 144 O MET A 72 -4.369 32.426 -58.567 1.00 49.99 O ANISOU 144 O MET A 72 8558 4281 6155 -777 -1257 680 O ATOM 145 CB MET A 72 -4.395 33.694 -61.669 1.00 66.43 C ANISOU 145 CB MET A 72 11277 6277 7688 -1315 -1637 1187 C ATOM 146 CG MET A 72 -3.244 33.580 -62.628 1.00 88.45 C ANISOU 146 CG MET A 72 14026 9404 10177 -1767 -1451 1435 C ATOM 147 SD MET A 72 -1.977 32.566 -61.852 1.00103.04 S ANISOU 147 SD MET A 72 15372 11700 12079 -1844 -1000 1351 S ATOM 148 CE MET A 72 -1.334 33.696 -60.618 1.00106.69 C ANISOU 148 CE MET A 72 15993 11870 12676 -2060 -1228 1475 C ATOM 149 N ALA A 73 -6.366 33.114 -59.351 1.00 58.28 N ANISOU 149 N ALA A 73 9927 4991 7225 -382 -1677 599 N ATOM 150 CA ALA A 73 -6.901 33.318 -58.011 1.00 56.01 C ANISOU 150 CA ALA A 73 9581 4552 7148 -54 -1737 395 C ATOM 151 C ALA A 73 -6.957 32.013 -57.232 1.00 53.49 C ANISOU 151 C ALA A 73 8821 4538 6964 84 -1392 201 C ATOM 152 O ALA A 73 -6.779 32.013 -56.009 1.00 55.46 O ANISOU 152 O ALA A 73 8980 4761 7333 187 -1328 90 O ATOM 153 CB ALA A 73 -8.288 33.956 -58.090 1.00 56.84 C ANISOU 153 CB ALA A 73 9851 4430 7314 341 -2051 284 C ATOM 154 N LEU A 74 -7.191 30.893 -57.920 1.00 52.68 N ANISOU 154 N LEU A 74 8489 4704 6824 72 -1193 164 N ATOM 155 CA LEU A 74 -7.207 29.593 -57.257 1.00 54.76 C ANISOU 155 CA LEU A 74 8402 5211 7194 160 -906 6 C ATOM 156 C LEU A 74 -5.863 29.295 -56.604 1.00 44.00 C ANISOU 156 C LEU A 74 6935 3948 5834 -29 -694 50 C ATOM 157 O LEU A 74 -5.784 29.059 -55.393 1.00 46.36 O ANISOU 157 O LEU A 74 7097 4253 6264 76 -612 -55 O ATOM 158 CB LEU A 74 -7.575 28.498 -58.259 1.00 59.23 C ANISOU 158 CB LEU A 74 8847 5981 7678 135 -789 -24 C ATOM 159 CG LEU A 74 -8.996 27.937 -58.197 1.00 63.81 C ANISOU 159 CG LEU A 74 9269 6622 8353 365 -856 -168 C ATOM 160 CD1 LEU A 74 -9.197 26.878 -59.271 1.00 60.68 C ANISOU 160 CD1 LEU A 74 8834 6381 7840 268 -783 -181 C ATOM 161 CD2 LEU A 74 -9.279 27.363 -56.819 1.00 60.26 C ANISOU 161 CD2 LEU A 74 8566 6258 8073 507 -721 -311 C ATOM 162 N TYR A 75 -4.789 29.304 -57.398 1.00 45.87 N ANISOU 162 N TYR A 75 7215 4307 5907 -311 -605 213 N ATOM 163 CA TYR A 75 -3.469 28.984 -56.864 1.00 46.23 C ANISOU 163 CA TYR A 75 7095 4527 5942 -481 -405 265 C ATOM 164 C TYR A 75 -3.040 29.985 -55.799 1.00 44.98 C ANISOU 164 C TYR A 75 7054 4170 5866 -562 -558 320 C ATOM 165 O TYR A 75 -2.413 29.609 -54.802 1.00 43.70 O ANISOU 165 O TYR A 75 6718 4095 5793 -561 -435 271 O ATOM 166 CB TYR A 75 -2.440 28.933 -57.995 1.00 46.16 C ANISOU 166 CB TYR A 75 7074 4766 5699 -763 -284 442 C ATOM 167 CG TYR A 75 -2.473 27.651 -58.799 1.00 52.53 C ANISOU 167 CG TYR A 75 7721 5833 6404 -656 -56 336 C ATOM 168 CD1 TYR A 75 -2.009 26.458 -58.259 1.00 52.84 C ANISOU 168 CD1 TYR A 75 7506 6057 6512 -510 178 193 C ATOM 169 CD2 TYR A 75 -2.958 27.634 -60.102 1.00 61.70 C ANISOU 169 CD2 TYR A 75 9034 7028 7382 -689 -107 374 C ATOM 170 CE1 TYR A 75 -2.034 25.283 -58.988 1.00 59.53 C ANISOU 170 CE1 TYR A 75 8286 7082 7252 -382 344 72 C ATOM 171 CE2 TYR A 75 -2.985 26.462 -60.840 1.00 61.15 C ANISOU 171 CE2 TYR A 75 8878 7166 7192 -581 75 251 C ATOM 172 CZ TYR A 75 -2.522 25.290 -60.277 1.00 56.42 C ANISOU 172 CZ TYR A 75 8057 6714 6666 -419 294 92 C ATOM 173 OH TYR A 75 -2.546 24.122 -61.003 1.00 47.68 O ANISOU 173 OH TYR A 75 6938 5754 5425 -283 433 -53 O ATOM 174 N SER A 76 -3.375 31.264 -55.985 1.00 41.44 N ANISOU 174 N SER A 76 6942 3422 5379 -624 -861 418 N ATOM 175 CA SER A 76 -2.945 32.282 -55.034 1.00 44.48 C ANISOU 175 CA SER A 76 7532 3558 5811 -719 -1062 466 C ATOM 176 C SER A 76 -3.661 32.135 -53.696 1.00 45.16 C ANISOU 176 C SER A 76 7555 3529 6074 -366 -1071 222 C ATOM 177 O SER A 76 -3.026 32.203 -52.638 1.00 43.85 O ANISOU 177 O SER A 76 7348 3351 5961 -423 -1046 197 O ATOM 178 CB SER A 76 -3.177 33.675 -55.618 1.00 48.53 C ANISOU 178 CB SER A 76 8507 3714 6220 -851 -1437 624 C ATOM 179 OG SER A 76 -2.407 33.867 -56.791 1.00 70.85 O ANISOU 179 OG SER A 76 11397 6684 8839 -1256 -1424 891 O ATOM 180 N ILE A 77 -4.978 31.929 -53.723 1.00 45.99 N ANISOU 180 N ILE A 77 7632 3593 6249 -12 -1107 51 N ATOM 181 CA ILE A 77 -5.746 31.840 -52.484 1.00 47.16 C ANISOU 181 CA ILE A 77 7694 3705 6520 327 -1101 -173 C ATOM 182 C ILE A 77 -5.347 30.600 -51.694 1.00 45.25 C ANISOU 182 C ILE A 77 7100 3742 6349 313 -793 -250 C ATOM 183 O ILE A 77 -5.115 30.665 -50.482 1.00 44.45 O ANISOU 183 O ILE A 77 6978 3616 6296 375 -771 -335 O ATOM 184 CB ILE A 77 -7.255 31.860 -52.789 1.00 58.94 C ANISOU 184 CB ILE A 77 9154 5193 8046 686 -1196 -313 C ATOM 185 CG1 ILE A 77 -7.674 33.245 -53.290 1.00 65.91 C ANISOU 185 CG1 ILE A 77 10450 5725 8869 793 -1572 -267 C ATOM 186 CG2 ILE A 77 -8.061 31.465 -51.561 1.00 57.35 C ANISOU 186 CG2 ILE A 77 8728 5126 7936 1011 -1092 -537 C ATOM 187 CD1 ILE A 77 -9.086 33.301 -53.825 1.00 68.01 C ANISOU 187 CD1 ILE A 77 10663 6023 9154 1142 -1700 -370 C ATOM 188 N VAL A 78 -5.255 29.452 -52.370 1.00 37.62 N ANISOU 188 N VAL A 78 5899 3022 5374 238 -578 -226 N ATOM 189 CA VAL A 78 -4.893 28.215 -51.683 1.00 39.31 C ANISOU 189 CA VAL A 78 5836 3450 5648 242 -330 -293 C ATOM 190 C VAL A 78 -3.495 28.323 -51.088 1.00 43.66 C ANISOU 190 C VAL A 78 6368 4032 6189 39 -277 -201 C ATOM 191 O VAL A 78 -3.239 27.855 -49.971 1.00 41.53 O ANISOU 191 O VAL A 78 5977 3819 5983 91 -190 -270 O ATOM 192 CB VAL A 78 -5.014 27.017 -52.644 1.00 41.14 C ANISOU 192 CB VAL A 78 5913 3873 5846 213 -168 -292 C ATOM 193 CG1 VAL A 78 -4.493 25.750 -51.989 1.00 35.97 C ANISOU 193 CG1 VAL A 78 5051 3376 5240 215 39 -345 C ATOM 194 CG2 VAL A 78 -6.459 26.835 -53.074 1.00 41.50 C ANISOU 194 CG2 VAL A 78 5938 3920 5912 386 -245 -380 C ATOM 195 N CYS A 79 -2.572 28.954 -51.816 1.00 44.10 N ANISOU 195 N CYS A 79 6532 4077 6146 -222 -342 -24 N ATOM 196 CA CYS A 79 -1.216 29.127 -51.307 1.00 42.55 C ANISOU 196 CA CYS A 79 6271 3969 5927 -460 -316 94 C ATOM 197 C CYS A 79 -1.201 30.011 -50.066 1.00 47.69 C ANISOU 197 C CYS A 79 7108 4383 6630 -450 -510 52 C ATOM 198 O CYS A 79 -0.602 29.653 -49.045 1.00 45.61 O ANISOU 198 O CYS A 79 6714 4201 6413 -466 -445 22 O ATOM 199 CB CYS A 79 -0.320 29.714 -52.397 1.00 39.85 C ANISOU 199 CB CYS A 79 5991 3717 5433 -796 -358 323 C ATOM 200 SG CYS A 79 1.361 30.072 -51.857 1.00 48.18 S ANISOU 200 SG CYS A 79 6914 4954 6436 -1165 -364 518 S ATOM 201 N VAL A 80 -1.862 31.169 -50.135 1.00 41.50 N ANISOU 201 N VAL A 80 6661 3288 5821 -397 -772 38 N ATOM 202 CA VAL A 80 -1.849 32.110 -49.017 1.00 43.75 C ANISOU 202 CA VAL A 80 7208 3299 6117 -358 -998 -28 C ATOM 203 C VAL A 80 -2.537 31.506 -47.798 1.00 45.31 C ANISOU 203 C VAL A 80 7264 3560 6393 -27 -877 -261 C ATOM 204 O VAL A 80 -2.028 31.587 -46.675 1.00 43.24 O ANISOU 204 O VAL A 80 7022 3274 6133 -61 -902 -302 O ATOM 205 CB VAL A 80 -2.499 33.443 -49.431 1.00 42.20 C ANISOU 205 CB VAL A 80 7455 2715 5862 -293 -1337 -22 C ATOM 206 CG1 VAL A 80 -2.723 34.327 -48.215 1.00 51.14 C ANISOU 206 CG1 VAL A 80 8903 3536 6991 -121 -1576 -175 C ATOM 207 CG2 VAL A 80 -1.632 34.159 -50.457 1.00 49.76 C ANISOU 207 CG2 VAL A 80 8613 3590 6704 -733 -1500 263 C ATOM 208 N VAL A 81 -3.707 30.895 -48.000 1.00 43.35 N ANISOU 208 N VAL A 81 6865 3418 6186 265 -754 -399 N ATOM 209 CA VAL A 81 -4.433 30.293 -46.885 1.00 46.33 C ANISOU 209 CA VAL A 81 7079 3922 6602 533 -624 -588 C ATOM 210 C VAL A 81 -3.641 29.131 -46.298 1.00 48.79 C ANISOU 210 C VAL A 81 7127 4462 6949 393 -403 -546 C ATOM 211 O VAL A 81 -3.562 28.969 -45.075 1.00 46.75 O ANISOU 211 O VAL A 81 6843 4236 6682 460 -371 -629 O ATOM 212 CB VAL A 81 -5.839 29.855 -47.338 1.00 47.71 C ANISOU 212 CB VAL A 81 7101 4226 6801 799 -552 -698 C ATOM 213 CG1 VAL A 81 -6.517 29.026 -46.256 1.00 50.80 C ANISOU 213 CG1 VAL A 81 7248 4848 7203 977 -372 -839 C ATOM 214 CG2 VAL A 81 -6.684 31.072 -47.684 1.00 44.41 C ANISOU 214 CG2 VAL A 81 6947 3581 6346 1036 -808 -774 C ATOM 215 N GLY A 82 -3.030 28.314 -47.159 1.00 42.80 N ANISOU 215 N GLY A 82 6191 3861 6210 223 -264 -425 N ATOM 216 CA GLY A 82 -2.248 27.191 -46.670 1.00 41.72 C ANISOU 216 CA GLY A 82 5831 3916 6105 150 -90 -394 C ATOM 217 C GLY A 82 -1.018 27.621 -45.892 1.00 45.69 C ANISOU 217 C GLY A 82 6367 4400 6592 -30 -170 -312 C ATOM 218 O GLY A 82 -0.716 27.061 -44.835 1.00 41.53 O ANISOU 218 O GLY A 82 5748 3946 6085 4 -115 -349 O ATOM 219 N LEU A 83 -0.292 28.617 -46.401 1.00 37.86 N ANISOU 219 N LEU A 83 5516 3318 5552 -258 -323 -177 N ATOM 220 CA LEU A 83 0.906 29.076 -45.706 1.00 41.27 C ANISOU 220 CA LEU A 83 5966 3755 5958 -495 -436 -70 C ATOM 221 C LEU A 83 0.556 29.765 -44.393 1.00 45.51 C ANISOU 221 C LEU A 83 6749 4066 6478 -402 -610 -196 C ATOM 222 O LEU A 83 1.214 29.535 -43.373 1.00 45.79 O ANISOU 222 O LEU A 83 6722 4165 6510 -464 -625 -193 O ATOM 223 CB LEU A 83 1.716 30.008 -46.609 1.00 41.52 C ANISOU 223 CB LEU A 83 6100 3763 5914 -838 -581 139 C ATOM 224 CG LEU A 83 2.402 29.330 -47.800 1.00 50.52 C ANISOU 224 CG LEU A 83 6949 5232 7015 -968 -384 280 C ATOM 225 CD1 LEU A 83 3.148 30.345 -48.658 1.00 48.07 C ANISOU 225 CD1 LEU A 83 6742 4939 6582 -1365 -530 520 C ATOM 226 CD2 LEU A 83 3.343 28.233 -47.325 1.00 50.51 C ANISOU 226 CD2 LEU A 83 6586 5555 7051 -938 -203 291 C ATOM 227 N PHE A 84 -0.485 30.600 -44.392 1.00 46.18 N ANISOU 227 N PHE A 84 7117 3898 6530 -218 -752 -321 N ATOM 228 CA PHE A 84 -0.850 31.321 -43.176 1.00 51.28 C ANISOU 228 CA PHE A 84 8034 4333 7117 -66 -921 -480 C ATOM 229 C PHE A 84 -1.341 30.369 -42.092 1.00 49.44 C ANISOU 229 C PHE A 84 7604 4295 6886 164 -722 -631 C ATOM 230 O PHE A 84 -0.913 30.457 -40.936 1.00 52.38 O ANISOU 230 O PHE A 84 8053 4649 7200 136 -784 -676 O ATOM 231 CB PHE A 84 -1.915 32.374 -43.481 1.00 52.21 C ANISOU 231 CB PHE A 84 8486 4164 7189 175 -1114 -611 C ATOM 232 CG PHE A 84 -2.538 32.970 -42.251 1.00 63.43 C ANISOU 232 CG PHE A 84 10158 5424 8519 473 -1236 -848 C ATOM 233 CD1 PHE A 84 -1.862 33.926 -41.513 1.00 71.04 C ANISOU 233 CD1 PHE A 84 11493 6106 9394 336 -1518 -859 C ATOM 234 CD2 PHE A 84 -3.794 32.568 -41.827 1.00 66.16 C ANISOU 234 CD2 PHE A 84 10363 5932 8842 880 -1073 -1062 C ATOM 235 CE1 PHE A 84 -2.426 34.472 -40.377 1.00 73.24 C ANISOU 235 CE1 PHE A 84 12039 6238 9550 650 -1631 -1111 C ATOM 236 CE2 PHE A 84 -4.364 33.112 -40.692 1.00 69.35 C ANISOU 236 CE2 PHE A 84 10971 6260 9119 1192 -1154 -1299 C ATOM 237 CZ PHE A 84 -3.679 34.067 -39.968 1.00 70.14 C ANISOU 237 CZ PHE A 84 11470 6065 9117 1098 -1425 -1334 C ATOM 238 N GLY A 85 -2.248 29.458 -42.447 1.00 44.61 N ANISOU 238 N GLY A 85 6757 3872 6319 356 -503 -693 N ATOM 239 CA GLY A 85 -2.815 28.569 -41.447 1.00 41.89 C ANISOU 239 CA GLY A 85 6247 3723 5947 521 -330 -802 C ATOM 240 C GLY A 85 -1.787 27.641 -40.830 1.00 45.37 C ANISOU 240 C GLY A 85 6526 4302 6410 343 -246 -696 C ATOM 241 O GLY A 85 -1.828 27.368 -39.627 1.00 46.18 O ANISOU 241 O GLY A 85 6639 4468 6438 396 -222 -761 O ATOM 242 N ASN A 86 -0.845 27.154 -41.636 1.00 37.27 N ANISOU 242 N ASN A 86 5350 3346 5464 153 -207 -537 N ATOM 243 CA ASN A 86 0.118 26.189 -41.118 1.00 35.97 C ANISOU 243 CA ASN A 86 5008 3333 5327 56 -139 -448 C ATOM 244 C ASN A 86 1.270 26.867 -40.387 1.00 40.23 C ANISOU 244 C ASN A 86 5633 3824 5829 -133 -322 -373 C ATOM 245 O ASN A 86 1.787 26.321 -39.407 1.00 40.16 O ANISOU 245 O ASN A 86 5560 3898 5799 -150 -328 -355 O ATOM 246 CB ASN A 86 0.632 25.305 -42.252 1.00 34.90 C ANISOU 246 CB ASN A 86 4653 3341 5268 10 -13 -344 C ATOM 247 CG ASN A 86 -0.409 24.311 -42.716 1.00 39.72 C ANISOU 247 CG ASN A 86 5190 3998 5905 167 142 -413 C ATOM 248 OD1 ASN A 86 -0.732 23.361 -42.002 1.00 38.34 O ANISOU 248 OD1 ASN A 86 4968 3875 5726 236 212 -443 O ATOM 249 ND2 ASN A 86 -0.952 24.530 -43.908 1.00 36.36 N ANISOU 249 ND2 ASN A 86 4776 3547 5492 187 170 -422 N ATOM 250 N PHE A 87 1.689 28.051 -40.840 1.00 39.11 N ANISOU 250 N PHE A 87 5656 3540 5664 -308 -502 -312 N ATOM 251 CA PHE A 87 2.687 28.795 -40.082 1.00 38.59 C ANISOU 251 CA PHE A 87 5718 3402 5544 -538 -728 -238 C ATOM 252 C PHE A 87 2.126 29.275 -38.750 1.00 42.93 C ANISOU 252 C PHE A 87 6550 3778 5984 -398 -848 -412 C ATOM 253 O PHE A 87 2.870 29.385 -37.769 1.00 44.51 O ANISOU 253 O PHE A 87 6806 3980 6126 -528 -984 -383 O ATOM 254 CB PHE A 87 3.210 29.976 -40.899 1.00 44.99 C ANISOU 254 CB PHE A 87 6693 4070 6330 -822 -933 -105 C ATOM 255 CG PHE A 87 4.423 29.648 -41.725 1.00 59.02 C ANISOU 255 CG PHE A 87 8152 6128 8146 -1100 -878 126 C ATOM 256 CD1 PHE A 87 4.295 29.046 -42.965 1.00 56.30 C ANISOU 256 CD1 PHE A 87 7583 5966 7841 -1040 -666 176 C ATOM 257 CD2 PHE A 87 5.694 29.940 -41.256 1.00 71.91 C ANISOU 257 CD2 PHE A 87 9690 7883 9748 -1417 -1040 287 C ATOM 258 CE1 PHE A 87 5.410 28.743 -43.725 1.00 58.43 C ANISOU 258 CE1 PHE A 87 7536 6562 8104 -1249 -586 365 C ATOM 259 CE2 PHE A 87 6.813 29.640 -42.011 1.00 76.67 C ANISOU 259 CE2 PHE A 87 9927 8842 10361 -1651 -967 499 C ATOM 260 CZ PHE A 87 6.670 29.040 -43.246 1.00 69.33 C ANISOU 260 CZ PHE A 87 8770 8119 9454 -1546 -724 529 C ATOM 261 N LEU A 88 0.823 29.562 -38.697 1.00 38.67 N ANISOU 261 N LEU A 88 6175 3123 5396 -119 -800 -599 N ATOM 262 CA LEU A 88 0.198 29.929 -37.432 1.00 44.99 C ANISOU 262 CA LEU A 88 7205 3839 6049 84 -860 -798 C ATOM 263 C LEU A 88 0.206 28.759 -36.456 1.00 45.56 C ANISOU 263 C LEU A 88 7071 4156 6082 138 -684 -804 C ATOM 264 O LEU A 88 0.457 28.944 -35.259 1.00 48.49 O ANISOU 264 O LEU A 88 7599 4507 6319 132 -784 -868 O ATOM 265 CB LEU A 88 -1.229 30.415 -37.679 1.00 41.93 C ANISOU 265 CB LEU A 88 6950 3373 5610 422 -816 -998 C ATOM 266 CG LEU A 88 -2.039 30.778 -36.434 1.00 47.36 C ANISOU 266 CG LEU A 88 7831 4060 6104 720 -826 -1244 C ATOM 267 CD1 LEU A 88 -1.340 31.877 -35.644 1.00 47.99 C ANISOU 267 CD1 LEU A 88 8333 3847 6053 629 -1142 -1309 C ATOM 268 CD2 LEU A 88 -3.447 31.199 -36.820 1.00 48.52 C ANISOU 268 CD2 LEU A 88 8010 4215 6208 1098 -766 -1435 C ATOM 269 N VAL A 89 -0.065 27.548 -36.950 1.00 39.78 N ANISOU 269 N VAL A 89 6035 3633 5447 178 -452 -733 N ATOM 270 CA VAL A 89 -0.005 26.359 -36.104 1.00 39.03 C ANISOU 270 CA VAL A 89 5787 3727 5316 188 -326 -697 C ATOM 271 C VAL A 89 1.412 26.148 -35.588 1.00 46.81 C ANISOU 271 C VAL A 89 6735 4730 6320 -16 -465 -556 C ATOM 272 O VAL A 89 1.630 25.887 -34.398 1.00 44.00 O ANISOU 272 O VAL A 89 6449 4420 5850 -29 -516 -566 O ATOM 273 CB VAL A 89 -0.509 25.125 -36.874 1.00 36.04 C ANISOU 273 CB VAL A 89 5159 3494 5041 238 -114 -635 C ATOM 274 CG1 VAL A 89 -0.251 23.861 -36.072 1.00 32.94 C ANISOU 274 CG1 VAL A 89 4669 3228 4617 202 -49 -554 C ATOM 275 CG2 VAL A 89 -1.987 25.266 -37.193 1.00 34.65 C ANISOU 275 CG2 VAL A 89 4976 3366 4822 421 10 -765 C ATOM 276 N MET A 90 2.399 26.252 -36.481 1.00 38.82 N ANISOU 276 N MET A 90 5589 3726 5434 -182 -529 -414 N ATOM 277 CA MET A 90 3.782 26.052 -36.068 1.00 44.65 C ANISOU 277 CA MET A 90 6210 4560 6196 -368 -665 -267 C ATOM 278 C MET A 90 4.234 27.131 -35.098 1.00 43.21 C ANISOU 278 C MET A 90 6289 4239 5888 -525 -929 -294 C ATOM 279 O MET A 90 5.022 26.855 -34.187 1.00 42.84 O ANISOU 279 O MET A 90 6212 4271 5795 -621 -1052 -226 O ATOM 280 CB MET A 90 4.696 26.012 -37.292 1.00 41.83 C ANISOU 280 CB MET A 90 5601 4328 5963 -509 -652 -112 C ATOM 281 CG MET A 90 4.554 24.741 -38.115 1.00 45.54 C ANISOU 281 CG MET A 90 5819 4953 6533 -338 -427 -88 C ATOM 282 SD MET A 90 5.740 24.659 -39.469 1.00 48.39 S ANISOU 282 SD MET A 90 5854 5557 6976 -457 -384 71 S ATOM 283 CE MET A 90 4.991 25.786 -40.641 1.00 42.55 C ANISOU 283 CE MET A 90 5288 4660 6216 -560 -369 47 C ATOM 284 N TYR A 91 3.741 28.359 -35.266 1.00 42.99 N ANISOU 284 N TYR A 91 6558 3981 5795 -541 -1052 -398 N ATOM 285 CA TYR A 91 4.078 29.423 -34.328 1.00 46.23 C ANISOU 285 CA TYR A 91 7316 4190 6058 -670 -1342 -459 C ATOM 286 C TYR A 91 3.500 29.138 -32.947 1.00 48.28 C ANISOU 286 C TYR A 91 7740 4466 6138 -471 -1311 -625 C ATOM 287 O TYR A 91 4.205 29.241 -31.937 1.00 46.72 O ANISOU 287 O TYR A 91 7654 4265 5833 -609 -1498 -599 O ATOM 288 CB TYR A 91 3.578 30.769 -34.854 1.00 47.66 C ANISOU 288 CB TYR A 91 7854 4060 6196 -672 -1509 -556 C ATOM 289 CG TYR A 91 3.588 31.869 -33.814 1.00 54.06 C ANISOU 289 CG TYR A 91 9145 4583 6812 -694 -1815 -704 C ATOM 290 CD1 TYR A 91 4.770 32.507 -33.459 1.00 60.28 C ANISOU 290 CD1 TYR A 91 10083 5261 7558 -1080 -2146 -567 C ATOM 291 CD2 TYR A 91 2.414 32.270 -33.187 1.00 56.57 C ANISOU 291 CD2 TYR A 91 9765 4764 6965 -325 -1785 -989 C ATOM 292 CE1 TYR A 91 4.783 33.512 -32.506 1.00 61.39 C ANISOU 292 CE1 TYR A 91 10732 5094 7500 -1109 -2467 -718 C ATOM 293 CE2 TYR A 91 2.418 33.272 -32.232 1.00 54.24 C ANISOU 293 CE2 TYR A 91 9958 4193 6458 -290 -2073 -1165 C ATOM 294 CZ TYR A 91 3.604 33.889 -31.897 1.00 59.64 C ANISOU 294 CZ TYR A 91 10854 4702 7106 -689 -2428 -1033 C ATOM 295 OH TYR A 91 3.611 34.888 -30.949 1.00 69.59 O ANISOU 295 OH TYR A 91 12665 5642 8135 -664 -2755 -1222 O ATOM 296 N VAL A 92 2.215 28.781 -32.884 1.00 46.23 N ANISOU 296 N VAL A 92 7483 4262 5822 -168 -1080 -785 N ATOM 297 CA VAL A 92 1.576 28.514 -31.597 1.00 52.27 C ANISOU 297 CA VAL A 92 8375 5116 6367 10 -1011 -935 C ATOM 298 C VAL A 92 2.257 27.347 -30.894 1.00 50.69 C ANISOU 298 C VAL A 92 7982 5115 6163 -113 -973 -777 C ATOM 299 O VAL A 92 2.426 27.353 -29.668 1.00 50.12 O ANISOU 299 O VAL A 92 8081 5070 5892 -130 -1070 -822 O ATOM 300 CB VAL A 92 0.068 28.262 -31.791 1.00 52.04 C ANISOU 300 CB VAL A 92 8279 5213 6281 318 -743 -1093 C ATOM 301 CG1 VAL A 92 -0.559 27.730 -30.510 1.00 57.30 C ANISOU 301 CG1 VAL A 92 8973 6098 6700 448 -608 -1189 C ATOM 302 CG2 VAL A 92 -0.628 29.541 -32.227 1.00 52.61 C ANISOU 302 CG2 VAL A 92 8612 5071 6308 519 -841 -1289 C ATOM 303 N ILE A 93 2.673 26.335 -31.657 1.00 43.19 N ANISOU 303 N ILE A 93 6704 4292 5414 -179 -857 -598 N ATOM 304 CA ILE A 93 3.352 25.188 -31.062 1.00 44.29 C ANISOU 304 CA ILE A 93 6686 4578 5562 -247 -863 -447 C ATOM 305 C ILE A 93 4.719 25.595 -30.524 1.00 53.04 C ANISOU 305 C ILE A 93 7829 5664 6661 -461 -1152 -340 C ATOM 306 O ILE A 93 5.080 25.269 -29.386 1.00 56.03 O ANISOU 306 O ILE A 93 8296 6093 6899 -504 -1268 -308 O ATOM 307 CB ILE A 93 3.465 24.041 -32.082 1.00 47.47 C ANISOU 307 CB ILE A 93 6782 5084 6172 -204 -700 -318 C ATOM 308 CG1 ILE A 93 2.103 23.377 -32.283 1.00 48.83 C ANISOU 308 CG1 ILE A 93 6937 5307 6309 -50 -454 -391 C ATOM 309 CG2 ILE A 93 4.500 23.025 -31.630 1.00 53.89 C ANISOU 309 CG2 ILE A 93 7450 5997 7030 -251 -797 -152 C ATOM 310 CD1 ILE A 93 2.122 22.246 -33.279 1.00 58.34 C ANISOU 310 CD1 ILE A 93 7924 6554 7688 -8 -328 -290 C ATOM 311 N VAL A 94 5.497 26.318 -31.330 1.00 50.31 N ANISOU 311 N VAL A 94 7405 5266 6443 -633 -1287 -263 N ATOM 312 CA VAL A 94 6.842 26.705 -30.915 1.00 56.10 C ANISOU 312 CA VAL A 94 8102 6038 7174 -897 -1577 -125 C ATOM 313 C VAL A 94 6.787 27.708 -29.767 1.00 62.86 C ANISOU 313 C VAL A 94 9377 6706 7802 -996 -1829 -248 C ATOM 314 O VAL A 94 7.618 27.668 -28.852 1.00 62.62 O ANISOU 314 O VAL A 94 9383 6728 7683 -1152 -2058 -170 O ATOM 315 CB VAL A 94 7.626 27.252 -32.122 1.00 61.86 C ANISOU 315 CB VAL A 94 8623 6816 8066 -1113 -1644 15 C ATOM 316 CG1 VAL A 94 8.905 27.944 -31.674 1.00 66.14 C ANISOU 316 CG1 VAL A 94 9159 7402 8568 -1467 -1985 160 C ATOM 317 CG2 VAL A 94 7.945 26.125 -33.092 1.00 55.28 C ANISOU 317 CG2 VAL A 94 7356 6232 7414 -992 -1422 134 C ATOM 318 N ARG A 95 5.798 28.601 -29.778 1.00 62.33 N ANISOU 318 N ARG A 95 9647 6417 7618 -874 -1809 -457 N ATOM 319 CA ARG A 95 5.728 29.674 -28.792 1.00 67.71 C ANISOU 319 CA ARG A 95 10797 6871 8060 -920 -2073 -619 C ATOM 320 C ARG A 95 5.049 29.253 -27.492 1.00 67.29 C ANISOU 320 C ARG A 95 10927 6895 7747 -702 -1982 -780 C ATOM 321 O ARG A 95 5.502 29.641 -26.410 1.00 73.63 O ANISOU 321 O ARG A 95 12003 7629 8342 -810 -2228 -825 O ATOM 322 CB ARG A 95 4.996 30.883 -29.386 1.00 66.52 C ANISOU 322 CB ARG A 95 10973 6423 7877 -826 -2132 -796 C ATOM 323 CG ARG A 95 4.871 32.079 -28.448 1.00 73.97 C ANISOU 323 CG ARG A 95 12490 7060 8555 -814 -2441 -1010 C ATOM 324 CD ARG A 95 6.220 32.724 -28.179 1.00 73.83 C ANISOU 324 CD ARG A 95 12621 6903 8528 -1269 -2864 -844 C ATOM 325 NE ARG A 95 6.097 33.925 -27.358 1.00 86.17 N ANISOU 325 NE ARG A 95 14818 8096 9825 -1272 -3213 -1064 N ATOM 326 CZ ARG A 95 6.225 33.943 -26.034 1.00 93.15 C ANISOU 326 CZ ARG A 95 15969 8974 10448 -1243 -3359 -1188 C ATOM 327 NH1 ARG A 95 6.482 32.822 -25.375 1.00 92.13 N ANISOU 327 NH1 ARG A 95 15519 9189 10296 -1232 -3193 -1087 N ATOM 328 NH2 ARG A 95 6.097 35.084 -25.369 1.00 94.95 N ANISOU 328 NH2 ARG A 95 16669 8936 10471 -1158 -3568 -1325 N ATOM 329 N TYR A 96 3.974 28.467 -27.564 1.00 66.56 N ANISOU 329 N TYR A 96 12201 6237 6851 -1442 173 -1500 N ATOM 330 CA TYR A 96 3.150 28.198 -26.389 1.00 65.56 C ANISOU 330 CA TYR A 96 12219 6089 6602 -1307 290 -1563 C ATOM 331 C TYR A 96 3.161 26.733 -25.971 1.00 68.07 C ANISOU 331 C TYR A 96 12149 6743 6971 -1258 142 -1478 C ATOM 332 O TYR A 96 3.553 26.431 -24.839 1.00 70.19 O ANISOU 332 O TYR A 96 12508 7110 7052 -1452 50 -1532 O ATOM 333 CB TYR A 96 1.714 28.678 -26.644 1.00 63.12 C ANISOU 333 CB TYR A 96 12055 5549 6378 -901 582 -1558 C ATOM 334 CG TYR A 96 1.607 30.169 -26.878 1.00 74.01 C ANISOU 334 CG TYR A 96 13739 6653 7729 -883 748 -1562 C ATOM 335 CD1 TYR A 96 1.701 31.066 -25.819 1.00 77.33 C ANISOU 335 CD1 TYR A 96 14489 6942 7952 -1019 848 -1628 C ATOM 336 CD2 TYR A 96 1.411 30.681 -28.155 1.00 76.49 C ANISOU 336 CD2 TYR A 96 14021 6839 8203 -732 806 -1489 C ATOM 337 CE1 TYR A 96 1.605 32.430 -26.026 1.00 77.55 C ANISOU 337 CE1 TYR A 96 14815 6710 7939 -1005 1009 -1627 C ATOM 338 CE2 TYR A 96 1.312 32.045 -28.373 1.00 78.90 C ANISOU 338 CE2 TYR A 96 14610 6897 8470 -710 958 -1477 C ATOM 339 CZ TYR A 96 1.410 32.914 -27.304 1.00 84.01 C ANISOU 339 CZ TYR A 96 15591 7410 8918 -845 1063 -1550 C ATOM 340 OH TYR A 96 1.313 34.271 -27.513 1.00 84.67 O ANISOU 340 OH TYR A 96 15987 7236 8949 -826 1225 -1539 O ATOM 341 N THR A 97 2.743 25.807 -26.840 1.00 67.89 N ANISOU 341 N THR A 97 11722 6892 7182 -1016 116 -1344 N ATOM 342 CA THR A 97 2.534 24.429 -26.399 1.00 68.61 C ANISOU 342 CA THR A 97 11505 7246 7316 -927 29 -1268 C ATOM 343 C THR A 97 3.847 23.682 -26.184 1.00 70.65 C ANISOU 343 C THR A 97 11542 7759 7542 -1201 -239 -1217 C ATOM 344 O THR A 97 3.906 22.780 -25.339 1.00 65.79 O ANISOU 344 O THR A 97 10823 7319 6856 -1222 -324 -1188 O ATOM 345 CB THR A 97 1.654 23.678 -27.400 1.00 67.58 C ANISOU 345 CB THR A 97 11045 7206 7427 -611 92 -1147 C ATOM 346 OG1 THR A 97 2.366 23.496 -28.629 1.00 66.39 O ANISOU 346 OG1 THR A 97 10654 7138 7431 -671 -34 -1065 O ATOM 347 CG2 THR A 97 0.374 24.457 -27.669 1.00 65.85 C ANISOU 347 CG2 THR A 97 10999 6766 7254 -327 343 -1165 C ATOM 348 N LYS A 98 4.889 24.019 -26.945 1.00 74.95 N ANISOU 348 N LYS A 98 12000 8336 8141 -1397 -367 -1190 N ATOM 349 CA LYS A 98 6.286 23.602 -26.778 1.00 79.85 C ANISOU 349 CA LYS A 98 12432 9185 8723 -1689 -613 -1139 C ATOM 350 C LYS A 98 6.598 22.185 -27.260 1.00 76.37 C ANISOU 350 C LYS A 98 11536 9019 8463 -1570 -733 -987 C ATOM 351 O LYS A 98 7.750 21.752 -27.106 1.00 90.01 O ANISOU 351 O LYS A 98 13066 10957 10176 -1770 -928 -918 O ATOM 352 CB LYS A 98 6.767 23.721 -25.322 1.00 79.28 C ANISOU 352 CB LYS A 98 12570 9169 8385 -1950 -722 -1208 C ATOM 353 CG LYS A 98 6.857 25.148 -24.813 1.00 85.42 C ANISOU 353 CG LYS A 98 13826 9688 8941 -2183 -644 -1367 C ATOM 354 CD LYS A 98 7.794 25.976 -25.676 1.00 87.92 C ANISOU 354 CD LYS A 98 14156 9950 9298 -2422 -712 -1371 C ATOM 355 CE LYS A 98 8.091 27.321 -25.035 1.00 93.16 C ANISOU 355 CE LYS A 98 15174 10438 9785 -2625 -632 -1442 C ATOM 356 NZ LYS A 98 6.847 28.080 -24.727 1.00 94.56 N ANISOU 356 NZ LYS A 98 15731 10296 9901 -2396 -352 -1540 N ATOM 357 N MET A 99 5.636 21.448 -27.822 1.00 48.25 N ANISOU 357 N MET A 99 7805 5464 5063 -1263 -623 -928 N ATOM 358 CA MET A 99 5.898 20.138 -28.429 1.00 58.94 C ANISOU 358 CA MET A 99 8775 7030 6590 -1149 -704 -795 C ATOM 359 C MET A 99 6.431 19.128 -27.412 1.00 59.86 C ANISOU 359 C MET A 99 8758 7359 6626 -1220 -852 -730 C ATOM 360 O MET A 99 7.364 18.373 -27.692 1.00 54.45 O ANISOU 360 O MET A 99 7800 6865 6024 -1271 -988 -621 O ATOM 361 CB MET A 99 6.861 20.259 -29.614 1.00 66.88 C ANISOU 361 CB MET A 99 9588 8092 7731 -1245 -775 -734 C ATOM 362 CG MET A 99 6.253 19.901 -30.958 1.00 65.96 C ANISOU 362 CG MET A 99 9315 7937 7811 -1023 -670 -679 C ATOM 363 SD MET A 99 7.507 19.743 -32.244 1.00 71.53 S ANISOU 363 SD MET A 99 9764 8754 8662 -1136 -748 -593 S ATOM 364 CE MET A 99 8.279 21.358 -32.162 1.00 66.71 C ANISOU 364 CE MET A 99 9410 8009 7927 -1437 -778 -683 C ATOM 365 N LYS A 100 5.831 19.106 -26.224 1.00 56.26 N ANISOU 365 N LYS A 100 8502 6868 6004 -1209 -814 -787 N ATOM 366 CA LYS A 100 6.210 18.133 -25.208 1.00 57.17 C ANISOU 366 CA LYS A 100 8524 7175 6025 -1258 -947 -715 C ATOM 367 C LYS A 100 5.427 16.832 -25.310 1.00 51.33 C ANISOU 367 C LYS A 100 7596 6505 5401 -1002 -877 -628 C ATOM 368 O LYS A 100 5.844 15.827 -24.724 1.00 53.76 O ANISOU 368 O LYS A 100 7769 6978 5679 -1008 -991 -529 O ATOM 369 CB LYS A 100 6.015 18.721 -23.807 1.00 60.34 C ANISOU 369 CB LYS A 100 9262 7510 6153 -1408 -945 -819 C ATOM 370 CG LYS A 100 6.864 19.948 -23.515 1.00 67.29 C ANISOU 370 CG LYS A 100 10374 8326 6866 -1726 -1034 -912 C ATOM 371 CD LYS A 100 6.481 20.567 -22.181 1.00 71.75 C ANISOU 371 CD LYS A 100 11342 8776 7143 -1859 -984 -1040 C ATOM 372 CE LYS A 100 7.309 21.806 -21.884 1.00 83.75 C ANISOU 372 CE LYS A 100 13139 10211 8470 -2215 -1068 -1146 C ATOM 373 NZ LYS A 100 8.754 21.483 -21.722 1.00 92.27 N ANISOU 373 NZ LYS A 100 13987 11565 9506 -2501 -1366 -1039 N ATOM 374 N THR A 101 4.315 16.826 -26.035 1.00 44.30 N ANISOU 374 N THR A 101 6698 5496 4636 -789 -699 -651 N ATOM 375 CA THR A 101 3.418 15.683 -26.097 1.00 41.13 C ANISOU 375 CA THR A 101 6160 5146 4323 -581 -615 -585 C ATOM 376 C THR A 101 3.440 15.060 -27.485 1.00 44.80 C ANISOU 376 C THR A 101 6368 5646 5007 -463 -602 -506 C ATOM 377 O THR A 101 3.807 15.699 -28.474 1.00 38.56 O ANISOU 377 O THR A 101 5544 4801 4307 -495 -604 -520 O ATOM 378 CB THR A 101 1.986 16.092 -25.739 1.00 49.95 C ANISOU 378 CB THR A 101 7458 6130 5390 -437 -413 -664 C ATOM 379 OG1 THR A 101 1.523 17.074 -26.675 1.00 49.70 O ANISOU 379 OG1 THR A 101 7483 5950 5449 -362 -303 -716 O ATOM 380 CG2 THR A 101 1.935 16.676 -24.334 1.00 46.85 C ANISOU 380 CG2 THR A 101 7359 5683 4758 -552 -394 -754 C ATOM 381 N ALA A 102 3.028 13.792 -27.542 1.00 42.68 N ANISOU 381 N ALA A 102 5948 5458 4809 -339 -579 -424 N ATOM 382 CA ALA A 102 2.952 13.092 -28.819 1.00 41.40 C ANISOU 382 CA ALA A 102 5584 5316 4829 -237 -549 -357 C ATOM 383 C ALA A 102 2.004 13.795 -29.782 1.00 40.52 C ANISOU 383 C ALA A 102 5505 5092 4797 -148 -425 -409 C ATOM 384 O ALA A 102 2.279 13.881 -30.985 1.00 42.55 O ANISOU 384 O ALA A 102 5662 5334 5172 -139 -428 -386 O ATOM 385 CB ALA A 102 2.513 11.644 -28.596 1.00 35.31 C ANISOU 385 CB ALA A 102 4712 4617 4089 -138 -521 -276 C ATOM 386 N THR A 103 0.884 14.312 -29.271 1.00 37.74 N ANISOU 386 N THR A 103 5293 4666 4380 -72 -309 -467 N ATOM 387 CA THR A 103 -0.106 14.943 -30.140 1.00 40.78 C ANISOU 387 CA THR A 103 5684 4964 4845 48 -194 -484 C ATOM 388 C THR A 103 0.461 16.193 -30.805 1.00 36.08 C ANISOU 388 C THR A 103 5187 4258 4266 -14 -213 -529 C ATOM 389 O THR A 103 0.288 16.400 -32.011 1.00 40.10 O ANISOU 389 O THR A 103 5618 4737 4882 37 -194 -497 O ATOM 390 CB THR A 103 -1.368 15.280 -29.345 1.00 50.32 C ANISOU 390 CB THR A 103 7011 6127 5981 162 -48 -523 C ATOM 391 OG1 THR A 103 -1.927 14.076 -28.806 1.00 58.98 O ANISOU 391 OG1 THR A 103 8010 7333 7066 201 -22 -474 O ATOM 392 CG2 THR A 103 -2.399 15.954 -30.241 1.00 50.62 C ANISOU 392 CG2 THR A 103 7024 6099 6112 312 66 -510 C ATOM 393 N ASN A 104 1.151 17.036 -30.033 1.00 37.62 N ANISOU 393 N ASN A 104 5570 4386 4337 -147 -252 -600 N ATOM 394 CA ASN A 104 1.732 18.244 -30.610 1.00 39.54 C ANISOU 394 CA ASN A 104 5938 4507 4580 -240 -264 -646 C ATOM 395 C ASN A 104 2.881 17.921 -31.554 1.00 40.50 C ANISOU 395 C ASN A 104 5880 4711 4796 -353 -383 -589 C ATOM 396 O ASN A 104 3.135 18.676 -32.500 1.00 40.82 O ANISOU 396 O ASN A 104 5953 4666 4891 -385 -369 -595 O ATOM 397 CB ASN A 104 2.197 19.185 -29.501 1.00 37.80 C ANISOU 397 CB ASN A 104 5990 4193 4179 -398 -278 -745 C ATOM 398 CG ASN A 104 1.041 19.867 -28.812 1.00 46.39 C ANISOU 398 CG ASN A 104 7318 5132 5178 -267 -102 -818 C ATOM 399 OD1 ASN A 104 -0.049 19.965 -29.374 1.00 48.59 O ANISOU 399 OD1 ASN A 104 7553 5357 5551 -54 29 -787 O ATOM 400 ND2 ASN A 104 1.266 20.341 -27.592 1.00 44.81 N ANISOU 400 ND2 ASN A 104 7367 4870 4787 -392 -95 -907 N ATOM 401 N ILE A 105 3.580 16.812 -31.315 1.00 38.70 N ANISOU 401 N ILE A 105 5470 4645 4591 -401 -485 -525 N ATOM 402 CA ILE A 105 4.627 16.381 -32.235 1.00 35.71 C ANISOU 402 CA ILE A 105 4896 4353 4318 -468 -563 -458 C ATOM 403 C ILE A 105 4.026 15.987 -33.581 1.00 37.17 C ANISOU 403 C ILE A 105 4970 4514 4640 -334 -482 -416 C ATOM 404 O ILE A 105 4.590 16.291 -34.640 1.00 39.96 O ANISOU 404 O ILE A 105 5269 4848 5064 -384 -487 -397 O ATOM 405 CB ILE A 105 5.439 15.236 -31.601 1.00 35.93 C ANISOU 405 CB ILE A 105 4758 4552 4341 -505 -670 -380 C ATOM 406 CG1 ILE A 105 6.276 15.771 -30.435 1.00 37.32 C ANISOU 406 CG1 ILE A 105 5029 4781 4370 -694 -791 -406 C ATOM 407 CG2 ILE A 105 6.322 14.552 -32.634 1.00 32.69 C ANISOU 407 CG2 ILE A 105 4122 4230 4069 -501 -697 -293 C ATOM 408 CD1 ILE A 105 6.971 14.699 -29.631 1.00 39.06 C ANISOU 408 CD1 ILE A 105 5101 5179 4560 -712 -910 -309 C ATOM 409 N TYR A 106 2.867 15.320 -33.563 1.00 34.96 N ANISOU 409 N TYR A 106 4661 4241 4382 -184 -408 -398 N ATOM 410 CA TYR A 106 2.182 14.978 -34.807 1.00 34.32 C ANISOU 410 CA TYR A 106 4491 4148 4400 -85 -347 -358 C ATOM 411 C TYR A 106 1.612 16.218 -35.486 1.00 40.41 C ANISOU 411 C TYR A 106 5380 4796 5178 -46 -290 -386 C ATOM 412 O TYR A 106 1.682 16.348 -36.715 1.00 33.25 O ANISOU 412 O TYR A 106 4428 3868 4337 -45 -283 -353 O ATOM 413 CB TYR A 106 1.065 13.968 -34.536 1.00 32.43 C ANISOU 413 CB TYR A 106 4188 3966 4168 28 -293 -327 C ATOM 414 CG TYR A 106 1.547 12.583 -34.155 1.00 38.02 C ANISOU 414 CG TYR A 106 4789 4771 4888 12 -330 -278 C ATOM 415 CD1 TYR A 106 2.618 11.994 -34.814 1.00 38.04 C ANISOU 415 CD1 TYR A 106 4686 4810 4956 -34 -370 -234 C ATOM 416 CD2 TYR A 106 0.930 11.866 -33.135 1.00 32.34 C ANISOU 416 CD2 TYR A 106 4082 4096 4111 56 -306 -268 C ATOM 417 CE1 TYR A 106 3.061 10.730 -34.473 1.00 39.42 C ANISOU 417 CE1 TYR A 106 4779 5052 5147 -14 -384 -174 C ATOM 418 CE2 TYR A 106 1.368 10.597 -32.781 1.00 31.03 C ANISOU 418 CE2 TYR A 106 3844 3995 3950 53 -333 -210 C ATOM 419 CZ TYR A 106 2.432 10.035 -33.456 1.00 34.94 C ANISOU 419 CZ TYR A 106 4242 4513 4518 29 -371 -160 C ATOM 420 OH TYR A 106 2.878 8.780 -33.121 1.00 37.20 O ANISOU 420 OH TYR A 106 4472 4844 4817 59 -379 -89 O ATOM 421 N ILE A 107 1.036 17.134 -34.704 1.00 34.40 N ANISOU 421 N ILE A 107 4788 3941 4340 -5 -237 -440 N ATOM 422 CA ILE A 107 0.442 18.341 -35.273 1.00 40.03 C ANISOU 422 CA ILE A 107 5637 4514 5060 70 -163 -450 C ATOM 423 C ILE A 107 1.506 19.193 -35.953 1.00 42.24 C ANISOU 423 C ILE A 107 6001 4707 5342 -71 -206 -468 C ATOM 424 O ILE A 107 1.298 19.700 -37.062 1.00 37.11 O ANISOU 424 O ILE A 107 5366 3990 4743 -30 -180 -430 O ATOM 425 CB ILE A 107 -0.310 19.132 -34.187 1.00 41.04 C ANISOU 425 CB ILE A 107 5960 4536 5096 155 -65 -510 C ATOM 426 CG1 ILE A 107 -1.523 18.341 -33.690 1.00 41.09 C ANISOU 426 CG1 ILE A 107 5859 4638 5115 309 5 -475 C ATOM 427 CG2 ILE A 107 -0.748 20.491 -34.717 1.00 38.68 C ANISOU 427 CG2 ILE A 107 5841 4055 4800 242 23 -516 C ATOM 428 CD1 ILE A 107 -2.248 19.002 -32.521 1.00 41.14 C ANISOU 428 CD1 ILE A 107 6052 4552 5026 403 131 -534 C ATOM 429 N PHE A 108 2.664 19.361 -35.308 1.00 35.77 N ANISOU 429 N PHE A 108 5231 3900 4460 -253 -279 -516 N ATOM 430 CA PHE A 108 3.728 20.150 -35.920 1.00 41.08 C ANISOU 430 CA PHE A 108 5966 4511 5133 -423 -319 -528 C ATOM 431 C PHE A 108 4.224 19.496 -37.203 1.00 41.68 C ANISOU 431 C PHE A 108 5840 4677 5318 -437 -345 -455 C ATOM 432 O PHE A 108 4.457 20.180 -38.206 1.00 37.04 O ANISOU 432 O PHE A 108 5310 4005 4758 -480 -320 -440 O ATOM 433 CB PHE A 108 4.887 20.347 -34.942 1.00 39.30 C ANISOU 433 CB PHE A 108 5787 4332 4814 -643 -413 -577 C ATOM 434 CG PHE A 108 5.969 21.251 -35.469 1.00 42.62 C ANISOU 434 CG PHE A 108 6278 4696 5220 -856 -450 -593 C ATOM 435 CD1 PHE A 108 7.011 20.742 -36.229 1.00 46.55 C ANISOU 435 CD1 PHE A 108 6556 5328 5804 -957 -511 -529 C ATOM 436 CD2 PHE A 108 5.933 22.615 -35.220 1.00 45.08 C ANISOU 436 CD2 PHE A 108 6888 4808 5431 -955 -403 -670 C ATOM 437 CE1 PHE A 108 7.997 21.573 -36.726 1.00 43.28 C ANISOU 437 CE1 PHE A 108 6190 4877 5378 -1169 -533 -537 C ATOM 438 CE2 PHE A 108 6.920 23.452 -35.712 1.00 46.34 C ANISOU 438 CE2 PHE A 108 7128 4910 5569 -1181 -431 -684 C ATOM 439 CZ PHE A 108 7.952 22.930 -36.466 1.00 44.51 C ANISOU 439 CZ PHE A 108 6646 4839 5426 -1295 -501 -615 C ATOM 440 N ASN A 109 4.399 18.172 -37.187 1.00 36.64 N ANISOU 440 N ASN A 109 4993 4193 4735 -402 -381 -408 N ATOM 441 CA ASN A 109 4.825 17.463 -38.389 1.00 38.44 C ANISOU 441 CA ASN A 109 5060 4489 5055 -402 -374 -347 C ATOM 442 C ASN A 109 3.816 17.627 -39.516 1.00 41.26 C ANISOU 442 C ASN A 109 5453 4778 5445 -290 -310 -318 C ATOM 443 O ASN A 109 4.199 17.738 -40.687 1.00 40.10 O ANISOU 443 O ASN A 109 5286 4615 5336 -335 -292 -287 O ATOM 444 CB ASN A 109 5.035 15.980 -38.071 1.00 39.64 C ANISOU 444 CB ASN A 109 5030 4782 5249 -355 -396 -304 C ATOM 445 CG ASN A 109 5.900 15.279 -39.097 1.00 38.92 C ANISOU 445 CG ASN A 109 4792 4755 5240 -387 -377 -250 C ATOM 446 OD1 ASN A 109 7.117 15.445 -39.111 1.00 43.31 O ANISOU 446 OD1 ASN A 109 5272 5366 5818 -499 -409 -233 O ATOM 447 ND2 ASN A 109 5.278 14.474 -39.949 1.00 39.15 N ANISOU 447 ND2 ASN A 109 4781 4785 5310 -297 -317 -222 N ATOM 448 N LEU A 110 2.524 17.647 -39.183 1.00 40.63 N ANISOU 448 N LEU A 110 5419 4674 5346 -148 -276 -316 N ATOM 449 CA LEU A 110 1.499 17.839 -40.201 1.00 36.80 C ANISOU 449 CA LEU A 110 4942 4156 4885 -40 -238 -264 C ATOM 450 C LEU A 110 1.527 19.260 -40.750 1.00 38.28 C ANISOU 450 C LEU A 110 5302 4192 5051 -48 -212 -263 C ATOM 451 O LEU A 110 1.437 19.466 -41.967 1.00 33.47 O ANISOU 451 O LEU A 110 4696 3559 4460 -47 -208 -208 O ATOM 452 CB LEU A 110 0.123 17.512 -39.620 1.00 34.33 C ANISOU 452 CB LEU A 110 4596 3886 4564 113 -206 -246 C ATOM 453 CG LEU A 110 -1.072 17.587 -40.575 1.00 42.10 C ANISOU 453 CG LEU A 110 5534 4890 5570 229 -188 -166 C ATOM 454 CD1 LEU A 110 -0.905 16.599 -41.722 1.00 37.24 C ANISOU 454 CD1 LEU A 110 4803 4367 4980 154 -226 -123 C ATOM 455 CD2 LEU A 110 -2.375 17.335 -39.831 1.00 36.08 C ANISOU 455 CD2 LEU A 110 4710 4193 4804 371 -147 -142 C ATOM 456 N ALA A 111 1.659 20.253 -39.867 1.00 37.27 N ANISOU 456 N ALA A 111 5347 3947 4868 -65 -188 -321 N ATOM 457 CA ALA A 111 1.675 21.642 -40.310 1.00 40.38 C ANISOU 457 CA ALA A 111 5953 4158 5233 -71 -144 -321 C ATOM 458 C ALA A 111 2.900 21.936 -41.166 1.00 41.27 C ANISOU 458 C ALA A 111 6082 4246 5352 -262 -175 -320 C ATOM 459 O ALA A 111 2.807 22.661 -42.162 1.00 40.23 O ANISOU 459 O ALA A 111 6053 4010 5221 -254 -146 -273 O ATOM 460 CB ALA A 111 1.626 22.579 -39.103 1.00 31.94 C ANISOU 460 CB ALA A 111 5107 2946 4083 -76 -94 -403 C ATOM 461 N LEU A 112 4.056 21.381 -40.794 1.00 36.20 N ANISOU 461 N LEU A 112 5330 3709 4715 -430 -229 -355 N ATOM 462 CA LEU A 112 5.262 21.585 -41.590 1.00 40.94 C ANISOU 462 CA LEU A 112 5903 4320 5333 -614 -243 -344 C ATOM 463 C LEU A 112 5.106 20.995 -42.987 1.00 38.12 C ANISOU 463 C LEU A 112 5436 4015 5031 -562 -218 -271 C ATOM 464 O LEU A 112 5.461 21.634 -43.984 1.00 34.28 O ANISOU 464 O LEU A 112 5036 3452 4538 -638 -187 -243 O ATOM 465 CB LEU A 112 6.466 20.971 -40.877 1.00 40.03 C ANISOU 465 CB LEU A 112 5632 4350 5226 -769 -307 -368 C ATOM 466 CG LEU A 112 7.811 21.040 -41.601 1.00 41.57 C ANISOU 466 CG LEU A 112 5731 4606 5456 -959 -312 -342 C ATOM 467 CD1 LEU A 112 8.209 22.488 -41.865 1.00 41.38 C ANISOU 467 CD1 LEU A 112 5931 4421 5371 -1125 -290 -372 C ATOM 468 CD2 LEU A 112 8.885 20.323 -40.796 1.00 45.01 C ANISOU 468 CD2 LEU A 112 5963 5225 5913 -1067 -386 -336 C ATOM 469 N ALA A 113 4.571 19.776 -43.080 1.00 31.62 N ANISOU 469 N ALA A 113 4451 3316 4249 -452 -227 -243 N ATOM 470 CA ALA A 113 4.363 19.162 -44.388 1.00 32.47 C ANISOU 470 CA ALA A 113 4490 3468 4380 -425 -202 -186 C ATOM 471 C ALA A 113 3.343 19.940 -45.208 1.00 36.70 C ANISOU 471 C ALA A 113 5158 3906 4880 -334 -191 -130 C ATOM 472 O ALA A 113 3.522 20.131 -46.417 1.00 37.48 O ANISOU 472 O ALA A 113 5301 3978 4963 -385 -172 -85 O ATOM 473 CB ALA A 113 3.920 17.711 -44.217 1.00 26.60 C ANISOU 473 CB ALA A 113 3586 2854 3666 -346 -209 -175 C ATOM 474 N ASP A 114 2.268 20.401 -44.567 1.00 35.20 N ANISOU 474 N ASP A 114 5032 3667 4675 -189 -196 -122 N ATOM 475 CA ASP A 114 1.241 21.147 -45.286 1.00 38.59 C ANISOU 475 CA ASP A 114 5561 4020 5082 -63 -189 -40 C ATOM 476 C ASP A 114 1.748 22.506 -45.751 1.00 41.43 C ANISOU 476 C ASP A 114 6137 4197 5406 -125 -154 -30 C ATOM 477 O ASP A 114 1.364 22.971 -46.830 1.00 38.49 O ANISOU 477 O ASP A 114 5840 3774 5009 -85 -155 58 O ATOM 478 CB ASP A 114 0.000 21.301 -44.406 1.00 38.51 C ANISOU 478 CB ASP A 114 5542 4011 5077 131 -176 -24 C ATOM 479 CG ASP A 114 -0.779 20.002 -44.270 1.00 51.63 C ANISOU 479 CG ASP A 114 6996 5858 6764 192 -210 0 C ATOM 480 OD1 ASP A 114 -0.683 19.154 -45.183 1.00 54.84 O1- ANISOU 480 OD1 ASP A 114 7305 6363 7168 117 -246 32 O1- ATOM 481 OD2 ASP A 114 -1.486 19.828 -43.256 1.00 56.10 O ANISOU 481 OD2 ASP A 114 7516 6460 7339 301 -188 -16 O ATOM 482 N ALA A 115 2.608 23.156 -44.962 1.00 39.13 N ANISOU 482 N ALA A 115 5963 3807 5099 -241 -129 -111 N ATOM 483 CA ALA A 115 3.194 24.418 -45.402 1.00 40.65 C ANISOU 483 CA ALA A 115 6384 3814 5248 -347 -88 -109 C ATOM 484 C ALA A 115 4.135 24.206 -46.583 1.00 42.56 C ANISOU 484 C ALA A 115 6579 4102 5491 -518 -89 -80 C ATOM 485 O ALA A 115 4.138 25.000 -47.531 1.00 42.31 O ANISOU 485 O ALA A 115 6706 3950 5422 -542 -59 -19 O ATOM 486 CB ALA A 115 3.928 25.090 -44.244 1.00 40.00 C ANISOU 486 CB ALA A 115 6440 3631 5128 -483 -71 -212 C ATOM 487 N LEU A 116 4.943 23.144 -46.544 1.00 39.38 N ANISOU 487 N LEU A 116 5969 3865 5128 -628 -108 -115 N ATOM 488 CA LEU A 116 5.849 22.868 -47.655 1.00 46.50 C ANISOU 488 CA LEU A 116 6816 4816 6034 -773 -75 -89 C ATOM 489 C LEU A 116 5.086 22.490 -48.917 1.00 41.35 C ANISOU 489 C LEU A 116 6167 4189 5356 -681 -72 -6 C ATOM 490 O LEU A 116 5.501 22.856 -50.024 1.00 40.37 O ANISOU 490 O LEU A 116 6130 4016 5191 -777 -30 36 O ATOM 491 CB LEU A 116 6.832 21.760 -47.271 1.00 41.31 C ANISOU 491 CB LEU A 116 5927 4331 5436 -864 -76 -131 C ATOM 492 CG LEU A 116 7.938 22.164 -46.294 1.00 45.04 C ANISOU 492 CG LEU A 116 6371 4822 5920 -1030 -94 -188 C ATOM 493 CD1 LEU A 116 8.667 20.941 -45.757 1.00 40.90 C ANISOU 493 CD1 LEU A 116 5585 4491 5463 -1046 -113 -198 C ATOM 494 CD2 LEU A 116 8.916 23.119 -46.966 1.00 42.26 C ANISOU 494 CD2 LEU A 116 6124 4392 5541 -1241 -45 -178 C ATOM 495 N ALA A 117 3.970 21.771 -48.771 1.00 37.55 N ANISOU 495 N ALA A 117 5594 3789 4883 -518 -117 20 N ATOM 496 CA ALA A 117 3.159 21.406 -49.928 1.00 38.91 C ANISOU 496 CA ALA A 117 5768 4009 5009 -457 -140 105 C ATOM 497 C ALA A 117 2.637 22.644 -50.645 1.00 40.28 C ANISOU 497 C ALA A 117 6139 4042 5122 -404 -149 198 C ATOM 498 O ALA A 117 2.754 22.764 -51.871 1.00 40.11 O ANISOU 498 O ALA A 117 6197 4009 5036 -473 -142 262 O ATOM 499 CB ALA A 117 1.999 20.507 -49.494 1.00 33.82 C ANISOU 499 CB ALA A 117 4982 3487 4380 -314 -198 122 C ATOM 500 N THR A 118 2.059 23.585 -49.894 1.00 37.59 N ANISOU 500 N THR A 118 5903 3585 4793 -274 -152 212 N ATOM 501 CA THR A 118 1.531 24.790 -50.518 1.00 39.93 C ANISOU 501 CA THR A 118 6406 3726 5039 -185 -146 318 C ATOM 502 C THR A 118 2.634 25.737 -50.971 1.00 40.13 C ANISOU 502 C THR A 118 6641 3583 5024 -364 -79 300 C ATOM 503 O THR A 118 2.367 26.629 -51.783 1.00 44.50 O ANISOU 503 O THR A 118 7384 4004 5518 -328 -69 402 O ATOM 504 CB THR A 118 0.573 25.508 -49.565 1.00 49.41 C ANISOU 504 CB THR A 118 7676 4829 6268 35 -132 341 C ATOM 505 OG1 THR A 118 1.233 25.771 -48.322 1.00 49.57 O ANISOU 505 OG1 THR A 118 7753 4766 6316 -36 -79 211 O ATOM 506 CG2 THR A 118 -0.659 24.648 -49.309 1.00 47.20 C ANISOU 506 CG2 THR A 118 7178 4733 6023 213 -194 394 C ATOM 507 N SER A 119 3.866 25.553 -50.486 1.00 38.77 N ANISOU 507 N SER A 119 6429 3424 4879 -562 -38 188 N ATOM 508 CA SER A 119 4.972 26.390 -50.935 1.00 42.05 C ANISOU 508 CA SER A 119 7012 3711 5256 -773 28 173 C ATOM 509 C SER A 119 5.354 26.124 -52.387 1.00 38.66 C ANISOU 509 C SER A 119 6586 3329 4774 -878 53 239 C ATOM 510 O SER A 119 6.067 26.938 -52.981 1.00 41.99 O ANISOU 510 O SER A 119 7180 3628 5146 -1034 116 259 O ATOM 511 CB SER A 119 6.195 26.191 -50.037 1.00 43.09 C ANISOU 511 CB SER A 119 7046 3895 5430 -970 50 55 C ATOM 512 OG SER A 119 6.815 24.941 -50.284 1.00 42.83 O ANISOU 512 OG SER A 119 6760 4071 5445 -1042 50 29 O ATOM 513 N THR A 120 4.902 25.013 -52.971 1.00 41.13 N ANISOU 513 N THR A 120 6737 3808 5082 -816 16 270 N ATOM 514 CA THR A 120 5.166 24.750 -54.381 1.00 44.69 C ANISOU 514 CA THR A 120 7232 4294 5455 -916 48 329 C ATOM 515 C THR A 120 4.185 25.459 -55.307 1.00 48.12 C ANISOU 515 C THR A 120 7851 4641 5791 -809 -6 471 C ATOM 516 O THR A 120 4.455 25.553 -56.510 1.00 48.32 O ANISOU 516 O THR A 120 7986 4653 5721 -915 24 532 O ATOM 517 CB THR A 120 5.121 23.245 -54.664 1.00 43.40 C ANISOU 517 CB THR A 120 6864 4324 5301 -920 42 295 C ATOM 518 OG1 THR A 120 3.763 22.788 -54.615 1.00 41.21 O ANISOU 518 OG1 THR A 120 6527 4125 5005 -747 -64 351 O ATOM 519 CG2 THR A 120 5.947 22.479 -53.639 1.00 41.11 C ANISOU 519 CG2 THR A 120 6374 4129 5119 -967 82 182 C ATOM 520 N LEU A 121 3.068 25.957 -54.777 1.00 45.47 N ANISOU 520 N LEU A 121 7550 4254 5474 -596 -77 535 N ATOM 521 CA LEU A 121 2.035 26.541 -55.629 1.00 42.50 C ANISOU 521 CA LEU A 121 7301 3832 5015 -454 -145 703 C ATOM 522 C LEU A 121 2.479 27.785 -56.391 1.00 42.33 C ANISOU 522 C LEU A 121 7572 3599 4913 -528 -87 784 C ATOM 523 O LEU A 121 2.042 27.945 -57.545 1.00 48.67 O ANISOU 523 O LEU A 121 8471 4413 5608 -512 -137 921 O ATOM 524 CB LEU A 121 0.787 26.838 -54.788 1.00 41.62 C ANISOU 524 CB LEU A 121 7136 3714 4963 -181 -206 764 C ATOM 525 CG LEU A 121 0.053 25.597 -54.275 1.00 47.59 C ANISOU 525 CG LEU A 121 7610 4700 5772 -97 -281 731 C ATOM 526 CD1 LEU A 121 -1.135 25.981 -53.407 1.00 46.36 C ANISOU 526 CD1 LEU A 121 7396 4537 5681 173 -311 796 C ATOM 527 CD2 LEU A 121 -0.389 24.723 -55.438 1.00 48.72 C ANISOU 527 CD2 LEU A 121 7661 5027 5822 -160 -372 811 C ATOM 528 N PRO A 122 3.290 28.700 -55.839 1.00 44.44 N ANISOU 528 N PRO A 122 8006 3671 5208 -623 9 716 N ATOM 529 CA PRO A 122 3.761 29.817 -56.676 1.00 48.60 C ANISOU 529 CA PRO A 122 8831 3992 5642 -732 75 795 C ATOM 530 C PRO A 122 4.522 29.355 -57.906 1.00 46.99 C ANISOU 530 C PRO A 122 8629 3876 5349 -953 111 807 C ATOM 531 O PRO A 122 4.412 29.980 -58.968 1.00 46.49 O ANISOU 531 O PRO A 122 8780 3714 5171 -978 117 935 O ATOM 532 CB PRO A 122 4.647 30.625 -55.719 1.00 44.16 C ANISOU 532 CB PRO A 122 8406 3247 5128 -866 173 678 C ATOM 533 CG PRO A 122 4.096 30.321 -54.361 1.00 41.67 C ANISOU 533 CG PRO A 122 7946 2976 4910 -701 137 597 C ATOM 534 CD PRO A 122 3.683 28.879 -54.426 1.00 40.84 C ANISOU 534 CD PRO A 122 7516 3154 4846 -635 53 580 C ATOM 535 N PHE A 123 5.288 28.267 -57.795 1.00 43.45 N ANISOU 535 N PHE A 123 7957 3606 4945 -1102 148 686 N ATOM 536 CA PHE A 123 5.943 27.704 -58.971 1.00 46.19 C ANISOU 536 CA PHE A 123 8302 4044 5206 -1284 210 692 C ATOM 537 C PHE A 123 4.920 27.166 -59.963 1.00 48.77 C ANISOU 537 C PHE A 123 8635 4477 5420 -1181 109 807 C ATOM 538 O PHE A 123 5.046 27.380 -61.174 1.00 47.05 O ANISOU 538 O PHE A 123 8585 4230 5062 -1283 134 893 O ATOM 539 CB PHE A 123 6.916 26.597 -58.558 1.00 45.53 C ANISOU 539 CB PHE A 123 7966 4124 5210 -1414 288 548 C ATOM 540 CG PHE A 123 8.028 27.066 -57.665 1.00 52.69 C ANISOU 540 CG PHE A 123 8834 4975 6211 -1558 369 451 C ATOM 541 CD1 PHE A 123 9.215 27.535 -58.203 1.00 52.11 C ANISOU 541 CD1 PHE A 123 8842 4851 6106 -1799 498 442 C ATOM 542 CD2 PHE A 123 7.887 27.034 -56.284 1.00 54.02 C ANISOU 542 CD2 PHE A 123 8882 5155 6488 -1473 313 374 C ATOM 543 CE1 PHE A 123 10.241 27.968 -57.385 1.00 55.66 C ANISOU 543 CE1 PHE A 123 9235 5280 6633 -1967 554 363 C ATOM 544 CE2 PHE A 123 8.910 27.466 -55.457 1.00 52.63 C ANISOU 544 CE2 PHE A 123 8675 4946 6374 -1639 364 290 C ATOM 545 CZ PHE A 123 10.089 27.934 -56.009 1.00 54.62 C ANISOU 545 CZ PHE A 123 8989 5166 6597 -1893 476 288 C ATOM 546 N GLN A 124 3.893 26.472 -59.464 1.00 47.06 N ANISOU 546 N GLN A 124 8240 4394 5249 -1000 -9 815 N ATOM 547 CA GLN A 124 2.889 25.892 -60.348 1.00 45.94 C ANISOU 547 CA GLN A 124 8075 4388 4990 -938 -129 924 C ATOM 548 C GLN A 124 2.046 26.969 -61.019 1.00 47.60 C ANISOU 548 C GLN A 124 8489 4497 5099 -814 -221 1125 C ATOM 549 O GLN A 124 1.646 26.818 -62.180 1.00 46.26 O ANISOU 549 O GLN A 124 8406 4397 4772 -863 -292 1241 O ATOM 550 CB GLN A 124 2.005 24.922 -59.563 1.00 38.61 C ANISOU 550 CB GLN A 124 6894 3634 4144 -796 -229 887 C ATOM 551 CG GLN A 124 2.752 23.701 -59.049 1.00 36.71 C ANISOU 551 CG GLN A 124 6467 3501 3980 -905 -146 715 C ATOM 552 CD GLN A 124 1.826 22.637 -58.494 1.00 39.59 C ANISOU 552 CD GLN A 124 6619 4037 4387 -800 -244 692 C ATOM 553 OE1 GLN A 124 0.846 22.254 -59.134 1.00 44.76 O ANISOU 553 OE1 GLN A 124 7258 4807 4941 -773 -360 787 O ATOM 554 NE2 GLN A 124 2.131 22.155 -57.295 1.00 37.08 N ANISOU 554 NE2 GLN A 124 6136 3746 4207 -758 -203 574 N ATOM 555 N SER A 125 1.761 28.060 -60.309 1.00 44.75 N ANISOU 555 N SER A 125 8221 3966 4815 -651 -217 1175 N ATOM 556 CA SER A 125 1.011 29.156 -60.911 1.00 48.84 C ANISOU 556 CA SER A 125 8951 4357 5249 -498 -282 1384 C ATOM 557 C SER A 125 1.775 29.750 -62.088 1.00 53.07 C ANISOU 557 C SER A 125 9763 4764 5638 -695 -210 1445 C ATOM 558 O SER A 125 1.260 29.815 -63.210 1.00 56.61 O ANISOU 558 O SER A 125 10313 5264 5932 -691 -301 1608 O ATOM 559 CB SER A 125 0.707 30.225 -59.862 1.00 58.34 C ANISOU 559 CB SER A 125 10248 5352 6566 -290 -238 1402 C ATOM 560 OG SER A 125 1.900 30.723 -59.285 1.00 77.79 O ANISOU 560 OG SER A 125 12841 7633 9082 -462 -87 1251 O ATOM 561 N VAL A 126 3.020 30.176 -61.847 1.00 51.16 N ANISOU 561 N VAL A 126 9640 4367 5430 -888 -49 1321 N ATOM 562 CA VAL A 126 3.857 30.732 -62.912 1.00 51.42 C ANISOU 562 CA VAL A 126 9929 4278 5328 -1107 50 1366 C ATOM 563 C VAL A 126 3.974 29.747 -64.066 1.00 53.81 C ANISOU 563 C VAL A 126 10181 4773 5490 -1259 31 1376 C ATOM 564 O VAL A 126 3.909 30.129 -65.241 1.00 51.45 O ANISOU 564 O VAL A 126 10101 4430 5016 -1332 20 1510 O ATOM 565 CB VAL A 126 5.243 31.114 -62.359 1.00 56.39 C ANISOU 565 CB VAL A 126 10609 4780 6036 -1331 226 1209 C ATOM 566 CG1 VAL A 126 6.167 31.547 -63.490 1.00 56.26 C ANISOU 566 CG1 VAL A 126 10821 4674 5882 -1588 350 1247 C ATOM 567 CG2 VAL A 126 5.114 32.215 -61.317 1.00 56.66 C ANISOU 567 CG2 VAL A 126 10780 4584 6162 -1217 250 1203 C ATOM 568 N ASN A 127 4.147 28.462 -63.747 1.00 49.91 N ANISOU 568 N ASN A 127 9425 4482 5057 -1311 37 1234 N ATOM 569 CA ASN A 127 4.192 27.440 -64.785 1.00 53.68 C ANISOU 569 CA ASN A 127 9879 5125 5391 -1450 34 1226 C ATOM 570 C ASN A 127 2.919 27.439 -65.622 1.00 60.12 C ANISOU 570 C ASN A 127 10770 6030 6045 -1344 -160 1415 C ATOM 571 O ASN A 127 2.970 27.165 -66.827 1.00 66.23 O ANISOU 571 O ASN A 127 11688 6857 6619 -1495 -164 1474 O ATOM 572 CB ASN A 127 4.426 26.066 -64.153 1.00 52.67 C ANISOU 572 CB ASN A 127 9470 5171 5369 -1475 68 1053 C ATOM 573 CG ASN A 127 4.524 24.958 -65.181 1.00 59.71 C ANISOU 573 CG ASN A 127 10378 6202 6107 -1628 101 1020 C ATOM 574 OD1 ASN A 127 5.579 24.740 -65.776 1.00 63.30 O ANISOU 574 OD1 ASN A 127 10915 6630 6507 -1817 282 948 O ATOM 575 ND2 ASN A 127 3.423 24.246 -65.391 1.00 65.68 N ANISOU 575 ND2 ASN A 127 11060 7109 6786 -1557 -62 1073 N ATOM 576 N TYR A 128 1.775 27.763 -65.013 1.00 61.86 N ANISOU 576 N TYR A 128 10891 6275 6337 -1092 -319 1523 N ATOM 577 CA TYR A 128 0.530 27.833 -65.769 1.00 64.74 C ANISOU 577 CA TYR A 128 11285 6756 6559 -977 -524 1737 C ATOM 578 C TYR A 128 0.438 29.116 -66.589 1.00 68.82 C ANISOU 578 C TYR A 128 12104 7097 6947 -938 -544 1943 C ATOM 579 O TYR A 128 0.053 29.078 -67.762 1.00 72.91 O ANISOU 579 O TYR A 128 12753 7695 7253 -1013 -649 2093 O ATOM 580 CB TYR A 128 -0.674 27.717 -64.835 1.00 52.59 C ANISOU 580 CB TYR A 128 9500 5330 5154 -705 -673 1799 C ATOM 581 CG TYR A 128 -1.952 28.209 -65.476 1.00 62.72 C ANISOU 581 CG TYR A 128 10807 6699 6324 -526 -880 2074 C ATOM 582 CD1 TYR A 128 -2.619 27.438 -66.420 1.00 72.45 C ANISOU 582 CD1 TYR A 128 11980 8173 7372 -633 -1051 2172 C ATOM 583 CD2 TYR A 128 -2.480 29.454 -65.154 1.00 61.54 C ANISOU 583 CD2 TYR A 128 10750 6388 6244 -255 -901 2246 C ATOM 584 CE1 TYR A 128 -3.781 27.890 -67.020 1.00 75.42 C ANISOU 584 CE1 TYR A 128 12350 8666 7641 -478 -1264 2449 C ATOM 585 CE2 TYR A 128 -3.640 29.913 -65.748 1.00 68.38 C ANISOU 585 CE2 TYR A 128 11615 7348 7019 -61 -1090 2528 C ATOM 586 CZ TYR A 128 -4.286 29.127 -66.679 1.00 74.70 C ANISOU 586 CZ TYR A 128 12316 8427 7641 -176 -1284 2636 C ATOM 587 OH TYR A 128 -5.442 29.583 -67.270 1.00 82.90 O ANISOU 587 OH TYR A 128 13320 9594 8583 11 -1496 2941 O ATOM 588 N LEU A 129 0.760 30.262 -65.983 1.00 67.11 N ANISOU 588 N LEU A 129 12025 6633 6840 -829 -447 1959 N ATOM 589 CA LEU A 129 0.747 31.545 -66.683 1.00 76.46 C ANISOU 589 CA LEU A 129 13538 7601 7912 -787 -436 2152 C ATOM 590 C LEU A 129 1.506 31.471 -67.997 1.00 75.70 C ANISOU 590 C LEU A 129 13671 7493 7601 -1074 -368 2169 C ATOM 591 O LEU A 129 0.930 31.610 -69.081 1.00 81.95 O ANISOU 591 O LEU A 129 14583 8353 8200 -1069 -494 2356 O ATOM 592 CB LEU A 129 1.390 32.646 -65.839 1.00 84.84 C ANISOU 592 CB LEU A 129 14765 8360 9109 -744 -272 2088 C ATOM 593 CG LEU A 129 0.688 33.430 -64.739 1.00 93.76 C ANISOU 593 CG LEU A 129 15884 9341 10398 -432 -286 2142 C ATOM 594 CD1 LEU A 129 0.942 32.770 -63.432 1.00 93.40 C ANISOU 594 CD1 LEU A 129 15575 9372 10540 -430 -233 1915 C ATOM 595 CD2 LEU A 129 1.258 34.828 -64.705 1.00104.03 C ANISOU 595 CD2 LEU A 129 17524 10304 11698 -447 -139 2170 C ATOM 596 N MET A 130 2.818 31.266 -67.891 1.00 69.65 N ANISOU 596 N MET A 130 12937 6655 6871 -1323 -161 1969 N ATOM 597 CA MET A 130 3.706 31.271 -69.041 1.00 76.07 C ANISOU 597 CA MET A 130 13931 7453 7520 -1589 -36 1940 C ATOM 598 C MET A 130 3.542 30.042 -69.919 1.00 67.04 C ANISOU 598 C MET A 130 12726 6542 6205 -1736 -90 1918 C ATOM 599 O MET A 130 4.119 30.006 -71.011 1.00 66.30 O ANISOU 599 O MET A 130 12757 6468 5965 -1920 1 1886 O ATOM 600 CB MET A 130 5.152 31.380 -68.559 1.00 78.91 C ANISOU 600 CB MET A 130 14271 7710 8001 -1790 206 1732 C ATOM 601 CG MET A 130 5.346 32.404 -67.450 1.00 79.21 C ANISOU 601 CG MET A 130 14340 7541 8216 -1684 256 1702 C ATOM 602 SD MET A 130 4.766 34.046 -67.921 1.00 91.71 S ANISOU 602 SD MET A 130 16199 8908 9738 -1504 202 1895 S ATOM 603 CE MET A 130 4.922 34.917 -66.365 1.00 94.83 C ANISOU 603 CE MET A 130 16600 9083 10347 -1382 273 1805 C ATOM 604 N GLY A 131 2.771 29.050 -69.478 1.00 57.77 N ANISOU 604 N GLY A 131 11307 5566 5075 -1640 -228 1888 N ATOM 605 CA GLY A 131 2.672 27.801 -70.212 1.00 66.69 C ANISOU 605 CA GLY A 131 12385 6905 6048 -1805 -257 1825 C ATOM 606 C GLY A 131 4.003 27.109 -70.389 1.00 70.85 C ANISOU 606 C GLY A 131 12922 7418 6580 -2048 2 1611 C ATOM 607 O GLY A 131 4.221 26.443 -71.406 1.00 68.92 O ANISOU 607 O GLY A 131 12804 7252 6132 -2241 57 1584 O ATOM 608 N THR A 132 4.907 27.258 -69.422 1.00 71.11 N ANISOU 608 N THR A 132 12825 7358 6835 -2042 168 1462 N ATOM 609 CA THR A 132 6.283 26.796 -69.540 1.00 68.12 C ANISOU 609 CA THR A 132 12431 6961 6489 -2249 432 1292 C ATOM 610 C THR A 132 6.927 26.854 -68.163 1.00 65.02 C ANISOU 610 C THR A 132 11797 6533 6374 -2182 519 1153 C ATOM 611 O THR A 132 6.625 27.755 -67.376 1.00 64.28 O ANISOU 611 O THR A 132 11697 6330 6398 -2046 438 1206 O ATOM 612 CB THR A 132 7.073 27.661 -70.537 1.00 74.02 C ANISOU 612 CB THR A 132 13420 7590 7115 -2404 572 1330 C ATOM 613 OG1 THR A 132 6.500 27.534 -71.844 1.00 87.22 O ANISOU 613 OG1 THR A 132 15266 9332 8543 -2450 477 1420 O ATOM 614 CG2 THR A 132 8.532 27.247 -70.598 1.00 65.17 C ANISOU 614 CG2 THR A 132 12203 6488 6071 -2576 848 1147 C ATOM 615 N TRP A 133 7.801 25.886 -67.875 1.00 62.25 N ANISOU 615 N TRP A 133 11261 6273 6117 -2272 686 984 N ATOM 616 CA TRP A 133 8.572 25.890 -66.639 1.00 59.33 C ANISOU 616 CA TRP A 133 10656 5898 5991 -2245 772 861 C ATOM 617 C TRP A 133 9.813 26.749 -66.835 1.00 60.73 C ANISOU 617 C TRP A 133 10934 5957 6184 -2436 965 854 C ATOM 618 O TRP A 133 10.702 26.361 -67.612 1.00 60.73 O ANISOU 618 O TRP A 133 10971 5994 6111 -2610 1166 812 O ATOM 619 CB TRP A 133 8.962 24.474 -66.239 1.00 55.70 C ANISOU 619 CB TRP A 133 9940 5593 5629 -2237 862 711 C ATOM 620 CG TRP A 133 9.773 24.414 -64.981 1.00 51.04 C ANISOU 620 CG TRP A 133 9091 5027 5276 -2211 933 604 C ATOM 621 CD1 TRP A 133 11.134 24.418 -64.880 1.00 46.45 C ANISOU 621 CD1 TRP A 133 8407 4460 4783 -2354 1141 536 C ATOM 622 CD2 TRP A 133 9.271 24.344 -63.640 1.00 48.16 C ANISOU 622 CD2 TRP A 133 8528 4692 5079 -2041 791 566 C ATOM 623 NE1 TRP A 133 11.510 24.353 -63.558 1.00 50.15 N ANISOU 623 NE1 TRP A 133 8623 4976 5457 -2292 1113 463 N ATOM 624 CE2 TRP A 133 10.385 24.307 -62.778 1.00 45.74 C ANISOU 624 CE2 TRP A 133 8021 4417 4943 -2102 905 473 C ATOM 625 CE3 TRP A 133 7.987 24.309 -63.085 1.00 48.43 C ANISOU 625 CE3 TRP A 133 8527 4743 5130 -1847 582 608 C ATOM 626 CZ2 TRP A 133 10.256 24.235 -61.393 1.00 43.95 C ANISOU 626 CZ2 TRP A 133 7593 4225 4882 -1987 809 416 C ATOM 627 CZ3 TRP A 133 7.860 24.237 -61.706 1.00 46.50 C ANISOU 627 CZ3 TRP A 133 8082 4524 5061 -1722 513 544 C ATOM 628 CH2 TRP A 133 8.989 24.202 -60.877 1.00 44.59 C ANISOU 628 CH2 TRP A 133 7675 4300 4967 -1797 623 446 C ATOM 629 N PRO A 134 9.931 27.900 -66.175 1.00 59.31 N ANISOU 629 N PRO A 134 10813 5634 6090 -2426 929 890 N ATOM 630 CA PRO A 134 11.081 28.789 -66.385 1.00 61.82 C ANISOU 630 CA PRO A 134 11205 5866 6418 -2610 1086 870 C ATOM 631 C PRO A 134 12.171 28.717 -65.321 1.00 52.54 C ANISOU 631 C PRO A 134 9774 4747 5442 -2704 1189 747 C ATOM 632 O PRO A 134 13.133 29.486 -65.414 1.00 59.88 O ANISOU 632 O PRO A 134 10712 5648 6391 -2847 1288 721 O ATOM 633 CB PRO A 134 10.413 30.166 -66.351 1.00 65.76 C ANISOU 633 CB PRO A 134 11950 6170 6867 -2520 959 987 C ATOM 634 CG PRO A 134 9.362 29.996 -65.274 1.00 60.39 C ANISOU 634 CG PRO A 134 11205 5455 6283 -2314 790 1015 C ATOM 635 CD PRO A 134 8.895 28.548 -65.348 1.00 59.94 C ANISOU 635 CD PRO A 134 10914 5625 6235 -2213 731 954 C ATOM 636 N PHE A 135 12.049 27.839 -64.329 1.00 55.12 N ANISOU 636 N PHE A 135 9847 5182 5914 -2611 1144 667 N ATOM 637 CA PHE A 135 12.913 27.877 -63.157 1.00 58.88 C ANISOU 637 CA PHE A 135 10082 5714 6574 -2678 1183 571 C ATOM 638 C PHE A 135 14.155 27.002 -63.283 1.00 60.51 C ANISOU 638 C PHE A 135 10027 6103 6861 -2807 1378 497 C ATOM 639 O PHE A 135 14.977 26.984 -62.359 1.00 60.28 O ANISOU 639 O PHE A 135 9760 6160 6982 -2881 1408 436 O ATOM 640 CB PHE A 135 12.116 27.471 -61.912 1.00 55.16 C ANISOU 640 CB PHE A 135 9439 5292 6228 -2456 1005 519 C ATOM 641 CG PHE A 135 10.916 28.339 -61.654 1.00 54.43 C ANISOU 641 CG PHE A 135 9566 5031 6086 -2296 837 597 C ATOM 642 CD1 PHE A 135 11.062 29.603 -61.103 1.00 57.42 C ANISOU 642 CD1 PHE A 135 10117 5221 6480 -2362 823 614 C ATOM 643 CD2 PHE A 135 9.641 27.892 -61.964 1.00 48.71 C ANISOU 643 CD2 PHE A 135 8876 4336 5296 -2082 702 659 C ATOM 644 CE1 PHE A 135 9.960 30.405 -60.868 1.00 56.04 C ANISOU 644 CE1 PHE A 135 10155 4872 6266 -2178 700 695 C ATOM 645 CE2 PHE A 135 8.535 28.687 -61.729 1.00 53.70 C ANISOU 645 CE2 PHE A 135 9674 4833 5897 -1904 560 753 C ATOM 646 CZ PHE A 135 8.695 29.946 -61.181 1.00 61.05 C ANISOU 646 CZ PHE A 135 10784 5558 6854 -1933 571 772 C ATOM 647 N GLY A 136 14.316 26.279 -64.386 1.00 60.91 N ANISOU 647 N GLY A 136 10116 6218 6810 -2833 1517 506 N ATOM 648 CA GLY A 136 15.516 25.497 -64.601 1.00 60.06 C ANISOU 648 CA GLY A 136 9773 6269 6778 -2920 1739 447 C ATOM 649 C GLY A 136 15.411 24.074 -64.089 1.00 59.72 C ANISOU 649 C GLY A 136 9471 6377 6844 -2746 1749 371 C ATOM 650 O GLY A 136 14.414 23.642 -63.503 1.00 56.41 O ANISOU 650 O GLY A 136 9024 5959 6449 -2559 1565 349 O ATOM 651 N ASN A 137 16.500 23.334 -64.312 1.00 60.77 N ANISOU 651 N ASN A 137 9398 6640 7050 -2796 1980 336 N ATOM 652 CA ASN A 137 16.530 21.908 -64.004 1.00 58.22 C ANISOU 652 CA ASN A 137 8860 6442 6820 -2619 2042 271 C ATOM 653 C ASN A 137 16.656 21.649 -62.506 1.00 56.97 C ANISOU 653 C ASN A 137 8389 6387 6868 -2504 1905 237 C ATOM 654 O ASN A 137 16.021 20.727 -61.979 1.00 56.23 O ANISOU 654 O ASN A 137 8213 6330 6821 -2314 1814 194 O ATOM 655 CB ASN A 137 17.685 21.242 -64.755 1.00 63.81 C ANISOU 655 CB ASN A 137 9461 7242 7542 -2681 2366 260 C ATOM 656 CG ASN A 137 17.603 19.730 -64.729 1.00 75.70 C ANISOU 656 CG ASN A 137 10855 8816 9092 -2485 2473 198 C ATOM 657 OD1 ASN A 137 16.538 19.151 -64.941 1.00 81.75 O ANISOU 657 OD1 ASN A 137 11798 9513 9749 -2379 2367 164 O ATOM 658 ND2 ASN A 137 18.730 19.081 -64.461 1.00 76.30 N ANISOU 658 ND2 ASN A 137 10634 9028 9328 -2439 2687 193 N ATOM 659 N ILE A 138 17.472 22.442 -61.808 1.00 55.50 N ANISOU 659 N ILE A 138 8042 6253 6792 -2640 1887 258 N ATOM 660 CA ILE A 138 17.691 22.214 -60.382 1.00 54.19 C ANISOU 660 CA ILE A 138 7584 6204 6802 -2562 1756 232 C ATOM 661 C ILE A 138 16.412 22.471 -59.595 1.00 53.99 C ANISOU 661 C ILE A 138 7686 6076 6753 -2432 1491 207 C ATOM 662 O ILE A 138 16.027 21.676 -58.729 1.00 50.32 O ANISOU 662 O ILE A 138 7060 5683 6376 -2257 1392 170 O ATOM 663 CB ILE A 138 18.854 23.085 -59.872 1.00 62.95 C ANISOU 663 CB ILE A 138 8517 7401 8001 -2792 1783 264 C ATOM 664 CG1 ILE A 138 20.164 22.678 -60.550 1.00 66.39 C ANISOU 664 CG1 ILE A 138 8743 7990 8494 -2892 2062 302 C ATOM 665 CG2 ILE A 138 18.974 22.983 -58.360 1.00 64.64 C ANISOU 665 CG2 ILE A 138 8477 7726 8356 -2742 1604 241 C ATOM 666 CD1 ILE A 138 21.350 23.522 -60.139 1.00 72.99 C ANISOU 666 CD1 ILE A 138 9377 8946 9409 -3157 2093 348 C ATOM 667 N LEU A 139 15.729 23.581 -59.889 1.00 52.91 N ANISOU 667 N LEU A 139 7841 5765 6496 -2502 1387 236 N ATOM 668 CA LEU A 139 14.492 23.892 -59.181 1.00 50.40 C ANISOU 668 CA LEU A 139 7643 5348 6160 -2356 1162 227 C ATOM 669 C LEU A 139 13.379 22.920 -59.543 1.00 50.50 C ANISOU 669 C LEU A 139 7709 5367 6112 -2151 1106 219 C ATOM 670 O LEU A 139 12.495 22.660 -58.719 1.00 48.57 O ANISOU 670 O LEU A 139 7421 5126 5908 -1989 946 198 O ATOM 671 CB LEU A 139 14.062 25.329 -59.473 1.00 52.50 C ANISOU 671 CB LEU A 139 8220 5413 6315 -2455 1094 281 C ATOM 672 CG LEU A 139 14.508 26.380 -58.452 1.00 63.26 C ANISOU 672 CG LEU A 139 9584 6714 7738 -2590 1026 263 C ATOM 673 CD1 LEU A 139 16.005 26.301 -58.194 1.00 76.19 C ANISOU 673 CD1 LEU A 139 10970 8507 9472 -2807 1148 242 C ATOM 674 CD2 LEU A 139 14.122 27.775 -58.917 1.00 61.59 C ANISOU 674 CD2 LEU A 139 9736 6263 7402 -2684 1004 323 C ATOM 675 N CYS A 140 13.400 22.377 -60.762 1.00 47.94 N ANISOU 675 N CYS A 140 7490 5047 5680 -2174 1238 235 N ATOM 676 CA CYS A 140 12.425 21.356 -61.128 1.00 45.04 C ANISOU 676 CA CYS A 140 7174 4700 5238 -2026 1190 219 C ATOM 677 C CYS A 140 12.571 20.123 -60.244 1.00 43.39 C ANISOU 677 C CYS A 140 6702 4615 5170 -1888 1201 150 C ATOM 678 O CYS A 140 11.575 19.587 -59.746 1.00 43.25 O ANISOU 678 O CYS A 140 6667 4610 5156 -1745 1059 132 O ATOM 679 CB CYS A 140 12.578 20.995 -62.608 1.00 51.30 C ANISOU 679 CB CYS A 140 8155 5470 5866 -2118 1355 236 C ATOM 680 SG CYS A 140 11.613 19.569 -63.163 1.00 59.60 S ANISOU 680 SG CYS A 140 9288 6558 6800 -2009 1339 197 S ATOM 681 N LYS A 141 13.808 19.673 -60.022 1.00 46.82 N ANISOU 681 N LYS A 141 6919 5148 5724 -1924 1371 125 N ATOM 682 CA LYS A 141 14.033 18.534 -59.136 1.00 48.70 C ANISOU 682 CA LYS A 141 6904 5499 6102 -1777 1386 82 C ATOM 683 C LYS A 141 13.633 18.859 -57.701 1.00 47.55 C ANISOU 683 C LYS A 141 6626 5380 6060 -1701 1172 72 C ATOM 684 O LYS A 141 13.055 18.016 -57.006 1.00 41.87 O ANISOU 684 O LYS A 141 5820 4699 5388 -1548 1090 42 O ATOM 685 CB LYS A 141 15.500 18.103 -59.194 1.00 46.54 C ANISOU 685 CB LYS A 141 6399 5341 5945 -1816 1612 90 C ATOM 686 CG LYS A 141 15.930 17.512 -60.527 1.00 50.52 C ANISOU 686 CG LYS A 141 7019 5820 6356 -1849 1876 85 C ATOM 687 CD LYS A 141 17.414 17.184 -60.528 1.00 56.71 C ANISOU 687 CD LYS A 141 7536 6734 7278 -1866 2117 113 C ATOM 688 CE LYS A 141 17.794 16.337 -61.731 1.00 57.81 C ANISOU 688 CE LYS A 141 7789 6840 7336 -1841 2418 94 C ATOM 689 NZ LYS A 141 17.124 15.004 -61.692 1.00 55.81 N ANISOU 689 NZ LYS A 141 7612 6537 7058 -1653 2443 36 N ATOM 690 N ILE A 142 13.929 20.076 -57.244 1.00 45.82 N ANISOU 690 N ILE A 142 6417 5130 5861 -1821 1090 94 N ATOM 691 CA ILE A 142 13.671 20.433 -55.852 1.00 44.45 C ANISOU 691 CA ILE A 142 6143 4976 5771 -1775 912 75 C ATOM 692 C ILE A 142 12.173 20.535 -55.592 1.00 42.99 C ANISOU 692 C ILE A 142 6122 4695 5518 -1635 743 67 C ATOM 693 O ILE A 142 11.661 19.997 -54.603 1.00 42.95 O ANISOU 693 O ILE A 142 6006 4738 5573 -1501 639 37 O ATOM 694 CB ILE A 142 14.397 21.742 -55.495 1.00 47.55 C ANISOU 694 CB ILE A 142 6554 5337 6176 -1976 886 91 C ATOM 695 CG1 ILE A 142 15.910 21.517 -55.468 1.00 49.83 C ANISOU 695 CG1 ILE A 142 6583 5787 6564 -2111 1027 110 C ATOM 696 CG2 ILE A 142 13.906 22.285 -54.160 1.00 45.00 C ANISOU 696 CG2 ILE A 142 6235 4979 5884 -1943 699 60 C ATOM 697 CD1 ILE A 142 16.711 22.768 -55.178 1.00 49.99 C ANISOU 697 CD1 ILE A 142 6614 5797 6585 -2366 1008 127 C ATOM 698 N VAL A 143 11.448 21.224 -56.475 1.00 40.26 N ANISOU 698 N VAL A 143 6029 4223 5043 -1659 716 107 N ATOM 699 CA VAL A 143 10.024 21.445 -56.245 1.00 39.82 C ANISOU 699 CA VAL A 143 6101 4097 4932 -1518 555 127 C ATOM 700 C VAL A 143 9.245 20.141 -56.377 1.00 39.12 C ANISOU 700 C VAL A 143 5947 4091 4828 -1384 530 110 C ATOM 701 O VAL A 143 8.340 19.863 -55.581 1.00 40.68 O ANISOU 701 O VAL A 143 6090 4312 5056 -1249 407 99 O ATOM 702 CB VAL A 143 9.493 22.531 -57.198 1.00 44.86 C ANISOU 702 CB VAL A 143 7015 4592 5437 -1567 530 206 C ATOM 703 CG1 VAL A 143 7.977 22.629 -57.104 1.00 44.25 C ANISOU 703 CG1 VAL A 143 7029 4479 5307 -1393 373 256 C ATOM 704 CG2 VAL A 143 10.133 23.871 -56.869 1.00 42.80 C ANISOU 704 CG2 VAL A 143 6854 4214 5192 -1699 544 216 C ATOM 705 N ILE A 144 9.581 19.318 -57.374 1.00 38.20 N ANISOU 705 N ILE A 144 5852 4011 4652 -1432 661 102 N ATOM 706 CA ILE A 144 8.886 18.043 -57.536 1.00 37.51 C ANISOU 706 CA ILE A 144 5742 3980 4528 -1341 653 75 C ATOM 707 C ILE A 144 9.134 17.142 -56.333 1.00 36.92 C ANISOU 707 C ILE A 144 5441 3991 4597 -1234 651 20 C ATOM 708 O ILE A 144 8.205 16.517 -55.806 1.00 38.64 O ANISOU 708 O ILE A 144 5625 4240 4818 -1129 550 6 O ATOM 709 CB ILE A 144 9.304 17.362 -58.854 1.00 45.46 C ANISOU 709 CB ILE A 144 6864 4982 5425 -1433 826 65 C ATOM 710 CG1 ILE A 144 8.552 17.983 -60.032 1.00 55.47 C ANISOU 710 CG1 ILE A 144 8388 6185 6504 -1514 764 131 C ATOM 711 CG2 ILE A 144 9.053 15.862 -58.789 1.00 41.03 C ANISOU 711 CG2 ILE A 144 6253 4470 4865 -1360 883 7 C ATOM 712 CD1 ILE A 144 8.666 17.189 -61.312 1.00 71.81 C ANISOU 712 CD1 ILE A 144 10618 8248 8417 -1611 906 112 C ATOM 713 N SER A 145 10.384 17.070 -55.869 1.00 41.49 N ANISOU 713 N SER A 145 5852 4619 5292 -1264 757 2 N ATOM 714 CA SER A 145 10.693 16.222 -54.723 1.00 41.47 C ANISOU 714 CA SER A 145 5632 4706 5420 -1156 748 -28 C ATOM 715 C SER A 145 9.984 16.714 -53.467 1.00 37.02 C ANISOU 715 C SER A 145 5024 4146 4898 -1087 556 -33 C ATOM 716 O SER A 145 9.398 15.918 -52.724 1.00 40.57 O ANISOU 716 O SER A 145 5400 4636 5380 -971 494 -54 O ATOM 717 CB SER A 145 12.205 16.162 -54.504 1.00 47.02 C ANISOU 717 CB SER A 145 6137 5492 6237 -1206 882 -16 C ATOM 718 OG SER A 145 12.531 15.246 -53.471 1.00 52.17 O ANISOU 718 OG SER A 145 6576 6240 7007 -1085 874 -21 O ATOM 719 N ILE A 146 10.026 18.025 -53.215 1.00 39.50 N ANISOU 719 N ILE A 146 5404 4403 5200 -1164 479 -17 N ATOM 720 CA ILE A 146 9.304 18.590 -52.077 1.00 38.64 C ANISOU 720 CA ILE A 146 5304 4268 5111 -1096 326 -29 C ATOM 721 C ILE A 146 7.816 18.292 -52.195 1.00 38.73 C ANISOU 721 C ILE A 146 5406 4252 5058 -968 236 -16 C ATOM 722 O ILE A 146 7.149 17.966 -51.203 1.00 33.92 O ANISOU 722 O ILE A 146 4728 3677 4484 -858 151 -35 O ATOM 723 CB ILE A 146 9.573 20.103 -51.973 1.00 42.12 C ANISOU 723 CB ILE A 146 5872 4608 5525 -1211 291 -16 C ATOM 724 CG1 ILE A 146 10.972 20.359 -51.411 1.00 41.64 C ANISOU 724 CG1 ILE A 146 5666 4617 5539 -1357 333 -33 C ATOM 725 CG2 ILE A 146 8.515 20.793 -51.120 1.00 40.43 C ANISOU 725 CG2 ILE A 146 5760 4310 5290 -1112 164 -22 C ATOM 726 CD1 ILE A 146 11.365 21.821 -51.406 1.00 50.00 C ANISOU 726 CD1 ILE A 146 6879 5564 6555 -1526 319 -28 C ATOM 727 N ASP A 147 7.277 18.373 -53.413 1.00 37.12 N ANISOU 727 N ASP A 147 5350 4004 4751 -991 253 25 N ATOM 728 CA ASP A 147 5.846 18.169 -53.603 1.00 37.29 C ANISOU 728 CA ASP A 147 5434 4031 4702 -893 148 61 C ATOM 729 C ASP A 147 5.441 16.730 -53.303 1.00 38.62 C ANISOU 729 C ASP A 147 5491 4294 4889 -831 151 24 C ATOM 730 O ASP A 147 4.434 16.494 -52.624 1.00 36.94 O ANISOU 730 O ASP A 147 5227 4121 4686 -732 52 31 O ATOM 731 CB ASP A 147 5.450 18.558 -55.024 1.00 36.68 C ANISOU 731 CB ASP A 147 5537 3909 4491 -958 150 128 C ATOM 732 CG ASP A 147 3.965 18.782 -55.169 1.00 40.30 C ANISOU 732 CG ASP A 147 6049 4384 4879 -860 7 205 C ATOM 733 OD1 ASP A 147 3.398 19.557 -54.374 1.00 38.20 O1- ANISOU 733 OD1 ASP A 147 5771 4081 4661 -746 -73 234 O1- ATOM 734 OD2 ASP A 147 3.365 18.191 -56.085 1.00 40.06 O ANISOU 734 OD2 ASP A 147 6073 4409 4740 -899 -20 241 O ATOM 735 N TYR A 148 6.206 15.751 -53.799 1.00 33.20 N ANISOU 735 N TYR A 148 4776 3634 4203 -887 281 -13 N ATOM 736 CA TYR A 148 5.888 14.360 -53.486 1.00 31.34 C ANISOU 736 CA TYR A 148 4473 3454 3982 -832 305 -50 C ATOM 737 C TYR A 148 6.174 14.041 -52.022 1.00 37.64 C ANISOU 737 C TYR A 148 5097 4298 4907 -736 277 -78 C ATOM 738 O TYR A 148 5.376 13.359 -51.368 1.00 38.27 O ANISOU 738 O TYR A 148 5133 4416 4994 -662 216 -88 O ATOM 739 CB TYR A 148 6.662 13.408 -54.399 1.00 32.20 C ANISOU 739 CB TYR A 148 4633 3545 4055 -896 485 -81 C ATOM 740 CG TYR A 148 6.031 13.194 -55.761 1.00 31.77 C ANISOU 740 CG TYR A 148 4780 3462 3830 -997 500 -70 C ATOM 741 CD1 TYR A 148 6.405 13.971 -56.847 1.00 32.62 C ANISOU 741 CD1 TYR A 148 5022 3522 3849 -1101 550 -39 C ATOM 742 CD2 TYR A 148 5.067 12.211 -55.960 1.00 34.94 C ANISOU 742 CD2 TYR A 148 5248 3886 4142 -1014 460 -86 C ATOM 743 CE1 TYR A 148 5.840 13.781 -58.097 1.00 40.74 C ANISOU 743 CE1 TYR A 148 6250 4533 4696 -1210 551 -22 C ATOM 744 CE2 TYR A 148 4.494 12.012 -57.209 1.00 43.26 C ANISOU 744 CE2 TYR A 148 6494 4928 5013 -1142 454 -74 C ATOM 745 CZ TYR A 148 4.885 12.803 -58.273 1.00 41.39 C ANISOU 745 CZ TYR A 148 6393 4651 4684 -1236 496 -40 C ATOM 746 OH TYR A 148 4.324 12.618 -59.520 1.00 39.52 O ANISOU 746 OH TYR A 148 6364 4410 4240 -1379 478 -20 O ATOM 747 N TYR A 149 7.301 14.526 -51.491 1.00 35.85 N ANISOU 747 N TYR A 149 4772 4079 4769 -752 316 -83 N ATOM 748 CA TYR A 149 7.659 14.238 -50.103 1.00 37.55 C ANISOU 748 CA TYR A 149 4827 4354 5085 -680 274 -98 C ATOM 749 C TYR A 149 6.558 14.668 -49.145 1.00 38.10 C ANISOU 749 C TYR A 149 4912 4422 5143 -610 130 -102 C ATOM 750 O TYR A 149 6.199 13.931 -48.221 1.00 36.32 O ANISOU 750 O TYR A 149 4608 4244 4950 -528 95 -116 O ATOM 751 CB TYR A 149 8.964 14.941 -49.731 1.00 33.32 C ANISOU 751 CB TYR A 149 4189 3849 4622 -754 300 -89 C ATOM 752 CG TYR A 149 10.141 14.018 -49.544 1.00 43.06 C ANISOU 752 CG TYR A 149 5246 5169 5948 -727 410 -73 C ATOM 753 CD1 TYR A 149 10.183 13.116 -48.485 1.00 40.48 C ANISOU 753 CD1 TYR A 149 4788 4909 5685 -617 379 -66 C ATOM 754 CD2 TYR A 149 11.221 14.061 -50.414 1.00 41.57 C ANISOU 754 CD2 TYR A 149 5015 4996 5783 -799 556 -50 C ATOM 755 CE1 TYR A 149 11.266 12.275 -48.310 1.00 39.96 C ANISOU 755 CE1 TYR A 149 4549 4922 5710 -559 482 -26 C ATOM 756 CE2 TYR A 149 12.305 13.227 -50.246 1.00 42.24 C ANISOU 756 CE2 TYR A 149 4912 5170 5967 -742 675 -15 C ATOM 757 CZ TYR A 149 12.325 12.337 -49.193 1.00 43.41 C ANISOU 757 CZ TYR A 149 4927 5383 6185 -612 633 4 C ATOM 758 OH TYR A 149 13.409 11.507 -49.029 1.00 46.71 O ANISOU 758 OH TYR A 149 5148 5891 6707 -523 753 64 O ATOM 759 N ASN A 150 6.008 15.859 -49.352 1.00 34.61 N ANISOU 759 N ASN A 150 4581 3917 4652 -630 63 -85 N ATOM 760 CA ASN A 150 5.089 16.429 -48.380 1.00 33.44 C ANISOU 760 CA ASN A 150 4450 3752 4502 -545 -40 -86 C ATOM 761 C ASN A 150 3.638 16.073 -48.645 1.00 35.99 C ANISOU 761 C ASN A 150 4803 4099 4773 -460 -94 -54 C ATOM 762 O ASN A 150 2.818 16.172 -47.727 1.00 39.73 O ANISOU 762 O ASN A 150 5245 4592 5260 -364 -153 -54 O ATOM 763 CB ASN A 150 5.279 17.945 -48.323 1.00 31.56 C ANISOU 763 CB ASN A 150 4331 3414 4247 -590 -65 -78 C ATOM 764 CG ASN A 150 6.610 18.315 -47.712 1.00 41.16 C ANISOU 764 CG ASN A 150 5492 4636 5510 -701 -42 -113 C ATOM 765 OD1 ASN A 150 6.764 18.297 -46.492 1.00 41.42 O ANISOU 765 OD1 ASN A 150 5464 4703 5573 -684 -90 -147 O ATOM 766 ND2 ASN A 150 7.591 18.614 -48.554 1.00 35.91 N ANISOU 766 ND2 ASN A 150 4841 3957 4845 -828 29 -100 N ATOM 767 N MET A 151 3.297 15.653 -49.862 1.00 32.39 N ANISOU 767 N MET A 151 4403 3655 4249 -506 -75 -22 N ATOM 768 CA MET A 151 2.027 14.963 -50.052 1.00 31.58 C ANISOU 768 CA MET A 151 4284 3622 4094 -466 -133 8 C ATOM 769 C MET A 151 1.959 13.727 -49.164 1.00 36.94 C ANISOU 769 C MET A 151 4856 4362 4817 -433 -112 -37 C ATOM 770 O MET A 151 0.981 13.520 -48.438 1.00 33.47 O ANISOU 770 O MET A 151 4355 3978 4383 -361 -173 -24 O ATOM 771 CB MET A 151 1.845 14.580 -51.523 1.00 30.72 C ANISOU 771 CB MET A 151 4272 3521 3877 -569 -115 39 C ATOM 772 CG MET A 151 0.618 13.717 -51.795 1.00 30.96 C ANISOU 772 CG MET A 151 4284 3646 3833 -587 -182 68 C ATOM 773 SD MET A 151 0.487 13.241 -53.533 1.00 39.03 S ANISOU 773 SD MET A 151 5463 4676 4689 -757 -167 92 S ATOM 774 CE MET A 151 -1.188 12.623 -53.593 1.00 51.80 C ANISOU 774 CE MET A 151 7020 6443 6220 -788 -310 154 C ATOM 775 N PHE A 152 3.006 12.903 -49.191 1.00 31.61 N ANISOU 775 N PHE A 152 4158 3676 4178 -473 -14 -80 N ATOM 776 CA PHE A 152 2.995 11.671 -48.413 1.00 34.82 C ANISOU 776 CA PHE A 152 4491 4119 4621 -432 18 -109 C ATOM 777 C PHE A 152 3.178 11.940 -46.923 1.00 30.28 C ANISOU 777 C PHE A 152 3817 3569 4121 -348 -29 -120 C ATOM 778 O PHE A 152 2.533 11.290 -46.094 1.00 33.97 O ANISOU 778 O PHE A 152 4238 4076 4592 -295 -56 -124 O ATOM 779 CB PHE A 152 4.073 10.717 -48.929 1.00 30.42 C ANISOU 779 CB PHE A 152 3949 3529 4082 -467 157 -133 C ATOM 780 CG PHE A 152 3.730 10.077 -50.244 1.00 36.72 C ANISOU 780 CG PHE A 152 4884 4294 4774 -560 222 -141 C ATOM 781 CD1 PHE A 152 2.700 9.155 -50.330 1.00 36.23 C ANISOU 781 CD1 PHE A 152 4876 4252 4639 -598 198 -149 C ATOM 782 CD2 PHE A 152 4.437 10.392 -51.390 1.00 38.00 C ANISOU 782 CD2 PHE A 152 5134 4408 4895 -635 311 -143 C ATOM 783 CE1 PHE A 152 2.376 8.560 -51.541 1.00 41.86 C ANISOU 783 CE1 PHE A 152 5745 4935 5226 -722 248 -163 C ATOM 784 CE2 PHE A 152 4.122 9.800 -52.605 1.00 37.87 C ANISOU 784 CE2 PHE A 152 5280 4356 4754 -741 375 -157 C ATOM 785 CZ PHE A 152 3.090 8.883 -52.677 1.00 36.08 C ANISOU 785 CZ PHE A 152 5120 4147 4442 -791 337 -170 C ATOM 786 N THR A 153 4.047 12.889 -46.563 1.00 29.43 N ANISOU 786 N THR A 153 3687 3437 4056 -356 -38 -126 N ATOM 787 CA THR A 153 4.245 13.211 -45.152 1.00 32.64 C ANISOU 787 CA THR A 153 4031 3868 4504 -309 -93 -142 C ATOM 788 C THR A 153 2.968 13.756 -44.525 1.00 40.17 C ANISOU 788 C THR A 153 5023 4818 5423 -239 -163 -141 C ATOM 789 O THR A 153 2.606 13.376 -43.405 1.00 37.00 O ANISOU 789 O THR A 153 4576 4454 5028 -180 -187 -154 O ATOM 790 CB THR A 153 5.393 14.209 -44.993 1.00 31.99 C ANISOU 790 CB THR A 153 3942 3762 4450 -381 -98 -150 C ATOM 791 OG1 THR A 153 6.611 13.610 -45.450 1.00 42.03 O ANISOU 791 OG1 THR A 153 5129 5070 5772 -427 -19 -136 O ATOM 792 CG2 THR A 153 5.558 14.611 -43.527 1.00 39.47 C ANISOU 792 CG2 THR A 153 4858 4733 5405 -368 -169 -173 C ATOM 793 N SER A 154 2.269 14.648 -45.232 1.00 32.83 N ANISOU 793 N SER A 154 4175 3844 4455 -231 -186 -114 N ATOM 794 CA SER A 154 0.988 15.145 -44.741 1.00 32.13 C ANISOU 794 CA SER A 154 4101 3761 4344 -130 -229 -91 C ATOM 795 C SER A 154 -0.010 14.006 -44.580 1.00 35.52 C ANISOU 795 C SER A 154 4447 4289 4762 -95 -238 -72 C ATOM 796 O SER A 154 -0.648 13.862 -43.530 1.00 30.51 O ANISOU 796 O SER A 154 3766 3692 4133 -21 -246 -79 O ATOM 797 CB SER A 154 0.439 16.205 -45.696 1.00 30.48 C ANISOU 797 CB SER A 154 3983 3496 4101 -107 -249 -35 C ATOM 798 OG SER A 154 -0.913 16.513 -45.397 1.00 40.32 O ANISOU 798 OG SER A 154 5206 4778 5337 18 -280 17 O ATOM 799 N ILE A 155 -0.138 13.172 -45.610 1.00 29.67 N ANISOU 799 N ILE A 155 3701 3584 3988 -168 -228 -53 N ATOM 800 CA ILE A 155 -1.135 12.110 -45.593 1.00 28.67 C ANISOU 800 CA ILE A 155 3518 3547 3829 -182 -240 -34 C ATOM 801 C ILE A 155 -0.782 11.044 -44.558 1.00 31.40 C ANISOU 801 C ILE A 155 3821 3905 4206 -174 -197 -77 C ATOM 802 O ILE A 155 -1.655 10.559 -43.829 1.00 30.86 O ANISOU 802 O ILE A 155 3697 3900 4129 -143 -208 -66 O ATOM 803 CB ILE A 155 -1.279 11.515 -47.004 1.00 35.93 C ANISOU 803 CB ILE A 155 4492 4482 4676 -301 -238 -13 C ATOM 804 CG1 ILE A 155 -1.993 12.509 -47.924 1.00 34.60 C ANISOU 804 CG1 ILE A 155 4349 4339 4457 -297 -312 63 C ATOM 805 CG2 ILE A 155 -2.022 10.211 -46.950 1.00 31.50 C ANISOU 805 CG2 ILE A 155 3905 3993 4072 -370 -234 -14 C ATOM 806 CD1 ILE A 155 -2.024 12.080 -49.375 1.00 40.15 C ANISOU 806 CD1 ILE A 155 5140 5056 5061 -438 -321 84 C ATOM 807 N PHE A 156 0.495 10.659 -44.476 1.00 27.48 N ANISOU 807 N PHE A 156 3340 3355 3746 -196 -143 -111 N ATOM 808 CA PHE A 156 0.881 9.635 -43.509 1.00 34.73 C ANISOU 808 CA PHE A 156 4222 4283 4693 -168 -106 -127 C ATOM 809 C PHE A 156 0.725 10.129 -42.076 1.00 36.96 C ANISOU 809 C PHE A 156 4461 4592 4992 -92 -151 -134 C ATOM 810 O PHE A 156 0.428 9.332 -41.179 1.00 32.87 O ANISOU 810 O PHE A 156 3918 4103 4466 -64 -141 -132 O ATOM 811 CB PHE A 156 2.321 9.176 -43.753 1.00 35.29 C ANISOU 811 CB PHE A 156 4290 4309 4810 -178 -36 -135 C ATOM 812 CG PHE A 156 2.521 8.448 -45.059 1.00 35.90 C ANISOU 812 CG PHE A 156 4442 4340 4858 -245 52 -139 C ATOM 813 CD1 PHE A 156 1.441 7.961 -45.778 1.00 39.73 C ANISOU 813 CD1 PHE A 156 5001 4832 5262 -319 48 -140 C ATOM 814 CD2 PHE A 156 3.797 8.247 -45.560 1.00 34.82 C ANISOU 814 CD2 PHE A 156 4303 4161 4765 -244 144 -139 C ATOM 815 CE1 PHE A 156 1.630 7.293 -46.978 1.00 37.95 C ANISOU 815 CE1 PHE A 156 4887 4552 4980 -407 133 -156 C ATOM 816 CE2 PHE A 156 3.994 7.582 -46.758 1.00 39.17 C ANISOU 816 CE2 PHE A 156 4956 4651 5275 -302 255 -152 C ATOM 817 CZ PHE A 156 2.909 7.104 -47.465 1.00 36.27 C ANISOU 817 CZ PHE A 156 4703 4271 4807 -391 249 -168 C ATOM 818 N THR A 157 0.912 11.431 -41.840 1.00 36.14 N ANISOU 818 N THR A 157 4376 4462 4894 -70 -190 -146 N ATOM 819 CA THR A 157 0.754 11.963 -40.490 1.00 29.55 C ANISOU 819 CA THR A 157 3545 3633 4048 -15 -217 -167 C ATOM 820 C THR A 157 -0.707 11.959 -40.060 1.00 36.33 C ANISOU 820 C THR A 157 4391 4535 4877 54 -212 -151 C ATOM 821 O THR A 157 -1.019 11.629 -38.911 1.00 37.69 O ANISOU 821 O THR A 157 4553 4738 5029 92 -203 -163 O ATOM 822 CB THR A 157 1.336 13.374 -40.404 1.00 28.36 C ANISOU 822 CB THR A 157 3464 3416 3896 -32 -243 -192 C ATOM 823 OG1 THR A 157 2.713 13.341 -40.796 1.00 31.50 O ANISOU 823 OG1 THR A 157 3838 3804 4326 -115 -244 -195 O ATOM 824 CG2 THR A 157 1.236 13.909 -38.973 1.00 31.15 C ANISOU 824 CG2 THR A 157 3866 3758 4211 1 -261 -229 C ATOM 825 N LEU A 158 -1.623 12.314 -40.964 1.00 32.63 N ANISOU 825 N LEU A 158 3913 4084 4402 70 -218 -113 N ATOM 826 CA LEU A 158 -3.029 12.302 -40.580 1.00 37.38 C ANISOU 826 CA LEU A 158 4456 4761 4987 143 -209 -77 C ATOM 827 C LEU A 158 -3.557 10.876 -40.452 1.00 34.87 C ANISOU 827 C LEU A 158 4069 4529 4651 82 -195 -62 C ATOM 828 O LEU A 158 -4.493 10.635 -39.682 1.00 39.21 O ANISOU 828 O LEU A 158 4561 5150 5187 124 -171 -44 O ATOM 829 CB LEU A 158 -3.859 13.128 -41.568 1.00 43.55 C ANISOU 829 CB LEU A 158 5219 5561 5767 188 -236 -11 C ATOM 830 CG LEU A 158 -4.079 12.665 -43.005 1.00 41.78 C ANISOU 830 CG LEU A 158 4970 5388 5518 92 -280 38 C ATOM 831 CD1 LEU A 158 -5.303 11.773 -43.095 1.00 34.21 C ANISOU 831 CD1 LEU A 158 3895 4574 4531 52 -299 92 C ATOM 832 CD2 LEU A 158 -4.220 13.866 -43.935 1.00 39.05 C ANISOU 832 CD2 LEU A 158 4670 5002 5167 139 -316 95 C ATOM 833 N CYS A 159 -2.972 9.921 -41.184 1.00 35.03 N ANISOU 833 N CYS A 159 4113 4533 4665 -20 -191 -70 N ATOM 834 CA CYS A 159 -3.260 8.515 -40.912 1.00 34.02 C ANISOU 834 CA CYS A 159 3975 4439 4512 -86 -157 -68 C ATOM 835 C CYS A 159 -2.764 8.118 -39.529 1.00 29.94 C ANISOU 835 C CYS A 159 3472 3899 4004 -35 -128 -91 C ATOM 836 O CYS A 159 -3.438 7.370 -38.811 1.00 37.46 O ANISOU 836 O CYS A 159 4407 4898 4928 -46 -99 -78 O ATOM 837 CB CYS A 159 -2.617 7.615 -41.968 1.00 33.73 C ANISOU 837 CB CYS A 159 4008 4347 4460 -190 -128 -80 C ATOM 838 SG CYS A 159 -3.343 7.719 -43.613 1.00 42.02 S ANISOU 838 SG CYS A 159 5074 5441 5448 -307 -168 -49 S ATOM 839 N THR A 160 -1.574 8.595 -39.153 1.00 35.02 N ANISOU 839 N THR A 160 4146 4483 4676 5 -140 -116 N ATOM 840 CA THR A 160 -1.020 8.286 -37.840 1.00 39.51 C ANISOU 840 CA THR A 160 4728 5049 5237 43 -140 -124 C ATOM 841 C THR A 160 -1.908 8.825 -36.727 1.00 37.17 C ANISOU 841 C THR A 160 4432 4794 4898 97 -137 -133 C ATOM 842 O THR A 160 -2.106 8.161 -35.703 1.00 39.82 O ANISOU 842 O THR A 160 4781 5154 5196 106 -116 -125 O ATOM 843 CB THR A 160 0.393 8.858 -37.723 1.00 37.94 C ANISOU 843 CB THR A 160 4535 4812 5068 48 -177 -137 C ATOM 844 OG1 THR A 160 1.232 8.260 -38.719 1.00 35.71 O ANISOU 844 OG1 THR A 160 4240 4498 4831 16 -147 -120 O ATOM 845 CG2 THR A 160 0.972 8.574 -36.345 1.00 31.21 C ANISOU 845 CG2 THR A 160 3688 3984 4188 73 -206 -127 C ATOM 846 N MET A 161 -2.456 10.027 -36.912 1.00 35.47 N ANISOU 846 N MET A 161 4218 4575 4684 143 -142 -146 N ATOM 847 CA MET A 161 -3.374 10.575 -35.922 1.00 35.47 C ANISOU 847 CA MET A 161 4228 4602 4646 219 -102 -154 C ATOM 848 C MET A 161 -4.644 9.738 -35.815 1.00 34.19 C ANISOU 848 C MET A 161 3981 4537 4471 215 -53 -111 C ATOM 849 O MET A 161 -5.222 9.631 -34.729 1.00 35.82 O ANISOU 849 O MET A 161 4193 4780 4636 254 2 -114 O ATOM 850 CB MET A 161 -3.703 12.028 -36.265 1.00 40.25 C ANISOU 850 CB MET A 161 4868 5160 5264 295 -94 -163 C ATOM 851 CG MET A 161 -2.470 12.924 -36.312 1.00 49.70 C ANISOU 851 CG MET A 161 6169 6254 6460 263 -136 -211 C ATOM 852 SD MET A 161 -2.828 14.667 -36.605 1.00 53.76 S ANISOU 852 SD MET A 161 6789 6662 6974 352 -104 -224 S ATOM 853 CE MET A 161 -3.570 15.122 -35.040 1.00 66.13 C ANISOU 853 CE MET A 161 8448 8207 8470 452 -10 -265 C ATOM 854 N SER A 162 -5.083 9.125 -36.916 1.00 28.80 N ANISOU 854 N SER A 162 3229 3903 3810 146 -70 -71 N ATOM 855 CA SER A 162 -6.237 8.233 -36.841 1.00 30.96 C ANISOU 855 CA SER A 162 3418 4283 4060 92 -34 -27 C ATOM 856 C SER A 162 -5.893 6.949 -36.097 1.00 27.50 C ANISOU 856 C SER A 162 3041 3822 3584 22 0 -38 C ATOM 857 O SER A 162 -6.664 6.490 -35.246 1.00 33.85 O ANISOU 857 O SER A 162 3820 4690 4352 14 55 -19 O ATOM 858 CB SER A 162 -6.751 7.912 -38.245 1.00 33.77 C ANISOU 858 CB SER A 162 3710 4701 4422 -6 -78 16 C ATOM 859 OG SER A 162 -7.884 7.067 -38.177 1.00 47.77 O ANISOU 859 OG SER A 162 5394 6595 6162 -98 -55 62 O ATOM 860 N VAL A 163 -4.747 6.345 -36.421 1.00 30.31 N ANISOU 860 N VAL A 163 3479 4088 3951 -18 -20 -55 N ATOM 861 CA VAL A 163 -4.311 5.136 -35.728 1.00 30.40 C ANISOU 861 CA VAL A 163 3563 4055 3932 -51 16 -46 C ATOM 862 C VAL A 163 -4.081 5.426 -34.250 1.00 34.14 C ANISOU 862 C VAL A 163 4071 4533 4369 26 21 -52 C ATOM 863 O VAL A 163 -4.410 4.611 -33.379 1.00 37.21 O ANISOU 863 O VAL A 163 4499 4934 4706 5 66 -28 O ATOM 864 CB VAL A 163 -3.044 4.572 -36.397 1.00 31.52 C ANISOU 864 CB VAL A 163 3772 4097 4108 -64 10 -48 C ATOM 865 CG1 VAL A 163 -2.474 3.417 -35.586 1.00 32.66 C ANISOU 865 CG1 VAL A 163 3996 4182 4230 -48 50 -16 C ATOM 866 CG2 VAL A 163 -3.347 4.134 -37.825 1.00 26.59 C ANISOU 866 CG2 VAL A 163 3162 3456 3486 -166 26 -52 C ATOM 867 N ASP A 164 -3.512 6.593 -33.948 1.00 33.76 N ANISOU 867 N ASP A 164 4030 4468 4329 96 -23 -85 N ATOM 868 CA ASP A 164 -3.257 6.973 -32.564 1.00 30.01 C ANISOU 868 CA ASP A 164 3619 3995 3790 141 -27 -101 C ATOM 869 C ASP A 164 -4.549 7.039 -31.758 1.00 34.12 C ANISOU 869 C ASP A 164 4133 4578 4255 162 56 -101 C ATOM 870 O ASP A 164 -4.601 6.574 -30.613 1.00 35.72 O ANISOU 870 O ASP A 164 4402 4792 4380 159 86 -92 O ATOM 871 CB ASP A 164 -2.532 8.317 -32.535 1.00 34.22 C ANISOU 871 CB ASP A 164 4186 4489 4329 174 -83 -149 C ATOM 872 CG ASP A 164 -2.344 8.849 -31.135 1.00 38.67 C ANISOU 872 CG ASP A 164 4848 5049 4796 190 -88 -181 C ATOM 873 OD1 ASP A 164 -1.590 8.222 -30.361 1.00 41.22 O1- ANISOU 873 OD1 ASP A 164 5211 5384 5068 161 -136 -154 O1- ATOM 874 OD2 ASP A 164 -2.941 9.900 -30.816 1.00 42.20 O ANISOU 874 OD2 ASP A 164 5347 5478 5210 235 -40 -227 O ATOM 875 N ARG A 165 -5.604 7.614 -32.340 1.00 31.74 N ANISOU 875 N ARG A 165 3744 4328 3988 191 98 -98 N ATOM 876 CA ARG A 165 -6.882 7.694 -31.643 1.00 36.70 C ANISOU 876 CA ARG A 165 4326 5039 4580 228 198 -82 C ATOM 877 C ARG A 165 -7.556 6.331 -31.555 1.00 38.55 C ANISOU 877 C ARG A 165 4513 5343 4792 125 242 -32 C ATOM 878 O ARG A 165 -8.209 6.025 -30.549 1.00 34.10 O ANISOU 878 O ARG A 165 3962 4829 4166 124 329 -20 O ATOM 879 CB ARG A 165 -7.790 8.707 -32.343 1.00 37.46 C ANISOU 879 CB ARG A 165 4312 5188 4734 312 227 -65 C ATOM 880 CG ARG A 165 -7.262 10.130 -32.279 1.00 39.84 C ANISOU 880 CG ARG A 165 4703 5391 5041 418 217 -116 C ATOM 881 CD ARG A 165 -7.852 11.001 -33.378 1.00 47.40 C ANISOU 881 CD ARG A 165 5565 6371 6074 497 211 -76 C ATOM 882 NE ARG A 165 -7.454 12.398 -33.230 1.00 52.02 N ANISOU 882 NE ARG A 165 6274 6835 6656 603 230 -123 N ATOM 883 CZ ARG A 165 -7.756 13.359 -34.096 1.00 56.13 C ANISOU 883 CZ ARG A 165 6767 7328 7232 695 227 -88 C ATOM 884 NH1 ARG A 165 -8.460 13.076 -35.186 1.00 47.41 N ANISOU 884 NH1 ARG A 165 5494 6334 6187 690 185 0 N ATOM 885 NH2 ARG A 165 -7.350 14.601 -33.872 1.00 58.79 N ANISOU 885 NH2 ARG A 165 7264 7523 7553 778 261 -137 N ATOM 886 N TYR A 166 -7.414 5.504 -32.593 1.00 35.25 N ANISOU 886 N TYR A 166 4066 4919 4410 24 197 -7 N ATOM 887 CA TYR A 166 -7.940 4.146 -32.529 1.00 33.77 C ANISOU 887 CA TYR A 166 3884 4762 4185 -106 242 32 C ATOM 888 C TYR A 166 -7.273 3.350 -31.412 1.00 28.93 C ANISOU 888 C TYR A 166 3416 4069 3506 -109 268 36 C ATOM 889 O TYR A 166 -7.945 2.634 -30.661 1.00 36.35 O ANISOU 889 O TYR A 166 4381 5047 4384 -169 345 66 O ATOM 890 CB TYR A 166 -7.754 3.451 -33.880 1.00 32.15 C ANISOU 890 CB TYR A 166 3681 4524 4009 -224 197 41 C ATOM 891 CG TYR A 166 -7.803 1.944 -33.799 1.00 32.95 C ANISOU 891 CG TYR A 166 3887 4574 4060 -363 246 64 C ATOM 892 CD1 TYR A 166 -9.014 1.275 -33.710 1.00 33.23 C ANISOU 892 CD1 TYR A 166 3869 4708 4050 -506 302 99 C ATOM 893 CD2 TYR A 166 -6.634 1.190 -33.815 1.00 34.57 C ANISOU 893 CD2 TYR A 166 4244 4627 4263 -349 245 58 C ATOM 894 CE1 TYR A 166 -9.065 -0.103 -33.633 1.00 37.25 C ANISOU 894 CE1 TYR A 166 4513 5142 4500 -655 358 116 C ATOM 895 CE2 TYR A 166 -6.674 -0.189 -33.739 1.00 31.86 C ANISOU 895 CE2 TYR A 166 4035 4201 3872 -458 311 84 C ATOM 896 CZ TYR A 166 -7.894 -0.830 -33.647 1.00 36.03 C ANISOU 896 CZ TYR A 166 4545 4804 4341 -622 368 106 C ATOM 897 OH TYR A 166 -7.946 -2.203 -33.569 1.00 44.80 O ANISOU 897 OH TYR A 166 5826 5806 5390 -752 445 129 O ATOM 898 N ILE A 167 -5.950 3.475 -31.281 1.00 30.53 N ANISOU 898 N ILE A 167 3707 4174 3717 -46 202 20 N ATOM 899 CA ILE A 167 -5.230 2.763 -30.229 1.00 33.93 C ANISOU 899 CA ILE A 167 4261 4546 4083 -30 202 50 C ATOM 900 C ILE A 167 -5.670 3.249 -28.852 1.00 37.15 C ANISOU 900 C ILE A 167 4710 5007 4399 8 243 40 C ATOM 901 O ILE A 167 -5.831 2.451 -27.920 1.00 34.00 O ANISOU 901 O ILE A 167 4399 4602 3915 -24 290 81 O ATOM 902 CB ILE A 167 -3.712 2.917 -30.436 1.00 39.01 C ANISOU 902 CB ILE A 167 4940 5116 4766 35 109 54 C ATOM 903 CG1 ILE A 167 -3.264 2.111 -31.659 1.00 38.10 C ANISOU 903 CG1 ILE A 167 4827 4925 4722 0 116 74 C ATOM 904 CG2 ILE A 167 -2.934 2.495 -29.188 1.00 35.40 C ANISOU 904 CG2 ILE A 167 4579 4638 4232 76 75 104 C ATOM 905 CD1 ILE A 167 -1.782 2.220 -31.953 1.00 35.60 C ANISOU 905 CD1 ILE A 167 4510 4554 4463 76 50 92 C ATOM 906 N ALA A 168 -5.895 4.557 -28.708 1.00 34.16 N ANISOU 906 N ALA A 168 4292 4665 4023 76 241 -13 N ATOM 907 CA ALA A 168 -6.291 5.111 -27.416 1.00 33.98 C ANISOU 907 CA ALA A 168 4342 4671 3896 116 305 -38 C ATOM 908 C ALA A 168 -7.602 4.509 -26.925 1.00 36.35 C ANISOU 908 C ALA A 168 4608 5051 4153 73 441 -6 C ATOM 909 O ALA A 168 -7.765 4.248 -25.726 1.00 39.08 O ANISOU 909 O ALA A 168 5060 5404 4384 62 504 3 O ATOM 910 CB ALA A 168 -6.409 6.631 -27.516 1.00 33.75 C ANISOU 910 CB ALA A 168 4301 4637 3886 202 314 -106 C ATOM 911 N VAL A 169 -8.544 4.275 -27.831 1.00 33.09 N ANISOU 911 N VAL A 169 4044 4710 3817 29 484 19 N ATOM 912 CA VAL A 169 -9.868 3.792 -27.450 1.00 33.26 C ANISOU 912 CA VAL A 169 3986 4843 3807 -31 613 59 C ATOM 913 C VAL A 169 -9.922 2.272 -27.423 1.00 36.39 C ANISOU 913 C VAL A 169 4443 5218 4165 -184 626 113 C ATOM 914 O VAL A 169 -10.458 1.676 -26.485 1.00 35.47 O ANISOU 914 O VAL A 169 4383 5132 3960 -242 726 144 O ATOM 915 CB VAL A 169 -10.933 4.374 -28.404 1.00 37.14 C ANISOU 915 CB VAL A 169 4257 5459 4394 -13 642 79 C ATOM 916 CG1 VAL A 169 -12.293 3.754 -28.131 1.00 36.50 C ANISOU 916 CG1 VAL A 169 4046 5530 4293 -108 764 141 C ATOM 917 CG2 VAL A 169 -10.996 5.882 -28.262 1.00 35.69 C ANISOU 917 CG2 VAL A 169 4049 5272 4238 165 670 38 C ATOM 918 N CYS A 170 -9.369 1.620 -28.447 1.00 33.56 N ANISOU 918 N CYS A 170 4100 4790 3862 -254 544 124 N ATOM 919 CA CYS A 170 -9.541 0.182 -28.605 1.00 38.11 C ANISOU 919 CA CYS A 170 4756 5321 4404 -411 579 171 C ATOM 920 C CYS A 170 -8.427 -0.636 -27.969 1.00 36.89 C ANISOU 920 C CYS A 170 4809 5014 4192 -382 556 199 C ATOM 921 O CYS A 170 -8.627 -1.830 -27.718 1.00 40.09 O ANISOU 921 O CYS A 170 5332 5359 4540 -491 620 248 O ATOM 922 CB CYS A 170 -9.658 -0.175 -30.092 1.00 34.39 C ANISOU 922 CB CYS A 170 4222 4844 4002 -518 530 167 C ATOM 923 SG CYS A 170 -11.144 0.511 -30.883 1.00 40.02 S ANISOU 923 SG CYS A 170 4667 5776 4765 -589 540 181 S ATOM 924 N HIS A 171 -7.269 -0.036 -27.701 1.00 32.66 N ANISOU 924 N HIS A 171 4322 4421 3668 -245 467 182 N ATOM 925 CA HIS A 171 -6.164 -0.713 -27.019 1.00 33.10 C ANISOU 925 CA HIS A 171 4536 4369 3671 -192 425 237 C ATOM 926 C HIS A 171 -5.583 0.209 -25.953 1.00 34.78 C ANISOU 926 C HIS A 171 4778 4618 3817 -91 362 223 C ATOM 927 O HIS A 171 -4.414 0.605 -26.023 1.00 36.09 O ANISOU 927 O HIS A 171 4948 4754 4011 -10 249 226 O ATOM 928 CB HIS A 171 -5.092 -1.142 -28.021 1.00 39.44 C ANISOU 928 CB HIS A 171 5359 5063 4564 -152 361 254 C ATOM 929 CG HIS A 171 -5.622 -1.984 -29.141 1.00 44.90 C ANISOU 929 CG HIS A 171 6064 5699 5298 -273 427 250 C ATOM 930 ND1 HIS A 171 -5.866 -3.334 -29.007 1.00 46.20 N ANISOU 930 ND1 HIS A 171 6384 5762 5410 -366 516 303 N ATOM 931 CD2 HIS A 171 -5.968 -1.663 -30.410 1.00 44.59 C ANISOU 931 CD2 HIS A 171 5926 5687 5329 -336 415 198 C ATOM 932 CE1 HIS A 171 -6.331 -3.810 -30.149 1.00 46.37 C ANISOU 932 CE1 HIS A 171 6412 5747 5462 -498 557 274 C ATOM 933 NE2 HIS A 171 -6.402 -2.817 -31.017 1.00 43.11 N ANISOU 933 NE2 HIS A 171 5838 5421 5120 -483 490 213 N ATOM 934 N PRO A 172 -6.378 0.562 -24.938 1.00 35.33 N ANISOU 934 N PRO A 172 4876 4760 3786 -108 438 207 N ATOM 935 CA PRO A 172 -5.914 1.566 -23.963 1.00 34.03 C ANISOU 935 CA PRO A 172 4774 4625 3533 -39 389 170 C ATOM 936 C PRO A 172 -4.682 1.147 -23.181 1.00 42.17 C ANISOU 936 C PRO A 172 5936 5608 4477 -9 275 238 C ATOM 937 O PRO A 172 -3.905 2.015 -22.763 1.00 42.46 O ANISOU 937 O PRO A 172 6000 5665 4468 28 172 209 O ATOM 938 CB PRO A 172 -7.132 1.746 -23.046 1.00 32.29 C ANISOU 938 CB PRO A 172 4585 4475 3209 -73 541 149 C ATOM 939 CG PRO A 172 -7.886 0.461 -23.163 1.00 33.23 C ANISOU 939 CG PRO A 172 4706 4594 3326 -177 637 216 C ATOM 940 CD PRO A 172 -7.709 0.031 -24.593 1.00 37.37 C ANISOU 940 CD PRO A 172 5127 5078 3994 -208 585 223 C ATOM 941 N VAL A 173 -4.473 -0.153 -22.963 1.00 35.97 N ANISOU 941 N VAL A 173 5240 4764 3664 -30 287 339 N ATOM 942 CA VAL A 173 -3.271 -0.592 -22.260 1.00 38.72 C ANISOU 942 CA VAL A 173 5689 5083 3940 26 167 438 C ATOM 943 C VAL A 173 -2.040 -0.387 -23.136 1.00 38.98 C ANISOU 943 C VAL A 173 5614 5094 4101 107 37 457 C ATOM 944 O VAL A 173 -1.029 0.172 -22.695 1.00 40.23 O ANISOU 944 O VAL A 173 5759 5305 4221 145 -104 481 O ATOM 945 CB VAL A 173 -3.410 -2.057 -21.813 1.00 45.97 C ANISOU 945 CB VAL A 173 6748 5920 4796 7 233 558 C ATOM 946 CG1 VAL A 173 -2.090 -2.561 -21.248 1.00 47.22 C ANISOU 946 CG1 VAL A 173 6980 6053 4909 102 97 694 C ATOM 947 CG2 VAL A 173 -4.515 -2.186 -20.774 1.00 45.55 C ANISOU 947 CG2 VAL A 173 6808 5907 4592 -85 358 549 C ATOM 948 N LYS A 174 -2.108 -0.831 -24.392 1.00 37.75 N ANISOU 948 N LYS A 174 5381 4872 4089 115 86 447 N ATOM 949 CA LYS A 174 -1.011 -0.593 -25.322 1.00 41.25 C ANISOU 949 CA LYS A 174 5717 5297 4660 190 -2 455 C ATOM 950 C LYS A 174 -0.820 0.891 -25.610 1.00 42.02 C ANISOU 950 C LYS A 174 5703 5473 4788 180 -79 352 C ATOM 951 O LYS A 174 0.294 1.308 -25.942 1.00 40.81 O ANISOU 951 O LYS A 174 5470 5342 4696 226 -186 371 O ATOM 952 CB LYS A 174 -1.253 -1.363 -26.623 1.00 45.68 C ANISOU 952 CB LYS A 174 6261 5756 5340 179 94 448 C ATOM 953 CG LYS A 174 -1.259 -2.879 -26.447 1.00 60.42 C ANISOU 953 CG LYS A 174 8277 7498 7180 192 181 553 C ATOM 954 CD LYS A 174 -1.661 -3.594 -27.726 1.00 66.87 C ANISOU 954 CD LYS A 174 9126 8200 8081 134 295 519 C ATOM 955 CE LYS A 174 -1.685 -5.103 -27.528 1.00 70.70 C ANISOU 955 CE LYS A 174 9813 8525 8526 135 404 615 C ATOM 956 NZ LYS A 174 -2.132 -5.817 -28.757 1.00 73.90 N ANISOU 956 NZ LYS A 174 10296 8802 8980 36 524 566 N ATOM 957 N ALA A 175 -1.878 1.696 -25.475 1.00 36.08 N ANISOU 957 N ALA A 175 4948 4762 3998 123 -16 254 N ATOM 958 CA ALA A 175 -1.752 3.135 -25.676 1.00 31.90 C ANISOU 958 CA ALA A 175 4360 4276 3486 123 -68 159 C ATOM 959 C ALA A 175 -0.753 3.754 -24.709 1.00 34.40 C ANISOU 959 C ALA A 175 4735 4638 3699 118 -198 171 C ATOM 960 O ALA A 175 -0.133 4.775 -25.027 1.00 37.29 O ANISOU 960 O ALA A 175 5055 5020 4093 106 -280 118 O ATOM 961 CB ALA A 175 -3.118 3.808 -25.525 1.00 31.50 C ANISOU 961 CB ALA A 175 4313 4255 3401 99 50 75 C ATOM 962 N LEU A 176 -0.583 3.153 -23.527 1.00 33.86 N ANISOU 962 N LEU A 176 4778 4593 3494 107 -227 246 N ATOM 963 CA LEU A 176 0.374 3.675 -22.557 1.00 37.50 C ANISOU 963 CA LEU A 176 5302 5120 3827 72 -376 272 C ATOM 964 C LEU A 176 1.800 3.627 -23.093 1.00 46.13 C ANISOU 964 C LEU A 176 6262 6252 5014 104 -529 350 C ATOM 965 O LEU A 176 2.621 4.487 -22.750 1.00 42.85 O ANISOU 965 O LEU A 176 5834 5908 4539 40 -666 334 O ATOM 966 CB LEU A 176 0.269 2.890 -21.245 1.00 33.54 C ANISOU 966 CB LEU A 176 4949 4643 3152 56 -383 362 C ATOM 967 CG LEU A 176 -1.062 2.977 -20.494 1.00 38.83 C ANISOU 967 CG LEU A 176 5760 5296 3697 11 -223 293 C ATOM 968 CD1 LEU A 176 -1.088 2.017 -19.304 1.00 39.67 C ANISOU 968 CD1 LEU A 176 6020 5416 3636 -8 -226 406 C ATOM 969 CD2 LEU A 176 -1.326 4.404 -20.030 1.00 34.89 C ANISOU 969 CD2 LEU A 176 5345 4816 3095 -47 -208 157 C ATOM 970 N ASP A 177 2.111 2.637 -23.931 1.00 45.43 N ANISOU 970 N ASP A 177 6078 6116 5066 192 -497 434 N ATOM 971 CA ASP A 177 3.427 2.532 -24.548 1.00 43.87 C ANISOU 971 CA ASP A 177 5729 5956 4982 250 -601 517 C ATOM 972 C ASP A 177 3.520 3.286 -25.868 1.00 44.03 C ANISOU 972 C ASP A 177 5633 5948 5148 238 -569 420 C ATOM 973 O ASP A 177 4.584 3.828 -26.188 1.00 45.83 O ANISOU 973 O ASP A 177 5740 6242 5430 227 -674 442 O ATOM 974 CB ASP A 177 3.784 1.061 -24.786 1.00 51.38 C ANISOU 974 CB ASP A 177 6667 6847 6009 377 -552 664 C ATOM 975 CG ASP A 177 3.799 0.247 -23.502 1.00 66.86 C ANISOU 975 CG ASP A 177 8752 8827 7825 404 -590 790 C ATOM 976 OD1 ASP A 177 4.270 0.768 -22.470 1.00 72.14 O ANISOU 976 OD1 ASP A 177 9441 9612 8355 347 -738 825 O ATOM 977 OD2 ASP A 177 3.335 -0.913 -23.527 1.00 67.38 O1- ANISOU 977 OD2 ASP A 177 8914 8784 7901 466 -474 855 O1- ATOM 978 N PHE A 178 2.432 3.342 -26.637 1.00 39.67 N ANISOU 978 N PHE A 178 5106 5314 4653 228 -433 325 N ATOM 979 CA PHE A 178 2.500 3.931 -27.971 1.00 36.59 C ANISOU 979 CA PHE A 178 4618 4891 4392 222 -402 253 C ATOM 980 C PHE A 178 2.442 5.454 -27.939 1.00 42.67 C ANISOU 980 C PHE A 178 5392 5692 5128 146 -453 145 C ATOM 981 O PHE A 178 3.086 6.115 -28.761 1.00 41.21 O ANISOU 981 O PHE A 178 5122 5510 5025 127 -492 119 O ATOM 982 CB PHE A 178 1.373 3.382 -28.848 1.00 39.40 C ANISOU 982 CB PHE A 178 4996 5165 4808 226 -259 211 C ATOM 983 CG PHE A 178 1.272 4.052 -30.193 1.00 50.00 C ANISOU 983 CG PHE A 178 6262 6480 6254 206 -232 138 C ATOM 984 CD1 PHE A 178 2.169 3.746 -31.204 1.00 54.30 C ANISOU 984 CD1 PHE A 178 6733 6994 6905 241 -230 172 C ATOM 985 CD2 PHE A 178 0.280 4.988 -30.446 1.00 48.54 C ANISOU 985 CD2 PHE A 178 6084 6302 6056 165 -197 46 C ATOM 986 CE1 PHE A 178 2.079 4.360 -32.442 1.00 50.61 C ANISOU 986 CE1 PHE A 178 6216 6501 6513 212 -204 109 C ATOM 987 CE2 PHE A 178 0.186 5.606 -31.682 1.00 52.43 C ANISOU 987 CE2 PHE A 178 6517 6773 6633 152 -184 -2 C ATOM 988 CZ PHE A 178 1.087 5.290 -32.680 1.00 47.01 C ANISOU 988 CZ PHE A 178 5774 6054 6034 163 -192 25 C ATOM 989 N ARG A 179 1.681 6.034 -27.016 1.00 36.86 N ANISOU 989 N ARG A 179 4774 4965 4268 103 -434 82 N ATOM 990 CA ARG A 179 1.359 7.460 -27.103 1.00 35.56 C ANISOU 990 CA ARG A 179 4658 4779 4074 53 -427 -33 C ATOM 991 C ARG A 179 2.346 8.327 -26.328 1.00 37.85 C ANISOU 991 C ARG A 179 5006 5116 4258 -42 -561 -50 C ATOM 992 O ARG A 179 1.969 9.254 -25.611 1.00 45.57 O ANISOU 992 O ARG A 179 6132 6069 5112 -100 -545 -136 O ATOM 993 CB ARG A 179 -0.069 7.695 -26.633 1.00 38.55 C ANISOU 993 CB ARG A 179 5136 5128 4384 73 -295 -98 C ATOM 994 CG ARG A 179 -1.093 6.859 -27.382 1.00 40.42 C ANISOU 994 CG ARG A 179 5297 5349 4712 124 -179 -74 C ATOM 995 CD ARG A 179 -2.502 7.285 -27.030 1.00 40.38 C ANISOU 995 CD ARG A 179 5335 5346 4660 148 -47 -129 C ATOM 996 NE ARG A 179 -2.949 8.418 -27.834 1.00 35.37 N ANISOU 996 NE ARG A 179 4661 4682 4095 186 -9 -193 N ATOM 997 CZ ARG A 179 -3.931 9.239 -27.479 1.00 42.06 C ANISOU 997 CZ ARG A 179 5556 5522 4905 239 100 -244 C ATOM 998 NH1 ARG A 179 -4.557 9.066 -26.321 1.00 37.45 N ANISOU 998 NH1 ARG A 179 5061 4961 4207 246 190 -252 N ATOM 999 NH2 ARG A 179 -4.280 10.239 -28.277 1.00 39.24 N ANISOU 999 NH2 ARG A 179 5163 5127 4620 297 131 -279 N ATOM 1000 N THR A 180 3.613 8.037 -26.485 1.00 36.81 N ANISOU 1000 N THR A 180 4763 5054 4169 -65 -686 34 N ATOM 1001 CA THR A 180 4.678 8.812 -25.876 1.00 39.33 C ANISOU 1001 CA THR A 180 5097 5453 4395 -192 -841 36 C ATOM 1002 C THR A 180 5.278 9.777 -26.890 1.00 38.70 C ANISOU 1002 C THR A 180 4939 5354 4412 -256 -866 -16 C ATOM 1003 O THR A 180 5.229 9.524 -28.098 1.00 35.56 O ANISOU 1003 O THR A 180 4428 4914 4171 -180 -794 -7 O ATOM 1004 CB THR A 180 5.784 7.895 -25.348 1.00 44.70 C ANISOU 1004 CB THR A 180 5661 6264 5061 -181 -980 195 C ATOM 1005 OG1 THR A 180 6.400 7.211 -26.447 1.00 42.00 O ANISOU 1005 OG1 THR A 180 5122 5932 4905 -79 -958 281 O ATOM 1006 CG2 THR A 180 5.215 6.872 -24.379 1.00 47.87 C ANISOU 1006 CG2 THR A 180 6157 6669 5362 -114 -951 264 C ATOM 1007 N PRO A 181 5.845 10.895 -26.429 1.00 40.61 N ANISOU 1007 N PRO A 181 4529 6830 4072 -470 28 -216 N ATOM 1008 CA PRO A 181 6.572 11.772 -27.360 1.00 39.23 C ANISOU 1008 CA PRO A 181 4420 6447 4037 -467 12 -368 C ATOM 1009 C PRO A 181 7.720 11.071 -28.062 1.00 42.47 C ANISOU 1009 C PRO A 181 4725 6779 4632 -514 -113 -257 C ATOM 1010 O PRO A 181 7.998 11.372 -29.230 1.00 36.97 O ANISOU 1010 O PRO A 181 4033 5895 4117 -489 -95 -312 O ATOM 1011 CB PRO A 181 7.067 12.916 -26.458 1.00 41.18 C ANISOU 1011 CB PRO A 181 4824 6757 4065 -566 9 -568 C ATOM 1012 CG PRO A 181 6.937 12.409 -25.049 1.00 43.69 C ANISOU 1012 CG PRO A 181 5102 7354 4145 -619 -35 -485 C ATOM 1013 CD PRO A 181 5.788 11.451 -25.065 1.00 42.41 C ANISOU 1013 CD PRO A 181 4839 7262 4013 -520 41 -307 C ATOM 1014 N ARG A 182 8.391 10.132 -27.389 1.00 40.41 N ANISOU 1014 N ARG A 182 4374 6670 4309 -545 -233 -90 N ATOM 1015 CA ARG A 182 9.486 9.408 -28.026 1.00 39.02 C ANISOU 1015 CA ARG A 182 4088 6455 4283 -509 -341 26 C ATOM 1016 C ARG A 182 8.993 8.599 -29.221 1.00 39.17 C ANISOU 1016 C ARG A 182 4105 6243 4533 -411 -280 125 C ATOM 1017 O ARG A 182 9.622 8.604 -30.286 1.00 38.52 O ANISOU 1017 O ARG A 182 3975 6036 4624 -374 -294 98 O ATOM 1018 CB ARG A 182 10.172 8.500 -27.007 1.00 46.89 C ANISOU 1018 CB ARG A 182 5015 7673 5127 -475 -472 217 C ATOM 1019 CG ARG A 182 11.445 7.845 -27.514 1.00 49.21 C ANISOU 1019 CG ARG A 182 5171 8008 5517 -366 -589 332 C ATOM 1020 CD ARG A 182 12.062 6.972 -26.433 1.00 61.23 C ANISOU 1020 CD ARG A 182 6643 9779 6844 -257 -720 547 C ATOM 1021 NE ARG A 182 13.430 6.576 -26.753 1.00 70.36 N ANISOU 1021 NE ARG A 182 7611 11101 8022 -109 -846 629 N ATOM 1022 CZ ARG A 182 13.754 5.473 -27.418 1.00 68.95 C ANISOU 1022 CZ ARG A 182 7447 10770 7982 140 -847 812 C ATOM 1023 NH1 ARG A 182 12.805 4.647 -27.839 1.00 62.21 N ANISOU 1023 NH1 ARG A 182 6819 9562 7257 201 -733 922 N ATOM 1024 NH2 ARG A 182 15.027 5.194 -27.662 1.00 72.71 N ANISOU 1024 NH2 ARG A 182 7714 11469 8444 321 -954 876 N ATOM 1025 N ASN A 183 7.871 7.894 -29.064 1.00 36.92 N ANISOU 1025 N ASN A 183 3871 5925 4231 -402 -204 231 N ATOM 1026 CA ASN A 183 7.355 7.091 -30.166 1.00 41.23 C ANISOU 1026 CA ASN A 183 4433 6273 4958 -375 -146 304 C ATOM 1027 C ASN A 183 6.777 7.955 -31.278 1.00 40.20 C ANISOU 1027 C ASN A 183 4283 6046 4945 -359 -61 137 C ATOM 1028 O ASN A 183 6.824 7.563 -32.450 1.00 35.89 O ANISOU 1028 O ASN A 183 3730 5338 4569 -331 -46 147 O ATOM 1029 CB ASN A 183 6.303 6.108 -29.658 1.00 36.80 C ANISOU 1029 CB ASN A 183 3936 5741 4304 -456 -81 453 C ATOM 1030 CG ASN A 183 6.917 4.848 -29.092 1.00 51.14 C ANISOU 1030 CG ASN A 183 5860 7500 6071 -428 -149 682 C ATOM 1031 OD1 ASN A 183 7.993 4.425 -29.516 1.00 51.81 O ANISOU 1031 OD1 ASN A 183 5957 7473 6256 -295 -229 745 O ATOM 1032 ND2 ASN A 183 6.236 4.238 -28.133 1.00 45.86 N ANISOU 1032 ND2 ASN A 183 5281 6919 5225 -531 -106 820 N ATOM 1033 N ALA A 184 6.229 9.124 -30.939 1.00 40.21 N ANISOU 1033 N ALA A 184 4303 6138 4838 -348 2 -14 N ATOM 1034 CA ALA A 184 5.719 10.020 -31.971 1.00 38.93 C ANISOU 1034 CA ALA A 184 4161 5876 4755 -267 84 -151 C ATOM 1035 C ALA A 184 6.839 10.493 -32.886 1.00 39.26 C ANISOU 1035 C ALA A 184 4237 5741 4939 -266 40 -220 C ATOM 1036 O ALA A 184 6.653 10.599 -34.104 1.00 40.27 O ANISOU 1036 O ALA A 184 4366 5738 5197 -210 80 -246 O ATOM 1037 CB ALA A 184 5.006 11.209 -31.330 1.00 35.93 C ANISOU 1037 CB ALA A 184 3861 5595 4197 -190 173 -294 C ATOM 1038 N LYS A 185 8.014 10.778 -32.319 1.00 36.41 N ANISOU 1038 N LYS A 185 3884 5421 4529 -350 -40 -251 N ATOM 1039 CA LYS A 185 9.151 11.164 -33.147 1.00 38.91 C ANISOU 1039 CA LYS A 185 4186 5643 4953 -401 -74 -310 C ATOM 1040 C LYS A 185 9.661 9.986 -33.966 1.00 44.38 C ANISOU 1040 C LYS A 185 4761 6288 5814 -339 -122 -176 C ATOM 1041 O LYS A 185 10.055 10.155 -35.126 1.00 39.25 O ANISOU 1041 O LYS A 185 4101 5519 5294 -326 -95 -215 O ATOM 1042 CB LYS A 185 10.265 11.745 -32.276 1.00 38.84 C ANISOU 1042 CB LYS A 185 4167 5787 4804 -556 -153 -388 C ATOM 1043 CG LYS A 185 9.939 13.122 -31.710 1.00 51.01 C ANISOU 1043 CG LYS A 185 5918 7286 6178 -650 -79 -578 C ATOM 1044 CD LYS A 185 10.919 13.538 -30.628 1.00 62.35 C ANISOU 1044 CD LYS A 185 7340 8931 7418 -863 -169 -661 C ATOM 1045 CE LYS A 185 10.579 14.918 -30.086 1.00 78.25 C ANISOU 1045 CE LYS A 185 9648 10838 9245 -976 -72 -881 C ATOM 1046 NZ LYS A 185 11.375 15.266 -28.875 1.00 87.36 N ANISOU 1046 NZ LYS A 185 10802 12236 10157 -1221 -162 -981 N ATOM 1047 N ILE A 186 9.658 8.784 -33.387 1.00 38.40 N ANISOU 1047 N ILE A 186 3954 5599 5037 -290 -178 -14 N ATOM 1048 CA ILE A 186 10.059 7.603 -34.144 1.00 41.58 C ANISOU 1048 CA ILE A 186 4327 5895 5578 -191 -198 110 C ATOM 1049 C ILE A 186 9.111 7.373 -35.317 1.00 41.00 C ANISOU 1049 C ILE A 186 4316 5634 5628 -183 -105 83 C ATOM 1050 O ILE A 186 9.546 7.066 -36.434 1.00 38.58 O ANISOU 1050 O ILE A 186 4001 5205 5454 -130 -90 74 O ATOM 1051 CB ILE A 186 10.132 6.373 -33.220 1.00 40.47 C ANISOU 1051 CB ILE A 186 4219 5802 5354 -124 -254 304 C ATOM 1052 CG1 ILE A 186 11.267 6.539 -32.207 1.00 44.84 C ANISOU 1052 CG1 ILE A 186 4664 6606 5768 -92 -373 345 C ATOM 1053 CG2 ILE A 186 10.323 5.100 -34.032 1.00 36.96 C ANISOU 1053 CG2 ILE A 186 3854 5154 5036 -2 -235 424 C ATOM 1054 CD1 ILE A 186 11.359 5.416 -31.191 1.00 41.00 C ANISOU 1054 CD1 ILE A 186 4239 6185 5155 16 -434 563 C ATOM 1055 N VAL A 187 7.805 7.531 -35.087 1.00 36.61 N ANISOU 1055 N VAL A 187 3800 5106 5006 -234 -42 63 N ATOM 1056 CA VAL A 187 6.828 7.309 -36.150 1.00 39.38 C ANISOU 1056 CA VAL A 187 4160 5376 5426 -247 31 36 C ATOM 1057 C VAL A 187 7.016 8.323 -37.273 1.00 42.51 C ANISOU 1057 C VAL A 187 4549 5702 5900 -187 63 -90 C ATOM 1058 O VAL A 187 6.954 7.973 -38.459 1.00 35.92 O ANISOU 1058 O VAL A 187 3716 4766 5165 -172 86 -100 O ATOM 1059 CB VAL A 187 5.399 7.346 -35.578 1.00 39.70 C ANISOU 1059 CB VAL A 187 4172 5580 5332 -310 91 41 C ATOM 1060 CG1 VAL A 187 4.375 7.415 -36.701 1.00 33.48 C ANISOU 1060 CG1 VAL A 187 3326 4823 4570 -316 152 -16 C ATOM 1061 CG2 VAL A 187 5.146 6.121 -34.710 1.00 41.42 C ANISOU 1061 CG2 VAL A 187 4438 5825 5473 -426 82 191 C ATOM 1062 N ASN A 188 7.253 9.591 -36.921 1.00 33.47 N ANISOU 1062 N ASN A 188 3438 4590 4688 -167 75 -189 N ATOM 1063 CA ASN A 188 7.520 10.608 -37.934 1.00 38.81 C ANISOU 1063 CA ASN A 188 4181 5153 5412 -126 121 -291 C ATOM 1064 C ASN A 188 8.732 10.239 -38.784 1.00 38.65 C ANISOU 1064 C ASN A 188 4119 5045 5520 -160 90 -277 C ATOM 1065 O ASN A 188 8.740 10.471 -39.999 1.00 39.18 O ANISOU 1065 O ASN A 188 4216 5014 5658 -128 135 -311 O ATOM 1066 CB ASN A 188 7.723 11.973 -37.271 1.00 32.78 C ANISOU 1066 CB ASN A 188 3550 4379 4528 -145 153 -402 C ATOM 1067 CG ASN A 188 6.423 12.582 -36.770 1.00 33.24 C ANISOU 1067 CG ASN A 188 3681 4503 4448 -20 226 -444 C ATOM 1068 OD1 ASN A 188 5.334 12.185 -37.185 1.00 37.65 O ANISOU 1068 OD1 ASN A 188 4153 5151 5002 84 258 -399 O ATOM 1069 ND2 ASN A 188 6.534 13.564 -35.881 1.00 37.05 N ANISOU 1069 ND2 ASN A 188 4316 4972 4790 -32 259 -542 N ATOM 1070 N VAL A 189 9.762 9.655 -38.167 1.00 36.58 N ANISOU 1070 N VAL A 189 3775 4858 5266 -198 17 -221 N ATOM 1071 CA VAL A 189 10.945 9.251 -38.924 1.00 37.30 C ANISOU 1071 CA VAL A 189 3780 4940 5454 -181 -3 -204 C ATOM 1072 C VAL A 189 10.618 8.080 -39.842 1.00 37.57 C ANISOU 1072 C VAL A 189 3829 4852 5596 -82 21 -138 C ATOM 1073 O VAL A 189 11.006 8.067 -41.017 1.00 35.01 O ANISOU 1073 O VAL A 189 3496 4455 5352 -53 64 -176 O ATOM 1074 CB VAL A 189 12.106 8.912 -37.970 1.00 43.19 C ANISOU 1074 CB VAL A 189 4394 5878 6138 -188 -96 -148 C ATOM 1075 CG1 VAL A 189 13.262 8.275 -38.735 1.00 39.82 C ANISOU 1075 CG1 VAL A 189 3834 5505 5792 -90 -108 -109 C ATOM 1076 CG2 VAL A 189 12.579 10.160 -37.239 1.00 39.82 C ANISOU 1076 CG2 VAL A 189 3963 5586 5582 -363 -116 -258 C ATOM 1077 N CYS A 190 9.907 7.075 -39.322 1.00 34.33 N ANISOU 1077 N CYS A 190 3468 4409 5165 -61 7 -46 N ATOM 1078 CA CYS A 190 9.513 5.938 -40.148 1.00 34.82 C ANISOU 1078 CA CYS A 190 3614 4318 5299 -32 44 -5 C ATOM 1079 C CYS A 190 8.655 6.382 -41.327 1.00 40.20 C ANISOU 1079 C CYS A 190 4313 4956 6005 -82 104 -99 C ATOM 1080 O CYS A 190 8.840 5.906 -42.453 1.00 37.01 O ANISOU 1080 O CYS A 190 3948 4446 5669 -57 138 -128 O ATOM 1081 CB CYS A 190 8.768 4.907 -39.301 1.00 35.54 C ANISOU 1081 CB CYS A 190 3806 4372 5324 -85 37 105 C ATOM 1082 SG CYS A 190 9.794 4.069 -38.061 1.00 41.55 S ANISOU 1082 SG CYS A 190 4604 5153 6031 45 -36 269 S ATOM 1083 N ASN A 191 7.707 7.291 -41.085 1.00 32.76 N ANISOU 1083 N ASN A 191 3346 4118 4984 -122 121 -146 N ATOM 1084 CA ASN A 191 6.882 7.808 -42.171 1.00 34.97 C ANISOU 1084 CA ASN A 191 3622 4417 5248 -109 167 -216 C ATOM 1085 C ASN A 191 7.715 8.577 -43.186 1.00 38.08 C ANISOU 1085 C ASN A 191 4041 4728 5700 -50 194 -276 C ATOM 1086 O ASN A 191 7.430 8.528 -44.389 1.00 37.26 O ANISOU 1086 O ASN A 191 3953 4596 5609 -31 225 -308 O ATOM 1087 CB ASN A 191 5.774 8.701 -41.613 1.00 31.04 C ANISOU 1087 CB ASN A 191 3090 4078 4624 -74 187 -240 C ATOM 1088 CG ASN A 191 4.679 7.908 -40.934 1.00 38.93 C ANISOU 1088 CG ASN A 191 4022 5233 5536 -170 186 -189 C ATOM 1089 OD1 ASN A 191 4.532 6.709 -41.168 1.00 42.78 O ANISOU 1089 OD1 ASN A 191 4529 5673 6051 -302 179 -147 O ATOM 1090 ND2 ASN A 191 3.895 8.577 -40.097 1.00 35.56 N ANISOU 1090 ND2 ASN A 191 3541 4988 4982 -119 208 -199 N ATOM 1091 N TRP A 192 8.742 9.291 -42.728 1.00 33.83 N ANISOU 1091 N TRP A 192 3508 4178 5169 -56 187 -294 N ATOM 1092 CA TRP A 192 9.609 9.999 -43.660 1.00 36.79 C ANISOU 1092 CA TRP A 192 3911 4492 5577 -65 230 -345 C ATOM 1093 C TRP A 192 10.428 9.023 -44.495 1.00 44.90 C ANISOU 1093 C TRP A 192 4874 5489 6696 -40 236 -330 C ATOM 1094 O TRP A 192 10.631 9.242 -45.696 1.00 38.01 O ANISOU 1094 O TRP A 192 4028 4571 5842 -30 292 -368 O ATOM 1095 CB TRP A 192 10.519 10.962 -42.901 1.00 35.05 C ANISOU 1095 CB TRP A 192 3706 4306 5307 -162 226 -384 C ATOM 1096 CG TRP A 192 11.408 11.747 -43.808 1.00 45.30 C ANISOU 1096 CG TRP A 192 5048 5557 6609 -247 289 -437 C ATOM 1097 CD1 TRP A 192 11.106 12.918 -44.441 1.00 48.31 C ANISOU 1097 CD1 TRP A 192 5624 5806 6925 -270 371 -480 C ATOM 1098 CD2 TRP A 192 12.744 11.413 -44.196 1.00 46.40 C ANISOU 1098 CD2 TRP A 192 5042 5798 6792 -316 292 -440 C ATOM 1099 NE1 TRP A 192 12.175 13.336 -45.195 1.00 50.57 N ANISOU 1099 NE1 TRP A 192 5916 6085 7215 -406 429 -510 N ATOM 1100 CE2 TRP A 192 13.194 12.430 -45.061 1.00 50.31 C ANISOU 1100 CE2 TRP A 192 5639 6230 7246 -441 382 -493 C ATOM 1101 CE3 TRP A 192 13.606 10.353 -43.894 1.00 50.00 C ANISOU 1101 CE3 TRP A 192 5294 6408 7296 -255 236 -393 C ATOM 1102 CZ2 TRP A 192 14.466 12.419 -45.629 1.00 50.26 C ANISOU 1102 CZ2 TRP A 192 5493 6359 7245 -556 421 -514 C ATOM 1103 CZ3 TRP A 192 14.868 10.344 -44.458 1.00 58.63 C ANISOU 1103 CZ3 TRP A 192 6233 7652 8393 -301 268 -412 C ATOM 1104 CH2 TRP A 192 15.286 11.371 -45.314 1.00 56.32 C ANISOU 1104 CH2 TRP A 192 6000 7342 8059 -474 362 -479 C ATOM 1105 N ILE A 193 10.906 7.939 -43.878 1.00 35.98 N ANISOU 1105 N ILE A 193 3685 4382 5604 1 190 -269 N ATOM 1106 CA ILE A 193 11.613 6.905 -44.628 1.00 37.96 C ANISOU 1106 CA ILE A 193 3922 4579 5923 97 214 -254 C ATOM 1107 C ILE A 193 10.703 6.311 -45.693 1.00 42.04 C ANISOU 1107 C ILE A 193 4552 4967 6453 89 259 -290 C ATOM 1108 O ILE A 193 11.120 6.086 -46.837 1.00 40.87 O ANISOU 1108 O ILE A 193 4424 4773 6333 134 315 -339 O ATOM 1109 CB ILE A 193 12.148 5.823 -43.672 1.00 37.67 C ANISOU 1109 CB ILE A 193 3867 4554 5891 207 163 -156 C ATOM 1110 CG1 ILE A 193 13.199 6.417 -42.731 1.00 38.83 C ANISOU 1110 CG1 ILE A 193 3843 4920 5989 209 103 -132 C ATOM 1111 CG2 ILE A 193 12.716 4.644 -44.456 1.00 38.06 C ANISOU 1111 CG2 ILE A 193 3981 4489 5992 375 211 -142 C ATOM 1112 CD1 ILE A 193 13.717 5.443 -41.690 1.00 45.19 C ANISOU 1112 CD1 ILE A 193 4619 5794 6759 364 34 -7 C ATOM 1113 N LEU A 194 9.442 6.055 -45.336 1.00 38.37 N ANISOU 1113 N LEU A 194 4149 4489 5941 9 238 -275 N ATOM 1114 CA LEU A 194 8.486 5.529 -46.303 1.00 45.61 C ANISOU 1114 CA LEU A 194 5140 5363 6828 -63 267 -324 C ATOM 1115 C LEU A 194 8.228 6.532 -47.421 1.00 47.31 C ANISOU 1115 C LEU A 194 5321 5652 7005 -48 296 -390 C ATOM 1116 O LEU A 194 8.177 6.159 -48.599 1.00 47.61 O ANISOU 1116 O LEU A 194 5406 5654 7031 -59 331 -446 O ATOM 1117 CB LEU A 194 7.183 5.158 -45.595 1.00 38.86 C ANISOU 1117 CB LEU A 194 4293 4579 5891 -196 240 -293 C ATOM 1118 CG LEU A 194 6.083 4.503 -46.429 1.00 46.77 C ANISOU 1118 CG LEU A 194 5338 5617 6816 -355 257 -351 C ATOM 1119 CD1 LEU A 194 6.568 3.183 -47.014 1.00 43.05 C ANISOU 1119 CD1 LEU A 194 5066 4906 6385 -402 300 -380 C ATOM 1120 CD2 LEU A 194 4.830 4.297 -45.588 1.00 48.90 C ANISOU 1120 CD2 LEU A 194 5546 6058 6976 -521 237 -317 C ATOM 1121 N SER A 195 8.069 7.811 -47.070 1.00 40.15 N ANISOU 1121 N SER A 195 4373 4828 6055 -14 290 -382 N ATOM 1122 CA SER A 195 7.892 8.842 -48.087 1.00 43.64 C ANISOU 1122 CA SER A 195 4847 5296 6438 39 330 -413 C ATOM 1123 C SER A 195 9.107 8.942 -49.002 1.00 43.33 C ANISOU 1123 C SER A 195 4835 5179 6451 45 387 -441 C ATOM 1124 O SER A 195 8.975 9.329 -50.168 1.00 41.40 O ANISOU 1124 O SER A 195 4640 4939 6151 70 429 -464 O ATOM 1125 CB SER A 195 7.614 10.191 -47.422 1.00 36.06 C ANISOU 1125 CB SER A 195 3931 4360 5409 98 337 -396 C ATOM 1126 OG SER A 195 6.424 10.147 -46.658 1.00 44.98 O ANISOU 1126 OG SER A 195 5008 5619 6462 131 303 -377 O ATOM 1127 N SER A 196 10.292 8.592 -48.496 1.00 38.09 N ANISOU 1127 N SER A 196 4115 4490 5866 34 390 -432 N ATOM 1128 CA SER A 196 11.506 8.664 -49.300 1.00 41.59 C ANISOU 1128 CA SER A 196 4523 4942 6337 40 457 -461 C ATOM 1129 C SER A 196 11.518 7.650 -50.438 1.00 42.19 C ANISOU 1129 C SER A 196 4634 4974 6425 99 499 -505 C ATOM 1130 O SER A 196 12.251 7.847 -51.413 1.00 46.33 O ANISOU 1130 O SER A 196 5143 5527 6932 111 576 -540 O ATOM 1131 CB SER A 196 12.734 8.461 -48.412 1.00 43.43 C ANISOU 1131 CB SER A 196 4623 5262 6616 45 438 -437 C ATOM 1132 OG SER A 196 12.835 9.486 -47.439 1.00 45.74 O ANISOU 1132 OG SER A 196 4904 5608 6868 -62 407 -426 O ATOM 1133 N ALA A 197 10.731 6.572 -50.337 1.00 42.37 N ANISOU 1133 N ALA A 197 4722 4923 6452 105 465 -513 N ATOM 1134 CA ALA A 197 10.681 5.576 -51.404 1.00 47.80 C ANISOU 1134 CA ALA A 197 5508 5532 7123 124 514 -585 C ATOM 1135 C ALA A 197 10.208 6.171 -52.722 1.00 49.56 C ANISOU 1135 C ALA A 197 5759 5823 7248 81 547 -639 C ATOM 1136 O ALA A 197 10.492 5.609 -53.784 1.00 50.31 O ANISOU 1136 O ALA A 197 5923 5884 7310 101 610 -715 O ATOM 1137 CB ALA A 197 9.772 4.412 -51.005 1.00 47.45 C ANISOU 1137 CB ALA A 197 5586 5379 7064 46 478 -593 C ATOM 1138 N ILE A 198 9.494 7.292 -52.676 1.00 42.68 N ANISOU 1138 N ILE A 198 4859 5047 6309 54 512 -599 N ATOM 1139 CA ILE A 198 9.100 8.026 -53.865 1.00 48.64 C ANISOU 1139 CA ILE A 198 5654 5883 6942 66 540 -611 C ATOM 1140 C ILE A 198 9.753 9.403 -53.914 1.00 52.39 C ANISOU 1140 C ILE A 198 6160 6345 7401 97 594 -552 C ATOM 1141 O ILE A 198 10.140 9.870 -54.987 1.00 47.98 O ANISOU 1141 O ILE A 198 5664 5800 6768 101 666 -555 O ATOM 1142 CB ILE A 198 7.559 8.133 -53.957 1.00 50.56 C ANISOU 1142 CB ILE A 198 5878 6274 7060 52 462 -603 C ATOM 1143 CG1 ILE A 198 6.950 6.744 -54.182 1.00 54.38 C ANISOU 1143 CG1 ILE A 198 6367 6781 7515 -82 430 -689 C ATOM 1144 CG2 ILE A 198 7.135 9.114 -55.039 1.00 48.54 C ANISOU 1144 CG2 ILE A 198 5662 6133 6646 141 476 -572 C ATOM 1145 CD1 ILE A 198 5.446 6.751 -54.290 1.00 56.06 C ANISOU 1145 CD1 ILE A 198 6488 7245 7568 -156 351 -696 C ATOM 1146 N GLY A 199 9.923 10.051 -52.755 1.00 44.98 N ANISOU 1146 N GLY A 199 5209 5371 6512 85 573 -504 N ATOM 1147 CA GLY A 199 10.474 11.397 -52.744 1.00 43.62 C ANISOU 1147 CA GLY A 199 5137 5143 6294 50 636 -465 C ATOM 1148 C GLY A 199 11.904 11.476 -53.244 1.00 47.58 C ANISOU 1148 C GLY A 199 5599 5657 6821 -55 730 -489 C ATOM 1149 O GLY A 199 12.292 12.467 -53.866 1.00 53.22 O ANISOU 1149 O GLY A 199 6441 6333 7448 -130 817 -464 O ATOM 1150 N LEU A 200 12.712 10.452 -52.968 1.00 46.67 N ANISOU 1150 N LEU A 200 5317 5613 6802 -53 724 -529 N ATOM 1151 CA LEU A 200 14.099 10.437 -53.423 1.00 52.06 C ANISOU 1151 CA LEU A 200 5886 6406 7487 -116 817 -555 C ATOM 1152 C LEU A 200 14.217 10.048 -54.896 1.00 51.35 C ANISOU 1152 C LEU A 200 5830 6345 7336 -64 904 -595 C ATOM 1153 O LEU A 200 14.953 10.714 -55.637 1.00 42.98 O ANISOU 1153 O LEU A 200 4776 5359 6196 -168 1013 -592 O ATOM 1154 CB LEU A 200 14.943 9.496 -52.557 1.00 57.90 C ANISOU 1154 CB LEU A 200 6420 7260 8321 -47 780 -567 C ATOM 1155 CG LEU A 200 15.347 10.002 -51.175 1.00 62.45 C ANISOU 1155 CG LEU A 200 6901 7912 8916 -148 716 -536 C ATOM 1156 CD1 LEU A 200 16.181 8.959 -50.451 1.00 66.58 C ANISOU 1156 CD1 LEU A 200 7208 8593 9496 -9 672 -523 C ATOM 1157 CD2 LEU A 200 16.107 11.312 -51.293 1.00 66.77 C ANISOU 1157 CD2 LEU A 200 7451 8545 9375 -396 792 -546 C ATOM 1158 N PRO A 201 13.545 8.983 -55.367 1.00 42.72 N ANISOU 1158 N PRO A 201 4777 5204 6252 57 872 -642 N ATOM 1159 CA PRO A 201 13.636 8.668 -56.805 1.00 45.63 C ANISOU 1159 CA PRO A 201 5204 5607 6525 88 959 -701 C ATOM 1160 C PRO A 201 13.171 9.792 -57.717 1.00 49.30 C ANISOU 1160 C PRO A 201 5808 6081 6845 19 996 -651 C ATOM 1161 O PRO A 201 13.757 9.980 -58.791 1.00 53.76 O ANISOU 1161 O PRO A 201 6395 6720 7313 -9 1107 -669 O ATOM 1162 CB PRO A 201 12.751 7.423 -56.945 1.00 43.87 C ANISOU 1162 CB PRO A 201 5057 5301 6312 162 896 -772 C ATOM 1163 CG PRO A 201 12.821 6.777 -55.620 1.00 46.80 C ANISOU 1163 CG PRO A 201 5369 5601 6812 205 827 -750 C ATOM 1164 CD PRO A 201 12.840 7.910 -54.636 1.00 42.90 C ANISOU 1164 CD PRO A 201 4806 5144 6349 132 777 -659 C ATOM 1165 N VAL A 202 12.136 10.547 -57.334 1.00 41.26 N ANISOU 1165 N VAL A 202 4894 5000 5784 23 916 -580 N ATOM 1166 CA VAL A 202 11.673 11.613 -58.220 1.00 46.30 C ANISOU 1166 CA VAL A 202 5709 5631 6253 33 955 -505 C ATOM 1167 C VAL A 202 12.703 12.729 -58.304 1.00 50.30 C ANISOU 1167 C VAL A 202 6309 6083 6719 -108 1080 -446 C ATOM 1168 O VAL A 202 12.744 13.466 -59.294 1.00 51.45 O ANISOU 1168 O VAL A 202 6627 6212 6708 -132 1166 -384 O ATOM 1169 CB VAL A 202 10.297 12.157 -57.787 1.00 40.72 C ANISOU 1169 CB VAL A 202 5089 4902 5481 151 851 -435 C ATOM 1170 CG1 VAL A 202 9.244 11.057 -57.841 1.00 36.87 C ANISOU 1170 CG1 VAL A 202 4483 4541 4984 208 738 -501 C ATOM 1171 CG2 VAL A 202 10.368 12.796 -56.410 1.00 44.68 C ANISOU 1171 CG2 VAL A 202 5613 5289 6072 127 828 -396 C ATOM 1172 N MET A 203 13.552 12.875 -57.284 1.00 50.01 N ANISOU 1172 N MET A 203 6170 6037 6793 -233 1095 -462 N ATOM 1173 CA MET A 203 14.636 13.849 -57.369 1.00 56.63 C ANISOU 1173 CA MET A 203 7071 6877 7570 -464 1223 -433 C ATOM 1174 C MET A 203 15.615 13.485 -58.477 1.00 53.71 C ANISOU 1174 C MET A 203 6585 6687 7137 -536 1352 -471 C ATOM 1175 O MET A 203 16.162 14.369 -59.148 1.00 52.82 O ANISOU 1175 O MET A 203 6608 6575 6888 -723 1487 -422 O ATOM 1176 CB MET A 203 15.351 13.956 -56.024 1.00 64.51 C ANISOU 1176 CB MET A 203 7922 7918 8670 -610 1192 -464 C ATOM 1177 CG MET A 203 16.660 14.719 -56.066 1.00 79.41 C ANISOU 1177 CG MET A 203 9775 9916 10482 -930 1322 -472 C ATOM 1178 SD MET A 203 16.906 15.735 -54.602 1.00 93.94 S ANISOU 1178 SD MET A 203 11718 11660 12316 -1191 1292 -480 S ATOM 1179 CE MET A 203 15.716 17.039 -54.903 1.00 88.64 C ANISOU 1179 CE MET A 203 11592 10573 11515 -1137 1334 -389 C ATOM 1180 N PHE A 204 15.836 12.187 -58.698 1.00 50.90 N ANISOU 1180 N PHE A 204 6012 6471 6856 -388 1331 -558 N ATOM 1181 CA PHE A 204 16.662 11.753 -59.819 1.00 49.90 C ANISOU 1181 CA PHE A 204 5786 6526 6648 -390 1465 -611 C ATOM 1182 C PHE A 204 15.880 11.759 -61.125 1.00 49.62 C ANISOU 1182 C PHE A 204 5952 6439 6464 -309 1489 -600 C ATOM 1183 O PHE A 204 16.419 12.136 -62.172 1.00 52.96 O ANISOU 1183 O PHE A 204 6423 6963 6737 -399 1629 -586 O ATOM 1184 CB PHE A 204 17.229 10.359 -59.547 1.00 58.38 C ANISOU 1184 CB PHE A 204 6611 7736 7834 -207 1453 -714 C ATOM 1185 CG PHE A 204 18.332 10.342 -58.530 1.00 61.45 C ANISOU 1185 CG PHE A 204 6731 8313 8302 -264 1460 -715 C ATOM 1186 CD1 PHE A 204 19.652 10.472 -58.924 1.00 66.61 C ANISOU 1186 CD1 PHE A 204 7152 9281 8876 -358 1604 -740 C ATOM 1187 CD2 PHE A 204 18.051 10.197 -57.181 1.00 63.92 C ANISOU 1187 CD2 PHE A 204 6995 8551 8741 -231 1322 -691 C ATOM 1188 CE1 PHE A 204 20.673 10.460 -57.994 1.00 72.05 C ANISOU 1188 CE1 PHE A 204 7535 10243 9600 -415 1595 -741 C ATOM 1189 CE2 PHE A 204 19.069 10.183 -56.244 1.00 64.58 C ANISOU 1189 CE2 PHE A 204 6810 8865 8862 -281 1311 -688 C ATOM 1190 CZ PHE A 204 20.382 10.315 -56.653 1.00 66.27 C ANISOU 1190 CZ PHE A 204 6764 9430 8986 -372 1440 -714 C ATOM 1191 N MET A 205 14.609 11.351 -61.084 1.00 41.16 N ANISOU 1191 N MET A 205 4979 5257 5403 -159 1355 -607 N ATOM 1192 CA MET A 205 13.825 11.236 -62.310 1.00 48.71 C ANISOU 1192 CA MET A 205 6077 6244 6188 -82 1351 -612 C ATOM 1193 C MET A 205 13.426 12.595 -62.871 1.00 49.31 C ANISOU 1193 C MET A 205 6393 6262 6081 -121 1387 -462 C ATOM 1194 O MET A 205 13.302 12.745 -64.092 1.00 50.17 O ANISOU 1194 O MET A 205 6614 6452 5994 -102 1447 -438 O ATOM 1195 CB MET A 205 12.575 10.398 -62.055 1.00 44.99 C ANISOU 1195 CB MET A 205 5600 5747 5749 36 1192 -670 C ATOM 1196 CG MET A 205 12.845 8.930 -61.781 1.00 58.86 C ANISOU 1196 CG MET A 205 7240 7497 7627 82 1180 -818 C ATOM 1197 SD MET A 205 11.516 8.188 -60.815 1.00 63.02 S ANISOU 1197 SD MET A 205 7761 7944 8241 104 999 -848 S ATOM 1198 CE MET A 205 10.095 9.045 -61.486 1.00 68.95 C ANISOU 1198 CE MET A 205 8599 8825 8775 117 903 -765 C ATOM 1199 N ALA A 206 13.203 13.583 -62.009 1.00 39.97 N ANISOU 1199 N ALA A 206 5330 4924 4934 -155 1357 -359 N ATOM 1200 CA ALA A 206 12.709 14.871 -62.474 1.00 46.95 C ANISOU 1200 CA ALA A 206 6529 5683 5628 -125 1396 -201 C ATOM 1201 C ALA A 206 13.765 15.586 -63.303 1.00 51.63 C ANISOU 1201 C ALA A 206 7269 6267 6081 -336 1590 -142 C ATOM 1202 O ALA A 206 14.952 15.582 -62.969 1.00 55.63 O ANISOU 1202 O ALA A 206 7642 6826 6667 -572 1696 -196 O ATOM 1203 CB ALA A 206 12.291 15.750 -61.296 1.00 37.78 C ANISOU 1203 CB ALA A 206 5518 4309 4527 -100 1347 -126 C ATOM 1204 N THR A 207 13.322 16.197 -64.396 1.00 53.48 N ANISOU 1204 N THR A 207 7763 6481 6077 -255 1639 -21 N ATOM 1205 CA THR A 207 14.208 16.977 -65.245 1.00 54.00 C ANISOU 1205 CA THR A 207 8036 6519 5963 -474 1839 67 C ATOM 1206 C THR A 207 13.359 17.872 -66.130 1.00 52.23 C ANISOU 1206 C THR A 207 8203 6178 5464 -292 1850 260 C ATOM 1207 O THR A 207 12.152 17.666 -66.279 1.00 55.37 O ANISOU 1207 O THR A 207 8606 6635 5796 23 1693 295 O ATOM 1208 CB THR A 207 15.115 16.081 -66.099 1.00 60.06 C ANISOU 1208 CB THR A 207 8543 7570 6707 -586 1942 -55 C ATOM 1209 OG1 THR A 207 16.126 16.880 -66.724 1.00 69.31 O ANISOU 1209 OG1 THR A 207 9867 8754 7715 -874 2160 25 O ATOM 1210 CG2 THR A 207 14.308 15.373 -67.175 1.00 51.07 C ANISOU 1210 CG2 THR A 207 7388 6595 5424 -355 1866 -88 C ATOM 1211 N THR A 208 14.006 18.878 -66.704 1.00 60.05 N ANISOU 1211 N THR A 208 9521 7026 6267 -498 2039 394 N ATOM 1212 CA THR A 208 13.395 19.723 -67.718 1.00 61.26 C ANISOU 1212 CA THR A 208 10094 7073 6111 -325 2086 607 C ATOM 1213 C THR A 208 13.792 19.207 -69.094 1.00 63.88 C ANISOU 1213 C THR A 208 10323 7691 6258 -384 2169 588 C ATOM 1214 O THR A 208 14.971 18.932 -69.343 1.00 78.15 O ANISOU 1214 O THR A 208 11966 9633 8095 -703 2327 496 O ATOM 1215 CB THR A 208 13.828 21.180 -67.559 1.00 61.63 C ANISOU 1215 CB THR A 208 10670 6726 6020 -531 2268 785 C ATOM 1216 OG1 THR A 208 15.260 21.255 -67.580 1.00 58.74 O ANISOU 1216 OG1 THR A 208 10219 6414 5687 -1034 2465 710 O ATOM 1217 CG2 THR A 208 13.307 21.756 -66.247 1.00 54.71 C ANISOU 1217 CG2 THR A 208 9969 5538 5279 -421 2191 797 C ATOM 1218 N LYS A 209 12.807 19.062 -69.975 1.00 61.86 N ANISOU 1218 N LYS A 209 10138 7579 5788 -69 2063 668 N ATOM 1219 CA LYS A 209 13.060 18.699 -71.360 1.00 74.00 C ANISOU 1219 CA LYS A 209 11653 9380 7084 -102 2141 668 C ATOM 1220 C LYS A 209 12.163 19.536 -72.258 1.00 80.79 C ANISOU 1220 C LYS A 209 12907 10204 7583 183 2112 924 C ATOM 1221 O LYS A 209 11.102 20.007 -71.838 1.00 76.57 O ANISOU 1221 O LYS A 209 12522 9561 7009 514 1968 1048 O ATOM 1222 CB LYS A 209 12.824 17.204 -71.615 1.00 76.15 C ANISOU 1222 CB LYS A 209 11486 9998 7449 -23 2011 421 C ATOM 1223 CG LYS A 209 11.414 16.735 -71.312 1.00 78.90 C ANISOU 1223 CG LYS A 209 11707 10458 7813 293 1752 388 C ATOM 1224 CD LYS A 209 11.107 15.431 -72.025 1.00 80.46 C ANISOU 1224 CD LYS A 209 11628 10997 7947 317 1659 178 C ATOM 1225 CE LYS A 209 11.183 15.610 -73.532 1.00 92.30 C ANISOU 1225 CE LYS A 209 13291 12702 9076 327 1744 253 C ATOM 1226 NZ LYS A 209 10.842 14.360 -74.266 1.00 96.81 N ANISOU 1226 NZ LYS A 209 13642 13599 9543 327 1657 23 N ATOM 1227 N TYR A 210 12.600 19.719 -73.500 1.00 83.61 N ANISOU 1227 N TYR A 210 13427 10687 7655 84 2255 1012 N ATOM 1228 CA TYR A 210 11.867 20.557 -74.436 1.00 91.20 C ANISOU 1228 CA TYR A 210 14802 11626 8226 359 2247 1289 C ATOM 1229 C TYR A 210 10.630 19.841 -74.959 1.00 92.18 C ANISOU 1229 C TYR A 210 14687 12140 8198 735 1994 1245 C ATOM 1230 O TYR A 210 10.657 18.639 -75.240 1.00 92.79 O ANISOU 1230 O TYR A 210 14362 12548 8344 652 1915 996 O ATOM 1231 CB TYR A 210 12.765 20.977 -75.598 1.00 96.10 C ANISOU 1231 CB TYR A 210 15680 12276 8560 97 2492 1406 C ATOM 1232 CG TYR A 210 13.582 22.209 -75.294 1.00106.77 C ANISOU 1232 CG TYR A 210 17502 13190 9876 -206 2739 1592 C ATOM 1233 CD1 TYR A 210 12.993 23.467 -75.287 1.00114.30 C ANISOU 1233 CD1 TYR A 210 19063 13755 10612 21 2768 1900 C ATOM 1234 CD2 TYR A 210 14.938 22.118 -75.009 1.00109.50 C ANISOU 1234 CD2 TYR A 210 17703 13524 10380 -721 2950 1456 C ATOM 1235 CE1 TYR A 210 13.730 24.599 -75.006 1.00120.46 C ANISOU 1235 CE1 TYR A 210 20359 14075 11337 -312 3012 2055 C ATOM 1236 CE2 TYR A 210 15.685 23.247 -74.727 1.00115.42 C ANISOU 1236 CE2 TYR A 210 18886 13902 11066 -1090 3180 1607 C ATOM 1237 CZ TYR A 210 15.075 24.485 -74.727 1.00122.00 C ANISOU 1237 CZ TYR A 210 20387 14282 11686 -911 3215 1900 C ATOM 1238 OH TYR A 210 15.812 25.613 -74.448 1.00128.00 O ANISOU 1238 OH TYR A 210 21492 14656 12487 -1287 3351 1961 O ATOM 1239 N ARG A 211 9.539 20.597 -75.087 1.00 90.65 N ANISOU 1239 N ARG A 211 14757 11916 7768 1152 1874 1487 N ATOM 1240 CA ARG A 211 8.251 20.057 -75.525 1.00 95.11 C ANISOU 1240 CA ARG A 211 15071 12928 8137 1519 1615 1472 C ATOM 1241 C ARG A 211 7.568 21.141 -76.362 1.00104.28 C ANISOU 1241 C ARG A 211 16671 14105 8847 1926 1605 1831 C ATOM 1242 O ARG A 211 6.895 22.023 -75.824 1.00109.68 O ANISOU 1242 O ARG A 211 17621 14576 9477 2297 1559 2044 O ATOM 1243 CB ARG A 211 7.397 19.636 -74.338 1.00101.43 C ANISOU 1243 CB ARG A 211 15554 13785 9200 1695 1408 1346 C ATOM 1244 CG ARG A 211 6.046 19.060 -74.718 1.00107.03 C ANISOU 1244 CG ARG A 211 15943 15030 9692 2007 1138 1313 C ATOM 1245 CD ARG A 211 6.198 17.725 -75.419 1.00113.27 C ANISOU 1245 CD ARG A 211 16368 16212 10458 1724 1077 1028 C ATOM 1246 NE ARG A 211 4.974 17.335 -76.111 1.00120.37 N ANISOU 1246 NE ARG A 211 17038 17680 11018 1958 842 1026 N ATOM 1247 CZ ARG A 211 4.824 16.193 -76.772 1.00120.52 C ANISOU 1247 CZ ARG A 211 16768 18094 10931 1738 751 772 C ATOM 1248 NH1 ARG A 211 5.821 15.321 -76.826 1.00117.65 N ANISOU 1248 NH1 ARG A 211 16334 17580 10786 1348 889 510 N ATOM 1249 NH2 ARG A 211 3.676 15.920 -77.376 1.00122.28 N ANISOU 1249 NH2 ARG A 211 16775 18881 10804 1915 527 774 N ATOM 1250 N GLN A 212 7.759 21.061 -77.682 1.00100.09 N ANISOU 1250 N GLN A 212 18049 10484 9495 -1278 400 2296 N ATOM 1251 CA GLN A 212 7.173 22.008 -78.633 1.00100.97 C ANISOU 1251 CA GLN A 212 18411 10464 9491 -1096 345 2538 C ATOM 1252 C GLN A 212 7.605 23.441 -78.321 1.00106.86 C ANISOU 1252 C GLN A 212 19369 10829 10404 -1256 440 2678 C ATOM 1253 O GLN A 212 6.787 24.360 -78.237 1.00103.67 O ANISOU 1253 O GLN A 212 19169 10144 10077 -1064 329 2777 O ATOM 1254 CB GLN A 212 5.647 21.891 -78.659 1.00101.41 C ANISOU 1254 CB GLN A 212 18528 10487 9516 -693 94 2511 C ATOM 1255 CG GLN A 212 5.132 20.468 -78.789 1.00103.31 C ANISOU 1255 CG GLN A 212 18540 11073 9642 -524 -18 2331 C ATOM 1256 CD GLN A 212 3.618 20.401 -78.829 1.00105.89 C ANISOU 1256 CD GLN A 212 18906 11364 9963 -122 -271 2292 C ATOM 1257 OE1 GLN A 212 2.979 21.033 -79.669 1.00111.06 O ANISOU 1257 OE1 GLN A 212 19720 11974 10506 80 -371 2463 O ATOM 1258 NE2 GLN A 212 3.035 19.636 -77.912 1.00102.10 N ANISOU 1258 NE2 GLN A 212 18269 10912 9613 0 -378 2069 N ATOM 1259 N GLY A 213 8.906 23.627 -78.149 1.00112.07 N ANISOU 1259 N GLY A 213 19961 11480 11139 -1607 646 2674 N ATOM 1260 CA GLY A 213 9.430 24.938 -77.765 1.00119.50 C ANISOU 1260 CA GLY A 213 21068 12064 12274 -1795 749 2769 C ATOM 1261 C GLY A 213 9.297 25.261 -76.294 1.00120.52 C ANISOU 1261 C GLY A 213 21185 11938 12670 -1848 690 2560 C ATOM 1262 O GLY A 213 10.246 25.756 -75.679 1.00126.75 O ANISOU 1262 O GLY A 213 21940 12588 13630 -2139 819 2496 O ATOM 1263 N SER A 214 8.131 24.992 -75.709 1.00113.95 N ANISOU 1263 N SER A 214 20368 11051 11876 -1568 497 2440 N ATOM 1264 CA SER A 214 7.926 25.199 -74.285 1.00101.89 C ANISOU 1264 CA SER A 214 18818 9319 10576 -1593 439 2223 C ATOM 1265 C SER A 214 8.679 24.139 -73.481 1.00 93.27 C ANISOU 1265 C SER A 214 17458 8465 9516 -1808 492 1997 C ATOM 1266 O SER A 214 9.149 23.129 -74.011 1.00 91.08 O ANISOU 1266 O SER A 214 16998 8513 9097 -1878 546 1992 O ATOM 1267 CB SER A 214 6.435 25.169 -73.952 1.00103.78 C ANISOU 1267 CB SER A 214 19133 9455 10843 -1213 229 2163 C ATOM 1268 OG SER A 214 5.847 23.950 -74.365 1.00110.89 O ANISOU 1268 OG SER A 214 19889 10669 11574 -1011 124 2118 O ATOM 1269 N ILE A 215 8.788 24.378 -72.177 1.00 86.52 N ANISOU 1269 N ILE A 215 16569 7452 8854 -1909 474 1804 N ATOM 1270 CA ILE A 215 9.570 23.536 -71.280 1.00 74.91 C ANISOU 1270 CA ILE A 215 14847 6175 7439 -2135 519 1598 C ATOM 1271 C ILE A 215 8.628 22.844 -70.305 1.00 73.44 C ANISOU 1271 C ILE A 215 14590 6020 7292 -1928 368 1420 C ATOM 1272 O ILE A 215 7.796 23.495 -69.659 1.00 68.89 O ANISOU 1272 O ILE A 215 14157 5192 6825 -1758 275 1355 O ATOM 1273 CB ILE A 215 10.636 24.349 -70.527 1.00 74.06 C ANISOU 1273 CB ILE A 215 14726 5902 7513 -2462 629 1508 C ATOM 1274 CG1 ILE A 215 11.606 24.994 -71.518 1.00 74.93 C ANISOU 1274 CG1 ILE A 215 14887 5982 7602 -2673 797 1693 C ATOM 1275 CG2 ILE A 215 11.377 23.467 -69.533 1.00 70.75 C ANISOU 1275 CG2 ILE A 215 14029 5702 7149 -2669 642 1287 C ATOM 1276 CD1 ILE A 215 12.652 25.870 -70.865 1.00 73.96 C ANISOU 1276 CD1 ILE A 215 14744 5679 7678 -2989 906 1610 C ATOM 1277 N ASP A 216 8.767 21.528 -70.196 1.00 63.22 N ANISOU 1277 N ASP A 216 13062 5034 5923 -1939 357 1339 N ATOM 1278 CA ASP A 216 7.994 20.717 -69.267 1.00 60.23 C ANISOU 1278 CA ASP A 216 12581 4718 5585 -1771 239 1184 C ATOM 1279 C ASP A 216 8.923 20.226 -68.166 1.00 67.54 C ANISOU 1279 C ASP A 216 13257 5788 6619 -2035 289 997 C ATOM 1280 O ASP A 216 9.946 19.593 -68.451 1.00 71.64 O ANISOU 1280 O ASP A 216 13570 6549 7101 -2257 386 1002 O ATOM 1281 CB ASP A 216 7.341 19.536 -69.989 1.00 67.22 C ANISOU 1281 CB ASP A 216 13291 5907 6342 -1520 166 1203 C ATOM 1282 CG ASP A 216 6.422 18.728 -69.088 1.00 79.44 C ANISOU 1282 CG ASP A 216 14596 7589 7999 -1269 39 995 C ATOM 1283 OD1 ASP A 216 6.093 19.201 -67.980 1.00 87.02 O ANISOU 1283 OD1 ASP A 216 15599 8374 9093 -1243 -2 868 O ATOM 1284 OD2 ASP A 216 6.026 17.615 -69.492 1.00 86.62 O ANISOU 1284 OD2 ASP A 216 15269 8780 8864 -1104 -9 950 O ATOM 1285 N CYS A 217 8.579 20.534 -66.917 1.00 67.20 N ANISOU 1285 N CYS A 217 13206 5620 6706 -1997 221 817 N ATOM 1286 CA CYS A 217 9.239 19.928 -65.763 1.00 53.84 C ANISOU 1286 CA CYS A 217 11229 4135 5095 -2160 221 615 C ATOM 1287 C CYS A 217 8.536 18.603 -65.500 1.00 58.60 C ANISOU 1287 C CYS A 217 11536 5045 5684 -1903 135 529 C ATOM 1288 O CYS A 217 7.434 18.567 -64.949 1.00 64.11 O ANISOU 1288 O CYS A 217 12250 5687 6422 -1639 43 442 O ATOM 1289 CB CYS A 217 9.187 20.861 -64.557 1.00 53.94 C ANISOU 1289 CB CYS A 217 11376 3896 5221 -2238 191 453 C ATOM 1290 SG CYS A 217 9.663 20.130 -62.958 1.00 63.09 S ANISOU 1290 SG CYS A 217 12210 5329 6434 -2344 139 191 S ATOM 1291 N THR A 218 9.162 17.507 -65.919 1.00 59.73 N ANISOU 1291 N THR A 218 11401 5502 5790 -1978 176 548 N ATOM 1292 CA THR A 218 8.511 16.207 -65.947 1.00 58.65 C ANISOU 1292 CA THR A 218 10991 5635 5659 -1737 114 497 C ATOM 1293 C THR A 218 9.435 15.157 -65.340 1.00 53.89 C ANISOU 1293 C THR A 218 10032 5326 5118 -1897 143 407 C ATOM 1294 O THR A 218 10.508 15.466 -64.813 1.00 56.41 O ANISOU 1294 O THR A 218 10312 5651 5470 -2174 189 367 O ATOM 1295 CB THR A 218 8.112 15.827 -67.382 1.00 60.96 C ANISOU 1295 CB THR A 218 11311 6009 5843 -1587 122 626 C ATOM 1296 OG1 THR A 218 7.373 14.600 -67.372 1.00 66.56 O ANISOU 1296 OG1 THR A 218 11752 6946 6592 -1344 54 545 O ATOM 1297 CG2 THR A 218 9.347 15.666 -68.260 1.00 52.90 C ANISOU 1297 CG2 THR A 218 10236 5120 4744 -1853 251 721 C ATOM 1298 N LEU A 219 9.000 13.904 -65.412 1.00 48.31 N ANISOU 1298 N LEU A 219 9054 4854 4446 -1713 109 370 N ATOM 1299 CA LEU A 219 9.744 12.764 -64.896 1.00 49.86 C ANISOU 1299 CA LEU A 219 8895 5325 4725 -1807 125 306 C ATOM 1300 C LEU A 219 10.194 11.880 -66.051 1.00 53.06 C ANISOU 1300 C LEU A 219 9114 5930 5116 -1826 192 356 C ATOM 1301 O LEU A 219 9.433 11.641 -66.994 1.00 52.12 O ANISOU 1301 O LEU A 219 9043 5818 4941 -1634 179 393 O ATOM 1302 CB LEU A 219 8.887 11.949 -63.924 1.00 46.61 C ANISOU 1302 CB LEU A 219 8298 5010 4402 -1582 48 218 C ATOM 1303 CG LEU A 219 8.347 12.685 -62.695 1.00 50.60 C ANISOU 1303 CG LEU A 219 8955 5362 4908 -1534 -8 139 C ATOM 1304 CD1 LEU A 219 7.312 11.838 -61.968 1.00 47.08 C ANISOU 1304 CD1 LEU A 219 8338 5015 4534 -1278 -54 79 C ATOM 1305 CD2 LEU A 219 9.478 13.065 -61.760 1.00 50.44 C ANISOU 1305 CD2 LEU A 219 8906 5376 4882 -1809 -1 83 C ATOM 1306 N THR A 220 11.432 11.401 -65.976 1.00 47.93 N ANISOU 1306 N THR A 220 8243 5451 4518 -2054 258 340 N ATOM 1307 CA THR A 220 11.973 10.459 -66.947 1.00 54.51 C ANISOU 1307 CA THR A 220 8850 6498 5364 -2083 337 351 C ATOM 1308 C THR A 220 12.137 9.101 -66.280 1.00 50.06 C ANISOU 1308 C THR A 220 7902 6152 4966 -2011 302 270 C ATOM 1309 O THR A 220 12.628 9.014 -65.150 1.00 53.32 O ANISOU 1309 O THR A 220 8196 6605 5459 -2104 262 235 O ATOM 1310 CB THR A 220 13.311 10.945 -67.508 1.00 64.09 C ANISOU 1310 CB THR A 220 10087 7735 6531 -2401 464 399 C ATOM 1311 OG1 THR A 220 14.201 11.261 -66.431 1.00 76.32 O ANISOU 1311 OG1 THR A 220 11556 9278 8166 -2622 451 349 O ATOM 1312 CG2 THR A 220 13.103 12.179 -68.374 1.00 68.94 C ANISOU 1312 CG2 THR A 220 11083 8131 6980 -2456 521 519 C ATOM 1313 N PHE A 221 11.726 8.049 -66.978 1.00 46.79 N ANISOU 1313 N PHE A 221 7299 5875 4605 -1842 314 240 N ATOM 1314 CA PHE A 221 11.647 6.718 -66.403 1.00 48.89 C ANISOU 1314 CA PHE A 221 7217 6299 5059 -1724 283 176 C ATOM 1315 C PHE A 221 12.604 5.770 -67.112 1.00 53.99 C ANISOU 1315 C PHE A 221 7571 7144 5798 -1820 373 137 C ATOM 1316 O PHE A 221 13.079 6.039 -68.218 1.00 48.36 O ANISOU 1316 O PHE A 221 6927 6469 4977 -1929 467 145 O ATOM 1317 CB PHE A 221 10.217 6.174 -66.483 1.00 45.77 C ANISOU 1317 CB PHE A 221 6805 5870 4715 -1420 217 139 C ATOM 1318 CG PHE A 221 9.217 7.005 -65.736 1.00 52.56 C ANISOU 1318 CG PHE A 221 7910 6546 5515 -1299 137 156 C ATOM 1319 CD1 PHE A 221 8.915 6.725 -64.413 1.00 47.57 C ANISOU 1319 CD1 PHE A 221 7183 5914 4978 -1236 89 142 C ATOM 1320 CD2 PHE A 221 8.586 8.074 -66.351 1.00 49.89 C ANISOU 1320 CD2 PHE A 221 7898 6036 5021 -1242 115 192 C ATOM 1321 CE1 PHE A 221 7.996 7.490 -63.722 1.00 54.42 C ANISOU 1321 CE1 PHE A 221 8266 6622 5788 -1124 34 134 C ATOM 1322 CE2 PHE A 221 7.669 8.844 -65.664 1.00 49.18 C ANISOU 1322 CE2 PHE A 221 8020 5765 4902 -1119 46 190 C ATOM 1323 CZ PHE A 221 7.374 8.552 -64.347 1.00 45.75 C ANISOU 1323 CZ PHE A 221 7477 5340 4564 -1064 13 146 C ATOM 1324 N SER A 222 12.882 4.650 -66.451 1.00 54.95 N ANISOU 1324 N SER A 222 7364 7391 6122 -1775 353 100 N ATOM 1325 CA SER A 222 13.674 3.595 -67.057 1.00 57.52 C ANISOU 1325 CA SER A 222 7371 7893 6590 -1819 433 41 C ATOM 1326 C SER A 222 12.869 2.895 -68.150 1.00 50.96 C ANISOU 1326 C SER A 222 6483 7101 5778 -1625 463 -40 C ATOM 1327 O SER A 222 11.653 3.067 -68.276 1.00 47.72 O ANISOU 1327 O SER A 222 6229 6594 5308 -1434 399 -46 O ATOM 1328 CB SER A 222 14.119 2.584 -66.000 1.00 59.56 C ANISOU 1328 CB SER A 222 7300 8246 7082 -1794 388 43 C ATOM 1329 OG SER A 222 14.819 3.217 -64.942 1.00 65.98 O ANISOU 1329 OG SER A 222 8160 9053 7857 -1959 333 101 O ATOM 1330 N HIS A 223 13.563 2.092 -68.941 1.00 51.15 N ANISOU 1330 N HIS A 223 6265 7277 5894 -1674 557 -124 N ATOM 1331 CA HIS A 223 12.876 1.338 -69.979 1.00 54.24 C ANISOU 1331 CA HIS A 223 6567 7731 6313 -1499 582 -241 C ATOM 1332 C HIS A 223 12.220 0.096 -69.377 1.00 48.11 C ANISOU 1332 C HIS A 223 5510 6947 5823 -1294 524 -304 C ATOM 1333 O HIS A 223 12.795 -0.541 -68.491 1.00 54.20 O ANISOU 1333 O HIS A 223 6043 7743 6808 -1327 518 -271 O ATOM 1334 CB HIS A 223 13.852 0.927 -71.081 1.00 60.35 C ANISOU 1334 CB HIS A 223 7181 8675 7075 -1626 723 -337 C ATOM 1335 CG HIS A 223 14.639 2.068 -71.646 1.00 76.95 C ANISOU 1335 CG HIS A 223 9523 10791 8922 -1860 816 -260 C ATOM 1336 ND1 HIS A 223 14.063 3.070 -72.397 1.00 81.43 N ANISOU 1336 ND1 HIS A 223 10451 11289 9199 -1848 816 -193 N ATOM 1337 CD2 HIS A 223 15.958 2.363 -71.574 1.00 82.30 C ANISOU 1337 CD2 HIS A 223 10125 11537 9609 -2114 919 -231 C ATOM 1338 CE1 HIS A 223 14.993 3.934 -72.761 1.00 85.70 C ANISOU 1338 CE1 HIS A 223 11141 11840 9581 -2093 929 -112 C ATOM 1339 NE2 HIS A 223 16.152 3.529 -72.275 1.00 85.52 N ANISOU 1339 NE2 HIS A 223 10850 11903 9740 -2266 997 -145 N ATOM 1340 N PRO A 224 11.003 -0.257 -69.819 1.00 47.34 N ANISOU 1340 N PRO A 224 5432 6809 5744 -1079 476 -385 N ATOM 1341 CA PRO A 224 10.189 0.546 -70.738 1.00 45.22 C ANISOU 1341 CA PRO A 224 5460 6507 5214 -1004 442 -403 C ATOM 1342 C PRO A 224 9.408 1.622 -69.990 1.00 44.62 C ANISOU 1342 C PRO A 224 5688 6257 5007 -950 345 -279 C ATOM 1343 O PRO A 224 8.883 1.352 -68.908 1.00 41.02 O ANISOU 1343 O PRO A 224 5158 5719 4707 -856 288 -248 O ATOM 1344 CB PRO A 224 9.252 -0.485 -71.359 1.00 46.82 C ANISOU 1344 CB PRO A 224 5470 6755 5563 -786 414 -574 C ATOM 1345 CG PRO A 224 9.065 -1.497 -70.280 1.00 46.77 C ANISOU 1345 CG PRO A 224 5179 6694 5898 -703 398 -578 C ATOM 1346 CD PRO A 224 10.376 -1.558 -69.526 1.00 46.51 C ANISOU 1346 CD PRO A 224 5029 6697 5945 -895 455 -476 C ATOM 1347 N THR A 225 9.337 2.825 -70.565 1.00 44.25 N ANISOU 1347 N THR A 225 5980 6152 4682 -1008 337 -206 N ATOM 1348 CA THR A 225 8.732 3.950 -69.858 1.00 45.39 C ANISOU 1348 CA THR A 225 6424 6109 4714 -977 257 -96 C ATOM 1349 C THR A 225 7.260 3.696 -69.559 1.00 38.94 C ANISOU 1349 C THR A 225 5601 5208 3986 -707 151 -150 C ATOM 1350 O THR A 225 6.763 4.085 -68.497 1.00 42.54 O ANISOU 1350 O THR A 225 6138 5537 4489 -655 100 -100 O ATOM 1351 CB THR A 225 8.897 5.236 -70.669 1.00 43.86 C ANISOU 1351 CB THR A 225 6590 5844 4232 -1072 275 1 C ATOM 1352 OG1 THR A 225 8.337 5.050 -71.974 1.00 48.48 O ANISOU 1352 OG1 THR A 225 7221 6515 4684 -937 260 -57 O ATOM 1353 CG2 THR A 225 10.368 5.597 -70.800 1.00 47.12 C ANISOU 1353 CG2 THR A 225 7010 6314 4579 -1370 398 62 C ATOM 1354 N TRP A 226 6.548 3.032 -70.475 1.00 38.02 N ANISOU 1354 N TRP A 226 5374 5172 3900 -536 122 -269 N ATOM 1355 CA TRP A 226 5.122 2.803 -70.270 1.00 39.85 C ANISOU 1355 CA TRP A 226 5579 5329 4234 -283 21 -339 C ATOM 1356 C TRP A 226 4.839 1.877 -69.093 1.00 47.19 C ANISOU 1356 C TRP A 226 6236 6233 5463 -222 35 -368 C ATOM 1357 O TRP A 226 3.725 1.900 -68.558 1.00 43.69 O ANISOU 1357 O TRP A 226 5800 5693 5108 -50 -24 -389 O ATOM 1358 CB TRP A 226 4.476 2.249 -71.544 1.00 42.72 C ANISOU 1358 CB TRP A 226 5855 5806 4571 -126 -25 -490 C ATOM 1359 CG TRP A 226 5.272 1.189 -72.245 1.00 50.16 C ANISOU 1359 CG TRP A 226 6527 6932 5601 -210 65 -612 C ATOM 1360 CD1 TRP A 226 6.125 1.366 -73.297 1.00 54.02 C ANISOU 1360 CD1 TRP A 226 7083 7558 5883 -341 135 -620 C ATOM 1361 CD2 TRP A 226 5.277 -0.214 -71.957 1.00 46.58 C ANISOU 1361 CD2 TRP A 226 5687 6535 5476 -164 107 -748 C ATOM 1362 NE1 TRP A 226 6.665 0.161 -73.676 1.00 52.01 N ANISOU 1362 NE1 TRP A 226 6501 7452 5809 -375 217 -778 N ATOM 1363 CE2 TRP A 226 6.161 -0.825 -72.869 1.00 52.52 C ANISOU 1363 CE2 TRP A 226 6284 7454 6216 -266 196 -856 C ATOM 1364 CE3 TRP A 226 4.624 -1.013 -71.013 1.00 44.50 C ANISOU 1364 CE3 TRP A 226 5196 6186 5526 -50 93 -783 C ATOM 1365 CZ2 TRP A 226 6.409 -2.197 -72.865 1.00 54.11 C ANISOU 1365 CZ2 TRP A 226 6108 7721 6729 -247 259 -1010 C ATOM 1366 CZ3 TRP A 226 4.871 -2.376 -71.011 1.00 40.82 C ANISOU 1366 CZ3 TRP A 226 4365 5778 5367 -39 158 -908 C ATOM 1367 CH2 TRP A 226 5.756 -2.953 -71.930 1.00 38.28 C ANISOU 1367 CH2 TRP A 226 3892 5604 5047 -132 234 -1026 C ATOM 1368 N TYR A 227 5.810 1.070 -68.670 1.00 36.79 N ANISOU 1368 N TYR A 227 4675 4997 4305 -353 117 -360 N ATOM 1369 CA TYR A 227 5.608 0.270 -67.467 1.00 34.92 C ANISOU 1369 CA TYR A 227 4214 4728 4328 -302 133 -335 C ATOM 1370 C TYR A 227 5.864 1.099 -66.213 1.00 35.02 C ANISOU 1370 C TYR A 227 4404 4658 4245 -393 120 -191 C ATOM 1371 O TYR A 227 4.987 1.237 -65.353 1.00 36.23 O ANISOU 1371 O TYR A 227 4601 4722 4445 -275 91 -166 O ATOM 1372 CB TYR A 227 6.510 -0.970 -67.489 1.00 34.39 C ANISOU 1372 CB TYR A 227 3806 4771 4492 -377 210 -372 C ATOM 1373 CG TYR A 227 6.290 -1.906 -66.316 1.00 37.16 C ANISOU 1373 CG TYR A 227 3913 5082 5124 -309 231 -317 C ATOM 1374 CD1 TYR A 227 6.934 -1.694 -65.099 1.00 38.71 C ANISOU 1374 CD1 TYR A 227 4128 5274 5305 -414 235 -162 C ATOM 1375 CD2 TYR A 227 5.434 -2.998 -66.422 1.00 34.42 C ANISOU 1375 CD2 TYR A 227 3319 4703 5055 -143 247 -417 C ATOM 1376 CE1 TYR A 227 6.731 -2.540 -64.025 1.00 38.49 C ANISOU 1376 CE1 TYR A 227 3898 5223 5501 -344 256 -80 C ATOM 1377 CE2 TYR A 227 5.224 -3.849 -65.351 1.00 36.70 C ANISOU 1377 CE2 TYR A 227 3399 4940 5606 -86 286 -335 C ATOM 1378 CZ TYR A 227 5.879 -3.615 -64.156 1.00 36.69 C ANISOU 1378 CZ TYR A 227 3439 4947 5553 -182 291 -151 C ATOM 1379 OH TYR A 227 5.682 -4.458 -63.089 1.00 38.13 O ANISOU 1379 OH TYR A 227 3432 5092 5964 -120 331 -38 O ATOM 1380 N TRP A 228 7.066 1.668 -66.098 1.00 35.69 N ANISOU 1380 N TRP A 228 4584 4782 4197 -608 147 -115 N ATOM 1381 CA TRP A 228 7.461 2.303 -64.845 1.00 39.72 C ANISOU 1381 CA TRP A 228 5207 5244 4640 -715 129 -10 C ATOM 1382 C TRP A 228 6.696 3.596 -64.585 1.00 35.87 C ANISOU 1382 C TRP A 228 5063 4602 3963 -666 75 11 C ATOM 1383 O TRP A 228 6.458 3.944 -63.423 1.00 36.20 O ANISOU 1383 O TRP A 228 5175 4588 3990 -657 53 51 O ATOM 1384 CB TRP A 228 8.971 2.545 -64.841 1.00 39.16 C ANISOU 1384 CB TRP A 228 5114 5261 4506 -968 166 37 C ATOM 1385 CG TRP A 228 9.737 1.263 -64.944 1.00 40.87 C ANISOU 1385 CG TRP A 228 4971 5618 4940 -998 215 16 C ATOM 1386 CD1 TRP A 228 10.457 0.817 -66.016 1.00 40.68 C ANISOU 1386 CD1 TRP A 228 4807 5695 4954 -1076 282 -54 C ATOM 1387 CD2 TRP A 228 9.825 0.238 -63.948 1.00 40.69 C ANISOU 1387 CD2 TRP A 228 4680 5642 5137 -938 208 66 C ATOM 1388 NE1 TRP A 228 11.000 -0.414 -65.741 1.00 43.77 N ANISOU 1388 NE1 TRP A 228 4850 6179 5602 -1063 313 -66 N ATOM 1389 CE2 TRP A 228 10.626 -0.793 -64.478 1.00 44.15 C ANISOU 1389 CE2 TRP A 228 4818 6189 5769 -976 264 22 C ATOM 1390 CE3 TRP A 228 9.311 0.096 -62.654 1.00 42.68 C ANISOU 1390 CE3 TRP A 228 4922 5859 5435 -852 169 151 C ATOM 1391 CZ2 TRP A 228 10.926 -1.948 -63.761 1.00 45.24 C ANISOU 1391 CZ2 TRP A 228 4650 6374 6165 -923 269 77 C ATOM 1392 CZ3 TRP A 228 9.608 -1.055 -61.944 1.00 43.77 C ANISOU 1392 CZ3 TRP A 228 4767 6064 5800 -807 180 222 C ATOM 1393 CH2 TRP A 228 10.408 -2.061 -62.500 1.00 43.51 C ANISOU 1393 CH2 TRP A 228 4440 6113 5977 -838 224 192 C ATOM 1394 N GLU A 229 6.300 4.318 -65.636 1.00 35.95 N ANISOU 1394 N GLU A 229 5290 4542 3826 -626 52 -15 N ATOM 1395 CA GLU A 229 5.499 5.520 -65.421 1.00 42.81 C ANISOU 1395 CA GLU A 229 6476 5236 4553 -548 -5 5 C ATOM 1396 C GLU A 229 4.133 5.172 -64.847 1.00 36.50 C ANISOU 1396 C GLU A 229 5608 4380 3880 -304 -44 -50 C ATOM 1397 O GLU A 229 3.654 5.833 -63.918 1.00 39.47 O ANISOU 1397 O GLU A 229 6130 4646 4220 -263 -62 -38 O ATOM 1398 CB GLU A 229 5.340 6.305 -66.724 1.00 39.70 C ANISOU 1398 CB GLU A 229 6324 4781 3980 -532 -29 18 C ATOM 1399 CG GLU A 229 4.497 7.563 -66.558 1.00 61.33 C ANISOU 1399 CG GLU A 229 9391 7310 6601 -429 -96 49 C ATOM 1400 CD GLU A 229 4.318 8.340 -67.847 1.00 69.54 C ANISOU 1400 CD GLU A 229 10684 8281 7458 -393 -130 101 C ATOM 1401 OE1 GLU A 229 4.733 7.839 -68.912 1.00 68.17 O ANISOU 1401 OE1 GLU A 229 10423 8251 7228 -431 -101 95 O ATOM 1402 OE2 GLU A 229 3.759 9.457 -67.789 1.00 74.45 O1- ANISOU 1402 OE2 GLU A 229 11595 8704 7988 -321 -184 149 O1- ATOM 1403 N ASN A 230 3.493 4.133 -65.381 1.00 35.07 N ANISOU 1403 N ASN A 230 5194 4272 3858 -147 -46 -129 N ATOM 1404 CA ASN A 230 2.183 3.750 -64.876 1.00 41.13 C ANISOU 1404 CA ASN A 230 5863 4985 4778 73 -67 -191 C ATOM 1405 C ASN A 230 2.279 3.089 -63.507 1.00 42.78 C ANISOU 1405 C ASN A 230 5890 5229 5137 50 -3 -144 C ATOM 1406 O ASN A 230 1.373 3.249 -62.682 1.00 40.17 O ANISOU 1406 O ASN A 230 5585 4827 4850 172 4 -155 O ATOM 1407 CB ASN A 230 1.488 2.847 -65.890 1.00 41.06 C ANISOU 1407 CB ASN A 230 5648 5042 4913 231 -92 -310 C ATOM 1408 CG ASN A 230 1.051 3.608 -67.124 1.00 42.59 C ANISOU 1408 CG ASN A 230 6054 5202 4924 318 -182 -352 C ATOM 1409 OD1 ASN A 230 0.380 4.633 -67.021 1.00 44.14 O ANISOU 1409 OD1 ASN A 230 6497 5268 5006 414 -247 -328 O ATOM 1410 ND2 ASN A 230 1.450 3.129 -68.297 1.00 41.24 N ANISOU 1410 ND2 ASN A 230 5797 5155 4716 290 -188 -411 N ATOM 1411 N LEU A 231 3.369 2.367 -63.237 1.00 41.11 N ANISOU 1411 N LEU A 231 5494 5131 4994 -101 47 -86 N ATOM 1412 CA LEU A 231 3.573 1.831 -61.894 1.00 38.53 C ANISOU 1412 CA LEU A 231 5027 4848 4764 -129 93 -3 C ATOM 1413 C LEU A 231 3.663 2.951 -60.865 1.00 40.74 C ANISOU 1413 C LEU A 231 5563 5073 4841 -199 73 47 C ATOM 1414 O LEU A 231 3.099 2.844 -59.769 1.00 42.65 O ANISOU 1414 O LEU A 231 5785 5310 5110 -123 102 75 O ATOM 1415 CB LEU A 231 4.832 0.966 -61.849 1.00 36.91 C ANISOU 1415 CB LEU A 231 4594 4772 4657 -275 126 60 C ATOM 1416 CG LEU A 231 5.149 0.389 -60.464 1.00 48.84 C ANISOU 1416 CG LEU A 231 5963 6349 6247 -300 155 181 C ATOM 1417 CD1 LEU A 231 4.047 -0.561 -60.005 1.00 43.51 C ANISOU 1417 CD1 LEU A 231 5097 5638 5798 -112 214 191 C ATOM 1418 CD2 LEU A 231 6.500 -0.304 -60.448 1.00 48.08 C ANISOU 1418 CD2 LEU A 231 5660 6375 6235 -444 161 248 C ATOM 1419 N LEU A 232 4.368 4.037 -61.198 1.00 36.08 N ANISOU 1419 N LEU A 232 5216 4442 4052 -350 33 50 N ATOM 1420 CA LEU A 232 4.448 5.171 -60.282 1.00 37.60 C ANISOU 1420 CA LEU A 232 5659 4559 4066 -424 10 59 C ATOM 1421 C LEU A 232 3.067 5.753 -60.014 1.00 33.96 C ANISOU 1421 C LEU A 232 5355 3959 3590 -226 3 -7 C ATOM 1422 O LEU A 232 2.700 6.004 -58.860 1.00 37.61 O ANISOU 1422 O LEU A 232 5868 4412 4011 -193 24 -15 O ATOM 1423 CB LEU A 232 5.381 6.245 -60.843 1.00 40.68 C ANISOU 1423 CB LEU A 232 6279 4890 4288 -624 -19 64 C ATOM 1424 CG LEU A 232 5.430 7.537 -60.022 1.00 38.72 C ANISOU 1424 CG LEU A 232 6312 4521 3878 -708 -45 38 C ATOM 1425 CD1 LEU A 232 5.965 7.266 -58.618 1.00 40.78 C ANISOU 1425 CD1 LEU A 232 6470 4912 4113 -799 -46 56 C ATOM 1426 CD2 LEU A 232 6.259 8.604 -60.716 1.00 43.48 C ANISOU 1426 CD2 LEU A 232 7143 5022 4355 -904 -57 48 C ATOM 1427 N LYS A 233 2.286 5.974 -61.075 1.00 31.01 N ANISOU 1427 N LYS A 233 5051 3489 3242 -86 -29 -62 N ATOM 1428 CA LYS A 233 0.939 6.509 -60.906 1.00 35.83 C ANISOU 1428 CA LYS A 233 5781 3965 3867 124 -48 -135 C ATOM 1429 C LYS A 233 0.087 5.592 -60.039 1.00 38.98 C ANISOU 1429 C LYS A 233 5948 4427 4436 269 19 -157 C ATOM 1430 O LYS A 233 -0.673 6.062 -59.184 1.00 35.70 O ANISOU 1430 O LYS A 233 5620 3944 3999 365 48 -200 O ATOM 1431 CB LYS A 233 0.284 6.722 -62.270 1.00 32.70 C ANISOU 1431 CB LYS A 233 5450 3493 3481 265 -116 -181 C ATOM 1432 CG LYS A 233 0.876 7.877 -63.061 1.00 33.94 C ANISOU 1432 CG LYS A 233 5907 3542 3445 155 -169 -136 C ATOM 1433 CD LYS A 233 0.230 8.004 -64.427 1.00 34.02 C ANISOU 1433 CD LYS A 233 5978 3514 3435 311 -248 -158 C ATOM 1434 CE LYS A 233 0.802 9.183 -65.197 1.00 41.13 C ANISOU 1434 CE LYS A 233 7201 4293 4133 203 -284 -73 C ATOM 1435 NZ LYS A 233 0.199 9.291 -66.554 1.00 48.12 N ANISOU 1435 NZ LYS A 233 8156 5171 4957 364 -372 -70 N ATOM 1436 N ILE A 234 0.213 4.278 -60.237 1.00 37.77 N ANISOU 1436 N ILE A 234 5494 4394 4464 281 59 -130 N ATOM 1437 CA ILE A 234 -0.554 3.322 -59.446 1.00 35.96 C ANISOU 1437 CA ILE A 234 5028 4210 4425 402 144 -126 C ATOM 1438 C ILE A 234 -0.105 3.342 -57.991 1.00 33.24 C ANISOU 1438 C ILE A 234 4702 3938 3988 307 207 -33 C ATOM 1439 O ILE A 234 -0.934 3.321 -57.074 1.00 42.00 O ANISOU 1439 O ILE A 234 5798 5039 5122 412 279 -42 O ATOM 1440 CB ILE A 234 -0.435 1.913 -60.056 1.00 41.35 C ANISOU 1440 CB ILE A 234 5387 4975 5350 422 175 -119 C ATOM 1441 CG1 ILE A 234 -1.135 1.859 -61.414 1.00 49.39 C ANISOU 1441 CG1 ILE A 234 6371 5942 6452 553 109 -250 C ATOM 1442 CG2 ILE A 234 -1.001 0.863 -59.111 1.00 41.05 C ANISOU 1442 CG2 ILE A 234 5099 4972 5525 502 287 -68 C ATOM 1443 CD1 ILE A 234 -2.552 2.379 -61.392 1.00 63.19 C ANISOU 1443 CD1 ILE A 234 8191 7584 8234 757 87 -352 C ATOM 1444 N CYS A 235 1.210 3.378 -57.754 1.00 39.51 N ANISOU 1444 N CYS A 235 5521 4824 4668 110 180 52 N ATOM 1445 CA CYS A 235 1.711 3.399 -56.383 1.00 42.53 C ANISOU 1445 CA CYS A 235 5919 5310 4932 20 210 136 C ATOM 1446 C CYS A 235 1.305 4.678 -55.665 1.00 44.32 C ANISOU 1446 C CYS A 235 6431 5460 4949 27 201 55 C ATOM 1447 O CYS A 235 0.994 4.653 -54.469 1.00 40.71 O ANISOU 1447 O CYS A 235 5980 5071 4418 58 260 75 O ATOM 1448 CB CYS A 235 3.231 3.240 -56.370 1.00 47.98 C ANISOU 1448 CB CYS A 235 6561 6116 5551 -191 157 220 C ATOM 1449 SG CYS A 235 3.807 1.577 -56.783 1.00 59.39 S ANISOU 1449 SG CYS A 235 7628 7674 7265 -194 189 329 S ATOM 1450 N VAL A 236 1.313 5.809 -56.374 1.00 39.48 N ANISOU 1450 N VAL A 236 6060 4703 4236 -2 134 -36 N ATOM 1451 CA VAL A 236 0.850 7.054 -55.771 1.00 40.98 C ANISOU 1451 CA VAL A 236 6522 4777 4272 23 128 -138 C ATOM 1452 C VAL A 236 -0.627 6.950 -55.422 1.00 33.44 C ANISOU 1452 C VAL A 236 5528 3762 3415 258 202 -210 C ATOM 1453 O VAL A 236 -1.052 7.349 -54.332 1.00 39.94 O ANISOU 1453 O VAL A 236 6433 4598 4142 296 261 -264 O ATOM 1454 CB VAL A 236 1.130 8.243 -56.708 1.00 40.85 C ANISOU 1454 CB VAL A 236 6768 4580 4171 -43 48 -195 C ATOM 1455 CG1 VAL A 236 0.443 9.498 -56.190 1.00 34.49 C ANISOU 1455 CG1 VAL A 236 6230 3603 3270 29 48 -317 C ATOM 1456 CG2 VAL A 236 2.627 8.472 -56.837 1.00 37.62 C ANISOU 1456 CG2 VAL A 236 6405 4234 3656 -306 1 -140 C ATOM 1457 N PHE A 237 -1.427 6.392 -56.333 1.00 34.16 N ANISOU 1457 N PHE A 237 5476 3801 3700 416 204 -227 N ATOM 1458 CA PHE A 237 -2.862 6.272 -56.098 1.00 38.59 C ANISOU 1458 CA PHE A 237 5966 4304 4395 641 272 -312 C ATOM 1459 C PHE A 237 -3.168 5.402 -54.884 1.00 38.19 C ANISOU 1459 C PHE A 237 5723 4392 4396 667 409 -252 C ATOM 1460 O PHE A 237 -4.100 5.696 -54.127 1.00 42.09 O ANISOU 1460 O PHE A 237 6247 4860 4884 787 498 -327 O ATOM 1461 CB PHE A 237 -3.542 5.709 -57.346 1.00 35.21 C ANISOU 1461 CB PHE A 237 5377 3826 4176 785 229 -350 C ATOM 1462 CG PHE A 237 -5.030 5.532 -57.208 1.00 41.21 C ANISOU 1462 CG PHE A 237 6018 4528 5112 1016 288 -454 C ATOM 1463 CD1 PHE A 237 -5.849 6.616 -56.939 1.00 41.72 C ANISOU 1463 CD1 PHE A 237 6274 4459 5117 1145 280 -569 C ATOM 1464 CD2 PHE A 237 -5.611 4.283 -57.374 1.00 40.94 C ANISOU 1464 CD2 PHE A 237 5665 4560 5330 1102 355 -451 C ATOM 1465 CE1 PHE A 237 -7.218 6.458 -56.823 1.00 45.53 C ANISOU 1465 CE1 PHE A 237 6621 4896 5782 1360 337 -679 C ATOM 1466 CE2 PHE A 237 -6.979 4.117 -57.263 1.00 37.81 C ANISOU 1466 CE2 PHE A 237 5133 4112 5122 1302 416 -561 C ATOM 1467 CZ PHE A 237 -7.784 5.205 -56.986 1.00 41.50 C ANISOU 1467 CZ PHE A 237 5781 4466 5520 1433 406 -675 C ATOM 1468 N AILE A 238 -2.384 4.350 -54.658 0.57 38.27 N ANISOU 1468 N AILE A 238 5539 4550 4454 558 437 -110 N ATOM 1469 N BILE A 238 -2.416 4.319 -54.694 0.43 38.36 N ANISOU 1469 N BILE A 238 5542 4559 4475 564 438 -111 N ATOM 1470 CA AILE A 238 -2.703 3.419 -53.581 0.57 40.87 C ANISOU 1470 CA AILE A 238 5678 5002 4849 594 574 -10 C ATOM 1471 CA BILE A 238 -2.676 3.431 -53.566 0.43 40.99 C ANISOU 1471 CA BILE A 238 5697 5020 4859 590 573 -8 C ATOM 1472 C AILE A 238 -2.078 3.821 -52.245 0.57 39.50 C ANISOU 1472 C AILE A 238 5640 4960 4407 480 601 50 C ATOM 1473 C BILE A 238 -2.170 4.046 -52.270 0.43 39.36 C ANISOU 1473 C BILE A 238 5666 4920 4369 489 594 19 C ATOM 1474 O AILE A 238 -2.669 3.566 -51.192 0.57 41.36 O ANISOU 1474 O AILE A 238 5832 5277 4606 547 728 84 O ATOM 1475 O BILE A 238 -2.912 4.168 -51.290 0.43 41.49 O ANISOU 1475 O BILE A 238 5961 5230 4574 572 710 -8 O ATOM 1476 CB AILE A 238 -2.299 1.986 -53.972 0.57 47.23 C ANISOU 1476 CB AILE A 238 6183 5879 5883 567 599 125 C ATOM 1477 CB BILE A 238 -2.038 2.051 -53.806 0.43 46.67 C ANISOU 1477 CB BILE A 238 6139 5834 5759 530 590 148 C ATOM 1478 CG1AILE A 238 -0.791 1.884 -54.204 0.57 47.57 C ANISOU 1478 CG1AILE A 238 6240 6008 5826 378 498 220 C ATOM 1479 CG1BILE A 238 -2.545 1.437 -55.107 0.43 46.23 C ANISOU 1479 CG1BILE A 238 5902 5684 5981 626 567 78 C ATOM 1480 CG2AILE A 238 -3.074 1.534 -55.205 0.57 45.13 C ANISOU 1480 CG2AILE A 238 5761 5502 5886 695 583 25 C ATOM 1481 CG2BILE A 238 -2.332 1.125 -52.636 0.43 49.82 C ANISOU 1481 CG2BILE A 238 6365 6345 6217 565 738 293 C ATOM 1482 CD1AILE A 238 -0.357 0.561 -54.806 0.57 46.50 C ANISOU 1482 CD1AILE A 238 5815 5910 5944 362 508 316 C ATOM 1483 CD1BILE A 238 -1.730 0.251 -55.549 0.43 44.33 C ANISOU 1483 CD1BILE A 238 5420 5508 5915 547 560 188 C ATOM 1484 N PHE A 239 -0.898 4.446 -52.251 1.00 35.93 N ANISOU 1484 N PHE A 239 5347 4546 3759 305 486 58 N ATOM 1485 CA PHE A 239 -0.277 4.879 -51.005 1.00 39.60 C ANISOU 1485 CA PHE A 239 5939 5152 3954 191 483 80 C ATOM 1486 C PHE A 239 -0.761 6.248 -50.553 1.00 39.94 C ANISOU 1486 C PHE A 239 6263 5101 3813 215 485 -110 C ATOM 1487 O PHE A 239 -0.740 6.539 -49.353 1.00 39.70 O ANISOU 1487 O PHE A 239 6319 5194 3573 189 532 -136 O ATOM 1488 CB PHE A 239 1.244 4.892 -51.145 1.00 45.10 C ANISOU 1488 CB PHE A 239 6644 5944 4550 -19 357 155 C ATOM 1489 CG PHE A 239 1.878 3.549 -50.960 1.00 51.51 C ANISOU 1489 CG PHE A 239 7186 6915 5472 -52 368 359 C ATOM 1490 CD1 PHE A 239 2.095 3.041 -49.688 1.00 54.40 C ANISOU 1490 CD1 PHE A 239 7485 7478 5707 -62 410 493 C ATOM 1491 CD2 PHE A 239 2.259 2.793 -52.053 1.00 52.60 C ANISOU 1491 CD2 PHE A 239 7138 7008 5841 -65 337 418 C ATOM 1492 CE1 PHE A 239 2.678 1.803 -49.513 1.00 51.55 C ANISOU 1492 CE1 PHE A 239 6877 7241 5467 -76 414 705 C ATOM 1493 CE2 PHE A 239 2.844 1.557 -51.885 1.00 57.00 C ANISOU 1493 CE2 PHE A 239 7439 7685 6535 -84 350 597 C ATOM 1494 CZ PHE A 239 3.053 1.060 -50.613 1.00 54.76 C ANISOU 1494 CZ PHE A 239 7091 7572 6142 -86 384 752 C ATOM 1495 N ALA A 240 -1.185 7.102 -51.478 1.00 39.12 N ANISOU 1495 N ALA A 240 6307 4782 3774 270 432 -245 N ATOM 1496 CA ALA A 240 -1.645 8.429 -51.102 1.00 41.39 C ANISOU 1496 CA ALA A 240 6861 4938 3927 305 432 -431 C ATOM 1497 C ALA A 240 -3.157 8.533 -51.005 1.00 40.28 C ANISOU 1497 C ALA A 240 6697 4698 3911 542 540 -538 C ATOM 1498 O ALA A 240 -3.657 9.479 -50.389 1.00 43.92 O ANISOU 1498 O ALA A 240 7339 5085 4265 597 580 -698 O ATOM 1499 CB ALA A 240 -1.129 9.476 -52.094 1.00 41.15 C ANISOU 1499 CB ALA A 240 7046 4706 3883 216 304 -503 C ATOM 1500 N PHE A 241 -3.899 7.589 -51.579 1.00 36.85 N ANISOU 1500 N PHE A 241 6029 4257 3714 682 592 -474 N ATOM 1501 CA PHE A 241 -5.349 7.694 -51.526 1.00 37.48 C ANISOU 1501 CA PHE A 241 6056 4243 3940 906 691 -592 C ATOM 1502 C PHE A 241 -6.003 6.433 -50.973 1.00 36.07 C ANISOU 1502 C PHE A 241 5590 4207 3908 989 854 -497 C ATOM 1503 O PHE A 241 -6.689 6.493 -49.949 1.00 38.51 O ANISOU 1503 O PHE A 241 5891 4583 4159 1062 1005 -548 O ATOM 1504 CB PHE A 241 -5.917 8.019 -52.908 1.00 39.16 C ANISOU 1504 CB PHE A 241 6282 4257 4341 1036 586 -665 C ATOM 1505 CG PHE A 241 -7.392 8.253 -52.898 1.00 37.29 C ANISOU 1505 CG PHE A 241 5990 3914 4265 1276 658 -810 C ATOM 1506 CD1 PHE A 241 -7.914 9.420 -52.364 1.00 38.43 C ANISOU 1506 CD1 PHE A 241 6344 3940 4316 1359 684 -975 C ATOM 1507 CD2 PHE A 241 -8.261 7.295 -53.389 1.00 47.36 C ANISOU 1507 CD2 PHE A 241 6983 5207 5804 1417 705 -800 C ATOM 1508 CE1 PHE A 241 -9.273 9.632 -52.336 1.00 47.74 C ANISOU 1508 CE1 PHE A 241 7448 5027 5664 1590 754 -1119 C ATOM 1509 CE2 PHE A 241 -9.622 7.502 -53.365 1.00 45.98 C ANISOU 1509 CE2 PHE A 241 6727 4946 5798 1637 770 -948 C ATOM 1510 CZ PHE A 241 -10.130 8.669 -52.840 1.00 45.33 C ANISOU 1510 CZ PHE A 241 6849 4754 5621 1729 795 -1103 C ATOM 1511 N ILE A 242 -5.796 5.290 -51.634 1.00 41.27 N ANISOU 1511 N ILE A 242 6790 4221 4671 -620 798 -512 N ATOM 1512 CA ILE A 242 -6.531 4.076 -51.276 1.00 42.31 C ANISOU 1512 CA ILE A 242 6912 4277 4884 -516 764 -611 C ATOM 1513 C ILE A 242 -6.198 3.641 -49.852 1.00 41.45 C ANISOU 1513 C ILE A 242 6481 4214 5055 -350 789 -571 C ATOM 1514 O ILE A 242 -7.088 3.469 -49.013 1.00 46.71 O ANISOU 1514 O ILE A 242 7055 4868 5826 -312 597 -568 O ATOM 1515 CB ILE A 242 -6.242 2.948 -52.279 1.00 44.97 C ANISOU 1515 CB ILE A 242 7495 4520 5070 -515 1017 -738 C ATOM 1516 CG1 ILE A 242 -6.722 3.334 -53.681 1.00 52.29 C ANISOU 1516 CG1 ILE A 242 8793 5401 5674 -698 950 -782 C ATOM 1517 CG2 ILE A 242 -6.896 1.658 -51.806 1.00 44.32 C ANISOU 1517 CG2 ILE A 242 7443 4315 5082 -440 988 -830 C ATOM 1518 CD1 ILE A 242 -8.200 3.646 -53.763 1.00 53.12 C ANISOU 1518 CD1 ILE A 242 9001 5480 5703 -796 566 -787 C ATOM 1519 N MET A 243 -4.912 3.424 -49.573 1.00 40.13 N ANISOU 1519 N MET A 243 6128 4124 4996 -248 1030 -535 N ATOM 1520 CA MET A 243 -4.505 3.021 -48.227 1.00 44.25 C ANISOU 1520 CA MET A 243 6356 4699 5759 -78 1029 -480 C ATOM 1521 C MET A 243 -4.921 4.030 -47.164 1.00 43.89 C ANISOU 1521 C MET A 243 6145 4723 5807 -118 762 -391 C ATOM 1522 O MET A 243 -5.448 3.608 -46.120 1.00 39.59 O ANISOU 1522 O MET A 243 5499 4160 5383 -24 650 -380 O ATOM 1523 CB MET A 243 -2.993 2.773 -48.189 1.00 49.27 C ANISOU 1523 CB MET A 243 6772 5466 6485 48 1301 -444 C ATOM 1524 CG MET A 243 -2.449 2.433 -46.806 1.00 58.03 C ANISOU 1524 CG MET A 243 7566 6657 7826 236 1264 -363 C ATOM 1525 SD MET A 243 -0.653 2.584 -46.669 1.00 70.56 S ANISOU 1525 SD MET A 243 8762 8518 9530 343 1491 -283 S ATOM 1526 CE MET A 243 -0.450 4.363 -46.702 1.00 73.55 C ANISOU 1526 CE MET A 243 9054 9049 9843 4 1330 -189 C ATOM 1527 N PRO A 244 -4.716 5.341 -47.338 1.00 38.63 N ANISOU 1527 N PRO A 244 5484 4117 5076 -255 662 -328 N ATOM 1528 CA PRO A 244 -5.170 6.283 -46.300 1.00 38.57 C ANISOU 1528 CA PRO A 244 5388 4130 5137 -261 407 -270 C ATOM 1529 C PRO A 244 -6.671 6.266 -46.069 1.00 36.85 C ANISOU 1529 C PRO A 244 5270 3845 4887 -215 191 -320 C ATOM 1530 O PRO A 244 -7.111 6.363 -44.917 1.00 38.08 O ANISOU 1530 O PRO A 244 5290 4035 5143 -125 65 -305 O ATOM 1531 CB PRO A 244 -4.690 7.637 -46.835 1.00 38.89 C ANISOU 1531 CB PRO A 244 5538 4177 5061 -446 358 -206 C ATOM 1532 CG PRO A 244 -3.541 7.294 -47.709 1.00 37.15 C ANISOU 1532 CG PRO A 244 5284 4039 4791 -528 648 -196 C ATOM 1533 CD PRO A 244 -3.901 6.020 -48.362 1.00 40.27 C ANISOU 1533 CD PRO A 244 5782 4374 5144 -414 803 -296 C ATOM 1534 N VAL A 245 -7.475 6.155 -47.129 1.00 34.21 N ANISOU 1534 N VAL A 245 5154 3445 4400 -280 143 -379 N ATOM 1535 CA VAL A 245 -8.923 6.085 -46.943 1.00 39.52 C ANISOU 1535 CA VAL A 245 5845 4119 5050 -244 -68 -425 C ATOM 1536 C VAL A 245 -9.295 4.834 -46.156 1.00 39.58 C ANISOU 1536 C VAL A 245 5710 4146 5185 -185 -2 -461 C ATOM 1537 O VAL A 245 -10.163 4.873 -45.277 1.00 39.65 O ANISOU 1537 O VAL A 245 5583 4226 5257 -131 -133 -460 O ATOM 1538 CB VAL A 245 -9.651 6.142 -48.300 1.00 42.28 C ANISOU 1538 CB VAL A 245 6444 4423 5196 -347 -160 -475 C ATOM 1539 CG1 VAL A 245 -11.121 5.780 -48.131 1.00 39.81 C ANISOU 1539 CG1 VAL A 245 6068 4177 4882 -329 -360 -530 C ATOM 1540 CG2 VAL A 245 -9.526 7.528 -48.910 1.00 44.96 C ANISOU 1540 CG2 VAL A 245 6968 4722 5392 -390 -291 -411 C ATOM 1541 N LEU A 246 -8.633 3.711 -46.442 1.00 34.41 N ANISOU 1541 N LEU A 246 5103 3419 4553 -187 216 -491 N ATOM 1542 CA LEU A 246 -8.915 2.488 -45.695 1.00 35.91 C ANISOU 1542 CA LEU A 246 5235 3565 4845 -141 280 -507 C ATOM 1543 C LEU A 246 -8.481 2.614 -44.239 1.00 39.03 C ANISOU 1543 C LEU A 246 5401 4031 5398 -11 272 -419 C ATOM 1544 O LEU A 246 -9.201 2.179 -43.333 1.00 39.66 O ANISOU 1544 O LEU A 246 5406 4134 5531 -2 210 -404 O ATOM 1545 CB LEU A 246 -8.228 1.294 -46.357 1.00 37.16 C ANISOU 1545 CB LEU A 246 5565 3576 4976 -119 516 -564 C ATOM 1546 CG LEU A 246 -8.816 0.843 -47.697 1.00 50.15 C ANISOU 1546 CG LEU A 246 7504 5117 6432 -272 523 -678 C ATOM 1547 CD1 LEU A 246 -7.984 -0.276 -48.303 1.00 47.65 C ANISOU 1547 CD1 LEU A 246 7399 4630 6074 -198 794 -753 C ATOM 1548 CD2 LEU A 246 -10.262 0.404 -47.520 1.00 48.16 C ANISOU 1548 CD2 LEU A 246 7283 4866 6150 -426 333 -719 C ATOM 1549 N ILE A 247 -7.312 3.210 -43.994 1.00 34.52 N ANISOU 1549 N ILE A 247 4718 3514 4883 59 330 -356 N ATOM 1550 CA ILE A 247 -6.798 3.305 -42.629 1.00 38.88 C ANISOU 1550 CA ILE A 247 5069 4142 5560 169 296 -273 C ATOM 1551 C ILE A 247 -7.724 4.153 -41.763 1.00 36.89 C ANISOU 1551 C ILE A 247 4760 3964 5293 158 91 -265 C ATOM 1552 O ILE A 247 -8.126 3.741 -40.668 1.00 37.49 O ANISOU 1552 O ILE A 247 4757 4073 5415 218 58 -236 O ATOM 1553 CB ILE A 247 -5.361 3.859 -42.628 1.00 39.10 C ANISOU 1553 CB ILE A 247 4960 4258 5639 195 369 -211 C ATOM 1554 CG1 ILE A 247 -4.383 2.814 -43.170 1.00 43.11 C ANISOU 1554 CG1 ILE A 247 5448 4740 6193 302 610 -217 C ATOM 1555 CG2 ILE A 247 -4.953 4.286 -41.223 1.00 38.28 C ANISOU 1555 CG2 ILE A 247 4667 4257 5622 257 247 -130 C ATOM 1556 CD1 ILE A 247 -2.954 3.313 -43.274 1.00 44.54 C ANISOU 1556 CD1 ILE A 247 5414 5082 6427 314 709 -156 C ATOM 1557 N ILE A 248 -8.086 5.345 -42.243 1.00 34.92 N ANISOU 1557 N ILE A 248 4579 3732 4958 99 -40 -289 N ATOM 1558 CA ILE A 248 -8.834 6.267 -41.392 1.00 35.13 C ANISOU 1558 CA ILE A 248 4566 3817 4964 155 -220 -293 C ATOM 1559 C ILE A 248 -10.285 5.825 -41.231 1.00 39.95 C ANISOU 1559 C ILE A 248 5144 4487 5549 179 -278 -346 C ATOM 1560 O ILE A 248 -10.882 6.032 -40.168 1.00 40.16 O ANISOU 1560 O ILE A 248 5068 4605 5586 262 -339 -348 O ATOM 1561 CB ILE A 248 -8.739 7.710 -41.925 1.00 34.18 C ANISOU 1561 CB ILE A 248 4583 3651 4752 118 -354 -296 C ATOM 1562 CG1 ILE A 248 -9.462 7.855 -43.265 1.00 41.24 C ANISOU 1562 CG1 ILE A 248 5642 4495 5533 64 -405 -338 C ATOM 1563 CG2 ILE A 248 -7.275 8.142 -42.036 1.00 34.38 C ANISOU 1563 CG2 ILE A 248 4606 3658 4800 18 -284 -232 C ATOM 1564 CD1 ILE A 248 -9.547 9.284 -43.766 1.00 42.90 C ANISOU 1564 CD1 ILE A 248 6053 4619 5626 54 -569 -323 C ATOM 1565 N THR A 249 -10.882 5.211 -42.255 1.00 33.10 N ANISOU 1565 N THR A 249 4352 3592 4631 88 -258 -393 N ATOM 1566 CA THR A 249 -12.263 4.761 -42.103 1.00 37.62 C ANISOU 1566 CA THR A 249 4838 4272 5183 56 -324 -437 C ATOM 1567 C THR A 249 -12.352 3.561 -41.164 1.00 37.73 C ANISOU 1567 C THR A 249 4769 4298 5268 16 -198 -406 C ATOM 1568 O THR A 249 -13.276 3.474 -40.347 1.00 39.51 O ANISOU 1568 O THR A 249 4849 4667 5496 18 -230 -406 O ATOM 1569 CB THR A 249 -12.882 4.431 -43.464 1.00 39.02 C ANISOU 1569 CB THR A 249 5133 4428 5266 -77 -377 -497 C ATOM 1570 OG1 THR A 249 -12.066 3.477 -44.155 1.00 46.06 O ANISOU 1570 OG1 THR A 249 6194 5160 6148 -176 -211 -508 O ATOM 1571 CG2 THR A 249 -13.026 5.695 -44.310 1.00 39.43 C ANISOU 1571 CG2 THR A 249 5292 4478 5214 -21 -545 -507 C ATOM 1572 N VAL A 250 -11.397 2.634 -41.252 1.00 39.37 N ANISOU 1572 N VAL A 250 5077 4358 5523 -7 -45 -372 N ATOM 1573 CA VAL A 250 -11.436 1.460 -40.383 1.00 38.80 C ANISOU 1573 CA VAL A 250 5004 4239 5500 -33 60 -322 C ATOM 1574 C VAL A 250 -11.073 1.838 -38.952 1.00 39.21 C ANISOU 1574 C VAL A 250 4929 4375 5594 98 45 -242 C ATOM 1575 O VAL A 250 -11.734 1.406 -38.000 1.00 39.16 O ANISOU 1575 O VAL A 250 4867 4440 5572 62 61 -205 O ATOM 1576 CB VAL A 250 -10.518 0.352 -40.930 1.00 41.51 C ANISOU 1576 CB VAL A 250 5533 4367 5871 -28 219 -315 C ATOM 1577 CG1 VAL A 250 -10.369 -0.772 -39.911 1.00 42.18 C ANISOU 1577 CG1 VAL A 250 5672 4352 6002 0 308 -232 C ATOM 1578 CG2 VAL A 250 -11.074 -0.193 -42.236 1.00 43.79 C ANISOU 1578 CG2 VAL A 250 6009 4556 6072 -196 234 -414 C ATOM 1579 N CYS A 251 -10.028 2.648 -38.772 1.00 29.75 N ANISOU 1579 N CYS A 251 3695 3182 4428 218 13 -212 N ATOM 1580 CA CYS A 251 -9.617 3.031 -37.423 1.00 33.57 C ANISOU 1580 CA CYS A 251 4090 3742 4922 320 -34 -144 C ATOM 1581 C CYS A 251 -10.692 3.862 -36.735 1.00 37.57 C ANISOU 1581 C CYS A 251 4526 4395 5353 340 -132 -189 C ATOM 1582 O CYS A 251 -11.067 3.581 -35.591 1.00 37.09 O ANISOU 1582 O CYS A 251 4424 4415 5255 365 -110 -150 O ATOM 1583 CB CYS A 251 -8.288 3.789 -37.469 1.00 28.43 C ANISOU 1583 CB CYS A 251 3404 3087 4311 382 -76 -112 C ATOM 1584 SG CYS A 251 -6.864 2.730 -37.803 1.00 41.82 S ANISOU 1584 SG CYS A 251 5083 4697 6109 455 68 -38 S ATOM 1585 N TYR A 252 -11.209 4.885 -37.421 1.00 33.61 N ANISOU 1585 N TYR A 252 4027 3931 4810 354 -233 -268 N ATOM 1586 CA TYR A 252 -12.259 5.708 -36.829 1.00 34.00 C ANISOU 1586 CA TYR A 252 4006 4124 4788 447 -318 -326 C ATOM 1587 C TYR A 252 -13.556 4.925 -36.672 1.00 42.08 C ANISOU 1587 C TYR A 252 4898 5299 5792 377 -252 -345 C ATOM 1588 O TYR A 252 -14.289 5.117 -35.694 1.00 37.40 O ANISOU 1588 O TYR A 252 4194 4873 5143 446 -230 -360 O ATOM 1589 CB TYR A 252 -12.486 6.959 -37.674 1.00 30.89 C ANISOU 1589 CB TYR A 252 3687 3699 4352 518 -460 -394 C ATOM 1590 CG TYR A 252 -11.427 8.023 -37.495 1.00 37.96 C ANISOU 1590 CG TYR A 252 4720 4475 5228 559 -544 -380 C ATOM 1591 CD1 TYR A 252 -10.905 8.308 -36.238 1.00 37.64 C ANISOU 1591 CD1 TYR A 252 4685 4450 5166 611 -558 -360 C ATOM 1592 CD2 TYR A 252 -10.950 8.745 -38.583 1.00 33.81 C ANISOU 1592 CD2 TYR A 252 4342 3822 4682 506 -617 -382 C ATOM 1593 CE1 TYR A 252 -9.938 9.283 -36.070 1.00 39.15 C ANISOU 1593 CE1 TYR A 252 5008 4539 5329 586 -660 -352 C ATOM 1594 CE2 TYR A 252 -9.982 9.719 -38.426 1.00 38.63 C ANISOU 1594 CE2 TYR A 252 5088 4325 5266 471 -693 -360 C ATOM 1595 CZ TYR A 252 -9.482 9.985 -37.169 1.00 40.56 C ANISOU 1595 CZ TYR A 252 5317 4591 5501 500 -722 -350 C ATOM 1596 OH TYR A 252 -8.519 10.954 -37.009 1.00 36.30 O ANISOU 1596 OH TYR A 252 4918 3950 4925 406 -822 -332 O ATOM 1597 N GLY A 253 -13.857 4.042 -37.626 1.00 34.67 N ANISOU 1597 N GLY A 253 3975 4316 4881 216 -212 -349 N ATOM 1598 CA GLY A 253 -15.051 3.221 -37.506 1.00 38.78 C ANISOU 1598 CA GLY A 253 4368 4987 5380 65 -159 -358 C ATOM 1599 C GLY A 253 -14.990 2.284 -36.315 1.00 39.48 C ANISOU 1599 C GLY A 253 4460 5082 5460 -13 -17 -272 C ATOM 1600 O GLY A 253 -15.953 2.160 -35.557 1.00 39.96 O ANISOU 1600 O GLY A 253 4364 5354 5466 -65 37 -268 O ATOM 1601 N LEU A 254 -13.853 1.607 -36.137 1.00 36.56 N ANISOU 1601 N LEU A 254 4269 4492 5130 -12 50 -193 N ATOM 1602 CA LEU A 254 -13.692 0.735 -34.979 1.00 40.39 C ANISOU 1602 CA LEU A 254 4818 4943 5586 -56 156 -84 C ATOM 1603 C LEU A 254 -13.660 1.532 -33.681 1.00 43.46 C ANISOU 1603 C LEU A 254 5124 5486 5900 96 136 -62 C ATOM 1604 O LEU A 254 -14.106 1.037 -32.640 1.00 39.76 O ANISOU 1604 O LEU A 254 4654 5106 5346 30 226 7 O ATOM 1605 CB LEU A 254 -12.422 -0.101 -35.122 1.00 32.00 C ANISOU 1605 CB LEU A 254 3960 3612 4586 -9 203 -2 C ATOM 1606 CG LEU A 254 -12.453 -1.159 -36.229 1.00 41.11 C ANISOU 1606 CG LEU A 254 5285 4560 5774 -156 268 -28 C ATOM 1607 CD1 LEU A 254 -11.169 -1.976 -36.235 1.00 42.60 C ANISOU 1607 CD1 LEU A 254 5673 4492 6022 -19 336 50 C ATOM 1608 CD2 LEU A 254 -13.672 -2.057 -36.072 1.00 41.99 C ANISOU 1608 CD2 LEU A 254 5434 4702 5820 -436 330 -15 C ATOM 1609 N MET A 255 -13.138 2.760 -33.727 1.00 35.93 N ANISOU 1609 N MET A 255 4145 4552 4953 275 21 -119 N ATOM 1610 CA MET A 255 -13.140 3.616 -32.546 1.00 38.38 C ANISOU 1610 CA MET A 255 4434 4984 5163 416 -16 -132 C ATOM 1611 C MET A 255 -14.564 3.970 -32.131 1.00 42.89 C ANISOU 1611 C MET A 255 4847 5808 5642 434 42 -207 C ATOM 1612 O MET A 255 -14.911 3.906 -30.945 1.00 42.02 O ANISOU 1612 O MET A 255 4723 5832 5409 457 128 -182 O ATOM 1613 CB MET A 255 -12.322 4.877 -32.831 1.00 37.59 C ANISOU 1613 CB MET A 255 4391 4810 5082 553 -165 -190 C ATOM 1614 CG MET A 255 -12.210 5.852 -31.674 1.00 45.32 C ANISOU 1614 CG MET A 255 5426 5859 5936 688 -233 -227 C ATOM 1615 SD MET A 255 -11.495 7.429 -32.185 1.00 43.07 S ANISOU 1615 SD MET A 255 5262 5448 5653 777 -424 -314 S ATOM 1616 CE MET A 255 -12.892 8.181 -33.019 1.00 38.56 C ANISOU 1616 CE MET A 255 4634 4950 5066 896 -444 -442 C ATOM 1617 N ILE A 256 -15.405 4.334 -33.100 1.00 37.56 N ANISOU 1617 N ILE A 256 4038 5226 5008 434 -1 -297 N ATOM 1618 CA ILE A 256 -16.792 4.677 -32.803 1.00 44.45 C ANISOU 1618 CA ILE A 256 4681 6398 5812 487 50 -372 C ATOM 1619 C ILE A 256 -17.558 3.450 -32.320 1.00 48.12 C ANISOU 1619 C ILE A 256 5023 7022 6238 235 224 -297 C ATOM 1620 O ILE A 256 -18.368 3.538 -31.390 1.00 44.25 O ANISOU 1620 O ILE A 256 4376 6796 5640 259 350 -310 O ATOM 1621 CB ILE A 256 -17.452 5.318 -34.037 1.00 44.45 C ANISOU 1621 CB ILE A 256 4557 6464 5869 561 -84 -467 C ATOM 1622 CG1 ILE A 256 -16.907 6.730 -34.247 1.00 47.29 C ANISOU 1622 CG1 ILE A 256 5070 6685 6213 828 -241 -538 C ATOM 1623 CG2 ILE A 256 -18.969 5.334 -33.899 1.00 44.34 C ANISOU 1623 CG2 ILE A 256 4212 6820 5816 576 -28 -525 C ATOM 1624 CD1 ILE A 256 -17.409 7.392 -35.512 1.00 58.01 C ANISOU 1624 CD1 ILE A 256 6390 8046 7604 919 -404 -603 C ATOM 1625 N LEU A 257 -17.306 2.288 -32.930 1.00 40.65 N ANISOU 1625 N LEU A 257 4175 5909 5361 -22 251 -220 N ATOM 1626 CA LEU A 257 -17.991 1.069 -32.508 1.00 50.46 C ANISOU 1626 CA LEU A 257 5377 7241 6553 -324 406 -135 C ATOM 1627 C LEU A 257 -17.675 0.728 -31.057 1.00 39.24 C ANISOU 1627 C LEU A 257 4082 5819 5008 -320 540 -26 C ATOM 1628 O LEU A 257 -18.563 0.311 -30.304 1.00 47.40 O ANISOU 1628 O LEU A 257 4995 7085 5931 -486 698 17 O ATOM 1629 CB LEU A 257 -17.615 -0.093 -33.429 1.00 53.32 C ANISOU 1629 CB LEU A 257 5939 7326 6992 -573 394 -83 C ATOM 1630 CG LEU A 257 -18.181 -0.034 -34.850 1.00 64.57 C ANISOU 1630 CG LEU A 257 7259 8788 8484 -684 280 -182 C ATOM 1631 CD1 LEU A 257 -17.673 -1.203 -35.685 1.00 67.76 C ANISOU 1631 CD1 LEU A 257 7953 8864 8927 -907 287 -149 C ATOM 1632 CD2 LEU A 257 -19.702 -0.008 -34.824 1.00 62.78 C ANISOU 1632 CD2 LEU A 257 6680 8958 8215 -858 302 -226 C ATOM 1633 N AARG A 258 -16.414 0.890 -30.647 0.65 45.62 N ANISOU 1633 N AARG A 258 5125 6392 5818 -150 474 28 N ATOM 1634 N BARG A 258 -16.418 0.906 -30.644 0.35 45.81 N ANISOU 1634 N BARG A 258 5146 6418 5841 -148 473 27 N ATOM 1635 CA AARG A 258 -16.061 0.639 -29.252 0.65 46.59 C ANISOU 1635 CA AARG A 258 5393 6516 5792 -125 554 138 C ATOM 1636 CA BARG A 258 -16.057 0.638 -29.255 0.35 46.35 C ANISOU 1636 CA BARG A 258 5363 6485 5762 -125 554 138 C ATOM 1637 C AARG A 258 -16.746 1.636 -28.327 0.65 47.31 C ANISOU 1637 C AARG A 258 5333 6912 5730 29 617 50 C ATOM 1638 C BARG A 258 -16.711 1.642 -28.313 0.35 47.28 C ANISOU 1638 C BARG A 258 5336 6902 5726 33 614 52 C ATOM 1639 O AARG A 258 -17.241 1.262 -27.256 0.65 52.72 O ANISOU 1639 O AARG A 258 6031 7757 6242 -65 778 118 O ATOM 1640 O BARG A 258 -17.148 1.278 -27.215 0.35 52.12 O ANISOU 1640 O BARG A 258 5976 7664 6164 -53 769 122 O ATOM 1641 CB AARG A 258 -14.542 0.694 -29.072 0.65 43.30 C ANISOU 1641 CB AARG A 258 5204 5832 5415 41 422 207 C ATOM 1642 CB BARG A 258 -14.537 0.658 -29.095 0.35 43.24 C ANISOU 1642 CB BARG A 258 5199 5818 5410 36 423 209 C ATOM 1643 CG AARG A 258 -14.073 0.510 -27.631 0.65 42.45 C ANISOU 1643 CG AARG A 258 5269 5726 5133 93 444 326 C ATOM 1644 CG BARG A 258 -14.039 0.262 -27.710 0.35 44.18 C ANISOU 1644 CG BARG A 258 5512 5907 5366 60 453 350 C ATOM 1645 CD AARG A 258 -14.350 -0.902 -27.123 0.65 46.50 C ANISOU 1645 CD AARG A 258 5956 6152 5559 -137 583 500 C ATOM 1646 CD BARG A 258 -13.827 -1.246 -27.576 0.35 48.11 C ANISOU 1646 CD BARG A 258 6234 6190 5856 -120 528 530 C ATOM 1647 NE AARG A 258 -13.640 -1.910 -27.907 0.65 48.61 N ANISOU 1647 NE AARG A 258 6395 6101 5972 -186 538 585 N ATOM 1648 NE BARG A 258 -15.077 -1.995 -27.466 0.35 49.42 N ANISOU 1648 NE BARG A 258 6368 6471 5939 -421 716 566 N ATOM 1649 CZ AARG A 258 -12.408 -2.333 -27.642 0.65 48.89 C ANISOU 1649 CZ AARG A 258 6632 5909 6034 -30 435 704 C ATOM 1650 CZ BARG A 258 -15.638 -2.670 -28.465 0.35 52.05 C ANISOU 1650 CZ BARG A 258 6668 6732 6378 -647 764 540 C ATOM 1651 NH1AARG A 258 -11.741 -1.838 -26.607 0.65 49.73 N ANISOU 1651 NH1AARG A 258 6788 6081 6025 139 334 762 N ATOM 1652 NH1BARG A 258 -16.776 -3.323 -28.269 0.35 58.83 N ANISOU 1652 NH1BARG A 258 7475 7732 7144 -977 925 581 N ATOM 1653 NH2AARG A 258 -11.842 -3.251 -28.413 0.65 49.03 N ANISOU 1653 NH2AARG A 258 6802 5645 6183 -28 425 758 N ATOM 1654 NH2BARG A 258 -15.063 -2.694 -29.659 0.35 43.16 N ANISOU 1654 NH2BARG A 258 5565 5404 5430 -572 656 472 N ATOM 1655 N LEU A 259 -16.794 2.909 -28.727 1.00 42.90 N ANISOU 1655 N LEU A 259 4666 6422 5212 273 503 -101 N ATOM 1656 CA LEU A 259 -17.423 3.922 -27.887 1.00 51.48 C ANISOU 1656 CA LEU A 259 5657 7757 6145 485 563 -213 C ATOM 1657 C LEU A 259 -18.933 3.736 -27.801 1.00 58.39 C ANISOU 1657 C LEU A 259 6208 9010 6968 402 752 -259 C ATOM 1658 O LEU A 259 -19.540 4.099 -26.788 1.00 57.30 O ANISOU 1658 O LEU A 259 5994 9128 6650 508 910 -305 O ATOM 1659 CB LEU A 259 -17.089 5.320 -28.409 1.00 46.17 C ANISOU 1659 CB LEU A 259 5017 6999 5525 773 378 -359 C ATOM 1660 CG LEU A 259 -15.641 5.769 -28.207 1.00 43.80 C ANISOU 1660 CG LEU A 259 5001 6413 5226 848 205 -332 C ATOM 1661 CD1 LEU A 259 -15.375 7.083 -28.926 1.00 41.89 C ANISOU 1661 CD1 LEU A 259 4818 6054 5044 1045 24 -461 C ATOM 1662 CD2 LEU A 259 -15.329 5.894 -26.720 1.00 38.49 C ANISOU 1662 CD2 LEU A 259 4504 5786 4334 903 253 -307 C ATOM 1663 N LYS A 260 -19.559 3.183 -28.841 1.00 45.85 N ANISOU 1663 N LYS A 260 4415 7488 5518 208 741 -253 N ATOM 1664 CA LYS A 260 -20.995 2.944 -28.786 1.00 53.40 C ANISOU 1664 CA LYS A 260 4995 8858 6434 76 904 -284 C ATOM 1665 C LYS A 260 -21.353 1.681 -28.012 1.00 56.66 C ANISOU 1665 C LYS A 260 5430 9368 6732 -307 1129 -132 C ATOM 1666 O LYS A 260 -22.532 1.480 -27.698 1.00 58.41 O ANISOU 1666 O LYS A 260 5322 9992 6878 -457 1316 -142 O ATOM 1667 CB LYS A 260 -21.582 2.877 -30.203 1.00 65.77 C ANISOU 1667 CB LYS A 260 6326 10492 8171 -18 766 -339 C ATOM 1668 CG LYS A 260 -21.754 1.475 -30.770 1.00 76.08 C ANISOU 1668 CG LYS A 260 7655 11715 9537 -486 796 -227 C ATOM 1669 CD LYS A 260 -22.435 1.523 -32.133 1.00 85.40 C ANISOU 1669 CD LYS A 260 8593 13013 10842 -576 635 -304 C ATOM 1670 CE LYS A 260 -22.787 0.133 -32.643 1.00 91.86 C ANISOU 1670 CE LYS A 260 9439 13779 11683 -1090 669 -217 C ATOM 1671 NZ LYS A 260 -23.407 0.172 -33.999 1.00 94.60 N ANISOU 1671 NZ LYS A 260 9585 14235 12123 -1203 474 -298 N ATOM 1672 N SER A 261 -20.371 0.845 -27.676 1.00 54.91 N ANISOU 1672 N SER A 261 5583 8798 6482 -463 1119 17 N ATOM 1673 CA SER A 261 -20.635 -0.396 -26.961 1.00 60.10 C ANISOU 1673 CA SER A 261 6362 9463 7010 -836 1311 189 C ATOM 1674 C SER A 261 -20.632 -0.234 -25.448 1.00 63.52 C ANISOU 1674 C SER A 261 6909 10039 7185 -761 1488 248 C ATOM 1675 O SER A 261 -21.109 -1.132 -24.747 1.00 69.84 O ANISOU 1675 O SER A 261 7768 10941 7828 -1083 1694 388 O ATOM 1676 CB SER A 261 -19.604 -1.459 -27.351 1.00 59.03 C ANISOU 1676 CB SER A 261 6621 8852 6955 -1001 1206 333 C ATOM 1677 OG SER A 261 -18.314 -1.104 -26.881 1.00 60.20 O ANISOU 1677 OG SER A 261 7056 8735 7083 -717 1081 370 O ATOM 1678 N VAL A 262 -20.108 0.874 -24.924 1.00 64.66 N ANISOU 1678 N VAL A 262 7130 10181 7256 -377 1412 146 N ATOM 1679 CA VAL A 262 -20.054 1.058 -23.479 1.00 69.71 C ANISOU 1679 CA VAL A 262 7936 10941 7611 -302 1564 186 C ATOM 1680 C VAL A 262 -21.449 1.371 -22.953 1.00 78.62 C ANISOU 1680 C VAL A 262 8707 12581 8584 -320 1852 97 C ATOM 1681 O VAL A 262 -22.229 2.091 -23.590 1.00 75.83 O ANISOU 1681 O VAL A 262 7977 12490 8347 -150 1853 -69 O ATOM 1682 CB VAL A 262 -19.039 2.156 -23.113 1.00 72.15 C ANISOU 1682 CB VAL A 262 8471 11070 7872 78 1367 88 C ATOM 1683 CG1 VAL A 262 -19.406 3.473 -23.753 1.00 71.18 C ANISOU 1683 CG1 VAL A 262 8118 11069 7859 402 1278 -142 C ATOM 1684 CG2 VAL A 262 -18.939 2.310 -21.602 1.00 72.08 C ANISOU 1684 CG2 VAL A 262 8693 11167 7527 138 1498 124 C ATOM 1685 N ARG A 263 -21.763 0.750 -21.842 1.00 88.59 N ANISOU 1685 N ARG A 263 10083 13992 9584 -537 2096 225 N ATOM 1686 CA ARG A 263 -23.011 0.921 -21.181 1.00 98.61 C ANISOU 1686 CA ARG A 263 11027 15778 10660 -590 2428 167 C ATOM 1687 C ARG A 263 -22.588 1.393 -19.866 1.00103.24 C ANISOU 1687 C ARG A 263 11930 16368 10930 -383 2520 157 C ATOM 1688 O ARG A 263 -21.887 0.716 -19.170 1.00106.40 O ANISOU 1688 O ARG A 263 12740 16525 11163 -553 2500 340 O ATOM 1689 CB ARG A 263 -23.671 -0.416 -20.997 1.00103.46 C ANISOU 1689 CB ARG A 263 11588 16525 11197 -1144 2655 371 C ATOM 1690 CG ARG A 263 -24.047 -1.077 -22.294 1.00108.12 C ANISOU 1690 CG ARG A 263 11946 17063 12073 -1446 2542 398 C ATOM 1691 CD ARG A 263 -25.009 -0.216 -23.092 1.00114.04 C ANISOU 1691 CD ARG A 263 12112 18225 12994 -1241 2531 185 C ATOM 1692 NE ARG A 263 -24.895 -0.506 -24.512 1.00116.98 N ANISOU 1692 NE ARG A 263 12402 18387 13660 -1360 2269 167 N ATOM 1693 CZ ARG A 263 -25.294 0.306 -25.475 1.00116.62 C ANISOU 1693 CZ ARG A 263 12002 18502 13805 -1099 2108 -5 C ATOM 1694 NH1 ARG A 263 -25.857 1.470 -25.179 1.00116.97 N ANISOU 1694 NH1 ARG A 263 11734 18909 13801 -671 2180 -178 N ATOM 1695 NH2 ARG A 263 -25.133 -0.053 -26.733 1.00115.34 N ANISOU 1695 NH2 ARG A 263 11838 18123 13863 -1250 1873 -5 N ATOM 1696 N MET A 264 -22.976 2.590 -19.526 1.00107.41 N ANISOU 1696 N MET A 264 12308 17146 11356 14 2595 -64 N ATOM 1697 CA MET A 264 -22.628 3.076 -18.230 1.00114.28 C ANISOU 1697 CA MET A 264 13516 18028 11875 203 2692 -101 C ATOM 1698 C MET A 264 -23.934 3.135 -17.475 1.00113.36 C ANISOU 1698 C MET A 264 13087 18479 11506 175 3133 -164 C ATOM 1699 O MET A 264 -24.834 3.845 -17.864 1.00113.15 O ANISOU 1699 O MET A 264 12621 18800 11570 427 3249 -357 O ATOM 1700 CB MET A 264 -21.983 4.448 -18.338 1.00121.50 C ANISOU 1700 CB MET A 264 14600 18744 12822 689 2446 -324 C ATOM 1701 CG MET A 264 -21.978 5.016 -19.747 1.00125.45 C ANISOU 1701 CG MET A 264 14844 19123 13698 873 2201 -446 C ATOM 1702 SD MET A 264 -23.574 4.681 -20.488 1.00131.50 S ANISOU 1702 SD MET A 264 14937 20398 14628 751 2446 -481 S ATOM 1703 CE MET A 264 -24.577 5.893 -19.647 1.00137.27 C ANISOU 1703 CE MET A 264 15460 21593 15103 1231 2739 -742 C ATOM 1704 N LEU A 265 -24.012 2.399 -16.379 1.00114.26 N ANISOU 1704 N LEU A 265 13433 18692 11286 -115 3379 6 N ATOM 1705 CA LEU A 265 -25.219 2.324 -15.562 1.00115.58 C ANISOU 1705 CA LEU A 265 13319 19432 11165 -216 3856 -21 C ATOM 1706 C LEU A 265 -25.952 3.617 -15.265 1.00115.06 C ANISOU 1706 C LEU A 265 12972 19757 10988 299 4053 -329 C ATOM 1707 O LEU A 265 -27.097 3.577 -14.878 1.00114.43 O ANISOU 1707 O LEU A 265 12587 19984 10908 242 4336 -361 O ATOM 1708 CB LEU A 265 -24.943 1.612 -14.236 1.00115.68 C ANISOU 1708 CB LEU A 265 13798 19415 10741 -505 4056 186 C ATOM 1709 CG LEU A 265 -25.208 0.120 -14.342 1.00115.15 C ANISOU 1709 CG LEU A 265 13735 19326 10690 -1141 4173 496 C ATOM 1710 CD1 LEU A 265 -23.996 -0.620 -14.863 1.00112.15 C ANISOU 1710 CD1 LEU A 265 13787 18311 10512 -1294 3761 696 C ATOM 1711 CD2 LEU A 265 -25.816 -0.516 -13.099 1.00119.72 C ANISOU 1711 CD2 LEU A 265 14489 20083 10916 -1444 4534 659 C ATOM 1712 N SER A 266 -25.354 4.757 -15.529 1.00114.06 N ANISOU 1712 N SER A 266 13022 19371 10945 791 3780 -542 N ATOM 1713 CA SER A 266 -26.043 5.981 -15.133 1.00116.49 C ANISOU 1713 CA SER A 266 13207 19883 11171 1288 3926 -827 C ATOM 1714 C SER A 266 -26.303 6.957 -16.279 1.00117.91 C ANISOU 1714 C SER A 266 13079 20010 11712 1706 3688 -1032 C ATOM 1715 O SER A 266 -27.440 7.083 -16.751 1.00127.10 O ANISOU 1715 O SER A 266 13735 21451 13107 1763 3783 -1086 O ATOM 1716 CB SER A 266 -25.253 6.694 -14.038 1.00111.09 C ANISOU 1716 CB SER A 266 13135 18973 10102 1555 3891 -942 C ATOM 1717 OG SER A 266 -25.894 7.900 -13.667 1.00114.21 O ANISOU 1717 OG SER A 266 13499 19428 10469 2010 3986 -1220 O ATOM 1718 N GLY A 267 -25.269 7.685 -16.706 1.00110.19 N ANISOU 1718 N GLY A 267 12436 18661 10771 2004 3359 -1140 N ATOM 1719 CA GLY A 267 -25.465 8.844 -17.560 1.00108.81 C ANISOU 1719 CA GLY A 267 12135 18351 10856 2464 3132 -1354 C ATOM 1720 C GLY A 267 -25.465 8.560 -19.047 1.00109.56 C ANISOU 1720 C GLY A 267 11887 18388 11352 2364 2884 -1284 C ATOM 1721 O GLY A 267 -24.526 8.944 -19.754 1.00106.95 O ANISOU 1721 O GLY A 267 11845 17582 11210 2425 2506 -1287 O ATOM 1722 N SER A 268 -26.527 7.911 -19.537 1.00117.85 N ANISOU 1722 N SER A 268 12779 20042 11959 566 3840 766 N ATOM 1723 CA SER A 268 -26.609 7.581 -20.956 1.00117.10 C ANISOU 1723 CA SER A 268 12428 19685 12380 551 3677 766 C ATOM 1724 C SER A 268 -26.714 8.826 -21.828 1.00110.17 C ANISOU 1724 C SER A 268 11501 18730 11627 813 3511 384 C ATOM 1725 O SER A 268 -26.297 8.798 -22.993 1.00110.31 O ANISOU 1725 O SER A 268 11427 18539 11946 832 3276 380 O ATOM 1726 CB SER A 268 -27.799 6.660 -21.213 1.00124.17 C ANISOU 1726 CB SER A 268 13030 20485 13664 397 3903 832 C ATOM 1727 OG SER A 268 -27.548 5.350 -20.735 1.00128.64 O ANISOU 1727 OG SER A 268 13654 21009 14213 133 4000 1216 O ATOM 1728 N LYS A 269 -27.274 9.914 -21.295 1.00106.08 N ANISOU 1728 N LYS A 269 11066 18350 10891 1022 3629 60 N ATOM 1729 CA LYS A 269 -27.382 11.145 -22.070 1.00102.33 C ANISOU 1729 CA LYS A 269 10604 17757 10519 1300 3469 -307 C ATOM 1730 C LYS A 269 -26.012 11.758 -22.328 1.00102.78 C ANISOU 1730 C LYS A 269 10942 17756 10354 1352 3186 -352 C ATOM 1731 O LYS A 269 -25.737 12.234 -23.437 1.00103.12 O ANISOU 1731 O LYS A 269 10956 17597 10626 1473 2972 -491 O ATOM 1732 CB LYS A 269 -28.290 12.139 -21.348 1.00101.24 C ANISOU 1732 CB LYS A 269 10525 17746 10194 1520 3670 -636 C ATOM 1733 N GLU A 270 -25.140 11.757 -21.315 1.00103.76 N ANISOU 1733 N GLU A 270 11351 18051 10024 1251 3171 -243 N ATOM 1734 CA GLU A 270 -23.790 12.279 -21.494 1.00107.44 C ANISOU 1734 CA GLU A 270 12110 18408 10304 1227 2853 -285 C ATOM 1735 C GLU A 270 -22.981 11.423 -22.460 1.00104.43 C ANISOU 1735 C GLU A 270 11638 17762 10278 1041 2586 6 C ATOM 1736 O GLU A 270 -22.075 11.934 -23.130 1.00109.67 O ANISOU 1736 O GLU A 270 12468 18164 11038 1029 2267 -87 O ATOM 1737 CB GLU A 270 -23.082 12.374 -20.143 1.00112.73 C ANISOU 1737 CB GLU A 270 13089 19331 10413 1134 2863 -225 C ATOM 1738 N LYS A 271 -23.287 10.127 -22.544 1.00100.41 N ANISOU 1738 N LYS A 271 10875 17310 9968 887 2725 348 N ATOM 1739 CA LYS A 271 -22.598 9.261 -23.496 1.00 92.31 C ANISOU 1739 CA LYS A 271 9751 16019 9302 733 2498 605 C ATOM 1740 C LYS A 271 -23.097 9.482 -24.918 1.00 87.07 C ANISOU 1740 C LYS A 271 8875 15093 9117 830 2401 430 C ATOM 1741 O LYS A 271 -22.294 9.551 -25.856 1.00 85.19 O ANISOU 1741 O LYS A 271 8699 14579 9092 795 2109 434 O ATOM 1742 CB LYS A 271 -22.772 7.796 -23.102 1.00 89.83 C ANISOU 1742 CB LYS A 271 9277 15809 9044 538 2687 1023 C ATOM 1743 CG LYS A 271 -22.185 6.818 -24.105 1.00 90.39 C ANISOU 1743 CG LYS A 271 9232 15591 9522 398 2490 1272 C ATOM 1744 CD LYS A 271 -23.153 5.688 -24.411 1.00 93.35 C ANISOU 1744 CD LYS A 271 9334 15881 10254 271 2704 1441 C ATOM 1745 CE LYS A 271 -22.565 4.714 -25.418 1.00 88.71 C ANISOU 1745 CE LYS A 271 8658 14988 10062 143 2514 1655 C ATOM 1746 NZ LYS A 271 -23.491 3.581 -25.697 1.00 91.01 N ANISOU 1746 NZ LYS A 271 8789 15076 10715 -18 2656 1740 N ATOM 1747 N ASP A 272 -24.416 9.585 -25.099 1.00 85.65 N ANISOU 1747 N ASP A 272 8430 15017 9096 954 2641 276 N ATOM 1748 CA ASP A 272 -24.960 9.852 -26.426 1.00 85.08 C ANISOU 1748 CA ASP A 272 8152 14734 9440 1080 2530 92 C ATOM 1749 C ASP A 272 -24.478 11.195 -26.958 1.00 79.45 C ANISOU 1749 C ASP A 272 7706 13803 8677 1276 2271 -211 C ATOM 1750 O ASP A 272 -24.233 11.343 -28.161 1.00 71.98 O ANISOU 1750 O ASP A 272 6742 12584 8023 1310 2041 -263 O ATOM 1751 CB ASP A 272 -26.489 9.808 -26.394 1.00 92.27 C ANISOU 1751 CB ASP A 272 8830 15674 10555 1149 2736 -55 C ATOM 1752 CG ASP A 272 -27.034 8.394 -26.363 1.00103.12 C ANISOU 1752 CG ASP A 272 9995 16994 12193 880 2870 201 C ATOM 1753 OD1 ASP A 272 -26.237 7.448 -26.199 1.00107.58 O ANISOU 1753 OD1 ASP A 272 10622 17518 12736 666 2833 512 O ATOM 1754 OD2 ASP A 272 -28.263 8.229 -26.512 1.00111.41 O ANISOU 1754 OD2 ASP A 272 10825 18026 13478 885 3010 82 O ATOM 1755 N ARG A 273 -24.325 12.183 -26.073 1.00 80.33 N ANISOU 1755 N ARG A 273 8095 14021 8407 1395 2312 -414 N ATOM 1756 CA ARG A 273 -23.901 13.510 -26.506 1.00 75.60 C ANISOU 1756 CA ARG A 273 7793 13182 7751 1566 2094 -714 C ATOM 1757 C ARG A 273 -22.468 13.489 -27.022 1.00 76.97 C ANISOU 1757 C ARG A 273 8193 13097 7955 1375 1769 -596 C ATOM 1758 O ARG A 273 -22.182 14.006 -28.108 1.00 71.69 O ANISOU 1758 O ARG A 273 7604 12131 7503 1434 1557 -705 O ATOM 1759 CB ARG A 273 -24.048 14.506 -25.356 1.00 78.78 C ANISOU 1759 CB ARG A 273 8456 13753 7724 1709 2230 -970 C ATOM 1760 N ASN A 274 -21.550 12.892 -26.256 1.00 81.13 N ANISOU 1760 N ASN A 274 8820 13750 8257 1153 1728 -368 N ATOM 1761 CA ASN A 274 -20.161 12.809 -26.699 1.00 81.73 C ANISOU 1761 CA ASN A 274 9055 13633 8367 971 1428 -256 C ATOM 1762 C ASN A 274 -20.029 11.976 -27.966 1.00 72.25 C ANISOU 1762 C ASN A 274 7629 12220 7604 893 1311 -70 C ATOM 1763 O ASN A 274 -19.188 12.275 -28.821 1.00 71.93 O ANISOU 1763 O ASN A 274 7697 11934 7700 833 1072 -104 O ATOM 1764 CB ASN A 274 -19.282 12.230 -25.588 1.00 90.34 C ANISOU 1764 CB ASN A 274 10245 14949 9129 786 1403 -31 C ATOM 1765 CG ASN A 274 -18.566 13.301 -24.792 1.00 93.48 C ANISOU 1765 CG ASN A 274 10987 15411 9121 773 1289 -260 C ATOM 1766 OD1 ASN A 274 -18.733 13.404 -23.576 1.00 93.91 O ANISOU 1766 OD1 ASN A 274 11150 15746 8787 787 1428 -286 O ATOM 1767 ND2 ASN A 274 -17.762 14.107 -25.476 1.00 88.75 N ANISOU 1767 ND2 ASN A 274 10571 14553 8598 729 1042 -437 N ATOM 1768 N LEU A 275 -20.847 10.931 -28.108 1.00 70.70 N ANISOU 1768 N LEU A 275 7123 12115 7627 876 1490 115 N ATOM 1769 CA LEU A 275 -20.783 10.110 -29.311 1.00 66.32 C ANISOU 1769 CA LEU A 275 6358 11358 7484 799 1387 261 C ATOM 1770 C LEU A 275 -21.252 10.882 -30.537 1.00 62.48 C ANISOU 1770 C LEU A 275 5849 10648 7242 969 1278 10 C ATOM 1771 O LEU A 275 -20.720 10.689 -31.636 1.00 62.81 O ANISOU 1771 O LEU A 275 5880 10458 7525 911 1085 51 O ATOM 1772 CB LEU A 275 -21.610 8.841 -29.128 1.00 72.59 C ANISOU 1772 CB LEU A 275 6839 12289 8451 715 1618 489 C ATOM 1773 CG LEU A 275 -20.820 7.591 -28.750 1.00 77.60 C ANISOU 1773 CG LEU A 275 7460 12936 9086 500 1603 858 C ATOM 1774 CD1 LEU A 275 -21.772 6.440 -28.509 1.00 88.31 C ANISOU 1774 CD1 LEU A 275 8548 14402 10604 404 1876 1062 C ATOM 1775 CD2 LEU A 275 -19.821 7.244 -29.841 1.00 73.97 C ANISOU 1775 CD2 LEU A 275 7018 12201 8886 419 1334 937 C ATOM 1776 N ARG A 276 -22.251 11.754 -30.375 1.00 61.37 N ANISOU 1776 N ARG A 276 5706 10580 7031 1199 1399 -248 N ATOM 1777 CA ARG A 276 -22.689 12.576 -31.498 1.00 57.99 C ANISOU 1777 CA ARG A 276 5300 9935 6797 1408 1273 -479 C ATOM 1778 C ARG A 276 -21.581 13.515 -31.952 1.00 52.50 C ANISOU 1778 C ARG A 276 4976 8965 6009 1387 1025 -583 C ATOM 1779 O ARG A 276 -21.376 13.709 -33.155 1.00 50.49 O ANISOU 1779 O ARG A 276 4754 8462 5967 1416 849 -615 O ATOM 1780 CB ARG A 276 -23.939 13.376 -31.127 1.00 61.23 C ANISOU 1780 CB ARG A 276 5650 10488 7128 1702 1451 -741 C ATOM 1781 CG ARG A 276 -25.203 12.552 -30.974 1.00 77.57 C ANISOU 1781 CG ARG A 276 7287 12821 9366 1738 1695 -691 C ATOM 1782 CD ARG A 276 -26.442 13.435 -31.054 1.00 82.77 C ANISOU 1782 CD ARG A 276 7859 13536 10052 2067 1785 -982 C ATOM 1783 NE ARG A 276 -26.309 14.652 -30.255 1.00 89.73 N ANISOU 1783 NE ARG A 276 9051 14452 10591 2277 1842 -1220 N ATOM 1784 CZ ARG A 276 -26.683 14.760 -28.984 1.00 93.08 C ANISOU 1784 CZ ARG A 276 9479 15155 10732 2304 2102 -1279 C ATOM 1785 NH1 ARG A 276 -27.218 13.722 -28.356 1.00 94.99 N ANISOU 1785 NH1 ARG A 276 9473 15602 11017 2093 2307 -1074 N ATOM 1786 NH2 ARG A 276 -26.523 15.908 -28.339 1.00 92.99 N ANISOU 1786 NH2 ARG A 276 9804 15109 10419 2480 2120 -1522 N ATOM 1787 N ARG A 277 -20.851 14.101 -31.000 1.00 51.28 N ANISOU 1787 N ARG A 277 5104 8858 5524 1317 1012 -641 N ATOM 1788 CA ARG A 277 -19.790 15.039 -31.353 1.00 55.03 C ANISOU 1788 CA ARG A 277 5929 9078 5904 1252 796 -761 C ATOM 1789 C ARG A 277 -18.608 14.324 -31.997 1.00 54.69 C ANISOU 1789 C ARG A 277 5851 8922 6007 996 610 -542 C ATOM 1790 O ARG A 277 -18.017 14.831 -32.958 1.00 43.51 O ANISOU 1790 O ARG A 277 4590 7241 4701 959 439 -606 O ATOM 1791 CB ARG A 277 -19.345 15.809 -30.110 1.00 63.64 C ANISOU 1791 CB ARG A 277 7305 10278 6596 1218 830 -908 C ATOM 1792 CG ARG A 277 -18.467 17.014 -30.400 1.00 74.64 C ANISOU 1792 CG ARG A 277 9088 11391 7880 1164 644 -1113 C ATOM 1793 CD ARG A 277 -18.324 17.891 -29.166 1.00 87.10 C ANISOU 1793 CD ARG A 277 10952 13075 9068 1177 705 -1337 C ATOM 1794 NE ARG A 277 -17.745 19.194 -29.482 1.00 94.98 N ANISOU 1794 NE ARG A 277 12349 13752 9988 1155 565 -1591 N ATOM 1795 CZ ARG A 277 -17.658 20.201 -28.619 1.00102.19 C ANISOU 1795 CZ ARG A 277 13582 14650 10595 1186 599 -1864 C ATOM 1796 NH1 ARG A 277 -18.114 20.059 -27.381 1.00101.71 N ANISOU 1796 NH1 ARG A 277 13482 14911 10253 1255 768 -1920 N ATOM 1797 NH2 ARG A 277 -17.117 21.352 -28.993 1.00106.17 N ANISOU 1797 NH2 ARG A 277 14464 14810 11065 1134 476 -2085 N ATOM 1798 N ILE A 278 -18.249 13.145 -31.487 1.00 50.99 N ANISOU 1798 N ILE A 278 5190 8648 5538 828 653 -279 N ATOM 1799 CA ILE A 278 -17.107 12.419 -32.036 1.00 49.06 C ANISOU 1799 CA ILE A 278 4893 8313 5433 619 486 -76 C ATOM 1800 C ILE A 278 -17.440 11.864 -33.415 1.00 48.06 C ANISOU 1800 C ILE A 278 4576 8001 5685 650 441 -16 C ATOM 1801 O ILE A 278 -16.641 11.969 -34.354 1.00 53.28 O ANISOU 1801 O ILE A 278 5307 8463 6475 563 276 -13 O ATOM 1802 CB ILE A 278 -16.662 11.307 -31.068 1.00 51.00 C ANISOU 1802 CB ILE A 278 5011 8802 5564 478 539 199 C ATOM 1803 CG1 ILE A 278 -16.136 11.920 -29.770 1.00 57.34 C ANISOU 1803 CG1 ILE A 278 6036 9800 5949 431 527 125 C ATOM 1804 CG2 ILE A 278 -15.596 10.432 -31.709 1.00 47.00 C ANISOU 1804 CG2 ILE A 278 4404 8200 5255 317 380 414 C ATOM 1805 CD1 ILE A 278 -15.828 10.901 -28.697 1.00 65.15 C ANISOU 1805 CD1 ILE A 278 6935 11060 6759 338 586 404 C ATOM 1806 N THR A 279 -18.625 11.266 -33.559 1.00 48.07 N ANISOU 1806 N THR A 279 4324 8080 5860 760 594 20 N ATOM 1807 CA THR A 279 -19.038 10.744 -34.858 1.00 51.54 C ANISOU 1807 CA THR A 279 4572 8367 6642 791 542 44 C ATOM 1808 C THR A 279 -19.117 11.858 -35.894 1.00 47.86 C ANISOU 1808 C THR A 279 4293 7670 6222 936 402 -178 C ATOM 1809 O THR A 279 -18.729 11.669 -37.053 1.00 46.32 O ANISOU 1809 O THR A 279 4093 7290 6217 891 267 -153 O ATOM 1810 CB THR A 279 -20.385 10.031 -34.730 1.00 54.64 C ANISOU 1810 CB THR A 279 4650 8919 7192 870 735 74 C ATOM 1811 OG1 THR A 279 -20.292 9.018 -33.719 1.00 63.23 O ANISOU 1811 OG1 THR A 279 5617 10195 8212 719 888 308 O ATOM 1812 CG2 THR A 279 -20.781 9.386 -36.048 1.00 51.56 C ANISOU 1812 CG2 THR A 279 4044 8393 7152 870 664 88 C ATOM 1813 N ARG A 280 -19.607 13.031 -35.489 1.00 46.07 N ANISOU 1813 N ARG A 280 4257 7438 5808 1121 439 -395 N ATOM 1814 CA ARG A 280 -19.668 14.169 -36.397 1.00 47.43 C ANISOU 1814 CA ARG A 280 4673 7354 5995 1280 310 -588 C ATOM 1815 C ARG A 280 -18.275 14.585 -36.853 1.00 48.06 C ANISOU 1815 C ARG A 280 5030 7216 6014 1082 142 -564 C ATOM 1816 O ARG A 280 -18.056 14.850 -38.042 1.00 45.33 O ANISOU 1816 O ARG A 280 4781 6645 5798 1096 18 -586 O ATOM 1817 CB ARG A 280 -20.382 15.332 -35.711 1.00 48.92 C ANISOU 1817 CB ARG A 280 5047 7562 5978 1522 397 -823 C ATOM 1818 CG ARG A 280 -20.939 16.389 -36.639 1.00 63.28 C ANISOU 1818 CG ARG A 280 7052 9136 7854 1797 303 -1015 C ATOM 1819 CD ARG A 280 -21.715 17.411 -35.829 1.00 78.29 C ANISOU 1819 CD ARG A 280 9104 11079 9566 2070 419 -1249 C ATOM 1820 NE ARG A 280 -20.849 18.104 -34.878 1.00 82.48 N ANISOU 1820 NE ARG A 280 9971 11560 9809 1928 433 -1331 N ATOM 1821 CZ ARG A 280 -21.228 18.495 -33.666 1.00 84.32 C ANISOU 1821 CZ ARG A 280 10261 11966 9809 2021 590 -1470 C ATOM 1822 NH1 ARG A 280 -22.461 18.251 -33.242 1.00 86.38 N ANISOU 1822 NH1 ARG A 280 10249 12472 10100 2255 772 -1531 N ATOM 1823 NH2 ARG A 280 -20.371 19.122 -32.873 1.00 84.38 N ANISOU 1823 NH2 ARG A 280 10589 11923 9548 1866 572 -1563 N ATOM 1824 N MET A 281 -17.317 14.638 -35.923 1.00 41.46 N ANISOU 1824 N MET A 281 4314 6467 4973 886 138 -521 N ATOM 1825 CA MET A 281 -15.951 15.004 -36.287 1.00 49.30 C ANISOU 1825 CA MET A 281 5518 7300 5915 664 -11 -511 C ATOM 1826 C MET A 281 -15.314 13.951 -37.185 1.00 49.10 C ANISOU 1826 C MET A 281 5285 7245 6126 511 -88 -314 C ATOM 1827 O MET A 281 -14.569 14.289 -38.112 1.00 41.14 O ANISOU 1827 O MET A 281 4412 6040 5180 408 -198 -334 O ATOM 1828 CB MET A 281 -15.108 15.218 -35.031 1.00 49.22 C ANISOU 1828 CB MET A 281 5625 7450 5627 491 -16 -522 C ATOM 1829 CG MET A 281 -14.931 16.679 -34.656 1.00 69.05 C ANISOU 1829 CG MET A 281 8520 9812 7903 507 -42 -780 C ATOM 1830 SD MET A 281 -14.024 17.598 -35.916 1.00 74.17 S ANISOU 1830 SD MET A 281 9469 10080 8634 362 -194 -871 S ATOM 1831 CE MET A 281 -12.413 16.825 -35.799 1.00 79.13 C ANISOU 1831 CE MET A 281 9938 10863 9265 -6 -308 -700 C ATOM 1832 N VAL A 282 -15.591 12.672 -36.922 1.00 50.89 N ANISOU 1832 N VAL A 282 5200 7654 6481 490 -16 -127 N ATOM 1833 CA VAL A 282 -15.078 11.607 -37.782 1.00 44.87 C ANISOU 1833 CA VAL A 282 4243 6843 5963 376 -74 41 C ATOM 1834 C VAL A 282 -15.591 11.785 -39.204 1.00 42.27 C ANISOU 1834 C VAL A 282 3918 6310 5831 485 -127 -43 C ATOM 1835 O VAL A 282 -14.828 11.704 -40.175 1.00 45.91 O ANISOU 1835 O VAL A 282 4426 6627 6390 382 -224 -19 O ATOM 1836 CB VAL A 282 -15.458 10.228 -37.216 1.00 43.21 C ANISOU 1836 CB VAL A 282 3735 6818 5864 354 35 249 C ATOM 1837 CG1 VAL A 282 -15.256 9.153 -38.272 1.00 42.99 C ANISOU 1837 CG1 VAL A 282 3513 6686 6135 293 -5 372 C ATOM 1838 CG2 VAL A 282 -14.636 9.921 -35.974 1.00 39.05 C ANISOU 1838 CG2 VAL A 282 3225 6481 5132 229 41 386 C ATOM 1839 N LEU A 283 -16.894 12.036 -39.349 1.00 43.45 N ANISOU 1839 N LEU A 283 4010 6469 6028 703 -67 -148 N ATOM 1840 CA LEU A 283 -17.464 12.209 -40.679 1.00 47.70 C ANISOU 1840 CA LEU A 283 4545 6849 6728 838 -145 -230 C ATOM 1841 C LEU A 283 -16.869 13.417 -41.391 1.00 47.05 C ANISOU 1841 C LEU A 283 4827 6520 6530 850 -261 -344 C ATOM 1842 O LEU A 283 -16.700 13.390 -42.614 1.00 41.03 O ANISOU 1842 O LEU A 283 4112 5606 5873 850 -353 -342 O ATOM 1843 CB LEU A 283 -18.985 12.331 -40.587 1.00 49.45 C ANISOU 1843 CB LEU A 283 4611 7173 7005 1093 -71 -340 C ATOM 1844 CG LEU A 283 -19.710 11.086 -40.066 1.00 57.36 C ANISOU 1844 CG LEU A 283 5231 8402 8161 1052 67 -231 C ATOM 1845 CD1 LEU A 283 -21.192 11.360 -39.867 1.00 50.34 C ANISOU 1845 CD1 LEU A 283 4168 7655 7302 1294 158 -372 C ATOM 1846 CD2 LEU A 283 -19.501 9.905 -41.002 1.00 60.15 C ANISOU 1846 CD2 LEU A 283 5379 8703 8774 917 14 -115 C ATOM 1847 N VAL A 284 -16.524 14.470 -40.648 1.00 43.86 N ANISOU 1847 N VAL A 284 4700 6065 5898 842 -250 -444 N ATOM 1848 CA VAL A 284 -15.973 15.667 -41.277 1.00 41.94 C ANISOU 1848 CA VAL A 284 4844 5548 5546 824 -339 -549 C ATOM 1849 C VAL A 284 -14.565 15.402 -41.803 1.00 40.71 C ANISOU 1849 C VAL A 284 4735 5318 5414 526 -402 -451 C ATOM 1850 O VAL A 284 -14.264 15.686 -42.968 1.00 41.57 O ANISOU 1850 O VAL A 284 4991 5231 5573 500 -468 -453 O ATOM 1851 CB VAL A 284 -15.998 16.856 -40.300 1.00 47.01 C ANISOU 1851 CB VAL A 284 5782 6131 5946 877 -300 -710 C ATOM 1852 CG1 VAL A 284 -15.199 18.021 -40.868 1.00 41.31 C ANISOU 1852 CG1 VAL A 284 5486 5096 5116 768 -377 -798 C ATOM 1853 CG2 VAL A 284 -17.431 17.288 -40.030 1.00 50.78 C ANISOU 1853 CG2 VAL A 284 6242 6642 6410 1229 -236 -840 C ATOM 1854 N VAL A 285 -13.683 14.852 -40.962 1.00 34.11 N ANISOU 1854 N VAL A 285 3770 4657 4534 308 -382 -363 N ATOM 1855 CA VAL A 285 -12.294 14.685 -41.388 1.00 37.45 C ANISOU 1855 CA VAL A 285 4212 5043 4974 36 -441 -296 C ATOM 1856 C VAL A 285 -12.192 13.673 -42.524 1.00 38.88 C ANISOU 1856 C VAL A 285 4179 5209 5386 24 -460 -179 C ATOM 1857 O VAL A 285 -11.316 13.793 -43.390 1.00 37.18 O ANISOU 1857 O VAL A 285 4045 4882 5200 -129 -498 -170 O ATOM 1858 CB VAL A 285 -11.383 14.300 -40.203 1.00 41.52 C ANISOU 1858 CB VAL A 285 4607 5786 5383 -158 -444 -231 C ATOM 1859 CG1 VAL A 285 -11.556 15.280 -39.048 1.00 47.21 C ANISOU 1859 CG1 VAL A 285 5547 6540 5849 -142 -425 -376 C ATOM 1860 CG2 VAL A 285 -11.631 12.866 -39.750 1.00 46.57 C ANISOU 1860 CG2 VAL A 285 4887 6652 6154 -111 -402 -47 C ATOM 1861 N VAL A 286 -13.080 12.678 -42.557 1.00 38.31 N ANISOU 1861 N VAL A 286 3835 5246 5475 170 -422 -104 N ATOM 1862 CA VAL A 286 -13.059 11.706 -43.646 1.00 41.29 C ANISOU 1862 CA VAL A 286 4025 5592 6072 162 -441 -28 C ATOM 1863 C VAL A 286 -13.629 12.317 -44.919 1.00 43.62 C ANISOU 1863 C VAL A 286 4495 5694 6384 297 -498 -129 C ATOM 1864 O VAL A 286 -13.077 12.133 -46.011 1.00 42.84 O ANISOU 1864 O VAL A 286 4434 5497 6347 216 -536 -113 O ATOM 1865 CB VAL A 286 -13.819 10.429 -43.234 1.00 41.63 C ANISOU 1865 CB VAL A 286 3735 5792 6289 236 -377 75 C ATOM 1866 CG1 VAL A 286 -13.973 9.487 -44.422 1.00 40.61 C ANISOU 1866 CG1 VAL A 286 3438 5599 6390 243 -401 105 C ATOM 1867 CG2 VAL A 286 -13.095 9.726 -42.092 1.00 37.79 C ANISOU 1867 CG2 VAL A 286 3107 5477 5774 102 -334 222 C ATOM 1868 N ALA A 287 -14.736 13.055 -44.803 1.00 37.74 N ANISOU 1868 N ALA A 287 3865 4906 5570 523 -505 -234 N ATOM 1869 CA ALA A 287 -15.328 13.687 -45.976 1.00 41.01 C ANISOU 1869 CA ALA A 287 4463 5144 5973 699 -586 -319 C ATOM 1870 C ALA A 287 -14.393 14.731 -46.574 1.00 38.64 C ANISOU 1870 C ALA A 287 4552 4611 5517 578 -623 -344 C ATOM 1871 O ALA A 287 -14.294 14.851 -47.800 1.00 42.37 O ANISOU 1871 O ALA A 287 5154 4948 5996 595 -680 -339 O ATOM 1872 CB ALA A 287 -16.674 14.316 -45.617 1.00 38.91 C ANISOU 1872 CB ALA A 287 4227 4895 5660 1002 -590 -431 C ATOM 1873 N VAL A 288 -13.700 15.495 -45.727 1.00 37.96 N ANISOU 1873 N VAL A 288 4666 4478 5279 436 -585 -376 N ATOM 1874 CA VAL A 288 -12.763 16.495 -46.233 1.00 41.92 C ANISOU 1874 CA VAL A 288 5538 4747 5642 260 -597 -405 C ATOM 1875 C VAL A 288 -11.639 15.823 -47.013 1.00 41.35 C ANISOU 1875 C VAL A 288 5353 4707 5651 4 -586 -313 C ATOM 1876 O VAL A 288 -11.283 16.255 -48.116 1.00 37.23 O ANISOU 1876 O VAL A 288 5056 4005 5083 -54 -596 -307 O ATOM 1877 CB VAL A 288 -12.218 17.358 -45.082 1.00 40.95 C ANISOU 1877 CB VAL A 288 5612 4593 5353 116 -561 -486 C ATOM 1878 CG1 VAL A 288 -10.996 18.137 -45.542 1.00 42.10 C ANISOU 1878 CG1 VAL A 288 6055 4545 5397 -182 -552 -503 C ATOM 1879 CG2 VAL A 288 -13.294 18.311 -44.587 1.00 39.17 C ANISOU 1879 CG2 VAL A 288 5616 4249 5019 396 -562 -614 C ATOM 1880 N PHE A 289 -11.069 14.749 -46.458 1.00 36.73 N ANISOU 1880 N PHE A 289 4426 4352 5179 -135 -557 -235 N ATOM 1881 CA PHE A 289 -10.011 14.038 -47.169 1.00 38.18 C ANISOU 1881 CA PHE A 289 4464 4586 5458 -338 -538 -162 C ATOM 1882 C PHE A 289 -10.509 13.517 -48.511 1.00 37.36 C ANISOU 1882 C PHE A 289 4321 4414 5458 -210 -559 -146 C ATOM 1883 O PHE A 289 -9.813 13.628 -49.528 1.00 36.96 O ANISOU 1883 O PHE A 289 4384 4275 5384 -338 -538 -139 O ATOM 1884 CB PHE A 289 -9.472 12.885 -46.319 1.00 36.26 C ANISOU 1884 CB PHE A 289 3851 4593 5334 -430 -518 -70 C ATOM 1885 CG PHE A 289 -8.263 12.210 -46.916 1.00 35.27 C ANISOU 1885 CG PHE A 289 3562 4533 5305 -622 -494 -13 C ATOM 1886 CD1 PHE A 289 -8.405 11.201 -47.859 1.00 39.24 C ANISOU 1886 CD1 PHE A 289 3888 5040 5981 -550 -480 29 C ATOM 1887 CD2 PHE A 289 -6.986 12.594 -46.544 1.00 33.71 C ANISOU 1887 CD2 PHE A 289 3377 4405 5026 -874 -483 -24 C ATOM 1888 CE1 PHE A 289 -7.297 10.590 -48.416 1.00 34.16 C ANISOU 1888 CE1 PHE A 289 3095 4459 5427 -698 -441 62 C ATOM 1889 CE2 PHE A 289 -5.872 11.984 -47.098 1.00 43.23 C ANISOU 1889 CE2 PHE A 289 4395 5701 6329 -1030 -450 14 C ATOM 1890 CZ PHE A 289 -6.030 10.981 -48.037 1.00 33.37 C ANISOU 1890 CZ PHE A 289 2983 4446 5252 -928 -421 58 C ATOM 1891 N ILE A 290 -11.718 12.954 -48.535 1.00 36.80 N ANISOU 1891 N ILE A 290 4088 4401 5493 28 -595 -152 N ATOM 1892 CA ILE A 290 -12.242 12.362 -49.760 1.00 40.36 C ANISOU 1892 CA ILE A 290 4466 4823 6044 144 -638 -161 C ATOM 1893 C ILE A 290 -12.568 13.441 -50.787 1.00 43.77 C ANISOU 1893 C ILE A 290 5269 5049 6312 255 -699 -216 C ATOM 1894 O ILE A 290 -12.258 13.296 -51.974 1.00 42.23 O ANISOU 1894 O ILE A 290 5159 4790 6096 216 -712 -210 O ATOM 1895 CB ILE A 290 -13.466 11.485 -49.440 1.00 40.87 C ANISOU 1895 CB ILE A 290 4232 5024 6275 335 -662 -171 C ATOM 1896 CG1 ILE A 290 -13.027 10.233 -48.680 1.00 45.01 C ANISOU 1896 CG1 ILE A 290 4422 5708 6971 207 -592 -78 C ATOM 1897 CG2 ILE A 290 -14.216 11.112 -50.713 1.00 40.33 C ANISOU 1897 CG2 ILE A 290 4127 4923 6273 480 -744 -229 C ATOM 1898 CD1 ILE A 290 -14.174 9.325 -48.289 1.00 51.52 C ANISOU 1898 CD1 ILE A 290 4998 6651 7926 326 -564 -69 C ATOM 1899 N VAL A 291 -13.188 14.540 -50.352 1.00 37.21 N ANISOU 1899 N VAL A 291 4686 4103 5347 408 -733 -268 N ATOM 1900 CA VAL A 291 -13.561 15.599 -51.287 1.00 44.30 C ANISOU 1900 CA VAL A 291 5977 4774 6082 559 -802 -298 C ATOM 1901 C VAL A 291 -12.322 16.260 -51.880 1.00 45.60 C ANISOU 1901 C VAL A 291 6465 4757 6104 294 -737 -254 C ATOM 1902 O VAL A 291 -12.290 16.599 -53.070 1.00 42.97 O ANISOU 1902 O VAL A 291 6380 4282 5664 328 -767 -228 O ATOM 1903 CB VAL A 291 -14.476 16.625 -50.590 1.00 45.98 C ANISOU 1903 CB VAL A 291 6387 4885 6198 809 -842 -370 C ATOM 1904 CG1 VAL A 291 -14.599 17.892 -51.424 1.00 42.39 C ANISOU 1904 CG1 VAL A 291 6430 4127 5548 938 -900 -376 C ATOM 1905 CG2 VAL A 291 -15.851 16.022 -50.334 1.00 45.71 C ANISOU 1905 CG2 VAL A 291 6029 5041 6296 1103 -906 -426 C ATOM 1906 N CYS A 292 -11.276 16.438 -51.070 1.00 42.73 N ANISOU 1906 N CYS A 292 6096 4415 5725 12 -645 -246 N ATOM 1907 CA CYS A 292 -10.102 17.178 -51.520 1.00 43.85 C ANISOU 1907 CA CYS A 292 6533 4392 5734 -280 -564 -224 C ATOM 1908 C CYS A 292 -9.166 16.339 -52.383 1.00 43.09 C ANISOU 1908 C CYS A 292 6253 4412 5706 -489 -495 -170 C ATOM 1909 O CYS A 292 -8.506 16.886 -53.275 1.00 38.94 O ANISOU 1909 O CYS A 292 6000 3741 5056 -656 -428 -143 O ATOM 1910 CB CYS A 292 -9.333 17.730 -50.318 1.00 40.86 C ANISOU 1910 CB CYS A 292 6196 4020 5310 -518 -507 -268 C ATOM 1911 SG CYS A 292 -10.142 19.125 -49.480 1.00 45.63 S ANISOU 1911 SG CYS A 292 7192 4382 5762 -337 -546 -368 S ATOM 1912 N TRP A 293 -9.086 15.030 -52.141 1.00 36.06 N ANISOU 1912 N TRP A 293 4925 3770 5008 -483 -495 -154 N ATOM 1913 CA TRP A 293 -8.083 14.191 -52.785 1.00 38.31 C ANISOU 1913 CA TRP A 293 5003 4176 5376 -675 -414 -124 C ATOM 1914 C TRP A 293 -8.622 13.276 -53.875 1.00 40.47 C ANISOU 1914 C TRP A 293 5152 4495 5732 -511 -448 -128 C ATOM 1915 O TRP A 293 -7.863 12.913 -54.777 1.00 39.22 O ANISOU 1915 O TRP A 293 4972 4363 5565 -646 -368 -125 O ATOM 1916 CB TRP A 293 -7.356 13.332 -51.741 1.00 31.17 C ANISOU 1916 CB TRP A 293 3710 3502 4630 -808 -382 -103 C ATOM 1917 CG TRP A 293 -6.184 14.025 -51.110 1.00 35.04 C ANISOU 1917 CG TRP A 293 4266 4015 5034 -1102 -320 -115 C ATOM 1918 CD1 TRP A 293 -6.004 14.298 -49.781 1.00 32.70 C ANISOU 1918 CD1 TRP A 293 3903 3804 4716 -1169 -352 -131 C ATOM 1919 CD2 TRP A 293 -5.030 14.540 -51.785 1.00 37.45 C ANISOU 1919 CD2 TRP A 293 4704 4274 5251 -1391 -213 -128 C ATOM 1920 NE1 TRP A 293 -4.807 14.946 -49.592 1.00 36.60 N ANISOU 1920 NE1 TRP A 293 4469 4312 5124 -1486 -294 -168 N ATOM 1921 CE2 TRP A 293 -4.191 15.107 -50.806 1.00 37.51 C ANISOU 1921 CE2 TRP A 293 4697 4347 5209 -1638 -197 -164 C ATOM 1922 CE3 TRP A 293 -4.624 14.574 -53.124 1.00 38.20 C ANISOU 1922 CE3 TRP A 293 4927 4296 5291 -1479 -120 -120 C ATOM 1923 CZ2 TRP A 293 -2.972 15.698 -51.122 1.00 42.29 C ANISOU 1923 CZ2 TRP A 293 5382 4947 5739 -1986 -90 -198 C ATOM 1924 CZ3 TRP A 293 -3.416 15.167 -53.436 1.00 39.60 C ANISOU 1924 CZ3 TRP A 293 5202 4464 5380 -1817 10 -137 C ATOM 1925 CH2 TRP A 293 -2.602 15.716 -52.439 1.00 44.36 C ANISOU 1925 CH2 TRP A 293 5758 5135 5964 -2077 26 -179 C ATOM 1926 N THR A 294 -9.894 12.878 -53.818 1.00 35.53 N ANISOU 1926 N THR A 294 4424 3895 5182 -237 -557 -154 N ATOM 1927 CA THR A 294 -10.429 11.995 -54.855 1.00 38.74 C ANISOU 1927 CA THR A 294 4701 4352 5664 -104 -606 -189 C ATOM 1928 C THR A 294 -10.381 12.610 -56.250 1.00 43.28 C ANISOU 1928 C THR A 294 5620 4793 6031 -84 -619 -198 C ATOM 1929 O THR A 294 -9.973 11.905 -57.190 1.00 37.41 O ANISOU 1929 O THR A 294 4798 4109 5305 -146 -577 -223 O ATOM 1930 CB THR A 294 -11.859 11.566 -54.504 1.00 39.95 C ANISOU 1930 CB THR A 294 4674 4572 5935 161 -726 -233 C ATOM 1931 OG1 THR A 294 -11.900 11.060 -53.165 1.00 42.89 O ANISOU 1931 OG1 THR A 294 4769 5062 6463 129 -688 -201 O ATOM 1932 CG2 THR A 294 -12.339 10.483 -55.462 1.00 39.76 C ANISOU 1932 CG2 THR A 294 4454 4626 6026 246 -779 -297 C ATOM 1933 N PRO A 295 -10.776 13.874 -56.470 1.00 38.48 N ANISOU 1933 N PRO A 295 5412 3996 5211 12 -672 -176 N ATOM 1934 CA PRO A 295 -10.812 14.378 -57.857 1.00 41.16 C ANISOU 1934 CA PRO A 295 6101 4210 5329 60 -695 -158 C ATOM 1935 C PRO A 295 -9.478 14.299 -58.581 1.00 40.37 C ANISOU 1935 C PRO A 295 6088 4109 5144 -241 -522 -124 C ATOM 1936 O PRO A 295 -9.428 13.789 -59.706 1.00 37.29 O ANISOU 1936 O PRO A 295 5707 3774 4688 -220 -516 -148 O ATOM 1937 CB PRO A 295 -11.291 15.826 -57.684 1.00 34.57 C ANISOU 1937 CB PRO A 295 5705 3131 4300 192 -755 -113 C ATOM 1938 CG PRO A 295 -12.081 15.805 -56.429 1.00 39.83 C ANISOU 1938 CG PRO A 295 6162 3857 5114 357 -828 -161 C ATOM 1939 CD PRO A 295 -11.336 14.865 -55.531 1.00 37.19 C ANISOU 1939 CD PRO A 295 5423 3716 4990 128 -723 -173 C ATOM 1940 N ILE A 296 -8.389 14.780 -57.974 1.00 33.55 N ANISOU 1940 N ILE A 296 5269 3205 4273 -529 -378 -87 N ATOM 1941 CA ILE A 296 -7.124 14.784 -58.702 1.00 32.57 C ANISOU 1941 CA ILE A 296 5212 3101 4061 -827 -194 -65 C ATOM 1942 C ILE A 296 -6.616 13.361 -58.916 1.00 45.92 C ANISOU 1942 C ILE A 296 6463 5038 5948 -876 -132 -126 C ATOM 1943 O ILE A 296 -6.043 13.054 -59.969 1.00 40.89 O ANISOU 1943 O ILE A 296 5861 4449 5226 -974 -21 -143 O ATOM 1944 CB ILE A 296 -6.080 15.674 -57.997 1.00 33.96 C ANISOU 1944 CB ILE A 296 5516 3196 4193 -1150 -61 -33 C ATOM 1945 CG1 ILE A 296 -4.809 15.778 -58.845 1.00 35.80 C ANISOU 1945 CG1 ILE A 296 5824 3458 4319 -1476 152 -14 C ATOM 1946 CG2 ILE A 296 -5.763 15.163 -56.589 1.00 39.02 C ANISOU 1946 CG2 ILE A 296 5760 4010 5058 -1219 -79 -72 C ATOM 1947 CD1 ILE A 296 -5.063 16.207 -60.288 1.00 35.41 C ANISOU 1947 CD1 ILE A 296 6182 3262 4009 -1418 188 42 C ATOM 1948 N HIS A 297 -6.844 12.460 -57.956 1.00 35.20 N ANISOU 1948 N HIS A 297 4707 3826 4843 -796 -193 -158 N ATOM 1949 CA HIS A 297 -6.381 11.086 -58.130 1.00 37.71 C ANISOU 1949 CA HIS A 297 4636 4330 5364 -816 -135 -210 C ATOM 1950 C HIS A 297 -7.130 10.381 -59.252 1.00 38.29 C ANISOU 1950 C HIS A 297 4711 4413 5423 -625 -203 -284 C ATOM 1951 O HIS A 297 -6.526 9.644 -60.039 1.00 40.38 O ANISOU 1951 O HIS A 297 4864 4764 5714 -690 -102 -344 O ATOM 1952 CB HIS A 297 -6.510 10.312 -56.820 1.00 31.05 C ANISOU 1952 CB HIS A 297 3419 3603 4774 -762 -188 -198 C ATOM 1953 CG HIS A 297 -5.345 10.506 -55.905 1.00 37.83 C ANISOU 1953 CG HIS A 297 4140 4555 5680 -989 -98 -157 C ATOM 1954 ND1 HIS A 297 -4.087 10.026 -56.197 1.00 39.40 N ANISOU 1954 ND1 HIS A 297 4145 4886 5941 -1169 40 -175 N ATOM 1955 CD2 HIS A 297 -5.236 11.152 -54.720 1.00 38.14 C ANISOU 1955 CD2 HIS A 297 4197 4594 5701 -1063 -132 -117 C ATOM 1956 CE1 HIS A 297 -3.255 10.359 -55.227 1.00 43.11 C ANISOU 1956 CE1 HIS A 297 4496 5449 6434 -1346 69 -144 C ATOM 1957 NE2 HIS A 297 -3.928 11.041 -54.318 1.00 42.96 N ANISOU 1957 NE2 HIS A 297 4616 5348 6358 -1294 -37 -111 N ATOM 1958 N ILE A 298 -8.443 10.593 -59.346 1.00 37.36 N ANISOU 1958 N ILE A 298 4708 4227 5262 -385 -376 -299 N ATOM 1959 CA ILE A 298 -9.211 9.972 -60.419 1.00 40.86 C ANISOU 1959 CA ILE A 298 5149 4703 5674 -210 -474 -392 C ATOM 1960 C ILE A 298 -8.865 10.613 -61.757 1.00 43.37 C ANISOU 1960 C ILE A 298 5843 4954 5682 -257 -422 -384 C ATOM 1961 O ILE A 298 -8.766 9.928 -62.782 1.00 46.82 O ANISOU 1961 O ILE A 298 6252 5467 6072 -244 -398 -474 O ATOM 1962 CB ILE A 298 -10.718 10.057 -60.114 1.00 46.71 C ANISOU 1962 CB ILE A 298 5863 5430 6456 59 -685 -422 C ATOM 1963 CG1 ILE A 298 -11.033 9.332 -58.803 1.00 49.51 C ANISOU 1963 CG1 ILE A 298 5839 5865 7106 76 -696 -421 C ATOM 1964 CG2 ILE A 298 -11.533 9.474 -61.258 1.00 41.76 C ANISOU 1964 CG2 ILE A 298 5226 4862 5778 226 -816 -541 C ATOM 1965 CD1 ILE A 298 -10.584 7.888 -58.780 1.00 48.01 C ANISOU 1965 CD1 ILE A 298 5299 5778 7166 -10 -618 -477 C ATOM 1966 N TYR A 299 -8.663 11.933 -61.765 1.00 39.57 N ANISOU 1966 N TYR A 299 5744 4317 4974 -320 -392 -277 N ATOM 1967 CA TYR A 299 -8.295 12.629 -62.994 1.00 44.17 C ANISOU 1967 CA TYR A 299 6740 4810 5233 -387 -318 -230 C ATOM 1968 C TYR A 299 -6.982 12.097 -63.557 1.00 43.45 C ANISOU 1968 C TYR A 299 6540 4834 5135 -654 -78 -264 C ATOM 1969 O TYR A 299 -6.859 11.879 -64.769 1.00 45.05 O ANISOU 1969 O TYR A 299 6890 5081 5147 -649 -27 -305 O ATOM 1970 CB TYR A 299 -8.197 14.130 -62.721 1.00 46.44 C ANISOU 1970 CB TYR A 299 7460 4865 5320 -450 -296 -96 C ATOM 1971 CG TYR A 299 -8.604 15.017 -63.877 1.00 47.76 C ANISOU 1971 CG TYR A 299 8148 4869 5131 -332 -350 -14 C ATOM 1972 CD1 TYR A 299 -8.254 14.704 -65.182 1.00 52.71 C ANISOU 1972 CD1 TYR A 299 8910 5568 5549 -382 -270 -26 C ATOM 1973 CD2 TYR A 299 -9.340 16.173 -63.655 1.00 50.45 C ANISOU 1973 CD2 TYR A 299 8863 4976 5328 -149 -480 80 C ATOM 1974 CE1 TYR A 299 -8.625 15.520 -66.235 1.00 60.66 C ANISOU 1974 CE1 TYR A 299 10425 6431 6192 -263 -327 74 C ATOM 1975 CE2 TYR A 299 -9.718 16.991 -64.698 1.00 52.74 C ANISOU 1975 CE2 TYR A 299 9659 5099 5281 -7 -545 183 C ATOM 1976 CZ TYR A 299 -9.357 16.662 -65.985 1.00 58.62 C ANISOU 1976 CZ TYR A 299 10543 5930 5802 -69 -472 190 C ATOM 1977 OH TYR A 299 -9.734 17.481 -67.021 1.00 65.76 O ANISOU 1977 OH TYR A 299 11980 6671 6334 84 -543 316 O ATOM 1978 N VAL A 300 -5.992 11.875 -62.689 1.00 39.62 N ANISOU 1978 N VAL A 300 5787 4422 4846 -877 68 -258 N ATOM 1979 CA VAL A 300 -4.701 11.364 -63.143 1.00 41.83 C ANISOU 1979 CA VAL A 300 5903 4843 5148 -1114 303 -304 C ATOM 1980 C VAL A 300 -4.859 9.974 -63.750 1.00 41.73 C ANISOU 1980 C VAL A 300 5606 4981 5267 -975 291 -446 C ATOM 1981 O VAL A 300 -4.248 9.655 -64.779 1.00 39.04 O ANISOU 1981 O VAL A 300 5309 4724 4802 -1057 446 -512 O ATOM 1982 CB VAL A 300 -3.689 11.374 -61.980 1.00 39.45 C ANISOU 1982 CB VAL A 300 5318 4623 5050 -1338 413 -279 C ATOM 1983 CG1 VAL A 300 -2.474 10.521 -62.309 1.00 45.05 C ANISOU 1983 CG1 VAL A 300 5708 5538 5870 -1498 619 -359 C ATOM 1984 CG2 VAL A 300 -3.260 12.802 -61.668 1.00 33.69 C ANISOU 1984 CG2 VAL A 300 4920 3740 4140 -1566 486 -176 C ATOM 1985 N ILE A 301 -5.694 9.131 -63.137 1.00 40.23 N ANISOU 1985 N ILE A 301 5141 4820 5325 -773 120 -503 N ATOM 1986 CA ILE A 301 -5.902 7.782 -63.657 1.00 44.41 C ANISOU 1986 CA ILE A 301 5417 5448 6008 -655 103 -652 C ATOM 1987 C ILE A 301 -6.592 7.829 -65.015 1.00 45.55 C ANISOU 1987 C ILE A 301 5836 5578 5891 -527 22 -737 C ATOM 1988 O ILE A 301 -6.216 7.102 -65.943 1.00 50.58 O ANISOU 1988 O ILE A 301 6431 6303 6486 -541 119 -867 O ATOM 1989 CB ILE A 301 -6.703 6.937 -62.649 1.00 44.34 C ANISOU 1989 CB ILE A 301 5085 5443 6320 -502 -51 -677 C ATOM 1990 CG1 ILE A 301 -5.907 6.746 -61.357 1.00 41.87 C ANISOU 1990 CG1 ILE A 301 4494 5176 6239 -617 33 -592 C ATOM 1991 CG2 ILE A 301 -7.084 5.591 -63.258 1.00 44.72 C ANISOU 1991 CG2 ILE A 301 4930 5538 6522 -386 -86 -846 C ATOM 1992 CD1 ILE A 301 -4.534 6.144 -61.564 1.00 54.72 C ANISOU 1992 CD1 ILE A 301 5917 6918 7955 -760 240 -635 C ATOM 1993 N ILE A 302 -7.611 8.680 -65.154 1.00 45.67 N ANISOU 1993 N ILE A 302 6139 5496 5719 -381 -165 -673 N ATOM 1994 CA ILE A 302 -8.360 8.740 -66.406 1.00 48.98 C ANISOU 1994 CA ILE A 302 6815 5926 5869 -222 -294 -747 C ATOM 1995 C ILE A 302 -7.469 9.226 -67.541 1.00 51.01 C ANISOU 1995 C ILE A 302 7400 6194 5787 -375 -99 -717 C ATOM 1996 O ILE A 302 -7.524 8.698 -68.658 1.00 50.19 O ANISOU 1996 O ILE A 302 7366 6185 5521 -326 -91 -843 O ATOM 1997 CB ILE A 302 -9.609 9.624 -66.240 1.00 48.51 C ANISOU 1997 CB ILE A 302 6982 5769 5683 2 -547 -669 C ATOM 1998 CG1 ILE A 302 -10.564 8.993 -65.226 1.00 55.47 C ANISOU 1998 CG1 ILE A 302 7494 6686 6896 149 -717 -732 C ATOM 1999 CG2 ILE A 302 -10.313 9.817 -67.575 1.00 48.96 C ANISOU 1999 CG2 ILE A 302 7339 5857 5409 180 -702 -723 C ATOM 2000 CD1 ILE A 302 -11.818 9.790 -64.998 1.00 50.89 C ANISOU 2000 CD1 ILE A 302 7063 6047 6227 396 -956 -683 C ATOM 2001 N LYS A 303 -6.624 10.226 -67.279 1.00 50.46 N ANISOU 2001 N LYS A 303 7540 6036 5598 -582 75 -560 N ATOM 2002 CA LYS A 303 -5.708 10.689 -68.315 1.00 54.03 C ANISOU 2002 CA LYS A 303 8291 6504 5733 -775 308 -519 C ATOM 2003 C LYS A 303 -4.666 9.640 -68.677 1.00 50.57 C ANISOU 2003 C LYS A 303 7542 6255 5416 -924 545 -668 C ATOM 2004 O LYS A 303 -4.126 9.681 -69.789 1.00 51.07 O ANISOU 2004 O LYS A 303 7807 6392 5206 -1019 722 -702 O ATOM 2005 CB LYS A 303 -5.013 11.983 -67.888 1.00 51.95 C ANISOU 2005 CB LYS A 303 8302 6089 5350 -1014 460 -329 C ATOM 2006 CG LYS A 303 -5.935 13.190 -67.821 1.00 61.59 C ANISOU 2006 CG LYS A 303 9963 7076 6361 -860 268 -175 C ATOM 2007 CD LYS A 303 -5.233 14.478 -68.245 1.00 75.40 C ANISOU 2007 CD LYS A 303 12206 8646 7798 -1102 466 3 C ATOM 2008 CE LYS A 303 -4.155 14.909 -67.260 1.00 81.93 C ANISOU 2008 CE LYS A 303 12890 9433 8807 -1445 673 49 C ATOM 2009 NZ LYS A 303 -2.834 14.262 -67.502 1.00 87.87 N ANISOU 2009 NZ LYS A 303 13339 10407 9640 -1741 968 -39 N ATOM 2010 N ALA A 304 -4.367 8.704 -67.774 1.00 46.29 N ANISOU 2010 N ALA A 304 6530 5793 5266 -929 561 -753 N ATOM 2011 CA ALA A 304 -3.456 7.624 -68.129 1.00 53.13 C ANISOU 2011 CA ALA A 304 7091 6825 6271 -1003 765 -910 C ATOM 2012 C ALA A 304 -4.120 6.590 -69.029 1.00 55.64 C ANISOU 2012 C ALA A 304 7373 7202 6566 -803 665 -1112 C ATOM 2013 O ALA A 304 -3.423 5.897 -69.778 1.00 57.36 O ANISOU 2013 O ALA A 304 7502 7541 6751 -848 856 -1262 O ATOM 2014 CB ALA A 304 -2.911 6.951 -66.871 1.00 47.34 C ANISOU 2014 CB ALA A 304 5893 6141 5953 -1040 798 -917 C ATOM 2015 N LEU A 305 -5.447 6.489 -68.993 1.00 55.18 N ANISOU 2015 N LEU A 305 7377 7071 6518 -588 375 -1140 N ATOM 2016 CA LEU A 305 -6.178 5.465 -69.728 1.00 55.74 C ANISOU 2016 CA LEU A 305 7373 7198 6607 -418 242 -1359 C ATOM 2017 C LEU A 305 -6.718 5.945 -71.067 1.00 64.03 C ANISOU 2017 C LEU A 305 8834 8286 7209 -333 150 -1400 C ATOM 2018 O LEU A 305 -6.627 5.215 -72.057 1.00 65.97 O ANISOU 2018 O LEU A 305 9094 8634 7335 -303 200 -1601 O ATOM 2019 CB LEU A 305 -7.339 4.937 -68.880 1.00 49.70 C ANISOU 2019 CB LEU A 305 6366 6370 6149 -252 -24 -1395 C ATOM 2020 CG LEU A 305 -6.953 4.135 -67.637 1.00 54.60 C ANISOU 2020 CG LEU A 305 6567 6960 7218 -294 41 -1384 C ATOM 2021 CD1 LEU A 305 -8.169 3.896 -66.759 1.00 50.28 C ANISOU 2021 CD1 LEU A 305 5851 6347 6908 -160 -202 -1367 C ATOM 2022 CD2 LEU A 305 -6.312 2.813 -68.041 1.00 56.37 C ANISOU 2022 CD2 LEU A 305 6554 7235 7629 -308 194 -1586 C ATOM 2023 N ILE A 306 -7.290 7.150 -71.124 1.00 58.11 N ANISOU 2023 N ILE A 306 8434 7451 6196 -274 10 -1218 N ATOM 2024 CA ILE A 306 -7.920 7.655 -72.335 1.00 67.25 C ANISOU 2024 CA ILE A 306 10004 8640 6909 -144 -129 -1224 C ATOM 2025 C ILE A 306 -7.352 9.028 -72.669 1.00 72.12 C ANISOU 2025 C ILE A 306 11084 9161 7159 -271 21 -978 C ATOM 2026 O ILE A 306 -6.737 9.696 -71.836 1.00 72.87 O ANISOU 2026 O ILE A 306 11175 9142 7371 -437 163 -810 O ATOM 2027 CB ILE A 306 -9.457 7.736 -72.206 1.00 74.13 C ANISOU 2027 CB ILE A 306 10879 9492 7795 133 -518 -1252 C ATOM 2028 CG1 ILE A 306 -9.855 8.930 -71.339 1.00 76.87 C ANISOU 2028 CG1 ILE A 306 11383 9676 8150 194 -621 -1010 C ATOM 2029 CG2 ILE A 306 -10.018 6.455 -71.612 1.00 78.55 C ANISOU 2029 CG2 ILE A 306 10955 10107 8785 198 -640 -1463 C ATOM 2030 CD1 ILE A 306 -11.348 9.085 -71.169 1.00 82.85 C ANISOU 2030 CD1 ILE A 306 12114 10438 8928 489 -988 -1037 C ATOM 2031 N THR A 307 -7.567 9.438 -73.918 1.00 64.55 N ANISOU 2031 N THR A 307 10544 8245 5738 -200 -13 -962 N ATOM 2032 CA THR A 307 -7.230 10.774 -74.393 1.00 70.31 C ANISOU 2032 CA THR A 307 11807 8849 6058 -288 96 -708 C ATOM 2033 C THR A 307 -8.504 11.612 -74.415 1.00 81.35 C ANISOU 2033 C THR A 307 13515 10119 7273 7 -259 -574 C ATOM 2034 O THR A 307 -9.489 11.228 -75.052 1.00 93.09 O ANISOU 2034 O THR A 307 15029 11722 8620 268 -541 -698 O ATOM 2035 CB THR A 307 -6.599 10.718 -75.786 1.00 84.71 C ANISOU 2035 CB THR A 307 13938 10805 7444 -394 311 -747 C ATOM 2036 OG1 THR A 307 -5.287 10.145 -75.702 1.00 93.33 O ANISOU 2036 OG1 THR A 307 14755 12005 8701 -678 688 -844 O ATOM 2037 CG2 THR A 307 -6.506 12.111 -76.394 1.00 83.65 C ANISOU 2037 CG2 THR A 307 14436 10516 6831 -439 372 -461 C ATOM 2038 N ILE A 308 -8.485 12.747 -73.722 1.00 82.28 N ANISOU 2038 N ILE A 308 13858 10007 7397 -27 -251 -338 N ATOM 2039 CA ILE A 308 -9.685 13.563 -73.538 1.00 92.90 C ANISOU 2039 CA ILE A 308 15451 11208 8640 288 -582 -214 C ATOM 2040 C ILE A 308 -9.582 14.841 -74.365 1.00100.78 C ANISOU 2040 C ILE A 308 17135 12021 9137 308 -541 44 C ATOM 2041 O ILE A 308 -8.471 15.349 -74.575 1.00100.35 O ANISOU 2041 O ILE A 308 17330 11868 8931 -10 -206 178 O ATOM 2042 CB ILE A 308 -9.914 13.868 -72.048 1.00 95.81 C ANISOU 2042 CB ILE A 308 15568 11428 9409 296 -638 -162 C ATOM 2043 CG1 ILE A 308 -8.669 14.496 -71.420 1.00 95.56 C ANISOU 2043 CG1 ILE A 308 15619 11235 9456 -67 -303 -18 C ATOM 2044 CG2 ILE A 308 -10.292 12.599 -71.299 1.00 94.07 C ANISOU 2044 CG2 ILE A 308 14720 11384 9639 346 -738 -392 C ATOM 2045 CD1 ILE A 308 -8.806 14.752 -69.929 1.00 93.49 C ANISOU 2045 CD1 ILE A 308 15106 10851 9566 -83 -347 9 C ATOM 2046 N PRO A 309 -10.697 15.388 -74.858 1.00107.03 N ANISOU 2046 N PRO A 309 18246 12763 9657 671 -868 125 N ATOM 2047 CA PRO A 309 -10.630 16.560 -75.750 1.00112.90 C ANISOU 2047 CA PRO A 309 19699 13316 9881 726 -843 393 C ATOM 2048 C PRO A 309 -10.254 17.823 -74.990 1.00108.59 C ANISOU 2048 C PRO A 309 19483 12397 9378 598 -701 649 C ATOM 2049 O PRO A 309 -10.976 18.266 -74.095 1.00108.73 O ANISOU 2049 O PRO A 309 19432 12263 9618 812 -905 681 O ATOM 2050 CB PRO A 309 -12.049 16.648 -76.323 1.00115.55 C ANISOU 2050 CB PRO A 309 20175 13739 9992 1216 -1298 373 C ATOM 2051 CG PRO A 309 -12.903 16.028 -75.274 1.00111.10 C ANISOU 2051 CG PRO A 309 19027 13274 9911 1397 -1539 175 C ATOM 2052 CD PRO A 309 -12.079 14.902 -74.701 1.00106.47 C ANISOU 2052 CD PRO A 309 17894 12835 9726 1056 -1281 -33 C ATOM 2053 N GLU A 310 -9.131 18.418 -75.379 1.00107.44 N ANISOU 2053 N GLU A 310 19709 12106 9006 242 -341 820 N ATOM 2054 CA GLU A 310 -8.588 19.606 -74.723 1.00105.77 C ANISOU 2054 CA GLU A 310 19798 11529 8862 22 -148 1033 C ATOM 2055 C GLU A 310 -9.529 20.782 -74.941 1.00101.57 C ANISOU 2055 C GLU A 310 19618 10718 8256 372 -390 1182 C ATOM 2056 O GLU A 310 -9.535 21.402 -76.006 1.00110.79 O ANISOU 2056 O GLU A 310 21146 11806 9144 422 -358 1304 O ATOM 2057 CB GLU A 310 -7.199 19.913 -75.267 1.00114.60 C ANISOU 2057 CB GLU A 310 21076 12612 9856 -456 297 1115 C ATOM 2058 CG GLU A 310 -6.524 18.720 -75.921 1.00119.89 C ANISOU 2058 CG GLU A 310 21490 13652 10409 -648 498 944 C ATOM 2059 CD GLU A 310 -5.102 19.006 -76.361 1.00126.69 C ANISOU 2059 CD GLU A 310 22411 14516 11210 -1127 958 1002 C ATOM 2060 OE1 GLU A 310 -4.620 20.139 -76.152 1.00130.51 O ANISOU 2060 OE1 GLU A 310 23138 14709 11741 -1335 1109 1167 O ATOM 2061 OE2 GLU A 310 -4.464 18.089 -76.918 1.00127.18 O ANISOU 2061 OE2 GLU A 310 22249 14882 11193 -1289 1168 849 O ATOM 2062 N THR A 311 -10.338 21.088 -73.931 1.00 94.81 N ANISOU 2062 N THR A 311 18650 9727 7648 626 -623 1162 N ATOM 2063 CA THR A 311 -11.302 22.180 -73.979 1.00 94.75 C ANISOU 2063 CA THR A 311 18911 9473 7615 991 -847 1252 C ATOM 2064 C THR A 311 -11.094 23.084 -72.767 1.00 96.99 C ANISOU 2064 C THR A 311 19267 9434 8149 873 -749 1297 C ATOM 2065 O THR A 311 -10.239 22.830 -71.912 1.00 90.79 O ANISOU 2065 O THR A 311 18303 8631 7562 514 -533 1264 O ATOM 2066 CB THR A 311 -12.745 21.657 -74.016 1.00 94.98 C ANISOU 2066 CB THR A 311 18660 9722 7707 1503 -1269 1116 C ATOM 2067 OG1 THR A 311 -13.003 20.876 -72.840 1.00 95.98 O ANISOU 2067 OG1 THR A 311 18320 9985 8163 1534 -1373 962 O ATOM 2068 CG2 THR A 311 -12.964 20.795 -75.247 1.00 90.62 C ANISOU 2068 CG2 THR A 311 18029 9501 6903 1603 -1380 1036 C ATOM 2069 N THR A 312 -11.897 24.150 -72.692 1.00 82.29 N ANISOU 2069 N THR A 312 12253 11440 7575 -1037 -1276 2032 N ATOM 2070 CA THR A 312 -11.830 25.053 -71.548 1.00 79.96 C ANISOU 2070 CA THR A 312 11842 10874 7665 -913 -1132 2169 C ATOM 2071 C THR A 312 -12.268 24.359 -70.264 1.00 80.22 C ANISOU 2071 C THR A 312 11766 10708 8005 -835 -1203 2006 C ATOM 2072 O THR A 312 -11.645 24.537 -69.210 1.00 78.83 O ANISOU 2072 O THR A 312 11548 10323 8082 -757 -1035 1881 O ATOM 2073 CB THR A 312 -12.694 26.285 -71.812 1.00 78.08 C ANISOU 2073 CB THR A 312 11538 10636 7494 -868 -1187 2622 C ATOM 2074 OG1 THR A 312 -12.166 27.007 -72.931 1.00 86.91 O ANISOU 2074 OG1 THR A 312 12748 11927 8349 -936 -1091 2799 O ATOM 2075 CG2 THR A 312 -12.725 27.195 -70.594 1.00 74.44 C ANISOU 2075 CG2 THR A 312 10977 9870 7438 -728 -1043 2736 C ATOM 2076 N PHE A 313 -13.334 23.557 -70.332 1.00 80.17 N ANISOU 2076 N PHE A 313 11709 10773 7977 -864 -1458 2015 N ATOM 2077 CA PHE A 313 -13.826 22.892 -69.130 1.00 77.78 C ANISOU 2077 CA PHE A 313 11284 10298 7970 -789 -1528 1905 C ATOM 2078 C PHE A 313 -12.825 21.867 -68.612 1.00 71.21 C ANISOU 2078 C PHE A 313 10495 9387 7174 -804 -1426 1500 C ATOM 2079 O PHE A 313 -12.668 21.711 -67.397 1.00 67.17 O ANISOU 2079 O PHE A 313 9895 8687 6939 -714 -1348 1406 O ATOM 2080 CB PHE A 313 -15.178 22.232 -69.399 1.00 80.51 C ANISOU 2080 CB PHE A 313 11550 10748 8293 -839 -1835 2028 C ATOM 2081 CG PHE A 313 -15.814 21.640 -68.170 1.00 83.53 C ANISOU 2081 CG PHE A 313 11778 10964 8996 -756 -1905 1991 C ATOM 2082 CD1 PHE A 313 -16.499 22.445 -67.273 1.00 88.19 C ANISOU 2082 CD1 PHE A 313 12225 11414 9871 -608 -1855 2255 C ATOM 2083 CD2 PHE A 313 -15.726 20.281 -67.911 1.00 82.08 C ANISOU 2083 CD2 PHE A 313 11593 10761 8833 -817 -2009 1700 C ATOM 2084 CE1 PHE A 313 -17.085 21.906 -66.142 1.00 91.16 C ANISOU 2084 CE1 PHE A 313 12456 11663 10519 -523 -1900 2238 C ATOM 2085 CE2 PHE A 313 -16.309 19.736 -66.781 1.00 86.33 C ANISOU 2085 CE2 PHE A 313 11976 11159 9668 -743 -2068 1700 C ATOM 2086 CZ PHE A 313 -16.990 20.550 -65.895 1.00 90.23 C ANISOU 2086 CZ PHE A 313 12325 11543 10417 -595 -2010 1973 C ATOM 2087 N GLN A 314 -12.137 21.159 -69.511 1.00 67.12 N ANISOU 2087 N GLN A 314 10110 9015 6378 -909 -1418 1262 N ATOM 2088 CA GLN A 314 -11.115 20.213 -69.072 1.00 68.30 C ANISOU 2088 CA GLN A 314 10291 9081 6578 -907 -1298 892 C ATOM 2089 C GLN A 314 -9.958 20.935 -68.395 1.00 62.26 C ANISOU 2089 C GLN A 314 9506 8183 5967 -835 -1018 855 C ATOM 2090 O GLN A 314 -9.480 20.515 -67.335 1.00 55.39 O ANISOU 2090 O GLN A 314 8564 7154 5330 -775 -939 686 O ATOM 2091 CB GLN A 314 -10.598 19.392 -70.251 1.00 71.69 C ANISOU 2091 CB GLN A 314 10881 9693 6666 -1016 -1315 649 C ATOM 2092 CG GLN A 314 -9.351 18.594 -69.893 1.00 88.41 C ANISOU 2092 CG GLN A 314 13028 11723 8841 -992 -1127 295 C ATOM 2093 CD GLN A 314 -8.632 18.015 -71.089 1.00103.89 C ANISOU 2093 CD GLN A 314 15162 13860 10453 -1066 -1055 60 C ATOM 2094 OE1 GLN A 314 -9.244 17.714 -72.111 1.00115.45 O ANISOU 2094 OE1 GLN A 314 16739 15501 11625 -1159 -1227 60 O ATOM 2095 NE2 GLN A 314 -7.322 17.846 -70.963 1.00108.31 N ANISOU 2095 NE2 GLN A 314 15739 14380 11034 -1024 -800 -143 N ATOM 2096 N THR A 315 -9.489 22.024 -69.006 1.00 57.52 N ANISOU 2096 N THR A 315 8964 7651 5240 -850 -877 1025 N ATOM 2097 CA THR A 315 -8.383 22.785 -68.437 1.00 56.67 C ANISOU 2097 CA THR A 315 8835 7414 5284 -808 -629 1010 C ATOM 2098 C THR A 315 -8.737 23.320 -67.056 1.00 54.16 C ANISOU 2098 C THR A 315 8402 6863 5313 -705 -616 1100 C ATOM 2099 O THR A 315 -7.980 23.139 -66.094 1.00 56.24 O ANISOU 2099 O THR A 315 8618 6987 5764 -668 -503 926 O ATOM 2100 CB THR A 315 -8.006 23.931 -69.376 1.00 58.78 C ANISOU 2100 CB THR A 315 9169 7787 5376 -851 -507 1239 C ATOM 2101 OG1 THR A 315 -7.302 23.410 -70.511 1.00 63.55 O ANISOU 2101 OG1 THR A 315 9885 8607 5655 -933 -440 1095 O ATOM 2102 CG2 THR A 315 -7.144 24.957 -68.654 1.00 56.49 C ANISOU 2102 CG2 THR A 315 8832 7313 5317 -814 -295 1302 C ATOM 2103 N VAL A 316 -9.892 23.979 -66.940 1.00 51.39 N ANISOU 2103 N VAL A 316 8005 6477 5043 -653 -730 1377 N ATOM 2104 CA VAL A 316 -10.287 24.570 -65.666 1.00 55.78 C ANISOU 2104 CA VAL A 316 8470 6817 5907 -537 -695 1469 C ATOM 2105 C VAL A 316 -10.496 23.490 -64.612 1.00 47.82 C ANISOU 2105 C VAL A 316 7378 5732 5058 -488 -768 1265 C ATOM 2106 O VAL A 316 -10.053 23.631 -63.466 1.00 50.50 O ANISOU 2106 O VAL A 316 7675 5913 5601 -422 -664 1166 O ATOM 2107 CB VAL A 316 -11.545 25.439 -65.847 1.00 53.30 C ANISOU 2107 CB VAL A 316 8113 6491 5648 -472 -791 1823 C ATOM 2108 CG1 VAL A 316 -12.050 25.928 -64.498 1.00 54.04 C ANISOU 2108 CG1 VAL A 316 8119 6364 6049 -329 -745 1890 C ATOM 2109 CG2 VAL A 316 -11.243 26.615 -66.761 1.00 54.96 C ANISOU 2109 CG2 VAL A 316 8394 6743 5746 -511 -694 2053 C ATOM 2110 N SER A 317 -11.163 22.393 -64.979 1.00 50.47 N ANISOU 2110 N SER A 317 7692 6180 5306 -529 -957 1204 N ATOM 2111 CA SER A 317 -11.410 21.328 -64.012 1.00 49.23 C ANISOU 2111 CA SER A 317 7441 5947 5318 -489 -1036 1044 C ATOM 2112 C SER A 317 -10.113 20.673 -63.555 1.00 44.14 C ANISOU 2112 C SER A 317 6814 5247 4711 -507 -903 738 C ATOM 2113 O SER A 317 -10.006 20.259 -62.396 1.00 43.44 O ANISOU 2113 O SER A 317 6637 5044 4824 -442 -883 646 O ATOM 2114 CB SER A 317 -12.355 20.283 -64.605 1.00 50.53 C ANISOU 2114 CB SER A 317 7581 6228 5390 -556 -1279 1043 C ATOM 2115 OG SER A 317 -11.782 19.666 -65.742 1.00 58.12 O ANISOU 2115 OG SER A 317 8665 7328 6088 -675 -1304 860 O ATOM 2116 N TRP A 318 -9.119 20.582 -64.442 1.00 45.31 N ANISOU 2116 N TRP A 318 7062 5487 4666 -588 -804 600 N ATOM 2117 CA TRP A 318 -7.839 19.984 -64.073 1.00 46.89 C ANISOU 2117 CA TRP A 318 7258 5644 4916 -598 -663 334 C ATOM 2118 C TRP A 318 -7.142 20.799 -62.993 1.00 57.36 C ANISOU 2118 C TRP A 318 8529 6826 6440 -541 -507 354 C ATOM 2119 O TRP A 318 -6.685 20.253 -61.981 1.00 38.72 O ANISOU 2119 O TRP A 318 6088 4373 4249 -503 -479 210 O ATOM 2120 CB TRP A 318 -6.953 19.856 -65.312 1.00 48.57 C ANISOU 2120 CB TRP A 318 7583 5999 4871 -681 -560 219 C ATOM 2121 CG TRP A 318 -5.523 19.499 -65.027 1.00 51.15 C ANISOU 2121 CG TRP A 318 7889 6289 5257 -680 -372 0 C ATOM 2122 CD1 TRP A 318 -4.442 20.326 -65.110 1.00 48.66 C ANISOU 2122 CD1 TRP A 318 7579 5972 4939 -699 -171 29 C ATOM 2123 CD2 TRP A 318 -5.018 18.219 -64.627 1.00 48.60 C ANISOU 2123 CD2 TRP A 318 7517 5922 5028 -662 -369 -257 C ATOM 2124 NE1 TRP A 318 -3.296 19.641 -64.791 1.00 48.89 N ANISOU 2124 NE1 TRP A 318 7554 5975 5048 -692 -45 -187 N ATOM 2125 CE2 TRP A 318 -3.622 18.346 -64.488 1.00 48.21 C ANISOU 2125 CE2 TRP A 318 7435 5858 5023 -661 -158 -365 C ATOM 2126 CE3 TRP A 318 -5.611 16.977 -64.376 1.00 47.40 C ANISOU 2126 CE3 TRP A 318 7332 5730 4948 -648 -526 -389 C ATOM 2127 CZ2 TRP A 318 -2.809 17.280 -64.103 1.00 49.10 C ANISOU 2127 CZ2 TRP A 318 7480 5924 5251 -632 -95 -593 C ATOM 2128 CZ3 TRP A 318 -4.803 15.922 -63.994 1.00 42.95 C ANISOU 2128 CZ3 TRP A 318 6714 5101 4502 -622 -461 -623 C ATOM 2129 CH2 TRP A 318 -3.418 16.079 -63.863 1.00 46.58 C ANISOU 2129 CH2 TRP A 318 7139 5554 5004 -607 -244 -720 C ATOM 2130 N HIS A 319 -7.051 22.115 -63.188 1.00 40.89 N ANISOU 2130 N HIS A 319 6486 4712 4339 -543 -414 537 N ATOM 2131 CA HIS A 319 -6.388 22.947 -62.193 1.00 48.50 C ANISOU 2131 CA HIS A 319 7418 5521 5488 -510 -282 540 C ATOM 2132 C HIS A 319 -7.219 23.072 -60.924 1.00 46.14 C ANISOU 2132 C HIS A 319 7051 5091 5390 -404 -350 598 C ATOM 2133 O HIS A 319 -6.659 23.242 -59.836 1.00 43.27 O ANISOU 2133 O HIS A 319 6650 4613 5177 -374 -279 505 O ATOM 2134 CB HIS A 319 -6.072 24.318 -62.786 1.00 41.28 C ANISOU 2134 CB HIS A 319 6574 4587 4525 -549 -166 722 C ATOM 2135 CG HIS A 319 -5.016 24.275 -63.844 1.00 47.80 C ANISOU 2135 CG HIS A 319 7448 5540 5173 -647 -49 664 C ATOM 2136 ND1 HIS A 319 -3.675 24.159 -63.549 1.00 42.39 N ANISOU 2136 ND1 HIS A 319 6726 4828 4550 -692 94 504 N ATOM 2137 CD2 HIS A 319 -5.103 24.307 -65.196 1.00 44.70 C ANISOU 2137 CD2 HIS A 319 7131 5322 4530 -705 -47 753 C ATOM 2138 CE1 HIS A 319 -2.980 24.132 -64.673 1.00 53.88 C ANISOU 2138 CE1 HIS A 319 8226 6430 5815 -763 199 502 C ATOM 2139 NE2 HIS A 319 -3.823 24.220 -65.686 1.00 45.55 N ANISOU 2139 NE2 HIS A 319 7250 5504 4552 -772 118 643 N ATOM 2140 N PHE A 320 -8.546 22.973 -61.036 1.00 44.49 N ANISOU 2140 N PHE A 320 6818 4908 5177 -348 -487 758 N ATOM 2141 CA PHE A 320 -9.380 22.972 -59.839 1.00 46.14 C ANISOU 2141 CA PHE A 320 6947 5016 5569 -231 -536 820 C ATOM 2142 C PHE A 320 -9.158 21.708 -59.019 1.00 45.94 C ANISOU 2142 C PHE A 320 6834 4994 5628 -218 -588 627 C ATOM 2143 O PHE A 320 -9.114 21.762 -57.784 1.00 43.91 O ANISOU 2143 O PHE A 320 6523 4646 5515 -141 -549 590 O ATOM 2144 CB PHE A 320 -10.853 23.114 -60.220 1.00 48.18 C ANISOU 2144 CB PHE A 320 7168 5318 5819 -175 -669 1066 C ATOM 2145 CG PHE A 320 -11.761 23.325 -59.042 1.00 66.95 C ANISOU 2145 CG PHE A 320 9458 7595 8384 -32 -678 1177 C ATOM 2146 CD1 PHE A 320 -11.960 24.594 -58.524 1.00 72.86 C ANISOU 2146 CD1 PHE A 320 10242 8206 9236 67 -558 1307 C ATOM 2147 CD2 PHE A 320 -12.413 22.256 -58.450 1.00 70.49 C ANISOU 2147 CD2 PHE A 320 9792 8079 8913 9 -794 1154 C ATOM 2148 CE1 PHE A 320 -12.791 24.793 -57.438 1.00 72.24 C ANISOU 2148 CE1 PHE A 320 10094 8042 9312 219 -538 1397 C ATOM 2149 CE2 PHE A 320 -13.247 22.449 -57.364 1.00 73.40 C ANISOU 2149 CE2 PHE A 320 10072 8377 9440 152 -779 1274 C ATOM 2150 CZ PHE A 320 -13.436 23.719 -56.858 1.00 71.48 C ANISOU 2150 CZ PHE A 320 9874 8012 9274 264 -643 1388 C ATOM 2151 N CYS A 321 -9.018 20.560 -59.686 1.00 38.53 N ANISOU 2151 N CYS A 321 5884 4156 4598 -289 -675 504 N ATOM 2152 CA CYS A 321 -8.755 19.318 -58.970 1.00 37.83 C ANISOU 2152 CA CYS A 321 5707 4051 4615 -278 -722 332 C ATOM 2153 C CYS A 321 -7.378 19.340 -58.319 1.00 38.04 C ANISOU 2153 C CYS A 321 5722 4024 4707 -290 -579 158 C ATOM 2154 O CYS A 321 -7.210 18.854 -57.194 1.00 40.50 O ANISOU 2154 O CYS A 321 5943 4283 5160 -239 -584 95 O ATOM 2155 CB CYS A 321 -8.891 18.127 -59.917 1.00 42.59 C ANISOU 2155 CB CYS A 321 6323 4744 5116 -356 -842 222 C ATOM 2156 SG CYS A 321 -10.586 17.839 -60.469 1.00 47.33 S ANISOU 2156 SG CYS A 321 6894 5410 5681 -364 -1072 423 S ATOM 2157 N ILE A 322 -6.383 19.902 -59.011 1.00 35.14 N ANISOU 2157 N ILE A 322 5433 3682 4238 -361 -455 102 N ATOM 2158 CA ILE A 322 -5.076 20.117 -58.396 1.00 35.71 C ANISOU 2158 CA ILE A 322 5476 3703 4389 -384 -324 -20 C ATOM 2159 C ILE A 322 -5.217 20.979 -57.148 1.00 39.64 C ANISOU 2159 C ILE A 322 5956 4088 5017 -325 -297 48 C ATOM 2160 O ILE A 322 -4.694 20.647 -56.076 1.00 37.75 O ANISOU 2160 O ILE A 322 5643 3811 4890 -305 -287 -48 O ATOM 2161 CB ILE A 322 -4.106 20.754 -59.407 1.00 39.56 C ANISOU 2161 CB ILE A 322 6039 4240 4753 -472 -190 -35 C ATOM 2162 CG1 ILE A 322 -3.779 19.773 -60.532 1.00 42.32 C ANISOU 2162 CG1 ILE A 322 6413 4711 4956 -518 -186 -157 C ATOM 2163 CG2 ILE A 322 -2.838 21.226 -58.711 1.00 41.06 C ANISOU 2163 CG2 ILE A 322 6183 4364 5053 -509 -67 -110 C ATOM 2164 CD1 ILE A 322 -2.849 20.342 -61.572 1.00 43.31 C ANISOU 2164 CD1 ILE A 322 6604 4916 4934 -593 -33 -155 C ATOM 2165 N ALA A 323 -5.934 22.099 -57.271 1.00 40.13 N ANISOU 2165 N ALA A 323 6090 4096 5061 -292 -285 217 N ATOM 2166 CA ALA A 323 -6.091 23.009 -56.141 1.00 40.25 C ANISOU 2166 CA ALA A 323 6121 3984 5188 -226 -240 260 C ATOM 2167 C ALA A 323 -6.810 22.333 -54.982 1.00 41.82 C ANISOU 2167 C ALA A 323 6235 4178 5478 -120 -317 253 C ATOM 2168 O ALA A 323 -6.485 22.580 -53.815 1.00 40.83 O ANISOU 2168 O ALA A 323 6098 3989 5426 -84 -280 186 O ATOM 2169 CB ALA A 323 -6.841 24.267 -56.582 1.00 38.09 C ANISOU 2169 CB ALA A 323 5937 3636 4899 -188 -207 457 C ATOM 2170 N LEU A 324 -7.786 21.470 -55.282 1.00 39.75 N ANISOU 2170 N LEU A 324 5909 3990 5205 -77 -430 327 N ATOM 2171 CA LEU A 324 -8.499 20.763 -54.222 1.00 45.08 C ANISOU 2171 CA LEU A 324 6480 4671 5976 20 -500 355 C ATOM 2172 C LEU A 324 -7.551 19.913 -53.386 1.00 42.26 C ANISOU 2172 C LEU A 324 6045 4330 5682 -4 -496 185 C ATOM 2173 O LEU A 324 -7.698 19.832 -52.160 1.00 39.12 O ANISOU 2173 O LEU A 324 5593 3917 5352 72 -492 189 O ATOM 2174 CB LEU A 324 -9.610 19.896 -54.815 1.00 43.49 C ANISOU 2174 CB LEU A 324 6208 4543 5773 35 -641 466 C ATOM 2175 CG LEU A 324 -10.972 20.573 -54.970 1.00 48.74 C ANISOU 2175 CG LEU A 324 6870 5199 6450 123 -675 706 C ATOM 2176 CD1 LEU A 324 -11.984 19.606 -55.566 1.00 48.40 C ANISOU 2176 CD1 LEU A 324 6736 5240 6415 103 -847 812 C ATOM 2177 CD2 LEU A 324 -11.456 21.099 -53.624 1.00 45.58 C ANISOU 2177 CD2 LEU A 324 6435 4731 6151 267 -600 781 C ATOM 2178 N GLY A 325 -6.572 19.273 -54.030 1.00 40.68 N ANISOU 2178 N GLY A 325 5834 4170 5454 -102 -490 47 N ATOM 2179 CA GLY A 325 -5.598 18.492 -53.285 1.00 42.40 C ANISOU 2179 CA GLY A 325 5958 4399 5752 -121 -481 -91 C ATOM 2180 C GLY A 325 -4.819 19.327 -52.287 1.00 43.10 C ANISOU 2180 C GLY A 325 6066 4444 5866 -127 -403 -138 C ATOM 2181 O GLY A 325 -4.540 18.880 -51.171 1.00 38.59 O ANISOU 2181 O GLY A 325 5410 3888 5362 -96 -428 -176 O ATOM 2182 N TYR A 326 -4.461 20.553 -52.670 1.00 36.00 N ANISOU 2182 N TYR A 326 5279 3487 4911 -177 -319 -131 N ATOM 2183 CA TYR A 326 -3.732 21.426 -51.761 1.00 35.84 C ANISOU 2183 CA TYR A 326 5297 3403 4919 -207 -263 -190 C ATOM 2184 C TYR A 326 -4.643 22.100 -50.743 1.00 40.18 C ANISOU 2184 C TYR A 326 5904 3889 5473 -98 -264 -125 C ATOM 2185 O TYR A 326 -4.145 22.602 -49.729 1.00 43.17 O ANISOU 2185 O TYR A 326 6313 4226 5863 -109 -244 -203 O ATOM 2186 CB TYR A 326 -2.940 22.467 -52.558 1.00 36.58 C ANISOU 2186 CB TYR A 326 5480 3436 4982 -316 -172 -204 C ATOM 2187 CG TYR A 326 -1.838 21.837 -53.381 1.00 39.48 C ANISOU 2187 CG TYR A 326 5777 3881 5344 -415 -135 -281 C ATOM 2188 CD1 TYR A 326 -0.581 21.608 -52.837 1.00 34.77 C ANISOU 2188 CD1 TYR A 326 5090 3303 4818 -490 -116 -386 C ATOM 2189 CD2 TYR A 326 -2.064 21.444 -54.692 1.00 34.82 C ANISOU 2189 CD2 TYR A 326 5207 3355 4670 -428 -119 -248 C ATOM 2190 CE1 TYR A 326 0.423 21.016 -53.582 1.00 35.29 C ANISOU 2190 CE1 TYR A 326 5074 3440 4896 -558 -58 -444 C ATOM 2191 CE2 TYR A 326 -1.069 20.854 -55.444 1.00 33.92 C ANISOU 2191 CE2 TYR A 326 5038 3314 4536 -497 -58 -333 C ATOM 2192 CZ TYR A 326 0.171 20.642 -54.889 1.00 34.96 C ANISOU 2192 CZ TYR A 326 5068 3454 4763 -553 -16 -426 C ATOM 2193 OH TYR A 326 1.162 20.053 -55.640 1.00 36.28 O ANISOU 2193 OH TYR A 326 5166 3693 4926 -600 70 -497 O ATOM 2194 N ATHR A 327 -5.957 22.108 -50.988 0.77 34.47 N ANISOU 2194 N ATHR A 327 5194 3163 4738 8 -288 15 N ATOM 2195 N BTHR A 327 -5.958 22.128 -50.982 0.23 37.11 N ANISOU 2195 N BTHR A 327 5531 3496 5073 8 -286 15 N ATOM 2196 CA ATHR A 327 -6.899 22.616 -49.996 0.77 39.51 C ANISOU 2196 CA ATHR A 327 5866 3757 5390 144 -266 90 C ATOM 2197 CA BTHR A 327 -6.872 22.639 -49.965 0.23 38.31 C ANISOU 2197 CA BTHR A 327 5716 3602 5237 143 -264 86 C ATOM 2198 C ATHR A 327 -6.949 21.714 -48.769 0.77 39.47 C ANISOU 2198 C ATHR A 327 5754 3837 5407 206 -316 56 C ATOM 2199 C BTHR A 327 -6.960 21.711 -48.763 0.23 38.70 C ANISOU 2199 C BTHR A 327 5656 3740 5309 207 -316 57 C ATOM 2200 O ATHR A 327 -7.284 22.174 -47.670 0.77 38.93 O ANISOU 2200 O ATHR A 327 5725 3748 5318 298 -275 55 O ATOM 2201 O BTHR A 327 -7.356 22.156 -47.680 0.23 38.50 O ANISOU 2201 O BTHR A 327 5668 3696 5265 305 -276 64 O ATOM 2202 CB ATHR A 327 -8.288 22.754 -50.625 0.77 37.33 C ANISOU 2202 CB ATHR A 327 5590 3476 5119 242 -282 284 C ATOM 2203 CB BTHR A 327 -8.272 22.854 -50.543 0.23 37.80 C ANISOU 2203 CB BTHR A 327 5658 3526 5178 247 -273 280 C ATOM 2204 OG1ATHR A 327 -8.189 23.532 -51.825 0.77 39.40 O ANISOU 2204 OG1ATHR A 327 5941 3682 5348 176 -248 338 O ATOM 2205 OG1BTHR A 327 -8.751 21.631 -51.113 0.23 36.31 O ANISOU 2205 OG1BTHR A 327 5348 3445 5002 238 -381 344 O ATOM 2206 CG2ATHR A 327 -9.256 23.441 -49.670 0.77 36.73 C ANISOU 2206 CG2ATHR A 327 5551 3339 5066 405 -219 375 C ATOM 2207 CG2BTHR A 327 -8.258 23.947 -51.601 0.23 38.49 C ANISOU 2207 CG2BTHR A 327 5860 3523 5241 201 -215 345 C ATOM 2208 N ASN A 328 -6.613 20.433 -48.934 1.00 37.95 N ANISOU 2208 N ASN A 328 5429 3738 5253 161 -396 31 N ATOM 2209 CA ASN A 328 -6.510 19.542 -47.787 1.00 34.67 C ANISOU 2209 CA ASN A 328 4894 3405 4872 206 -445 18 C ATOM 2210 C ASN A 328 -5.457 20.049 -46.812 1.00 42.24 C ANISOU 2210 C ASN A 328 5894 4362 5791 155 -415 -113 C ATOM 2211 O ASN A 328 -5.640 19.978 -45.592 1.00 41.57 O ANISOU 2211 O ASN A 328 5789 4333 5674 227 -422 -105 O ATOM 2212 CB ASN A 328 -6.179 18.125 -48.260 1.00 33.38 C ANISOU 2212 CB ASN A 328 4589 3303 4791 154 -529 4 C ATOM 2213 CG ASN A 328 -6.369 17.087 -47.173 1.00 37.08 C ANISOU 2213 CG ASN A 328 4909 3851 5329 219 -592 61 C ATOM 2214 OD1 ASN A 328 -5.407 16.485 -46.693 1.00 41.71 O ANISOU 2214 OD1 ASN A 328 5408 4479 5959 171 -617 -12 O ATOM 2215 ND2 ASN A 328 -7.617 16.872 -46.778 1.00 35.00 N ANISOU 2215 ND2 ASN A 328 4598 3616 5086 331 -616 218 N ATOM 2216 N SER A 329 -4.354 20.589 -47.338 1.00 39.43 N ANISOU 2216 N SER A 329 5597 3955 5430 25 -384 -227 N ATOM 2217 CA SER A 329 -3.346 21.212 -46.493 1.00 39.61 C ANISOU 2217 CA SER A 329 5665 3963 5422 -52 -375 -348 C ATOM 2218 C SER A 329 -3.847 22.506 -45.865 1.00 47.08 C ANISOU 2218 C SER A 329 6784 4809 6296 4 -314 -371 C ATOM 2219 O SER A 329 -3.344 22.904 -44.808 1.00 48.88 O ANISOU 2219 O SER A 329 7060 5043 6469 -25 -329 -472 O ATOM 2220 CB SER A 329 -2.075 21.475 -47.303 1.00 43.26 C ANISOU 2220 CB SER A 329 6123 4390 5923 -212 -354 -434 C ATOM 2221 OG SER A 329 -1.530 20.264 -47.794 1.00 42.58 O ANISOU 2221 OG SER A 329 5882 4390 5907 -246 -388 -435 O ATOM 2222 N CYS A 330 -4.828 23.164 -46.487 1.00 40.13 N ANISOU 2222 N CYS A 330 5998 3835 5414 85 -249 -280 N ATOM 2223 CA CYS A 330 -5.420 24.363 -45.905 1.00 42.73 C ANISOU 2223 CA CYS A 330 6491 4044 5702 172 -168 -293 C ATOM 2224 C CYS A 330 -6.389 24.035 -44.778 1.00 49.84 C ANISOU 2224 C CYS A 330 7369 5023 6546 346 -155 -238 C ATOM 2225 O CYS A 330 -6.523 24.822 -43.834 1.00 41.74 O ANISOU 2225 O CYS A 330 6473 3939 5448 409 -95 -320 O ATOM 2226 CB CYS A 330 -6.154 25.173 -46.976 1.00 44.61 C ANISOU 2226 CB CYS A 330 6814 4154 5981 215 -97 -177 C ATOM 2227 SG CYS A 330 -5.111 25.842 -48.283 1.00 47.63 S ANISOU 2227 SG CYS A 330 7251 4437 6408 26 -77 -210 S ATOM 2228 N LEU A 331 -7.075 22.896 -44.860 1.00 40.93 N ANISOU 2228 N LEU A 331 6082 4021 5449 423 -204 -99 N ATOM 2229 CA LEU A 331 -8.082 22.543 -43.869 1.00 42.24 C ANISOU 2229 CA LEU A 331 6198 4275 5576 594 -179 2 C ATOM 2230 C LEU A 331 -7.528 21.710 -42.721 1.00 42.25 C ANISOU 2230 C LEU A 331 6106 4430 5520 579 -243 -48 C ATOM 2231 O LEU A 331 -8.116 21.716 -41.634 1.00 42.05 O ANISOU 2231 O LEU A 331 6086 4481 5409 710 -197 -8 O ATOM 2232 CB LEU A 331 -9.237 21.793 -44.541 1.00 38.65 C ANISOU 2232 CB LEU A 331 5607 3869 5211 681 -207 217 C ATOM 2233 CG LEU A 331 -10.006 22.599 -45.593 1.00 45.28 C ANISOU 2233 CG LEU A 331 6518 4590 6097 722 -154 322 C ATOM 2234 CD1 LEU A 331 -11.029 21.733 -46.312 1.00 43.97 C ANISOU 2234 CD1 LEU A 331 6198 4493 6016 765 -229 529 C ATOM 2235 CD2 LEU A 331 -10.680 23.809 -44.960 1.00 50.98 C ANISOU 2235 CD2 LEU A 331 7379 5210 6782 875 -13 339 C ATOM 2236 N ASN A 332 -6.419 21.002 -42.936 1.00 33.22 N ANISOU 2236 N ASN A 332 4866 3338 4416 432 -338 -120 N ATOM 2237 CA ASN A 332 -5.813 20.227 -41.855 1.00 40.13 C ANISOU 2237 CA ASN A 332 5636 4362 5248 411 -411 -145 C ATOM 2238 C ASN A 332 -5.482 21.051 -40.613 1.00 42.34 C ANISOU 2238 C ASN A 332 6056 4669 5364 421 -383 -272 C ATOM 2239 O ASN A 332 -5.663 20.523 -39.502 1.00 44.41 O ANISOU 2239 O ASN A 332 6253 5084 5538 494 -407 -221 O ATOM 2240 CB ASN A 332 -4.564 19.503 -42.372 1.00 35.44 C ANISOU 2240 CB ASN A 332 4924 3793 4749 251 -501 -206 C ATOM 2241 CG ASN A 332 -4.904 18.285 -43.206 1.00 38.05 C ANISOU 2241 CG ASN A 332 5091 4144 5222 265 -547 -88 C ATOM 2242 OD1 ASN A 332 -6.037 17.803 -43.186 1.00 44.48 O ANISOU 2242 OD1 ASN A 332 5846 4985 6070 379 -546 59 O ATOM 2243 ND2 ASN A 332 -3.923 17.777 -43.941 1.00 39.09 N ANISOU 2243 ND2 ASN A 332 5147 4259 5445 148 -585 -153 N ATOM 2244 N PRO A 333 -4.996 22.298 -40.703 1.00 38.90 N ANISOU 2244 N PRO A 333 5809 4094 4876 345 -341 -435 N ATOM 2245 CA PRO A 333 -4.837 23.093 -39.473 1.00 44.34 C ANISOU 2245 CA PRO A 333 6660 4795 5392 364 -317 -577 C ATOM 2246 C PRO A 333 -6.130 23.262 -38.701 1.00 49.44 C ANISOU 2246 C PRO A 333 7370 5486 5931 587 -205 -499 C ATOM 2247 O PRO A 333 -6.105 23.296 -37.465 1.00 56.97 O ANISOU 2247 O PRO A 333 8377 6560 6708 637 -204 -562 O ATOM 2248 CB PRO A 333 -4.314 24.442 -39.985 1.00 50.31 C ANISOU 2248 CB PRO A 333 7612 5332 6171 252 -278 -741 C ATOM 2249 CG PRO A 333 -3.669 24.132 -41.264 1.00 44.88 C ANISOU 2249 CG PRO A 333 6817 4594 5643 117 -322 -698 C ATOM 2250 CD PRO A 333 -4.449 23.008 -41.873 1.00 36.54 C ANISOU 2250 CD PRO A 333 5586 3628 4670 219 -322 -504 C ATOM 2251 N VAL A 334 -7.265 23.369 -39.392 1.00 43.96 N ANISOU 2251 N VAL A 334 6662 4712 5328 724 -109 -352 N ATOM 2252 CA VAL A 334 -8.540 23.488 -38.696 1.00 42.00 C ANISOU 2252 CA VAL A 334 6438 4515 5004 952 16 -241 C ATOM 2253 C VAL A 334 -8.925 22.157 -38.067 1.00 49.70 C ANISOU 2253 C VAL A 334 7198 5723 5963 1026 -35 -60 C ATOM 2254 O VAL A 334 -9.261 22.087 -36.879 1.00 50.19 O ANISOU 2254 O VAL A 334 7280 5926 5865 1143 20 -46 O ATOM 2255 CB VAL A 334 -9.633 23.992 -39.654 1.00 47.12 C ANISOU 2255 CB VAL A 334 7104 5016 5783 1071 122 -102 C ATOM 2256 CG1 VAL A 334 -10.961 24.102 -38.921 1.00 51.15 C ANISOU 2256 CG1 VAL A 334 7610 5588 6238 1322 268 39 C ATOM 2257 CG2 VAL A 334 -9.237 25.331 -40.259 1.00 54.94 C ANISOU 2257 CG2 VAL A 334 8302 5766 6808 1000 176 -255 C ATOM 2258 N LEU A 335 -8.859 21.078 -38.851 1.00 42.29 N ANISOU 2258 N LEU A 335 6055 4826 5187 955 -139 79 N ATOM 2259 CA LEU A 335 -9.373 19.791 -38.395 1.00 43.08 C ANISOU 2259 CA LEU A 335 5935 5105 5330 1028 -187 288 C ATOM 2260 C LEU A 335 -8.516 19.198 -37.285 1.00 40.27 C ANISOU 2260 C LEU A 335 5519 4924 4857 971 -269 243 C ATOM 2261 O LEU A 335 -9.045 18.612 -36.335 1.00 46.11 O ANISOU 2261 O LEU A 335 6160 5837 5524 1086 -248 391 O ATOM 2262 CB LEU A 335 -9.459 18.815 -39.569 1.00 44.55 C ANISOU 2262 CB LEU A 335 5943 5251 5733 950 -288 412 C ATOM 2263 CG LEU A 335 -10.340 19.216 -40.752 1.00 53.16 C ANISOU 2263 CG LEU A 335 7058 6205 6937 989 -246 497 C ATOM 2264 CD1 LEU A 335 -10.269 18.161 -41.846 1.00 53.81 C ANISOU 2264 CD1 LEU A 335 6985 6268 7193 884 -371 574 C ATOM 2265 CD2 LEU A 335 -11.774 19.426 -40.299 1.00 54.61 C ANISOU 2265 CD2 LEU A 335 7210 6429 7111 1195 -135 692 C ATOM 2266 N TYR A 336 -7.193 19.337 -37.383 1.00 38.13 N ANISOU 2266 N TYR A 336 5292 4627 4570 792 -364 64 N ATOM 2267 CA TYR A 336 -6.286 18.592 -36.523 1.00 36.77 C ANISOU 2267 CA TYR A 336 5007 4627 4335 712 -479 62 C ATOM 2268 C TYR A 336 -5.520 19.447 -35.524 1.00 41.70 C ANISOU 2268 C TYR A 336 5808 5309 4729 648 -496 -139 C ATOM 2269 O TYR A 336 -4.908 18.889 -34.606 1.00 47.50 O ANISOU 2269 O TYR A 336 6455 6229 5364 602 -593 -115 O ATOM 2270 CB TYR A 336 -5.287 17.801 -37.378 1.00 40.31 C ANISOU 2270 CB TYR A 336 5302 5034 4980 550 -601 58 C ATOM 2271 CG TYR A 336 -5.948 16.732 -38.216 1.00 36.37 C ANISOU 2271 CG TYR A 336 4623 4501 4696 597 -617 242 C ATOM 2272 CD1 TYR A 336 -6.325 15.520 -37.651 1.00 44.65 C ANISOU 2272 CD1 TYR A 336 5466 5682 5815 666 -667 447 C ATOM 2273 CD2 TYR A 336 -6.205 16.937 -39.566 1.00 38.09 C ANISOU 2273 CD2 TYR A 336 4877 4552 5043 564 -590 214 C ATOM 2274 CE1 TYR A 336 -6.934 14.539 -38.405 1.00 41.75 C ANISOU 2274 CE1 TYR A 336 4942 5259 5662 692 -698 602 C ATOM 2275 CE2 TYR A 336 -6.813 15.959 -40.332 1.00 37.63 C ANISOU 2275 CE2 TYR A 336 4672 4462 5164 589 -627 359 C ATOM 2276 CZ TYR A 336 -7.174 14.762 -39.744 1.00 37.99 C ANISOU 2276 CZ TYR A 336 4521 4617 5296 648 -684 543 C ATOM 2277 OH TYR A 336 -7.780 13.785 -40.493 1.00 41.06 O ANISOU 2277 OH TYR A 336 4772 4950 5881 656 -736 674 O ATOM 2278 N ALA A 337 -5.528 20.769 -35.667 1.00 41.62 N ANISOU 2278 N ALA A 337 6038 5142 4633 636 -416 -332 N ATOM 2279 CA ALA A 337 -4.845 21.652 -34.725 1.00 40.93 C ANISOU 2279 CA ALA A 337 6148 5080 4324 561 -442 -554 C ATOM 2280 C ALA A 337 -5.840 22.510 -33.971 1.00 42.77 C ANISOU 2280 C ALA A 337 6591 5299 4360 747 -281 -618 C ATOM 2281 O ALA A 337 -6.023 22.330 -32.762 1.00 47.21 O ANISOU 2281 O ALA A 337 7181 6061 4696 830 -270 -611 O ATOM 2282 CB ALA A 337 -3.805 22.511 -35.452 1.00 40.85 C ANISOU 2282 CB ALA A 337 6251 4873 4396 358 -499 -756 C ATOM 2283 N PHE A 338 -6.516 23.446 -34.648 1.00 42.79 N ANISOU 2283 N PHE A 338 6742 5076 4438 830 -142 -668 N ATOM 2284 CA PHE A 338 -7.403 24.377 -33.961 1.00 51.49 C ANISOU 2284 CA PHE A 338 8063 6128 5375 1019 35 -752 C ATOM 2285 C PHE A 338 -8.590 23.685 -33.300 1.00 53.22 C ANISOU 2285 C PHE A 338 8162 6546 5515 1258 150 -525 C ATOM 2286 O PHE A 338 -9.168 24.243 -32.363 1.00 52.31 O ANISOU 2286 O PHE A 338 8206 6480 5188 1423 293 -596 O ATOM 2287 CB PHE A 338 -7.895 25.450 -34.936 1.00 50.83 C ANISOU 2287 CB PHE A 338 8122 5746 5444 1067 160 -803 C ATOM 2288 CG PHE A 338 -6.794 26.313 -35.493 1.00 62.73 C ANISOU 2288 CG PHE A 338 9773 7042 7020 844 76 -1023 C ATOM 2289 CD1 PHE A 338 -6.030 27.110 -34.655 1.00 74.94 C ANISOU 2289 CD1 PHE A 338 11538 8546 8391 737 32 -1296 C ATOM 2290 CD2 PHE A 338 -6.529 26.334 -36.853 1.00 68.50 C ANISOU 2290 CD2 PHE A 338 10420 7621 7984 734 37 -950 C ATOM 2291 CE1 PHE A 338 -5.018 27.905 -35.163 1.00 77.44 C ANISOU 2291 CE1 PHE A 338 11966 8658 8798 516 -54 -1477 C ATOM 2292 CE2 PHE A 338 -5.520 27.129 -37.368 1.00 65.34 C ANISOU 2292 CE2 PHE A 338 10133 7036 7658 529 -27 -1120 C ATOM 2293 CZ PHE A 338 -4.763 27.913 -36.521 1.00 71.54 C ANISOU 2293 CZ PHE A 338 11115 7766 8300 417 -75 -1376 C ATOM 2294 N LEU A 339 -8.963 22.491 -33.753 1.00 52.02 N ANISOU 2294 N LEU A 339 7735 6503 5528 1281 97 -255 N ATOM 2295 CA LEU A 339 -10.037 21.734 -33.123 1.00 52.69 C ANISOU 2295 CA LEU A 339 7665 6785 5568 1484 188 -1 C ATOM 2296 C LEU A 339 -9.527 20.643 -32.189 1.00 53.87 C ANISOU 2296 C LEU A 339 7654 7212 5602 1434 67 101 C ATOM 2297 O LEU A 339 -10.338 19.926 -31.597 1.00 58.78 O ANISOU 2297 O LEU A 339 8126 8021 6188 1587 132 339 O ATOM 2298 CB LEU A 339 -10.954 21.126 -34.189 1.00 53.30 C ANISOU 2298 CB LEU A 339 7536 6792 5922 1550 207 262 C ATOM 2299 CG LEU A 339 -11.822 22.138 -34.945 1.00 59.15 C ANISOU 2299 CG LEU A 339 8397 7313 6762 1667 358 257 C ATOM 2300 CD1 LEU A 339 -12.700 21.444 -35.975 1.00 61.20 C ANISOU 2300 CD1 LEU A 339 8434 7541 7280 1706 335 533 C ATOM 2301 CD2 LEU A 339 -12.667 22.960 -33.980 1.00 55.62 C ANISOU 2301 CD2 LEU A 339 8110 6895 6128 1904 579 227 C ATOM 2302 N ASP A 340 -8.211 20.499 -32.044 1.00 51.25 N ANISOU 2302 N ASP A 340 7332 6917 5224 1224 -107 -47 N ATOM 2303 CA ASP A 340 -7.663 19.574 -31.062 1.00 50.20 C ANISOU 2303 CA ASP A 340 7058 7055 4962 1178 -227 51 C ATOM 2304 C ASP A 340 -8.004 20.050 -29.655 1.00 55.64 C ANISOU 2304 C ASP A 340 7912 7939 5289 1310 -126 -16 C ATOM 2305 O ASP A 340 -8.012 21.251 -29.377 1.00 59.44 O ANISOU 2305 O ASP A 340 8677 8317 5591 1336 -35 -274 O ATOM 2306 CB ASP A 340 -6.148 19.454 -31.230 1.00 50.12 C ANISOU 2306 CB ASP A 340 7024 7032 4987 925 -432 -95 C ATOM 2307 CG ASP A 340 -5.505 18.603 -30.149 1.00 54.70 C ANISOU 2307 CG ASP A 340 7464 7899 5419 871 -570 9 C ATOM 2308 OD1 ASP A 340 -5.577 17.359 -30.244 1.00 54.79 O ANISOU 2308 OD1 ASP A 340 7204 8013 5600 887 -634 269 O ATOM 2309 OD2 ASP A 340 -4.931 19.180 -29.202 1.00 55.29 O ANISOU 2309 OD2 ASP A 340 7702 8093 5211 809 -622 -167 O ATOM 2310 N GLU A 341 -8.279 19.096 -28.762 1.00 61.54 N ANISOU 2310 N GLU A 341 8487 8968 5928 1394 -139 217 N ATOM 2311 CA GLU A 341 -8.791 19.438 -27.436 1.00 69.20 C ANISOU 2311 CA GLU A 341 9596 10163 6534 1558 -9 201 C ATOM 2312 C GLU A 341 -7.788 20.271 -26.645 1.00 65.00 C ANISOU 2312 C GLU A 341 9328 9689 5682 1425 -99 -129 C ATOM 2313 O GLU A 341 -8.147 21.289 -26.043 1.00 66.97 O ANISOU 2313 O GLU A 341 9860 9922 5664 1531 46 -346 O ATOM 2314 CB GLU A 341 -9.154 18.164 -26.672 1.00 87.63 C ANISOU 2314 CB GLU A 341 11662 12806 8827 1646 -28 552 C ATOM 2315 CG GLU A 341 -10.373 18.308 -25.775 1.00102.93 C ANISOU 2315 CG GLU A 341 13644 14930 10536 1916 210 691 C ATOM 2316 CD GLU A 341 -11.676 18.131 -26.533 1.00110.21 C ANISOU 2316 CD GLU A 341 14424 15716 11735 2092 378 922 C ATOM 2317 OE1 GLU A 341 -12.287 17.047 -26.420 1.00112.37 O ANISOU 2317 OE1 GLU A 341 14413 16133 12149 2170 385 1283 O ATOM 2318 OE2 GLU A 341 -12.083 19.069 -27.251 1.00111.51 O ANISOU 2318 OE2 GLU A 341 14749 15626 11993 2144 492 760 O ATOM 2319 N ASN A 342 -6.521 19.849 -26.626 1.00 55.81 N ANISOU 2319 N ASN A 342 8074 8586 4544 1190 -340 -172 N ATOM 2320 CA ASN A 342 -5.515 20.580 -25.863 1.00 59.45 C ANISOU 2320 CA ASN A 342 8759 9118 4710 1029 -468 -466 C ATOM 2321 C ASN A 342 -5.040 21.825 -26.603 1.00 64.98 C ANISOU 2321 C ASN A 342 9706 9487 5498 898 -474 -802 C ATOM 2322 O ASN A 342 -4.878 22.888 -25.991 1.00 68.28 O ANISOU 2322 O ASN A 342 10429 9866 5649 876 -446 -1100 O ATOM 2323 CB ASN A 342 -4.329 19.668 -25.541 1.00 60.27 C ANISOU 2323 CB ASN A 342 8646 9426 4829 826 -733 -351 C ATOM 2324 CG ASN A 342 -4.690 18.561 -24.573 1.00 58.49 C ANISOU 2324 CG ASN A 342 8213 9555 4456 942 -742 -33 C ATOM 2325 OD1 ASN A 342 -4.885 18.805 -23.385 1.00 60.81 O ANISOU 2325 OD1 ASN A 342 8648 10099 4356 1019 -705 -76 O ATOM 2326 ND2 ASN A 342 -4.775 17.334 -25.077 1.00 58.27 N ANISOU 2326 ND2 ASN A 342 7853 9547 4740 955 -791 290 N ATOM 2327 N PHE A 343 -4.806 21.707 -27.915 1.00 58.15 N ANISOU 2327 N PHE A 343 8716 8379 5000 806 -510 -759 N ATOM 2328 CA PHE A 343 -4.370 22.853 -28.710 1.00 67.35 C ANISOU 2328 CA PHE A 343 10084 9225 6281 680 -508 -1029 C ATOM 2329 C PHE A 343 -5.390 23.983 -28.650 1.00 75.79 C ANISOU 2329 C PHE A 343 11433 10114 7252 870 -272 -1185 C ATOM 2330 O PHE A 343 -5.022 25.164 -28.658 1.00 79.57 O ANISOU 2330 O PHE A 343 12182 10387 7665 785 -264 -1481 O ATOM 2331 CB PHE A 343 -4.130 22.409 -30.155 1.00 62.08 C ANISOU 2331 CB PHE A 343 9214 8369 6006 593 -550 -901 C ATOM 2332 CG PHE A 343 -3.437 23.437 -31.014 1.00 61.49 C ANISOU 2332 CG PHE A 343 9292 8003 6070 419 -583 -1131 C ATOM 2333 CD1 PHE A 343 -4.151 24.468 -31.603 1.00 65.05 C ANISOU 2333 CD1 PHE A 343 9941 8187 6587 517 -412 -1239 C ATOM 2334 CD2 PHE A 343 -2.076 23.349 -31.261 1.00 59.92 C ANISOU 2334 CD2 PHE A 343 9012 7796 5958 162 -781 -1205 C ATOM 2335 CE1 PHE A 343 -3.523 25.403 -32.401 1.00 63.36 C ANISOU 2335 CE1 PHE A 343 9855 7703 6517 356 -441 -1417 C ATOM 2336 CE2 PHE A 343 -1.440 24.282 -32.061 1.00 59.42 C ANISOU 2336 CE2 PHE A 343 9069 7471 6037 -1 -805 -1385 C ATOM 2337 CZ PHE A 343 -2.166 25.310 -32.633 1.00 48.89 C ANISOU 2337 CZ PHE A 343 7942 5870 4763 92 -636 -1489 C ATOM 2338 N LYS A 344 -6.677 23.636 -28.578 1.00 78.56 N ANISOU 2338 N LYS A 344 11711 10528 7611 1131 -76 -976 N ATOM 2339 CA LYS A 344 -7.730 24.645 -28.510 1.00 83.34 C ANISOU 2339 CA LYS A 344 12547 10971 8147 1350 175 -1082 C ATOM 2340 C LYS A 344 -7.545 25.549 -27.298 1.00 86.07 C ANISOU 2340 C LYS A 344 13218 11374 8110 1375 222 -1389 C ATOM 2341 O LYS A 344 -7.657 26.776 -27.401 1.00 93.20 O ANISOU 2341 O LYS A 344 14407 12017 8989 1402 330 -1655 O ATOM 2342 CB LYS A 344 -9.096 23.959 -28.461 1.00 84.70 C ANISOU 2342 CB LYS A 344 12536 11272 8375 1622 361 -760 C ATOM 2343 CG LYS A 344 -10.252 24.779 -29.006 1.00 88.19 C ANISOU 2343 CG LYS A 344 13086 11480 8943 1840 608 -749 C ATOM 2344 CD LYS A 344 -11.568 24.025 -28.864 1.00 91.41 C ANISOU 2344 CD LYS A 344 13273 12053 9404 2094 772 -397 C ATOM 2345 CE LYS A 344 -11.520 22.677 -29.569 1.00 91.48 C ANISOU 2345 CE LYS A 344 12926 12154 9680 1997 613 -84 C ATOM 2346 NZ LYS A 344 -12.789 21.914 -29.394 1.00 95.26 N ANISOU 2346 NZ LYS A 344 13173 12790 10230 2220 750 274 N ATOM 2347 N ARG A 345 -7.240 24.955 -26.141 1.00 93.57 N ANISOU 2347 N ARG A 345 14136 12662 8757 1361 136 -1358 N ATOM 2348 CA ARG A 345 -7.148 25.717 -24.899 1.00 93.28 C ANISOU 2348 CA ARG A 345 14414 12730 8296 1399 183 -1645 C ATOM 2349 C ARG A 345 -6.035 26.755 -24.955 1.00 98.22 C ANISOU 2349 C ARG A 345 15304 13138 8876 1139 19 -2033 C ATOM 2350 O ARG A 345 -6.197 27.877 -24.459 1.00 99.54 O ANISOU 2350 O ARG A 345 15819 13162 8839 1193 128 -2354 O ATOM 2351 CB ARG A 345 -6.925 24.766 -23.724 1.00 92.68 C ANISOU 2351 CB ARG A 345 14216 13094 7905 1400 81 -1494 C ATOM 2352 CG ARG A 345 -8.018 23.723 -23.555 1.00 94.35 C ANISOU 2352 CG ARG A 345 14158 13534 8155 1648 241 -1090 C ATOM 2353 CD ARG A 345 -7.499 22.444 -22.900 1.00 96.66 C ANISOU 2353 CD ARG A 345 14183 14203 8340 1559 50 -825 C ATOM 2354 NE ARG A 345 -6.785 22.694 -21.651 1.00104.45 N ANISOU 2354 NE ARG A 345 15361 15450 8876 1459 -75 -1025 N ATOM 2355 CZ ARG A 345 -5.473 22.546 -21.496 1.00104.25 C ANISOU 2355 CZ ARG A 345 15308 15497 8806 1172 -375 -1125 C ATOM 2356 NH1 ARG A 345 -4.723 22.142 -22.512 1.00 98.59 N ANISOU 2356 NH1 ARG A 345 14376 14608 8474 975 -554 -1043 N ATOM 2357 NH2 ARG A 345 -4.910 22.797 -20.321 1.00112.71 N ANISOU 2357 NH2 ARG A 345 16560 16826 9437 1084 -495 -1300 N ATOM 2358 N CYS A 346 -4.898 26.402 -25.555 1.00103.09 N ANISOU 2358 N CYS A 346 15757 13715 9696 856 -239 -2008 N ATOM 2359 CA CYS A 346 -3.748 27.298 -25.548 1.00113.60 C ANISOU 2359 CA CYS A 346 17296 14874 10995 576 -427 -2339 C ATOM 2360 C CYS A 346 -3.944 28.511 -26.448 1.00119.03 C ANISOU 2360 C CYS A 346 18192 15118 11915 574 -304 -2541 C ATOM 2361 O CYS A 346 -3.238 29.509 -26.266 1.00122.36 O ANISOU 2361 O CYS A 346 18869 15353 12270 390 -402 -2864 O ATOM 2362 CB CYS A 346 -2.494 26.538 -25.975 1.00113.30 C ANISOU 2362 CB CYS A 346 16982 14928 11140 292 -716 -2212 C ATOM 2363 SG CYS A 346 -2.175 25.035 -25.028 1.00115.03 S ANISOU 2363 SG CYS A 346 16904 15642 11159 283 -881 -1919 S ATOM 2364 N PHE A 347 -4.909 28.453 -27.369 1.00118.10 N ANISOU 2364 N PHE A 347 17973 14835 12066 772 -99 -2347 N ATOM 2365 CA PHE A 347 -5.073 29.387 -28.498 1.00119.97 C ANISOU 2365 CA PHE A 347 18312 14665 12608 760 -1 -2427 C ATOM 2366 C PHE A 347 -3.869 30.297 -28.764 1.00125.27 C ANISOU 2366 C PHE A 347 19150 15092 13356 455 -181 -2708 C ATOM 2367 O PHE A 347 -3.939 31.516 -28.608 1.00130.00 O ANISOU 2367 O PHE A 347 20061 15416 13917 456 -101 -2991 O ATOM 2368 CB PHE A 347 -6.346 30.243 -28.334 1.00118.65 C ANISOU 2368 CB PHE A 347 18375 14316 12392 1063 306 -2505 C ATOM 2369 CG PHE A 347 -6.597 30.750 -26.936 1.00121.96 C ANISOU 2369 CG PHE A 347 19089 14848 12403 1182 399 -2764 C ATOM 2370 CD1 PHE A 347 -7.522 30.125 -26.116 1.00121.92 C ANISOU 2370 CD1 PHE A 347 19022 15140 12160 1448 563 -2605 C ATOM 2371 CD2 PHE A 347 -5.950 31.880 -26.461 1.00123.35 C ANISOU 2371 CD2 PHE A 347 19612 14822 12434 1035 336 -3169 C ATOM 2372 CE1 PHE A 347 -7.771 30.596 -24.840 1.00124.65 C ANISOU 2372 CE1 PHE A 347 19652 15610 12099 1574 672 -2848 C ATOM 2373 CE2 PHE A 347 -6.193 32.354 -25.187 1.00124.88 C ANISOU 2373 CE2 PHE A 347 20106 15119 12226 1147 426 -3438 C ATOM 2374 CZ PHE A 347 -7.104 31.712 -24.377 1.00127.32 C ANISOU 2374 CZ PHE A 347 20357 15750 12270 1424 602 -3280 C TER 2375 PHE A 347 ATOM 2376 N GLN B 3 -20.907 5.514 -1.080 1.00103.21 N ANISOU 2376 N GLN B 3 10234 18311 10672 -419 3523 -1211 N ATOM 2377 CA GLN B 3 -21.306 5.944 -2.415 1.00 97.57 C ANISOU 2377 CA GLN B 3 9237 17494 10341 -564 3008 -1754 C ATOM 2378 C GLN B 3 -20.355 5.409 -3.489 1.00 90.54 C ANISOU 2378 C GLN B 3 8580 16142 9679 -805 2640 -1747 C ATOM 2379 O GLN B 3 -20.524 4.291 -3.974 1.00 97.37 O ANISOU 2379 O GLN B 3 9224 16687 11086 -1186 2861 -1660 O ATOM 2380 CB GLN B 3 -21.380 7.472 -2.478 1.00 88.71 C ANISOU 2380 CB GLN B 3 8256 16691 8760 -149 2525 -2147 C ATOM 2381 CG GLN B 3 -20.288 8.189 -1.696 1.00 87.73 C ANISOU 2381 CG GLN B 3 8699 16682 7954 195 2338 -1975 C ATOM 2382 CD GLN B 3 -20.077 9.609 -2.175 1.00 85.69 C ANISOU 2382 CD GLN B 3 8642 16506 7409 497 1790 -2416 C ATOM 2383 OE1 GLN B 3 -20.934 10.183 -2.847 1.00 92.59 O ANISOU 2383 OE1 GLN B 3 9257 17478 8446 574 1623 -2807 O ATOM 2384 NE2 GLN B 3 -18.927 10.183 -1.838 1.00 76.44 N ANISOU 2384 NE2 GLN B 3 7927 15279 5837 694 1522 -2382 N ATOM 2385 N VAL B 4 -19.362 6.216 -3.859 1.00 85.02 N ANISOU 2385 N VAL B 4 8323 15378 8604 -580 2120 -1853 N ATOM 2386 CA VAL B 4 -18.361 5.851 -4.855 1.00 74.38 C ANISOU 2386 CA VAL B 4 7259 13586 7416 -732 1790 -1825 C ATOM 2387 C VAL B 4 -17.107 5.385 -4.130 1.00 69.06 C ANISOU 2387 C VAL B 4 6999 12794 6447 -713 1918 -1347 C ATOM 2388 O VAL B 4 -16.658 6.027 -3.172 1.00 68.61 O ANISOU 2388 O VAL B 4 7172 13009 5888 -407 1892 -1261 O ATOM 2389 CB VAL B 4 -18.053 7.033 -5.792 1.00 70.98 C ANISOU 2389 CB VAL B 4 7048 13085 6835 -472 1224 -2241 C ATOM 2390 CG1 VAL B 4 -16.798 6.762 -6.609 1.00 67.11 C ANISOU 2390 CG1 VAL B 4 6954 12124 6421 -552 971 -2119 C ATOM 2391 CG2 VAL B 4 -19.239 7.303 -6.706 1.00 68.19 C ANISOU 2391 CG2 VAL B 4 6320 12814 6777 -432 1045 -2722 C ATOM 2392 N GLN B 5 -16.544 4.266 -4.581 1.00 67.57 N ANISOU 2392 N GLN B 5 6902 12215 6558 -1000 2028 -1071 N ATOM 2393 CA GLN B 5 -15.339 3.682 -3.996 1.00 69.18 C ANISOU 2393 CA GLN B 5 7482 12290 6516 -960 2141 -614 C ATOM 2394 C GLN B 5 -14.286 3.551 -5.093 1.00 70.84 C ANISOU 2394 C GLN B 5 7950 12062 6903 -1069 1762 -646 C ATOM 2395 O GLN B 5 -14.347 2.632 -5.917 1.00 68.29 O ANISOU 2395 O GLN B 5 7568 11373 7006 -1367 1841 -574 O ATOM 2396 CB GLN B 5 -15.646 2.332 -3.354 1.00 81.80 C ANISOU 2396 CB GLN B 5 8993 13803 8283 -1158 2789 -144 C ATOM 2397 CG GLN B 5 -14.430 1.618 -2.785 1.00 88.91 C ANISOU 2397 CG GLN B 5 10310 14574 8897 -1048 2925 352 C ATOM 2398 CD GLN B 5 -14.789 0.316 -2.096 1.00101.94 C ANISOU 2398 CD GLN B 5 11949 16110 10672 -1166 3676 860 C ATOM 2399 OE1 GLN B 5 -15.667 0.278 -1.232 1.00107.62 O ANISOU 2399 OE1 GLN B 5 12510 17074 11308 -1060 4171 976 O ATOM 2400 NE2 GLN B 5 -14.115 -0.763 -2.480 1.00102.64 N ANISOU 2400 NE2 GLN B 5 12231 15789 10978 -1367 3829 1186 N ATOM 2401 N LEU B 6 -13.320 4.467 -5.103 1.00 58.92 N ANISOU 2401 N LEU B 6 6720 10560 5106 -824 1379 -771 N ATOM 2402 CA LEU B 6 -12.233 4.434 -6.072 1.00 60.19 C ANISOU 2402 CA LEU B 6 7142 10284 5443 -883 1090 -775 C ATOM 2403 C LEU B 6 -11.122 3.531 -5.548 1.00 62.34 C ANISOU 2403 C LEU B 6 7632 10433 5623 -914 1230 -322 C ATOM 2404 O LEU B 6 -10.580 3.769 -4.463 1.00 72.34 O ANISOU 2404 O LEU B 6 8999 11991 6498 -667 1226 -209 O ATOM 2405 CB LEU B 6 -11.704 5.842 -6.343 1.00 56.40 C ANISOU 2405 CB LEU B 6 6824 9794 4812 -626 707 -1136 C ATOM 2406 CG LEU B 6 -12.703 6.828 -6.954 1.00 57.14 C ANISOU 2406 CG LEU B 6 6794 9977 4938 -496 555 -1580 C ATOM 2407 CD1 LEU B 6 -12.066 8.195 -7.156 1.00 59.13 C ANISOU 2407 CD1 LEU B 6 7276 10132 5060 -230 286 -1883 C ATOM 2408 CD2 LEU B 6 -13.254 6.290 -8.267 1.00 54.28 C ANISOU 2408 CD2 LEU B 6 6371 9305 4949 -646 511 -1685 C ATOM 2409 N VAL B 7 -10.789 2.499 -6.315 1.00 63.62 N ANISOU 2409 N VAL B 7 7878 10180 6114 -1165 1331 -92 N ATOM 2410 CA VAL B 7 -9.765 1.530 -5.943 1.00 65.97 C ANISOU 2410 CA VAL B 7 8396 10320 6349 -1182 1491 362 C ATOM 2411 C VAL B 7 -8.514 1.838 -6.756 1.00 57.44 C ANISOU 2411 C VAL B 7 7545 8883 5395 -1143 1151 302 C ATOM 2412 O VAL B 7 -8.484 1.629 -7.974 1.00 50.30 O ANISOU 2412 O VAL B 7 6715 7562 4836 -1307 1071 230 O ATOM 2413 CB VAL B 7 -10.241 0.090 -6.174 1.00 74.94 C ANISOU 2413 CB VAL B 7 9484 11194 7794 -1492 1924 696 C ATOM 2414 CG1 VAL B 7 -9.142 -0.897 -5.809 1.00 76.49 C ANISOU 2414 CG1 VAL B 7 9969 11215 7880 -1448 2108 1192 C ATOM 2415 CG2 VAL B 7 -11.504 -0.186 -5.366 1.00 76.70 C ANISOU 2415 CG2 VAL B 7 9432 11710 8002 -1550 2365 745 C ATOM 2416 N GLU B 8 -7.479 2.337 -6.087 1.00 53.19 N ANISOU 2416 N GLU B 8 7110 8500 4600 -896 958 303 N ATOM 2417 CA GLU B 8 -6.212 2.667 -6.723 1.00 59.37 C ANISOU 2417 CA GLU B 8 8043 8940 5573 -857 698 233 C ATOM 2418 C GLU B 8 -5.219 1.530 -6.519 1.00 61.25 C ANISOU 2418 C GLU B 8 8434 9030 5809 -863 820 676 C ATOM 2419 O GLU B 8 -5.153 0.935 -5.439 1.00 66.50 O ANISOU 2419 O GLU B 8 9119 10016 6134 -704 982 949 O ATOM 2420 CB GLU B 8 -5.647 3.969 -6.154 1.00 67.00 C ANISOU 2420 CB GLU B 8 8945 10133 6378 -602 387 -146 C ATOM 2421 CG GLU B 8 -6.539 5.184 -6.364 1.00 69.46 C ANISOU 2421 CG GLU B 8 9160 10558 6673 -548 281 -582 C ATOM 2422 CD GLU B 8 -6.397 6.205 -5.251 1.00 63.48 C ANISOU 2422 CD GLU B 8 8302 10227 5592 -277 80 -898 C ATOM 2423 OE1 GLU B 8 -6.079 5.800 -4.115 1.00 67.54 O ANISOU 2423 OE1 GLU B 8 8796 11108 5759 -96 73 -744 O ATOM 2424 OE2 GLU B 8 -6.603 7.409 -5.507 1.00 56.88 O1- ANISOU 2424 OE2 GLU B 8 7441 9351 4820 -198 -64 -1308 O1- ATOM 2425 N SER B 9 -4.448 1.232 -7.562 1.00 51.98 N ANISOU 2425 N SER B 9 7407 7362 4981 -984 772 764 N ATOM 2426 CA SER B 9 -3.491 0.138 -7.528 1.00 50.79 C ANISOU 2426 CA SER B 9 7416 7017 4866 -985 895 1187 C ATOM 2427 C SER B 9 -2.211 0.561 -8.233 1.00 45.36 C ANISOU 2427 C SER B 9 6797 5959 4480 -936 683 1088 C ATOM 2428 O SER B 9 -2.194 1.513 -9.017 1.00 48.87 O ANISOU 2428 O SER B 9 7237 6152 5180 -961 551 761 O ATOM 2429 CB SER B 9 -4.059 -1.125 -8.192 1.00 50.24 C ANISOU 2429 CB SER B 9 7479 6619 4990 -1255 1225 1522 C ATOM 2430 OG SER B 9 -5.357 -1.419 -7.706 1.00 69.56 O ANISOU 2430 OG SER B 9 9785 9317 7327 -1365 1478 1534 O ATOM 2431 N GLY B 10 -1.131 -0.166 -7.945 1.00 49.30 N ANISOU 2431 N GLY B 10 6311 5763 6658 1163 -606 275 N ATOM 2432 CA GLY B 10 0.100 -0.048 -8.700 1.00 52.26 C ANISOU 2432 CA GLY B 10 6472 6671 6712 1322 -613 84 C ATOM 2433 C GLY B 10 1.175 0.837 -8.105 1.00 59.42 C ANISOU 2433 C GLY B 10 7148 8157 7270 1187 -508 156 C ATOM 2434 O GLY B 10 2.263 0.926 -8.685 1.00 66.60 O ANISOU 2434 O GLY B 10 7848 9529 7928 1327 -500 2 O ATOM 2435 N GLY B 11 0.918 1.490 -6.979 1.00 54.99 N ANISOU 2435 N GLY B 11 6629 7588 6678 886 -400 367 N ATOM 2436 CA GLY B 11 1.912 2.356 -6.381 1.00 59.49 C ANISOU 2436 CA GLY B 11 7014 8714 6874 683 -298 443 C ATOM 2437 C GLY B 11 3.027 1.563 -5.710 1.00 58.82 C ANISOU 2437 C GLY B 11 6772 8926 6652 960 -441 564 C ATOM 2438 O GLY B 11 3.178 0.355 -5.885 1.00 63.28 O ANISOU 2438 O GLY B 11 7319 9295 7431 1370 -601 548 O ATOM 2439 N GLY B 12 3.822 2.280 -4.917 1.00 58.31 N ANISOU 2439 N GLY B 12 6576 9330 6249 701 -383 712 N ATOM 2440 CA GLY B 12 4.867 1.646 -4.139 1.00 58.39 C ANISOU 2440 CA GLY B 12 6402 9641 6141 869 -565 932 C ATOM 2441 C GLY B 12 6.239 2.261 -4.328 1.00 58.13 C ANISOU 2441 C GLY B 12 6030 10303 5753 848 -565 924 C ATOM 2442 O GLY B 12 6.363 3.436 -4.689 1.00 53.41 O ANISOU 2442 O GLY B 12 5401 10009 4884 544 -382 793 O ATOM 2443 N LEU B 13 7.276 1.458 -4.101 1.00 63.07 N ANISOU 2443 N LEU B 13 6375 11162 6428 1179 -773 1080 N ATOM 2444 CA LEU B 13 8.661 1.907 -4.128 1.00 66.87 C ANISOU 2444 CA LEU B 13 6477 12303 6627 1177 -810 1142 C ATOM 2445 C LEU B 13 9.321 1.538 -5.451 1.00 68.34 C ANISOU 2445 C LEU B 13 6384 12613 6969 1630 -759 826 C ATOM 2446 O LEU B 13 9.125 0.434 -5.967 1.00 72.79 O ANISOU 2446 O LEU B 13 6941 12784 7930 2069 -806 705 O ATOM 2447 CB LEU B 13 9.443 1.282 -2.973 1.00 74.83 C ANISOU 2447 CB LEU B 13 7290 13498 7645 1208 -1091 1585 C ATOM 2448 CG LEU B 13 8.949 1.569 -1.556 1.00 82.74 C ANISOU 2448 CG LEU B 13 8582 14443 8414 672 -1152 1922 C ATOM 2449 CD1 LEU B 13 9.412 0.478 -0.610 1.00 90.76 C ANISOU 2449 CD1 LEU B 13 9467 15408 9610 819 -1519 2376 C ATOM 2450 CD2 LEU B 13 9.457 2.917 -1.089 1.00 83.71 C ANISOU 2450 CD2 LEU B 13 8688 15132 7987 93 -1015 1979 C ATOM 2451 N VAL B 14 10.114 2.466 -5.988 1.00 62.67 N ANISOU 2451 N VAL B 14 5450 12436 5925 1487 -632 675 N ATOM 2452 CA VAL B 14 10.877 2.241 -7.209 1.00 64.62 C ANISOU 2452 CA VAL B 14 5420 12884 6247 1827 -530 351 C ATOM 2453 C VAL B 14 12.198 2.989 -7.116 1.00 66.35 C ANISOU 2453 C VAL B 14 5257 13815 6138 1700 -509 419 C ATOM 2454 O VAL B 14 12.294 4.042 -6.480 1.00 70.04 O ANISOU 2454 O VAL B 14 5778 14629 6206 1240 -497 584 O ATOM 2455 CB VAL B 14 10.115 2.695 -8.472 1.00 84.12 C ANISOU 2455 CB VAL B 14 8141 15177 8645 1718 -334 -55 C ATOM 2456 CG1 VAL B 14 9.116 1.642 -8.903 1.00 77.66 C ANISOU 2456 CG1 VAL B 14 7586 13698 8224 1981 -363 -187 C ATOM 2457 CG2 VAL B 14 9.449 4.039 -8.223 1.00 57.36 C ANISOU 2457 CG2 VAL B 14 4989 11880 4927 1170 -245 -1 C ATOM 2458 N ARG B 15 13.218 2.439 -7.772 1.00 70.21 N ANISOU 2458 N ARG B 15 5356 14503 6819 2095 -470 270 N ATOM 2459 CA ARG B 15 14.484 3.139 -7.890 1.00 72.06 C ANISOU 2459 CA ARG B 15 5194 15411 6776 2000 -417 277 C ATOM 2460 C ARG B 15 14.341 4.309 -8.863 1.00 73.95 C ANISOU 2460 C ARG B 15 5586 15925 6588 1667 -175 -91 C ATOM 2461 O ARG B 15 13.477 4.288 -9.746 1.00 66.45 O ANISOU 2461 O ARG B 15 4941 14632 5675 1651 -48 -401 O ATOM 2462 CB ARG B 15 15.582 2.191 -8.371 1.00 77.65 C ANISOU 2462 CB ARG B 15 5406 16189 7907 2531 -384 192 C ATOM 2463 CG ARG B 15 15.900 1.052 -7.411 1.00 96.07 C ANISOU 2463 CG ARG B 15 7483 18282 10735 2875 -662 631 C ATOM 2464 CD ARG B 15 17.150 0.296 -7.847 1.00109.00 C ANISOU 2464 CD ARG B 15 8517 20042 12858 3374 -594 588 C ATOM 2465 NE ARG B 15 16.952 -0.422 -9.104 1.00118.42 N ANISOU 2465 NE ARG B 15 9759 20837 14400 3748 -266 46 N ATOM 2466 CZ ARG B 15 17.010 -1.744 -9.229 1.00126.69 C ANISOU 2466 CZ ARG B 15 10639 21375 16120 4262 -235 24 C ATOM 2467 NH1 ARG B 15 17.275 -2.501 -8.173 1.00131.03 N ANISOU 2467 NH1 ARG B 15 10928 21752 17106 4492 -560 560 N ATOM 2468 NH2 ARG B 15 16.814 -2.311 -10.412 1.00128.45 N ANISOU 2468 NH2 ARG B 15 10967 21257 16582 4506 124 -527 N ATOM 2469 N PRO B 16 15.155 5.354 -8.705 1.00 73.24 N ANISOU 2469 N PRO B 16 5296 16451 6080 1358 -135 -27 N ATOM 2470 CA PRO B 16 15.127 6.461 -9.669 1.00 70.07 C ANISOU 2470 CA PRO B 16 5004 16334 5286 1045 81 -357 C ATOM 2471 C PRO B 16 15.362 5.963 -11.086 1.00 69.59 C ANISOU 2471 C PRO B 16 4861 16206 5374 1334 268 -811 C ATOM 2472 O PRO B 16 16.182 5.074 -11.325 1.00 72.40 O ANISOU 2472 O PRO B 16 4869 16594 6044 1753 313 -897 O ATOM 2473 CB PRO B 16 16.262 7.373 -9.193 1.00 70.89 C ANISOU 2473 CB PRO B 16 4796 17144 4995 775 73 -186 C ATOM 2474 CG PRO B 16 16.345 7.106 -7.727 1.00 72.03 C ANISOU 2474 CG PRO B 16 4895 17286 5187 693 -169 301 C ATOM 2475 CD PRO B 16 16.038 5.642 -7.562 1.00 72.07 C ANISOU 2475 CD PRO B 16 4864 16760 5758 1190 -316 396 C ATOM 2476 N GLY B 17 14.618 6.539 -12.027 1.00 67.61 N ANISOU 2476 N GLY B 17 4933 15836 4921 1071 390 -1092 N ATOM 2477 CA GLY B 17 14.655 6.091 -13.401 1.00 68.45 C ANISOU 2477 CA GLY B 17 5087 15823 5097 1207 561 -1533 C ATOM 2478 C GLY B 17 13.770 4.904 -13.706 1.00 70.47 C ANISOU 2478 C GLY B 17 5583 15432 5761 1496 544 -1652 C ATOM 2479 O GLY B 17 13.663 4.518 -14.877 1.00 71.96 O ANISOU 2479 O GLY B 17 5890 15489 5963 1525 708 -2042 O ATOM 2480 N GLY B 18 13.134 4.312 -12.698 1.00 69.89 N ANISOU 2480 N GLY B 18 5615 14945 5995 1658 356 -1335 N ATOM 2481 CA GLY B 18 12.250 3.185 -12.899 1.00 67.02 C ANISOU 2481 CA GLY B 18 5500 13937 6028 1917 317 -1415 C ATOM 2482 C GLY B 18 10.870 3.616 -13.357 1.00 66.20 C ANISOU 2482 C GLY B 18 5855 13476 5820 1571 264 -1462 C ATOM 2483 O GLY B 18 10.600 4.788 -13.628 1.00 61.77 O ANISOU 2483 O GLY B 18 5407 13143 4920 1143 272 -1449 O ATOM 2484 N SER B 19 9.975 2.633 -13.435 1.00 63.30 N ANISOU 2484 N SER B 19 5736 12516 5797 1761 199 -1488 N ATOM 2485 CA SER B 19 8.633 2.850 -13.953 1.00 67.77 C ANISOU 2485 CA SER B 19 6707 12685 6359 1468 123 -1516 C ATOM 2486 C SER B 19 7.587 2.248 -13.025 1.00 61.87 C ANISOU 2486 C SER B 19 6166 11371 5972 1582 -42 -1233 C ATOM 2487 O SER B 19 7.821 1.231 -12.367 1.00 60.92 O ANISOU 2487 O SER B 19 5951 11040 6155 1966 -86 -1137 O ATOM 2488 CB SER B 19 8.472 2.255 -15.360 1.00 62.79 C ANISOU 2488 CB SER B 19 6250 11890 5714 1466 235 -1928 C ATOM 2489 OG SER B 19 9.261 2.960 -16.303 1.00 87.27 O ANISOU 2489 OG SER B 19 9237 15502 8418 1228 395 -2201 O ATOM 2490 N LEU B 20 6.426 2.900 -12.987 1.00 47.43 N ANISOU 2490 N LEU B 20 5412 7389 5220 752 -1065 -150 N ATOM 2491 CA LEU B 20 5.252 2.418 -12.274 1.00 48.60 C ANISOU 2491 CA LEU B 20 5690 7420 5354 680 -1051 41 C ATOM 2492 C LEU B 20 4.020 2.664 -13.128 1.00 43.83 C ANISOU 2492 C LEU B 20 5093 6677 4883 720 -879 20 C ATOM 2493 O LEU B 20 3.946 3.649 -13.866 1.00 46.07 O ANISOU 2493 O LEU B 20 5344 7003 5157 753 -687 -91 O ATOM 2494 CB LEU B 20 5.060 3.115 -10.920 1.00 50.47 C ANISOU 2494 CB LEU B 20 6047 7813 5316 464 -922 82 C ATOM 2495 CG LEU B 20 5.872 2.644 -9.719 1.00 58.95 C ANISOU 2495 CG LEU B 20 7130 9115 6155 412 -1137 196 C ATOM 2496 CD1 LEU B 20 5.557 3.508 -8.512 1.00 66.42 C ANISOU 2496 CD1 LEU B 20 8193 10284 6761 184 -962 135 C ATOM 2497 CD2 LEU B 20 5.589 1.180 -9.424 1.00 59.59 C ANISOU 2497 CD2 LEU B 20 7238 9052 6352 538 -1341 528 C ATOM 2498 N ARG B 21 3.045 1.767 -13.012 1.00 37.34 N ANISOU 2498 N ARG B 21 4290 5696 4203 719 -941 152 N ATOM 2499 CA ARG B 21 1.749 1.931 -13.662 1.00 43.08 C ANISOU 2499 CA ARG B 21 4969 6350 5050 734 -813 133 C ATOM 2500 C ARG B 21 0.675 1.955 -12.584 1.00 47.90 C ANISOU 2500 C ARG B 21 5660 6909 5629 564 -658 316 C ATOM 2501 O ARG B 21 0.468 0.958 -11.884 1.00 47.36 O ANISOU 2501 O ARG B 21 5629 6724 5642 493 -753 493 O ATOM 2502 CB ARG B 21 1.488 0.816 -14.673 1.00 45.86 C ANISOU 2502 CB ARG B 21 5194 6575 5654 858 -1013 33 C ATOM 2503 CG ARG B 21 0.136 0.920 -15.363 1.00 42.56 C ANISOU 2503 CG ARG B 21 4662 6167 5341 867 -941 -22 C ATOM 2504 CD ARG B 21 -0.018 -0.138 -16.442 1.00 46.53 C ANISOU 2504 CD ARG B 21 5011 6605 6063 966 -1161 -244 C ATOM 2505 NE ARG B 21 1.007 -0.012 -17.475 1.00 55.23 N ANISOU 2505 NE ARG B 21 6068 7865 7054 1163 -1248 -448 N ATOM 2506 CZ ARG B 21 1.101 -0.806 -18.537 1.00 56.52 C ANISOU 2506 CZ ARG B 21 6101 8046 7327 1286 -1422 -729 C ATOM 2507 NH1 ARG B 21 0.230 -1.790 -18.710 1.00 51.73 N ANISOU 2507 NH1 ARG B 21 5389 7272 6994 1204 -1546 -874 N ATOM 2508 NH2 ARG B 21 2.066 -0.616 -19.426 1.00 53.33 N ANISOU 2508 NH2 ARG B 21 5658 7835 6771 1473 -1450 -899 N ATOM 2509 N LEU B 22 0.005 3.092 -12.443 1.00 41.89 N ANISOU 2509 N LEU B 22 4922 6221 4773 515 -385 295 N ATOM 2510 CA LEU B 22 -1.147 3.196 -11.564 1.00 41.73 C ANISOU 2510 CA LEU B 22 4938 6177 4740 380 -181 432 C ATOM 2511 C LEU B 22 -2.420 2.892 -12.340 1.00 45.36 C ANISOU 2511 C LEU B 22 5220 6563 5452 437 -160 447 C ATOM 2512 O LEU B 22 -2.541 3.215 -13.525 1.00 40.69 O ANISOU 2512 O LEU B 22 4499 6024 4935 598 -204 330 O ATOM 2513 CB LEU B 22 -1.245 4.592 -10.945 1.00 41.57 C ANISOU 2513 CB LEU B 22 5012 6253 4530 308 140 356 C ATOM 2514 CG LEU B 22 0.016 5.146 -10.283 1.00 47.53 C ANISOU 2514 CG LEU B 22 5889 7133 5037 218 133 224 C ATOM 2515 CD1 LEU B 22 -0.277 6.477 -9.609 1.00 44.63 C ANISOU 2515 CD1 LEU B 22 5607 6803 4547 105 495 72 C ATOM 2516 CD2 LEU B 22 0.584 4.148 -9.287 1.00 47.54 C ANISOU 2516 CD2 LEU B 22 5966 7246 4852 129 -92 366 C ATOM 2517 N SER B 23 -3.371 2.262 -11.660 1.00 40.21 N ANISOU 2517 N SER B 23 4536 5830 4912 301 -92 602 N ATOM 2518 CA SER B 23 -4.687 2.010 -12.222 1.00 44.05 C ANISOU 2518 CA SER B 23 4797 6281 5658 303 -53 597 C ATOM 2519 C SER B 23 -5.747 2.374 -11.196 1.00 49.66 C ANISOU 2519 C SER B 23 5501 7018 6351 164 267 755 C ATOM 2520 O SER B 23 -5.524 2.282 -9.985 1.00 49.30 O ANISOU 2520 O SER B 23 5632 6980 6118 27 396 905 O ATOM 2521 CB SER B 23 -4.857 0.548 -12.657 1.00 42.62 C ANISOU 2521 CB SER B 23 4490 5914 5791 245 -309 575 C ATOM 2522 OG SER B 23 -4.802 -0.325 -11.547 1.00 58.40 O ANISOU 2522 OG SER B 23 6605 7733 7852 74 -276 817 O ATOM 2523 N CYS B 24 -6.904 2.792 -11.695 1.00 47.56 N ANISOU 2523 N CYS B 24 5004 6816 6251 222 396 723 N ATOM 2524 CA CYS B 24 -8.008 3.219 -10.849 1.00 47.41 C ANISOU 2524 CA CYS B 24 4916 6839 6258 128 741 843 C ATOM 2525 C CYS B 24 -9.314 2.799 -11.499 1.00 49.37 C ANISOU 2525 C CYS B 24 4795 7113 6848 126 710 834 C ATOM 2526 O CYS B 24 -9.536 3.073 -12.682 1.00 48.18 O ANISOU 2526 O CYS B 24 4439 7081 6785 313 548 702 O ATOM 2527 CB CYS B 24 -7.982 4.734 -10.641 1.00 44.88 C ANISOU 2527 CB CYS B 24 4685 6612 5754 259 1045 777 C ATOM 2528 SG CYS B 24 -9.398 5.409 -9.755 1.00 62.77 S ANISOU 2528 SG CYS B 24 6821 8938 8089 216 1522 858 S ATOM 2529 N VAL B 25 -10.176 2.146 -10.727 1.00 50.04 N ANISOU 2529 N VAL B 25 4773 7131 7109 -88 870 983 N ATOM 2530 CA VAL B 25 -11.432 1.631 -11.250 1.00 58.81 C ANISOU 2530 CA VAL B 25 5477 8266 8603 -157 839 948 C ATOM 2531 C VAL B 25 -12.563 2.006 -10.304 1.00 65.26 C ANISOU 2531 C VAL B 25 6156 9154 9487 -260 1260 1113 C ATOM 2532 O VAL B 25 -12.379 2.107 -9.087 1.00 61.89 O ANISOU 2532 O VAL B 25 5973 8697 8844 -379 1542 1288 O ATOM 2533 CB VAL B 25 -11.369 0.099 -11.464 1.00 62.76 C ANISOU 2533 CB VAL B 25 5892 8527 9425 -374 582 924 C ATOM 2534 CG1 VAL B 25 -11.273 -0.632 -10.129 1.00 67.36 C ANISOU 2534 CG1 VAL B 25 6677 8894 10022 -619 796 1234 C ATOM 2535 CG2 VAL B 25 -12.563 -0.389 -12.275 1.00 68.71 C ANISOU 2535 CG2 VAL B 25 6166 9344 10598 -457 469 749 C ATOM 2536 N ASP B 26 -13.733 2.255 -10.884 1.00 73.26 N ANISOU 2536 N ASP B 26 6750 10321 10766 -192 1304 1045 N ATOM 2537 CA ASP B 26 -15.001 2.327 -10.164 1.00 79.94 C ANISOU 2537 CA ASP B 26 7323 11235 11814 -318 1674 1177 C ATOM 2538 C ASP B 26 -15.860 1.227 -10.780 1.00 84.11 C ANISOU 2538 C ASP B 26 7405 11738 12814 -518 1463 1093 C ATOM 2539 O ASP B 26 -16.589 1.461 -11.748 1.00 83.36 O ANISOU 2539 O ASP B 26 6892 11871 12911 -381 1295 926 O ATOM 2540 CB ASP B 26 -15.658 3.708 -10.276 1.00 74.79 C ANISOU 2540 CB ASP B 26 6505 10800 11113 -29 1945 1157 C ATOM 2541 CG ASP B 26 -16.893 3.840 -9.401 1.00 81.88 C ANISOU 2541 CG ASP B 26 7136 11777 12196 -140 2394 1285 C ATOM 2542 OD1 ASP B 26 -17.134 2.938 -8.573 1.00 84.80 O ANISOU 2542 OD1 ASP B 26 7522 12043 12655 -458 2543 1429 O ATOM 2543 OD2 ASP B 26 -17.627 4.842 -9.539 1.00 81.14 O ANISOU 2543 OD2 ASP B 26 6806 11844 12180 109 2628 1270 O ATOM 2544 N SER B 27 -15.749 0.017 -10.224 1.00 83.86 N ANISOU 2544 N SER B 27 7449 11433 12980 -843 1467 1210 N ATOM 2545 CA SER B 27 -16.395 -1.151 -10.814 1.00 85.65 C ANISOU 2545 CA SER B 27 7285 11526 13731 -1096 1260 1066 C ATOM 2546 C SER B 27 -17.913 -1.038 -10.828 1.00 87.46 C ANISOU 2546 C SER B 27 6950 11957 14325 -1204 1466 1044 C ATOM 2547 O SER B 27 -18.569 -1.764 -11.582 1.00 94.39 O ANISOU 2547 O SER B 27 7382 12842 15640 -1376 1234 802 O ATOM 2548 CB SER B 27 -15.980 -2.415 -10.059 1.00 88.85 C ANISOU 2548 CB SER B 27 7912 11506 14340 -1414 1328 1284 C ATOM 2549 OG SER B 27 -14.570 -2.545 -10.013 1.00 84.18 O ANISOU 2549 OG SER B 27 7795 10758 13430 -1287 1128 1323 O ATOM 2550 N GLU B 28 -18.486 -0.151 -10.018 1.00 91.55 N ANISOU 2550 N GLU B 28 7445 12651 14687 -1111 1899 1247 N ATOM 2551 CA GLU B 28 -19.931 0.022 -9.966 1.00 97.88 C ANISOU 2551 CA GLU B 28 7676 13670 15843 -1179 2140 1248 C ATOM 2552 C GLU B 28 -20.464 0.899 -11.092 1.00101.04 C ANISOU 2552 C GLU B 28 7673 14461 16255 -828 1907 1023 C ATOM 2553 O GLU B 28 -21.679 1.118 -11.159 1.00103.60 O ANISOU 2553 O GLU B 28 7452 15031 16879 -822 2060 1011 O ATOM 2554 CB GLU B 28 -20.344 0.614 -8.613 1.00 94.26 C ANISOU 2554 CB GLU B 28 7344 13260 15213 -1196 2748 1543 C ATOM 2555 CG GLU B 28 -19.859 -0.176 -7.406 1.00 94.45 C ANISOU 2555 CG GLU B 28 7764 13004 15118 -1498 3015 1854 C ATOM 2556 CD GLU B 28 -18.455 0.209 -6.972 1.00 94.73 C ANISOU 2556 CD GLU B 28 8455 12969 14570 -1336 2945 1925 C ATOM 2557 OE1 GLU B 28 -18.255 1.373 -6.563 1.00 95.23 O ANISOU 2557 OE1 GLU B 28 8725 13226 14233 -1094 3168 1895 O ATOM 2558 OE2 GLU B 28 -17.549 -0.649 -7.048 1.00 91.36 O ANISOU 2558 OE2 GLU B 28 8309 12284 14122 -1451 2671 1986 O ATOM 2559 N ARG B 29 -19.594 1.404 -11.965 1.00101.06 N ANISOU 2559 N ARG B 29 7909 14552 15939 -519 1559 884 N ATOM 2560 CA ARG B 29 -19.938 2.304 -13.063 1.00108.41 C ANISOU 2560 CA ARG B 29 8531 15873 16788 -114 1337 768 C ATOM 2561 C ARG B 29 -20.639 3.571 -12.586 1.00104.69 C ANISOU 2561 C ARG B 29 7924 15574 16279 185 1768 966 C ATOM 2562 O ARG B 29 -21.249 4.279 -13.398 1.00111.64 O ANISOU 2562 O ARG B 29 8413 16796 17208 532 1652 953 O ATOM 2563 CB ARG B 29 -20.798 1.602 -14.124 1.00117.36 C ANISOU 2563 CB ARG B 29 9025 17298 18269 -213 937 490 C ATOM 2564 CG ARG B 29 -20.226 0.289 -14.629 1.00120.23 C ANISOU 2564 CG ARG B 29 9461 17451 18769 -531 543 202 C ATOM 2565 CD ARG B 29 -18.776 0.441 -15.067 1.00116.73 C ANISOU 2565 CD ARG B 29 9575 16886 17892 -332 305 156 C ATOM 2566 NE ARG B 29 -18.268 -0.772 -15.701 1.00118.66 N ANISOU 2566 NE ARG B 29 9834 16961 18291 -571 -81 -179 N ATOM 2567 CZ ARG B 29 -18.173 -0.941 -17.015 1.00118.67 C ANISOU 2567 CZ ARG B 29 9607 17286 18196 -434 -540 -542 C ATOM 2568 NH1 ARG B 29 -18.544 0.030 -17.839 1.00117.20 N ANISOU 2568 NH1 ARG B 29 9163 17639 17728 -38 -687 -535 N ATOM 2569 NH2 ARG B 29 -17.700 -2.077 -17.505 1.00119.70 N ANISOU 2569 NH2 ARG B 29 9768 17209 18503 -670 -836 -904 N ATOM 2570 N THR B 30 -20.564 3.880 -11.290 1.00 94.30 N ANISOU 2570 N THR B 30 6915 14048 14866 83 2269 1147 N ATOM 2571 CA THR B 30 -21.216 5.062 -10.745 1.00 86.52 C ANISOU 2571 CA THR B 30 5821 13174 13879 354 2744 1272 C ATOM 2572 C THR B 30 -20.422 6.340 -10.979 1.00 74.19 C ANISOU 2572 C THR B 30 4637 11557 11995 764 2806 1293 C ATOM 2573 O THR B 30 -20.934 7.427 -10.691 1.00 87.95 O ANISOU 2573 O THR B 30 6315 13331 13773 1045 3167 1349 O ATOM 2574 CB THR B 30 -21.465 4.882 -9.246 1.00 79.19 C ANISOU 2574 CB THR B 30 5066 12095 12928 72 3288 1404 C ATOM 2575 OG1 THR B 30 -20.228 4.596 -8.582 1.00 89.50 O ANISOU 2575 OG1 THR B 30 7012 13148 13845 -100 3288 1438 O ATOM 2576 CG2 THR B 30 -22.440 3.738 -9.000 1.00 83.57 C ANISOU 2576 CG2 THR B 30 5163 12688 13902 -321 3340 1448 C ATOM 2577 N SER B 31 -19.197 6.241 -11.488 1.00 64.11 N ANISOU 2577 N SER B 31 4940 13261 6157 423 233 -642 N ATOM 2578 CA SER B 31 -18.394 7.418 -11.788 1.00 66.47 C ANISOU 2578 CA SER B 31 5414 13397 6444 688 188 -861 C ATOM 2579 C SER B 31 -17.336 7.040 -12.813 1.00 57.31 C ANISOU 2579 C SER B 31 4474 11897 5404 632 63 -676 C ATOM 2580 O SER B 31 -17.040 5.862 -13.022 1.00 58.60 O ANISOU 2580 O SER B 31 4686 11971 5607 339 47 -363 O ATOM 2581 CB SER B 31 -17.734 7.993 -10.531 1.00 63.86 C ANISOU 2581 CB SER B 31 5163 13222 5879 662 312 -975 C ATOM 2582 OG SER B 31 -16.685 7.154 -10.080 1.00 65.05 O ANISOU 2582 OG SER B 31 5446 13342 5927 358 323 -691 O ATOM 2583 N TYR B 32 -16.766 8.062 -13.445 1.00 57.28 N ANISOU 2583 N TYR B 32 4738 11552 5473 901 -33 -856 N ATOM 2584 CA TYR B 32 -15.725 7.870 -14.447 1.00 55.06 C ANISOU 2584 CA TYR B 32 4872 10728 5322 852 -165 -684 C ATOM 2585 C TYR B 32 -14.387 8.336 -13.892 1.00 53.23 C ANISOU 2585 C TYR B 32 4905 10329 4991 809 -88 -690 C ATOM 2586 O TYR B 32 -14.159 9.553 -13.801 1.00 52.95 O ANISOU 2586 O TYR B 32 5015 10168 4938 1059 -84 -965 O ATOM 2587 CB TYR B 32 -16.052 8.638 -15.729 1.00 55.68 C ANISOU 2587 CB TYR B 32 5159 10419 5578 1167 -350 -838 C ATOM 2588 CG TYR B 32 -17.400 8.343 -16.344 1.00 59.28 C ANISOU 2588 CG TYR B 32 5350 11029 6146 1248 -483 -862 C ATOM 2589 CD1 TYR B 32 -17.721 7.069 -16.789 1.00 67.83 C ANISOU 2589 CD1 TYR B 32 6334 12144 7294 974 -552 -605 C ATOM 2590 CD2 TYR B 32 -18.341 9.350 -16.512 1.00 59.93 C ANISOU 2590 CD2 TYR B 32 5280 11200 6290 1600 -549 -1140 C ATOM 2591 CE1 TYR B 32 -18.947 6.798 -17.365 1.00 65.72 C ANISOU 2591 CE1 TYR B 32 5812 12018 7141 1024 -704 -632 C ATOM 2592 CE2 TYR B 32 -19.570 9.090 -17.089 1.00 65.37 C ANISOU 2592 CE2 TYR B 32 5695 12034 7107 1676 -701 -1150 C ATOM 2593 CZ TYR B 32 -19.867 7.812 -17.513 1.00 69.12 C ANISOU 2593 CZ TYR B 32 6103 12519 7639 1361 -775 -893 C ATOM 2594 OH TYR B 32 -21.090 7.544 -18.087 1.00 79.75 O ANISOU 2594 OH TYR B 32 7268 13903 9131 1368 -912 -888 O ATOM 2595 N PRO B 33 -13.479 7.438 -13.510 1.00 49.61 N ANISOU 2595 N PRO B 33 4509 9853 4486 501 -33 -398 N ATOM 2596 CA PRO B 33 -12.115 7.873 -13.170 1.00 47.96 C ANISOU 2596 CA PRO B 33 4565 9416 4243 459 -9 -378 C ATOM 2597 C PRO B 33 -11.458 8.524 -14.377 1.00 50.71 C ANISOU 2597 C PRO B 33 5302 9165 4800 649 -113 -434 C ATOM 2598 O PRO B 33 -11.341 7.917 -15.445 1.00 43.28 O ANISOU 2598 O PRO B 33 4529 7890 4028 604 -183 -243 O ATOM 2599 CB PRO B 33 -11.414 6.569 -12.769 1.00 44.50 C ANISOU 2599 CB PRO B 33 4085 9041 3782 98 42 16 C ATOM 2600 CG PRO B 33 -12.527 5.633 -12.405 1.00 58.74 C ANISOU 2600 CG PRO B 33 5539 11270 5510 -53 101 130 C ATOM 2601 CD PRO B 33 -13.665 5.992 -13.307 1.00 54.03 C ANISOU 2601 CD PRO B 33 4878 10613 5037 176 13 -67 C ATOM 2602 N MET B 34 -11.046 9.782 -14.210 1.00 44.83 N ANISOU 2602 N MET B 34 4721 8276 4037 861 -109 -706 N ATOM 2603 CA MET B 34 -10.529 10.551 -15.336 1.00 50.68 C ANISOU 2603 CA MET B 34 5832 8454 4971 1076 -186 -789 C ATOM 2604 C MET B 34 -9.345 11.446 -15.009 1.00 52.09 C ANISOU 2604 C MET B 34 6244 8380 5169 1107 -148 -904 C ATOM 2605 O MET B 34 -8.750 11.988 -15.944 1.00 47.93 O ANISOU 2605 O MET B 34 6045 7346 4821 1243 -182 -922 O ATOM 2606 CB MET B 34 -11.643 11.420 -15.942 1.00 48.92 C ANISOU 2606 CB MET B 34 5593 8201 4792 1424 -260 -1065 C ATOM 2607 CG MET B 34 -12.708 10.647 -16.707 1.00 56.64 C ANISOU 2607 CG MET B 34 6427 9260 5833 1426 -362 -945 C ATOM 2608 SD MET B 34 -14.147 11.655 -17.121 1.00 63.39 S ANISOU 2608 SD MET B 34 7134 10221 6730 1835 -463 -1264 S ATOM 2609 CE MET B 34 -13.388 12.985 -18.051 1.00 66.74 C ANISOU 2609 CE MET B 34 8050 10020 7287 2149 -522 -1422 C ATOM 2610 N GLY B 35 -8.977 11.629 -13.748 1.00 48.18 N ANISOU 2610 N GLY B 35 5607 8205 4492 979 -82 -982 N ATOM 2611 CA GLY B 35 -7.904 12.539 -13.398 1.00 41.74 C ANISOU 2611 CA GLY B 35 4994 7169 3696 995 -71 -1127 C ATOM 2612 C GLY B 35 -6.931 11.927 -12.420 1.00 48.71 C ANISOU 2612 C GLY B 35 5790 8246 4474 673 -58 -919 C ATOM 2613 O GLY B 35 -7.273 11.047 -11.628 1.00 42.56 O ANISOU 2613 O GLY B 35 4752 7909 3510 471 -30 -759 O ATOM 2614 N TRP B 36 -5.689 12.408 -12.485 1.00 48.98 N ANISOU 2614 N TRP B 36 6038 7933 4637 623 -83 -910 N ATOM 2615 CA TRP B 36 -4.628 12.019 -11.569 1.00 46.49 C ANISOU 2615 CA TRP B 36 5653 7758 4252 338 -111 -732 C ATOM 2616 C TRP B 36 -4.048 13.266 -10.922 1.00 46.58 C ANISOU 2616 C TRP B 36 5772 7732 4192 384 -138 -1059 C ATOM 2617 O TRP B 36 -3.636 14.199 -11.620 1.00 42.69 O ANISOU 2617 O TRP B 36 5528 6785 3907 556 -137 -1233 O ATOM 2618 CB TRP B 36 -3.511 11.252 -12.281 1.00 45.08 C ANISOU 2618 CB TRP B 36 5600 7168 4361 180 -124 -348 C ATOM 2619 CG TRP B 36 -3.887 9.886 -12.750 1.00 43.17 C ANISOU 2619 CG TRP B 36 5257 6968 4178 63 -91 5 C ATOM 2620 CD1 TRP B 36 -4.113 9.498 -14.037 1.00 37.84 C ANISOU 2620 CD1 TRP B 36 4748 5915 3714 159 -59 126 C ATOM 2621 CD2 TRP B 36 -4.066 8.718 -11.940 1.00 42.94 C ANISOU 2621 CD2 TRP B 36 4962 7364 3988 -185 -83 281 C ATOM 2622 NE1 TRP B 36 -4.424 8.162 -14.080 1.00 46.40 N ANISOU 2622 NE1 TRP B 36 5683 7155 4791 -22 -31 442 N ATOM 2623 CE2 TRP B 36 -4.405 7.659 -12.805 1.00 45.73 C ANISOU 2623 CE2 TRP B 36 5326 7556 4494 -231 -38 552 C ATOM 2624 CE3 TRP B 36 -3.978 8.466 -10.567 1.00 45.91 C ANISOU 2624 CE3 TRP B 36 5113 8238 4092 -378 -109 329 C ATOM 2625 CZ2 TRP B 36 -4.658 6.368 -12.343 1.00 43.07 C ANISOU 2625 CZ2 TRP B 36 4769 7518 4078 -461 -5 868 C ATOM 2626 CZ3 TRP B 36 -4.227 7.184 -10.110 1.00 50.61 C ANISOU 2626 CZ3 TRP B 36 5496 9143 4593 -596 -78 664 C ATOM 2627 CH2 TRP B 36 -4.565 6.151 -10.996 1.00 40.13 C ANISOU 2627 CH2 TRP B 36 4170 7616 3460 -633 -22 926 C ATOM 2628 N PHE B 37 -4.014 13.275 -9.594 1.00 43.68 N ANISOU 2628 N PHE B 37 5238 7835 3525 220 -160 -1142 N ATOM 2629 CA PHE B 37 -3.403 14.345 -8.825 1.00 49.04 C ANISOU 2629 CA PHE B 37 6013 8528 4092 198 -204 -1446 C ATOM 2630 C PHE B 37 -2.376 13.740 -7.881 1.00 51.80 C ANISOU 2630 C PHE B 37 6257 9099 4327 -141 -315 -1198 C ATOM 2631 O PHE B 37 -2.350 12.527 -7.656 1.00 52.91 O ANISOU 2631 O PHE B 37 6220 9467 4414 -330 -331 -822 O ATOM 2632 CB PHE B 37 -4.451 15.145 -8.032 1.00 52.09 C ANISOU 2632 CB PHE B 37 6330 9198 4262 340 -120 -1801 C ATOM 2633 CG PHE B 37 -5.364 15.969 -8.893 1.00 58.12 C ANISOU 2633 CG PHE B 37 7196 9657 5229 672 -38 -2011 C ATOM 2634 CD1 PHE B 37 -6.367 15.368 -9.640 1.00 60.62 C ANISOU 2634 CD1 PHE B 37 7402 10019 5612 810 1 -1896 C ATOM 2635 CD2 PHE B 37 -5.222 17.345 -8.953 1.00 54.38 C ANISOU 2635 CD2 PHE B 37 6923 8844 4894 820 -15 -2281 C ATOM 2636 CE1 PHE B 37 -7.207 16.125 -10.435 1.00 57.23 C ANISOU 2636 CE1 PHE B 37 7049 9318 5377 1097 33 -2043 C ATOM 2637 CE2 PHE B 37 -6.059 18.107 -9.744 1.00 59.87 C ANISOU 2637 CE2 PHE B 37 7700 9250 5796 1088 46 -2380 C ATOM 2638 CZ PHE B 37 -7.052 17.496 -10.486 1.00 63.20 C ANISOU 2638 CZ PHE B 37 7999 9736 6277 1229 54 -2260 C ATOM 2639 N ARG B 38 -1.522 14.596 -7.327 1.00 45.79 N ANISOU 2639 N ARG B 38 5602 8261 3536 -220 -404 -1404 N ATOM 2640 CA ARG B 38 -0.531 14.128 -6.374 1.00 51.02 C ANISOU 2640 CA ARG B 38 6157 9153 4075 -540 -554 -1189 C ATOM 2641 C ARG B 38 -0.221 15.242 -5.390 1.00 51.55 C ANISOU 2641 C ARG B 38 6312 9378 3897 -598 -636 -1595 C ATOM 2642 O ARG B 38 -0.398 16.427 -5.682 1.00 58.23 O ANISOU 2642 O ARG B 38 7345 9952 4828 -397 -574 -1987 O ATOM 2643 CB ARG B 38 0.750 13.649 -7.069 1.00 48.72 C ANISOU 2643 CB ARG B 38 5901 8414 4195 -666 -634 -817 C ATOM 2644 CG ARG B 38 1.662 14.766 -7.544 1.00 53.12 C ANISOU 2644 CG ARG B 38 6670 8467 5045 -607 -672 -1034 C ATOM 2645 CD ARG B 38 2.842 14.219 -8.328 1.00 49.26 C ANISOU 2645 CD ARG B 38 6194 7522 5000 -710 -697 -643 C ATOM 2646 NE ARG B 38 3.636 15.287 -8.927 1.00 48.31 N ANISOU 2646 NE ARG B 38 6283 6872 5201 -635 -687 -842 N ATOM 2647 CZ ARG B 38 4.659 15.085 -9.751 1.00 46.53 C ANISOU 2647 CZ ARG B 38 6114 6155 5412 -677 -656 -579 C ATOM 2648 NH1 ARG B 38 5.017 13.852 -10.079 1.00 42.33 N ANISOU 2648 NH1 ARG B 38 5451 5583 5050 -783 -630 -114 N ATOM 2649 NH2 ARG B 38 5.325 16.116 -10.248 1.00 49.66 N ANISOU 2649 NH2 ARG B 38 6700 6081 6088 -613 -626 -781 N ATOM 2650 N ARG B 39 0.239 14.840 -4.209 1.00 52.67 N ANISOU 2650 N ARG B 39 6337 9837 3839 -849 -748 -1431 N ATOM 2651 CA ARG B 39 0.637 15.778 -3.165 1.00 55.24 C ANISOU 2651 CA ARG B 39 6761 10224 4005 -929 -828 -1714 C ATOM 2652 C ARG B 39 1.976 15.321 -2.608 1.00 60.00 C ANISOU 2652 C ARG B 39 7282 10900 4616 -1245 -1074 -1440 C ATOM 2653 O ARG B 39 2.068 14.245 -2.008 1.00 52.34 O ANISOU 2653 O ARG B 39 6138 10202 3548 -1402 -1114 -1061 O ATOM 2654 CB ARG B 39 -0.415 15.863 -2.060 1.00 56.35 C ANISOU 2654 CB ARG B 39 6852 10712 3847 -878 -694 -1840 C ATOM 2655 CG ARG B 39 -0.092 16.882 -0.981 1.00 63.84 C ANISOU 2655 CG ARG B 39 7945 11716 4595 -950 -762 -2154 C ATOM 2656 CD ARG B 39 -1.104 16.813 0.148 1.00 77.75 C ANISOU 2656 CD ARG B 39 9651 13854 6038 -934 -625 -2236 C ATOM 2657 NE ARG B 39 -1.220 15.459 0.681 1.00 84.04 N ANISOU 2657 NE ARG B 39 10230 15001 6701 -1101 -635 -1838 N ATOM 2658 CZ ARG B 39 -0.405 14.943 1.595 1.00102.05 C ANISOU 2658 CZ ARG B 39 12466 17487 8821 -1354 -802 -1621 C ATOM 2659 NH1 ARG B 39 0.593 15.669 2.081 1.00104.06 N ANISOU 2659 NH1 ARG B 39 12866 17655 9017 -1481 -998 -1775 N ATOM 2660 NH2 ARG B 39 -0.585 13.701 2.022 1.00108.11 N ANISOU 2660 NH2 ARG B 39 13041 18528 9506 -1480 -779 -1246 N ATOM 2661 N ALA B 40 3.011 16.128 -2.826 1.00 74.27 N ANISOU 2661 N ALA B 40 10488 10998 6734 -733 -1556 -2179 N ATOM 2662 CA ALA B 40 4.308 15.875 -2.233 1.00 76.27 C ANISOU 2662 CA ALA B 40 10881 11167 6932 -831 -1851 -2041 C ATOM 2663 C ALA B 40 4.244 16.134 -0.728 1.00 83.40 C ANISOU 2663 C ALA B 40 11887 12468 7335 -872 -1965 -2464 C ATOM 2664 O ALA B 40 3.350 16.836 -0.251 1.00 85.33 O ANISOU 2664 O ALA B 40 12016 12981 7425 -765 -1854 -2975 O ATOM 2665 CB ALA B 40 5.367 16.755 -2.895 1.00 75.99 C ANISOU 2665 CB ALA B 40 10721 10600 7551 -740 -2123 -2006 C ATOM 2666 N PRO B 41 5.177 15.562 0.044 1.00 88.18 N ANISOU 2666 N PRO B 41 12689 13145 7670 -1025 -2209 -2296 N ATOM 2667 CA PRO B 41 5.102 15.699 1.512 1.00 91.65 C ANISOU 2667 CA PRO B 41 13255 14051 7516 -1119 -2318 -2657 C ATOM 2668 C PRO B 41 4.968 17.128 2.021 1.00 99.77 C ANISOU 2668 C PRO B 41 14116 15080 8714 -888 -2437 -3354 C ATOM 2669 O PRO B 41 4.247 17.358 3.000 1.00113.45 O ANISOU 2669 O PRO B 41 15843 17218 10046 -890 -2274 -3672 O ATOM 2670 CB PRO B 41 6.416 15.059 1.976 1.00 88.59 C ANISOU 2670 CB PRO B 41 13088 13499 7074 -1266 -2693 -2329 C ATOM 2671 CG PRO B 41 6.713 14.042 0.940 1.00 80.92 C ANISOU 2671 CG PRO B 41 12134 12238 6373 -1328 -2656 -1756 C ATOM 2672 CD PRO B 41 6.238 14.622 -0.365 1.00 84.23 C ANISOU 2672 CD PRO B 41 12298 12374 7330 -1135 -2399 -1780 C ATOM 2673 N GLY B 42 5.633 18.094 1.393 1.00 90.42 N ANISOU 2673 N GLY B 42 12791 13307 8256 -686 -2679 -3452 N ATOM 2674 CA GLY B 42 5.574 19.459 1.880 1.00 95.83 C ANISOU 2674 CA GLY B 42 13321 13891 9199 -455 -2913 -4118 C ATOM 2675 C GLY B 42 4.921 20.438 0.926 1.00100.78 C ANISOU 2675 C GLY B 42 13698 14132 10460 -231 -2900 -4336 C ATOM 2676 O GLY B 42 4.833 21.634 1.222 1.00102.43 O ANISOU 2676 O GLY B 42 13750 14135 11036 -15 -3149 -4854 O ATOM 2677 N LYS B 43 4.451 19.946 -0.216 1.00 92.59 N ANISOU 2677 N LYS B 43 12625 12958 9598 -285 -2629 -3897 N ATOM 2678 CA LYS B 43 3.888 20.786 -1.259 1.00 91.49 C ANISOU 2678 CA LYS B 43 12288 12395 10078 -123 -2664 -3975 C ATOM 2679 C LYS B 43 2.361 20.764 -1.204 1.00 86.44 C ANISOU 2679 C LYS B 43 11516 12141 9186 -5 -2352 -4357 C ATOM 2680 O LYS B 43 1.745 20.047 -0.413 1.00 86.60 O ANISOU 2680 O LYS B 43 11581 12807 8516 -93 -2057 -4508 O ATOM 2681 CB LYS B 43 4.387 20.330 -2.632 1.00 95.74 C ANISOU 2681 CB LYS B 43 12844 12550 10983 -266 -2591 -3267 C ATOM 2682 CG LYS B 43 5.182 21.377 -3.393 1.00103.03 C ANISOU 2682 CG LYS B 43 13657 12838 12650 -261 -2972 -3139 C ATOM 2683 CD LYS B 43 5.462 20.919 -4.817 1.00102.32 C ANISOU 2683 CD LYS B 43 13532 12533 12811 -432 -2819 -2490 C ATOM 2684 CE LYS B 43 6.210 21.981 -5.607 1.00105.41 C ANISOU 2684 CE LYS B 43 13800 12370 13881 -527 -3192 -2297 C ATOM 2685 NZ LYS B 43 6.372 21.591 -7.035 1.00103.45 N ANISOU 2685 NZ LYS B 43 13482 12027 13798 -727 -3011 -1703 N ATOM 2686 N GLU B 44 1.749 21.569 -2.065 1.00 83.85 N ANISOU 2686 N GLU B 44 11011 11416 9433 167 -2449 -4500 N ATOM 2687 CA GLU B 44 0.306 21.576 -2.242 1.00 86.79 C ANISOU 2687 CA GLU B 44 11214 12055 9708 302 -2184 -4839 C ATOM 2688 C GLU B 44 -0.102 20.495 -3.241 1.00 75.30 C ANISOU 2688 C GLU B 44 9840 10656 8116 132 -1796 -4192 C ATOM 2689 O GLU B 44 0.728 19.926 -3.953 1.00 70.55 O ANISOU 2689 O GLU B 44 9382 9803 7619 -42 -1789 -3538 O ATOM 2690 CB GLU B 44 -0.167 22.949 -2.723 1.00 96.38 C ANISOU 2690 CB GLU B 44 12206 12735 11678 583 -2572 -5305 C ATOM 2691 CG GLU B 44 -1.511 23.381 -2.167 1.00106.58 C ANISOU 2691 CG GLU B 44 13217 14388 12892 832 -2402 -5941 C ATOM 2692 CD GLU B 44 -1.374 24.219 -0.911 1.00115.00 C ANISOU 2692 CD GLU B 44 14120 15621 13955 1016 -2568 -6450 C ATOM 2693 OE1 GLU B 44 -0.532 25.141 -0.903 1.00120.36 O ANISOU 2693 OE1 GLU B 44 14807 15763 15160 1115 -3048 -6497 O ATOM 2694 OE2 GLU B 44 -2.100 23.951 0.069 1.00121.27 O1- ANISOU 2694 OE2 GLU B 44 14761 17093 14225 1040 -2230 -6776 O1- ATOM 2695 N ARG B 45 -1.402 20.213 -3.292 1.00 78.31 N ANISOU 2695 N ARG B 45 10088 11396 8270 197 -1482 -4430 N ATOM 2696 CA ARG B 45 -1.918 19.261 -4.268 1.00 77.82 C ANISOU 2696 CA ARG B 45 10077 11355 8135 73 -1152 -3882 C ATOM 2697 C ARG B 45 -1.753 19.825 -5.673 1.00 72.94 C ANISOU 2697 C ARG B 45 9431 10051 8232 141 -1365 -3554 C ATOM 2698 O ARG B 45 -2.064 20.993 -5.923 1.00 78.40 O ANISOU 2698 O ARG B 45 9974 10351 9465 340 -1686 -3932 O ATOM 2699 CB ARG B 45 -3.387 18.947 -3.985 1.00 86.12 C ANISOU 2699 CB ARG B 45 10951 12939 8832 124 -799 -4264 C ATOM 2700 CG ARG B 45 -3.977 17.857 -4.875 1.00 90.36 C ANISOU 2700 CG ARG B 45 11544 13545 9242 -16 -460 -3715 C ATOM 2701 CD ARG B 45 -5.320 17.362 -4.349 1.00100.80 C ANISOU 2701 CD ARG B 45 12694 15532 10072 -58 -78 -4049 C ATOM 2702 NE ARG B 45 -6.413 18.288 -4.635 1.00113.11 N ANISOU 2702 NE ARG B 45 13943 17004 12032 233 -117 -4675 N ATOM 2703 CZ ARG B 45 -7.626 18.201 -4.096 1.00122.99 C ANISOU 2703 CZ ARG B 45 14924 18714 13094 251 156 -4953 C ATOM 2704 NH1 ARG B 45 -7.902 17.233 -3.232 1.00126.11 N ANISOU 2704 NH1 ARG B 45 15345 19696 12874 -42 477 -4676 N ATOM 2705 NH2 ARG B 45 -8.562 19.085 -4.414 1.00126.62 N ANISOU 2705 NH2 ARG B 45 15070 18988 14054 538 46 -5441 N ATOM 2706 N GLU B 46 -1.254 19.000 -6.593 1.00 69.45 N ANISOU 2706 N GLU B 46 9122 9473 7793 -39 -1232 -2862 N ATOM 2707 CA GLU B 46 -0.953 19.457 -7.942 1.00 67.42 C ANISOU 2707 CA GLU B 46 8846 8671 8099 -61 -1415 -2474 C ATOM 2708 C GLU B 46 -1.534 18.503 -8.978 1.00 61.80 C ANISOU 2708 C GLU B 46 8156 8045 7278 -133 -1094 -2033 C ATOM 2709 O GLU B 46 -1.554 17.284 -8.782 1.00 50.98 O ANISOU 2709 O GLU B 46 6875 7045 5450 -238 -798 -1797 O ATOM 2710 CB GLU B 46 0.562 19.610 -8.154 1.00 71.85 C ANISOU 2710 CB GLU B 46 9487 8960 8853 -227 -1656 -2097 C ATOM 2711 CG GLU B 46 1.339 18.306 -8.197 1.00 74.14 C ANISOU 2711 CG GLU B 46 9894 9519 8756 -404 -1428 -1640 C ATOM 2712 CD GLU B 46 2.839 18.525 -8.214 1.00 79.83 C ANISOU 2712 CD GLU B 46 10627 10034 9669 -539 -1682 -1415 C ATOM 2713 OE1 GLU B 46 3.331 19.324 -7.389 1.00 87.67 O ANISOU 2713 OE1 GLU B 46 11620 10906 10786 -496 -1970 -1729 O ATOM 2714 OE2 GLU B 46 3.524 17.906 -9.054 1.00 75.39 O1- ANISOU 2714 OE2 GLU B 46 10043 9456 9144 -680 -1602 -969 O1- ATOM 2715 N PHE B 47 -2.010 19.077 -10.077 1.00 56.12 N ANISOU 2715 N PHE B 47 7365 6953 7005 -84 -1214 -1922 N ATOM 2716 CA PHE B 47 -2.528 18.291 -11.187 1.00 49.98 C ANISOU 2716 CA PHE B 47 6602 6208 6179 -140 -963 -1512 C ATOM 2717 C PHE B 47 -1.399 17.531 -11.870 1.00 48.50 C ANISOU 2717 C PHE B 47 6496 6039 5894 -346 -891 -934 C ATOM 2718 O PHE B 47 -0.313 18.073 -12.097 1.00 47.69 O ANISOU 2718 O PHE B 47 6389 5712 6021 -470 -1131 -754 O ATOM 2719 CB PHE B 47 -3.237 19.212 -12.182 1.00 53.11 C ANISOU 2719 CB PHE B 47 6917 6167 7094 -58 -1197 -1533 C ATOM 2720 CG PHE B 47 -3.649 18.536 -13.460 1.00 52.32 C ANISOU 2720 CG PHE B 47 6842 6054 6983 -133 -1004 -1079 C ATOM 2721 CD1 PHE B 47 -4.805 17.777 -13.516 1.00 45.64 C ANISOU 2721 CD1 PHE B 47 5958 5467 5916 -22 -695 -1188 C ATOM 2722 CD2 PHE B 47 -2.890 18.681 -14.610 1.00 47.70 C ANISOU 2722 CD2 PHE B 47 6295 5238 6593 -335 -1137 -560 C ATOM 2723 CE1 PHE B 47 -5.190 17.161 -14.696 1.00 46.53 C ANISOU 2723 CE1 PHE B 47 6092 5551 6036 -68 -551 -801 C ATOM 2724 CE2 PHE B 47 -3.268 18.069 -15.793 1.00 44.29 C ANISOU 2724 CE2 PHE B 47 5872 4849 6109 -398 -967 -188 C ATOM 2725 CZ PHE B 47 -4.419 17.311 -15.835 1.00 43.14 C ANISOU 2725 CZ PHE B 47 5710 4903 5779 -243 -689 -318 C ATOM 2726 N VAL B 48 -1.652 16.263 -12.186 1.00 43.18 N ANISOU 2726 N VAL B 48 5863 5648 4896 -383 -583 -679 N ATOM 2727 CA VAL B 48 -0.692 15.407 -12.883 1.00 45.57 C ANISOU 2727 CA VAL B 48 6182 6018 5115 -521 -516 -234 C ATOM 2728 C VAL B 48 -1.142 15.122 -14.315 1.00 46.81 C ANISOU 2728 C VAL B 48 6283 6105 5397 -538 -405 72 C ATOM 2729 O VAL B 48 -0.452 15.458 -15.273 1.00 43.66 O ANISOU 2729 O VAL B 48 5817 5579 5192 -670 -507 349 O ATOM 2730 CB VAL B 48 -0.435 14.102 -12.107 1.00 39.61 C ANISOU 2730 CB VAL B 48 5517 5599 3934 -549 -369 -186 C ATOM 2731 CG1 VAL B 48 0.491 13.191 -12.898 1.00 41.14 C ANISOU 2731 CG1 VAL B 48 5671 5837 4122 -627 -356 170 C ATOM 2732 CG2 VAL B 48 0.151 14.405 -10.743 1.00 42.09 C ANISOU 2732 CG2 VAL B 48 5905 5998 4090 -574 -519 -441 C ATOM 2733 N ALA B 49 -2.305 14.489 -14.465 1.00 40.43 N ANISOU 2733 N ALA B 49 5488 5425 4450 -434 -194 26 N ATOM 2734 CA ALA B 49 -2.799 14.141 -15.790 1.00 42.53 C ANISOU 2734 CA ALA B 49 5710 5641 4806 -430 -97 288 C ATOM 2735 C ALA B 49 -4.298 13.912 -15.713 1.00 45.04 C ANISOU 2735 C ALA B 49 6024 6006 5082 -286 58 96 C ATOM 2736 O ALA B 49 -4.846 13.582 -14.658 1.00 43.31 O ANISOU 2736 O ALA B 49 5820 6003 4632 -237 178 -165 O ATOM 2737 CB ALA B 49 -2.095 12.898 -16.346 1.00 35.65 C ANISOU 2737 CB ALA B 49 4817 4989 3741 -487 24 581 C ATOM 2738 N SER B 50 -4.954 14.098 -16.855 1.00 41.95 N ANISOU 2738 N SER B 50 5597 5447 4895 -251 48 232 N ATOM 2739 CA SER B 50 -6.364 13.774 -16.989 1.00 39.22 C ANISOU 2739 CA SER B 50 5217 5139 4548 -114 194 83 C ATOM 2740 C SER B 50 -6.623 13.334 -18.420 1.00 41.93 C ANISOU 2740 C SER B 50 5554 5410 4968 -122 228 410 C ATOM 2741 O SER B 50 -5.799 13.544 -19.315 1.00 36.73 O ANISOU 2741 O SER B 50 4899 4676 4379 -247 119 706 O ATOM 2742 CB SER B 50 -7.262 14.958 -16.623 1.00 38.76 C ANISOU 2742 CB SER B 50 5085 4856 4785 17 30 -334 C ATOM 2743 OG SER B 50 -7.098 16.020 -17.545 1.00 46.95 O ANISOU 2743 OG SER B 50 6133 5475 6232 -17 -294 -199 O ATOM 2744 N ILE B 51 -7.784 12.720 -18.628 1.00 38.88 N ANISOU 2744 N ILE B 51 5137 5093 4543 -8 383 344 N ATOM 2745 CA ILE B 51 -8.157 12.227 -19.945 1.00 41.65 C ANISOU 2745 CA ILE B 51 5483 5394 4949 14 411 608 C ATOM 2746 C ILE B 51 -9.666 12.349 -20.089 1.00 39.92 C ANISOU 2746 C ILE B 51 5207 5064 4898 165 443 394 C ATOM 2747 O ILE B 51 -10.415 12.229 -19.115 1.00 39.43 O ANISOU 2747 O ILE B 51 5075 5143 4764 236 570 75 O ATOM 2748 CB ILE B 51 -7.668 10.775 -20.161 1.00 40.54 C ANISOU 2748 CB ILE B 51 5346 5526 4530 -7 570 826 C ATOM 2749 CG1 ILE B 51 -7.718 10.406 -21.647 1.00 44.05 C ANISOU 2749 CG1 ILE B 51 5760 5957 5020 8 554 1075 C ATOM 2750 CG2 ILE B 51 -8.474 9.795 -19.314 1.00 34.57 C ANISOU 2750 CG2 ILE B 51 4589 4956 3590 46 738 699 C ATOM 2751 CD1 ILE B 51 -6.952 9.152 -21.986 1.00 42.26 C ANISOU 2751 CD1 ILE B 51 5485 5978 4593 12 616 1217 C ATOM 2752 N THR B 52 -10.106 12.613 -21.315 1.00 45.46 N ANISOU 2752 N THR B 52 5534 6708 5031 842 53 -964 N ATOM 2753 CA THR B 52 -11.524 12.751 -21.596 1.00 44.74 C ANISOU 2753 CA THR B 52 5256 6722 5022 1008 -48 -1190 C ATOM 2754 C THR B 52 -12.242 11.420 -21.383 1.00 44.14 C ANISOU 2754 C THR B 52 4908 6851 5010 877 147 -1278 C ATOM 2755 O THR B 52 -11.628 10.352 -21.293 1.00 39.94 O ANISOU 2755 O THR B 52 4401 6324 4452 676 314 -1144 O ATOM 2756 CB THR B 52 -11.744 13.234 -23.030 1.00 46.72 C ANISOU 2756 CB THR B 52 5638 6858 5256 1129 -300 -1174 C ATOM 2757 OG1 THR B 52 -11.144 12.306 -23.941 1.00 43.15 O ANISOU 2757 OG1 THR B 52 5249 6401 4746 973 -230 -1022 O ATOM 2758 CG2 THR B 52 -11.123 14.608 -23.232 1.00 46.55 C ANISOU 2758 CG2 THR B 52 5921 6597 5167 1224 -509 -1068 C ATOM 2759 N TRP B 53 -13.572 11.505 -21.308 1.00 43.47 N ANISOU 2759 N TRP B 53 4563 6935 5019 994 106 -1516 N ATOM 2760 CA TRP B 53 -14.396 10.309 -21.172 1.00 51.58 C ANISOU 2760 CA TRP B 53 5305 8163 6132 827 272 -1611 C ATOM 2761 C TRP B 53 -14.114 9.307 -22.286 1.00 52.90 C ANISOU 2761 C TRP B 53 5545 8244 6311 685 233 -1507 C ATOM 2762 O TRP B 53 -14.055 8.096 -22.043 1.00 53.32 O ANISOU 2762 O TRP B 53 5540 8332 6388 453 405 -1449 O ATOM 2763 CB TRP B 53 -15.875 10.699 -21.166 1.00 49.34 C ANISOU 2763 CB TRP B 53 4687 8099 5962 997 185 -1909 C ATOM 2764 CG TRP B 53 -16.789 9.549 -21.422 1.00 64.20 C ANISOU 2764 CG TRP B 53 6263 10167 7962 805 277 -2014 C ATOM 2765 CD1 TRP B 53 -17.308 8.692 -20.496 1.00 72.32 C ANISOU 2765 CD1 TRP B 53 7038 11409 9031 561 556 -2051 C ATOM 2766 CD2 TRP B 53 -17.289 9.117 -22.694 1.00 58.45 C ANISOU 2766 CD2 TRP B 53 5467 9418 7322 813 78 -2088 C ATOM 2767 NE1 TRP B 53 -18.103 7.756 -21.111 1.00 77.71 N ANISOU 2767 NE1 TRP B 53 7488 12191 9848 386 540 -2142 N ATOM 2768 CE2 TRP B 53 -18.106 7.995 -22.461 1.00 71.57 C ANISOU 2768 CE2 TRP B 53 6814 11272 9106 553 235 -2183 C ATOM 2769 CE3 TRP B 53 -17.126 9.572 -24.005 1.00 55.21 C ANISOU 2769 CE3 TRP B 53 5253 8844 6882 1003 -224 -2079 C ATOM 2770 CZ2 TRP B 53 -18.758 7.320 -23.490 1.00 75.75 C ANISOU 2770 CZ2 TRP B 53 7204 11825 9754 486 74 -2295 C ATOM 2771 CZ3 TRP B 53 -17.772 8.901 -25.026 1.00 61.11 C ANISOU 2771 CZ3 TRP B 53 5876 9631 7712 967 -375 -2189 C ATOM 2772 CH2 TRP B 53 -18.579 7.788 -24.763 1.00 67.26 C ANISOU 2772 CH2 TRP B 53 6325 10594 8638 716 -239 -2309 C ATOM 2773 N SER B 54 -13.933 9.792 -23.514 1.00 48.51 N ANISOU 2773 N SER B 54 5151 7561 5719 828 -4 -1482 N ATOM 2774 CA SER B 54 -13.695 8.906 -24.648 1.00 45.76 C ANISOU 2774 CA SER B 54 4887 7152 5348 742 -61 -1419 C ATOM 2775 C SER B 54 -12.343 8.210 -24.589 1.00 40.69 C ANISOU 2775 C SER B 54 4458 6400 4602 582 93 -1192 C ATOM 2776 O SER B 54 -12.125 7.258 -25.348 1.00 44.20 O ANISOU 2776 O SER B 54 4958 6811 5025 506 84 -1166 O ATOM 2777 CB SER B 54 -13.796 9.693 -25.952 1.00 46.43 C ANISOU 2777 CB SER B 54 5133 7145 5363 953 -350 -1435 C ATOM 2778 OG SER B 54 -12.810 10.708 -25.992 1.00 46.82 O ANISOU 2778 OG SER B 54 5466 7041 5284 1023 -396 -1255 O ATOM 2779 N GLY B 55 -11.438 8.651 -23.717 1.00 40.59 N ANISOU 2779 N GLY B 55 4560 6337 4526 552 209 -1056 N ATOM 2780 CA GLY B 55 -10.089 8.126 -23.710 1.00 37.66 C ANISOU 2780 CA GLY B 55 4366 5884 4058 447 318 -863 C ATOM 2781 C GLY B 55 -9.202 8.642 -24.819 1.00 37.25 C ANISOU 2781 C GLY B 55 4519 5753 3882 515 209 -735 C ATOM 2782 O GLY B 55 -8.060 8.190 -24.938 1.00 39.69 O ANISOU 2782 O GLY B 55 4930 6044 4107 446 301 -600 O ATOM 2783 N ILE B 56 -9.686 9.583 -25.625 1.00 43.76 N ANISOU 2783 N ILE B 56 5409 6542 4678 653 13 -774 N ATOM 2784 CA ILE B 56 -8.950 10.037 -26.803 1.00 40.99 C ANISOU 2784 CA ILE B 56 5278 6129 4168 688 -82 -633 C ATOM 2785 C ILE B 56 -7.912 11.093 -26.443 1.00 43.48 C ANISOU 2785 C ILE B 56 5753 6355 4414 637 -67 -451 C ATOM 2786 O ILE B 56 -6.756 11.010 -26.866 1.00 46.44 O ANISOU 2786 O ILE B 56 6233 6744 4668 540 19 -283 O ATOM 2787 CB ILE B 56 -9.934 10.562 -27.872 1.00 45.59 C ANISOU 2787 CB ILE B 56 5915 6684 4721 856 -332 -734 C ATOM 2788 CG1 ILE B 56 -10.872 9.445 -28.339 1.00 45.02 C ANISOU 2788 CG1 ILE B 56 5673 6708 4725 876 -370 -922 C ATOM 2789 CG2 ILE B 56 -9.177 11.158 -29.053 1.00 41.37 C ANISOU 2789 CG2 ILE B 56 5663 6083 3974 876 -423 -552 C ATOM 2790 CD1 ILE B 56 -11.921 9.905 -29.339 1.00 45.29 C ANISOU 2790 CD1 ILE B 56 5727 6738 4744 1066 -653 -1063 C ATOM 2791 N ASP B 57 -8.297 12.099 -25.658 1.00 39.30 N ANISOU 2791 N ASP B 57 5230 5743 3959 700 -155 -499 N ATOM 2792 CA ASP B 57 -7.468 13.288 -25.475 1.00 43.39 C ANISOU 2792 CA ASP B 57 5947 6118 4422 654 -224 -344 C ATOM 2793 C ASP B 57 -6.909 13.379 -24.060 1.00 46.96 C ANISOU 2793 C ASP B 57 6329 6568 4945 571 -104 -340 C ATOM 2794 O ASP B 57 -7.623 13.797 -23.135 1.00 43.70 O ANISOU 2794 O ASP B 57 5848 6137 4618 677 -152 -491 O ATOM 2795 CB ASP B 57 -8.281 14.542 -25.805 1.00 50.68 C ANISOU 2795 CB ASP B 57 7024 6880 5353 830 -502 -408 C ATOM 2796 CG ASP B 57 -8.733 14.575 -27.250 1.00 53.34 C ANISOU 2796 CG ASP B 57 7491 7196 5579 924 -663 -386 C ATOM 2797 OD1 ASP B 57 -7.864 14.545 -28.145 1.00 53.84 O ANISOU 2797 OD1 ASP B 57 7726 7250 5479 801 -621 -181 O ATOM 2798 OD2 ASP B 57 -9.958 14.611 -27.488 1.00 60.64 O ANISOU 2798 OD2 ASP B 57 8332 8141 6569 1128 -831 -586 O ATOM 2799 N PRO B 58 -5.647 13.019 -23.841 1.00 41.16 N ANISOU 2799 N PRO B 58 5602 5873 4164 407 40 -191 N ATOM 2800 CA PRO B 58 -5.025 13.224 -22.530 1.00 40.30 C ANISOU 2800 CA PRO B 58 5462 5747 4104 340 102 -183 C ATOM 2801 C PRO B 58 -4.452 14.624 -22.375 1.00 43.72 C ANISOU 2801 C PRO B 58 6078 6002 4531 284 -54 -89 C ATOM 2802 O PRO B 58 -4.090 15.297 -23.341 1.00 45.44 O ANISOU 2802 O PRO B 58 6459 6123 4682 213 -154 54 O ATOM 2803 CB PRO B 58 -3.902 12.179 -22.526 1.00 36.70 C ANISOU 2803 CB PRO B 58 4923 5418 3603 215 283 -80 C ATOM 2804 CG PRO B 58 -3.489 12.113 -23.963 1.00 36.94 C ANISOU 2804 CG PRO B 58 5019 5487 3529 172 281 35 C ATOM 2805 CD PRO B 58 -4.762 12.283 -24.760 1.00 38.65 C ANISOU 2805 CD PRO B 58 5290 5656 3740 307 153 -59 C ATOM 2806 N THR B 59 -4.371 15.055 -21.118 1.00 45.28 N ANISOU 2806 N THR B 59 6272 6147 4787 304 -82 -167 N ATOM 2807 CA THR B 59 -3.781 16.337 -20.759 1.00 41.57 C ANISOU 2807 CA THR B 59 5984 5478 4334 237 -255 -106 C ATOM 2808 C THR B 59 -2.773 16.103 -19.646 1.00 46.68 C ANISOU 2808 C THR B 59 6558 6182 4998 122 -172 -87 C ATOM 2809 O THR B 59 -3.105 15.488 -18.627 1.00 42.82 O ANISOU 2809 O THR B 59 5957 5799 4514 215 -74 -218 O ATOM 2810 CB THR B 59 -4.850 17.342 -20.312 1.00 43.68 C ANISOU 2810 CB THR B 59 6366 5581 4648 453 -468 -289 C ATOM 2811 OG1 THR B 59 -5.787 17.549 -21.376 1.00 43.95 O ANISOU 2811 OG1 THR B 59 6464 5568 4669 591 -585 -320 O ATOM 2812 CG2 THR B 59 -4.213 18.675 -19.941 1.00 46.03 C ANISOU 2812 CG2 THR B 59 6904 5613 4971 380 -690 -234 C ATOM 2813 N TYR B 60 -1.547 16.581 -19.843 1.00 43.09 N ANISOU 2813 N TYR B 60 6162 5669 4542 -91 -212 78 N ATOM 2814 CA TYR B 60 -0.459 16.352 -18.905 1.00 47.26 C ANISOU 2814 CA TYR B 60 6595 6270 5092 -205 -164 95 C ATOM 2815 C TYR B 60 0.054 17.675 -18.361 1.00 48.16 C ANISOU 2815 C TYR B 60 6875 6160 5265 -314 -389 107 C ATOM 2816 O TYR B 60 0.088 18.681 -19.076 1.00 44.76 O ANISOU 2816 O TYR B 60 6630 5531 4848 -423 -542 213 O ATOM 2817 CB TYR B 60 0.696 15.596 -19.568 1.00 44.86 C ANISOU 2817 CB TYR B 60 6132 6160 4754 -375 -5 248 C ATOM 2818 CG TYR B 60 0.291 14.285 -20.199 1.00 42.69 C ANISOU 2818 CG TYR B 60 5732 6068 4419 -266 180 228 C ATOM 2819 CD1 TYR B 60 0.084 13.154 -19.421 1.00 39.64 C ANISOU 2819 CD1 TYR B 60 5238 5792 4032 -144 289 122 C ATOM 2820 CD2 TYR B 60 0.117 14.179 -21.575 1.00 41.39 C ANISOU 2820 CD2 TYR B 60 5594 5946 4185 -292 228 319 C ATOM 2821 CE1 TYR B 60 -0.288 11.953 -19.992 1.00 41.05 C ANISOU 2821 CE1 TYR B 60 5338 6087 4170 -65 424 99 C ATOM 2822 CE2 TYR B 60 -0.253 12.983 -22.158 1.00 40.32 C ANISOU 2822 CE2 TYR B 60 5365 5956 3997 -186 363 274 C ATOM 2823 CZ TYR B 60 -0.455 11.873 -21.362 1.00 40.02 C ANISOU 2823 CZ TYR B 60 5222 5996 3990 -78 452 161 C ATOM 2824 OH TYR B 60 -0.823 10.680 -21.934 1.00 36.98 O ANISOU 2824 OH TYR B 60 4778 5706 3568 9 553 112 O ATOM 2825 N ALA B 61 0.450 17.668 -17.092 1.00 46.74 N ANISOU 2825 N ALA B 61 6660 5992 5107 -289 -430 2 N ATOM 2826 CA ALA B 61 1.187 18.796 -16.544 1.00 48.89 C ANISOU 2826 CA ALA B 61 7066 6066 5446 -434 -655 10 C ATOM 2827 C ALA B 61 2.561 18.862 -17.195 1.00 50.71 C ANISOU 2827 C ALA B 61 7190 6364 5714 -761 -622 220 C ATOM 2828 O ALA B 61 3.167 17.830 -17.498 1.00 49.47 O ANISOU 2828 O ALA B 61 6800 6473 5526 -807 -418 285 O ATOM 2829 CB ALA B 61 1.318 18.669 -15.025 1.00 43.47 C ANISOU 2829 CB ALA B 61 6362 5410 4744 -312 -709 -168 C ATOM 2830 N ASP B 62 3.047 20.086 -17.425 1.00 55.04 N ANISOU 2830 N ASP B 62 7909 6673 6330 -993 -827 320 N ATOM 2831 CA ASP B 62 4.325 20.263 -18.110 1.00 60.32 C ANISOU 2831 CA ASP B 62 8456 7431 7033 -1363 -776 535 C ATOM 2832 C ASP B 62 5.450 19.509 -17.415 1.00 64.01 C ANISOU 2832 C ASP B 62 8610 8173 7537 -1431 -683 490 C ATOM 2833 O ASP B 62 6.383 19.038 -18.076 1.00 60.50 O ANISOU 2833 O ASP B 62 7919 7984 7083 -1622 -515 620 O ATOM 2834 CB ASP B 62 4.670 21.750 -18.211 1.00 66.60 C ANISOU 2834 CB ASP B 62 9515 7879 7912 -1641 -1049 639 C ATOM 2835 CG ASP B 62 3.912 22.452 -19.321 1.00 79.45 C ANISOU 2835 CG ASP B 62 11446 9264 9478 -1662 -1124 781 C ATOM 2836 OD1 ASP B 62 3.616 21.801 -20.345 1.00 82.69 O ANISOU 2836 OD1 ASP B 62 11781 9862 9776 -1616 -914 886 O ATOM 2837 OD2 ASP B 62 3.614 23.657 -19.171 1.00 88.46 O1- ANISOU 2837 OD2 ASP B 62 12925 10010 10674 -1705 -1423 778 O1- ATOM 2838 N SER B 63 5.369 19.367 -16.090 1.00 48.14 N ANISOU 2838 N SER B 63 6605 6137 5550 -1250 -794 293 N ATOM 2839 CA SER B 63 6.415 18.697 -15.330 1.00 54.99 C ANISOU 2839 CA SER B 63 7216 7235 6444 -1273 -770 232 C ATOM 2840 C SER B 63 6.522 17.210 -15.645 1.00 49.22 C ANISOU 2840 C SER B 63 6245 6826 5631 -1113 -505 239 C ATOM 2841 O SER B 63 7.573 16.613 -15.387 1.00 52.80 O ANISOU 2841 O SER B 63 6447 7505 6108 -1154 -472 226 O ATOM 2842 CB SER B 63 6.169 18.884 -13.833 1.00 61.36 C ANISOU 2842 CB SER B 63 8153 7922 7240 -1076 -963 19 C ATOM 2843 OG SER B 63 7.042 18.071 -13.069 1.00 78.04 O ANISOU 2843 OG SER B 63 10049 10260 9341 -1025 -950 -51 O ATOM 2844 N VAL B 64 5.468 16.594 -16.181 1.00 44.70 N ANISOU 2844 N VAL B 64 5744 6269 4969 -921 -346 239 N ATOM 2845 CA VAL B 64 5.440 15.153 -16.403 1.00 47.25 C ANISOU 2845 CA VAL B 64 5903 6832 5217 -749 -135 222 C ATOM 2846 C VAL B 64 5.138 14.780 -17.846 1.00 47.58 C ANISOU 2846 C VAL B 64 5905 6968 5206 -778 45 337 C ATOM 2847 O VAL B 64 5.064 13.588 -18.159 1.00 48.17 O ANISOU 2847 O VAL B 64 5871 7212 5220 -631 202 312 O ATOM 2848 CB VAL B 64 4.434 14.462 -15.459 1.00 41.68 C ANISOU 2848 CB VAL B 64 5314 6084 4439 -473 -112 80 C ATOM 2849 CG1 VAL B 64 4.690 14.860 -14.008 1.00 43.16 C ANISOU 2849 CG1 VAL B 64 5582 6191 4627 -421 -291 -41 C ATOM 2850 CG2 VAL B 64 3.004 14.788 -15.869 1.00 40.48 C ANISOU 2850 CG2 VAL B 64 5334 5788 4258 -376 -84 53 C ATOM 2851 N ALA B 65 4.971 15.760 -18.739 1.00 51.45 N ANISOU 2851 N ALA B 65 6514 7334 5702 -956 5 461 N ATOM 2852 CA ALA B 65 4.534 15.463 -20.101 1.00 52.59 C ANISOU 2852 CA ALA B 65 6679 7549 5754 -952 151 562 C ATOM 2853 C ALA B 65 5.523 14.572 -20.843 1.00 53.60 C ANISOU 2853 C ALA B 65 6543 8004 5820 -1006 352 622 C ATOM 2854 O ALA B 65 5.115 13.746 -21.667 1.00 53.30 O ANISOU 2854 O ALA B 65 6483 8084 5685 -871 494 615 O ATOM 2855 CB ALA B 65 4.313 16.764 -20.873 1.00 49.10 C ANISOU 2855 CB ALA B 65 6460 6895 5303 -1152 38 711 C ATOM 2856 N ASP B 66 6.818 14.715 -20.567 1.00 50.42 N ANISOU 2856 N ASP B 66 5921 7763 5472 -1184 354 653 N ATOM 2857 CA ASP B 66 7.832 13.933 -21.263 1.00 53.12 C ANISOU 2857 CA ASP B 66 5963 8465 5754 -1212 545 678 C ATOM 2858 C ASP B 66 7.940 12.502 -20.753 1.00 54.29 C ANISOU 2858 C ASP B 66 5968 8768 5890 -900 599 508 C ATOM 2859 O ASP B 66 8.550 11.667 -21.431 1.00 57.35 O ANISOU 2859 O ASP B 66 6146 9438 6205 -819 752 483 O ATOM 2860 CB ASP B 66 9.199 14.613 -21.140 1.00 67.47 C ANISOU 2860 CB ASP B 66 7540 10442 7652 -1525 522 752 C ATOM 2861 CG ASP B 66 9.166 16.070 -21.559 1.00 89.71 C ANISOU 2861 CG ASP B 66 10545 13048 10492 -1887 434 944 C ATOM 2862 OD1 ASP B 66 8.399 16.408 -22.485 1.00 98.16 O ANISOU 2862 OD1 ASP B 66 11856 13989 11451 -1913 480 1066 O ATOM 2863 OD2 ASP B 66 9.908 16.878 -20.960 1.00 97.39 O ANISOU 2863 OD2 ASP B 66 11448 13963 11593 -2146 291 971 O ATOM 2864 N ARG B 67 7.366 12.193 -19.588 1.00 51.23 N ANISOU 2864 N ARG B 67 5711 8202 5552 -717 475 391 N ATOM 2865 CA ARG B 67 7.595 10.914 -18.934 1.00 47.15 C ANISOU 2865 CA ARG B 67 5109 7785 5021 -458 482 259 C ATOM 2866 C ARG B 67 6.334 10.127 -18.607 1.00 46.80 C ANISOU 2866 C ARG B 67 5288 7566 4927 -240 496 193 C ATOM 2867 O ARG B 67 6.426 8.907 -18.427 1.00 45.66 O ANISOU 2867 O ARG B 67 5120 7485 4744 -39 529 117 O ATOM 2868 CB ARG B 67 8.384 11.120 -17.628 1.00 53.03 C ANISOU 2868 CB ARG B 67 5772 8529 5846 -463 309 186 C ATOM 2869 CG ARG B 67 9.690 11.878 -17.804 1.00 63.78 C ANISOU 2869 CG ARG B 67 6863 10078 7292 -714 268 230 C ATOM 2870 CD ARG B 67 10.357 12.192 -16.467 1.00 64.71 C ANISOU 2870 CD ARG B 67 6927 10159 7499 -722 43 135 C ATOM 2871 NE ARG B 67 9.636 13.207 -15.699 1.00 58.04 N ANISOU 2871 NE ARG B 67 6363 9003 6686 -809 -121 138 N ATOM 2872 CZ ARG B 67 9.096 13.000 -14.502 1.00 54.39 C ANISOU 2872 CZ ARG B 67 6105 8380 6181 -614 -248 33 C ATOM 2873 NH1 ARG B 67 9.200 11.812 -13.922 1.00 54.43 N ANISOU 2873 NH1 ARG B 67 6098 8472 6112 -352 -242 -50 N ATOM 2874 NH2 ARG B 67 8.462 13.985 -13.878 1.00 52.77 N ANISOU 2874 NH2 ARG B 67 6137 7925 5990 -672 -389 8 N ATOM 2875 N PHE B 68 5.176 10.774 -18.504 1.00 46.31 N ANISOU 2875 N PHE B 68 5436 7290 4869 -274 460 210 N ATOM 2876 CA PHE B 68 3.949 10.113 -18.085 1.00 40.66 C ANISOU 2876 CA PHE B 68 4884 6446 4120 -112 485 140 C ATOM 2877 C PHE B 68 3.003 9.957 -19.268 1.00 45.63 C ANISOU 2877 C PHE B 68 5572 7052 4714 -95 575 162 C ATOM 2878 O PHE B 68 2.960 10.801 -20.167 1.00 36.36 O ANISOU 2878 O PHE B 68 4416 5869 3532 -212 570 241 O ATOM 2879 CB PHE B 68 3.231 10.892 -16.974 1.00 42.13 C ANISOU 2879 CB PHE B 68 5224 6455 4327 -112 376 88 C ATOM 2880 CG PHE B 68 3.928 10.865 -15.632 1.00 38.32 C ANISOU 2880 CG PHE B 68 4742 5977 3841 -76 268 35 C ATOM 2881 CD1 PHE B 68 5.235 10.421 -15.504 1.00 39.37 C ANISOU 2881 CD1 PHE B 68 4713 6256 3988 -74 232 40 C ATOM 2882 CD2 PHE B 68 3.255 11.280 -14.493 1.00 36.84 C ANISOU 2882 CD2 PHE B 68 4711 5668 3618 -18 194 -43 C ATOM 2883 CE1 PHE B 68 5.861 10.407 -14.268 1.00 42.85 C ANISOU 2883 CE1 PHE B 68 5166 6697 4418 -19 91 -22 C ATOM 2884 CE2 PHE B 68 3.874 11.269 -13.256 1.00 40.56 C ANISOU 2884 CE2 PHE B 68 5217 6142 4050 31 77 -98 C ATOM 2885 CZ PHE B 68 5.178 10.831 -13.143 1.00 43.89 C ANISOU 2885 CZ PHE B 68 5496 6686 4495 29 10 -84 C ATOM 2886 N THR B 69 2.241 8.866 -19.258 1.00 40.93 N ANISOU 2886 N THR B 69 5029 6432 4090 39 638 97 N ATOM 2887 CA THR B 69 1.167 8.652 -20.218 1.00 41.77 C ANISOU 2887 CA THR B 69 5194 6500 4177 69 686 79 C ATOM 2888 C THR B 69 -0.056 8.146 -19.473 1.00 45.25 C ANISOU 2888 C THR B 69 5719 6833 4641 132 697 -4 C ATOM 2889 O THR B 69 0.062 7.346 -18.540 1.00 44.35 O ANISOU 2889 O THR B 69 5634 6703 4514 177 718 -29 O ATOM 2890 CB THR B 69 1.556 7.650 -21.317 1.00 43.27 C ANISOU 2890 CB THR B 69 5322 6813 4305 141 766 71 C ATOM 2891 OG1 THR B 69 1.946 6.409 -20.718 1.00 55.84 O ANISOU 2891 OG1 THR B 69 6905 8417 5895 259 780 11 O ATOM 2892 CG2 THR B 69 2.702 8.190 -22.153 1.00 39.95 C ANISOU 2892 CG2 THR B 69 4784 6566 3831 59 805 154 C ATOM 2893 N THR B 70 -1.226 8.628 -19.871 1.00 40.27 N ANISOU 2893 N THR B 70 5126 6141 4034 131 678 -45 N ATOM 2894 CA THR B 70 -2.473 8.201 -19.263 1.00 36.05 C ANISOU 2894 CA THR B 70 4608 5563 3526 162 714 -138 C ATOM 2895 C THR B 70 -3.387 7.637 -20.339 1.00 38.44 C ANISOU 2895 C THR B 70 4885 5872 3849 184 729 -192 C ATOM 2896 O THR B 70 -3.301 8.008 -21.513 1.00 33.67 O ANISOU 2896 O THR B 70 4287 5283 3222 200 678 -168 O ATOM 2897 CB THR B 70 -3.169 9.352 -18.516 1.00 40.11 C ANISOU 2897 CB THR B 70 5145 6031 4065 177 655 -201 C ATOM 2898 OG1 THR B 70 -4.250 8.833 -17.729 1.00 44.05 O ANISOU 2898 OG1 THR B 70 5613 6558 4566 194 739 -295 O ATOM 2899 CG2 THR B 70 -3.711 10.382 -19.491 1.00 40.87 C ANISOU 2899 CG2 THR B 70 5259 6077 4192 206 546 -219 C ATOM 2900 N SER B 71 -4.244 6.708 -19.935 1.00 38.10 N ANISOU 2900 N SER B 71 4824 5817 3835 166 792 -258 N ATOM 2901 CA SER B 71 -5.206 6.127 -20.855 1.00 38.57 C ANISOU 2901 CA SER B 71 4841 5876 3937 165 780 -337 C ATOM 2902 C SER B 71 -6.432 5.722 -20.062 1.00 45.20 C ANISOU 2902 C SER B 71 5608 6728 4836 92 850 -422 C ATOM 2903 O SER B 71 -6.392 5.598 -18.834 1.00 34.58 O ANISOU 2903 O SER B 71 4287 5392 3461 41 938 -396 O ATOM 2904 CB SER B 71 -4.627 4.925 -21.607 1.00 42.11 C ANISOU 2904 CB SER B 71 5345 6302 4354 182 785 -321 C ATOM 2905 OG SER B 71 -4.470 3.812 -20.747 1.00 43.77 O ANISOU 2905 OG SER B 71 5620 6444 4567 134 844 -301 O ATOM 2906 N ARG B 72 -7.532 5.526 -20.778 1.00 35.13 N ANISOU 2906 N ARG B 72 4237 5479 3633 79 813 -530 N ATOM 2907 CA ARG B 72 -8.784 5.139 -20.156 1.00 39.51 C ANISOU 2907 CA ARG B 72 4656 6097 4259 -25 894 -627 C ATOM 2908 C ARG B 72 -9.390 3.986 -20.936 1.00 44.04 C ANISOU 2908 C ARG B 72 5195 6631 4907 -122 866 -686 C ATOM 2909 O ARG B 72 -9.515 4.056 -22.163 1.00 37.47 O ANISOU 2909 O ARG B 72 4358 5785 4096 -39 732 -748 O ATOM 2910 CB ARG B 72 -9.757 6.318 -20.090 1.00 41.74 C ANISOU 2910 CB ARG B 72 4778 6492 4589 70 844 -762 C ATOM 2911 CG ARG B 72 -11.007 6.001 -19.311 1.00 42.19 C ANISOU 2911 CG ARG B 72 4630 6694 4706 -36 971 -881 C ATOM 2912 CD ARG B 72 -11.914 7.204 -19.151 1.00 45.82 C ANISOU 2912 CD ARG B 72 4910 7295 5204 123 913 -1056 C ATOM 2913 NE ARG B 72 -13.137 6.811 -18.461 1.00 64.36 N ANISOU 2913 NE ARG B 72 6995 9852 7606 8 1067 -1190 N ATOM 2914 CZ ARG B 72 -14.234 6.388 -19.077 1.00 65.98 C ANISOU 2914 CZ ARG B 72 6961 10167 7940 -56 1034 -1334 C ATOM 2915 NH1 ARG B 72 -14.269 6.322 -20.399 1.00 76.07 N ANISOU 2915 NH1 ARG B 72 8267 11346 9289 17 827 -1368 N ATOM 2916 NH2 ARG B 72 -15.297 6.036 -18.374 1.00 80.21 N ANISOU 2916 NH2 ARG B 72 8486 12201 9790 -202 1209 -1448 N ATOM 2917 N ASP B 73 -9.740 2.923 -20.218 1.00 41.96 N ANISOU 2917 N ASP B 73 4941 6332 4668 -309 978 -659 N ATOM 2918 CA ASP B 73 -10.444 1.778 -20.787 1.00 44.53 C ANISOU 2918 CA ASP B 73 5240 6589 5091 -461 942 -722 C ATOM 2919 C ASP B 73 -11.934 2.062 -20.659 1.00 46.13 C ANISOU 2919 C ASP B 73 5153 6964 5409 -570 981 -871 C ATOM 2920 O ASP B 73 -12.527 1.854 -19.599 1.00 45.25 O ANISOU 2920 O ASP B 73 4940 6948 5303 -751 1153 -855 O ATOM 2921 CB ASP B 73 -10.043 0.495 -20.067 1.00 47.48 C ANISOU 2921 CB ASP B 73 5811 6798 5432 -635 1020 -597 C ATOM 2922 CG ASP B 73 -10.600 -0.756 -20.727 1.00 53.81 C ANISOU 2922 CG ASP B 73 6656 7452 6338 -799 936 -654 C ATOM 2923 OD1 ASP B 73 -11.630 -0.675 -21.430 1.00 53.48 O ANISOU 2923 OD1 ASP B 73 6410 7494 6416 -858 867 -804 O ATOM 2924 OD2 ASP B 73 -10.005 -1.835 -20.527 1.00 53.85 O ANISOU 2924 OD2 ASP B 73 6911 7241 6309 -862 909 -560 O ATOM 2925 N VAL B 74 -12.544 2.544 -21.745 1.00 42.80 N ANISOU 2925 N VAL B 74 5214 6218 4830 -827 369 -716 N ATOM 2926 CA VAL B 74 -13.960 2.885 -21.699 1.00 45.23 C ANISOU 2926 CA VAL B 74 5301 6779 5104 -915 324 -901 C ATOM 2927 C VAL B 74 -14.831 1.656 -21.473 1.00 52.60 C ANISOU 2927 C VAL B 74 6191 7780 6015 -1213 305 -784 C ATOM 2928 O VAL B 74 -15.964 1.787 -21.003 1.00 59.27 O ANISOU 2928 O VAL B 74 6770 8948 6801 -1358 307 -881 O ATOM 2929 CB VAL B 74 -14.386 3.618 -22.985 1.00 49.24 C ANISOU 2929 CB VAL B 74 5875 7139 5695 -714 229 -1099 C ATOM 2930 CG1 VAL B 74 -13.549 4.873 -23.185 1.00 42.90 C ANISOU 2930 CG1 VAL B 74 5116 6246 4937 -451 253 -1182 C ATOM 2931 CG2 VAL B 74 -14.273 2.697 -24.190 1.00 45.38 C ANISOU 2931 CG2 VAL B 74 5664 6314 5263 -718 156 -1024 C ATOM 2932 N ALA B 75 -14.329 0.458 -21.779 1.00 48.98 N ANISOU 2932 N ALA B 75 5976 7019 5613 -1312 289 -576 N ATOM 2933 CA ALA B 75 -15.162 -0.734 -21.661 1.00 56.14 C ANISOU 2933 CA ALA B 75 6873 7914 6542 -1623 251 -459 C ATOM 2934 C ALA B 75 -15.370 -1.133 -20.204 1.00 57.43 C ANISOU 2934 C ALA B 75 6838 8396 6587 -1873 349 -260 C ATOM 2935 O ALA B 75 -16.464 -1.570 -19.828 1.00 56.30 O ANISOU 2935 O ALA B 75 6503 8472 6415 -2151 351 -234 O ATOM 2936 CB ALA B 75 -14.547 -1.888 -22.455 1.00 52.22 C ANISOU 2936 CB ALA B 75 6731 6945 6166 -1630 192 -321 C ATOM 2937 N ASN B 76 -14.340 -0.993 -19.366 1.00 58.01 N ANISOU 2937 N ASN B 76 6937 8528 6576 -1790 429 -108 N ATOM 2938 CA ASN B 76 -14.448 -1.363 -17.958 1.00 64.22 C ANISOU 2938 CA ASN B 76 7556 9647 7199 -2008 519 105 C ATOM 2939 C ASN B 76 -14.190 -0.200 -17.006 1.00 58.14 C ANISOU 2939 C ASN B 76 6556 9287 6245 -1876 597 -27 C ATOM 2940 O ASN B 76 -14.007 -0.432 -15.804 1.00 59.43 O ANISOU 2940 O ASN B 76 6613 9742 6226 -2004 670 154 O ATOM 2941 CB ASN B 76 -13.508 -2.528 -17.631 1.00 67.47 C ANISOU 2941 CB ASN B 76 8212 9782 7644 -2079 516 465 C ATOM 2942 CG ASN B 76 -12.179 -2.418 -18.331 1.00 76.89 C ANISOU 2942 CG ASN B 76 9660 10604 8952 -1777 480 463 C ATOM 2943 OD1 ASN B 76 -11.291 -1.688 -17.891 1.00 81.30 O ANISOU 2943 OD1 ASN B 76 10165 11289 9436 -1590 515 442 O ATOM 2944 ND2 ASN B 76 -12.027 -3.153 -19.428 1.00 86.15 N ANISOU 2944 ND2 ASN B 76 11100 11329 10304 -1731 409 474 N ATOM 2945 N AASN B 77 -14.172 1.037 -17.506 0.45 50.55 N ANISOU 2945 N AASN B 77 5531 8349 5325 -1627 575 -336 N ATOM 2946 N BASN B 77 -14.159 1.035 -17.512 0.55 50.16 N ANISOU 2946 N BASN B 77 5485 8296 5277 -1626 574 -335 N ATOM 2947 CA AASN B 77 -14.090 2.230 -16.660 0.45 50.86 C ANISOU 2947 CA AASN B 77 5349 8754 5220 -1504 630 -537 C ATOM 2948 CA BASN B 77 -14.087 2.236 -16.678 0.55 50.78 C ANISOU 2948 CA BASN B 77 5341 8739 5213 -1501 629 -539 C ATOM 2949 C AASN B 77 -12.825 2.236 -15.804 0.45 48.95 C ANISOU 2949 C AASN B 77 5170 8556 4872 -1454 658 -378 C ATOM 2950 C BASN B 77 -12.827 2.250 -15.814 0.55 48.86 C ANISOU 2950 C BASN B 77 5158 8543 4862 -1451 658 -382 C ATOM 2951 O AASN B 77 -12.854 2.597 -14.626 0.45 50.98 O ANISOU 2951 O AASN B 77 5236 9219 4915 -1505 717 -409 O ATOM 2952 O BASN B 77 -12.859 2.629 -14.641 0.55 50.94 O ANISOU 2952 O BASN B 77 5230 9213 4912 -1499 716 -418 O ATOM 2953 CB AASN B 77 -15.334 2.365 -15.779 0.45 55.40 C ANISOU 2953 CB AASN B 77 5595 9836 5618 -1681 709 -632 C ATOM 2954 CB BASN B 77 -15.342 2.376 -15.813 0.55 55.53 C ANISOU 2954 CB BASN B 77 5614 9845 5640 -1677 707 -638 C ATOM 2955 CG AASN B 77 -16.260 3.463 -16.246 0.45 58.96 C ANISOU 2955 CG AASN B 77 5850 10425 6126 -1520 685 -1002 C ATOM 2956 CG BASN B 77 -15.581 3.799 -15.360 0.55 56.07 C ANISOU 2956 CG BASN B 77 5457 10226 5622 -1477 738 -989 C ATOM 2957 OD1AASN B 77 -17.171 3.230 -17.041 0.45 65.23 O ANISOU 2957 OD1AASN B 77 6604 11147 7034 -1573 630 -1065 O ATOM 2958 OD1BASN B 77 -15.107 4.748 -15.983 0.55 56.39 O ANISOU 2958 OD1BASN B 77 5586 10042 5796 -1221 673 -1192 O ATOM 2959 ND2AASN B 77 -16.034 4.672 -15.749 0.45 58.49 N ANISOU 2959 ND2AASN B 77 5668 10558 5998 -1315 709 -1257 N ATOM 2960 ND2BASN B 77 -16.325 3.956 -14.273 0.55 59.39 N ANISOU 2960 ND2BASN B 77 5587 11162 5818 -1594 841 -1062 N ATOM 2961 N THR B 78 -11.705 1.840 -16.396 1.00 46.76 N ANISOU 2961 N THR B 78 5146 7889 4730 -1343 612 -220 N ATOM 2962 CA THR B 78 -10.423 1.811 -15.706 1.00 42.08 C ANISOU 2962 CA THR B 78 4602 7317 4071 -1274 613 -60 C ATOM 2963 C THR B 78 -9.549 2.947 -16.220 1.00 44.48 C ANISOU 2963 C THR B 78 4938 7470 4493 -1022 582 -265 C ATOM 2964 O THR B 78 -9.448 3.161 -17.433 1.00 40.46 O ANISOU 2964 O THR B 78 4573 6629 4171 -885 557 -347 O ATOM 2965 CB THR B 78 -9.722 0.464 -15.898 1.00 49.58 C ANISOU 2965 CB THR B 78 5783 7958 5098 -1325 590 299 C ATOM 2966 OG1 THR B 78 -10.578 -0.590 -15.437 1.00 50.14 O ANISOU 2966 OG1 THR B 78 5838 8125 5089 -1595 612 511 O ATOM 2967 CG2 THR B 78 -8.417 0.420 -15.117 1.00 46.06 C ANISOU 2967 CG2 THR B 78 5344 7584 4572 -1240 574 480 C ATOM 2968 N LEU B 79 -8.935 3.679 -15.297 1.00 38.20 N ANISOU 2968 N LEU B 79 4008 6928 3579 -976 580 -345 N ATOM 2969 CA LEU B 79 -8.013 4.759 -15.616 1.00 39.33 C ANISOU 2969 CA LEU B 79 4160 6938 3844 -787 545 -516 C ATOM 2970 C LEU B 79 -6.588 4.303 -15.337 1.00 40.44 C ANISOU 2970 C LEU B 79 4371 6994 4000 -746 517 -274 C ATOM 2971 O LEU B 79 -6.318 3.685 -14.303 1.00 39.70 O ANISOU 2971 O LEU B 79 4218 7143 3724 -850 506 -81 O ATOM 2972 CB LEU B 79 -8.340 6.009 -14.794 1.00 34.98 C ANISOU 2972 CB LEU B 79 3395 6716 3179 -764 536 -840 C ATOM 2973 CG LEU B 79 -7.409 7.215 -14.916 1.00 38.10 C ANISOU 2973 CG LEU B 79 3779 6992 3707 -618 483 -1035 C ATOM 2974 CD1 LEU B 79 -7.484 7.830 -16.308 1.00 38.30 C ANISOU 2974 CD1 LEU B 79 3936 6622 3996 -469 475 -1139 C ATOM 2975 CD2 LEU B 79 -7.741 8.245 -13.844 1.00 38.05 C ANISOU 2975 CD2 LEU B 79 3568 7344 3546 -622 462 -1359 C ATOM 2976 N TYR B 80 -5.678 4.600 -16.260 1.00 38.00 N ANISOU 2976 N TYR B 80 4176 6363 3899 -590 507 -266 N ATOM 2977 CA TYR B 80 -4.287 4.193 -16.135 1.00 38.67 C ANISOU 2977 CA TYR B 80 4296 6362 4034 -520 486 -46 C ATOM 2978 C TYR B 80 -3.371 5.406 -16.132 1.00 39.12 C ANISOU 2978 C TYR B 80 4248 6425 4191 -430 455 -216 C ATOM 2979 O TYR B 80 -3.642 6.416 -16.788 1.00 42.01 O ANISOU 2979 O TYR B 80 4620 6657 4684 -370 467 -443 O ATOM 2980 CB TYR B 80 -3.859 3.265 -17.274 1.00 37.99 C ANISOU 2980 CB TYR B 80 4430 5890 4116 -414 523 158 C ATOM 2981 CG TYR B 80 -4.572 1.937 -17.310 1.00 46.23 C ANISOU 2981 CG TYR B 80 5610 6846 5109 -514 531 350 C ATOM 2982 CD1 TYR B 80 -4.189 0.901 -16.469 1.00 44.54 C ANISOU 2982 CD1 TYR B 80 5408 6715 4800 -582 502 640 C ATOM 2983 CD2 TYR B 80 -5.611 1.711 -18.201 1.00 40.80 C ANISOU 2983 CD2 TYR B 80 5044 5978 4482 -549 550 253 C ATOM 2984 CE1 TYR B 80 -4.833 -0.319 -16.505 1.00 45.64 C ANISOU 2984 CE1 TYR B 80 5690 6723 4930 -700 503 836 C ATOM 2985 CE2 TYR B 80 -6.259 0.493 -18.246 1.00 43.77 C ANISOU 2985 CE2 TYR B 80 5542 6246 4842 -678 542 418 C ATOM 2986 CZ TYR B 80 -5.866 -0.517 -17.395 1.00 42.73 C ANISOU 2986 CZ TYR B 80 5435 6161 4641 -762 523 713 C ATOM 2987 OH TYR B 80 -6.510 -1.731 -17.434 1.00 49.94 O ANISOU 2987 OH TYR B 80 6487 6919 5571 -916 509 895 O ATOM 2988 N LEU B 81 -2.268 5.285 -15.399 1.00 37.52 N ANISOU 2988 N LEU B 81 3946 6367 3943 -428 402 -86 N ATOM 2989 CA LEU B 81 -1.191 6.270 -15.435 1.00 36.98 C ANISOU 2989 CA LEU B 81 3766 6277 4007 -371 362 -196 C ATOM 2990 C LEU B 81 0.126 5.514 -15.503 1.00 40.42 C ANISOU 2990 C LEU B 81 4195 6650 4515 -287 350 95 C ATOM 2991 O LEU B 81 0.528 4.869 -14.529 1.00 42.54 O ANISOU 2991 O LEU B 81 4382 7156 4625 -322 278 270 O ATOM 2992 CB LEU B 81 -1.229 7.196 -14.218 1.00 35.86 C ANISOU 2992 CB LEU B 81 3426 6486 3712 -470 268 -440 C ATOM 2993 CG LEU B 81 -0.176 8.307 -14.227 1.00 43.97 C ANISOU 2993 CG LEU B 81 4332 7470 4906 -457 202 -594 C ATOM 2994 CD1 LEU B 81 -0.384 9.234 -15.419 1.00 40.20 C ANISOU 2994 CD1 LEU B 81 3948 6636 4690 -392 263 -753 C ATOM 2995 CD2 LEU B 81 -0.195 9.093 -12.924 1.00 43.26 C ANISOU 2995 CD2 LEU B 81 4060 7742 4635 -560 83 -860 C ATOM 2996 N GLN B 82 0.789 5.583 -16.651 1.00 37.94 N ANISOU 2996 N GLN B 82 3957 6035 4424 -160 423 157 N ATOM 2997 CA GLN B 82 2.106 4.990 -16.821 1.00 39.10 C ANISOU 2997 CA GLN B 82 4058 6128 4670 -42 430 399 C ATOM 2998 C GLN B 82 3.153 6.058 -16.533 1.00 44.28 C ANISOU 2998 C GLN B 82 4486 6906 5432 -75 374 295 C ATOM 2999 O GLN B 82 3.188 7.098 -17.199 1.00 43.39 O ANISOU 2999 O GLN B 82 4366 6643 5478 -92 420 126 O ATOM 3000 CB GLN B 82 2.273 4.424 -18.231 1.00 43.71 C ANISOU 3000 CB GLN B 82 4833 6361 5414 123 562 515 C ATOM 3001 CG GLN B 82 3.639 3.807 -18.505 1.00 41.88 C ANISOU 3001 CG GLN B 82 4538 6076 5298 291 597 744 C ATOM 3002 CD GLN B 82 3.857 2.507 -17.757 1.00 42.27 C ANISOU 3002 CD GLN B 82 4608 6204 5247 347 525 995 C ATOM 3003 OE1 GLN B 82 2.940 1.701 -17.606 1.00 44.59 O ANISOU 3003 OE1 GLN B 82 5079 6427 5437 301 512 1057 O ATOM 3004 NE2 GLN B 82 5.079 2.299 -17.280 1.00 50.11 N ANISOU 3004 NE2 GLN B 82 5412 7345 6283 440 469 1158 N ATOM 3005 N MET B 83 3.989 5.809 -15.531 1.00 42.97 N ANISOU 3005 N MET B 83 4134 7010 5183 -95 260 407 N ATOM 3006 CA MET B 83 5.014 6.748 -15.098 1.00 39.65 C ANISOU 3006 CA MET B 83 3462 6751 4852 -162 168 303 C ATOM 3007 C MET B 83 6.378 6.151 -15.410 1.00 44.04 C ANISOU 3007 C MET B 83 3893 7293 5549 -20 185 567 C ATOM 3008 O MET B 83 6.720 5.081 -14.899 1.00 50.89 O ANISOU 3008 O MET B 83 4742 8285 6308 77 128 808 O ATOM 3009 CB MET B 83 4.885 7.046 -13.602 1.00 47.07 C ANISOU 3009 CB MET B 83 4246 8089 5549 -304 -10 172 C ATOM 3010 CG MET B 83 3.554 7.675 -13.200 1.00 49.09 C ANISOU 3010 CG MET B 83 4584 8419 5649 -420 -16 -122 C ATOM 3011 SD MET B 83 3.430 8.014 -11.427 1.00 67.16 S ANISOU 3011 SD MET B 83 6689 11235 7593 -565 -205 -305 S ATOM 3012 CE MET B 83 3.462 6.355 -10.757 1.00 53.86 C ANISOU 3012 CE MET B 83 5051 9771 5643 -508 -229 122 C ATOM 3013 N ASN B 84 7.149 6.837 -16.248 1.00 51.38 N ANISOU 3013 N ASN B 84 4118 11031 4374 -704 522 180 N ATOM 3014 CA ASN B 84 8.482 6.401 -16.630 1.00 51.88 C ANISOU 3014 CA ASN B 84 3894 11385 4434 -736 654 95 C ATOM 3015 C ASN B 84 9.513 7.404 -16.130 1.00 54.65 C ANISOU 3015 C ASN B 84 4181 11727 4857 -945 595 318 C ATOM 3016 O ASN B 84 9.186 8.548 -15.805 1.00 52.32 O ANISOU 3016 O ASN B 84 4073 11228 4576 -1099 478 541 O ATOM 3017 CB ASN B 84 8.602 6.246 -18.156 1.00 54.10 C ANISOU 3017 CB ASN B 84 4073 12025 4455 -782 789 24 C ATOM 3018 CG ASN B 84 7.630 5.223 -18.718 1.00 63.03 C ANISOU 3018 CG ASN B 84 5262 13147 5540 -600 809 -265 C ATOM 3019 OD1 ASN B 84 7.418 4.162 -18.131 1.00 64.91 O ANISOU 3019 OD1 ASN B 84 5473 13198 5991 -414 819 -506 O ATOM 3020 ND2 ASN B 84 7.025 5.544 -19.855 1.00 74.29 N ANISOU 3020 ND2 ASN B 84 6747 14773 6704 -666 802 -228 N ATOM 3021 N SER B 85 10.768 6.953 -16.072 1.00 54.80 N ANISOU 3021 N SER B 85 3910 11957 4955 -943 674 228 N ATOM 3022 CA SER B 85 11.906 7.801 -15.709 1.00 63.14 C ANISOU 3022 CA SER B 85 4818 13087 6085 -1172 636 398 C ATOM 3023 C SER B 85 11.631 8.581 -14.424 1.00 59.34 C ANISOU 3023 C SER B 85 4556 12226 5766 -1241 409 509 C ATOM 3024 O SER B 85 11.833 9.795 -14.344 1.00 56.30 O ANISOU 3024 O SER B 85 4240 11748 5406 -1503 341 704 O ATOM 3025 CB SER B 85 12.264 8.744 -16.858 1.00 68.44 C ANISOU 3025 CB SER B 85 5468 13972 6564 -1441 735 616 C ATOM 3026 OG SER B 85 12.575 8.015 -18.032 1.00 76.94 O ANISOU 3026 OG SER B 85 6461 15293 7479 -1328 874 451 O ATOM 3027 N LEU B 86 11.162 7.864 -13.408 1.00 54.04 N ANISOU 3027 N LEU B 86 3990 11334 5210 -1011 299 373 N ATOM 3028 CA LEU B 86 10.726 8.504 -12.175 1.00 57.53 C ANISOU 3028 CA LEU B 86 4650 11471 5738 -1042 101 420 C ATOM 3029 C LEU B 86 11.892 9.180 -11.462 1.00 58.82 C ANISOU 3029 C LEU B 86 4655 11691 6003 -1238 -16 463 C ATOM 3030 O LEU B 86 12.990 8.623 -11.360 1.00 61.93 O ANISOU 3030 O LEU B 86 4750 12325 6457 -1207 3 410 O ATOM 3031 CB LEU B 86 10.059 7.473 -11.264 1.00 51.75 C ANISOU 3031 CB LEU B 86 4019 10580 5062 -765 38 299 C ATOM 3032 CG LEU B 86 8.644 7.090 -11.718 1.00 55.40 C ANISOU 3032 CG LEU B 86 4692 10900 5458 -634 104 252 C ATOM 3033 CD1 LEU B 86 8.181 5.769 -11.123 1.00 50.46 C ANISOU 3033 CD1 LEU B 86 4077 10169 4925 -382 111 142 C ATOM 3034 CD2 LEU B 86 7.666 8.200 -11.365 1.00 54.21 C ANISOU 3034 CD2 LEU B 86 4812 10516 5268 -723 5 333 C ATOM 3035 N LYS B 87 11.650 10.398 -10.987 1.00 58.33 N ANISOU 3035 N LYS B 87 4773 11404 5985 -1438 -143 535 N ATOM 3036 CA LYS B 87 12.620 11.178 -10.231 1.00 60.05 C ANISOU 3036 CA LYS B 87 4870 11628 6319 -1668 -286 525 C ATOM 3037 C LYS B 87 12.156 11.318 -8.787 1.00 55.28 C ANISOU 3037 C LYS B 87 4444 10828 5731 -1578 -489 383 C ATOM 3038 O LYS B 87 11.046 10.919 -8.424 1.00 52.77 O ANISOU 3038 O LYS B 87 4350 10356 5342 -1363 -495 332 O ATOM 3039 CB LYS B 87 12.812 12.568 -10.850 1.00 59.93 C ANISOU 3039 CB LYS B 87 4902 11483 6385 -2020 -271 692 C ATOM 3040 CG LYS B 87 12.852 12.593 -12.366 1.00 71.79 C ANISOU 3040 CG LYS B 87 6328 13168 7783 -2109 -56 898 C ATOM 3041 CD LYS B 87 12.705 14.017 -12.881 1.00 79.01 C ANISOU 3041 CD LYS B 87 7385 13844 8791 -2423 -67 1147 C ATOM 3042 CE LYS B 87 12.730 14.066 -14.397 1.00 89.29 C ANISOU 3042 CE LYS B 87 8611 15400 9917 -2523 143 1414 C ATOM 3043 NZ LYS B 87 12.484 15.441 -14.910 1.00 98.06 N ANISOU 3043 NZ LYS B 87 9889 16236 11134 -2808 119 1747 N ATOM 3044 N HIS B 88 13.023 11.908 -7.959 1.00 55.65 N ANISOU 3044 N HIS B 88 4365 10922 5855 -1766 -653 305 N ATOM 3045 CA HIS B 88 12.645 12.184 -6.576 1.00 60.38 C ANISOU 3045 CA HIS B 88 5120 11405 6417 -1720 -852 132 C ATOM 3046 C HIS B 88 11.453 13.129 -6.506 1.00 62.04 C ANISOU 3046 C HIS B 88 5673 11236 6663 -1756 -865 79 C ATOM 3047 O HIS B 88 10.601 13.001 -5.619 1.00 62.54 O ANISOU 3047 O HIS B 88 5925 11211 6626 -1585 -933 -58 O ATOM 3048 CB HIS B 88 13.821 12.779 -5.804 1.00 68.11 C ANISOU 3048 CB HIS B 88 5880 12532 7466 -1963 -1042 13 C ATOM 3049 CG HIS B 88 13.401 13.735 -4.731 1.00 81.90 C ANISOU 3049 CG HIS B 88 7828 14072 9216 -2075 -1227 -213 C ATOM 3050 ND1 HIS B 88 12.802 13.324 -3.560 1.00 85.37 N ANISOU 3050 ND1 HIS B 88 8401 14579 9459 -1860 -1340 -365 N ATOM 3051 CD2 HIS B 88 13.462 15.087 -4.667 1.00 86.66 C ANISOU 3051 CD2 HIS B 88 8524 14397 10007 -2379 -1306 -332 C ATOM 3052 CE1 HIS B 88 12.526 14.379 -2.814 1.00 86.37 C ANISOU 3052 CE1 HIS B 88 8678 14523 9616 -2014 -1476 -617 C ATOM 3053 NE2 HIS B 88 12.916 15.461 -3.463 1.00 87.92 N ANISOU 3053 NE2 HIS B 88 8858 14468 10079 -2324 -1466 -616 N ATOM 3054 N GLU B 89 11.380 14.091 -7.429 1.00 59.98 N ANISOU 3054 N GLU B 89 5481 10758 6549 -1971 -797 204 N ATOM 3055 CA GLU B 89 10.270 15.036 -7.443 1.00 61.55 C ANISOU 3055 CA GLU B 89 5985 10557 6844 -1975 -820 180 C ATOM 3056 C GLU B 89 8.934 14.364 -7.728 1.00 58.90 C ANISOU 3056 C GLU B 89 5834 10174 6373 -1663 -719 217 C ATOM 3057 O GLU B 89 7.889 14.994 -7.530 1.00 60.36 O ANISOU 3057 O GLU B 89 6248 10065 6620 -1588 -752 150 O ATOM 3058 CB GLU B 89 10.534 16.139 -8.472 1.00 72.86 C ANISOU 3058 CB GLU B 89 7433 11765 8484 -2263 -772 404 C ATOM 3059 CG GLU B 89 10.620 15.648 -9.908 1.00 85.77 C ANISOU 3059 CG GLU B 89 8967 13612 10012 -2254 -575 705 C ATOM 3060 CD GLU B 89 11.077 16.730 -10.871 1.00101.09 C ANISOU 3060 CD GLU B 89 10880 15410 12118 -2588 -524 997 C ATOM 3061 OE1 GLU B 89 11.737 17.690 -10.421 1.00107.28 O ANISOU 3061 OE1 GLU B 89 11628 15987 13146 -2884 -632 958 O ATOM 3062 OE2 GLU B 89 10.776 16.620 -12.078 1.00104.14 O1- ANISOU 3062 OE2 GLU B 89 11276 15907 12386 -2572 -378 1272 O1- ATOM 3063 N ASP B 90 8.940 13.111 -8.180 1.00 49.67 N ANISOU 3063 N ASP B 90 4548 9271 5052 -1481 -600 292 N ATOM 3064 CA ASP B 90 7.717 12.346 -8.378 1.00 45.64 C ANISOU 3064 CA ASP B 90 4173 8736 4431 -1212 -512 290 C ATOM 3065 C ASP B 90 7.262 11.624 -7.116 1.00 44.49 C ANISOU 3065 C ASP B 90 4081 8639 4185 -1012 -571 129 C ATOM 3066 O ASP B 90 6.162 11.062 -7.105 1.00 47.86 O ANISOU 3066 O ASP B 90 4621 9020 4545 -818 -502 113 O ATOM 3067 CB ASP B 90 7.909 11.328 -9.507 1.00 48.38 C ANISOU 3067 CB ASP B 90 4370 9318 4696 -1130 -350 405 C ATOM 3068 CG ASP B 90 8.303 11.980 -10.824 1.00 54.63 C ANISOU 3068 CG ASP B 90 5097 10160 5500 -1329 -263 600 C ATOM 3069 OD1 ASP B 90 7.718 13.026 -11.176 1.00 50.15 O ANISOU 3069 OD1 ASP B 90 4699 9359 4995 -1423 -298 716 O ATOM 3070 OD2 ASP B 90 9.203 11.447 -11.505 1.00 56.35 O1- ANISOU 3070 OD2 ASP B 90 5081 10663 5665 -1383 -155 649 O1- ATOM 3071 N THR B 91 8.077 11.616 -6.063 1.00 52.80 N ANISOU 3071 N THR B 91 5035 9820 5208 -1067 -698 27 N ATOM 3072 CA THR B 91 7.677 11.011 -4.798 1.00 53.04 C ANISOU 3072 CA THR B 91 5115 9952 5086 -898 -764 -78 C ATOM 3073 C THR B 91 6.533 11.813 -4.189 1.00 52.51 C ANISOU 3073 C THR B 91 5282 9681 4988 -865 -793 -246 C ATOM 3074 O THR B 91 6.696 12.995 -3.869 1.00 60.88 O ANISOU 3074 O THR B 91 6406 10588 6135 -1023 -896 -404 O ATOM 3075 CB THR B 91 8.862 10.949 -3.837 1.00 53.65 C ANISOU 3075 CB THR B 91 5013 10274 5098 -979 -928 -139 C ATOM 3076 OG1 THR B 91 9.802 9.970 -4.297 1.00 52.44 O ANISOU 3076 OG1 THR B 91 4613 10331 4982 -922 -891 14 O ATOM 3077 CG2 THR B 91 8.399 10.580 -2.429 1.00 51.05 C ANISOU 3077 CG2 THR B 91 4761 10088 4546 -839 -1019 -234 C ATOM 3078 N ALA B 92 5.382 11.171 -4.026 1.00 47.41 N ANISOU 3078 N ALA B 92 4743 9024 4249 -662 -696 -236 N ATOM 3079 CA ALA B 92 4.172 11.830 -3.545 1.00 49.61 C ANISOU 3079 CA ALA B 92 5204 9144 4503 -587 -684 -404 C ATOM 3080 C ALA B 92 3.109 10.761 -3.327 1.00 49.37 C ANISOU 3080 C ALA B 92 5203 9207 4347 -383 -558 -342 C ATOM 3081 O ALA B 92 3.300 9.587 -3.662 1.00 42.59 O ANISOU 3081 O ALA B 92 4249 8459 3474 -315 -486 -170 O ATOM 3082 CB ALA B 92 3.675 12.890 -4.533 1.00 46.35 C ANISOU 3082 CB ALA B 92 4896 8415 4301 -644 -665 -397 C ATOM 3083 N VAL B 93 1.986 11.178 -2.756 1.00 49.33 N ANISOU 3083 N VAL B 93 5315 9146 4284 -291 -523 -502 N ATOM 3084 CA VAL B 93 0.774 10.369 -2.739 1.00 50.39 C ANISOU 3084 CA VAL B 93 5466 9326 4354 -133 -379 -449 C ATOM 3085 C VAL B 93 -0.032 10.732 -3.978 1.00 43.38 C ANISOU 3085 C VAL B 93 4615 8220 3650 -91 -319 -416 C ATOM 3086 O VAL B 93 -0.357 11.904 -4.195 1.00 45.79 O ANISOU 3086 O VAL B 93 5000 8321 4075 -97 -373 -530 O ATOM 3087 CB VAL B 93 -0.043 10.605 -1.461 1.00 50.09 C ANISOU 3087 CB VAL B 93 5486 9422 4126 -52 -350 -644 C ATOM 3088 CG1 VAL B 93 -1.339 9.816 -1.514 1.00 53.03 C ANISOU 3088 CG1 VAL B 93 5841 9844 4463 76 -182 -574 C ATOM 3089 CG2 VAL B 93 0.768 10.234 -0.225 1.00 51.50 C ANISOU 3089 CG2 VAL B 93 5620 9900 4049 -97 -432 -646 C ATOM 3090 N TYR B 94 -0.355 9.736 -4.793 1.00 43.79 N ANISOU 3090 N TYR B 94 4599 8307 3733 -43 -222 -264 N ATOM 3091 CA TYR B 94 -1.090 9.957 -6.029 1.00 43.57 C ANISOU 3091 CA TYR B 94 4575 8161 3820 -5 -185 -221 C ATOM 3092 C TYR B 94 -2.562 9.642 -5.810 1.00 49.03 C ANISOU 3092 C TYR B 94 5260 8876 4494 130 -93 -297 C ATOM 3093 O TYR B 94 -2.902 8.585 -5.270 1.00 48.15 O ANISOU 3093 O TYR B 94 5093 8891 4310 160 2 -275 O ATOM 3094 CB TYR B 94 -0.514 9.107 -7.161 1.00 43.90 C ANISOU 3094 CB TYR B 94 4516 8273 3892 -53 -142 -79 C ATOM 3095 CG TYR B 94 0.785 9.659 -7.702 1.00 43.50 C ANISOU 3095 CG TYR B 94 4436 8215 3877 -194 -211 3 C ATOM 3096 CD1 TYR B 94 1.948 9.606 -6.948 1.00 44.83 C ANISOU 3096 CD1 TYR B 94 4557 8455 4020 -275 -271 -1 C ATOM 3097 CD2 TYR B 94 0.846 10.243 -8.965 1.00 40.42 C ANISOU 3097 CD2 TYR B 94 4041 7786 3529 -259 -220 107 C ATOM 3098 CE1 TYR B 94 3.135 10.114 -7.428 1.00 49.29 C ANISOU 3098 CE1 TYR B 94 5053 9040 4636 -429 -324 67 C ATOM 3099 CE2 TYR B 94 2.035 10.756 -9.456 1.00 39.88 C ANISOU 3099 CE2 TYR B 94 3924 7741 3488 -423 -256 212 C ATOM 3100 CZ TYR B 94 3.176 10.685 -8.681 1.00 45.30 C ANISOU 3100 CZ TYR B 94 4544 8485 4183 -514 -301 177 C ATOM 3101 OH TYR B 94 4.361 11.191 -9.156 1.00 46.81 O ANISOU 3101 OH TYR B 94 4644 8723 4419 -702 -327 274 O ATOM 3102 N TYR B 95 -3.426 10.563 -6.225 1.00 45.04 N ANISOU 3102 N TYR B 95 4793 8241 4077 208 -124 -364 N ATOM 3103 CA TYR B 95 -4.863 10.443 -6.029 1.00 44.34 C ANISOU 3103 CA TYR B 95 4657 8195 3994 347 -46 -463 C ATOM 3104 C TYR B 95 -5.558 10.281 -7.373 1.00 44.25 C ANISOU 3104 C TYR B 95 4571 8181 4062 392 -53 -374 C ATOM 3105 O TYR B 95 -5.272 11.019 -8.321 1.00 44.19 O ANISOU 3105 O TYR B 95 4601 8066 4123 378 -153 -269 O ATOM 3106 CB TYR B 95 -5.430 11.668 -5.306 1.00 45.26 C ANISOU 3106 CB TYR B 95 4840 8193 4166 458 -85 -665 C ATOM 3107 CG TYR B 95 -4.812 11.956 -3.953 1.00 50.24 C ANISOU 3107 CG TYR B 95 5535 8879 4673 411 -94 -828 C ATOM 3108 CD1 TYR B 95 -3.717 12.800 -3.834 1.00 47.22 C ANISOU 3108 CD1 TYR B 95 5246 8346 4351 303 -224 -870 C ATOM 3109 CD2 TYR B 95 -5.338 11.397 -2.792 1.00 42.24 C ANISOU 3109 CD2 TYR B 95 4475 8110 3466 456 24 -941 C ATOM 3110 CE1 TYR B 95 -3.154 13.073 -2.601 1.00 55.39 C ANISOU 3110 CE1 TYR B 95 6318 9481 5248 248 -258 -1065 C ATOM 3111 CE2 TYR B 95 -4.781 11.666 -1.551 1.00 49.44 C ANISOU 3111 CE2 TYR B 95 5435 9157 4193 413 2 -1099 C ATOM 3112 CZ TYR B 95 -3.689 12.504 -1.464 1.00 57.04 C ANISOU 3112 CZ TYR B 95 6484 9977 5211 314 -152 -1183 C ATOM 3113 OH TYR B 95 -3.129 12.776 -0.238 1.00 62.24 O ANISOU 3113 OH TYR B 95 7170 10815 5664 259 -200 -1383 O ATOM 3114 N CYS B 96 -6.473 9.324 -7.442 1.00 47.09 N ANISOU 3114 N CYS B 96 4812 8679 4401 428 47 -403 N ATOM 3115 CA CYS B 96 -7.387 9.193 -8.564 1.00 48.30 C ANISOU 3115 CA CYS B 96 4856 8891 4606 484 26 -387 C ATOM 3116 C CYS B 96 -8.595 10.095 -8.343 1.00 45.10 C ANISOU 3116 C CYS B 96 4408 8449 4279 660 -5 -489 C ATOM 3117 O CYS B 96 -9.120 10.186 -7.230 1.00 45.13 O ANISOU 3117 O CYS B 96 4393 8482 4274 726 81 -632 O ATOM 3118 CB CYS B 96 -7.831 7.737 -8.712 1.00 56.35 C ANISOU 3118 CB CYS B 96 5739 10055 5617 417 142 -417 C ATOM 3119 SG CYS B 96 -9.092 7.411 -9.962 1.00 65.38 S ANISOU 3119 SG CYS B 96 6693 11347 6800 457 109 -478 S ATOM 3120 N ALA B 97 -9.023 10.771 -9.405 1.00 48.57 N ANISOU 3120 N ALA B 97 4817 8853 4785 749 -129 -408 N ATOM 3121 CA ALA B 97 -10.188 11.644 -9.366 1.00 46.21 C ANISOU 3121 CA ALA B 97 4445 8503 4610 962 -188 -481 C ATOM 3122 C ALA B 97 -11.198 11.194 -10.414 1.00 45.12 C ANISOU 3122 C ALA B 97 4108 8575 4459 1019 -237 -444 C ATOM 3123 O ALA B 97 -10.827 10.869 -11.546 1.00 49.26 O ANISOU 3123 O ALA B 97 4621 9207 4890 929 -312 -303 O ATOM 3124 CB ALA B 97 -9.796 13.105 -9.602 1.00 51.83 C ANISOU 3124 CB ALA B 97 5302 8923 5469 1055 -340 -380 C ATOM 3125 N ALA B 98 -12.474 11.175 -10.032 1.00 46.19 N ANISOU 3125 N ALA B 98 4062 8818 4669 1164 -193 -596 N ATOM 3126 CA ALA B 98 -13.538 10.682 -10.894 1.00 53.82 C ANISOU 3126 CA ALA B 98 4786 10032 5629 1206 -243 -611 C ATOM 3127 C ALA B 98 -14.661 11.704 -10.990 1.00 59.18 C ANISOU 3127 C ALA B 98 5325 10696 6464 1492 -357 -639 C ATOM 3128 O ALA B 98 -14.878 12.503 -10.075 1.00 62.74 O ANISOU 3128 O ALA B 98 5816 10974 7050 1656 -314 -755 O ATOM 3129 CB ALA B 98 -14.105 9.349 -10.384 1.00 50.63 C ANISOU 3129 CB ALA B 98 4208 9833 5196 1061 -59 -776 C ATOM 3130 N ARG B 99 -15.378 11.662 -12.111 1.00 57.43 N ANISOU 3130 N ARG B 99 4917 10679 6222 1566 -510 -554 N ATOM 3131 CA ARG B 99 -16.548 12.497 -12.336 1.00 61.78 C ANISOU 3131 CA ARG B 99 5270 11271 6934 1866 -648 -556 C ATOM 3132 C ARG B 99 -17.812 11.653 -12.270 1.00 68.80 C ANISOU 3132 C ARG B 99 5803 12509 7828 1862 -575 -767 C ATOM 3133 O ARG B 99 -17.831 10.507 -12.735 1.00 67.86 O ANISOU 3133 O ARG B 99 5581 12629 7574 1627 -534 -820 O ATOM 3134 CB ARG B 99 -16.489 13.200 -13.696 1.00 64.56 C ANISOU 3134 CB ARG B 99 5639 11642 7249 1979 -922 -246 C ATOM 3135 CG ARG B 99 -15.282 14.088 -13.914 1.00 72.78 C ANISOU 3135 CG ARG B 99 7000 12344 8309 1951 -1001 23 C ATOM 3136 CD ARG B 99 -15.559 15.096 -15.019 1.00 83.06 C ANISOU 3136 CD ARG B 99 8285 13612 9661 2155 -1274 378 C ATOM 3137 NE ARG B 99 -14.339 15.717 -15.526 1.00 93.49 N ANISOU 3137 NE ARG B 99 9883 14703 10936 2031 -1344 710 N ATOM 3138 CZ ARG B 99 -13.713 16.730 -14.937 1.00 96.20 C ANISOU 3138 CZ ARG B 99 10453 14566 11533 2075 -1341 787 C ATOM 3139 NH1 ARG B 99 -14.187 17.239 -13.808 1.00 93.42 N ANISOU 3139 NH1 ARG B 99 10095 13926 11475 2265 -1274 513 N ATOM 3140 NH2 ARG B 99 -12.610 17.231 -15.474 1.00 99.07 N ANISOU 3140 NH2 ARG B 99 11032 14755 11856 1913 -1397 1110 N ATOM 3141 N ALA B 100 -18.866 12.226 -11.696 1.00 65.96 N ANISOU 3141 N ALA B 100 5237 12172 7655 2118 -556 -912 N ATOM 3142 CA ALA B 100 -20.172 11.598 -11.753 1.00 68.33 C ANISOU 3142 CA ALA B 100 5136 12835 7992 2138 -517 -1088 C ATOM 3143 C ALA B 100 -20.753 11.736 -13.160 1.00 78.83 C ANISOU 3143 C ALA B 100 6260 14409 9282 2244 -807 -940 C ATOM 3144 O ALA B 100 -20.453 12.700 -13.870 1.00 75.58 O ANISOU 3144 O ALA B 100 5979 13851 8887 2438 -1037 -682 O ATOM 3145 CB ALA B 100 -21.117 12.228 -10.734 1.00 65.31 C ANISOU 3145 CB ALA B 100 4552 12450 7812 2406 -399 -1304 C ATOM 3146 N PRO B 101 -21.578 10.779 -13.590 1.00 87.62 N ANISOU 3146 N PRO B 101 7096 15860 10337 2079 -799 -1074 N ATOM 3147 CA PRO B 101 -22.163 10.875 -14.938 1.00 96.11 C ANISOU 3147 CA PRO B 101 8055 17138 11323 2119 -1066 -946 C ATOM 3148 C PRO B 101 -23.024 12.109 -15.141 1.00101.85 C ANISOU 3148 C PRO B 101 8649 17813 12237 2513 -1263 -817 C ATOM 3149 O PRO B 101 -23.181 12.562 -16.282 1.00109.41 O ANISOU 3149 O PRO B 101 9595 18868 13109 2620 -1532 -577 O ATOM 3150 CB PRO B 101 -22.986 9.584 -15.051 1.00 96.33 C ANISOU 3150 CB PRO B 101 7876 17405 11320 1819 -951 -1194 C ATOM 3151 CG PRO B 101 -22.342 8.646 -14.080 1.00 95.55 C ANISOU 3151 CG PRO B 101 7890 17187 11229 1543 -660 -1341 C ATOM 3152 CD PRO B 101 -21.911 9.505 -12.934 1.00 91.28 C ANISOU 3152 CD PRO B 101 7472 16414 10798 1757 -535 -1304 C ATOM 3153 N VAL B 102 -23.586 12.668 -14.074 1.00103.77 N ANISOU 3153 N VAL B 102 8794 17903 12732 2733 -1130 -966 N ATOM 3154 CA VAL B 102 -24.381 13.885 -14.177 1.00109.03 C ANISOU 3154 CA VAL B 102 9328 18449 13651 3145 -1304 -872 C ATOM 3155 C VAL B 102 -23.470 15.106 -14.212 1.00112.13 C ANISOU 3155 C VAL B 102 9970 18470 14162 3435 -1456 -621 C ATOM 3156 O VAL B 102 -23.117 15.599 -15.284 1.00116.94 O ANISOU 3156 O VAL B 102 10687 19047 14699 3512 -1729 -262 O ATOM 3157 CB VAL B 102 -25.391 13.994 -13.021 1.00109.58 C ANISOU 3157 CB VAL B 102 9179 18506 13949 3265 -1079 -1179 C ATOM 3158 CG1 VAL B 102 -26.455 12.915 -13.143 1.00111.20 C ANISOU 3158 CG1 VAL B 102 9101 19068 14082 3006 -986 -1354 C ATOM 3159 CG2 VAL B 102 -24.675 13.896 -11.682 1.00105.16 C ANISOU 3159 CG2 VAL B 102 8798 17766 13390 3188 -778 -1385 C ATOM 3160 N ASP B 110 -12.949 20.541 -12.306 1.00120.85 N ANISOU 3160 N ASP B 110 14117 15883 15919 2496 -1392 520 N ATOM 3161 CA ASP B 110 -13.117 20.071 -10.936 1.00118.18 C ANISOU 3161 CA ASP B 110 13731 15632 15539 2492 -1179 -16 C ATOM 3162 C ASP B 110 -13.764 18.689 -10.930 1.00107.87 C ANISOU 3162 C ASP B 110 12194 14911 13879 2437 -1043 -159 C ATOM 3163 O ASP B 110 -14.519 18.346 -11.840 1.00110.91 O ANISOU 3163 O ASP B 110 12390 15580 14172 2536 -1142 28 O ATOM 3164 CB ASP B 110 -13.955 21.064 -10.128 1.00125.76 C ANISOU 3164 CB ASP B 110 14630 16244 16909 2853 -1196 -337 C ATOM 3165 CG ASP B 110 -13.765 20.908 -8.631 1.00127.58 C ANISOU 3165 CG ASP B 110 14894 16483 17098 2798 -982 -878 C ATOM 3166 OD1 ASP B 110 -13.762 19.759 -8.142 1.00126.02 O ANISOU 3166 OD1 ASP B 110 14609 16738 16534 2626 -799 -1044 O ATOM 3167 OD2 ASP B 110 -13.613 21.938 -7.941 1.00131.01 O ANISOU 3167 OD2 ASP B 110 15440 16469 17867 2923 -1004 -1135 O ATOM 3168 N TYR B 111 -13.470 17.900 -9.900 1.00 96.36 N ANISOU 3168 N TYR B 111 10745 13636 12234 2269 -829 -479 N ATOM 3169 CA TYR B 111 -13.914 16.518 -9.821 1.00 84.90 C ANISOU 3169 CA TYR B 111 9106 12666 10486 2148 -680 -585 C ATOM 3170 C TYR B 111 -14.814 16.315 -8.610 1.00 83.03 C ANISOU 3170 C TYR B 111 8699 12576 10275 2288 -496 -984 C ATOM 3171 O TYR B 111 -14.750 17.056 -7.626 1.00 90.12 O ANISOU 3171 O TYR B 111 9672 13251 11317 2403 -438 -1246 O ATOM 3172 CB TYR B 111 -12.720 15.557 -9.759 1.00 77.41 C ANISOU 3172 CB TYR B 111 8298 11852 9263 1795 -576 -521 C ATOM 3173 CG TYR B 111 -11.868 15.586 -11.006 1.00 73.17 C ANISOU 3173 CG TYR B 111 7872 11292 8638 1637 -711 -156 C ATOM 3174 CD1 TYR B 111 -10.899 16.563 -11.184 1.00 68.81 C ANISOU 3174 CD1 TYR B 111 7534 10389 8221 1574 -811 32 C ATOM 3175 CD2 TYR B 111 -12.039 14.642 -12.010 1.00 75.10 C ANISOU 3175 CD2 TYR B 111 7988 11888 8661 1534 -728 -18 C ATOM 3176 CE1 TYR B 111 -10.122 16.599 -12.323 1.00 71.05 C ANISOU 3176 CE1 TYR B 111 7893 10709 8392 1410 -905 389 C ATOM 3177 CE2 TYR B 111 -11.265 14.669 -13.154 1.00 72.14 C ANISOU 3177 CE2 TYR B 111 7692 11569 8148 1392 -828 287 C ATOM 3178 CZ TYR B 111 -10.308 15.650 -13.304 1.00 70.33 C ANISOU 3178 CZ TYR B 111 7668 11026 8028 1330 -906 512 C ATOM 3179 OH TYR B 111 -9.531 15.685 -14.437 1.00 72.99 O ANISOU 3179 OH TYR B 111 8062 11473 8199 1169 -976 839 O ATOM 3180 N ASP B 112 -15.653 15.285 -8.695 1.00 73.99 N ANISOU 3180 N ASP B 112 7304 11831 8977 2256 -394 -1045 N ATOM 3181 CA ASP B 112 -16.649 14.999 -7.671 1.00 74.96 C ANISOU 3181 CA ASP B 112 7200 12184 9099 2367 -197 -1373 C ATOM 3182 C ASP B 112 -16.189 13.972 -6.647 1.00 67.70 C ANISOU 3182 C ASP B 112 6329 11475 7919 2098 46 -1500 C ATOM 3183 O ASP B 112 -16.660 14.001 -5.506 1.00 69.74 O ANISOU 3183 O ASP B 112 6493 11871 8136 2167 232 -1774 O ATOM 3184 CB ASP B 112 -17.943 14.504 -8.325 1.00 81.19 C ANISOU 3184 CB ASP B 112 7636 13299 9914 2473 -226 -1357 C ATOM 3185 CG ASP B 112 -18.403 15.405 -9.454 1.00 86.41 C ANISOU 3185 CG ASP B 112 8224 13821 10786 2742 -505 -1152 C ATOM 3186 OD1 ASP B 112 -18.552 16.623 -9.221 1.00 89.84 O ANISOU 3186 OD1 ASP B 112 8710 13929 11496 3033 -595 -1208 O ATOM 3187 OD2 ASP B 112 -18.601 14.896 -10.578 1.00 86.09 O1- ANISOU 3187 OD2 ASP B 112 8074 13995 10640 2665 -643 -933 O1- ATOM 3188 N TYR B 113 -15.288 13.068 -7.022 1.00 59.25 N ANISOU 3188 N TYR B 113 5391 10453 6668 1810 51 -1299 N ATOM 3189 CA TYR B 113 -14.843 11.999 -6.142 1.00 54.11 C ANISOU 3189 CA TYR B 113 4777 9982 5800 1568 254 -1339 C ATOM 3190 C TYR B 113 -13.329 11.881 -6.200 1.00 54.31 C ANISOU 3190 C TYR B 113 5081 9830 5725 1373 194 -1182 C ATOM 3191 O TYR B 113 -12.705 12.161 -7.228 1.00 59.35 O ANISOU 3191 O TYR B 113 5826 10306 6417 1338 29 -991 O ATOM 3192 CB TYR B 113 -15.486 10.656 -6.517 1.00 55.24 C ANISOU 3192 CB TYR B 113 4703 10409 5877 1406 354 -1274 C ATOM 3193 CG TYR B 113 -16.991 10.722 -6.638 1.00 61.52 C ANISOU 3193 CG TYR B 113 5166 11422 6787 1570 390 -1413 C ATOM 3194 CD1 TYR B 113 -17.798 10.758 -5.507 1.00 58.31 C ANISOU 3194 CD1 TYR B 113 4585 11214 6358 1649 600 -1630 C ATOM 3195 CD2 TYR B 113 -17.606 10.746 -7.884 1.00 58.35 C ANISOU 3195 CD2 TYR B 113 4595 11085 6491 1646 215 -1334 C ATOM 3196 CE1 TYR B 113 -19.175 10.819 -5.613 1.00 64.57 C ANISOU 3196 CE1 TYR B 113 5024 12239 7270 1801 645 -1770 C ATOM 3197 CE2 TYR B 113 -18.982 10.807 -8.001 1.00 61.72 C ANISOU 3197 CE2 TYR B 113 4673 11745 7031 1802 226 -1466 C ATOM 3198 CZ TYR B 113 -19.761 10.842 -6.862 1.00 69.55 C ANISOU 3198 CZ TYR B 113 5478 12909 8040 1880 447 -1687 C ATOM 3199 OH TYR B 113 -21.130 10.902 -6.974 1.00 74.50 O ANISOU 3199 OH TYR B 113 5739 13774 8794 2024 464 -1820 O ATOM 3200 N TRP B 114 -12.746 11.454 -5.083 1.00 48.86 N ANISOU 3200 N TRP B 114 4481 9218 4867 1244 331 -1247 N ATOM 3201 CA TRP B 114 -11.303 11.339 -4.945 1.00 53.11 C ANISOU 3201 CA TRP B 114 5239 9632 5307 1073 277 -1128 C ATOM 3202 C TRP B 114 -10.962 10.031 -4.252 1.00 53.54 C ANISOU 3202 C TRP B 114 5276 9898 5168 884 431 -1043 C ATOM 3203 O TRP B 114 -11.653 9.619 -3.317 1.00 55.60 O ANISOU 3203 O TRP B 114 5425 10381 5317 888 601 -1133 O ATOM 3204 CB TRP B 114 -10.726 12.515 -4.146 1.00 62.44 C ANISOU 3204 CB TRP B 114 6580 10639 6506 1146 219 -1309 C ATOM 3205 CG TRP B 114 -10.963 13.840 -4.788 1.00 68.00 C ANISOU 3205 CG TRP B 114 7328 11034 7476 1329 58 -1356 C ATOM 3206 CD1 TRP B 114 -12.115 14.572 -4.759 1.00 73.49 C ANISOU 3206 CD1 TRP B 114 7895 11678 8350 1588 55 -1533 C ATOM 3207 CD2 TRP B 114 -10.025 14.598 -5.558 1.00 63.38 C ANISOU 3207 CD2 TRP B 114 6910 10132 7038 1272 -124 -1189 C ATOM 3208 NE1 TRP B 114 -11.952 15.738 -5.467 1.00 75.50 N ANISOU 3208 NE1 TRP B 114 8248 11559 8880 1714 -135 -1464 N ATOM 3209 CE2 TRP B 114 -10.677 15.778 -5.967 1.00 68.55 C ANISOU 3209 CE2 TRP B 114 7556 10514 7977 1501 -241 -1236 C ATOM 3210 CE3 TRP B 114 -8.697 14.393 -5.942 1.00 61.05 C ANISOU 3210 CE3 TRP B 114 6751 9765 6679 1049 -193 -990 C ATOM 3211 CZ2 TRP B 114 -10.045 16.749 -6.738 1.00 70.82 C ANISOU 3211 CZ2 TRP B 114 7989 10436 8486 1488 -421 -1044 C ATOM 3212 CZ3 TRP B 114 -8.072 15.357 -6.706 1.00 65.18 C ANISOU 3212 CZ3 TRP B 114 7395 9977 7393 1021 -353 -832 C ATOM 3213 CH2 TRP B 114 -8.746 16.521 -7.097 1.00 68.38 C ANISOU 3213 CH2 TRP B 114 7812 10090 8080 1226 -465 -838 C ATOM 3214 N GLY B 115 -9.900 9.381 -4.716 1.00 51.38 N ANISOU 3214 N GLY B 115 5098 9559 4866 724 377 -852 N ATOM 3215 CA GLY B 115 -9.404 8.212 -4.026 1.00 54.68 C ANISOU 3215 CA GLY B 115 5522 10104 5151 574 490 -731 C ATOM 3216 C GLY B 115 -8.671 8.581 -2.751 1.00 56.58 C ANISOU 3216 C GLY B 115 5880 10418 5201 558 498 -783 C ATOM 3217 O GLY B 115 -8.309 9.734 -2.513 1.00 50.42 O ANISOU 3217 O GLY B 115 5198 9539 4419 629 397 -942 O ATOM 3218 N GLN B 116 -8.454 7.577 -1.903 1.00 52.90 N ANISOU 3218 N GLN B 116 5395 10128 4576 458 608 -644 N ATOM 3219 CA GLN B 116 -7.687 7.823 -0.689 1.00 56.62 C ANISOU 3219 CA GLN B 116 5959 10751 4801 433 590 -667 C ATOM 3220 C GLN B 116 -6.205 8.020 -0.970 1.00 51.19 C ANISOU 3220 C GLN B 116 5392 9922 4136 368 412 -588 C ATOM 3221 O GLN B 116 -5.472 8.441 -0.071 1.00 47.97 O ANISOU 3221 O GLN B 116 5053 9634 3539 346 343 -657 O ATOM 3222 CB GLN B 116 -7.889 6.681 0.308 1.00 59.12 C ANISOU 3222 CB GLN B 116 6213 11332 4917 348 749 -462 C ATOM 3223 CG GLN B 116 -9.321 6.554 0.801 1.00 67.90 C ANISOU 3223 CG GLN B 116 7176 12664 5958 379 958 -546 C ATOM 3224 CD GLN B 116 -9.416 5.861 2.144 1.00 74.76 C ANISOU 3224 CD GLN B 116 8009 13888 6509 295 1114 -370 C ATOM 3225 OE1 GLN B 116 -8.872 6.337 3.141 1.00 76.18 O ANISOU 3225 OE1 GLN B 116 8274 14238 6431 310 1053 -443 O ATOM 3226 NE2 GLN B 116 -10.107 4.729 2.176 1.00 81.11 N ANISOU 3226 NE2 GLN B 116 8693 14741 7385 183 1282 -121 N ATOM 3227 N GLY B 117 -5.753 7.740 -2.184 1.00 52.20 N ANISOU 3227 N GLY B 117 5520 9844 4468 331 340 -469 N ATOM 3228 CA GLY B 117 -4.378 7.978 -2.558 1.00 57.42 C ANISOU 3228 CA GLY B 117 6251 10398 5166 264 194 -404 C ATOM 3229 C GLY B 117 -3.524 6.726 -2.449 1.00 62.29 C ANISOU 3229 C GLY B 117 6828 11071 5767 197 204 -169 C ATOM 3230 O GLY B 117 -3.837 5.777 -1.726 1.00 65.06 O ANISOU 3230 O GLY B 117 7137 11547 6034 192 304 -30 O ATOM 3231 N THR B 118 -2.422 6.732 -3.192 1.00 54.70 N ANISOU 3231 N THR B 118 5866 10009 4908 149 105 -107 N ATOM 3232 CA THR B 118 -1.459 5.642 -3.152 1.00 55.92 C ANISOU 3232 CA THR B 118 5959 10190 5099 125 93 86 C ATOM 3233 C THR B 118 -0.062 6.235 -3.103 1.00 52.30 C ANISOU 3233 C THR B 118 5499 9764 4608 71 -57 79 C ATOM 3234 O THR B 118 0.276 7.105 -3.912 1.00 49.46 O ANISOU 3234 O THR B 118 5157 9307 4328 18 -116 -12 O ATOM 3235 CB THR B 118 -1.604 4.716 -4.363 1.00 66.12 C ANISOU 3235 CB THR B 118 7171 11344 6606 129 166 136 C ATOM 3236 OG1 THR B 118 -2.956 4.249 -4.444 1.00 76.13 O ANISOU 3236 OG1 THR B 118 8414 12586 7925 145 291 107 O ATOM 3237 CG2 THR B 118 -0.678 3.523 -4.227 1.00 66.68 C ANISOU 3237 CG2 THR B 118 7166 11394 6775 147 166 309 C ATOM 3238 N GLN B 119 0.740 5.770 -2.151 1.00 50.41 N ANISOU 3238 N GLN B 119 5223 9679 4252 75 -123 201 N ATOM 3239 CA GLN B 119 2.079 6.310 -1.974 1.00 50.75 C ANISOU 3239 CA GLN B 119 5220 9807 4256 10 -282 179 C ATOM 3240 C GLN B 119 2.993 5.848 -3.100 1.00 54.21 C ANISOU 3240 C GLN B 119 5539 10155 4903 -1 -286 257 C ATOM 3241 O GLN B 119 3.082 4.652 -3.398 1.00 56.94 O ANISOU 3241 O GLN B 119 5804 10456 5374 83 -216 395 O ATOM 3242 CB GLN B 119 2.651 5.886 -0.621 1.00 51.67 C ANISOU 3242 CB GLN B 119 5297 10181 4154 37 -377 304 C ATOM 3243 CG GLN B 119 4.114 6.258 -0.431 1.00 57.45 C ANISOU 3243 CG GLN B 119 5921 11046 4860 -29 -562 292 C ATOM 3244 CD GLN B 119 4.336 7.758 -0.375 1.00 59.37 C ANISOU 3244 CD GLN B 119 6221 11278 5060 -172 -664 8 C ATOM 3245 OE1 GLN B 119 5.220 8.293 -1.044 1.00 67.55 O ANISOU 3245 OE1 GLN B 119 7181 12240 6245 -282 -737 -43 O ATOM 3246 NE2 GLN B 119 3.537 8.443 0.433 1.00 56.19 N ANISOU 3246 NE2 GLN B 119 5938 10940 4473 -177 -658 -187 N ATOM 3247 N VAL B 120 3.662 6.802 -3.737 1.00 47.78 N ANISOU 3247 N VAL B 120 4704 9307 4142 -111 -354 157 N ATOM 3248 CA VAL B 120 4.738 6.524 -4.677 1.00 48.78 C ANISOU 3248 CA VAL B 120 4677 9448 4407 -148 -357 213 C ATOM 3249 C VAL B 120 5.999 7.156 -4.113 1.00 44.60 C ANISOU 3249 C VAL B 120 4050 9068 3828 -259 -516 193 C ATOM 3250 O VAL B 120 6.050 8.374 -3.908 1.00 53.96 O ANISOU 3250 O VAL B 120 5310 10217 4977 -400 -598 66 O ATOM 3251 CB VAL B 120 4.432 7.059 -6.084 1.00 44.46 C ANISOU 3251 CB VAL B 120 4153 8786 3954 -219 -275 160 C ATOM 3252 CG1 VAL B 120 5.670 6.973 -6.961 1.00 47.34 C ANISOU 3252 CG1 VAL B 120 4335 9251 4399 -293 -267 198 C ATOM 3253 CG2 VAL B 120 3.283 6.282 -6.703 1.00 44.26 C ANISOU 3253 CG2 VAL B 120 4168 8672 3975 -113 -141 153 C ATOM 3254 N THR B 121 7.005 6.331 -3.848 1.00 46.11 N ANISOU 3254 N THR B 121 4060 9411 4051 -192 -571 305 N ATOM 3255 CA THR B 121 8.263 6.789 -3.276 1.00 58.85 C ANISOU 3255 CA THR B 121 5518 11225 5616 -290 -743 289 C ATOM 3256 C THR B 121 9.395 6.356 -4.192 1.00 55.98 C ANISOU 3256 C THR B 121 4904 10938 5430 -291 -710 343 C ATOM 3257 O THR B 121 9.550 5.163 -4.474 1.00 53.01 O ANISOU 3257 O THR B 121 4416 10556 5169 -107 -637 444 O ATOM 3258 CB THR B 121 8.467 6.237 -1.863 1.00 60.39 C ANISOU 3258 CB THR B 121 5681 11630 5634 -183 -882 391 C ATOM 3259 OG1 THR B 121 7.376 6.641 -1.028 1.00 62.36 O ANISOU 3259 OG1 THR B 121 6145 11873 5678 -187 -876 313 O ATOM 3260 CG2 THR B 121 9.767 6.752 -1.275 1.00 64.52 C ANISOU 3260 CG2 THR B 121 6012 12414 6088 -295 -1094 342 C ATOM 3261 N VAL B 122 10.175 7.323 -4.658 1.00 55.90 N ANISOU 3261 N VAL B 122 4792 10985 5462 -503 -750 264 N ATOM 3262 CA VAL B 122 11.301 7.075 -5.547 1.00 57.01 C ANISOU 3262 CA VAL B 122 4655 11265 5741 -542 -695 294 C ATOM 3263 C VAL B 122 12.570 7.176 -4.713 1.00 66.42 C ANISOU 3263 C VAL B 122 5596 12719 6923 -595 -890 299 C ATOM 3264 O VAL B 122 12.991 8.273 -4.330 1.00 74.57 O ANISOU 3264 O VAL B 122 6614 13805 7915 -837 -1018 204 O ATOM 3265 CB VAL B 122 11.315 8.058 -6.723 1.00 57.34 C ANISOU 3265 CB VAL B 122 4720 11236 5832 -773 -584 260 C ATOM 3266 CG1 VAL B 122 12.417 7.697 -7.697 1.00 56.31 C ANISOU 3266 CG1 VAL B 122 4278 11320 5799 -807 -477 289 C ATOM 3267 CG2 VAL B 122 9.962 8.062 -7.418 1.00 52.42 C ANISOU 3267 CG2 VAL B 122 4348 10393 5178 -711 -445 262 C ATOM 3268 N SER B 123 13.180 6.029 -4.428 1.00 57.45 N ANISOU 3268 N SER B 123 4248 11732 5850 -367 -929 402 N ATOM 3269 CA SER B 123 14.354 5.966 -3.575 1.00 61.03 C ANISOU 3269 CA SER B 123 4426 12480 6281 -360 -1146 438 C ATOM 3270 C SER B 123 15.301 4.892 -4.087 1.00 62.19 C ANISOU 3270 C SER B 123 4231 12761 6637 -144 -1096 519 C ATOM 3271 O SER B 123 14.878 3.887 -4.667 1.00 68.82 O ANISOU 3271 O SER B 123 5103 13430 7617 82 -934 564 O ATOM 3272 CB SER B 123 13.980 5.675 -2.115 1.00 55.58 C ANISOU 3272 CB SER B 123 3859 11877 5383 -236 -1341 530 C ATOM 3273 OG SER B 123 15.140 5.518 -1.318 1.00 59.08 O ANISOU 3273 OG SER B 123 4066 12582 5801 -198 -1543 582 O ATOM 3274 N SER B 124 16.595 5.121 -3.855 1.00 67.44 N ANISOU 3274 N SER B 124 4632 13635 7357 -213 -1209 494 N ATOM 3275 CA SER B 124 17.632 4.177 -4.249 1.00 72.16 C ANISOU 3275 CA SER B 124 4928 14308 8180 8 -1158 533 C ATOM 3276 C SER B 124 17.680 2.945 -3.355 1.00 81.77 C ANISOU 3276 C SER B 124 6105 15506 9460 368 -1298 732 C ATOM 3277 O SER B 124 18.260 1.928 -3.754 1.00 85.68 O ANISOU 3277 O SER B 124 6378 15968 10209 634 -1238 772 O ATOM 3278 CB SER B 124 18.995 4.869 -4.241 1.00 69.51 C ANISOU 3278 CB SER B 124 4341 14176 7892 -192 -1232 446 C ATOM 3279 OG SER B 124 19.373 5.247 -2.928 1.00 78.83 O ANISOU 3279 OG SER B 124 5532 15487 8933 -250 -1503 474 O ATOM 3280 N ALA B 125 17.085 3.005 -2.165 1.00 83.47 N ANISOU 3280 N ALA B 125 6528 15732 9454 387 -1474 863 N ATOM 3281 CA ALA B 125 17.036 1.874 -1.248 1.00 90.93 C ANISOU 3281 CA ALA B 125 7472 16658 10421 703 -1608 1136 C ATOM 3282 C ALA B 125 16.017 0.806 -1.659 1.00 98.64 C ANISOU 3282 C ALA B 125 8549 17375 11556 951 -1461 1284 C ATOM 3283 O ALA B 125 15.637 -0.018 -0.823 1.00 97.95 O ANISOU 3283 O ALA B 125 8546 17219 11451 1162 -1558 1571 O ATOM 3284 CB ALA B 125 16.739 2.369 0.170 1.00 88.41 C ANISOU 3284 CB ALA B 125 7356 16486 9750 601 -1813 1220 C ATOM 3285 N ALA B 126 15.587 0.787 -2.912 1.00105.49 N ANISOU 3285 N ALA B 126 9437 18060 12584 912 -1213 1096 N ATOM 3286 CA ALA B 126 14.612 -0.171 -3.406 1.00108.66 C ANISOU 3286 CA ALA B 126 10036 18069 13179 1081 -1014 1126 C ATOM 3287 C ALA B 126 15.270 -1.132 -4.395 1.00112.85 C ANISOU 3287 C ALA B 126 10286 18492 14100 1320 -873 1016 C ATOM 3288 O ALA B 126 16.466 -1.041 -4.691 1.00119.64 O ANISOU 3288 O ALA B 126 10787 19608 15063 1366 -915 932 O ATOM 3289 CB ALA B 126 13.425 0.551 -4.047 1.00104.79 C ANISOU 3289 CB ALA B 126 9868 17408 12538 839 -826 940 C ATOM 3290 N ALA B 127 14.471 -2.067 -4.906 1.00111.40 N ANISOU 3290 N ALA B 127 10247 17933 14149 1470 -698 981 N ATOM 3291 CA ALA B 127 14.949 -3.032 -5.893 1.00112.94 C ANISOU 3291 CA ALA B 127 10200 17975 14735 1708 -539 788 C ATOM 3292 C ALA B 127 13.946 -3.217 -7.030 1.00112.71 C ANISOU 3292 C ALA B 127 10364 17701 14761 1623 -275 503 C ATOM 3293 O ALA B 127 14.333 -3.418 -8.182 1.00114.87 O ANISOU 3293 O ALA B 127 10446 18033 15166 1665 -94 190 O ATOM 3294 CB ALA B 127 15.249 -4.369 -5.224 1.00116.15 C ANISOU 3294 CB ALA B 127 10492 18123 15517 2085 -653 1048 C TER 3295 ALA B 127 HETATM 3296 C9 OLC A 401 -13.491 6.683 -51.899 1.00 70.20 C HETATM 3297 C8 OLC A 401 -14.221 7.550 -52.928 1.00 74.14 C HETATM 3298 C24 OLC A 401 -15.883 8.387 -66.279 1.00 92.07 C HETATM 3299 C7 OLC A 401 -14.401 6.755 -54.222 1.00 81.59 C HETATM 3300 C6 OLC A 401 -14.932 7.673 -55.324 1.00 82.68 C HETATM 3301 C5 OLC A 401 -14.749 6.993 -56.683 1.00 78.14 C HETATM 3302 C4 OLC A 401 -15.506 7.778 -57.755 1.00 81.17 C HETATM 3303 C3 OLC A 401 -15.159 7.219 -59.137 1.00 83.76 C HETATM 3304 C2 OLC A 401 -15.994 7.933 -60.203 1.00 88.70 C HETATM 3305 C21 OLC A 401 -15.865 7.938 -63.817 1.00 90.97 C HETATM 3306 C1 OLC A 401 -15.427 7.622 -61.590 1.00 90.88 C HETATM 3307 C22 OLC A 401 -15.413 8.900 -64.918 1.00 90.92 C HETATM 3308 O19 OLC A 401 -14.769 6.603 -61.792 1.00 95.15 O HETATM 3309 O25 OLC A 401 -15.326 9.205 -67.312 1.00 92.84 O HETATM 3310 O23 OLC A 401 -15.971 10.196 -64.685 1.00 92.88 O HETATM 3311 O20 OLC A 401 -15.687 8.560 -62.540 1.00 89.24 O HETATM 3312 C10 OLC A 402 -11.364 3.376 -55.863 1.00 79.47 C HETATM 3313 C9 OLC A 402 -12.281 3.161 -57.069 1.00 77.26 C HETATM 3314 C11 OLC A 402 -11.534 4.802 -55.335 1.00 82.94 C HETATM 3315 C8 OLC A 402 -12.050 4.273 -58.093 1.00 77.85 C HETATM 3316 C24 OLC A 402 -14.881 6.157 -69.003 1.00 97.49 C HETATM 3317 C7 OLC A 402 -11.899 3.665 -59.488 1.00 80.01 C HETATM 3318 C6 OLC A 402 -10.421 3.658 -59.885 1.00 79.24 C HETATM 3319 C5 OLC A 402 -10.303 3.785 -61.405 1.00 78.90 C HETATM 3320 C4 OLC A 402 -10.907 5.118 -61.854 1.00 74.55 C HETATM 3321 C3 OLC A 402 -11.934 4.875 -62.964 1.00 73.84 C HETATM 3322 C2 OLC A 402 -11.298 5.142 -64.330 1.00 75.39 C HETATM 3323 C21 OLC A 402 -13.223 6.089 -67.129 1.00 89.81 C HETATM 3324 C1 OLC A 402 -12.328 4.868 -65.429 1.00 84.83 C HETATM 3325 C22 OLC A 402 -13.493 5.670 -68.577 1.00 96.36 C HETATM 3326 O19 OLC A 402 -13.319 4.175 -65.204 1.00 93.96 O HETATM 3327 O25 OLC A 402 -15.147 5.738 -70.344 1.00 96.56 O HETATM 3328 O23 OLC A 402 -12.501 6.235 -69.438 1.00 96.06 O HETATM 3329 O20 OLC A 402 -12.052 5.429 -66.638 1.00 85.78 O HETATM 3330 C1 CLR A 403 -13.844 13.206 -67.299 1.00 94.94 C HETATM 3331 C2 CLR A 403 -13.104 13.421 -68.608 1.00 96.67 C HETATM 3332 C3 CLR A 403 -13.557 14.749 -69.198 1.00 99.90 C HETATM 3333 C4 CLR A 403 -13.598 15.758 -68.229 1.00 95.32 C HETATM 3334 C5 CLR A 403 -13.521 15.525 -66.854 1.00 92.44 C HETATM 3335 C6 CLR A 403 -13.627 16.617 -65.992 1.00 88.57 C HETATM 3336 C7 CLR A 403 -13.544 16.463 -64.611 1.00 88.81 C HETATM 3337 C8 CLR A 403 -13.346 15.201 -64.059 1.00 86.15 C HETATM 3338 C9 CLR A 403 -13.951 14.135 -64.965 1.00 88.62 C HETATM 3339 C10 CLR A 403 -13.301 14.241 -66.335 1.00 92.02 C HETATM 3340 C11 CLR A 403 -13.704 12.756 -64.349 1.00 85.71 C HETATM 3341 C12 CLR A 403 -14.356 12.675 -62.964 1.00 85.56 C HETATM 3342 C13 CLR A 403 -13.778 13.775 -62.062 1.00 80.35 C HETATM 3343 C14 CLR A 403 -14.047 15.110 -62.717 1.00 84.60 C HETATM 3344 C15 CLR A 403 -13.481 16.077 -61.692 1.00 85.34 C HETATM 3345 C16 CLR A 403 -13.897 15.420 -60.361 1.00 84.74 C HETATM 3346 C17 CLR A 403 -14.543 14.076 -60.764 1.00 79.66 C HETATM 3347 C18 CLR A 403 -12.278 13.561 -61.808 1.00 67.07 C HETATM 3348 C19 CLR A 403 -11.792 14.000 -66.182 1.00 90.30 C HETATM 3349 C20 CLR A 403 -14.373 13.084 -59.591 1.00 75.46 C HETATM 3350 C21 CLR A 403 -15.084 11.746 -59.816 1.00 78.74 C HETATM 3351 C22 CLR A 403 -14.986 13.762 -58.361 1.00 71.12 C HETATM 3352 C23 CLR A 403 -15.052 12.818 -57.159 1.00 65.31 C HETATM 3353 C24 CLR A 403 -16.076 13.384 -56.170 1.00 64.07 C HETATM 3354 C25 CLR A 403 -15.674 13.053 -54.732 1.00 63.19 C HETATM 3355 C26 CLR A 403 -16.554 13.852 -53.768 1.00 64.54 C HETATM 3356 C27 CLR A 403 -15.868 11.557 -54.476 1.00 59.02 C HETATM 3357 O1 CLR A 403 -12.710 15.127 -70.291 1.00105.00 O HETATM 3358 P PO4 A 404 10.495 3.041 -74.343 1.00118.77 P HETATM 3359 O1 PO4 A 404 11.500 3.736 -75.231 1.00120.39 O HETATM 3360 O2 PO4 A 404 9.163 3.746 -74.444 1.00118.23 O HETATM 3361 O3 PO4 A 404 10.341 1.606 -74.787 1.00121.30 O HETATM 3362 O4 PO4 A 404 10.977 3.076 -72.913 1.00110.97 O HETATM 3363 O1 P6G A 405 4.229 0.398 -28.647 1.00 72.00 O HETATM 3364 C2 P6G A 405 3.315 -0.691 -28.487 1.00 77.23 C HETATM 3365 C3 P6G A 405 2.012 -0.381 -29.230 1.00 79.22 C HETATM 3366 O4 P6G A 405 2.172 -0.669 -30.622 1.00 78.95 O HETATM 3367 C5 P6G A 405 1.128 -0.027 -31.360 1.00 82.31 C HETATM 3368 C6 P6G A 405 1.066 -0.602 -32.778 1.00 85.92 C HETATM 3369 O7 P6G A 405 1.091 0.470 -33.723 1.00 90.20 O HETATM 3370 C8 P6G A 405 0.583 0.033 -34.988 1.00 89.25 C HETATM 3371 C9 P6G A 405 1.489 0.540 -36.115 1.00 88.95 C HETATM 3372 O10 P6G A 405 1.060 1.833 -36.562 1.00 88.89 O HETATM 3373 C11 P6G A 405 1.537 2.857 -35.682 1.00 83.25 C HETATM 3374 C12 P6G A 405 2.080 4.034 -36.496 1.00 77.87 C HETATM 3375 O13 P6G A 405 1.045 4.573 -37.324 1.00 77.68 O HETATM 3376 C14 P6G A 405 1.352 4.341 -38.703 1.00 72.44 C HETATM 3377 C15 P6G A 405 0.470 5.235 -39.579 1.00 71.24 C HETATM 3378 O16 P6G A 405 0.403 4.702 -40.905 1.00 74.96 O HETATM 3379 C17 P6G A 405 1.318 5.391 -41.761 1.00 72.71 C HETATM 3380 C18 P6G A 405 2.067 4.378 -42.628 1.00 75.76 C HETATM 3381 O19 P6G A 405 1.267 4.026 -43.759 1.00 81.56 O HETATM 3382 O7 P6G A 406 0.766 34.044 -45.949 1.00 91.05 O HETATM 3383 C8 P6G A 406 1.932 34.869 -45.986 1.00 90.55 C HETATM 3384 C9 P6G A 406 2.614 34.839 -44.619 1.00 90.82 C HETATM 3385 O10 P6G A 406 1.683 34.369 -43.643 1.00 90.39 O HETATM 3386 C11 P6G A 406 2.394 33.887 -42.501 1.00 91.31 C HETATM 3387 C12 P6G A 406 1.590 34.208 -41.241 1.00 92.95 C HETATM 3388 O13 P6G A 406 2.123 33.485 -40.129 1.00 92.65 O HETATM 3389 C14 P6G A 406 2.010 34.303 -38.963 1.00 88.21 C HETATM 3390 C15 P6G A 406 2.178 33.442 -37.712 1.00 83.81 C HETATM 3391 O16 P6G A 406 2.057 34.268 -36.551 1.00 85.01 O HETATM 3392 C17 P6G A 406 3.222 35.086 -36.416 1.00 84.52 C HETATM 3393 C18 P6G A 406 3.082 35.965 -35.172 1.00 88.36 C HETATM 3394 O19 P6G A 406 4.305 36.670 -34.944 1.00 89.28 O HETATM 3395 CAP VF1 A 407 2.290 15.541 -57.816 1.00 33.88 C HETATM 3396 CAO VF1 A 407 1.904 15.578 -56.324 1.00 38.06 C HETATM 3397 NBB VF1 A 407 1.066 16.759 -56.069 1.00 37.28 N HETATM 3398 CAB VF1 A 407 0.683 16.848 -54.649 1.00 40.63 C HETATM 3399 CAZ VF1 A 407 -0.146 16.749 -56.925 1.00 34.18 C HETATM 3400 CAQ VF1 A 407 -1.053 15.501 -56.684 1.00 41.38 C HETATM 3401 CAW VF1 A 407 -0.738 14.375 -57.485 1.00 40.00 C HETATM 3402 CAM VF1 A 407 -1.477 13.210 -57.306 1.00 39.15 C HETATM 3403 CAL VF1 A 407 -1.210 12.087 -58.083 1.00 44.90 C HETATM 3404 CAU VF1 A 407 -0.216 12.125 -59.050 1.00 45.21 C HETATM 3405 OAD VF1 A 407 0.041 11.022 -59.809 1.00 37.71 O HETATM 3406 CAN VF1 A 407 0.515 13.291 -59.237 1.00 40.78 C HETATM 3407 CAX VF1 A 407 0.259 14.428 -58.476 1.00 34.42 C HETATM 3408 CBF VF1 A 407 1.037 15.590 -58.711 1.00 35.95 C HETATM 3409 CBA VF1 A 407 1.517 15.721 -60.173 1.00 34.27 C HETATM 3410 NAS VF1 A 407 2.861 16.363 -60.197 1.00 39.60 N HETATM 3411 CBE VF1 A 407 0.679 16.781 -60.933 1.00 38.05 C HETATM 3412 OAT VF1 A 407 0.975 16.736 -62.355 1.00 41.66 O HETATM 3413 CAA VF1 A 407 0.531 15.496 -62.920 1.00 43.50 C HETATM 3414 CAF VF1 A 407 -0.812 16.656 -60.704 1.00 36.03 C HETATM 3415 CAE VF1 A 407 -1.091 16.847 -59.236 1.00 30.51 C HETATM 3416 CBD VF1 A 407 0.210 16.816 -58.401 1.00 31.67 C HETATM 3417 CAR VF1 A 407 1.011 18.058 -58.770 1.00 35.44 C HETATM 3418 CBC VF1 A 407 1.247 18.048 -60.316 1.00 41.07 C HETATM 3419 CAC VF1 A 407 0.692 19.318 -60.986 1.00 39.42 C HETATM 3420 CAY VF1 A 407 2.678 17.731 -60.738 1.00 37.19 C HETATM 3421 CAV VF1 A 407 3.695 18.801 -60.279 1.00 39.36 C HETATM 3422 CAJ VF1 A 407 4.035 19.841 -61.140 1.00 42.51 C HETATM 3423 CAH VF1 A 407 4.944 20.817 -60.748 1.00 45.93 C HETATM 3424 CAG VF1 A 407 5.528 20.751 -59.488 1.00 48.22 C HETATM 3425 CAI VF1 A 407 5.198 19.710 -58.626 1.00 43.93 C HETATM 3426 CAK VF1 A 407 4.288 18.737 -59.022 1.00 38.96 C HETATM 3427 O HOH A 501 0.405 9.081 -29.776 1.00 50.63 O HETATM 3428 O HOH A 502 -4.411 11.333 -51.637 1.00 44.89 O HETATM 3429 O HOH A 503 16.817 25.779 -61.432 1.00 52.05 O HETATM 3430 O HOH A 504 13.065 26.124 -67.125 1.00 52.99 O HETATM 3431 O HOH A 505 -9.684 -4.080 -29.283 1.00 74.52 O HETATM 3432 O HOH A 506 0.797 24.762 -63.273 1.00 41.60 O HETATM 3433 O HOH A 507 -2.857 24.565 -67.962 1.00 71.85 O HETATM 3434 O HOH A 508 3.038 10.542 -60.042 1.00 38.12 O HETATM 3435 O HOH A 509 -2.237 18.588 -49.508 1.00 47.84 O HETATM 3436 O HOH A 510 3.517 20.319 -25.563 1.00 50.86 O HETATM 3437 O HOH A 511 -10.756 2.506 -24.142 1.00 35.92 O HETATM 3438 O HOH A 512 -1.797 21.061 -41.087 1.00 47.34 O HETATM 3439 O HOH A 513 8.146 5.590 -25.615 1.00 45.31 O HETATM 3440 O HOH A 514 -7.716 16.050 -44.390 1.00 44.06 O HETATM 3441 O HOH A 515 -9.891 -3.313 -32.378 1.00 58.21 O HETATM 3442 O HOH A 516 -8.672 14.283 -42.817 1.00 39.82 O HETATM 3443 O HOH A 517 18.812 16.638 -65.169 1.00 66.51 O HETATM 3444 O HOH A 518 0.682 7.179 -67.918 1.00 53.16 O HETATM 3445 O HOH A 519 -2.208 10.645 -65.997 1.00 38.81 O HETATM 3446 O HOH A 520 -0.473 14.752 -66.579 1.00 66.27 O HETATM 3447 O HOH A 521 -0.321 22.903 -61.550 1.00 37.38 O HETATM 3448 O HOH A 522 2.481 8.161 -30.630 1.00 59.18 O HETATM 3449 O HOH A 523 16.180 12.390 -65.113 1.00 55.67 O HETATM 3450 O HOH A 524 4.326 11.214 -39.431 1.00 39.33 O HETATM 3451 O HOH A 525 -1.324 8.778 -59.410 1.00 34.08 O HETATM 3452 O HOH A 526 5.469 23.232 -67.975 1.00 62.32 O HETATM 3453 O HOH A 527 -8.537 16.817 -55.951 1.00 38.35 O HETATM 3454 O HOH A 528 -5.384 16.537 -27.689 1.00 59.97 O HETATM 3455 O HOH A 529 -1.011 17.810 -26.126 1.00 43.51 O HETATM 3456 O HOH A 530 -7.123 11.424 -39.368 1.00 36.16 O HETATM 3457 O HOH A 531 -14.157 -1.639 -31.972 1.00 47.22 O HETATM 3458 O HOH A 532 -2.837 16.438 -47.545 1.00 38.72 O HETATM 3459 O HOH A 533 2.711 18.446 -51.879 1.00 41.42 O HETATM 3460 O HOH A 534 8.335 17.202 -37.435 1.00 55.52 O HETATM 3461 O HOH A 535 7.152 12.266 -41.279 1.00 33.98 O HETATM 3462 O HOH A 536 6.820 3.530 -24.616 1.00 70.91 O HETATM 3463 O HOH A 537 -29.865 10.457 -26.241 1.00 73.00 O HETATM 3464 O HOH A 538 -3.466 11.956 -32.583 1.00 61.69 O HETATM 3465 O HOH A 539 -12.042 -0.071 -24.492 1.00 62.18 O HETATM 3466 O HOH A 540 7.169 17.291 -34.838 1.00 50.54 O HETATM 3467 O HOH A 541 -4.574 26.805 -43.618 1.00 44.21 O HETATM 3468 O HOH A 542 -4.348 7.272 -24.196 1.00 41.05 O HETATM 3469 O HOH A 543 2.665 24.847 -68.381 1.00 74.66 O HETATM 3470 O HOH A 544 -1.011 11.194 -29.226 1.00 54.30 O HETATM 3471 O HOH A 545 8.496 -0.726 -75.636 1.00 68.36 O HETATM 3472 O HOH A 546 -3.778 8.928 -58.784 1.00 37.31 O HETATM 3473 O HOH A 547 9.965 4.472 -27.490 1.00 55.38 O HETATM 3474 O HOH A 548 -3.250 18.196 -55.959 1.00 38.74 O HETATM 3475 O HOH A 549 0.866 11.845 -62.417 1.00 42.65 O HETATM 3476 O HOH A 550 10.622 8.724 -69.575 1.00 48.18 O HETATM 3477 O HOH A 551 12.420 9.438 -30.419 1.00 56.08 O HETATM 3478 O HOH A 552 7.341 1.693 -27.184 1.00 65.59 O HETATM 3479 O HOH A 553 2.319 12.288 -25.083 1.00 39.95 O HETATM 3480 O HOH A 554 0.172 23.669 -65.537 1.00 60.94 O HETATM 3481 O HOH A 555 -0.237 13.567 -26.349 1.00 44.33 O HETATM 3482 O HOH A 556 -1.451 20.561 -38.152 1.00 45.13 O HETATM 3483 O HOH A 557 8.798 9.874 -24.293 1.00 46.60 O HETATM 3484 O HOH A 558 -0.614 21.334 -63.943 1.00 48.59 O HETATM 3485 O HOH A 559 -1.856 18.622 -53.223 1.00 50.88 O HETATM 3486 O HOH A 560 -1.530 11.535 -26.687 1.00 46.30 O HETATM 3487 O HOH A 561 -12.188 -3.206 -32.114 1.00 66.78 O HETATM 3488 O HOH A 562 -0.759 12.751 -64.757 1.00 50.45 O HETATM 3489 O HOH A 563 3.155 10.788 -62.591 1.00 47.27 O HETATM 3490 O HOH A 564 16.527 -0.391 -67.632 1.00 74.23 O HETATM 3491 O HOH A 565 0.173 17.626 -51.392 1.00 41.33 O HETATM 3492 O HOH A 566 9.480 7.295 -23.797 1.00 48.45 O HETATM 3493 O HOH A 567 9.665 16.474 -33.206 1.00 61.36 O HETATM 3494 O HOH B 201 -21.962 3.957 0.325 1.00 54.10 O HETATM 3495 O HOH B 202 7.504 16.149 -11.685 1.00 65.85 O HETATM 3496 O HOH B 203 -7.501 -0.384 -8.961 1.00 60.33 O HETATM 3497 O HOH B 204 3.219 12.348 -22.449 1.00 44.62 O HETATM 3498 O HOH B 205 -0.517 10.459 -24.420 1.00 43.48 O HETATM 3499 O HOH B 206 2.972 -0.333 -10.761 1.00 61.23 O HETATM 3500 O HOH B 207 -8.808 15.965 -19.423 1.00 55.70 O HETATM 3501 O HOH B 208 8.626 14.699 -3.943 1.00 52.89 O HETATM 3502 O HOH B 209 2.594 18.099 -4.452 1.00 58.41 O HETATM 3503 O HOH B 210 -6.907 6.164 -23.751 1.00 34.47 O HETATM 3504 O HOH B 211 -8.042 16.019 -21.757 1.00 53.66 O HETATM 3505 O HOH B 212 -14.737 13.924 -21.127 1.00 51.25 O HETATM 3506 O HOH B 213 12.175 10.624 -3.194 1.00 58.16 O HETATM 3507 O HOH B 214 -9.103 4.957 -2.531 1.00 50.81 O HETATM 3508 O HOH B 215 -9.558 -2.748 -14.140 1.00 61.04 O HETATM 3509 O HOH B 216 11.565 4.357 -16.726 1.00 54.28 O HETATM 3510 O HOH B 217 -0.042 20.785 -12.440 1.00 61.68 O HETATM 3511 O HOH B 218 -0.972 17.793 -22.263 1.00 59.05 O HETATM 3512 O HOH B 219 7.935 16.824 -18.677 1.00 60.96 O HETATM 3513 O HOH B 220 5.214 4.404 -21.631 1.00 50.21 O HETATM 3514 O HOH B 221 -1.595 21.979 -10.416 1.00 61.17 O HETATM 3515 O HOH B 222 3.673 21.290 -14.577 1.00 52.04 O HETATM 3516 O HOH B 223 -1.127 -2.424 -5.952 1.00 64.59 O HETATM 3517 O HOH B 224 -1.450 15.702 -25.035 1.00 53.09 O HETATM 3518 O HOH B 225 7.229 8.598 -21.714 1.00 65.42 O HETATM 3519 O HOH B 226 -2.013 2.173 -1.118 1.00 83.06 O HETATM 3520 O HOH B 227 8.446 17.159 -4.087 1.00 69.27 O CONECT 29 35 CONECT 35 29 36 CONECT 36 35 37 43 CONECT 37 36 38 CONECT 38 37 39 CONECT 39 38 40 CONECT 40 39 41 42 CONECT 41 40 CONECT 42 40 CONECT 43 36 44 45 CONECT 44 43 CONECT 45 43 CONECT 680 1290 CONECT 1290 680 CONECT 2528 3119 CONECT 3119 2528 CONECT 3296 3297 CONECT 3297 3296 3299 CONECT 3298 3307 3309 CONECT 3299 3297 3300 CONECT 3300 3299 3301 CONECT 3301 3300 3302 CONECT 3302 3301 3303 CONECT 3303 3302 3304 CONECT 3304 3303 3306 CONECT 3305 3307 3311 CONECT 3306 3304 3308 3311 CONECT 3307 3298 3305 3310 CONECT 3308 3306 CONECT 3309 3298 CONECT 3310 3307 CONECT 3311 3305 3306 CONECT 3312 3313 3314 CONECT 3313 3312 3315 CONECT 3314 3312 CONECT 3315 3313 3317 CONECT 3316 3325 3327 CONECT 3317 3315 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 3322 CONECT 3322 3321 3324 CONECT 3323 3325 3329 CONECT 3324 3322 3326 3329 CONECT 3325 3316 3323 3328 CONECT 3326 3324 CONECT 3327 3316 CONECT 3328 3325 CONECT 3329 3323 3324 CONECT 3330 3331 3339 CONECT 3331 3330 3332 CONECT 3332 3331 3333 3357 CONECT 3333 3332 3334 CONECT 3334 3333 3335 3339 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 3343 CONECT 3338 3337 3339 3340 CONECT 3339 3330 3334 3338 3348 CONECT 3340 3338 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 3346 3347 CONECT 3343 3337 3342 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3342 3345 3349 CONECT 3347 3342 CONECT 3348 3339 CONECT 3349 3346 3350 3351 CONECT 3350 3349 CONECT 3351 3349 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 3355 3356 CONECT 3355 3354 CONECT 3356 3354 CONECT 3357 3332 CONECT 3358 3359 3360 3361 3362 CONECT 3359 3358 CONECT 3360 3358 CONECT 3361 3358 CONECT 3362 3358 CONECT 3363 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 CONECT 3382 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 CONECT 3395 3396 3408 CONECT 3396 3395 3397 CONECT 3397 3396 3398 3399 CONECT 3398 3397 CONECT 3399 3397 3400 3416 CONECT 3400 3399 3401 CONECT 3401 3400 3402 3407 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 3406 CONECT 3405 3404 CONECT 3406 3404 3407 CONECT 3407 3401 3406 3408 CONECT 3408 3395 3407 3409 3416 CONECT 3409 3408 3410 3411 CONECT 3410 3409 3420 CONECT 3411 3409 3412 3414 3418 CONECT 3412 3411 3413 CONECT 3413 3412 CONECT 3414 3411 3415 CONECT 3415 3414 3416 CONECT 3416 3399 3408 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3411 3417 3419 3420 CONECT 3419 3418 CONECT 3420 3410 3418 3421 CONECT 3421 3420 3422 3426 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3421 3425 MASTER 528 0 8 12 16 0 0 6 3484 2 147 33 END