HEADER MEMBRANE PROTEIN 15-JUN-18 6GT3 TITLE CRYSTAL STRUCTURE OF THE A2A-STAR2-BRIL562 IN COMPLEX WITH AZD4635 AT TITLE 2 2.0A RESOLUTION CAVEAT 6GT3 OLC A 2420 HAS WRONG CHIRALITY AT ATOM C22 OLC A 2421 HAS CAVEAT 2 6GT3 WRONG CHIRALITY AT ATOM C22 OLC A 2422 HAS WRONG CHIRALITY CAVEAT 3 6GT3 AT ATOM C22 OLC A 2423 HAS WRONG CHIRALITY AT ATOM C22 OLC CAVEAT 4 6GT3 A 2424 HAS WRONG CHIRALITY AT ATOM C22 OLC A 2425 HAS WRONG CAVEAT 5 6GT3 CHIRALITY AT ATOM C22 OLC A 2426 HAS WRONG CHIRALITY AT CAVEAT 6 6GT3 ATOM C22 OLC A 2427 HAS WRONG CHIRALITY AT ATOM C22 OLC A CAVEAT 7 6GT3 2428 HAS WRONG CHIRALITY AT ATOM C22 OLC A 2429 HAS WRONG CAVEAT 8 6GT3 CHIRALITY AT ATOM C22 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS 7TM, GPCR, SIGNALLING PROTEIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.BORODOVSKY,Y.WANG,N.DENG,M.YE,T.L.STEPHEN,K.GOODWIN,R.GOODWIN, AUTHOR 2 N.STRITTMATTER,J.SHAW,K.SACHSENMEIER,J.D.CLARKE,C.HAY,C.REIMER, AUTHOR 3 S.P.ANDREWS,G.A.BROWN,M.CONGREVE,R.K.Y.CHENG,A.S.DORE,J.S.MASON, AUTHOR 4 F.H.MARSHALL,M.P.WEIR,P.LYNE,R.WOESSNER REVDAT 2 08-JUL-20 6GT3 1 JRNL REVDAT 1 26-JUN-19 6GT3 0 JRNL AUTH A.BORODOVSKY,C.M.BARBON,Y.WANG,M.YE,L.PRICKETT,D.CHANDRA, JRNL AUTH 2 J.SHAW,N.DENG,K.SACHSENMEIER,J.D.CLARKE,B.LINGHU,G.A.BROWN, JRNL AUTH 3 J.BROWN,M.CONGREVE,R.K.Y.CHENG,A.S.DORE,E.HURRELL,W.SHAO, JRNL AUTH 4 R.WOESSNER,C.REIMER,L.DREW,S.FAWELL,A.G.SCHULLER,D.A.MELE JRNL TITL SMALL MOLECULE AZD4635 INHIBITOR OF A2AR SIGNALING RESCUES JRNL TITL 2 IMMUNE CELL FUNCTION INCLUDING CD103+ DENDRITIC CELLS JRNL TITL 3 ENHANCING ANTI-TUMOR IMMUNITY JRNL REF J IMMUNOTHER CANCER 2020 JRNL REFN ESSN 2051-1426 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.80 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 33848 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 1710 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 33.8672 - 4.5755 0.98 2903 127 0.1920 0.1800 REMARK 3 2 4.5755 - 3.6331 0.99 2759 137 0.1595 0.1984 REMARK 3 3 3.6331 - 3.1742 0.99 2722 136 0.1697 0.1651 REMARK 3 4 3.1742 - 2.8842 0.98 2721 134 0.1763 0.1937 REMARK 3 5 2.8842 - 2.6775 0.97 2624 169 0.1697 0.1806 REMARK 3 6 2.6775 - 2.5197 0.98 2668 128 0.1725 0.2081 REMARK 3 7 2.5197 - 2.3936 0.98 2647 157 0.1786 0.2358 REMARK 3 8 2.3936 - 2.2894 0.98 2648 136 0.1877 0.2541 REMARK 3 9 2.2894 - 2.2013 0.98 2607 148 0.1973 0.2078 REMARK 3 10 2.2013 - 2.1253 0.97 2661 137 0.2098 0.2136 REMARK 3 11 2.1253 - 2.0589 0.97 2610 149 0.2296 0.2352 REMARK 3 12 2.0589 - 2.0001 0.97 2568 152 0.2571 0.2958 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.760 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 3756 REMARK 3 ANGLE : 0.980 5023 REMARK 3 CHIRALITY : 0.022 555 REMARK 3 PLANARITY : 0.003 617 REMARK 3 DIHEDRAL : 10.153 1195 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' (RESID -1 THROUGH 34) REMARK 3 ORIGIN FOR THE GROUP (A): -30.9004 -4.1925 7.0880 REMARK 3 T TENSOR REMARK 3 T11: 0.1877 T22: 0.2943 REMARK 3 T33: 0.1014 T12: -0.0008 REMARK 3 T13: -0.0234 T23: 0.0032 REMARK 3 L TENSOR REMARK 3 L11: 1.7118 L22: 6.6432 REMARK 3 L33: 4.5414 L12: -0.0964 REMARK 3 L13: 0.7578 L23: -1.7531 REMARK 3 S TENSOR REMARK 3 S11: -0.0266 S12: 0.0705 S13: 0.0629 REMARK 3 S21: -0.3828 S22: 0.1913 S23: 0.6355 REMARK 3 S31: -0.2201 S32: -0.4078 S33: -0.1035 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' (RESID 35 THROUGH 38) REMARK 3 ORIGIN FOR THE GROUP (A): -30.7382 -29.8243 15.4850 REMARK 3 T TENSOR REMARK 3 T11: 0.6344 T22: 0.3170 REMARK 3 T33: 0.4063 T12: -0.1569 REMARK 3 T13: -0.1172 T23: 0.0913 REMARK 3 L TENSOR REMARK 3 L11: 7.7836 L22: 7.4861 REMARK 3 L33: 1.3492 L12: 6.7218 REMARK 3 L13: 2.8299 L23: 3.1634 REMARK 3 S TENSOR REMARK 3 S11: 0.9466 S12: -0.3452 S13: -1.0817 REMARK 3 S21: -0.6235 S22: 0.0932 S23: 0.8374 REMARK 3 S31: 1.2919 S32: -0.8739 S33: -0.8659 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' (RESID 39 THROUGH 73) REMARK 3 ORIGIN FOR THE GROUP (A): -29.8647 -4.0663 17.2462 REMARK 3 T TENSOR REMARK 3 T11: 0.1065 T22: 0.2449 REMARK 3 T33: 0.0861 T12: -0.0232 REMARK 3 T13: 0.0182 T23: 0.0003 REMARK 3 L TENSOR REMARK 3 L11: 1.2984 L22: 6.9527 REMARK 3 L33: 1.6567 L12: -0.9752 REMARK 3 L13: 0.8719 L23: -0.7383 REMARK 3 S TENSOR REMARK 3 S11: 0.0424 S12: -0.0751 S13: 0.0060 REMARK 3 S21: -0.2762 S22: -0.0164 S23: 0.2325 REMARK 3 S31: 0.0390 S32: -0.2251 S33: -0.0486 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' (RESID 74 THROUGH 108) REMARK 3 ORIGIN FOR THE GROUP (A): -22.4798 -8.9565 24.1185 REMARK 3 T TENSOR REMARK 3 T11: 0.1158 T22: 0.2530 REMARK 3 T33: 0.0769 T12: -0.0097 REMARK 3 T13: -0.0141 T23: 0.0133 REMARK 3 L TENSOR REMARK 3 L11: 2.8504 L22: 5.8178 REMARK 3 L33: 1.1133 L12: -2.7524 REMARK 3 L13: 0.0456 L23: 0.6006 REMARK 3 S TENSOR REMARK 3 S11: -0.1901 S12: -0.2192 S13: 0.0091 REMARK 3 S21: 0.1461 S22: 0.2526 S23: -0.0324 REMARK 3 S31: 0.1816 S32: -0.1791 S33: -0.0359 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' (RESID 109 THROUGH 117) REMARK 3 ORIGIN FOR THE GROUP (A): -19.5518 -31.9645 28.9462 REMARK 3 T TENSOR REMARK 3 T11: 0.7758 T22: 0.4183 REMARK 3 T33: 0.5308 T12: -0.0230 REMARK 3 T13: 0.0658 T23: 0.0990 REMARK 3 L TENSOR REMARK 3 L11: 6.6191 L22: 5.1793 REMARK 3 L33: 4.5402 L12: -1.8065 REMARK 3 L13: -4.7582 L23: 3.6168 REMARK 3 S TENSOR REMARK 3 S11: -0.5431 S12: -1.5956 S13: -1.4148 REMARK 3 S21: 0.6034 S22: 0.4147 S23: 0.7763 REMARK 3 S31: 1.3810 S32: 0.4077 S33: 0.1078 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' (RESID 118 THROUGH 137) REMARK 3 ORIGIN FOR THE GROUP (A): -27.2533 -11.9515 29.9332 REMARK 3 T TENSOR REMARK 3 T11: 0.2101 T22: 0.2810 REMARK 3 T33: 0.1088 T12: -0.0203 REMARK 3 T13: 0.0125 T23: 0.0441 REMARK 3 L TENSOR REMARK 3 L11: 2.5426 L22: 7.0781 REMARK 3 L33: 1.6101 L12: 1.3515 REMARK 3 L13: -0.0349 L23: -0.2759 REMARK 3 S TENSOR REMARK 3 S11: 0.1146 S12: -0.3013 S13: -0.1909 REMARK 3 S21: 0.4106 S22: -0.2847 S23: 0.0931 REMARK 3 S31: 0.4081 S32: -0.1394 S33: 0.1743 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' (RESID 138 THROUGH 161) REMARK 3 ORIGIN FOR THE GROUP (A): -27.5490 16.6921 27.6966 REMARK 3 T TENSOR REMARK 3 T11: 0.2366 T22: 0.2531 REMARK 3 T33: 0.2645 T12: 0.0665 REMARK 3 T13: -0.0341 T23: -0.0377 REMARK 3 L TENSOR REMARK 3 L11: 4.8754 L22: 6.8784 REMARK 3 L33: 4.7192 L12: -2.2458 REMARK 3 L13: 2.4604 L23: -3.8278 REMARK 3 S TENSOR REMARK 3 S11: -0.0895 S12: -0.0109 S13: 0.6932 REMARK 3 S21: 0.3108 S22: -0.0962 S23: 0.3700 REMARK 3 S31: -0.7299 S32: -0.0915 S33: 0.1384 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' (RESID 162 THROUGH 186) REMARK 3 ORIGIN FOR THE GROUP (A): -19.3002 7.8343 25.3217 REMARK 3 T TENSOR REMARK 3 T11: 0.1168 T22: 0.2031 REMARK 3 T33: 0.1098 T12: 0.0103 REMARK 3 T13: -0.0013 T23: 0.0007 REMARK 3 L TENSOR REMARK 3 L11: 5.3262 L22: 5.1036 REMARK 3 L33: 1.9390 L12: -2.9587 REMARK 3 L13: 0.5545 L23: -0.4535 REMARK 3 S TENSOR REMARK 3 S11: 0.0811 S12: 0.0739 S13: 0.2348 REMARK 3 S21: -0.1469 S22: -0.0947 S23: 0.0516 REMARK 3 S31: -0.1686 S32: -0.0765 S33: 0.0012 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' (RESID 187 THROUGH 208) REMARK 3 ORIGIN FOR THE GROUP (A): -7.5081 -19.4753 22.2137 REMARK 3 T TENSOR REMARK 3 T11: 0.1916 T22: 0.2121 REMARK 3 T33: 0.2609 T12: 0.0616 REMARK 3 T13: -0.0195 T23: 0.0167 REMARK 3 L TENSOR REMARK 3 L11: 3.4384 L22: 1.6611 REMARK 3 L33: 2.4886 L12: -1.8797 REMARK 3 L13: -0.8041 L23: 1.6183 REMARK 3 S TENSOR REMARK 3 S11: -0.1221 S12: -0.0969 S13: -0.2940 REMARK 3 S21: 0.4419 S22: 0.2715 S23: -0.4590 REMARK 3 S31: 0.4538 S32: 0.3570 S33: -0.1115 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' (RESID 219 THROUGH 259) REMARK 3 ORIGIN FOR THE GROUP (A): -12.4221 -12.6722 15.1850 REMARK 3 T TENSOR REMARK 3 T11: 0.1298 T22: 0.1955 REMARK 3 T33: 0.1747 T12: 0.0615 REMARK 3 T13: 0.0378 T23: 0.0194 REMARK 3 L TENSOR REMARK 3 L11: 0.9460 L22: 5.1257 REMARK 3 L33: 1.8234 L12: 0.5449 REMARK 3 L13: 0.7199 L23: 0.0247 REMARK 3 S TENSOR REMARK 3 S11: 0.0472 S12: 0.0200 S13: -0.2417 REMARK 3 S21: -0.4900 S22: 0.0918 S23: -0.2824 REMARK 3 S31: 0.3137 S32: 0.2016 S33: -0.0738 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' (RESID 260 THROUGH 265) REMARK 3 ORIGIN FOR THE GROUP (A): -8.6587 16.5849 16.4736 REMARK 3 T TENSOR REMARK 3 T11: 0.3652 T22: 0.3904 REMARK 3 T33: 0.3968 T12: -0.0497 REMARK 3 T13: -0.0341 T23: 0.0711 REMARK 3 L TENSOR REMARK 3 L11: 5.5637 L22: 3.5494 REMARK 3 L33: 5.4642 L12: 4.3200 REMARK 3 L13: 5.4494 L23: 4.3371 REMARK 3 S TENSOR REMARK 3 S11: -0.7028 S12: 1.1610 S13: 0.3352 REMARK 3 S21: 0.3040 S22: 0.4845 S23: -0.7663 REMARK 3 S31: -0.4013 S32: 1.4927 S33: 0.2179 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' (RESID 266 THROUGH 292) REMARK 3 ORIGIN FOR THE GROUP (A): -20.5739 -4.8065 8.3846 REMARK 3 T TENSOR REMARK 3 T11: 0.1939 T22: 0.2742 REMARK 3 T33: 0.1210 T12: 0.0164 REMARK 3 T13: 0.0076 T23: -0.0120 REMARK 3 L TENSOR REMARK 3 L11: 2.4544 L22: 5.9590 REMARK 3 L33: 3.2349 L12: 2.3591 REMARK 3 L13: 0.4024 L23: 0.3184 REMARK 3 S TENSOR REMARK 3 S11: -0.2282 S12: 0.3362 S13: -0.1174 REMARK 3 S21: -0.5386 S22: 0.2740 S23: 0.2560 REMARK 3 S31: 0.2287 S32: -0.0033 S33: -0.0508 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' (RESID 293 THROUGH 307) REMARK 3 ORIGIN FOR THE GROUP (A): -27.2934 -5.7612 15.7654 REMARK 3 T TENSOR REMARK 3 T11: 0.1847 T22: 0.4048 REMARK 3 T33: 0.1327 T12: -0.0088 REMARK 3 T13: 0.0711 T23: -0.0057 REMARK 3 L TENSOR REMARK 3 L11: 2.1609 L22: 1.9273 REMARK 3 L33: 2.6070 L12: 0.8369 REMARK 3 L13: 0.6263 L23: -0.5033 REMARK 3 S TENSOR REMARK 3 S11: -0.0793 S12: -0.1219 S13: -0.0502 REMARK 3 S21: -0.0968 S22: 0.1196 S23: 0.0890 REMARK 3 S31: 0.2403 S32: -0.2125 S33: -0.0423 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' (RESID 1001 THROUGH 1021) REMARK 3 ORIGIN FOR THE GROUP (A): 5.6833 -48.9293 16.8370 REMARK 3 T TENSOR REMARK 3 T11: 0.3676 T22: 0.3536 REMARK 3 T33: 1.5058 T12: 0.2619 REMARK 3 T13: 0.3315 T23: 0.0369 REMARK 3 L TENSOR REMARK 3 L11: 5.4012 L22: 6.9447 REMARK 3 L33: 4.0326 L12: -5.3394 REMARK 3 L13: -1.6716 L23: 2.1817 REMARK 3 S TENSOR REMARK 3 S11: -0.3514 S12: -0.0940 S13: 0.1323 REMARK 3 S21: -0.6121 S22: -0.3679 S23: -1.1952 REMARK 3 S31: -0.2688 S32: 0.4677 S33: -0.0811 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' (RESID 1022 THROUGH 1042) REMARK 3 ORIGIN FOR THE GROUP (A): 4.0083 -52.7958 25.6960 REMARK 3 T TENSOR REMARK 3 T11: 0.3824 T22: 0.4237 REMARK 3 T33: 1.1044 T12: 0.0447 REMARK 3 T13: -0.1583 T23: -0.2097 REMARK 3 L TENSOR REMARK 3 L11: 2.7399 L22: 5.3077 REMARK 3 L33: 8.9639 L12: -2.4786 REMARK 3 L13: -3.0896 L23: -1.2584 REMARK 3 S TENSOR REMARK 3 S11: -0.4866 S12: -0.8822 S13: 1.5492 REMARK 3 S21: 0.2883 S22: -0.3714 S23: -0.5057 REMARK 3 S31: -0.5940 S32: 0.2312 S33: 0.5715 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' (RESID 1058 THROUGH 1081) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0653 -57.8514 23.6785 REMARK 3 T TENSOR REMARK 3 T11: 0.4464 T22: 0.4604 REMARK 3 T33: 0.8098 T12: 0.0093 REMARK 3 T13: -0.0091 T23: 0.1729 REMARK 3 L TENSOR REMARK 3 L11: 8.4759 L22: 4.4093 REMARK 3 L33: 8.1387 L12: -0.9313 REMARK 3 L13: 3.1301 L23: 1.9010 REMARK 3 S TENSOR REMARK 3 S11: 0.1730 S12: -1.5334 S13: -0.3003 REMARK 3 S21: 0.4165 S22: 0.8047 S23: 1.1878 REMARK 3 S31: 0.0657 S32: -1.1393 S33: -0.8655 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' (RESID 1082 THROUGH 1093) REMARK 3 ORIGIN FOR THE GROUP (A): 6.2813 -65.1731 18.6414 REMARK 3 T TENSOR REMARK 3 T11: 0.6383 T22: 0.3681 REMARK 3 T33: 0.8367 T12: 0.1560 REMARK 3 T13: 0.0877 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 4.5933 L22: 4.4722 REMARK 3 L33: 7.7296 L12: -4.1591 REMARK 3 L13: 1.2143 L23: -1.4135 REMARK 3 S TENSOR REMARK 3 S11: -0.1063 S12: 0.3977 S13: -0.0870 REMARK 3 S21: -1.0129 S22: -0.7318 S23: -0.5621 REMARK 3 S31: 0.7176 S32: 0.3258 S33: 0.8641 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'A' (RESID 1094 THROUGH 1101) REMARK 3 ORIGIN FOR THE GROUP (A): -4.3936 -55.2460 12.7724 REMARK 3 T TENSOR REMARK 3 T11: 0.8099 T22: 0.3818 REMARK 3 T33: 0.7501 T12: 0.1775 REMARK 3 T13: -0.0003 T23: 0.0839 REMARK 3 L TENSOR REMARK 3 L11: 6.7264 L22: 4.2712 REMARK 3 L33: 9.4283 L12: 5.1348 REMARK 3 L13: -0.7475 L23: -0.6153 REMARK 3 S TENSOR REMARK 3 S11: 0.6904 S12: 1.2585 S13: -0.4179 REMARK 3 S21: -1.5450 S22: -0.1121 S23: 0.7745 REMARK 3 S31: 0.5023 S32: 0.0429 S33: -0.5090 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'A' (RESID 1102 THROUGH 1106) REMARK 3 ORIGIN FOR THE GROUP (A): -7.7786 -46.8052 13.6810 REMARK 3 T TENSOR REMARK 3 T11: 0.9310 T22: 0.4656 REMARK 3 T33: 0.6702 T12: 0.3153 REMARK 3 T13: 0.0063 T23: -0.1093 REMARK 3 L TENSOR REMARK 3 L11: 6.7424 L22: 6.5864 REMARK 3 L33: 5.9133 L12: -3.8412 REMARK 3 L13: 5.0868 L23: -5.9183 REMARK 3 S TENSOR REMARK 3 S11: -0.6877 S12: -0.9834 S13: -0.5552 REMARK 3 S21: -0.4378 S22: 0.1026 S23: -0.5069 REMARK 3 S31: -0.9333 S32: -0.7869 S33: 0.4831 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 6GT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-18. REMARK 100 THE DEPOSITION ID IS D_1200010512. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-JUN-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.3-5.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS V1.0 REMARK 200 DATA SCALING SOFTWARE : AIMLESS V1.0 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33848 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 33.860 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 3.100 REMARK 200 R MERGE (I) : 0.11100 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.99400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.350 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER V1.0 REMARK 200 STARTING MODEL: 5IU4 REMARK 200 REMARK 200 REMARK: 0.060-0.080 MM LONG PLATE-SHAPED CRYSTALS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRI-SODIUM CITRATE PH 5.3-5.4, REMARK 280 0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2%(V/V) 2,5-HEXANEDIOL, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.38800 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.38800 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.77500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.85700 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.77500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.85700 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.38800 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.77500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.85700 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.38800 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.77500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.85700 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O MET A 1033 O HOH A 2501 2.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A1101 -60.60 -124.40 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 OLA A 2406 REMARK 610 OLA A 2407 REMARK 610 OLA A 2408 REMARK 610 OLA A 2409 REMARK 610 OLA A 2410 REMARK 610 OLA A 2412 REMARK 610 OLA A 2413 REMARK 610 OLA A 2414 REMARK 610 OLA A 2415 REMARK 610 OLA A 2416 REMARK 610 OLA A 2417 REMARK 610 OLA A 2418 REMARK 610 OLA A 2419 REMARK 610 OLC A 2420 REMARK 610 OLC A 2421 REMARK 610 OLC A 2422 REMARK 610 OLC A 2423 REMARK 610 OLC A 2424 REMARK 610 OLC A 2425 REMARK 610 OLC A 2428 REMARK 610 OLC A 2429 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A2400 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 127.7 REMARK 620 3 HOH A2582 O 76.0 121.5 REMARK 620 4 HOH A2514 O 101.8 126.1 86.7 REMARK 620 5 HOH A2574 O 91.2 71.1 165.9 90.3 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue F9Q A 2401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2413 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2415 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2416 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2417 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2418 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2419 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2420 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2421 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2422 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2423 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2424 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2425 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2426 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2427 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2428 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2429 DBREF 6GT3 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 6GT3 A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127 DBREF 6GT3 A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 6GT3 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 6GT3 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 6GT3 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 6GT3 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 6GT3 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 6GT3 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 6GT3 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 6GT3 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 6GT3 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 6GT3 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 6GT3 LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 6GT3 ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 6GT3 ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 6GT3 ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 6GT3 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 6GT3 ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 6GT3 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6GT3 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6GT3 LEU A 1106 UNP P0ABE7 LINKER SEQADV 6GT3 ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 6GT3 ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 6GT3 ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 6GT3 ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 6GT3 HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 34 A 433 HIS HIS HIS HIS HET NA A2400 1 HET F9Q A2401 22 HET CLR A2402 28 HET CLR A2403 28 HET CLR A2404 28 HET OLA A2405 20 HET OLA A2406 15 HET OLA A2407 9 HET OLA A2408 9 HET OLA A2409 9 HET OLA A2410 18 HET OLA A2411 20 HET OLA A2412 15 HET OLA A2413 12 HET OLA A2414 8 HET OLA A2415 11 HET OLA A2416 14 HET OLA A2417 13 HET OLA A2418 19 HET OLA A2419 9 HET OLC A2420 17 HET OLC A2421 23 HET OLC A2422 16 HET OLC A2423 14 HET OLC A2424 15 HET OLC A2425 22 HET OLC A2426 25 HET OLC A2427 25 HET OLC A2428 24 HET OLC A2429 22 HETNAM NA SODIUM ION HETNAM F9Q 6-(2-CHLORANYL-6-METHYL-PYRIDIN-4-YL)-5-(4- HETNAM 2 F9Q FLUOROPHENYL)-1,2,4-TRIAZIN-3-AMINE HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 NA NA 1+ FORMUL 3 F9Q C15 H11 CL F N5 FORMUL 4 CLR 3(C27 H46 O) FORMUL 7 OLA 15(C18 H34 O2) FORMUL 22 OLC 10(C21 H40 O4) FORMUL 32 HOH *136(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ARG A 111 VAL A 116 1 6 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21 HELIX 14 AB5 LYS A 1059 GLU A 1081 1 23 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 SER A 305 1 14 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A2400 1555 1555 2.49 LINK OG SER A 91 NA NA A2400 1555 1555 2.52 LINK NA NA A2400 O HOH A2582 1555 1555 2.42 LINK NA NA A2400 O HOH A2514 1555 1555 2.46 LINK NA NA A2400 O HOH A2574 1555 1555 2.42 SITE 1 AC1 5 ASP A 52 SER A 91 HOH A2514 HOH A2574 SITE 2 AC1 5 HOH A2582 SITE 1 AC2 14 ILE A 66 LEU A 85 PHE A 168 GLU A 169 SITE 2 AC2 14 MET A 177 TRP A 246 LEU A 249 HIS A 250 SITE 3 AC2 14 ASN A 253 HIS A 278 HOH A2529 HOH A2561 SITE 4 AC2 14 HOH A2573 HOH A2593 SITE 1 AC3 9 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC3 9 CLR A2404 OLC A2422 OLC A2427 OLC A2428 SITE 3 AC3 9 HOH A2533 SITE 1 AC4 6 LEU A 247 PRO A 248 SER A 263 OLA A2406 SITE 2 AC4 6 OLA A2412 HOH A2520 SITE 1 AC5 10 LEU A 187 CYS A 254 PHE A 255 PHE A 258 SITE 2 AC5 10 CYS A 259 CLR A2402 OLA A2419 OLC A2422 SITE 3 AC5 10 OLC A2427 HOH A2542 SITE 1 AC6 2 THR A 65 OLC A2427 SITE 1 AC7 1 CLR A2403 SITE 1 AC8 2 LEU A 241 LEU A 244 SITE 1 AC9 4 PHE A 44 ALA A 97 VAL A 116 HOH A2504 SITE 1 AD1 2 THR A 279 PHE A 286 SITE 1 AD2 3 TYR A 271 VAL A 275 TYR A 290 SITE 1 AD3 7 ILE A 127 LEU A 131 CYS A 185 PRO A 189 SITE 2 AD3 7 VAL A 196 OLA A2416 OLC A2421 SITE 1 AD4 1 CLR A2403 SITE 1 AD5 5 SER A 7 LEU A 19 TRP A 29 PHE A 286 SITE 2 AD5 5 HOH A2575 SITE 1 AD6 2 ILE A 3 OLA A2417 SITE 1 AD7 2 VAL A 130 OLA A2411 SITE 1 AD8 4 SER A 6 LEU A 14 THR A 68 OLA A2415 SITE 1 AD9 3 TRP A 32 PHE A 201 LYS A 233 SITE 1 AE1 3 ALA A 236 ALA A 239 CLR A2404 SITE 1 AE2 5 TYR A 179 PHE A 258 OLC A2421 OLC A2422 SITE 2 AE2 5 HOH A2557 SITE 1 AE3 14 HIS A 75 ALA A 134 MET A 140 LEU A 141 SITE 2 AE3 14 GLY A 142 ASN A 144 ASN A 175 TYR A 179 SITE 3 AE3 14 ALA A 184 OLA A2411 OLC A2420 OLC A2426 SITE 4 AE3 14 HOH A2503 HOH A2536 SITE 1 AE4 5 PHE A 258 CLR A2402 CLR A2404 OLC A2420 SITE 2 AE4 5 HOH A2542 SITE 1 AE5 4 ALA A 202 ARG A 205 OLC A2428 OLC A2429 SITE 1 AE6 4 ALA A 73 CYS A 74 HIS A 75 GLY A 162 SITE 1 AE7 5 PHE A 255 ASP A 261 CYS A 262 OLC A2427 SITE 2 AE7 5 HOH A2520 SITE 1 AE8 5 PHE A 133 MET A 140 LEU A 141 OLC A2421 SITE 2 AE8 5 HOH A2541 SITE 1 AE9 8 THR A 65 CYS A 71 CYS A 259 CLR A2402 SITE 2 AE9 8 CLR A2404 OLA A2405 OLC A2425 HOH A2596 SITE 1 AF1 10 TYR A 43 LEU A 54 LEU A 58 PHE A 83 SITE 2 AF1 10 GLY A 118 ILE A 125 TRP A 129 CLR A2402 SITE 3 AF1 10 OLC A2423 OLC A2429 SITE 1 AF2 7 CYS A 28 TRP A 32 TYR A 43 ALA A 50 SITE 2 AF2 7 ARG A 205 OLC A2423 OLC A2428 CRYST1 39.550 179.714 140.776 90.00 90.00 90.00 C 2 2 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 0.025284 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005564 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007103 0.00000 ATOM 1 N GLY A -1 -21.018 24.740 1.363 1.00102.98 N ANISOU 1 N GLY A -1 18826 9370 10932 -2103 -1567 1300 N ATOM 2 CA GLY A -1 -21.628 23.702 2.173 1.00 99.98 C ANISOU 2 CA GLY A -1 18257 9149 10580 -1847 -1519 1136 C ATOM 3 C GLY A -1 -22.868 23.114 1.529 1.00 97.37 C ANISOU 3 C GLY A -1 17864 8923 10211 -1466 -1428 1099 C ATOM 4 O GLY A -1 -23.952 23.692 1.612 1.00 99.91 O ANISOU 4 O GLY A -1 18433 9060 10469 -1133 -1520 1024 O ATOM 5 N ALA A 0 -22.703 21.962 0.885 1.00 92.40 N ANISOU 5 N ALA A 0 16886 8596 9627 -1507 -1252 1162 N ATOM 6 CA ALA A 0 -23.801 21.277 0.209 1.00 88.10 C ANISOU 6 CA ALA A 0 16237 8187 9050 -1187 -1193 1146 C ATOM 7 C ALA A 0 -24.924 20.929 1.183 1.00 85.80 C ANISOU 7 C ALA A 0 15937 7874 8789 -805 -1248 982 C ATOM 8 O ALA A 0 -24.663 20.679 2.360 1.00 86.73 O ANISOU 8 O ALA A 0 16019 7987 8947 -826 -1249 873 O ATOM 9 CB ALA A 0 -23.290 20.020 -0.483 1.00 83.19 C ANISOU 9 CB ALA A 0 15253 7903 8451 -1320 -993 1219 C ATOM 10 N PRO A 1 -26.178 20.925 0.694 1.00 82.70 N ANISOU 10 N PRO A 1 15568 7470 8386 -452 -1295 978 N ATOM 11 CA PRO A 1 -27.357 20.599 1.505 1.00 77.38 C ANISOU 11 CA PRO A 1 14827 6800 7774 -41 -1314 859 C ATOM 12 C PRO A 1 -27.192 19.308 2.300 1.00 66.23 C ANISOU 12 C PRO A 1 13113 5629 6424 -45 -1193 779 C ATOM 13 O PRO A 1 -26.920 18.260 1.714 1.00 64.29 O ANISOU 13 O PRO A 1 12587 5651 6190 -166 -1104 835 O ATOM 14 CB PRO A 1 -28.465 20.456 0.461 1.00 81.14 C ANISOU 14 CB PRO A 1 15215 7347 8267 221 -1378 941 C ATOM 15 CG PRO A 1 -28.053 21.372 -0.630 1.00 84.30 C ANISOU 15 CG PRO A 1 15862 7599 8571 28 -1453 1063 C ATOM 16 CD PRO A 1 -26.550 21.297 -0.684 1.00 84.64 C ANISOU 16 CD PRO A 1 15901 7691 8566 -420 -1345 1104 C ATOM 17 N PRO A 2 -27.349 19.392 3.631 1.00 60.18 N ANISOU 17 N PRO A 2 12428 4763 5674 95 -1181 642 N ATOM 18 CA PRO A 2 -27.165 18.264 4.551 1.00 54.17 C ANISOU 18 CA PRO A 2 11442 4187 4955 93 -1077 559 C ATOM 19 C PRO A 2 -28.052 17.069 4.217 1.00 51.19 C ANISOU 19 C PRO A 2 10719 4086 4643 336 -1002 587 C ATOM 20 O PRO A 2 -27.685 15.937 4.522 1.00 52.45 O ANISOU 20 O PRO A 2 10630 4483 4817 232 -912 571 O ATOM 21 CB PRO A 2 -27.550 18.856 5.911 1.00 53.96 C ANISOU 21 CB PRO A 2 11660 3946 4897 317 -1084 401 C ATOM 22 CG PRO A 2 -27.324 20.320 5.764 1.00 55.19 C ANISOU 22 CG PRO A 2 12188 3812 4970 243 -1212 409 C ATOM 23 CD PRO A 2 -27.697 20.632 4.346 1.00 60.34 C ANISOU 23 CD PRO A 2 12807 4475 5645 267 -1263 554 C ATOM 24 N ILE A 3 -29.199 17.320 3.595 1.00 51.74 N ANISOU 24 N ILE A 3 10757 4142 4759 641 -1063 636 N ATOM 25 CA ILE A 3 -30.145 16.254 3.287 1.00 55.72 C ANISOU 25 CA ILE A 3 10914 4907 5351 870 -1048 673 C ATOM 26 C ILE A 3 -29.616 15.338 2.180 1.00 54.45 C ANISOU 26 C ILE A 3 10543 5005 5139 593 -1044 756 C ATOM 27 O ILE A 3 -30.058 14.198 2.046 1.00 51.39 O ANISOU 27 O ILE A 3 9856 4878 4793 665 -1026 758 O ATOM 28 CB ILE A 3 -31.520 16.825 2.875 1.00 59.19 C ANISOU 28 CB ILE A 3 11328 5263 5897 1250 -1155 727 C ATOM 29 CG1 ILE A 3 -32.608 15.752 2.977 1.00 62.14 C ANISOU 29 CG1 ILE A 3 11293 5892 6425 1526 -1145 750 C ATOM 30 CG2 ILE A 3 -31.461 17.409 1.479 1.00 63.45 C ANISOU 30 CG2 ILE A 3 11994 5739 6377 1110 -1303 848 C ATOM 31 CD1 ILE A 3 -33.970 16.212 2.500 1.00 68.27 C ANISOU 31 CD1 ILE A 3 11934 6634 7370 1866 -1270 840 C ATOM 32 N MET A 4 -28.659 15.832 1.399 1.00 53.18 N ANISOU 32 N MET A 4 10540 4776 4889 281 -1044 816 N ATOM 33 CA MET A 4 -28.081 15.042 0.316 1.00 46.75 C ANISOU 33 CA MET A 4 9562 4185 4015 43 -978 880 C ATOM 34 C MET A 4 -27.142 13.967 0.856 1.00 45.29 C ANISOU 34 C MET A 4 9141 4227 3839 -165 -810 824 C ATOM 35 O MET A 4 -27.290 12.786 0.536 1.00 43.62 O ANISOU 35 O MET A 4 8667 4274 3634 -152 -749 803 O ATOM 36 CB MET A 4 -27.342 15.947 -0.672 1.00 47.23 C ANISOU 36 CB MET A 4 9861 4100 3983 -193 -983 977 C ATOM 37 CG MET A 4 -28.241 16.951 -1.374 1.00 45.00 C ANISOU 37 CG MET A 4 9812 3612 3675 -4 -1160 1043 C ATOM 38 SD MET A 4 -27.368 17.951 -2.594 1.00 58.65 S ANISOU 38 SD MET A 4 11837 5184 5265 -291 -1152 1171 S ATOM 39 CE MET A 4 -26.886 16.697 -3.780 1.00 66.22 C ANISOU 39 CE MET A 4 12587 6443 6129 -456 -1001 1219 C ATOM 40 N GLY A 5 -26.177 14.378 1.674 1.00 39.92 N ANISOU 40 N GLY A 5 8557 3442 3168 -365 -758 799 N ATOM 41 CA GLY A 5 -25.266 13.437 2.300 1.00 36.51 C ANISOU 41 CA GLY A 5 7894 3211 2769 -560 -628 757 C ATOM 42 C GLY A 5 -26.011 12.529 3.257 1.00 38.88 C ANISOU 42 C GLY A 5 7987 3667 3119 -326 -614 632 C ATOM 43 O GLY A 5 -25.671 11.354 3.415 1.00 38.66 O ANISOU 43 O GLY A 5 7648 3905 3136 -392 -504 576 O ATOM 44 N SER A 6 -27.037 13.082 3.896 1.00 39.88 N ANISOU 44 N SER A 6 8227 3639 3285 -30 -693 565 N ATOM 45 CA SER A 6 -27.898 12.307 4.778 1.00 40.70 C ANISOU 45 CA SER A 6 8069 3905 3490 229 -634 437 C ATOM 46 C SER A 6 -28.618 11.218 3.998 1.00 32.19 C ANISOU 46 C SER A 6 6686 3091 2453 328 -632 473 C ATOM 47 O SER A 6 -28.746 10.092 4.472 1.00 34.30 O ANISOU 47 O SER A 6 6651 3591 2791 347 -547 395 O ATOM 48 CB SER A 6 -28.917 13.210 5.475 1.00 42.86 C ANISOU 48 CB SER A 6 8536 3947 3800 569 -672 389 C ATOM 49 OG SER A 6 -28.275 14.273 6.154 1.00 53.29 O ANISOU 49 OG SER A 6 10234 4966 5047 473 -709 346 O ATOM 50 N SER A 7 -29.079 11.564 2.800 1.00 33.30 N ANISOU 50 N SER A 7 6947 3168 2536 375 -757 599 N ATOM 51 CA SER A 7 -29.822 10.634 1.955 1.00 33.55 C ANISOU 51 CA SER A 7 6767 3398 2583 451 -833 646 C ATOM 52 C SER A 7 -29.021 9.374 1.652 1.00 28.96 C ANISOU 52 C SER A 7 6002 3059 1941 219 -717 607 C ATOM 53 O SER A 7 -29.539 8.264 1.760 1.00 30.18 O ANISOU 53 O SER A 7 5885 3414 2169 283 -716 557 O ATOM 54 CB SER A 7 -30.235 11.313 0.648 1.00 40.50 C ANISOU 54 CB SER A 7 7844 4144 3399 475 -1000 773 C ATOM 55 OG SER A 7 -31.066 12.431 0.901 1.00 49.96 O ANISOU 55 OG SER A 7 9202 5111 4669 737 -1121 818 O ATOM 56 N VAL A 8 -27.758 9.551 1.275 1.00 29.00 N ANISOU 56 N VAL A 8 6095 3044 1878 -46 -596 623 N ATOM 57 CA VAL A 8 -26.882 8.422 0.980 1.00 32.56 C ANISOU 57 CA VAL A 8 6336 3708 2327 -225 -437 582 C ATOM 58 C VAL A 8 -26.671 7.562 2.221 1.00 30.14 C ANISOU 58 C VAL A 8 5805 3551 2095 -219 -354 474 C ATOM 59 O VAL A 8 -26.840 6.344 2.178 1.00 25.67 O ANISOU 59 O VAL A 8 5011 3175 1568 -193 -312 415 O ATOM 60 CB VAL A 8 -25.517 8.889 0.445 1.00 28.60 C ANISOU 60 CB VAL A 8 5937 3153 1776 -478 -298 651 C ATOM 61 CG1 VAL A 8 -24.540 7.725 0.392 1.00 31.76 C ANISOU 61 CG1 VAL A 8 6096 3768 2204 -603 -105 614 C ATOM 62 CG2 VAL A 8 -25.679 9.524 -0.928 1.00 32.70 C ANISOU 62 CG2 VAL A 8 6669 3560 2197 -492 -345 749 C ATOM 63 N TYR A 9 -26.310 8.209 3.325 1.00 27.15 N ANISOU 63 N TYR A 9 5485 3064 1767 -243 -342 433 N ATOM 64 CA TYR A 9 -26.100 7.516 4.589 1.00 23.61 C ANISOU 64 CA TYR A 9 4821 2728 1421 -233 -274 314 C ATOM 65 C TYR A 9 -27.355 6.765 5.035 1.00 22.61 C ANISOU 65 C TYR A 9 4499 2718 1372 9 -292 246 C ATOM 66 O TYR A 9 -27.280 5.597 5.404 1.00 20.97 O ANISOU 66 O TYR A 9 4061 2693 1212 -9 -225 186 O ATOM 67 CB TYR A 9 -25.658 8.507 5.671 1.00 24.60 C ANISOU 67 CB TYR A 9 5122 2656 1567 -281 -307 275 C ATOM 68 CG TYR A 9 -25.724 7.948 7.075 1.00 26.16 C ANISOU 68 CG TYR A 9 5194 2922 1825 -212 -272 149 C ATOM 69 CD1 TYR A 9 -24.834 6.967 7.496 1.00 22.03 C ANISOU 69 CD1 TYR A 9 4455 2568 1348 -370 -215 117 C ATOM 70 CD2 TYR A 9 -26.674 8.404 7.979 1.00 24.17 C ANISOU 70 CD2 TYR A 9 5057 2553 1574 30 -280 74 C ATOM 71 CE1 TYR A 9 -24.892 6.452 8.777 1.00 21.25 C ANISOU 71 CE1 TYR A 9 4286 2513 1274 -313 -203 15 C ATOM 72 CE2 TYR A 9 -26.739 7.896 9.264 1.00 25.51 C ANISOU 72 CE2 TYR A 9 5167 2772 1752 93 -220 -33 C ATOM 73 CZ TYR A 9 -25.847 6.921 9.657 1.00 30.64 C ANISOU 73 CZ TYR A 9 5630 3583 2427 -92 -200 -60 C ATOM 74 OH TYR A 9 -25.910 6.413 10.933 1.00 30.55 O ANISOU 74 OH TYR A 9 5605 3606 2398 -34 -161 -153 O ATOM 75 N ILE A 10 -28.506 7.428 4.984 1.00 23.96 N ANISOU 75 N ILE A 10 4748 2779 1575 234 -379 273 N ATOM 76 CA ILE A 10 -29.760 6.805 5.407 1.00 27.26 C ANISOU 76 CA ILE A 10 4929 3313 2117 462 -381 248 C ATOM 77 C ILE A 10 -30.144 5.623 4.511 1.00 22.91 C ANISOU 77 C ILE A 10 4173 2950 1581 415 -448 287 C ATOM 78 O ILE A 10 -30.559 4.571 5.001 1.00 21.83 O ANISOU 78 O ILE A 10 3784 2973 1536 445 -405 245 O ATOM 79 CB ILE A 10 -30.915 7.831 5.431 1.00 28.62 C ANISOU 79 CB ILE A 10 5190 3325 2360 743 -457 303 C ATOM 80 CG1 ILE A 10 -30.715 8.829 6.575 1.00 27.11 C ANISOU 80 CG1 ILE A 10 5226 2931 2145 844 -365 227 C ATOM 81 CG2 ILE A 10 -32.256 7.133 5.588 1.00 26.44 C ANISOU 81 CG2 ILE A 10 4586 3200 2261 956 -468 335 C ATOM 82 CD1 ILE A 10 -31.755 9.931 6.619 1.00 29.91 C ANISOU 82 CD1 ILE A 10 5718 3085 2562 1162 -405 275 C ATOM 83 N THR A 11 -29.995 5.796 3.201 1.00 23.76 N ANISOU 83 N THR A 11 4435 3016 1575 329 -560 370 N ATOM 84 CA THR A 11 -30.340 4.744 2.248 1.00 23.58 C ANISOU 84 CA THR A 11 4327 3121 1512 275 -662 400 C ATOM 85 C THR A 11 -29.493 3.493 2.473 1.00 23.26 C ANISOU 85 C THR A 11 4166 3236 1437 119 -519 312 C ATOM 86 O THR A 11 -30.005 2.372 2.453 1.00 21.01 O ANISOU 86 O THR A 11 3707 3071 1204 126 -568 286 O ATOM 87 CB THR A 11 -30.162 5.221 0.794 1.00 25.26 C ANISOU 87 CB THR A 11 4808 3230 1560 195 -774 494 C ATOM 88 OG1 THR A 11 -30.930 6.412 0.583 1.00 27.38 O ANISOU 88 OG1 THR A 11 5232 3327 1844 356 -941 593 O ATOM 89 CG2 THR A 11 -30.624 4.154 -0.179 1.00 25.65 C ANISOU 89 CG2 THR A 11 4769 3374 1601 146 -879 494 C ATOM 90 N VAL A 12 -28.198 3.696 2.692 1.00 20.92 N ANISOU 90 N VAL A 12 3944 2923 1081 -23 -356 281 N ATOM 91 CA VAL A 12 -27.282 2.593 2.959 1.00 19.43 C ANISOU 91 CA VAL A 12 3575 2867 940 -129 -204 206 C ATOM 92 C VAL A 12 -27.639 1.891 4.269 1.00 21.58 C ANISOU 92 C VAL A 12 3666 3234 1299 -70 -183 130 C ATOM 93 O VAL A 12 -27.655 0.661 4.335 1.00 19.88 O ANISOU 93 O VAL A 12 3300 3132 1121 -85 -157 84 O ATOM 94 CB VAL A 12 -25.816 3.082 3.002 1.00 22.79 C ANISOU 94 CB VAL A 12 4047 3251 1360 -277 -58 223 C ATOM 95 CG1 VAL A 12 -24.896 1.996 3.541 1.00 21.55 C ANISOU 95 CG1 VAL A 12 3688 3216 1284 -333 69 163 C ATOM 96 CG2 VAL A 12 -25.365 3.533 1.611 1.00 21.33 C ANISOU 96 CG2 VAL A 12 4025 2998 1082 -347 -22 307 C ATOM 97 N GLU A 13 -27.938 2.675 5.302 1.00 19.33 N ANISOU 97 N GLU A 13 3377 2875 1091 19 -176 112 N ATOM 98 CA GLU A 13 -28.333 2.124 6.597 1.00 17.94 C ANISOU 98 CA GLU A 13 3032 2768 1015 100 -117 45 C ATOM 99 C GLU A 13 -29.581 1.254 6.475 1.00 17.36 C ANISOU 99 C GLU A 13 2760 2800 1035 203 -172 67 C ATOM 100 O GLU A 13 -29.649 0.170 7.053 1.00 17.94 O ANISOU 100 O GLU A 13 2673 2981 1161 178 -121 30 O ATOM 101 CB GLU A 13 -28.577 3.249 7.608 1.00 21.67 C ANISOU 101 CB GLU A 13 3626 3104 1504 216 -88 22 C ATOM 102 CG GLU A 13 -27.316 3.957 8.093 1.00 22.37 C ANISOU 102 CG GLU A 13 3899 3077 1525 69 -71 -9 C ATOM 103 CD GLU A 13 -26.635 3.229 9.238 1.00 30.34 C ANISOU 103 CD GLU A 13 4826 4156 2545 -10 -18 -81 C ATOM 104 OE1 GLU A 13 -26.594 3.783 10.359 1.00 29.62 O ANISOU 104 OE1 GLU A 13 4884 3953 2418 32 -14 -135 O ATOM 105 OE2 GLU A 13 -26.139 2.105 9.020 1.00 32.80 O ANISOU 105 OE2 GLU A 13 4963 4614 2886 -104 9 -83 O ATOM 106 N LEU A 14 -30.563 1.731 5.717 1.00 19.27 N ANISOU 106 N LEU A 14 3009 2999 1313 305 -301 147 N ATOM 107 CA LEU A 14 -31.804 0.989 5.516 1.00 20.49 C ANISOU 107 CA LEU A 14 2938 3246 1601 375 -407 205 C ATOM 108 C LEU A 14 -31.566 -0.309 4.749 1.00 18.86 C ANISOU 108 C LEU A 14 2710 3122 1333 213 -494 190 C ATOM 109 O LEU A 14 -32.194 -1.329 5.032 1.00 19.05 O ANISOU 109 O LEU A 14 2536 3238 1466 192 -531 201 O ATOM 110 CB LEU A 14 -32.831 1.853 4.782 1.00 24.68 C ANISOU 110 CB LEU A 14 3480 3699 2200 516 -581 316 C ATOM 111 CG LEU A 14 -33.402 3.035 5.569 1.00 28.15 C ANISOU 111 CG LEU A 14 3912 4042 2741 750 -493 341 C ATOM 112 CD1 LEU A 14 -34.342 3.858 4.700 1.00 33.47 C ANISOU 112 CD1 LEU A 14 4599 4624 3493 903 -697 468 C ATOM 113 CD2 LEU A 14 -34.112 2.548 6.823 1.00 30.30 C ANISOU 113 CD2 LEU A 14 3914 4419 3181 876 -322 332 C ATOM 114 N ALA A 15 -30.655 -0.272 3.781 1.00 18.67 N ANISOU 114 N ALA A 15 2916 3051 1128 101 -510 172 N ATOM 115 CA ALA A 15 -30.311 -1.468 3.019 1.00 18.64 C ANISOU 115 CA ALA A 15 2977 3089 1018 -21 -554 138 C ATOM 116 C ALA A 15 -29.644 -2.505 3.922 1.00 20.42 C ANISOU 116 C ALA A 15 3077 3394 1286 -73 -396 52 C ATOM 117 O ALA A 15 -29.892 -3.702 3.800 1.00 19.21 O ANISOU 117 O ALA A 15 2874 3253 1172 -115 -446 25 O ATOM 118 CB ALA A 15 -29.404 -1.115 1.852 1.00 19.06 C ANISOU 118 CB ALA A 15 3238 3060 945 -68 -483 132 C ATOM 119 N ILE A 16 -28.799 -2.035 4.832 1.00 15.74 N ANISOU 119 N ILE A 16 2459 2791 730 -64 -227 13 N ATOM 120 CA ILE A 16 -28.147 -2.919 5.793 1.00 14.46 C ANISOU 120 CA ILE A 16 2185 2637 673 -90 -108 -48 C ATOM 121 C ILE A 16 -29.165 -3.514 6.765 1.00 15.90 C ANISOU 121 C ILE A 16 2181 2951 910 -52 -134 -44 C ATOM 122 O ILE A 16 -29.091 -4.696 7.108 1.00 16.44 O ANISOU 122 O ILE A 16 2175 3040 1030 -97 -117 -70 O ATOM 123 CB ILE A 16 -27.051 -2.174 6.578 1.00 15.06 C ANISOU 123 CB ILE A 16 2284 2660 780 -104 3 -66 C ATOM 124 CG1 ILE A 16 -25.919 -1.762 5.638 1.00 20.92 C ANISOU 124 CG1 ILE A 16 3127 3350 1472 -155 58 -43 C ATOM 125 CG2 ILE A 16 -26.501 -3.037 7.710 1.00 16.12 C ANISOU 125 CG2 ILE A 16 2304 2806 1015 -120 62 -105 C ATOM 126 CD1 ILE A 16 -24.924 -0.831 6.276 1.00 20.39 C ANISOU 126 CD1 ILE A 16 3071 3269 1407 -229 111 -30 C ATOM 127 N ALA A 17 -30.118 -2.694 7.195 1.00 15.13 N ANISOU 127 N ALA A 17 2011 2837 899 57 -147 6 N ATOM 128 CA ALA A 17 -31.144 -3.136 8.134 1.00 17.76 C ANISOU 128 CA ALA A 17 2142 3234 1373 125 -105 43 C ATOM 129 C ALA A 17 -31.962 -4.304 7.582 1.00 20.84 C ANISOU 129 C ALA A 17 2387 3681 1850 45 -243 98 C ATOM 130 O ALA A 17 -32.211 -5.281 8.288 1.00 21.78 O ANISOU 130 O ALA A 17 2381 3855 2040 -3 -193 107 O ATOM 131 CB ALA A 17 -32.059 -1.978 8.496 1.00 17.05 C ANISOU 131 CB ALA A 17 2000 3109 1371 300 -67 101 C ATOM 132 N AVAL A 18 -32.385 -4.176 6.328 0.88 20.28 N ANISOU 132 N AVAL A 18 2366 3575 1763 16 -440 144 N ATOM 133 N BVAL A 18 -32.362 -4.221 6.317 0.12 20.48 N ANISOU 133 N BVAL A 18 2395 3602 1786 11 -441 142 N ATOM 134 CA AVAL A 18 -33.148 -5.221 5.655 0.88 21.68 C ANISOU 134 CA AVAL A 18 2466 3768 2004 -94 -648 199 C ATOM 135 CA BVAL A 18 -33.192 -5.274 5.737 0.12 21.25 C ANISOU 135 CA BVAL A 18 2392 3719 1962 -95 -642 201 C ATOM 136 C AVAL A 18 -32.352 -6.521 5.610 0.88 19.53 C ANISOU 136 C AVAL A 18 2317 3481 1623 -223 -626 110 C ATOM 137 C BVAL A 18 -32.388 -6.546 5.446 0.12 19.85 C ANISOU 137 C BVAL A 18 2374 3514 1654 -232 -654 113 C ATOM 138 O AVAL A 18 -32.871 -7.595 5.918 0.88 19.40 O ANISOU 138 O AVAL A 18 2185 3485 1702 -314 -688 140 O ATOM 139 O BVAL A 18 -32.948 -7.640 5.414 0.12 20.70 O ANISOU 139 O BVAL A 18 2409 3622 1834 -340 -776 143 O ATOM 140 CB AVAL A 18 -33.532 -4.800 4.219 0.88 21.89 C ANISOU 140 CB AVAL A 18 2635 3723 1959 -115 -905 249 C ATOM 141 CB BVAL A 18 -33.897 -4.802 4.444 0.12 22.79 C ANISOU 141 CB BVAL A 18 2648 3859 2151 -98 -914 281 C ATOM 142 CG1AVAL A 18 -34.156 -5.965 3.460 0.88 21.56 C ANISOU 142 CG1AVAL A 18 2604 3656 1932 -271 -1176 285 C ATOM 143 CG1BVAL A 18 -34.824 -3.632 4.745 0.12 23.94 C ANISOU 143 CG1BVAL A 18 2600 4023 2474 74 -917 390 C ATOM 144 CG2AVAL A 18 -34.479 -3.611 4.249 0.88 24.42 C ANISOU 144 CG2AVAL A 18 2802 4045 2431 36 -969 362 C ATOM 145 CG2BVAL A 18 -32.889 -4.427 3.376 0.12 21.42 C ANISOU 145 CG2BVAL A 18 2829 3595 1716 -129 -937 209 C ATOM 146 N LEU A 19 -31.080 -6.407 5.245 1.00 17.78 N ANISOU 146 N LEU A 19 2320 3217 1219 -225 -525 16 N ATOM 147 CA LEU A 19 -30.213 -7.571 5.095 1.00 21.26 C ANISOU 147 CA LEU A 19 2892 3580 1604 -275 -462 -67 C ATOM 148 C LEU A 19 -29.923 -8.231 6.441 1.00 20.23 C ANISOU 148 C LEU A 19 2623 3524 1541 -286 -336 -87 C ATOM 149 O LEU A 19 -29.894 -9.456 6.545 1.00 21.74 O ANISOU 149 O LEU A 19 2840 3678 1741 -347 -370 -108 O ATOM 150 CB LEU A 19 -28.901 -7.182 4.415 1.00 19.93 C ANISOU 150 CB LEU A 19 2919 3294 1358 -206 -321 -121 C ATOM 151 CG LEU A 19 -28.995 -6.745 2.955 1.00 21.77 C ANISOU 151 CG LEU A 19 3339 3463 1470 -176 -406 -115 C ATOM 152 CD1 LEU A 19 -27.625 -6.332 2.434 1.00 23.81 C ANISOU 152 CD1 LEU A 19 3693 3692 1660 -110 -214 -138 C ATOM 153 CD2 LEU A 19 -29.590 -7.856 2.103 1.00 24.59 C ANISOU 153 CD2 LEU A 19 3788 3776 1779 -231 -565 -137 C ATOM 154 N ALA A 20 -29.706 -7.415 7.467 1.00 19.82 N ANISOU 154 N ALA A 20 2471 3541 1518 -220 -202 -81 N ATOM 155 CA ALA A 20 -29.409 -7.929 8.801 1.00 19.74 C ANISOU 155 CA ALA A 20 2384 3561 1555 -216 -87 -94 C ATOM 156 C ALA A 20 -30.597 -8.696 9.371 1.00 21.41 C ANISOU 156 C ALA A 20 2439 3805 1892 -260 -120 -16 C ATOM 157 O ALA A 20 -30.429 -9.702 10.062 1.00 19.86 O ANISOU 157 O ALA A 20 2238 3602 1707 -311 -85 -17 O ATOM 158 CB ALA A 20 -29.016 -6.797 9.730 1.00 12.64 C ANISOU 158 CB ALA A 20 1485 2644 672 -134 33 -101 C ATOM 159 N ILE A 21 -31.800 -8.216 9.077 1.00 17.45 N ANISOU 159 N ILE A 21 1794 3335 1502 -242 -189 72 N ATOM 160 CA ILE A 21 -33.013 -8.863 9.559 1.00 22.30 C ANISOU 160 CA ILE A 21 2188 3998 2288 -298 -208 187 C ATOM 161 C ILE A 21 -33.264 -10.181 8.828 1.00 22.65 C ANISOU 161 C ILE A 21 2268 3985 2352 -474 -415 204 C ATOM 162 O ILE A 21 -33.440 -11.222 9.460 1.00 27.02 O ANISOU 162 O ILE A 21 2777 4530 2960 -572 -393 242 O ATOM 163 CB ILE A 21 -34.236 -7.939 9.407 1.00 23.54 C ANISOU 163 CB ILE A 21 2122 4211 2610 -208 -230 304 C ATOM 164 CG1 ILE A 21 -34.108 -6.741 10.353 1.00 21.54 C ANISOU 164 CG1 ILE A 21 1875 3978 2330 -15 8 285 C ATOM 165 CG2 ILE A 21 -35.521 -8.700 9.693 1.00 24.25 C ANISOU 165 CG2 ILE A 21 1917 4364 2932 -301 -274 462 C ATOM 166 CD1 ILE A 21 -35.177 -5.691 10.163 1.00 23.44 C ANISOU 166 CD1 ILE A 21 1934 4248 2725 141 13 386 C ATOM 167 N LEU A 22 -33.262 -10.133 7.498 1.00 21.86 N ANISOU 167 N LEU A 22 2301 3821 2183 -518 -625 176 N ATOM 168 CA LEU A 22 -33.535 -11.315 6.684 1.00 19.99 C ANISOU 168 CA LEU A 22 2186 3486 1924 -687 -866 178 C ATOM 169 C LEU A 22 -32.550 -12.452 6.944 1.00 21.45 C ANISOU 169 C LEU A 22 2584 3583 1983 -724 -795 74 C ATOM 170 O LEU A 22 -32.953 -13.599 7.130 1.00 23.69 O ANISOU 170 O LEU A 22 2875 3799 2327 -864 -899 113 O ATOM 171 CB LEU A 22 -33.514 -10.956 5.197 1.00 24.70 C ANISOU 171 CB LEU A 22 3004 3985 2396 -686 -1066 137 C ATOM 172 CG LEU A 22 -34.718 -10.177 4.661 1.00 30.39 C ANISOU 172 CG LEU A 22 3547 4730 3271 -681 -1256 261 C ATOM 173 CD1 LEU A 22 -34.528 -9.854 3.188 1.00 27.96 C ANISOU 173 CD1 LEU A 22 3538 4278 2806 -641 -1383 193 C ATOM 174 CD2 LEU A 22 -36.000 -10.961 4.883 1.00 37.09 C ANISOU 174 CD2 LEU A 22 4149 5570 4375 -821 -1412 396 C ATOM 175 N GLY A 23 -31.262 -12.131 6.953 1.00 19.77 N ANISOU 175 N GLY A 23 2533 3363 1617 -601 -627 -40 N ATOM 176 CA GLY A 23 -30.235 -13.141 7.128 1.00 17.03 C ANISOU 176 CA GLY A 23 2367 2931 1172 -587 -554 -129 C ATOM 177 C GLY A 23 -30.272 -13.816 8.484 1.00 22.77 C ANISOU 177 C GLY A 23 2976 3678 1999 -615 -464 -83 C ATOM 178 O GLY A 23 -30.092 -15.029 8.589 1.00 22.97 O ANISOU 178 O GLY A 23 3128 3593 2005 -675 -519 -100 O ATOM 179 N ASN A 24 -30.514 -13.036 9.531 1.00 19.52 N ANISOU 179 N ASN A 24 2368 3381 1668 -565 -325 -22 N ATOM 180 CA ASN A 24 -30.465 -13.577 10.881 1.00 22.48 C ANISOU 180 CA ASN A 24 2689 3768 2083 -578 -215 25 C ATOM 181 C ASN A 24 -31.774 -14.229 11.315 1.00 19.84 C ANISOU 181 C ASN A 24 2202 3443 1892 -722 -258 163 C ATOM 182 O ASN A 24 -31.774 -15.114 12.169 1.00 21.64 O ANISOU 182 O ASN A 24 2461 3629 2133 -787 -212 213 O ATOM 183 CB ASN A 24 -30.052 -12.484 11.863 1.00 19.78 C ANISOU 183 CB ASN A 24 2290 3513 1711 -458 -39 18 C ATOM 184 CG ASN A 24 -28.589 -12.111 11.717 1.00 19.34 C ANISOU 184 CG ASN A 24 2360 3436 1552 -366 -10 -86 C ATOM 185 OD1 ASN A 24 -27.705 -12.860 12.134 1.00 20.51 O ANISOU 185 OD1 ASN A 24 2594 3533 1667 -352 -9 -115 O ATOM 186 ND2 ASN A 24 -28.324 -10.964 11.103 1.00 13.96 N ANISOU 186 ND2 ASN A 24 1674 2772 860 -303 6 -119 N ATOM 187 N VAL A 25 -32.884 -13.802 10.722 1.00 19.22 N ANISOU 187 N VAL A 25 1948 3415 1939 -779 -354 246 N ATOM 188 CA VAL A 25 -34.147 -14.509 10.905 1.00 24.59 C ANISOU 188 CA VAL A 25 2433 4102 2808 -956 -438 407 C ATOM 189 C VAL A 25 -34.002 -15.913 10.323 1.00 25.84 C ANISOU 189 C VAL A 25 2802 4089 2928 -1133 -662 381 C ATOM 190 O VAL A 25 -34.490 -16.891 10.891 1.00 25.79 O ANISOU 190 O VAL A 25 2755 4031 3014 -1294 -683 487 O ATOM 191 CB VAL A 25 -35.327 -13.760 10.240 1.00 25.68 C ANISOU 191 CB VAL A 25 2307 4324 3126 -977 -557 519 C ATOM 192 CG1 VAL A 25 -36.487 -14.704 9.954 1.00 30.35 C ANISOU 192 CG1 VAL A 25 2724 4879 3929 -1226 -779 682 C ATOM 193 CG2 VAL A 25 -35.782 -12.603 11.118 1.00 22.29 C ANISOU 193 CG2 VAL A 25 1638 4043 2787 -802 -290 592 C ATOM 194 N LEU A 26 -33.300 -16.000 9.197 1.00 23.22 N ANISOU 194 N LEU A 26 2733 3651 2440 -1097 -808 240 N ATOM 195 CA LEU A 26 -33.013 -17.276 8.551 1.00 25.00 C ANISOU 195 CA LEU A 26 3259 3670 2570 -1211 -1003 175 C ATOM 196 C LEU A 26 -32.190 -18.190 9.461 1.00 21.44 C ANISOU 196 C LEU A 26 2954 3134 2059 -1172 -871 139 C ATOM 197 O LEU A 26 -32.417 -19.399 9.515 1.00 29.18 O ANISOU 197 O LEU A 26 4081 3951 3055 -1322 -1004 172 O ATOM 198 CB LEU A 26 -32.278 -17.038 7.231 1.00 28.24 C ANISOU 198 CB LEU A 26 3962 3989 2780 -1106 -1085 19 C ATOM 199 CG LEU A 26 -32.078 -18.221 6.285 1.00 36.30 C ANISOU 199 CG LEU A 26 5334 4749 3711 -1125 -1218 -60 C ATOM 200 CD1 LEU A 26 -33.417 -18.820 5.881 1.00 39.36 C ANISOU 200 CD1 LEU A 26 5677 5035 4242 -1344 -1478 65 C ATOM 201 CD2 LEU A 26 -31.291 -17.781 5.059 1.00 33.77 C ANISOU 201 CD2 LEU A 26 5239 4369 3224 -936 -1146 -190 C ATOM 202 N VAL A 27 -31.236 -17.603 10.174 1.00 19.42 N ANISOU 202 N VAL A 27 2673 2970 1737 -981 -643 81 N ATOM 203 CA VAL A 27 -30.411 -18.352 11.117 1.00 25.33 C ANISOU 203 CA VAL A 27 3539 3648 2436 -922 -545 65 C ATOM 204 C VAL A 27 -31.258 -18.935 12.250 1.00 23.78 C ANISOU 204 C VAL A 27 3229 3457 2350 -1078 -511 226 C ATOM 205 O VAL A 27 -31.158 -20.123 12.565 1.00 22.70 O ANISOU 205 O VAL A 27 3261 3162 2202 -1165 -581 257 O ATOM 206 CB VAL A 27 -29.292 -17.464 11.713 1.00 21.44 C ANISOU 206 CB VAL A 27 3006 3265 1877 -718 -358 0 C ATOM 207 CG1 VAL A 27 -28.619 -18.157 12.889 1.00 20.26 C ANISOU 207 CG1 VAL A 27 2939 3057 1701 -675 -299 28 C ATOM 208 CG2 VAL A 27 -28.272 -17.104 10.645 1.00 20.96 C ANISOU 208 CG2 VAL A 27 3064 3182 1719 -575 -354 -134 C ATOM 209 N CYS A 28 -32.095 -18.096 12.853 1.00 21.99 N ANISOU 209 N CYS A 28 2732 3399 2224 -1100 -381 338 N ATOM 210 CA CYS A 28 -32.957 -18.534 13.948 1.00 22.60 C ANISOU 210 CA CYS A 28 2677 3507 2402 -1234 -274 516 C ATOM 211 C CYS A 28 -33.939 -19.598 13.476 1.00 26.30 C ANISOU 211 C CYS A 28 3113 3863 3017 -1503 -476 637 C ATOM 212 O CYS A 28 -34.204 -20.571 14.182 1.00 27.41 O ANISOU 212 O CYS A 28 3312 3912 3191 -1653 -462 754 O ATOM 213 CB CYS A 28 -33.717 -17.349 14.546 1.00 23.27 C ANISOU 213 CB CYS A 28 2478 3793 2572 -1163 -56 609 C ATOM 214 SG CYS A 28 -32.665 -16.062 15.251 1.00 25.21 S ANISOU 214 SG CYS A 28 2816 4129 2634 -891 150 480 S ATOM 215 N TRP A 29 -34.469 -19.406 12.273 1.00 27.77 N ANISOU 215 N TRP A 29 3233 4038 3282 -1582 -691 620 N ATOM 216 CA TRP A 29 -35.429 -20.339 11.694 1.00 32.23 C ANISOU 216 CA TRP A 29 3775 4477 3994 -1873 -963 736 C ATOM 217 C TRP A 29 -34.792 -21.709 11.456 1.00 28.89 C ANISOU 217 C TRP A 29 3761 3776 3439 -1962 -1137 652 C ATOM 218 O TRP A 29 -35.427 -22.741 11.665 1.00 31.60 O ANISOU 218 O TRP A 29 4136 3982 3888 -2220 -1274 787 O ATOM 219 CB TRP A 29 -35.990 -19.774 10.386 1.00 35.78 C ANISOU 219 CB TRP A 29 4141 4947 4506 -1912 -1209 713 C ATOM 220 CG TRP A 29 -37.295 -20.377 9.962 1.00 52.39 C ANISOU 220 CG TRP A 29 6123 6969 6812 -2078 -1401 867 C ATOM 221 CD1 TRP A 29 -37.973 -21.387 10.581 1.00 60.35 C ANISOU 221 CD1 TRP A 29 7068 7906 7957 -2268 -1415 1025 C ATOM 222 CD2 TRP A 29 -38.085 -20.002 8.826 1.00 61.46 C ANISOU 222 CD2 TRP A 29 7206 8101 8046 -2080 -1619 888 C ATOM 223 NE1 TRP A 29 -39.133 -21.666 9.899 1.00 64.87 N ANISOU 223 NE1 TRP A 29 7513 8431 8704 -2397 -1640 1142 N ATOM 224 CE2 TRP A 29 -39.225 -20.830 8.818 1.00 64.74 C ANISOU 224 CE2 TRP A 29 7498 8442 8658 -2288 -1777 1063 C ATOM 225 CE3 TRP A 29 -37.938 -19.047 7.815 1.00 63.94 C ANISOU 225 CE3 TRP A 29 7568 8445 8280 -1934 -1701 786 C ATOM 226 CZ2 TRP A 29 -40.212 -20.732 7.839 1.00 68.52 C ANISOU 226 CZ2 TRP A 29 7891 8881 9263 -2363 -2036 1142 C ATOM 227 CZ3 TRP A 29 -38.919 -18.951 6.844 1.00 65.34 C ANISOU 227 CZ3 TRP A 29 7685 8571 8571 -2002 -1945 862 C ATOM 228 CH2 TRP A 29 -40.041 -19.789 6.863 1.00 68.85 C ANISOU 228 CH2 TRP A 29 7998 8945 9218 -2218 -2121 1040 C ATOM 229 N ALA A 30 -33.533 -21.710 11.028 1.00 28.40 N ANISOU 229 N ALA A 30 4006 3624 3160 -1741 -1119 443 N ATOM 230 CA ALA A 30 -32.811 -22.953 10.765 1.00 32.54 C ANISOU 230 CA ALA A 30 4944 3871 3550 -1743 -1247 343 C ATOM 231 C ALA A 30 -32.602 -23.762 12.042 1.00 29.80 C ANISOU 231 C ALA A 30 4652 3451 3218 -1779 -1132 443 C ATOM 232 O ALA A 30 -32.795 -24.978 12.056 1.00 31.40 O ANISOU 232 O ALA A 30 5090 3412 3427 -1951 -1297 491 O ATOM 233 CB ALA A 30 -31.471 -22.659 10.100 1.00 26.05 C ANISOU 233 CB ALA A 30 4363 3009 2526 -1448 -1175 124 C ATOM 234 N VAL A 31 -32.204 -23.083 13.114 1.00 26.59 N ANISOU 234 N VAL A 31 4076 3229 2798 -1623 -871 476 N ATOM 235 CA VAL A 31 -31.970 -23.752 14.388 1.00 27.22 C ANISOU 235 CA VAL A 31 4245 3245 2852 -1642 -762 579 C ATOM 236 C VAL A 31 -33.278 -24.311 14.944 1.00 29.92 C ANISOU 236 C VAL A 31 4442 3574 3353 -1958 -772 816 C ATOM 237 O VAL A 31 -33.316 -25.427 15.457 1.00 31.81 O ANISOU 237 O VAL A 31 4884 3620 3583 -2099 -832 911 O ATOM 238 CB VAL A 31 -31.324 -22.800 15.416 1.00 28.90 C ANISOU 238 CB VAL A 31 4345 3650 2985 -1426 -511 566 C ATOM 239 CG1 VAL A 31 -31.235 -23.465 16.784 1.00 26.35 C ANISOU 239 CG1 VAL A 31 4145 3258 2608 -1473 -417 700 C ATOM 240 CG2 VAL A 31 -29.943 -22.364 14.936 1.00 23.08 C ANISOU 240 CG2 VAL A 31 3723 2912 2133 -1150 -517 369 C ATOM 241 N TRP A 32 -34.350 -23.535 14.816 1.00 30.46 N ANISOU 241 N TRP A 32 4146 3842 3585 -2066 -710 928 N ATOM 242 CA TRP A 32 -35.673 -23.960 15.262 1.00 35.68 C ANISOU 242 CA TRP A 32 4565 4531 4459 -2370 -691 1189 C ATOM 243 C TRP A 32 -36.137 -25.231 14.553 1.00 39.67 C ANISOU 243 C TRP A 32 5249 4787 5037 -2588 -1013 1213 C ATOM 244 O TRP A 32 -36.648 -26.152 15.189 1.00 41.17 O ANISOU 244 O TRP A 32 5466 4886 5292 -2733 -998 1355 O ATOM 245 CB TRP A 32 -36.692 -22.839 15.038 1.00 39.35 C ANISOU 245 CB TRP A 32 4578 5256 5116 -2335 -586 1268 C ATOM 246 CG TRP A 32 -38.091 -23.189 15.455 1.00 49.97 C ANISOU 246 CG TRP A 32 5629 6653 6703 -2460 -514 1472 C ATOM 247 CD1 TRP A 32 -39.022 -23.872 14.724 1.00 53.55 C ANISOU 247 CD1 TRP A 32 6002 7010 7335 -2651 -778 1548 C ATOM 248 CD2 TRP A 32 -38.723 -22.862 16.699 1.00 55.47 C ANISOU 248 CD2 TRP A 32 6097 7499 7479 -2397 -140 1620 C ATOM 249 NE1 TRP A 32 -40.188 -23.996 15.439 1.00 58.29 N ANISOU 249 NE1 TRP A 32 6287 7706 8153 -2738 -594 1750 N ATOM 250 CE2 TRP A 32 -40.031 -23.384 16.654 1.00 60.76 C ANISOU 250 CE2 TRP A 32 6514 8165 8408 -2575 -182 1789 C ATOM 251 CE3 TRP A 32 -38.308 -22.181 17.848 1.00 53.77 C ANISOU 251 CE3 TRP A 32 5910 7403 7119 -2197 227 1615 C ATOM 252 CZ2 TRP A 32 -40.928 -23.246 17.714 1.00 66.03 C ANISOU 252 CZ2 TRP A 32 6934 8947 9207 -2564 166 1951 C ATOM 253 CZ3 TRP A 32 -39.199 -22.045 18.899 1.00 57.91 C ANISOU 253 CZ3 TRP A 32 6249 8014 7742 -2165 565 1757 C ATOM 254 CH2 TRP A 32 -40.494 -22.574 18.824 1.00 64.61 C ANISOU 254 CH2 TRP A 32 6825 8863 8862 -2351 551 1923 C ATOM 255 N LEU A 33 -35.953 -25.279 13.238 1.00 39.82 N ANISOU 255 N LEU A 33 5427 4693 5011 -2570 -1289 1058 N ATOM 256 CA LEU A 33 -36.474 -26.382 12.433 1.00 45.70 C ANISOU 256 CA LEU A 33 6370 5212 5782 -2722 -1596 1068 C ATOM 257 C LEU A 33 -35.623 -27.649 12.501 1.00 44.87 C ANISOU 257 C LEU A 33 6760 4790 5499 -2720 -1711 979 C ATOM 258 O LEU A 33 -36.156 -28.758 12.533 1.00 49.19 O ANISOU 258 O LEU A 33 7435 5166 6089 -2893 -1866 1075 O ATOM 259 CB LEU A 33 -36.615 -25.947 10.973 1.00 49.78 C ANISOU 259 CB LEU A 33 6939 5711 6264 -2656 -1818 944 C ATOM 260 CG LEU A 33 -37.745 -24.969 10.651 1.00 55.72 C ANISOU 260 CG LEU A 33 7243 6700 7229 -2685 -1817 1062 C ATOM 261 CD1 LEU A 33 -37.739 -24.624 9.170 1.00 57.50 C ANISOU 261 CD1 LEU A 33 7629 6854 7364 -2608 -2050 935 C ATOM 262 CD2 LEU A 33 -39.090 -25.550 11.066 1.00 60.21 C ANISOU 262 CD2 LEU A 33 7536 7292 8050 -2916 -1868 1304 C ATOM 263 N ASN A 34 -34.305 -27.486 12.514 1.00 39.17 N ANISOU 263 N ASN A 34 6316 3981 4587 -2508 -1639 796 N ATOM 264 CA ASN A 34 -33.401 -28.629 12.437 1.00 42.09 C ANISOU 264 CA ASN A 34 7173 4030 4789 -2413 -1742 683 C ATOM 265 C ASN A 34 -32.864 -29.052 13.802 1.00 44.37 C ANISOU 265 C ASN A 34 7555 4252 5051 -2393 -1579 777 C ATOM 266 O ASN A 34 -32.182 -28.281 14.478 1.00 39.24 O ANISOU 266 O ASN A 34 6769 3794 4346 -2163 -1341 745 O ATOM 267 CB ASN A 34 -32.241 -28.312 11.489 1.00 42.62 C ANISOU 267 CB ASN A 34 7514 4011 4669 -2117 -1755 416 C ATOM 268 CG ASN A 34 -31.424 -29.540 11.130 1.00 47.93 C ANISOU 268 CG ASN A 34 8681 4347 5182 -1955 -1852 297 C ATOM 269 OD1 ASN A 34 -31.737 -30.654 11.549 1.00 51.90 O ANISOU 269 OD1 ASN A 34 9354 4665 5702 -2088 -1959 404 O ATOM 270 ND2 ASN A 34 -30.377 -29.340 10.339 1.00 47.81 N ANISOU 270 ND2 ASN A 34 8883 4270 5011 -1641 -1790 82 N ATOM 271 N ASER A 35 -33.171 -30.284 14.197 0.54 41.24 N ANISOU 271 N ASER A 35 6859 3767 5042 -2000 -1835 1181 N ATOM 272 N BSER A 35 -33.175 -30.283 14.198 0.46 41.24 N ANISOU 272 N BSER A 35 6858 3768 5043 -2000 -1835 1182 N ATOM 273 CA ASER A 35 -32.741 -30.812 15.487 0.54 41.18 C ANISOU 273 CA ASER A 35 6793 3798 5055 -2180 -1721 1347 C ATOM 274 CA BSER A 35 -32.740 -30.817 15.485 0.46 41.19 C ANISOU 274 CA BSER A 35 6796 3797 5056 -2180 -1723 1347 C ATOM 275 C ASER A 35 -31.231 -31.036 15.527 0.54 42.55 C ANISOU 275 C ASER A 35 7312 3751 5104 -1875 -1647 1095 C ATOM 276 C BSER A 35 -31.230 -31.030 15.526 0.46 42.44 C ANISOU 276 C BSER A 35 7298 3739 5090 -1874 -1644 1094 C ATOM 277 O ASER A 35 -30.625 -31.041 16.598 0.54 40.22 O ANISOU 277 O ASER A 35 6959 3545 4778 -1931 -1463 1207 O ATOM 278 O BSER A 35 -30.623 -31.021 16.597 0.46 40.29 O ANISOU 278 O BSER A 35 6965 3560 4784 -1926 -1455 1205 O ATOM 279 CB ASER A 35 -33.471 -32.120 15.802 0.54 45.44 C ANISOU 279 CB ASER A 35 7358 4127 5780 -2606 -2190 1622 C ATOM 280 CB BSER A 35 -33.459 -32.134 15.789 0.46 45.45 C ANISOU 280 CB BSER A 35 7366 4121 5781 -2602 -2196 1619 C ATOM 281 OG ASER A 35 -33.135 -33.130 14.866 0.54 47.10 O ANISOU 281 OG ASER A 35 7934 3913 6047 -2458 -2637 1433 O ATOM 282 OG BSER A 35 -34.859 -31.943 15.878 0.46 48.05 O ANISOU 282 OG BSER A 35 7307 4688 6260 -2888 -2210 1801 O ATOM 283 N ASN A 36 -30.631 -31.222 14.356 1.00 41.97 N ANISOU 283 N ASN A 36 7585 3392 4970 -1603 -1793 721 N ATOM 284 CA ASN A 36 -29.188 -31.408 14.258 1.00 42.52 C ANISOU 284 CA ASN A 36 7923 3218 5013 -1301 -1694 341 C ATOM 285 C ASN A 36 -28.428 -30.114 14.537 1.00 39.46 C ANISOU 285 C ASN A 36 7436 3171 4387 -986 -1111 186 C ATOM 286 O ASN A 36 -27.223 -30.132 14.790 1.00 43.32 O ANISOU 286 O ASN A 36 8048 3525 4886 -747 -949 -78 O ATOM 287 CB ASN A 36 -28.810 -31.948 12.878 1.00 49.41 C ANISOU 287 CB ASN A 36 9084 3823 5868 -1157 -1890 -122 C ATOM 288 CG ASN A 36 -29.307 -33.362 12.648 1.00 54.89 C ANISOU 288 CG ASN A 36 9741 4277 6837 -1325 -2362 -28 C ATOM 289 OD1 ASN A 36 -29.403 -34.158 13.583 1.00 55.90 O ANISOU 289 OD1 ASN A 36 9733 4296 7211 -1465 -2600 261 O ATOM 290 ND2 ASN A 36 -29.624 -33.683 11.400 1.00 56.18 N ANISOU 290 ND2 ASN A 36 10027 4392 6925 -1338 -2492 -257 N ATOM 291 N LEU A 37 -29.139 -28.992 14.489 1.00 33.52 N ANISOU 291 N LEU A 37 6422 2819 3496 -982 -829 332 N ATOM 292 CA LEU A 37 -28.540 -27.695 14.773 1.00 31.79 C ANISOU 292 CA LEU A 37 6053 2928 3098 -701 -288 213 C ATOM 293 C LEU A 37 -28.856 -27.237 16.191 1.00 34.05 C ANISOU 293 C LEU A 37 5911 3568 3459 -857 30 510 C ATOM 294 O LEU A 37 -28.425 -26.169 16.612 1.00 33.08 O ANISOU 294 O LEU A 37 5591 3744 3235 -658 503 425 O ATOM 295 CB LEU A 37 -29.023 -26.646 13.769 1.00 30.28 C ANISOU 295 CB LEU A 37 5828 2903 2775 -600 -213 146 C ATOM 296 CG LEU A 37 -28.463 -26.748 12.350 1.00 34.13 C ANISOU 296 CG LEU A 37 6792 3179 2996 -502 -365 -221 C ATOM 297 CD1 LEU A 37 -29.070 -25.676 11.457 1.00 31.24 C ANISOU 297 CD1 LEU A 37 6403 2978 2487 -530 -411 -136 C ATOM 298 CD2 LEU A 37 -26.946 -26.640 12.372 1.00 32.93 C ANISOU 298 CD2 LEU A 37 6708 3036 2769 -200 -12 -574 C ATOM 299 N GLN A 38 -29.608 -28.046 16.928 1.00 35.87 N ANISOU 299 N GLN A 38 5999 3786 3843 -1271 -214 832 N ATOM 300 CA GLN A 38 -30.022 -27.663 18.273 1.00 35.32 C ANISOU 300 CA GLN A 38 5524 4120 3777 -1588 115 1074 C ATOM 301 C GLN A 38 -29.039 -28.148 19.332 1.00 34.57 C ANISOU 301 C GLN A 38 5567 3989 3580 -1666 139 1155 C ATOM 302 O GLN A 38 -29.229 -29.196 19.945 1.00 39.79 O ANISOU 302 O GLN A 38 6258 4534 4325 -1958 -226 1350 O ATOM 303 CB GLN A 38 -31.426 -28.188 18.565 1.00 37.32 C ANISOU 303 CB GLN A 38 5510 4458 4210 -2101 -112 1355 C ATOM 304 CG GLN A 38 -32.492 -27.526 17.710 1.00 40.75 C ANISOU 304 CG GLN A 38 5654 4965 4863 -2024 -131 1276 C ATOM 305 CD GLN A 38 -33.879 -28.079 17.953 1.00 47.36 C ANISOU 305 CD GLN A 38 6194 5850 5950 -2519 -362 1492 C ATOM 306 OE1 GLN A 38 -34.066 -29.001 18.746 1.00 47.08 O ANISOU 306 OE1 GLN A 38 6200 5838 5850 -2802 -490 1626 O ATOM 307 NE2 GLN A 38 -34.865 -27.514 17.266 1.00 49.31 N ANISOU 307 NE2 GLN A 38 6125 6111 6498 -2474 -446 1432 N ATOM 308 N ASN A 39 -27.983 -27.367 19.529 1.00 34.54 N ANISOU 308 N ASN A 39 5224 3827 4072 -1073 -1189 391 N ATOM 309 CA ASN A 39 -26.997 -27.626 20.569 1.00 36.95 C ANISOU 309 CA ASN A 39 5548 4145 4347 -1028 -1118 423 C ATOM 310 C ASN A 39 -26.659 -26.331 21.298 1.00 37.97 C ANISOU 310 C ASN A 39 5536 4466 4423 -987 -928 436 C ATOM 311 O ASN A 39 -27.125 -25.260 20.910 1.00 32.80 O ANISOU 311 O ASN A 39 4771 3936 3754 -980 -834 412 O ATOM 312 CB ASN A 39 -25.735 -28.253 19.976 1.00 36.66 C ANISOU 312 CB ASN A 39 5669 3977 4282 -857 -1168 310 C ATOM 313 CG ASN A 39 -25.255 -27.531 18.730 1.00 36.53 C ANISOU 313 CG ASN A 39 5690 3986 4203 -693 -1076 179 C ATOM 314 OD1 ASN A 39 -24.636 -26.470 18.813 1.00 37.12 O ANISOU 314 OD1 ASN A 39 5652 4189 4264 -606 -909 151 O ATOM 315 ND2 ASN A 39 -25.537 -28.107 17.566 1.00 34.98 N ANISOU 315 ND2 ASN A 39 5685 3644 3963 -649 -1191 102 N ATOM 316 N VAL A 40 -25.850 -26.432 22.348 1.00 37.14 N ANISOU 316 N VAL A 40 5458 4361 4292 -955 -906 472 N ATOM 317 CA VAL A 40 -25.491 -25.270 23.157 1.00 31.50 C ANISOU 317 CA VAL A 40 4659 3787 3523 -915 -781 483 C ATOM 318 C VAL A 40 -24.795 -24.195 22.331 1.00 30.34 C ANISOU 318 C VAL A 40 4420 3719 3387 -779 -696 368 C ATOM 319 O VAL A 40 -25.114 -23.010 22.442 1.00 33.57 O ANISOU 319 O VAL A 40 4726 4266 3762 -780 -585 365 O ATOM 320 CB VAL A 40 -24.580 -25.667 24.334 1.00 31.20 C ANISOU 320 CB VAL A 40 4720 3674 3459 -883 -854 523 C ATOM 321 CG1 VAL A 40 -23.981 -24.430 24.984 1.00 27.99 C ANISOU 321 CG1 VAL A 40 4257 3367 3010 -810 -791 499 C ATOM 322 CG2 VAL A 40 -25.356 -26.491 25.350 1.00 33.19 C ANISOU 322 CG2 VAL A 40 5090 3865 3656 -1025 -882 668 C ATOM 323 N THR A 41 -23.852 -24.620 21.496 1.00 27.42 N ANISOU 323 N THR A 41 4098 3247 3073 -655 -727 280 N ATOM 324 CA THR A 41 -23.097 -23.701 20.654 1.00 25.33 C ANISOU 324 CA THR A 41 3759 3025 2840 -517 -603 191 C ATOM 325 C THR A 41 -24.023 -22.843 19.797 1.00 23.76 C ANISOU 325 C THR A 41 3530 2930 2567 -544 -520 167 C ATOM 326 O THR A 41 -23.839 -21.632 19.691 1.00 23.32 O ANISOU 326 O THR A 41 3372 2981 2508 -502 -404 147 O ATOM 327 CB THR A 41 -22.119 -24.454 19.733 1.00 33.64 C ANISOU 327 CB THR A 41 4897 3924 3959 -369 -593 113 C ATOM 328 OG1 THR A 41 -21.574 -25.583 20.426 1.00 41.00 O ANISOU 328 OG1 THR A 41 5889 4723 4965 -365 -730 140 O ATOM 329 CG2 THR A 41 -20.990 -23.536 19.294 1.00 31.36 C ANISOU 329 CG2 THR A 41 4488 3655 3773 -220 -424 63 C ATOM 330 N ASN A 42 -25.029 -23.474 19.201 1.00 22.26 N ANISOU 330 N ASN A 42 3435 2686 2338 -619 -614 172 N ATOM 331 CA ASN A 42 -25.947 -22.764 18.323 1.00 19.77 C ANISOU 331 CA ASN A 42 3112 2427 1974 -641 -602 147 C ATOM 332 C ASN A 42 -26.997 -21.955 19.079 1.00 19.83 C ANISOU 332 C ASN A 42 2950 2579 2005 -764 -567 227 C ATOM 333 O ASN A 42 -27.670 -21.110 18.495 1.00 19.35 O ANISOU 333 O ASN A 42 2837 2582 1933 -769 -547 208 O ATOM 334 CB ASN A 42 -26.629 -23.743 17.368 1.00 21.87 C ANISOU 334 CB ASN A 42 3553 2537 2220 -670 -778 118 C ATOM 335 CG ASN A 42 -25.686 -24.267 16.303 1.00 25.95 C ANISOU 335 CG ASN A 42 4293 2906 2660 -500 -763 13 C ATOM 336 OD1 ASN A 42 -24.633 -23.682 16.048 1.00 27.26 O ANISOU 336 OD1 ASN A 42 4446 3104 2807 -356 -577 -33 O ATOM 337 ND2 ASN A 42 -26.063 -25.370 15.667 1.00 27.85 N ANISOU 337 ND2 ASN A 42 4745 2967 2871 -508 -949 -21 N ATOM 338 N TYR A 43 -27.140 -22.205 20.375 1.00 21.44 N ANISOU 338 N TYR A 43 3092 2817 2236 -850 -551 317 N ATOM 339 CA TYR A 43 -28.021 -21.374 21.189 1.00 21.27 C ANISOU 339 CA TYR A 43 2934 2927 2222 -931 -451 393 C ATOM 340 C TYR A 43 -27.404 -19.988 21.364 1.00 20.92 C ANISOU 340 C TYR A 43 2824 3003 2121 -832 -327 342 C ATOM 341 O TYR A 43 -28.107 -18.980 21.373 1.00 19.05 O ANISOU 341 O TYR A 43 2484 2871 1884 -845 -246 350 O ATOM 342 CB TYR A 43 -28.296 -22.032 22.543 1.00 21.62 C ANISOU 342 CB TYR A 43 3000 2950 2263 -1028 -429 512 C ATOM 343 CG TYR A 43 -29.034 -23.348 22.424 1.00 30.93 C ANISOU 343 CG TYR A 43 4217 3999 3536 -1152 -544 589 C ATOM 344 CD1 TYR A 43 -29.827 -23.621 21.315 1.00 34.64 C ANISOU 344 CD1 TYR A 43 4648 4404 4111 -1201 -665 567 C ATOM 345 CD2 TYR A 43 -28.932 -24.320 23.411 1.00 34.49 C ANISOU 345 CD2 TYR A 43 4764 4366 3976 -1221 -563 688 C ATOM 346 CE1 TYR A 43 -30.499 -24.822 21.193 1.00 35.51 C ANISOU 346 CE1 TYR A 43 4786 4363 4343 -1325 -814 639 C ATOM 347 CE2 TYR A 43 -29.602 -25.526 23.297 1.00 35.55 C ANISOU 347 CE2 TYR A 43 4926 4360 4221 -1347 -674 771 C ATOM 348 CZ TYR A 43 -30.384 -25.770 22.186 1.00 37.15 C ANISOU 348 CZ TYR A 43 5061 4496 4558 -1403 -805 745 C ATOM 349 OH TYR A 43 -31.056 -26.965 22.062 1.00 39.36 O ANISOU 349 OH TYR A 43 5363 4607 4985 -1538 -958 828 O ATOM 350 N PHE A 44 -26.081 -19.943 21.485 1.00 15.81 N ANISOU 350 N PHE A 44 2223 2321 1464 -732 -327 291 N ATOM 351 CA PHE A 44 -25.373 -18.670 21.557 1.00 14.91 C ANISOU 351 CA PHE A 44 2035 2282 1347 -644 -243 245 C ATOM 352 C PHE A 44 -25.339 -18.002 20.187 1.00 14.43 C ANISOU 352 C PHE A 44 1951 2238 1292 -574 -181 176 C ATOM 353 O PHE A 44 -25.340 -16.776 20.082 1.00 15.23 O ANISOU 353 O PHE A 44 1977 2423 1386 -540 -101 156 O ATOM 354 CB PHE A 44 -23.959 -18.871 22.097 1.00 15.13 C ANISOU 354 CB PHE A 44 2081 2229 1437 -567 -292 227 C ATOM 355 CG PHE A 44 -23.921 -19.234 23.555 1.00 25.33 C ANISOU 355 CG PHE A 44 3448 3495 2680 -618 -375 292 C ATOM 356 CD1 PHE A 44 -24.222 -18.289 24.523 1.00 28.71 C ANISOU 356 CD1 PHE A 44 3886 4001 3023 -632 -339 318 C ATOM 357 CD2 PHE A 44 -23.590 -20.516 23.957 1.00 22.36 C ANISOU 357 CD2 PHE A 44 3177 2998 2321 -638 -490 327 C ATOM 358 CE1 PHE A 44 -24.194 -18.617 25.867 1.00 29.16 C ANISOU 358 CE1 PHE A 44 4092 4008 2980 -660 -408 379 C ATOM 359 CE2 PHE A 44 -23.559 -20.851 25.299 1.00 25.32 C ANISOU 359 CE2 PHE A 44 3678 3326 2615 -678 -572 396 C ATOM 360 CZ PHE A 44 -23.861 -19.901 26.254 1.00 28.97 C ANISOU 360 CZ PHE A 44 4185 3860 2961 -686 -526 423 C ATOM 361 N VAL A 45 -25.316 -18.819 19.139 1.00 17.97 N ANISOU 361 N VAL A 45 2505 2587 1734 -544 -225 139 N ATOM 362 CA VAL A 45 -25.430 -18.322 17.774 1.00 16.70 C ANISOU 362 CA VAL A 45 2413 2409 1523 -473 -178 80 C ATOM 363 C VAL A 45 -26.764 -17.602 17.585 1.00 17.61 C ANISOU 363 C VAL A 45 2473 2608 1610 -549 -217 100 C ATOM 364 O VAL A 45 -26.820 -16.522 16.997 1.00 16.60 O ANISOU 364 O VAL A 45 2332 2530 1447 -497 -150 71 O ATOM 365 CB VAL A 45 -25.305 -19.464 16.742 1.00 20.96 C ANISOU 365 CB VAL A 45 3157 2792 2016 -420 -249 34 C ATOM 366 CG1 VAL A 45 -25.675 -18.975 15.348 1.00 19.82 C ANISOU 366 CG1 VAL A 45 3166 2605 1759 -351 -237 -22 C ATOM 367 CG2 VAL A 45 -23.896 -20.042 16.758 1.00 18.06 C ANISOU 367 CG2 VAL A 45 2824 2330 1707 -305 -166 7 C ATOM 368 N VAL A 46 -27.833 -18.202 18.101 1.00 18.76 N ANISOU 368 N VAL A 46 2572 2754 1801 -671 -321 159 N ATOM 369 CA VAL A 46 -29.158 -17.599 18.018 1.00 16.53 C ANISOU 369 CA VAL A 46 2180 2531 1569 -746 -360 193 C ATOM 370 C VAL A 46 -29.215 -16.294 18.810 1.00 14.69 C ANISOU 370 C VAL A 46 1801 2446 1336 -730 -213 212 C ATOM 371 O VAL A 46 -29.777 -15.305 18.339 1.00 18.91 O ANISOU 371 O VAL A 46 2275 3030 1879 -709 -202 194 O ATOM 372 CB VAL A 46 -30.249 -18.567 18.517 1.00 22.91 C ANISOU 372 CB VAL A 46 2919 3289 2497 -889 -464 281 C ATOM 373 CG1 VAL A 46 -31.573 -17.838 18.707 1.00 24.97 C ANISOU 373 CG1 VAL A 46 2985 3620 2884 -960 -450 340 C ATOM 374 CG2 VAL A 46 -30.408 -19.719 17.539 1.00 24.61 C ANISOU 374 CG2 VAL A 46 3296 3330 2726 -908 -672 250 C ATOM 375 N SER A 47 -28.627 -16.284 20.003 1.00 17.87 N ANISOU 375 N SER A 47 2178 2894 1718 -730 -127 244 N ATOM 376 CA ASER A 47 -28.567 -15.066 20.807 0.81 17.99 C ANISOU 376 CA ASER A 47 2116 3016 1703 -697 -13 248 C ATOM 377 CA BSER A 47 -28.568 -15.067 20.805 0.19 17.98 C ANISOU 377 CA BSER A 47 2115 3015 1702 -697 -13 248 C ATOM 378 C SER A 47 -27.837 -13.970 20.038 1.00 18.24 C ANISOU 378 C SER A 47 2150 3068 1714 -598 22 174 C ATOM 379 O SER A 47 -28.227 -12.802 20.074 1.00 13.73 O ANISOU 379 O SER A 47 1509 2569 1137 -573 76 163 O ATOM 380 CB ASER A 47 -27.876 -15.327 22.149 0.81 18.74 C ANISOU 380 CB ASER A 47 2267 3105 1749 -695 13 280 C ATOM 381 CB BSER A 47 -27.881 -15.330 22.146 0.19 18.53 C ANISOU 381 CB BSER A 47 2240 3079 1722 -696 13 281 C ATOM 382 OG ASER A 47 -27.813 -14.143 22.928 0.81 13.58 O ANISOU 382 OG ASER A 47 1593 2524 1041 -650 91 272 O ATOM 383 OG BSER A 47 -26.512 -15.647 21.965 0.19 17.33 O ANISOU 383 OG BSER A 47 2152 2851 1583 -631 -45 235 O ATOM 384 N LEU A 48 -26.780 -14.362 19.335 1.00 16.98 N ANISOU 384 N LEU A 48 2069 2827 1556 -535 10 133 N ATOM 385 CA LEU A 48 -26.008 -13.437 18.518 1.00 15.54 C ANISOU 385 CA LEU A 48 1894 2635 1376 -443 87 88 C ATOM 386 C LEU A 48 -26.851 -12.952 17.340 1.00 17.45 C ANISOU 386 C LEU A 48 2191 2878 1562 -429 72 66 C ATOM 387 O LEU A 48 -26.823 -11.772 16.984 1.00 16.80 O ANISOU 387 O LEU A 48 2084 2833 1467 -386 132 52 O ATOM 388 CB LEU A 48 -24.721 -14.112 18.031 1.00 12.81 C ANISOU 388 CB LEU A 48 1613 2180 1075 -367 128 66 C ATOM 389 CG LEU A 48 -23.699 -13.305 17.238 1.00 28.25 C ANISOU 389 CG LEU A 48 3560 4093 3082 -265 271 47 C ATOM 390 CD1 LEU A 48 -23.185 -12.132 18.057 1.00 19.77 C ANISOU 390 CD1 LEU A 48 2334 3068 2108 -268 294 63 C ATOM 391 CD2 LEU A 48 -22.549 -14.204 16.795 1.00 29.21 C ANISOU 391 CD2 LEU A 48 3728 4089 3283 -182 345 39 C ATOM 392 N ALA A 49 -27.612 -13.866 16.746 1.00 16.05 N ANISOU 392 N ALA A 49 2104 2637 1359 -469 -43 64 N ATOM 393 CA ALA A 49 -28.493 -13.526 15.634 1.00 16.58 C ANISOU 393 CA ALA A 49 2258 2664 1379 -459 -137 42 C ATOM 394 C ALA A 49 -29.614 -12.595 16.088 1.00 18.82 C ANISOU 394 C ALA A 49 2370 3043 1736 -512 -166 71 C ATOM 395 O ALA A 49 -30.035 -11.710 15.344 1.00 16.07 O ANISOU 395 O ALA A 49 2053 2689 1362 -472 -203 50 O ATOM 396 CB ALA A 49 -29.071 -14.788 15.005 1.00 17.11 C ANISOU 396 CB ALA A 49 2464 2603 1433 -499 -319 33 C ATOM 397 N ALA A 50 -30.090 -12.798 17.313 1.00 15.27 N ANISOU 397 N ALA A 50 1759 2668 1374 -589 -135 125 N ATOM 398 CA ALA A 50 -31.138 -11.952 17.878 1.00 20.03 C ANISOU 398 CA ALA A 50 2189 3357 2065 -618 -104 160 C ATOM 399 C ALA A 50 -30.649 -10.519 18.066 1.00 19.42 C ANISOU 399 C ALA A 50 2089 3356 1934 -536 8 125 C ATOM 400 O ALA A 50 -31.389 -9.565 17.830 1.00 19.09 O ANISOU 400 O ALA A 50 1972 3345 1935 -512 -4 119 O ATOM 401 CB ALA A 50 -31.626 -12.522 19.203 1.00 20.19 C ANISOU 401 CB ALA A 50 2093 3421 2156 -696 -26 236 C ATOM 402 N ALA A 51 -29.400 -10.377 18.500 1.00 14.70 N ANISOU 402 N ALA A 51 1546 2767 1272 -493 92 105 N ATOM 403 CA ALA A 51 -28.788 -9.063 18.652 1.00 14.30 C ANISOU 403 CA ALA A 51 1479 2753 1200 -425 166 76 C ATOM 404 C ALA A 51 -28.705 -8.353 17.306 1.00 14.05 C ANISOU 404 C ALA A 51 1521 2678 1141 -369 151 47 C ATOM 405 O ALA A 51 -28.962 -7.155 17.207 1.00 15.02 O ANISOU 405 O ALA A 51 1608 2830 1268 -332 168 36 O ATOM 406 CB ALA A 51 -27.403 -9.186 19.273 1.00 14.99 C ANISOU 406 CB ALA A 51 1594 2811 1289 -400 205 70 C ATOM 407 N ASP A 52 -28.353 -9.103 16.268 1.00 13.26 N ANISOU 407 N ASP A 52 1559 2489 992 -352 121 37 N ATOM 408 CA ASP A 52 -28.205 -8.529 14.936 1.00 18.75 C ANISOU 408 CA ASP A 52 2406 3111 1607 -283 129 18 C ATOM 409 C ASP A 52 -29.560 -8.165 14.325 1.00 17.99 C ANISOU 409 C ASP A 52 2335 3000 1501 -296 -30 11 C ATOM 410 O ASP A 52 -29.662 -7.202 13.563 1.00 15.48 O ANISOU 410 O ASP A 52 2106 2649 1128 -240 -39 2 O ATOM 411 CB ASP A 52 -27.441 -9.492 14.025 1.00 18.70 C ANISOU 411 CB ASP A 52 2599 2989 1518 -235 168 5 C ATOM 412 CG ASP A 52 -25.964 -9.585 14.382 1.00 26.12 C ANISOU 412 CG ASP A 52 3491 3912 2523 -193 345 19 C ATOM 413 OD1 ASP A 52 -25.415 -8.604 14.939 1.00 25.67 O ANISOU 413 OD1 ASP A 52 3298 3900 2556 -188 426 37 O ATOM 414 OD2 ASP A 52 -25.347 -10.635 14.103 1.00 34.88 O ANISOU 414 OD2 ASP A 52 4691 4942 3620 -161 385 12 O ATOM 415 N ILE A 53 -30.596 -8.930 14.660 1.00 18.70 N ANISOU 415 N ILE A 53 2336 3095 1673 -371 -165 25 N ATOM 416 CA ILE A 53 -31.954 -8.592 14.245 1.00 19.00 C ANISOU 416 CA ILE A 53 2318 3106 1797 -392 -344 31 C ATOM 417 C ILE A 53 -32.385 -7.267 14.875 1.00 15.99 C ANISOU 417 C ILE A 53 1757 2822 1496 -368 -269 39 C ATOM 418 O ILE A 53 -32.975 -6.414 14.211 1.00 18.40 O ANISOU 418 O ILE A 53 2085 3089 1818 -326 -372 26 O ATOM 419 CB ILE A 53 -32.961 -9.703 14.624 1.00 21.86 C ANISOU 419 CB ILE A 53 2551 3440 2316 -494 -481 70 C ATOM 420 CG1 ILE A 53 -32.713 -10.955 13.781 1.00 22.91 C ANISOU 420 CG1 ILE A 53 2907 3431 2367 -509 -628 48 C ATOM 421 CG2 ILE A 53 -34.394 -9.225 14.428 1.00 22.11 C ANISOU 421 CG2 ILE A 53 2418 3442 2539 -521 -649 93 C ATOM 422 CD1 ILE A 53 -33.563 -12.148 14.178 1.00 22.32 C ANISOU 422 CD1 ILE A 53 2709 3303 2467 -626 -772 96 C ATOM 423 N LEU A 54 -32.068 -7.093 16.155 1.00 13.48 N ANISOU 423 N LEU A 54 1298 2610 1212 -382 -105 55 N ATOM 424 CA LEU A 54 -32.389 -5.856 16.862 1.00 16.64 C ANISOU 424 CA LEU A 54 1572 3089 1660 -338 -18 51 C ATOM 425 C LEU A 54 -31.568 -4.671 16.354 1.00 16.45 C ANISOU 425 C LEU A 54 1659 3048 1545 -263 19 17 C ATOM 426 O LEU A 54 -31.970 -3.518 16.509 1.00 16.77 O ANISOU 426 O LEU A 54 1639 3111 1620 -215 27 3 O ATOM 427 CB LEU A 54 -32.176 -6.031 18.367 1.00 18.54 C ANISOU 427 CB LEU A 54 1726 3412 1906 -356 133 71 C ATOM 428 CG LEU A 54 -33.145 -6.983 19.068 1.00 23.33 C ANISOU 428 CG LEU A 54 2203 4039 2624 -427 161 133 C ATOM 429 CD1 LEU A 54 -32.791 -7.138 20.542 1.00 22.17 C ANISOU 429 CD1 LEU A 54 2076 3936 2413 -420 321 154 C ATOM 430 CD2 LEU A 54 -34.576 -6.495 18.905 1.00 27.22 C ANISOU 430 CD2 LEU A 54 2511 4530 3302 -419 129 160 C ATOM 431 N VAL A 55 -30.415 -4.949 15.754 1.00 14.32 N ANISOU 431 N VAL A 55 1540 2722 1178 -249 60 11 N ATOM 432 CA VAL A 55 -29.636 -3.893 15.120 1.00 12.11 C ANISOU 432 CA VAL A 55 1362 2396 844 -189 120 5 C ATOM 433 C VAL A 55 -30.423 -3.325 13.940 1.00 15.31 C ANISOU 433 C VAL A 55 1885 2729 1202 -149 -3 1 C ATOM 434 O VAL A 55 -30.489 -2.110 13.749 1.00 16.36 O ANISOU 434 O VAL A 55 2029 2851 1337 -104 0 0 O ATOM 435 CB VAL A 55 -28.253 -4.396 14.639 1.00 14.16 C ANISOU 435 CB VAL A 55 1740 2587 1052 -173 237 20 C ATOM 436 CG1 VAL A 55 -27.587 -3.363 13.737 1.00 12.48 C ANISOU 436 CG1 VAL A 55 1646 2296 799 -113 329 43 C ATOM 437 CG2 VAL A 55 -27.360 -4.721 15.830 1.00 14.84 C ANISOU 437 CG2 VAL A 55 1701 2715 1222 -202 312 25 C ATOM 438 N GLY A 56 -31.038 -4.211 13.165 1.00 15.87 N ANISOU 438 N GLY A 56 2064 2730 1234 -165 -146 -2 N ATOM 439 CA GLY A 56 -31.816 -3.795 12.011 1.00 15.96 C ANISOU 439 CA GLY A 56 2237 2635 1193 -124 -333 -10 C ATOM 440 C GLY A 56 -33.127 -3.129 12.384 1.00 17.79 C ANISOU 440 C GLY A 56 2264 2900 1597 -130 -480 -13 C ATOM 441 O GLY A 56 -33.528 -2.140 11.772 1.00 22.27 O ANISOU 441 O GLY A 56 2905 3406 2152 -74 -581 -17 O ATOM 442 N VAL A 57 -33.792 -3.669 13.400 1.00 19.66 N ANISOU 442 N VAL A 57 2245 3220 2005 -190 -471 0 N ATOM 443 CA VAL A 57 -35.109 -3.186 13.804 1.00 22.67 C ANISOU 443 CA VAL A 57 2386 3620 2606 -188 -565 11 C ATOM 444 C VAL A 57 -35.047 -1.909 14.651 1.00 20.65 C ANISOU 444 C VAL A 57 2005 3457 2384 -125 -403 -2 C ATOM 445 O VAL A 57 -35.887 -1.020 14.501 1.00 24.29 O ANISOU 445 O VAL A 57 2372 3891 2967 -70 -492 -8 O ATOM 446 CB VAL A 57 -35.875 -4.280 14.589 1.00 25.48 C ANISOU 446 CB VAL A 57 2512 4013 3157 -274 -561 53 C ATOM 447 CG1 VAL A 57 -37.178 -3.736 15.168 1.00 31.55 C ANISOU 447 CG1 VAL A 57 2979 4805 4203 -259 -566 84 C ATOM 448 CG2 VAL A 57 -36.143 -5.484 13.698 1.00 25.45 C ANISOU 448 CG2 VAL A 57 2626 3880 3163 -338 -794 61 C ATOM 449 N LEU A 58 -34.054 -1.812 15.530 1.00 17.99 N ANISOU 449 N LEU A 58 1680 3205 1950 -125 -196 -10 N ATOM 450 CA LEU A 58 -33.998 -0.702 16.479 1.00 20.03 C ANISOU 450 CA LEU A 58 1854 3528 2230 -62 -67 -32 C ATOM 451 C LEU A 58 -32.755 0.178 16.350 1.00 14.72 C ANISOU 451 C LEU A 58 1333 2833 1428 -27 -7 -54 C ATOM 452 O LEU A 58 -32.869 1.396 16.216 1.00 15.77 O ANISOU 452 O LEU A 58 1483 2937 1573 37 -31 -73 O ATOM 453 CB LEU A 58 -34.093 -1.233 17.911 1.00 19.38 C ANISOU 453 CB LEU A 58 1650 3535 2178 -83 98 -19 C ATOM 454 CG LEU A 58 -35.442 -1.840 18.307 1.00 20.03 C ANISOU 454 CG LEU A 58 1521 3637 2452 -108 115 27 C ATOM 455 CD1 LEU A 58 -35.401 -2.353 19.739 1.00 18.85 C ANISOU 455 CD1 LEU A 58 1326 3561 2277 -119 329 54 C ATOM 456 CD2 LEU A 58 -36.563 -0.824 18.124 1.00 24.52 C ANISOU 456 CD2 LEU A 58 1940 4181 3196 -27 70 20 C ATOM 457 N ALA A 59 -31.575 -0.431 16.400 1.00 12.69 N ANISOU 457 N ALA A 59 1165 2571 1085 -70 66 -43 N ATOM 458 CA ALA A 59 -30.327 0.333 16.430 1.00 16.92 C ANISOU 458 CA ALA A 59 1782 3068 1579 -52 135 -45 C ATOM 459 C ALA A 59 -30.126 1.203 15.189 1.00 15.89 C ANISOU 459 C ALA A 59 1786 2843 1409 -16 99 -26 C ATOM 460 O ALA A 59 -29.686 2.346 15.293 1.00 16.68 O ANISOU 460 O ALA A 59 1901 2904 1533 14 120 -26 O ATOM 461 CB ALA A 59 -29.137 -0.603 16.604 1.00 17.37 C ANISOU 461 CB ALA A 59 1872 3114 1615 -101 211 -25 C ATOM 462 N ILE A 60 -30.439 0.667 14.014 1.00 13.51 N ANISOU 462 N ILE A 60 1616 2481 1035 -17 32 -7 N ATOM 463 CA ILE A 60 -30.258 1.441 12.789 1.00 14.03 C ANISOU 463 CA ILE A 60 1883 2434 1015 28 8 22 C ATOM 464 C ILE A 60 -31.298 2.568 12.663 1.00 15.79 C ANISOU 464 C ILE A 60 2080 2634 1286 81 -139 3 C ATOM 465 O ILE A 60 -30.933 3.688 12.311 1.00 17.35 O ANISOU 465 O ILE A 60 2367 2763 1461 117 -117 24 O ATOM 466 CB ILE A 60 -30.275 0.530 11.538 1.00 20.29 C ANISOU 466 CB ILE A 60 2915 3132 1662 36 -39 41 C ATOM 467 CG1 ILE A 60 -28.981 -0.291 11.479 1.00 19.53 C ANISOU 467 CG1 ILE A 60 2878 3022 1520 17 162 69 C ATOM 468 CG2 ILE A 60 -30.439 1.354 10.264 1.00 16.28 C ANISOU 468 CG2 ILE A 60 2675 2485 1024 100 -108 70 C ATOM 469 CD1 ILE A 60 -28.881 -1.212 10.277 1.00 17.89 C ANISOU 469 CD1 ILE A 60 2959 2703 1137 51 157 79 C ATOM 470 N PRO A 61 -32.588 2.294 12.958 1.00 18.88 N ANISOU 470 N PRO A 61 2330 3066 1776 87 -283 -28 N ATOM 471 CA PRO A 61 -33.502 3.444 13.027 1.00 21.80 C ANISOU 471 CA PRO A 61 2623 3414 2246 154 -395 -49 C ATOM 472 C PRO A 61 -33.078 4.492 14.058 1.00 20.16 C ANISOU 472 C PRO A 61 2319 3257 2085 188 -269 -73 C ATOM 473 O PRO A 61 -33.266 5.687 13.823 1.00 19.99 O ANISOU 473 O PRO A 61 2341 3171 2082 250 -330 -81 O ATOM 474 CB PRO A 61 -34.834 2.806 13.426 1.00 16.78 C ANISOU 474 CB PRO A 61 1769 2821 1785 146 -504 -63 C ATOM 475 CG PRO A 61 -34.763 1.438 12.855 1.00 19.02 C ANISOU 475 CG PRO A 61 2140 3076 2011 77 -571 -43 C ATOM 476 CD PRO A 61 -33.325 1.016 13.010 1.00 15.49 C ANISOU 476 CD PRO A 61 1818 2664 1404 39 -372 -32 C ATOM 477 N PHE A 62 -32.519 4.047 15.181 1.00 17.17 N ANISOU 477 N PHE A 62 1841 2967 1715 154 -126 -89 N ATOM 478 CA PHE A 62 -31.998 4.964 16.190 1.00 15.59 C ANISOU 478 CA PHE A 62 1611 2779 1532 189 -49 -121 C ATOM 479 C PHE A 62 -30.845 5.785 15.623 1.00 16.07 C ANISOU 479 C PHE A 62 1810 2740 1557 175 -36 -88 C ATOM 480 O PHE A 62 -30.777 6.994 15.835 1.00 16.35 O ANISOU 480 O PHE A 62 1868 2718 1628 223 -71 -106 O ATOM 481 CB PHE A 62 -31.527 4.208 17.438 1.00 13.67 C ANISOU 481 CB PHE A 62 1302 2616 1275 154 59 -139 C ATOM 482 CG PHE A 62 -32.643 3.688 18.301 1.00 18.36 C ANISOU 482 CG PHE A 62 1763 3295 1917 183 109 -159 C ATOM 483 CD1 PHE A 62 -33.969 3.912 17.967 1.00 20.38 C ANISOU 483 CD1 PHE A 62 1905 3554 2285 235 58 -159 C ATOM 484 CD2 PHE A 62 -32.359 2.980 19.460 1.00 16.92 C ANISOU 484 CD2 PHE A 62 1567 3171 1689 162 213 -166 C ATOM 485 CE1 PHE A 62 -34.990 3.429 18.766 1.00 20.86 C ANISOU 485 CE1 PHE A 62 1803 3678 2446 260 154 -154 C ATOM 486 CE2 PHE A 62 -33.375 2.496 20.263 1.00 16.53 C ANISOU 486 CE2 PHE A 62 1412 3187 1682 191 316 -161 C ATOM 487 CZ PHE A 62 -34.692 2.722 19.917 1.00 21.34 C ANISOU 487 CZ PHE A 62 1869 3802 2437 238 309 -149 C ATOM 488 N ALA A 63 -29.943 5.117 14.907 1.00 13.79 N ANISOU 488 N ALA A 63 1610 2415 1216 115 30 -33 N ATOM 489 CA ALA A 63 -28.789 5.773 14.295 1.00 14.13 C ANISOU 489 CA ALA A 63 1758 2345 1264 95 104 30 C ATOM 490 C ALA A 63 -29.217 6.812 13.264 1.00 17.93 C ANISOU 490 C ALA A 63 2389 2723 1700 143 34 62 C ATOM 491 O ALA A 63 -28.628 7.889 13.173 1.00 16.42 O ANISOU 491 O ALA A 63 2240 2437 1563 145 57 98 O ATOM 492 CB ALA A 63 -27.870 4.739 13.651 1.00 14.04 C ANISOU 492 CB ALA A 63 1815 2308 1213 46 237 90 C ATOM 493 N ILE A 64 -30.239 6.479 12.482 1.00 21.20 N ANISOU 493 N ILE A 64 2894 3132 2030 178 -79 53 N ATOM 494 CA ILE A 64 -30.773 7.405 11.491 1.00 21.38 C ANISOU 494 CA ILE A 64 3093 3037 1995 235 -200 79 C ATOM 495 C ILE A 64 -31.345 8.644 12.181 1.00 21.12 C ANISOU 495 C ILE A 64 2946 3002 2077 292 -298 31 C ATOM 496 O ILE A 64 -31.090 9.774 11.762 1.00 18.05 O ANISOU 496 O ILE A 64 2674 2499 1684 318 -322 68 O ATOM 497 CB ILE A 64 -31.857 6.731 10.622 1.00 19.65 C ANISOU 497 CB ILE A 64 2985 2788 1694 266 -383 67 C ATOM 498 CG1 ILE A 64 -31.228 5.662 9.724 1.00 19.53 C ANISOU 498 CG1 ILE A 64 3189 2722 1511 236 -295 113 C ATOM 499 CG2 ILE A 64 -32.592 7.761 9.779 1.00 21.07 C ANISOU 499 CG2 ILE A 64 3330 2834 1842 339 -580 80 C ATOM 500 CD1 ILE A 64 -32.239 4.775 9.016 1.00 19.03 C ANISOU 500 CD1 ILE A 64 3240 2613 1376 253 -519 86 C ATOM 501 N THR A 65 -32.096 8.423 13.255 1.00 16.75 N ANISOU 501 N THR A 65 2180 2561 1625 320 -331 -45 N ATOM 502 CA THR A 65 -32.697 9.512 14.019 1.00 20.64 C ANISOU 502 CA THR A 65 2574 3049 2218 403 -391 -105 C ATOM 503 C THR A 65 -31.631 10.412 14.651 1.00 21.07 C ANISOU 503 C THR A 65 2663 3051 2291 390 -321 -107 C ATOM 504 O THR A 65 -31.774 11.634 14.680 1.00 22.88 O ANISOU 504 O THR A 65 2940 3190 2562 451 -399 -124 O ATOM 505 CB THR A 65 -33.625 8.968 15.125 1.00 23.52 C ANISOU 505 CB THR A 65 2722 3538 2675 446 -358 -173 C ATOM 506 OG1 THR A 65 -34.510 7.988 14.569 1.00 25.48 O ANISOU 506 OG1 THR A 65 2900 3817 2963 428 -435 -154 O ATOM 507 CG2 THR A 65 -34.448 10.089 15.740 1.00 29.07 C ANISOU 507 CG2 THR A 65 3348 4216 3482 570 -401 -235 C ATOM 508 N AILE A 66 -30.561 9.804 15.152 0.50 21.06 N ANISOU 508 N AILE A 66 2634 3084 2283 311 -205 -90 N ATOM 509 N BILE A 66 -30.573 9.782 15.156 0.50 21.08 N ANISOU 509 N BILE A 66 2635 3089 2285 311 -205 -90 N ATOM 510 CA AILE A 66 -29.476 10.556 15.775 0.50 22.98 C ANISOU 510 CA AILE A 66 2890 3246 2596 282 -190 -86 C ATOM 511 CA BILE A 66 -29.436 10.474 15.757 0.50 23.51 C ANISOU 511 CA BILE A 66 2955 3317 2661 276 -182 -83 C ATOM 512 C AILE A 66 -28.750 11.443 14.764 0.50 24.48 C ANISOU 512 C AILE A 66 3201 3279 2820 245 -185 9 C ATOM 513 C BILE A 66 -28.757 11.418 14.771 0.50 24.44 C ANISOU 513 C BILE A 66 3195 3277 2814 245 -184 8 C ATOM 514 O AILE A 66 -28.329 12.555 15.091 0.50 26.00 O ANISOU 514 O AILE A 66 3416 3358 3103 251 -248 9 O ATOM 515 O BILE A 66 -28.373 12.536 15.122 0.50 25.90 O ANISOU 515 O BILE A 66 3401 3352 3088 254 -251 4 O ATOM 516 CB AILE A 66 -28.463 9.611 16.457 0.50 26.97 C ANISOU 516 CB AILE A 66 3322 3795 3129 202 -104 -77 C ATOM 517 CB BILE A 66 -28.392 9.461 16.282 0.50 26.14 C ANISOU 517 CB BILE A 66 3220 3692 3019 190 -87 -63 C ATOM 518 CG1AILE A 66 -29.091 8.978 17.695 0.50 29.06 C ANISOU 518 CG1AILE A 66 3511 4180 3349 246 -107 -166 C ATOM 519 CG1BILE A 66 -28.877 8.816 17.578 0.50 28.73 C ANISOU 519 CG1BILE A 66 3469 4136 3312 224 -93 -150 C ATOM 520 CG2AILE A 66 -27.201 10.354 16.860 0.50 32.22 C ANISOU 520 CG2AILE A 66 3988 4326 3930 151 -134 -47 C ATOM 521 CG2BILE A 66 -27.049 10.130 16.522 0.50 30.87 C ANISOU 521 CG2BILE A 66 3817 4156 3758 129 -94 -17 C ATOM 522 CD1AILE A 66 -28.158 8.059 18.443 0.50 27.89 C ANISOU 522 CD1AILE A 66 3324 4058 3216 177 -66 -162 C ATOM 523 CD1BILE A 66 -28.849 9.746 18.758 0.50 30.72 C ANISOU 523 CD1BILE A 66 3754 4333 3584 290 -176 -229 C ATOM 524 N SER A 67 -28.622 10.960 13.531 1.00 24.01 N ANISOU 524 N SER A 67 3251 3193 2680 214 -108 95 N ATOM 525 CA SER A 67 -27.922 11.711 12.491 1.00 25.02 C ANISOU 525 CA SER A 67 3536 3159 2812 184 -41 212 C ATOM 526 C SER A 67 -28.576 13.061 12.187 1.00 25.99 C ANISOU 526 C SER A 67 3767 3174 2933 251 -191 206 C ATOM 527 O SER A 67 -27.925 13.959 11.653 1.00 26.31 O ANISOU 527 O SER A 67 3916 3059 3022 220 -149 301 O ATOM 528 CB SER A 67 -27.831 10.880 11.207 1.00 21.98 C ANISOU 528 CB SER A 67 3329 2753 2270 174 79 293 C ATOM 529 OG SER A 67 -29.095 10.779 10.573 1.00 21.57 O ANISOU 529 OG SER A 67 3409 2713 2074 248 -83 252 O ATOM 530 N THR A 68 -29.853 13.205 12.533 1.00 29.05 N ANISOU 530 N THR A 68 4112 3631 3295 344 -353 104 N ATOM 531 CA THR A 68 -30.571 14.455 12.294 1.00 28.61 C ANISOU 531 CA THR A 68 4142 3469 3260 429 -516 85 C ATOM 532 C THR A 68 -30.274 15.511 13.356 1.00 29.25 C ANISOU 532 C THR A 68 4149 3495 3470 454 -570 26 C ATOM 533 O THR A 68 -30.440 16.704 13.111 1.00 28.76 O ANISOU 533 O THR A 68 4186 3295 3445 500 -681 37 O ATOM 534 CB THR A 68 -32.100 14.238 12.240 1.00 29.32 C ANISOU 534 CB THR A 68 4177 3628 3337 536 -674 3 C ATOM 535 OG1 THR A 68 -32.591 13.901 13.544 1.00 25.04 O ANISOU 535 OG1 THR A 68 3414 3221 2879 582 -649 -105 O ATOM 536 CG2 THR A 68 -32.449 13.133 11.260 1.00 26.60 C ANISOU 536 CG2 THR A 68 3919 3311 2876 510 -688 46 C ATOM 537 N GLY A 69 -29.842 15.073 14.534 1.00 29.84 N ANISOU 537 N GLY A 69 4085 3654 3598 430 -518 -39 N ATOM 538 CA GLY A 69 -29.567 15.991 15.627 1.00 30.11 C ANISOU 538 CA GLY A 69 4104 3614 3724 467 -606 -113 C ATOM 539 C GLY A 69 -30.828 16.658 16.148 1.00 29.25 C ANISOU 539 C GLY A 69 3996 3517 3599 628 -713 -230 C ATOM 540 O GLY A 69 -30.794 17.796 16.619 1.00 30.40 O ANISOU 540 O GLY A 69 4214 3537 3798 693 -823 -281 O ATOM 541 N PHE A 70 -31.941 15.936 16.062 1.00 23.98 N ANISOU 541 N PHE A 70 3239 2985 2888 697 -679 -269 N ATOM 542 CA PHE A 70 -33.248 16.440 16.477 1.00 26.59 C ANISOU 542 CA PHE A 70 3512 3330 3260 863 -737 -364 C ATOM 543 C PHE A 70 -33.279 16.837 17.952 1.00 25.46 C ANISOU 543 C PHE A 70 3373 3189 3112 965 -698 -481 C ATOM 544 O PHE A 70 -32.496 16.336 18.759 1.00 21.79 O ANISOU 544 O PHE A 70 2929 2761 2591 905 -633 -499 O ATOM 545 CB PHE A 70 -34.329 15.388 16.203 1.00 25.61 C ANISOU 545 CB PHE A 70 3232 3342 3156 890 -692 -363 C ATOM 546 CG PHE A 70 -34.295 14.221 17.154 1.00 27.89 C ANISOU 546 CG PHE A 70 3400 3787 3410 861 -527 -395 C ATOM 547 CD1 PHE A 70 -33.213 13.358 17.178 1.00 27.60 C ANISOU 547 CD1 PHE A 70 3394 3799 3293 721 -451 -346 C ATOM 548 CD2 PHE A 70 -35.349 13.988 18.021 1.00 33.52 C ANISOU 548 CD2 PHE A 70 3969 4582 4186 980 -431 -464 C ATOM 549 CE1 PHE A 70 -33.177 12.290 18.055 1.00 33.63 C ANISOU 549 CE1 PHE A 70 4072 4688 4017 696 -322 -371 C ATOM 550 CE2 PHE A 70 -35.322 12.920 18.897 1.00 32.02 C ANISOU 550 CE2 PHE A 70 3701 4517 3947 952 -262 -476 C ATOM 551 CZ PHE A 70 -34.236 12.070 18.914 1.00 34.68 C ANISOU 551 CZ PHE A 70 4095 4899 4181 807 -228 -433 C ATOM 552 N CYS A 71 -34.189 17.743 18.293 1.00 25.55 N ANISOU 552 N CYS A 71 3394 3140 3175 1135 -747 -562 N ATOM 553 CA CYS A 71 -34.367 18.169 19.676 1.00 27.23 C ANISOU 553 CA CYS A 71 3672 3332 3344 1277 -689 -685 C ATOM 554 C CYS A 71 -35.004 17.054 20.496 1.00 30.12 C ANISOU 554 C CYS A 71 3912 3867 3665 1328 -473 -720 C ATOM 555 O CYS A 71 -35.971 16.431 20.061 1.00 30.64 O ANISOU 555 O CYS A 71 3781 4033 3826 1350 -396 -685 O ATOM 556 CB CYS A 71 -35.226 19.435 19.747 1.00 30.11 C ANISOU 556 CB CYS A 71 4083 3573 3785 1470 -769 -762 C ATOM 557 SG CYS A 71 -34.476 20.898 18.991 1.00 44.40 S ANISOU 557 SG CYS A 71 6086 5143 5642 1423 -1028 -725 S ATOM 558 N ALA A 72 -34.460 16.804 21.681 1.00 24.95 N ANISOU 558 N ALA A 72 3384 3219 2877 1345 -396 -781 N ATOM 559 CA ALA A 72 -34.972 15.741 22.536 1.00 25.07 C ANISOU 559 CA ALA A 72 3329 3375 2820 1390 -167 -798 C ATOM 560 C ALA A 72 -34.591 15.959 23.990 1.00 27.52 C ANISOU 560 C ALA A 72 3895 3618 2942 1496 -112 -900 C ATOM 561 O ALA A 72 -33.586 16.606 24.287 1.00 28.58 O ANISOU 561 O ALA A 72 4242 3608 3009 1464 -305 -941 O ATOM 562 CB ALA A 72 -34.458 14.390 22.061 1.00 27.26 C ANISOU 562 CB ALA A 72 3487 3780 3091 1195 -134 -700 C ATOM 563 N ALA A 73 -35.402 15.418 24.895 1.00 31.37 N ANISOU 563 N ALA A 73 4379 4188 3353 1627 146 -933 N ATOM 564 CA ALA A 73 -35.028 15.357 26.299 1.00 34.09 C ANISOU 564 CA ALA A 73 5030 4471 3453 1725 223 -1016 C ATOM 565 C ALA A 73 -33.722 14.582 26.401 1.00 27.08 C ANISOU 565 C ALA A 73 4226 3587 2476 1525 68 -973 C ATOM 566 O ALA A 73 -33.573 13.529 25.777 1.00 25.26 O ANISOU 566 O ALA A 73 3782 3490 2327 1362 107 -873 O ATOM 567 CB ALA A 73 -36.121 14.702 27.126 1.00 37.04 C ANISOU 567 CB ALA A 73 5354 4939 3782 1840 580 -997 C ATOM 568 N CYS A 74 -32.774 15.112 27.167 1.00 23.65 N ANISOU 568 N CYS A 74 1916 3694 3377 1167 -834 -698 N ATOM 569 CA CYS A 74 -31.412 14.588 27.166 1.00 24.43 C ANISOU 569 CA CYS A 74 2043 3723 3518 1099 -850 -725 C ATOM 570 C CYS A 74 -31.338 13.099 27.498 1.00 25.08 C ANISOU 570 C CYS A 74 2164 3955 3410 1058 -775 -683 C ATOM 571 O CYS A 74 -30.598 12.358 26.858 1.00 22.15 O ANISOU 571 O CYS A 74 1795 3559 3061 951 -747 -605 O ATOM 572 CB CYS A 74 -30.537 15.378 28.139 1.00 29.21 C ANISOU 572 CB CYS A 74 2673 4200 4224 1183 -966 -934 C ATOM 573 SG CYS A 74 -28.776 14.990 27.998 1.00 40.85 S ANISOU 573 SG CYS A 74 4137 5516 5869 1089 -1012 -987 S ATOM 574 N HIS A 75 -32.110 12.654 28.484 1.00 22.32 N ANISOU 574 N HIS A 75 1839 3763 2880 1163 -731 -730 N ATOM 575 CA HIS A 75 -32.076 11.244 28.866 1.00 24.68 C ANISOU 575 CA HIS A 75 2167 4206 3005 1153 -647 -683 C ATOM 576 C HIS A 75 -32.790 10.369 27.838 1.00 23.37 C ANISOU 576 C HIS A 75 1940 4102 2837 1013 -556 -504 C ATOM 577 O HIS A 75 -32.514 9.173 27.725 1.00 24.19 O ANISOU 577 O HIS A 75 2058 4270 2862 943 -498 -439 O ATOM 578 CB HIS A 75 -32.681 11.055 30.255 1.00 28.62 C ANISOU 578 CB HIS A 75 2705 4867 3303 1361 -603 -770 C ATOM 579 CG HIS A 75 -31.884 11.703 31.343 1.00 29.94 C ANISOU 579 CG HIS A 75 2978 4980 3417 1530 -734 -981 C ATOM 580 ND1 HIS A 75 -30.887 11.044 32.031 1.00 32.72 N ANISOU 580 ND1 HIS A 75 3434 5344 3656 1601 -791 -1073 N ATOM 581 CD2 HIS A 75 -31.918 12.960 31.846 1.00 31.37 C ANISOU 581 CD2 HIS A 75 3186 5077 3655 1647 -850 -1138 C ATOM 582 CE1 HIS A 75 -30.350 11.863 32.916 1.00 28.76 C ANISOU 582 CE1 HIS A 75 3022 4764 3140 1759 -953 -1292 C ATOM 583 NE2 HIS A 75 -30.957 13.032 32.825 1.00 35.34 N ANISOU 583 NE2 HIS A 75 3808 5541 4077 1785 -991 -1337 N ATOM 584 N GLY A 76 -33.705 10.970 27.086 1.00 26.64 N ANISOU 584 N GLY A 76 2291 4484 3346 984 -567 -441 N ATOM 585 CA GLY A 76 -34.340 10.283 25.978 1.00 27.00 C ANISOU 585 CA GLY A 76 2293 4547 3418 866 -545 -310 C ATOM 586 C GLY A 76 -33.326 10.086 24.870 1.00 23.76 C ANISOU 586 C GLY A 76 1939 4042 3046 761 -589 -248 C ATOM 587 O GLY A 76 -33.229 9.008 24.285 1.00 21.39 O ANISOU 587 O GLY A 76 1657 3777 2694 669 -564 -175 O ATOM 588 N CYS A 77 -32.564 11.139 24.594 1.00 23.01 N ANISOU 588 N CYS A 77 1858 3826 3057 793 -649 -280 N ATOM 589 CA CYS A 77 -31.490 11.080 23.611 1.00 24.19 C ANISOU 589 CA CYS A 77 2027 3891 3274 741 -667 -222 C ATOM 590 C CYS A 77 -30.434 10.074 24.043 1.00 24.48 C ANISOU 590 C CYS A 77 2091 3946 3265 678 -622 -249 C ATOM 591 O CYS A 77 -29.862 9.363 23.217 1.00 17.46 O ANISOU 591 O CYS A 77 1215 3063 2355 612 -599 -175 O ATOM 592 CB CYS A 77 -30.855 12.460 23.417 1.00 23.93 C ANISOU 592 CB CYS A 77 1958 3695 3441 812 -718 -264 C ATOM 593 SG CYS A 77 -29.382 12.453 22.367 1.00 28.64 S ANISOU 593 SG CYS A 77 2560 4115 4208 762 -666 -188 S ATOM 594 N LEU A 78 -30.187 10.019 25.347 1.00 19.68 N ANISOU 594 N LEU A 78 1501 3357 2620 728 -623 -364 N ATOM 595 CA LEU A 78 -29.214 9.093 25.911 1.00 19.85 C ANISOU 595 CA LEU A 78 1562 3392 2587 703 -608 -409 C ATOM 596 C LEU A 78 -29.567 7.642 25.609 1.00 17.44 C ANISOU 596 C LEU A 78 1285 3208 2133 622 -529 -308 C ATOM 597 O LEU A 78 -28.694 6.844 25.264 1.00 16.32 O ANISOU 597 O LEU A 78 1165 3048 1987 550 -511 -280 O ATOM 598 CB LEU A 78 -29.111 9.287 27.423 1.00 24.44 C ANISOU 598 CB LEU A 78 2187 4006 3094 838 -651 -566 C ATOM 599 CG LEU A 78 -27.853 9.909 28.020 1.00 29.10 C ANISOU 599 CG LEU A 78 2791 4445 3819 890 -762 -729 C ATOM 600 CD1 LEU A 78 -27.898 9.761 29.533 1.00 24.45 C ANISOU 600 CD1 LEU A 78 2293 3940 3058 1070 -822 -893 C ATOM 601 CD2 LEU A 78 -26.592 9.280 27.445 1.00 18.91 C ANISOU 601 CD2 LEU A 78 1479 3061 2644 781 -756 -697 C ATOM 602 N PHE A 79 -30.846 7.304 25.742 1.00 17.05 N ANISOU 602 N PHE A 79 1214 3271 1994 636 -482 -261 N ATOM 603 CA PHE A 79 -31.285 5.929 25.535 1.00 19.84 C ANISOU 603 CA PHE A 79 1562 3722 2253 561 -411 -176 C ATOM 604 C PHE A 79 -31.101 5.485 24.088 1.00 18.39 C ANISOU 604 C PHE A 79 1403 3481 2102 441 -434 -88 C ATOM 605 O PHE A 79 -30.582 4.400 23.829 1.00 18.83 O ANISOU 605 O PHE A 79 1496 3556 2104 368 -403 -50 O ATOM 606 CB PHE A 79 -32.750 5.747 25.942 1.00 17.45 C ANISOU 606 CB PHE A 79 1171 3531 1928 605 -355 -145 C ATOM 607 CG PHE A 79 -33.260 4.353 25.707 1.00 26.44 C ANISOU 607 CG PHE A 79 2257 4744 3044 519 -287 -57 C ATOM 608 CD1 PHE A 79 -32.952 3.333 26.591 1.00 26.03 C ANISOU 608 CD1 PHE A 79 2202 4804 2886 551 -192 -32 C ATOM 609 CD2 PHE A 79 -34.024 4.057 24.590 1.00 25.41 C ANISOU 609 CD2 PHE A 79 2082 4563 3011 424 -338 -5 C ATOM 610 CE1 PHE A 79 -33.407 2.047 26.372 1.00 28.42 C ANISOU 610 CE1 PHE A 79 2436 5150 3214 460 -118 62 C ATOM 611 CE2 PHE A 79 -34.482 2.772 24.364 1.00 23.52 C ANISOU 611 CE2 PHE A 79 1777 4355 2804 338 -303 53 C ATOM 612 CZ PHE A 79 -34.175 1.767 25.255 1.00 28.65 C ANISOU 612 CZ PHE A 79 2404 5100 3382 340 -180 94 C ATOM 613 N AILE A 80 -31.565 6.326 23.167 0.50 17.98 N ANISOU 613 N AILE A 80 1339 3376 2115 451 -498 -59 N ATOM 614 N BILE A 80 -31.508 6.319 23.136 0.50 18.23 N ANISOU 614 N BILE A 80 1374 3406 2148 449 -498 -57 N ATOM 615 CA AILE A 80 -31.401 6.114 21.734 0.50 19.33 C ANISOU 615 CA AILE A 80 1558 3522 2264 409 -546 20 C ATOM 616 CA BILE A 80 -31.385 5.946 21.729 0.50 18.75 C ANISOU 616 CA BILE A 80 1488 3454 2181 398 -541 23 C ATOM 617 C AILE A 80 -29.938 5.881 21.390 0.50 18.26 C ANISOU 617 C AILE A 80 1455 3365 2117 385 -515 43 C ATOM 618 C BILE A 80 -29.937 6.004 21.244 0.50 18.63 C ANISOU 618 C BILE A 80 1504 3408 2168 393 -522 51 C ATOM 619 O AILE A 80 -29.595 4.985 20.618 0.50 17.59 O ANISOU 619 O AILE A 80 1450 3278 1954 321 -491 105 O ATOM 620 O BILE A 80 -29.604 5.431 20.206 0.50 18.72 O ANISOU 620 O BILE A 80 1627 3374 2113 344 -496 128 O ATOM 621 CB AILE A 80 -31.914 7.327 20.930 0.50 22.54 C ANISOU 621 CB AILE A 80 1964 3883 2717 493 -632 48 C ATOM 622 CB BILE A 80 -32.253 6.835 20.821 0.50 21.11 C ANISOU 622 CB BILE A 80 1790 3724 2508 463 -637 56 C ATOM 623 CG1AILE A 80 -33.419 7.512 21.127 0.50 26.82 C ANISOU 623 CG1AILE A 80 2448 4442 3302 513 -679 24 C ATOM 624 CG1BILE A 80 -31.691 8.254 20.749 0.50 19.05 C ANISOU 624 CG1BILE A 80 1513 3398 2328 562 -658 52 C ATOM 625 CG2AILE A 80 -31.597 7.167 19.454 0.50 29.58 C ANISOU 625 CG2AILE A 80 2978 4740 3520 506 -669 149 C ATOM 626 CG2BILE A 80 -33.688 6.846 21.309 0.50 27.00 C ANISOU 626 CG2BILE A 80 2452 4494 3311 472 -658 21 C ATOM 627 CD1AILE A 80 -34.260 6.720 20.153 0.50 28.32 C ANISOU 627 CD1AILE A 80 2660 4637 3463 478 -766 59 C ATOM 628 CD1BILE A 80 -32.412 9.135 19.754 0.50 18.94 C ANISOU 628 CD1BILE A 80 1550 3330 2317 654 -746 110 C ATOM 629 N ALA A 81 -29.081 6.699 21.989 1.00 15.70 N ANISOU 629 N ALA A 81 1091 2963 1912 428 -502 -22 N ATOM 630 CA ALA A 81 -27.658 6.689 21.697 1.00 17.58 C ANISOU 630 CA ALA A 81 1367 3059 2254 383 -430 -14 C ATOM 631 C ALA A 81 -26.983 5.438 22.256 1.00 19.07 C ANISOU 631 C ALA A 81 1556 3309 2379 327 -407 -51 C ATOM 632 O ALA A 81 -26.085 4.879 21.629 1.00 19.68 O ANISOU 632 O ALA A 81 1689 3311 2479 262 -331 -1 O ATOM 633 CB ALA A 81 -26.997 7.947 22.254 1.00 22.13 C ANISOU 633 CB ALA A 81 1860 3490 3057 444 -456 -108 C ATOM 634 N CYS A 82 -27.430 4.993 23.427 1.00 18.58 N ANISOU 634 N CYS A 82 1481 3344 2235 359 -439 -123 N ATOM 635 CA CYS A 82 -26.747 3.920 24.145 1.00 15.56 C ANISOU 635 CA CYS A 82 1137 2982 1793 339 -417 -160 C ATOM 636 C CYS A 82 -27.248 2.521 23.804 1.00 16.56 C ANISOU 636 C CYS A 82 1313 3200 1779 260 -359 -72 C ATOM 637 O CYS A 82 -26.569 1.538 24.093 1.00 13.42 O ANISOU 637 O CYS A 82 946 2815 1338 233 -337 -77 O ATOM 638 CB CYS A 82 -26.866 4.137 25.658 1.00 17.62 C ANISOU 638 CB CYS A 82 1420 3264 2010 449 -449 -268 C ATOM 639 SG CYS A 82 -25.928 5.548 26.285 1.00 21.63 S ANISOU 639 SG CYS A 82 1892 3615 2710 543 -558 -426 S ATOM 640 N PHE A 83 -28.425 2.419 23.198 1.00 13.67 N ANISOU 640 N PHE A 83 944 2877 1373 228 -354 -4 N ATOM 641 CA PHE A 83 -29.007 1.101 22.975 1.00 18.04 C ANISOU 641 CA PHE A 83 1510 3488 1856 156 -323 54 C ATOM 642 C PHE A 83 -28.102 0.206 22.130 1.00 16.87 C ANISOU 642 C PHE A 83 1426 3313 1671 80 -318 90 C ATOM 643 O PHE A 83 -28.073 -1.006 22.330 1.00 15.97 O ANISOU 643 O PHE A 83 1327 3228 1513 28 -288 110 O ATOM 644 CB PHE A 83 -30.383 1.204 22.320 1.00 17.32 C ANISOU 644 CB PHE A 83 1378 3407 1794 140 -366 87 C ATOM 645 CG PHE A 83 -31.068 -0.123 22.172 1.00 20.56 C ANISOU 645 CG PHE A 83 1748 3855 2208 67 -362 123 C ATOM 646 CD1 PHE A 83 -31.474 -0.835 23.292 1.00 23.91 C ANISOU 646 CD1 PHE A 83 2078 4374 2634 69 -277 148 C ATOM 647 CD2 PHE A 83 -31.291 -0.670 20.920 1.00 18.10 C ANISOU 647 CD2 PHE A 83 1486 3491 1901 15 -451 135 C ATOM 648 CE1 PHE A 83 -32.097 -2.065 23.165 1.00 24.39 C ANISOU 648 CE1 PHE A 83 2055 4453 2758 -12 -262 194 C ATOM 649 CE2 PHE A 83 -31.914 -1.898 20.784 1.00 22.22 C ANISOU 649 CE2 PHE A 83 1946 4019 2478 -55 -479 143 C ATOM 650 CZ PHE A 83 -32.317 -2.597 21.908 1.00 22.63 C ANISOU 650 CZ PHE A 83 1866 4145 2588 -85 -378 178 C ATOM 651 N VAL A 84 -27.349 0.798 21.206 1.00 13.29 N ANISOU 651 N VAL A 84 1009 2803 1236 83 -331 110 N ATOM 652 CA VAL A 84 -26.467 0.005 20.354 1.00 14.85 C ANISOU 652 CA VAL A 84 1312 2931 1399 29 -277 148 C ATOM 653 C VAL A 84 -25.320 -0.590 21.179 1.00 12.54 C ANISOU 653 C VAL A 84 994 2618 1151 13 -233 99 C ATOM 654 O VAL A 84 -24.772 -1.633 20.827 1.00 13.09 O ANISOU 654 O VAL A 84 1125 2668 1181 -37 -197 118 O ATOM 655 CB VAL A 84 -25.905 0.839 19.175 1.00 19.53 C ANISOU 655 CB VAL A 84 2003 3395 2022 62 -212 206 C ATOM 656 CG1 VAL A 84 -24.903 1.875 19.667 1.00 15.47 C ANISOU 656 CG1 VAL A 84 1410 2770 1699 89 -146 172 C ATOM 657 CG2 VAL A 84 -25.275 -0.072 18.121 1.00 21.94 C ANISOU 657 CG2 VAL A 84 2454 3645 2238 38 -140 260 C ATOM 658 N LEU A 85 -24.976 0.065 22.286 1.00 12.35 N ANISOU 658 N LEU A 85 889 2595 1209 75 -263 18 N ATOM 659 CA LEU A 85 -23.943 -0.441 23.185 1.00 12.28 C ANISOU 659 CA LEU A 85 861 2565 1238 102 -278 -59 C ATOM 660 C LEU A 85 -24.400 -1.737 23.847 1.00 12.54 C ANISOU 660 C LEU A 85 937 2708 1121 96 -277 -34 C ATOM 661 O LEU A 85 -23.593 -2.625 24.122 1.00 11.91 O ANISOU 661 O LEU A 85 893 2604 1029 90 -272 -52 O ATOM 662 CB LEU A 85 -23.593 0.597 24.253 1.00 13.99 C ANISOU 662 CB LEU A 85 1003 2753 1561 213 -366 -186 C ATOM 663 CG LEU A 85 -23.121 1.968 23.760 1.00 18.06 C ANISOU 663 CG LEU A 85 1444 3121 2298 221 -366 -219 C ATOM 664 CD1 LEU A 85 -22.991 2.948 24.915 1.00 14.38 C ANISOU 664 CD1 LEU A 85 935 2599 1931 334 -482 -361 C ATOM 665 CD2 LEU A 85 -21.801 1.830 23.032 1.00 18.48 C ANISOU 665 CD2 LEU A 85 1469 3008 2544 160 -284 -208 C ATOM 666 N VAL A 86 -25.700 -1.831 24.109 1.00 13.01 N ANISOU 666 N VAL A 86 996 2842 1107 99 -254 15 N ATOM 667 CA VAL A 86 -26.287 -3.036 24.682 1.00 14.79 C ANISOU 667 CA VAL A 86 1230 3155 1234 86 -210 73 C ATOM 668 C VAL A 86 -26.154 -4.209 23.718 1.00 17.43 C ANISOU 668 C VAL A 86 1603 3456 1565 -33 -196 131 C ATOM 669 O VAL A 86 -25.771 -5.309 24.112 1.00 13.46 O ANISOU 669 O VAL A 86 1145 2946 1023 -47 -162 153 O ATOM 670 CB VAL A 86 -27.777 -2.832 25.029 1.00 13.11 C ANISOU 670 CB VAL A 86 938 3035 1008 106 -173 124 C ATOM 671 CG1 VAL A 86 -28.364 -4.101 25.640 1.00 13.77 C ANISOU 671 CG1 VAL A 86 1022 3154 1057 87 -66 212 C ATOM 672 CG2 VAL A 86 -27.951 -1.644 25.967 1.00 13.64 C ANISOU 672 CG2 VAL A 86 981 3148 1054 249 -189 58 C ATOM 673 N LEU A 87 -26.468 -3.962 22.449 1.00 11.99 N ANISOU 673 N LEU A 87 923 2725 906 -94 -227 148 N ATOM 674 CA LEU A 87 -26.431 -5.008 21.438 1.00 15.89 C ANISOU 674 CA LEU A 87 1482 3176 1379 -175 -243 175 C ATOM 675 C LEU A 87 -25.001 -5.463 21.168 1.00 16.66 C ANISOU 675 C LEU A 87 1663 3200 1466 -180 -201 157 C ATOM 676 O LEU A 87 -24.736 -6.658 21.021 1.00 16.42 O ANISOU 676 O LEU A 87 1681 3145 1413 -226 -191 167 O ATOM 677 CB LEU A 87 -27.089 -4.524 20.145 1.00 12.47 C ANISOU 677 CB LEU A 87 1087 2714 938 -178 -314 180 C ATOM 678 CG LEU A 87 -28.547 -4.076 20.301 1.00 13.16 C ANISOU 678 CG LEU A 87 1078 2830 1094 -165 -368 178 C ATOM 679 CD1 LEU A 87 -29.153 -3.697 18.957 1.00 13.96 C ANISOU 679 CD1 LEU A 87 1249 2876 1178 -136 -484 161 C ATOM 680 CD2 LEU A 87 -29.373 -5.158 20.985 1.00 13.73 C ANISOU 680 CD2 LEU A 87 1029 2955 1234 -228 -361 202 C ATOM 681 N ALA A 88 -24.082 -4.505 21.109 1.00 13.16 N ANISOU 681 N ALA A 88 1217 2704 1081 -134 -171 125 N ATOM 682 CA ALA A 88 -22.675 -4.818 20.904 1.00 14.36 C ANISOU 682 CA ALA A 88 1399 2763 1293 -133 -113 100 C ATOM 683 C ALA A 88 -22.141 -5.637 22.071 1.00 14.40 C ANISOU 683 C ALA A 88 1380 2790 1301 -111 -142 55 C ATOM 684 O ALA A 88 -21.395 -6.597 21.874 1.00 15.69 O ANISOU 684 O ALA A 88 1589 2906 1468 -134 -117 51 O ATOM 685 CB ALA A 88 -21.861 -3.544 20.730 1.00 11.73 C ANISOU 685 CB ALA A 88 1012 2334 1111 -91 -65 73 C ATOM 686 N GLN A 89 -22.531 -5.260 23.286 1.00 11.38 N ANISOU 686 N GLN A 89 951 2476 896 -41 -194 22 N ATOM 687 CA GLN A 89 -22.058 -5.963 24.475 1.00 12.08 C ANISOU 687 CA GLN A 89 1067 2585 937 35 -231 -16 C ATOM 688 C GLN A 89 -22.594 -7.387 24.510 1.00 13.55 C ANISOU 688 C GLN A 89 1321 2803 1025 -19 -180 73 C ATOM 689 O GLN A 89 -21.876 -8.315 24.883 1.00 11.89 O ANISOU 689 O GLN A 89 1167 2557 794 6 -186 65 O ATOM 690 CB GLN A 89 -22.460 -5.227 25.752 1.00 12.26 C ANISOU 690 CB GLN A 89 1077 2677 903 170 -287 -67 C ATOM 691 CG GLN A 89 -21.624 -5.637 26.954 1.00 18.03 C ANISOU 691 CG GLN A 89 1877 3383 1592 313 -362 -147 C ATOM 692 CD GLN A 89 -20.143 -5.376 26.737 1.00 19.36 C ANISOU 692 CD GLN A 89 1977 3442 1937 333 -469 -279 C ATOM 693 OE1 GLN A 89 -19.755 -4.316 26.245 1.00 21.29 O ANISOU 693 OE1 GLN A 89 2113 3609 2369 306 -491 -344 O ATOM 694 NE2 GLN A 89 -19.309 -6.346 27.094 1.00 15.21 N ANISOU 694 NE2 GLN A 89 1504 2876 1398 380 -515 -310 N ATOM 695 N ASER A 90 -23.857 -7.547 24.125 0.60 14.81 N ANISOU 695 N ASER A 90 1460 3008 1161 -89 -141 151 N ATOM 696 N BSER A 90 -23.854 -7.553 24.121 0.40 14.84 N ANISOU 696 N BSER A 90 1464 3010 1164 -90 -141 151 N ATOM 697 CA ASER A 90 -24.485 -8.862 24.070 0.60 15.31 C ANISOU 697 CA ASER A 90 1545 3061 1210 -160 -94 231 C ATOM 698 CA BSER A 90 -24.477 -8.871 24.082 0.40 15.38 C ANISOU 698 CA BSER A 90 1555 3069 1218 -159 -93 231 C ATOM 699 C ASER A 90 -23.770 -9.758 23.068 0.60 14.07 C ANISOU 699 C ASER A 90 1448 2819 1078 -235 -113 214 C ATOM 700 C BSER A 90 -23.787 -9.767 23.058 0.40 14.20 C ANISOU 700 C BSER A 90 1464 2836 1095 -237 -113 215 C ATOM 701 O ASER A 90 -23.566 -10.945 23.320 0.60 13.63 O ANISOU 701 O ASER A 90 1438 2722 1017 -255 -90 247 O ATOM 702 O BSER A 90 -23.618 -10.965 23.284 0.40 14.05 O ANISOU 702 O BSER A 90 1490 2775 1073 -260 -90 249 O ATOM 703 CB ASER A 90 -25.967 -8.736 23.708 0.60 16.05 C ANISOU 703 CB ASER A 90 1553 3185 1360 -225 -81 283 C ATOM 704 CB BSER A 90 -25.970 -8.754 23.764 0.40 16.34 C ANISOU 704 CB BSER A 90 1590 3224 1395 -223 -77 285 C ATOM 705 OG ASER A 90 -26.573 -10.012 23.583 0.60 13.44 O ANISOU 705 OG ASER A 90 1205 2804 1098 -309 -46 346 O ATOM 706 OG BSER A 90 -26.177 -8.139 22.505 0.40 19.23 O ANISOU 706 OG BSER A 90 1943 3571 1793 -270 -156 243 O ATOM 707 N SER A 91 -23.387 -9.176 21.936 1.00 13.96 N ANISOU 707 N SER A 91 1450 2770 1083 -258 -139 172 N ATOM 708 CA SER A 91 -22.657 -9.899 20.900 1.00 12.63 C ANISOU 708 CA SER A 91 1365 2521 911 -293 -132 152 C ATOM 709 C SER A 91 -21.319 -10.395 21.437 1.00 15.59 C ANISOU 709 C SER A 91 1759 2847 1318 -251 -104 118 C ATOM 710 O SER A 91 -20.926 -11.536 21.201 1.00 16.08 O ANISOU 710 O SER A 91 1881 2856 1374 -276 -97 118 O ATOM 711 CB SER A 91 -22.435 -9.008 19.673 1.00 11.61 C ANISOU 711 CB SER A 91 1284 2359 769 -275 -114 139 C ATOM 712 OG SER A 91 -23.667 -8.617 19.089 1.00 15.11 O ANISOU 712 OG SER A 91 1731 2838 1172 -288 -182 155 O ATOM 713 N ILE A 92 -20.633 -9.530 22.176 1.00 14.02 N ANISOU 713 N ILE A 92 1500 2652 1175 -177 -112 70 N ATOM 714 CA ILE A 92 -19.351 -9.869 22.781 1.00 13.36 C ANISOU 714 CA ILE A 92 1405 2509 1162 -112 -134 4 C ATOM 715 C ILE A 92 -19.466 -11.048 23.749 1.00 15.09 C ANISOU 715 C ILE A 92 1691 2750 1294 -74 -168 32 C ATOM 716 O ILE A 92 -18.654 -11.973 23.708 1.00 12.50 O ANISOU 716 O ILE A 92 1402 2355 992 -63 -174 12 O ATOM 717 CB ILE A 92 -18.758 -8.651 23.514 1.00 17.61 C ANISOU 717 CB ILE A 92 1847 3034 1809 -21 -196 -88 C ATOM 718 CG1 ILE A 92 -18.273 -7.616 22.497 1.00 23.53 C ANISOU 718 CG1 ILE A 92 2524 3701 2717 -56 -120 -103 C ATOM 719 CG2 ILE A 92 -17.620 -9.067 24.431 1.00 13.42 C ANISOU 719 CG2 ILE A 92 1301 2448 1351 84 -292 -187 C ATOM 720 CD1 ILE A 92 -17.852 -6.306 23.119 1.00 26.13 C ANISOU 720 CD1 ILE A 92 2728 3985 3214 14 -187 -197 C ATOM 721 N PHE A 93 -20.478 -11.014 24.612 1.00 12.15 N ANISOU 721 N PHE A 93 1336 2458 824 -42 -166 93 N ATOM 722 CA PHE A 93 -20.726 -12.112 25.547 1.00 17.48 C ANISOU 722 CA PHE A 93 2098 3138 1407 11 -141 166 C ATOM 723 C PHE A 93 -21.019 -13.425 24.816 1.00 17.35 C ANISOU 723 C PHE A 93 2115 3054 1424 -108 -89 236 C ATOM 724 O PHE A 93 -20.502 -14.480 25.188 1.00 15.84 O ANISOU 724 O PHE A 93 2000 2803 1217 -74 -86 258 O ATOM 725 CB PHE A 93 -21.885 -11.764 26.485 1.00 18.14 C ANISOU 725 CB PHE A 93 2190 3307 1397 72 -80 248 C ATOM 726 CG PHE A 93 -21.529 -10.749 27.542 1.00 22.32 C ANISOU 726 CG PHE A 93 2743 3892 1844 251 -154 167 C ATOM 727 CD1 PHE A 93 -20.292 -10.784 28.169 1.00 31.49 C ANISOU 727 CD1 PHE A 93 3963 5012 2989 395 -281 56 C ATOM 728 CD2 PHE A 93 -22.427 -9.757 27.901 1.00 18.65 C ANISOU 728 CD2 PHE A 93 2237 3494 1356 289 -122 176 C ATOM 729 CE1 PHE A 93 -19.963 -9.851 29.139 1.00 33.88 C ANISOU 729 CE1 PHE A 93 4288 5293 3292 557 -379 -57 C ATOM 730 CE2 PHE A 93 -22.103 -8.823 28.870 1.00 21.11 C ANISOU 730 CE2 PHE A 93 2582 3799 1639 457 -201 73 C ATOM 731 CZ PHE A 93 -20.869 -8.868 29.488 1.00 25.14 C ANISOU 731 CZ PHE A 93 3156 4237 2158 587 -335 -48 C ATOM 732 N SER A 94 -21.846 -13.356 23.777 1.00 12.74 N ANISOU 732 N SER A 94 1482 2467 891 -230 -74 254 N ATOM 733 CA SER A 94 -22.169 -14.541 22.987 1.00 15.08 C ANISOU 733 CA SER A 94 1805 2681 1243 -332 -72 279 C ATOM 734 C SER A 94 -20.926 -15.114 22.313 1.00 15.19 C ANISOU 734 C SER A 94 1888 2618 1264 -323 -99 207 C ATOM 735 O SER A 94 -20.726 -16.326 22.299 1.00 15.24 O ANISOU 735 O SER A 94 1949 2544 1298 -344 -98 224 O ATOM 736 CB SER A 94 -23.233 -14.217 21.936 1.00 16.39 C ANISOU 736 CB SER A 94 1916 2852 1460 -422 -114 265 C ATOM 737 OG SER A 94 -24.481 -13.936 22.546 1.00 19.03 O ANISOU 737 OG SER A 94 2155 3231 1845 -443 -77 335 O ATOM 738 N LEU A 95 -20.092 -14.236 21.765 1.00 15.59 N ANISOU 738 N LEU A 95 1928 2678 1319 -287 -102 134 N ATOM 739 CA LEU A 95 -18.863 -14.658 21.102 1.00 16.12 C ANISOU 739 CA LEU A 95 2037 2663 1423 -265 -82 72 C ATOM 740 C LEU A 95 -17.896 -15.318 22.082 1.00 18.71 C ANISOU 740 C LEU A 95 2372 2949 1787 -189 -107 50 C ATOM 741 O LEU A 95 -17.256 -16.318 21.757 1.00 18.22 O ANISOU 741 O LEU A 95 2363 2807 1754 -187 -102 28 O ATOM 742 CB LEU A 95 -18.189 -13.467 20.415 1.00 15.20 C ANISOU 742 CB LEU A 95 1881 2539 1356 -234 -25 27 C ATOM 743 CG LEU A 95 -18.872 -12.914 19.164 1.00 16.04 C ANISOU 743 CG LEU A 95 2043 2658 1395 -265 8 47 C ATOM 744 CD1 LEU A 95 -18.242 -11.596 18.733 1.00 16.78 C ANISOU 744 CD1 LEU A 95 2092 2728 1555 -220 104 43 C ATOM 745 CD2 LEU A 95 -18.809 -13.928 18.037 1.00 15.17 C ANISOU 745 CD2 LEU A 95 2066 2482 1216 -270 16 28 C ATOM 746 N LEU A 96 -17.796 -14.758 23.284 1.00 12.83 N ANISOU 746 N LEU A 96 1592 2255 1029 -102 -152 45 N ATOM 747 CA LEU A 96 -16.916 -15.311 24.307 1.00 19.18 C ANISOU 747 CA LEU A 96 2430 3020 1836 18 -221 9 C ATOM 748 C LEU A 96 -17.411 -16.684 24.755 1.00 19.97 C ANISOU 748 C LEU A 96 2645 3089 1855 13 -197 112 C ATOM 749 O LEU A 96 -16.619 -17.602 24.965 1.00 21.49 O ANISOU 749 O LEU A 96 2895 3203 2069 70 -232 92 O ATOM 750 CB LEU A 96 -16.816 -14.361 25.503 1.00 20.64 C ANISOU 750 CB LEU A 96 2592 3266 1985 154 -309 -38 C ATOM 751 CG LEU A 96 -15.934 -14.803 26.675 1.00 24.24 C ANISOU 751 CG LEU A 96 3116 3684 2409 339 -438 -102 C ATOM 752 CD1 LEU A 96 -14.526 -15.145 26.204 1.00 21.28 C ANISOU 752 CD1 LEU A 96 2667 3196 2224 355 -499 -221 C ATOM 753 CD2 LEU A 96 -15.896 -13.725 27.752 1.00 25.85 C ANISOU 753 CD2 LEU A 96 3314 3945 2561 502 -562 -187 C ATOM 754 N ALA A 97 -18.727 -16.816 24.884 1.00 16.74 N ANISOU 754 N ALA A 97 2250 2719 1391 -55 -129 224 N ATOM 755 CA ALA A 97 -19.345 -18.066 25.308 1.00 20.84 C ANISOU 755 CA ALA A 97 2847 3175 1896 -76 -64 348 C ATOM 756 C ALA A 97 -19.136 -19.172 24.279 1.00 20.95 C ANISOU 756 C ALA A 97 2877 3074 2008 -181 -72 324 C ATOM 757 O ALA A 97 -18.927 -20.331 24.635 1.00 19.87 O ANISOU 757 O ALA A 97 2819 2841 1891 -158 -56 378 O ATOM 758 CB ALA A 97 -20.823 -17.858 25.560 1.00 22.06 C ANISOU 758 CB ALA A 97 2955 3370 2055 -141 34 464 C ATOM 759 N ILE A 98 -19.205 -18.807 23.003 1.00 18.47 N ANISOU 759 N ILE A 98 2513 2764 1742 -272 -98 242 N ATOM 760 CA ILE A 98 -18.997 -19.761 21.922 1.00 18.40 C ANISOU 760 CA ILE A 98 2547 2651 1793 -336 -125 189 C ATOM 761 C ILE A 98 -17.569 -20.300 21.963 1.00 20.38 C ANISOU 761 C ILE A 98 2852 2838 2054 -250 -138 124 C ATOM 762 O ILE A 98 -17.346 -21.503 21.824 1.00 21.27 O ANISOU 762 O ILE A 98 3029 2842 2211 -258 -152 125 O ATOM 763 CB ILE A 98 -19.290 -19.121 20.550 1.00 15.00 C ANISOU 763 CB ILE A 98 2105 2247 1347 -388 -152 109 C ATOM 764 CG1 ILE A 98 -20.796 -18.884 20.396 1.00 15.04 C ANISOU 764 CG1 ILE A 98 2049 2278 1389 -475 -185 150 C ATOM 765 CG2 ILE A 98 -18.780 -20.000 19.421 1.00 16.27 C ANISOU 765 CG2 ILE A 98 2358 2307 1516 -388 -181 24 C ATOM 766 CD1 ILE A 98 -21.181 -18.093 19.161 1.00 14.84 C ANISOU 766 CD1 ILE A 98 2038 2291 1310 -483 -241 75 C ATOM 767 N ALA A 99 -16.612 -19.402 22.176 1.00 19.08 N ANISOU 767 N ALA A 99 2639 2723 1887 -166 -142 60 N ATOM 768 CA ALA A 99 -15.205 -19.778 22.281 1.00 19.89 C ANISOU 768 CA ALA A 99 2743 2755 2059 -73 -165 -19 C ATOM 769 C ALA A 99 -14.973 -20.734 23.449 1.00 21.22 C ANISOU 769 C ALA A 99 2986 2872 2203 17 -224 30 C ATOM 770 O ALA A 99 -14.289 -21.748 23.307 1.00 19.09 O ANISOU 770 O ALA A 99 2768 2502 1985 51 -244 1 O ATOM 771 CB ALA A 99 -14.335 -18.536 22.431 1.00 14.80 C ANISOU 771 CB ALA A 99 1982 2146 1495 -3 -173 -104 C ATOM 772 N ILE A 100 -15.550 -20.405 24.601 1.00 19.26 N ANISOU 772 N ILE A 100 2769 2689 1861 79 -241 110 N ATOM 773 CA ILE A 100 -15.396 -21.224 25.797 1.00 20.78 C ANISOU 773 CA ILE A 100 3084 2834 1976 212 -276 185 C ATOM 774 C ILE A 100 -16.052 -22.588 25.603 1.00 20.41 C ANISOU 774 C ILE A 100 3122 2679 1955 126 -195 306 C ATOM 775 O ILE A 100 -15.491 -23.614 25.992 1.00 22.67 O ANISOU 775 O ILE A 100 3506 2861 2247 209 -222 331 O ATOM 776 CB ILE A 100 -15.986 -20.517 27.037 1.00 21.40 C ANISOU 776 CB ILE A 100 3217 3009 1904 330 -274 259 C ATOM 777 CG1 ILE A 100 -15.187 -19.244 27.338 1.00 20.69 C ANISOU 777 CG1 ILE A 100 3044 2990 1828 442 -406 103 C ATOM 778 CG2 ILE A 100 -15.984 -21.444 28.249 1.00 19.60 C ANISOU 778 CG2 ILE A 100 3180 2724 1544 498 -265 381 C ATOM 779 CD1 ILE A 100 -15.705 -18.448 28.519 1.00 21.15 C ANISOU 779 CD1 ILE A 100 3172 3145 1719 591 -435 136 C ATOM 780 N ASP A 101 -17.227 -22.597 24.980 1.00 19.28 N ANISOU 780 N ASP A 101 2927 2539 1861 -34 -114 368 N ATOM 781 CA ASP A 101 -17.931 -23.842 24.684 1.00 23.97 C ANISOU 781 CA ASP A 101 3551 2994 2561 -138 -58 455 C ATOM 782 C ASP A 101 -17.088 -24.760 23.800 1.00 25.04 C ANISOU 782 C ASP A 101 3720 3014 2780 -157 -127 347 C ATOM 783 O ASP A 101 -17.026 -25.969 24.027 1.00 22.76 O ANISOU 783 O ASP A 101 3507 2582 2560 -148 -115 407 O ATOM 784 CB ASP A 101 -19.275 -23.552 24.010 1.00 24.82 C ANISOU 784 CB ASP A 101 3553 3115 2764 -301 -19 479 C ATOM 785 CG ASP A 101 -20.017 -24.818 23.617 1.00 31.65 C ANISOU 785 CG ASP A 101 4405 3799 3822 -420 1 529 C ATOM 786 OD1 ASP A 101 -20.663 -25.427 24.495 1.00 35.89 O ANISOU 786 OD1 ASP A 101 4954 4245 4437 -422 125 700 O ATOM 787 OD2 ASP A 101 -19.961 -25.199 22.429 1.00 30.51 O ANISOU 787 OD2 ASP A 101 4244 3588 3760 -496 -100 398 O ATOM 788 N ARG A 102 -16.431 -24.184 22.797 1.00 20.41 N ANISOU 788 N ARG A 102 3086 2478 2192 -168 -176 197 N ATOM 789 CA ARG A 102 -15.585 -24.971 21.907 1.00 23.62 C ANISOU 789 CA ARG A 102 3532 2783 2658 -157 -212 88 C ATOM 790 C ARG A 102 -14.332 -25.471 22.623 1.00 21.96 C ANISOU 790 C ARG A 102 3366 2517 2459 -14 -247 66 C ATOM 791 O ARG A 102 -13.836 -26.559 22.327 1.00 24.60 O ANISOU 791 O ARG A 102 3761 2724 2860 8 -270 32 O ATOM 792 CB ARG A 102 -15.203 -24.157 20.669 1.00 25.94 C ANISOU 792 CB ARG A 102 3786 3139 2930 -171 -197 -38 C ATOM 793 CG ARG A 102 -16.368 -23.859 19.726 1.00 30.53 C ANISOU 793 CG ARG A 102 4367 3746 3486 -277 -210 -51 C ATOM 794 CD ARG A 102 -16.974 -25.134 19.135 1.00 39.00 C ANISOU 794 CD ARG A 102 5506 4674 4639 -341 -282 -81 C ATOM 795 NE ARG A 102 -17.980 -25.739 20.007 1.00 44.76 N ANISOU 795 NE ARG A 102 6192 5332 5482 -423 -286 42 N ATOM 796 CZ ARG A 102 -18.190 -27.047 20.113 1.00 47.08 C ANISOU 796 CZ ARG A 102 6520 5452 5916 -459 -315 66 C ATOM 797 NH1 ARG A 102 -17.463 -27.898 19.402 1.00 49.65 N ANISOU 797 NH1 ARG A 102 6931 5670 6262 -416 -373 -48 N ATOM 798 NH2 ARG A 102 -19.126 -27.507 20.933 1.00 46.11 N ANISOU 798 NH2 ARG A 102 6342 5246 5932 -531 -263 210 N ATOM 799 N TYR A 103 -13.828 -24.683 23.568 1.00 21.52 N ANISOU 799 N TYR A 103 3281 2546 2350 100 -279 68 N ATOM 800 CA TYR A 103 -12.663 -25.097 24.342 1.00 24.86 C ANISOU 800 CA TYR A 103 3741 2911 2792 269 -368 24 C ATOM 801 C TYR A 103 -12.985 -26.289 25.240 1.00 27.49 C ANISOU 801 C TYR A 103 4231 3141 3072 335 -372 163 C ATOM 802 O TYR A 103 -12.212 -27.244 25.316 1.00 27.28 O ANISOU 802 O TYR A 103 4269 2997 3101 418 -426 134 O ATOM 803 CB TYR A 103 -12.126 -23.944 25.192 1.00 26.35 C ANISOU 803 CB TYR A 103 3865 3197 2948 400 -454 -36 C ATOM 804 CG TYR A 103 -11.009 -24.381 26.112 1.00 35.88 C ANISOU 804 CG TYR A 103 5122 4335 4175 610 -605 -102 C ATOM 805 CD1 TYR A 103 -9.740 -24.646 25.615 1.00 36.20 C ANISOU 805 CD1 TYR A 103 5066 4289 4401 661 -666 -251 C ATOM 806 CD2 TYR A 103 -11.227 -24.549 27.475 1.00 40.99 C ANISOU 806 CD2 TYR A 103 5927 4994 4653 783 -685 -13 C ATOM 807 CE1 TYR A 103 -8.716 -25.058 26.449 1.00 40.42 C ANISOU 807 CE1 TYR A 103 5628 4746 4983 867 -842 -333 C ATOM 808 CE2 TYR A 103 -10.211 -24.961 28.316 1.00 43.59 C ANISOU 808 CE2 TYR A 103 6334 5254 4976 1015 -865 -88 C ATOM 809 CZ TYR A 103 -8.957 -25.213 27.798 1.00 44.17 C ANISOU 809 CZ TYR A 103 6279 5238 5266 1050 -964 -258 C ATOM 810 OH TYR A 103 -7.941 -25.622 28.633 1.00 47.84 O ANISOU 810 OH TYR A 103 6802 5621 5753 1294 -1180 -354 O ATOM 811 N ILE A 104 -14.123 -26.223 25.924 1.00 27.21 N ANISOU 811 N ILE A 104 4257 3136 2944 308 -291 327 N ATOM 812 CA ILE A 104 -14.578 -27.326 26.761 1.00 28.76 C ANISOU 812 CA ILE A 104 4609 3211 3108 366 -224 509 C ATOM 813 C ILE A 104 -14.760 -28.597 25.934 1.00 29.97 C ANISOU 813 C ILE A 104 4768 3188 3432 237 -191 518 C ATOM 814 O ILE A 104 -14.406 -29.694 26.368 1.00 30.37 O ANISOU 814 O ILE A 104 4940 3091 3510 322 -194 589 O ATOM 815 CB ILE A 104 -15.904 -26.984 27.472 1.00 30.87 C ANISOU 815 CB ILE A 104 4906 3526 3298 336 -72 700 C ATOM 816 CG1 ILE A 104 -15.719 -25.778 28.395 1.00 31.09 C ANISOU 816 CG1 ILE A 104 4967 3718 3129 504 -119 680 C ATOM 817 CG2 ILE A 104 -16.414 -28.178 28.262 1.00 32.30 C ANISOU 817 CG2 ILE A 104 5244 3542 3488 389 67 925 C ATOM 818 CD1 ILE A 104 -16.992 -25.341 29.095 1.00 30.14 C ANISOU 818 CD1 ILE A 104 4878 3657 2915 501 54 861 C ATOM 819 N ALA A 105 -15.296 -28.439 24.729 1.00 25.60 N ANISOU 819 N ALA A 105 4098 2641 2988 54 -180 434 N ATOM 820 CA ALA A 105 -15.568 -29.579 23.861 1.00 30.70 C ANISOU 820 CA ALA A 105 4749 3114 3803 -61 -189 403 C ATOM 821 C ALA A 105 -14.291 -30.294 23.425 1.00 34.32 C ANISOU 821 C ALA A 105 5261 3486 4292 31 -277 272 C ATOM 822 O ALA A 105 -14.296 -31.503 23.201 1.00 40.14 O ANISOU 822 O ALA A 105 6059 4040 5151 9 -291 282 O ATOM 823 CB ALA A 105 -16.361 -29.132 22.643 1.00 27.31 C ANISOU 823 CB ALA A 105 4212 2723 3442 -223 -211 302 C ATOM 824 N ILE A 106 -13.195 -29.550 23.312 1.00 33.08 N ANISOU 824 N ILE A 106 5064 3441 4065 134 -330 145 N ATOM 825 CA ILE A 106 -11.953 -30.124 22.811 1.00 37.67 C ANISOU 825 CA ILE A 106 5658 3942 4714 223 -388 7 C ATOM 826 C ILE A 106 -10.990 -30.516 23.936 1.00 39.10 C ANISOU 826 C ILE A 106 5905 4074 4879 417 -466 33 C ATOM 827 O ILE A 106 -10.192 -31.442 23.782 1.00 41.07 O ANISOU 827 O ILE A 106 6198 4193 5212 496 -517 -28 O ATOM 828 CB ILE A 106 -11.247 -29.152 21.835 1.00 42.80 C ANISOU 828 CB ILE A 106 6194 4699 5370 224 -368 -157 C ATOM 829 CG1 ILE A 106 -10.174 -29.881 21.027 1.00 49.26 C ANISOU 829 CG1 ILE A 106 7022 5409 6287 293 -371 -294 C ATOM 830 CG2 ILE A 106 -10.662 -27.952 22.570 1.00 44.70 C ANISOU 830 CG2 ILE A 106 6337 5067 5580 317 -393 -177 C ATOM 831 CD1 ILE A 106 -9.567 -29.030 19.947 1.00 51.91 C ANISOU 831 CD1 ILE A 106 7267 5816 6639 301 -277 -420 C ATOM 832 N ALA A 107 -11.078 -29.828 25.071 1.00 33.68 N ANISOU 832 N ALA A 107 5241 3482 4073 518 -494 113 N ATOM 833 CA ALA A 107 -10.171 -30.080 26.185 1.00 36.49 C ANISOU 833 CA ALA A 107 5688 3799 4377 751 -618 113 C ATOM 834 C ALA A 107 -10.683 -31.206 27.076 1.00 43.73 C ANISOU 834 C ALA A 107 6817 4581 5218 829 -578 318 C ATOM 835 O ALA A 107 -9.906 -32.030 27.556 1.00 49.61 O ANISOU 835 O ALA A 107 7674 5207 5970 998 -673 315 O ATOM 836 CB ALA A 107 -9.967 -28.812 27.000 1.00 39.13 C ANISOU 836 CB ALA A 107 5980 4284 4602 872 -702 73 C ATOM 837 N ILE A 108 -11.993 -31.235 27.295 1.00 42.02 N ANISOU 837 N ILE A 108 6649 4364 4953 713 -423 505 N ATOM 838 CA ILE A 108 -12.603 -32.269 28.125 1.00 43.27 C ANISOU 838 CA ILE A 108 6996 4365 5079 772 -311 744 C ATOM 839 C ILE A 108 -13.897 -32.811 27.511 1.00 38.50 C ANISOU 839 C ILE A 108 6325 3647 4655 525 -139 863 C ATOM 840 O ILE A 108 -14.977 -32.633 28.072 1.00 41.61 O ANISOU 840 O ILE A 108 6742 4043 5026 482 29 1056 O ATOM 841 CB ILE A 108 -12.896 -31.738 29.543 1.00 48.19 C ANISOU 841 CB ILE A 108 7786 5072 5451 980 -265 907 C ATOM 842 CG1 ILE A 108 -13.463 -30.317 29.479 1.00 44.66 C ANISOU 842 CG1 ILE A 108 7209 4836 4923 903 -238 859 C ATOM 843 CG2 ILE A 108 -11.629 -31.745 30.382 1.00 54.09 C ANISOU 843 CG2 ILE A 108 8677 5829 6045 1291 -477 817 C ATOM 844 CD1 ILE A 108 -13.901 -29.773 30.821 1.00 47.26 C ANISOU 844 CD1 ILE A 108 7715 5249 4991 1111 -170 1016 C ATOM 845 N PRO A 109 -13.787 -33.494 26.360 1.00 46.19 N ANISOU 845 N PRO A 109 8285 4008 5258 773 30 253 N ATOM 846 CA PRO A 109 -14.978 -33.979 25.652 1.00 48.03 C ANISOU 846 CA PRO A 109 8680 3633 5936 390 125 361 C ATOM 847 C PRO A 109 -15.752 -35.047 26.425 1.00 54.18 C ANISOU 847 C PRO A 109 9558 4154 6875 462 395 942 C ATOM 848 O PRO A 109 -16.954 -35.202 26.209 1.00 52.74 O ANISOU 848 O PRO A 109 9388 3644 7006 120 516 994 O ATOM 849 CB PRO A 109 -14.399 -34.564 24.360 1.00 48.81 C ANISOU 849 CB PRO A 109 8963 3223 6358 298 57 115 C ATOM 850 CG PRO A 109 -13.010 -34.958 24.722 1.00 44.75 C ANISOU 850 CG PRO A 109 8439 2911 5654 735 28 163 C ATOM 851 CD PRO A 109 -12.542 -33.908 25.688 1.00 45.89 C ANISOU 851 CD PRO A 109 8316 3824 5296 956 -63 30 C ATOM 852 N LEU A 110 -15.072 -35.766 27.313 1.00 57.40 N ANISOU 852 N LEU A 110 10031 4709 7071 926 514 1362 N ATOM 853 CA LEU A 110 -15.699 -36.859 28.050 1.00 64.68 C ANISOU 853 CA LEU A 110 11128 5304 8142 1060 875 1979 C ATOM 854 C LEU A 110 -16.729 -36.362 29.061 1.00 68.11 C ANISOU 854 C LEU A 110 11460 6047 8373 965 1033 2203 C ATOM 855 O LEU A 110 -17.650 -37.093 29.428 1.00 70.72 O ANISOU 855 O LEU A 110 11924 5973 8975 856 1397 2589 O ATOM 856 CB LEU A 110 -14.638 -37.701 28.761 1.00 67.48 C ANISOU 856 CB LEU A 110 11614 5784 8240 1696 963 2422 C ATOM 857 CG LEU A 110 -13.711 -38.519 27.860 1.00 67.41 C ANISOU 857 CG LEU A 110 11746 5321 8545 1825 926 2326 C ATOM 858 CD1 LEU A 110 -12.753 -39.356 28.693 1.00 70.34 C ANISOU 858 CD1 LEU A 110 12234 5850 8643 2542 1029 2837 C ATOM 859 CD2 LEU A 110 -14.519 -39.400 26.919 1.00 68.48 C ANISOU 859 CD2 LEU A 110 11941 4712 9366 1325 1130 2245 C ATOM 860 N ARG A 111 -16.575 -35.121 29.509 1.00 65.32 N ANISOU 860 N ARG A 111 10862 6378 7578 982 815 1925 N ATOM 861 CA ARG A 111 -17.495 -34.555 30.487 1.00 67.12 C ANISOU 861 CA ARG A 111 10966 6948 7589 887 965 2083 C ATOM 862 C ARG A 111 -18.156 -33.277 29.980 1.00 55.93 C ANISOU 862 C ARG A 111 9314 5681 6257 439 795 1566 C ATOM 863 O ARG A 111 -18.699 -32.498 30.762 1.00 52.96 O ANISOU 863 O ARG A 111 8761 5722 5638 372 857 1554 O ATOM 864 CB ARG A 111 -16.770 -34.287 31.808 1.00 75.77 C ANISOU 864 CB ARG A 111 11971 8816 8001 1403 943 2303 C ATOM 865 CG ARG A 111 -15.358 -33.746 31.655 1.00 79.91 C ANISOU 865 CG ARG A 111 12316 9872 8173 1699 604 1895 C ATOM 866 CD ARG A 111 -14.669 -33.637 33.008 1.00 89.87 C ANISOU 866 CD ARG A 111 13451 11960 8736 2265 566 2098 C ATOM 867 NE ARG A 111 -13.244 -33.345 32.880 1.00 93.47 N ANISOU 867 NE ARG A 111 13699 12910 8907 2604 259 1692 N ATOM 868 CZ ARG A 111 -12.412 -33.212 33.909 1.00 98.29 C ANISOU 868 CZ ARG A 111 14110 14350 8885 3148 125 1703 C ATOM 869 NH1 ARG A 111 -12.861 -33.343 35.149 1.00103.32 N ANISOU 869 NH1 ARG A 111 14784 15421 9051 3438 274 2156 N ATOM 870 NH2 ARG A 111 -11.130 -32.948 33.697 1.00 98.21 N ANISOU 870 NH2 ARG A 111 13848 14766 8701 3411 -152 1229 N ATOM 871 N TYR A 112 -18.114 -33.075 28.666 1.00 49.67 N ANISOU 871 N TYR A 112 8536 4539 5796 162 604 1155 N ATOM 872 CA TYR A 112 -18.755 -31.920 28.048 1.00 44.95 C ANISOU 872 CA TYR A 112 7774 4013 5293 -195 460 713 C ATOM 873 C TYR A 112 -20.271 -31.962 28.238 1.00 49.16 C ANISOU 873 C TYR A 112 8228 4330 6122 -514 630 842 C ATOM 874 O TYR A 112 -20.877 -30.981 28.667 1.00 44.72 O ANISOU 874 O TYR A 112 7465 4094 5433 -640 640 717 O ATOM 875 CB TYR A 112 -18.410 -31.850 26.557 1.00 41.71 C ANISOU 875 CB TYR A 112 7469 3241 5137 -359 247 315 C ATOM 876 CG TYR A 112 -19.160 -30.775 25.799 1.00 40.12 C ANISOU 876 CG TYR A 112 7168 3039 5037 -658 117 -64 C ATOM 877 CD1 TYR A 112 -18.679 -29.474 25.743 1.00 36.20 C ANISOU 877 CD1 TYR A 112 6569 2921 4265 -621 42 -402 C ATOM 878 CD2 TYR A 112 -20.347 -31.063 25.135 1.00 45.09 C ANISOU 878 CD2 TYR A 112 7792 3290 6051 -950 95 -106 C ATOM 879 CE1 TYR A 112 -19.361 -28.489 25.052 1.00 35.64 C ANISOU 879 CE1 TYR A 112 6453 2811 4277 -820 -28 -682 C ATOM 880 CE2 TYR A 112 -21.036 -30.086 24.444 1.00 43.21 C ANISOU 880 CE2 TYR A 112 7461 3098 5859 -1128 -54 -421 C ATOM 881 CZ TYR A 112 -20.538 -28.801 24.405 1.00 39.23 C ANISOU 881 CZ TYR A 112 6918 2933 5056 -1038 -105 -664 C ATOM 882 OH TYR A 112 -21.221 -27.827 23.716 1.00 41.72 O ANISOU 882 OH TYR A 112 6994 3426 5432 -1039 -193 -846 O ATOM 883 N ASN A 113 -20.874 -33.104 27.918 1.00 55.30 N ANISOU 883 N ASN A 113 9135 4542 7334 -657 799 1047 N ATOM 884 CA ASN A 113 -22.326 -33.252 27.972 1.00 57.44 C ANISOU 884 CA ASN A 113 9285 4550 7990 -1003 983 1070 C ATOM 885 C ASN A 113 -22.897 -33.081 29.377 1.00 59.20 C ANISOU 885 C ASN A 113 9419 5064 8009 -945 1284 1415 C ATOM 886 O ASN A 113 -24.026 -32.620 29.542 1.00 59.19 O ANISOU 886 O ASN A 113 9215 5079 8195 -1225 1370 1303 O ATOM 887 CB ASN A 113 -22.738 -34.615 27.411 1.00 64.35 C ANISOU 887 CB ASN A 113 10296 4742 9413 -1175 1192 1165 C ATOM 888 CG ASN A 113 -22.446 -34.748 25.929 1.00 66.01 C ANISOU 888 CG ASN A 113 10499 4734 9848 -1297 862 731 C ATOM 889 OD1 ASN A 113 -22.502 -33.770 25.182 1.00 61.99 O ANISOU 889 OD1 ASN A 113 9871 4451 9230 -1380 534 338 O ATOM 890 ND2 ASN A 113 -22.134 -35.963 25.495 1.00 72.84 N ANISOU 890 ND2 ASN A 113 11389 5329 10959 -1235 894 795 N ATOM 891 N GLY A 114 -22.115 -33.451 30.385 1.00 62.09 N ANISOU 891 N GLY A 114 9933 5689 7971 -553 1441 1823 N ATOM 892 CA GLY A 114 -22.549 -33.330 31.764 1.00 66.81 C ANISOU 892 CA GLY A 114 10497 6617 8270 -434 1742 2182 C ATOM 893 C GLY A 114 -22.310 -31.944 32.334 1.00 64.73 C ANISOU 893 C GLY A 114 9990 7091 7512 -370 1552 1926 C ATOM 894 O GLY A 114 -22.910 -31.563 33.339 1.00 69.71 O ANISOU 894 O GLY A 114 10516 8027 7944 -397 1771 2072 O ATOM 895 N LEU A 115 -21.428 -31.189 31.686 1.00 57.31 N ANISOU 895 N LEU A 115 8960 6411 6403 -306 1199 1512 N ATOM 896 CA LEU A 115 -21.080 -29.849 32.143 1.00 52.96 C ANISOU 896 CA LEU A 115 8161 6517 5443 -266 1074 1178 C ATOM 897 C LEU A 115 -21.853 -28.779 31.381 1.00 50.30 C ANISOU 897 C LEU A 115 7634 6077 5400 -645 969 742 C ATOM 898 O LEU A 115 -22.359 -27.825 31.971 1.00 43.13 O ANISOU 898 O LEU A 115 6505 5515 4366 -760 1064 600 O ATOM 899 CB LEU A 115 -19.574 -29.614 31.995 1.00 53.60 C ANISOU 899 CB LEU A 115 8235 6966 5166 54 840 946 C ATOM 900 CG LEU A 115 -19.070 -28.170 32.078 1.00 56.43 C ANISOU 900 CG LEU A 115 8315 7874 5251 12 727 406 C ATOM 901 CD1 LEU A 115 -19.368 -27.559 33.437 1.00 60.73 C ANISOU 901 CD1 LEU A 115 8638 9047 5389 73 900 447 C ATOM 902 CD2 LEU A 115 -17.581 -28.104 31.775 1.00 57.93 C ANISOU 902 CD2 LEU A 115 8484 8314 5211 285 534 111 C ATOM 903 N VAL A 116 -21.943 -28.948 30.067 1.00 45.33 N ANISOU 903 N VAL A 116 7097 4979 5146 -806 785 534 N ATOM 904 CA VAL A 116 -22.558 -27.944 29.210 1.00 43.02 C ANISOU 904 CA VAL A 116 6674 4602 5069 -1053 647 144 C ATOM 905 C VAL A 116 -23.912 -28.411 28.681 1.00 43.43 C ANISOU 905 C VAL A 116 6682 4207 5614 -1337 665 181 C ATOM 906 O VAL A 116 -23.981 -29.182 27.725 1.00 46.75 O ANISOU 906 O VAL A 116 7233 4198 6331 -1412 543 136 O ATOM 907 CB VAL A 116 -21.640 -27.594 28.025 1.00 42.81 C ANISOU 907 CB VAL A 116 6780 4461 5024 -988 410 -195 C ATOM 908 CG1 VAL A 116 -22.160 -26.373 27.301 1.00 44.23 C ANISOU 908 CG1 VAL A 116 6865 4639 5301 -1135 330 -545 C ATOM 909 CG2 VAL A 116 -20.218 -27.357 28.512 1.00 40.84 C ANISOU 909 CG2 VAL A 116 6537 4615 4364 -716 410 -289 C ATOM 910 N THR A 117 -24.985 -27.938 29.308 1.00 40.52 N ANISOU 910 N THR A 117 6088 3965 5343 -1505 825 203 N ATOM 911 CA THR A 117 -26.340 -28.324 28.922 1.00 42.37 C ANISOU 911 CA THR A 117 6184 3845 6071 -1785 861 161 C ATOM 912 C THR A 117 -27.130 -27.142 28.368 1.00 40.43 C ANISOU 912 C THR A 117 5700 3710 5952 -1901 694 -188 C ATOM 913 O THR A 117 -26.727 -25.989 28.516 1.00 37.97 O ANISOU 913 O THR A 117 5340 3727 5361 -1791 666 -333 O ATOM 914 CB THR A 117 -27.120 -28.921 30.111 1.00 55.38 C ANISOU 914 CB THR A 117 7749 5459 7833 -1899 1257 488 C ATOM 915 OG1 THR A 117 -27.335 -27.907 31.101 1.00 45.89 O ANISOU 915 OG1 THR A 117 6365 4720 6353 -1884 1402 488 O ATOM 916 CG2 THR A 117 -26.351 -30.078 30.732 1.00 49.19 C ANISOU 916 CG2 THR A 117 7251 4561 6878 -1692 1479 921 C ATOM 917 N GLY A 118 -28.262 -27.439 27.737 1.00 31.40 N ANISOU 917 N GLY A 118 5338 2679 3912 -601 416 847 N ATOM 918 CA GLY A 118 -29.112 -26.410 27.165 1.00 32.15 C ANISOU 918 CA GLY A 118 5330 2995 3892 -666 406 673 C ATOM 919 C GLY A 118 -29.761 -25.535 28.220 1.00 34.04 C ANISOU 919 C GLY A 118 5455 3464 4016 -778 402 738 C ATOM 920 O GLY A 118 -29.942 -24.334 28.019 1.00 34.71 O ANISOU 920 O GLY A 118 5412 3755 4020 -748 381 655 O ATOM 921 N THR A 119 -30.112 -26.143 29.348 1.00 34.46 N ANISOU 921 N THR A 119 5577 3460 4058 -914 443 886 N ATOM 922 CA THR A 119 -30.733 -25.422 30.453 1.00 37.96 C ANISOU 922 CA THR A 119 5968 4085 4369 -1044 503 943 C ATOM 923 C THR A 119 -29.772 -24.400 31.053 1.00 33.76 C ANISOU 923 C THR A 119 5418 3711 3698 -918 437 1032 C ATOM 924 O THR A 119 -30.141 -23.250 31.291 1.00 36.45 O ANISOU 924 O THR A 119 5652 4255 3941 -941 470 958 O ATOM 925 CB THR A 119 -31.204 -26.389 31.556 1.00 44.99 C ANISOU 925 CB THR A 119 7009 4848 5239 -1232 590 1103 C ATOM 926 OG1 THR A 119 -32.142 -27.320 31.004 1.00 48.49 O ANISOU 926 OG1 THR A 119 7447 5133 5845 -1367 648 1015 O ATOM 927 CG2 THR A 119 -31.863 -25.628 32.694 1.00 48.61 C ANISOU 927 CG2 THR A 119 7457 5480 5531 -1382 718 1138 C ATOM 928 N ARG A 120 -28.536 -24.826 31.292 1.00 31.77 N ANISOU 928 N ARG A 120 5257 3341 3475 -788 332 1190 N ATOM 929 CA ARG A 120 -27.512 -23.935 31.826 1.00 33.44 C ANISOU 929 CA ARG A 120 5439 3666 3599 -672 220 1287 C ATOM 930 C ARG A 120 -27.156 -22.848 30.816 1.00 33.18 C ANISOU 930 C ARG A 120 5229 3771 3606 -520 209 1126 C ATOM 931 O ARG A 120 -26.887 -21.707 31.191 1.00 32.14 O ANISOU 931 O ARG A 120 5026 3813 3371 -490 166 1123 O ATOM 932 CB ARG A 120 -26.265 -24.728 32.219 1.00 33.84 C ANISOU 932 CB ARG A 120 5579 3514 3763 -561 74 1505 C ATOM 933 CG ARG A 120 -26.505 -25.715 33.352 1.00 38.36 C ANISOU 933 CG ARG A 120 6370 3944 4261 -718 40 1715 C ATOM 934 CD ARG A 120 -25.314 -26.634 33.565 1.00 39.54 C ANISOU 934 CD ARG A 120 6582 3836 4605 -590 -138 1936 C ATOM 935 NE ARG A 120 -25.575 -27.625 34.605 1.00 43.27 N ANISOU 935 NE ARG A 120 7207 4203 5031 -697 -158 2077 N ATOM 936 CZ ARG A 120 -24.731 -28.594 34.943 1.00 47.18 C ANISOU 936 CZ ARG A 120 7739 4479 5708 -595 -292 2244 C ATOM 937 NH1 ARG A 120 -25.053 -29.451 35.902 1.00 52.16 N ANISOU 937 NH1 ARG A 120 8525 5030 6264 -706 -303 2367 N ATOM 938 NH2 ARG A 120 -23.565 -28.708 34.321 1.00 47.92 N ANISOU 938 NH2 ARG A 120 7705 4423 6079 -378 -401 2283 N ATOM 939 N ALA A 121 -27.164 -23.206 29.535 1.00 32.33 N ANISOU 939 N ALA A 121 5084 3570 3629 -439 254 992 N ATOM 940 CA ALA A 121 -26.869 -22.253 28.472 1.00 29.37 C ANISOU 940 CA ALA A 121 4595 3299 3264 -315 262 846 C ATOM 941 C ALA A 121 -27.935 -21.163 28.406 1.00 27.93 C ANISOU 941 C ALA A 121 4313 3332 2968 -412 277 716 C ATOM 942 O ALA A 121 -27.623 -19.988 28.214 1.00 29.81 O ANISOU 942 O ALA A 121 4449 3717 3160 -334 248 673 O ATOM 943 CB ALA A 121 -26.755 -22.967 27.131 1.00 33.73 C ANISOU 943 CB ALA A 121 5212 3680 3923 -248 325 723 C ATOM 944 N ALA A 122 -29.193 -21.561 28.571 1.00 25.13 N ANISOU 944 N ALA A 122 3966 2972 2611 -583 325 658 N ATOM 945 CA ALA A 122 -30.307 -20.621 28.550 1.00 25.62 C ANISOU 945 CA ALA A 122 3889 3196 2651 -678 349 538 C ATOM 946 C ALA A 122 -30.193 -19.612 29.688 1.00 26.91 C ANISOU 946 C ALA A 122 4001 3522 2701 -693 385 596 C ATOM 947 O ALA A 122 -30.486 -18.429 29.514 1.00 27.72 O ANISOU 947 O ALA A 122 3970 3769 2795 -666 381 502 O ATOM 948 CB ALA A 122 -31.631 -21.365 28.630 1.00 31.04 C ANISOU 948 CB ALA A 122 4558 3805 3429 -868 410 486 C ATOM 949 N GLY A 123 -29.764 -20.088 30.853 1.00 25.69 N ANISOU 949 N GLY A 123 3982 3326 2452 -745 407 752 N ATOM 950 CA GLY A 123 -29.569 -19.224 32.003 1.00 24.33 C ANISOU 950 CA GLY A 123 3843 3282 2118 -784 427 808 C ATOM 951 C GLY A 123 -28.427 -18.253 31.782 1.00 25.63 C ANISOU 951 C GLY A 123 3949 3531 2259 -616 296 823 C ATOM 952 O GLY A 123 -28.515 -17.083 32.151 1.00 26.18 O ANISOU 952 O GLY A 123 3957 3742 2247 -621 311 762 O ATOM 953 N ILE A 124 -27.351 -18.744 31.175 1.00 21.97 N ANISOU 953 N ILE A 124 3492 2958 1896 -470 190 897 N ATOM 954 CA ILE A 124 -26.193 -17.912 30.867 1.00 22.32 C ANISOU 954 CA ILE A 124 3448 3050 1983 -310 86 919 C ATOM 955 C ILE A 124 -26.566 -16.803 29.885 1.00 23.24 C ANISOU 955 C ILE A 124 3417 3290 2125 -252 128 748 C ATOM 956 O ILE A 124 -26.179 -15.646 30.061 1.00 21.43 O ANISOU 956 O ILE A 124 3109 3174 1860 -206 85 731 O ATOM 957 CB ILE A 124 -25.037 -18.754 30.286 1.00 21.50 C ANISOU 957 CB ILE A 124 3346 2765 2058 -162 28 1014 C ATOM 958 CG1 ILE A 124 -24.454 -19.667 31.367 1.00 34.98 C ANISOU 958 CG1 ILE A 124 5180 4336 3775 -196 -86 1228 C ATOM 959 CG2 ILE A 124 -23.949 -17.857 29.716 1.00 24.13 C ANISOU 959 CG2 ILE A 124 3539 3134 2494 0 -18 1005 C ATOM 960 CD1 ILE A 124 -23.405 -20.629 30.853 1.00 36.67 C ANISOU 960 CD1 ILE A 124 5367 4323 4242 -46 -125 1326 C ATOM 961 N ILE A 125 -27.327 -17.164 28.857 1.00 21.01 N ANISOU 961 N ILE A 125 3114 2966 1902 -267 187 630 N ATOM 962 CA ILE A 125 -27.789 -16.198 27.865 1.00 19.11 C ANISOU 962 CA ILE A 125 2767 2816 1678 -231 183 490 C ATOM 963 C ILE A 125 -28.636 -15.109 28.522 1.00 17.74 C ANISOU 963 C ILE A 125 2485 2791 1463 -312 205 425 C ATOM 964 O ILE A 125 -28.468 -13.923 28.236 1.00 18.11 O ANISOU 964 O ILE A 125 2436 2932 1512 -245 171 375 O ATOM 965 CB ILE A 125 -28.595 -16.889 26.749 1.00 22.19 C ANISOU 965 CB ILE A 125 3198 3114 2119 -276 186 385 C ATOM 966 CG1 ILE A 125 -27.672 -17.780 25.911 1.00 23.31 C ANISOU 966 CG1 ILE A 125 3469 3093 2296 -177 207 406 C ATOM 967 CG2 ILE A 125 -29.287 -15.863 25.865 1.00 19.55 C ANISOU 967 CG2 ILE A 125 2769 2867 1792 -275 124 263 C ATOM 968 CD1 ILE A 125 -28.389 -18.586 24.844 1.00 24.02 C ANISOU 968 CD1 ILE A 125 3670 3061 2396 -243 200 293 C ATOM 969 N ALA A 126 -29.532 -15.518 29.416 1.00 21.28 N ANISOU 969 N ALA A 126 2953 3241 1890 -458 291 425 N ATOM 970 CA ALA A 126 -30.375 -14.578 30.148 1.00 21.02 C ANISOU 970 CA ALA A 126 2824 3317 1845 -544 383 348 C ATOM 971 C ALA A 126 -29.538 -13.610 30.984 1.00 21.19 C ANISOU 971 C ALA A 126 2884 3428 1738 -500 363 390 C ATOM 972 O ALA A 126 -29.792 -12.404 30.993 1.00 18.73 O ANISOU 972 O ALA A 126 2461 3204 1451 -477 383 297 O ATOM 973 CB ALA A 126 -31.359 -15.331 31.036 1.00 20.57 C ANISOU 973 CB ALA A 126 2816 3217 1784 -723 541 353 C ATOM 974 N ILE A 127 -28.545 -14.145 31.687 1.00 21.49 N ANISOU 974 N ILE A 127 3082 3423 1660 -495 298 534 N ATOM 975 CA ILE A 127 -27.662 -13.332 32.517 1.00 21.95 C ANISOU 975 CA ILE A 127 3203 3542 1595 -475 217 591 C ATOM 976 C ILE A 127 -26.874 -12.342 31.668 1.00 19.25 C ANISOU 976 C ILE A 127 2716 3245 1354 -319 112 558 C ATOM 977 O ILE A 127 -26.753 -11.166 32.013 1.00 19.80 O ANISOU 977 O ILE A 127 2743 3396 1383 -314 99 501 O ATOM 978 CB ILE A 127 -26.681 -14.211 33.325 1.00 26.61 C ANISOU 978 CB ILE A 127 3981 4042 2089 -496 89 786 C ATOM 979 CG1 ILE A 127 -27.443 -15.042 34.359 1.00 31.24 C ANISOU 979 CG1 ILE A 127 4745 4564 2562 -652 200 815 C ATOM 980 CG2 ILE A 127 -25.624 -13.356 34.013 1.00 23.55 C ANISOU 980 CG2 ILE A 127 3620 3668 1659 -442 -71 825 C ATOM 981 CD1 ILE A 127 -26.591 -16.077 35.062 1.00 35.62 C ANISOU 981 CD1 ILE A 127 5465 4983 3086 -647 50 999 C ATOM 982 N CYS A 128 -26.349 -12.821 30.546 1.00 17.17 N ANISOU 982 N CYS A 128 2396 2910 1219 -201 65 586 N ATOM 983 CA CYS A 128 -25.524 -11.986 29.683 1.00 16.27 C ANISOU 983 CA CYS A 128 2170 2814 1198 -63 6 573 C ATOM 984 C CYS A 128 -26.313 -10.838 29.053 1.00 15.96 C ANISOU 984 C CYS A 128 2018 2863 1184 -55 45 433 C ATOM 985 O CYS A 128 -25.765 -9.759 28.830 1.00 18.38 O ANISOU 985 O CYS A 128 2248 3213 1523 14 2 421 O ATOM 986 CB CYS A 128 -24.864 -12.837 28.598 1.00 16.01 C ANISOU 986 CB CYS A 128 2144 2659 1280 44 16 616 C ATOM 987 SG CYS A 128 -23.575 -13.939 29.238 1.00 26.73 S ANISOU 987 SG CYS A 128 3560 3871 2727 95 -64 805 S ATOM 988 N TRP A 129 -27.593 -11.060 28.772 1.00 15.68 N ANISOU 988 N TRP A 129 1956 2833 1168 -129 109 338 N ATOM 989 CA TRP A 129 -28.434 -9.987 28.250 1.00 14.83 C ANISOU 989 CA TRP A 129 1716 2782 1137 -124 109 223 C ATOM 990 C TRP A 129 -28.701 -8.926 29.315 1.00 16.65 C ANISOU 990 C TRP A 129 1891 3089 1345 -170 167 167 C ATOM 991 O TRP A 129 -28.687 -7.731 29.023 1.00 14.62 O ANISOU 991 O TRP A 129 1534 2868 1152 -113 135 113 O ATOM 992 CB TRP A 129 -29.754 -10.537 27.709 1.00 15.95 C ANISOU 992 CB TRP A 129 1807 2883 1370 -199 124 147 C ATOM 993 CG TRP A 129 -29.666 -10.926 26.266 1.00 17.59 C ANISOU 993 CG TRP A 129 2064 3023 1598 -145 24 144 C ATOM 994 CD1 TRP A 129 -29.520 -12.186 25.760 1.00 16.34 C ANISOU 994 CD1 TRP A 129 2036 2766 1406 -162 21 170 C ATOM 995 CD2 TRP A 129 -29.698 -10.042 25.139 1.00 19.15 C ANISOU 995 CD2 TRP A 129 2228 3223 1824 -77 -83 112 C ATOM 996 NE1 TRP A 129 -29.468 -12.140 24.387 1.00 17.82 N ANISOU 996 NE1 TRP A 129 2297 2899 1574 -118 -66 137 N ATOM 997 CE2 TRP A 129 -29.575 -10.836 23.981 1.00 20.85 C ANISOU 997 CE2 TRP A 129 2593 3347 1982 -70 -140 113 C ATOM 998 CE3 TRP A 129 -29.825 -8.656 24.996 1.00 15.08 C ANISOU 998 CE3 TRP A 129 1597 2762 1370 -30 -136 84 C ATOM 999 CZ2 TRP A 129 -29.574 -10.290 22.697 1.00 22.27 C ANISOU 999 CZ2 TRP A 129 2847 3496 2120 -33 -251 96 C ATOM 1000 CZ3 TRP A 129 -29.820 -8.115 23.722 1.00 17.88 C ANISOU 1000 CZ3 TRP A 129 1994 3082 1719 19 -262 86 C ATOM 1001 CH2 TRP A 129 -29.697 -8.931 22.589 1.00 21.42 C ANISOU 1001 CH2 TRP A 129 2627 3446 2065 10 -320 95 C ATOM 1002 N VAL A 130 -28.939 -9.362 30.548 1.00 17.63 N ANISOU 1002 N VAL A 130 2111 3221 1367 -282 264 178 N ATOM 1003 CA VAL A 130 -29.136 -8.429 31.653 1.00 16.43 C ANISOU 1003 CA VAL A 130 1980 3122 1142 -349 355 107 C ATOM 1004 C VAL A 130 -27.880 -7.586 31.870 1.00 21.30 C ANISOU 1004 C VAL A 130 2637 3768 1688 -278 224 157 C ATOM 1005 O VAL A 130 -27.960 -6.368 32.039 1.00 16.74 O ANISOU 1005 O VAL A 130 1995 3222 1143 -263 243 65 O ATOM 1006 CB VAL A 130 -29.500 -9.159 32.967 1.00 20.66 C ANISOU 1006 CB VAL A 130 2699 3643 1506 -509 496 128 C ATOM 1007 CG1 VAL A 130 -29.448 -8.198 34.148 1.00 21.55 C ANISOU 1007 CG1 VAL A 130 2926 3796 1467 -588 587 54 C ATOM 1008 CG2 VAL A 130 -30.876 -9.798 32.859 1.00 19.21 C ANISOU 1008 CG2 VAL A 130 2431 3423 1445 -601 672 57 C ATOM 1009 N LEU A 131 -26.721 -8.239 31.849 1.00 15.64 N ANISOU 1009 N LEU A 131 2005 3016 920 -235 89 301 N ATOM 1010 CA ALEU A 131 -25.448 -7.546 32.021 0.79 16.79 C ANISOU 1010 CA ALEU A 131 2150 3166 1064 -174 -62 369 C ATOM 1011 CA BLEU A 131 -25.449 -7.549 32.024 0.21 16.87 C ANISOU 1011 CA BLEU A 131 2161 3176 1074 -174 -61 369 C ATOM 1012 C LEU A 131 -25.168 -6.589 30.868 1.00 17.69 C ANISOU 1012 C LEU A 131 2093 3289 1341 -50 -89 328 C ATOM 1013 O LEU A 131 -24.534 -5.550 31.056 1.00 17.88 O ANISOU 1013 O LEU A 131 2075 3328 1391 -26 -160 319 O ATOM 1014 CB ALEU A 131 -24.299 -8.549 32.150 0.79 15.93 C ANISOU 1014 CB ALEU A 131 2109 2982 960 -140 -201 546 C ATOM 1015 CB BLEU A 131 -24.310 -8.563 32.156 0.21 16.32 C ANISOU 1015 CB BLEU A 131 2161 3032 1009 -141 -200 546 C ATOM 1016 CG ALEU A 131 -24.259 -9.387 33.427 0.79 17.69 C ANISOU 1016 CG ALEU A 131 2542 3138 1041 -256 -244 618 C ATOM 1017 CG BLEU A 131 -22.973 -8.037 32.677 0.21 17.58 C ANISOU 1017 CG BLEU A 131 2320 3146 1213 -115 -389 630 C ATOM 1018 CD1ALEU A 131 -23.093 -10.363 33.382 0.79 21.87 C ANISOU 1018 CD1ALEU A 131 3083 3553 1672 -187 -407 796 C ATOM 1019 CD1BLEU A 131 -23.163 -7.342 34.015 0.21 22.85 C ANISOU 1019 CD1BLEU A 131 3146 3826 1709 -241 -420 561 C ATOM 1020 CD2ALEU A 131 -24.172 -8.487 34.654 0.79 18.94 C ANISOU 1020 CD2ALEU A 131 2830 3305 1062 -347 -285 557 C ATOM 1021 CD2BLEU A 131 -21.970 -9.172 32.807 0.21 20.97 C ANISOU 1021 CD2BLEU A 131 2778 3453 1738 -72 -520 798 C ATOM 1022 N ASER A 132 -25.633 -6.941 29.673 0.82 13.36 N ANISOU 1022 N ASER A 132 1472 2717 886 13 -45 307 N ATOM 1023 N BSER A 132 -25.643 -6.941 29.676 0.18 15.79 N ANISOU 1023 N BSER A 132 1780 3025 1193 12 -44 307 N ATOM 1024 CA ASER A 132 -25.438 -6.091 28.503 0.82 12.76 C ANISOU 1024 CA ASER A 132 1292 2635 920 111 -69 285 C ATOM 1025 CA BSER A 132 -25.448 -6.103 28.497 0.18 13.58 C ANISOU 1025 CA BSER A 132 1396 2739 1024 111 -69 285 C ATOM 1026 C ASER A 132 -26.224 -4.788 28.629 0.82 12.49 C ANISOU 1026 C ASER A 132 1166 2641 937 94 -50 170 C ATOM 1027 C BSER A 132 -26.227 -4.797 28.618 0.18 12.48 C ANISOU 1027 C BSER A 132 1166 2640 937 95 -50 170 C ATOM 1028 O ASER A 132 -25.734 -3.720 28.260 0.82 12.45 O ANISOU 1028 O ASER A 132 1097 2632 1001 153 -96 170 O ATOM 1029 O BSER A 132 -25.737 -3.736 28.232 0.18 12.86 O ANISOU 1029 O BSER A 132 1150 2684 1054 154 -96 171 O ATOM 1030 CB ASER A 132 -25.840 -6.831 27.228 0.82 13.43 C ANISOU 1030 CB ASER A 132 1396 2672 1036 150 -48 286 C ATOM 1031 CB BSER A 132 -25.864 -6.850 27.226 0.18 13.34 C ANISOU 1031 CB BSER A 132 1385 2660 1024 148 -47 285 C ATOM 1032 OG ASER A 132 -25.013 -7.961 27.028 0.82 12.50 O ANISOU 1032 OG ASER A 132 1357 2484 907 184 -35 379 O ATOM 1033 OG BSER A 132 -27.257 -7.105 27.212 0.18 14.07 O ANISOU 1033 OG BSER A 132 1455 2763 1129 75 -18 198 O ATOM 1034 N PHE A 133 -27.442 -4.879 29.155 1.00 14.29 N ANISOU 1034 N PHE A 133 1375 2887 1166 14 38 72 N ATOM 1035 CA PHE A 133 -28.252 -3.691 29.399 1.00 18.20 C ANISOU 1035 CA PHE A 133 1760 3389 1767 3 92 -52 C ATOM 1036 C PHE A 133 -27.603 -2.828 30.477 1.00 17.85 C ANISOU 1036 C PHE A 133 1778 3363 1641 -30 106 -87 C ATOM 1037 O PHE A 133 -27.564 -1.605 30.360 1.00 14.11 O ANISOU 1037 O PHE A 133 1225 2872 1266 11 89 -148 O ATOM 1038 CB PHE A 133 -29.681 -4.067 29.807 1.00 18.75 C ANISOU 1038 CB PHE A 133 1766 3447 1910 -82 232 -154 C ATOM 1039 CG PHE A 133 -30.617 -4.243 28.644 1.00 17.28 C ANISOU 1039 CG PHE A 133 1438 3217 1911 -47 164 -167 C ATOM 1040 CD1 PHE A 133 -31.323 -3.161 28.138 1.00 19.04 C ANISOU 1040 CD1 PHE A 133 1483 3397 2354 4 118 -234 C ATOM 1041 CD2 PHE A 133 -30.790 -5.486 28.054 1.00 18.88 C ANISOU 1041 CD2 PHE A 133 1696 3399 2078 -73 115 -108 C ATOM 1042 CE1 PHE A 133 -32.184 -3.316 27.063 1.00 21.32 C ANISOU 1042 CE1 PHE A 133 1654 3628 2818 22 -16 -225 C ATOM 1043 CE2 PHE A 133 -31.650 -5.648 26.979 1.00 20.01 C ANISOU 1043 CE2 PHE A 133 1740 3488 2373 -66 1 -121 C ATOM 1044 CZ PHE A 133 -32.349 -4.561 26.483 1.00 22.68 C ANISOU 1044 CZ PHE A 133 1905 3789 2924 -22 -84 -171 C ATOM 1045 N ALA A 134 -27.085 -3.473 31.519 1.00 14.74 N ANISOU 1045 N ALA A 134 1550 2989 1063 -114 112 -42 N ATOM 1046 CA ALA A 134 -26.427 -2.761 32.610 1.00 18.44 C ANISOU 1046 CA ALA A 134 2137 3463 1407 -178 76 -69 C ATOM 1047 C ALA A 134 -25.194 -2.005 32.119 1.00 17.88 C ANISOU 1047 C ALA A 134 1997 3374 1423 -93 -98 6 C ATOM 1048 O ALA A 134 -25.009 -0.830 32.432 1.00 20.05 O ANISOU 1048 O ALA A 134 2257 3632 1729 -103 -117 -73 O ATOM 1049 CB ALA A 134 -26.044 -3.729 33.722 1.00 17.91 C ANISOU 1049 CB ALA A 134 2298 3401 1106 -296 48 9 C ATOM 1050 N ILE A 135 -24.354 -2.687 31.348 1.00 17.00 N ANISOU 1050 N ILE A 135 1841 3246 1372 -15 -198 151 N ATOM 1051 CA ILE A 135 -23.145 -2.080 30.801 1.00 17.46 C ANISOU 1051 CA ILE A 135 1806 3269 1560 63 -317 235 C ATOM 1052 C ILE A 135 -23.471 -0.993 29.781 1.00 13.74 C ANISOU 1052 C ILE A 135 1206 2782 1234 141 -271 178 C ATOM 1053 O ILE A 135 -22.951 0.124 29.858 1.00 15.11 O ANISOU 1053 O ILE A 135 1327 2927 1487 148 -327 161 O ATOM 1054 CB ILE A 135 -22.239 -3.142 30.141 1.00 18.60 C ANISOU 1054 CB ILE A 135 1919 3371 1776 136 -360 390 C ATOM 1055 CG1 ILE A 135 -21.607 -4.037 31.209 1.00 18.67 C ANISOU 1055 CG1 ILE A 135 2034 3358 1700 70 -480 489 C ATOM 1056 CG2 ILE A 135 -21.157 -2.482 29.294 1.00 20.17 C ANISOU 1056 CG2 ILE A 135 1993 3499 2170 221 -386 454 C ATOM 1057 CD1 ILE A 135 -20.806 -5.190 30.646 1.00 18.84 C ANISOU 1057 CD1 ILE A 135 2017 3286 1857 147 -491 619 C ATOM 1058 N GLY A 136 -24.342 -1.322 28.832 1.00 12.71 N ANISOU 1058 N GLY A 136 1039 2652 1137 187 -198 158 N ATOM 1059 CA GLY A 136 -24.675 -0.415 27.747 1.00 11.96 C ANISOU 1059 CA GLY A 136 858 2523 1165 256 -200 141 C ATOM 1060 C GLY A 136 -25.439 0.824 28.173 1.00 13.55 C ANISOU 1060 C GLY A 136 989 2707 1453 238 -183 16 C ATOM 1061 O GLY A 136 -25.278 1.893 27.582 1.00 14.15 O ANISOU 1061 O GLY A 136 999 2731 1647 289 -226 25 O ATOM 1062 N LEU A 137 -26.274 0.687 29.198 1.00 14.00 N ANISOU 1062 N LEU A 137 1068 2788 1464 164 -96 -102 N ATOM 1063 CA LEU A 137 -27.072 1.811 29.675 1.00 14.62 C ANISOU 1063 CA LEU A 137 1075 2822 1659 151 -21 -250 C ATOM 1064 C LEU A 137 -26.491 2.442 30.935 1.00 15.20 C ANISOU 1064 C LEU A 137 1256 2889 1631 71 3 -331 C ATOM 1065 O LEU A 137 -27.171 3.197 31.627 1.00 16.49 O ANISOU 1065 O LEU A 137 1416 3007 1843 33 126 -491 O ATOM 1066 CB LEU A 137 -28.514 1.372 29.936 1.00 16.72 C ANISOU 1066 CB LEU A 137 1278 3084 1992 113 119 -356 C ATOM 1067 CG LEU A 137 -29.242 0.749 28.740 1.00 17.29 C ANISOU 1067 CG LEU A 137 1247 3143 2179 165 50 -291 C ATOM 1068 CD1 LEU A 137 -30.704 0.513 29.073 1.00 17.76 C ANISOU 1068 CD1 LEU A 137 1178 3169 2400 121 182 -407 C ATOM 1069 CD2 LEU A 137 -29.100 1.623 27.500 1.00 19.19 C ANISOU 1069 CD2 LEU A 137 1408 3321 2564 264 -106 -220 C ATOM 1070 N THR A 138 -25.235 2.131 31.235 1.00 14.17 N ANISOU 1070 N THR A 138 1149 2611 1623 222 -554 -144 N ATOM 1071 CA THR A 138 -24.538 2.768 32.354 1.00 13.50 C ANISOU 1071 CA THR A 138 1053 2695 1383 155 -350 -107 C ATOM 1072 C THR A 138 -24.573 4.313 32.289 1.00 16.19 C ANISOU 1072 C THR A 138 1433 3093 1627 171 -228 -185 C ATOM 1073 O THR A 138 -24.746 4.958 33.325 1.00 15.34 O ANISOU 1073 O THR A 138 1332 3052 1445 125 -94 -180 O ATOM 1074 CB THR A 138 -23.071 2.270 32.451 1.00 19.86 C ANISOU 1074 CB THR A 138 1926 3565 2056 179 -367 -82 C ATOM 1075 OG1 THR A 138 -23.051 0.975 33.065 1.00 22.84 O ANISOU 1075 OG1 THR A 138 2263 3896 2518 134 -440 19 O ATOM 1076 CG2 THR A 138 -22.220 3.216 33.285 1.00 22.03 C ANISOU 1076 CG2 THR A 138 2217 3977 2175 99 -255 -58 C ATOM 1077 N PRO A 139 -24.434 4.914 31.085 1.00 14.12 N ANISOU 1077 N PRO A 139 1229 2789 1347 260 -286 -253 N ATOM 1078 CA PRO A 139 -24.586 6.377 31.048 1.00 12.55 C ANISOU 1078 CA PRO A 139 1061 2594 1113 260 -203 -298 C ATOM 1079 C PRO A 139 -25.927 6.905 31.573 1.00 18.42 C ANISOU 1079 C PRO A 139 1736 3297 1964 271 -114 -315 C ATOM 1080 O PRO A 139 -25.984 8.029 32.066 1.00 13.87 O ANISOU 1080 O PRO A 139 1230 2714 1327 284 -17 -370 O ATOM 1081 CB PRO A 139 -24.434 6.699 29.559 1.00 16.61 C ANISOU 1081 CB PRO A 139 1625 3071 1614 370 -290 -314 C ATOM 1082 CG PRO A 139 -23.505 5.647 29.062 1.00 13.15 C ANISOU 1082 CG PRO A 139 1232 2678 1085 449 -348 -280 C ATOM 1083 CD PRO A 139 -23.900 4.399 29.806 1.00 12.63 C ANISOU 1083 CD PRO A 139 1124 2565 1109 392 -406 -278 C ATOM 1084 N AMET A 140 -26.983 6.103 31.480 0.53 14.13 N ANISOU 1084 N AMET A 140 1057 2713 1600 278 -160 -248 N ATOM 1085 N BMET A 140 -26.981 6.099 31.462 0.47 14.13 N ANISOU 1085 N BMET A 140 1056 2711 1600 279 -163 -248 N ATOM 1086 CA AMET A 140 -28.286 6.518 31.991 0.53 15.60 C ANISOU 1086 CA AMET A 140 1096 2901 1930 319 -33 -180 C ATOM 1087 CA BMET A 140 -28.304 6.477 31.957 0.47 18.45 C ANISOU 1087 CA BMET A 140 1452 3258 2299 318 -42 -177 C ATOM 1088 C AMET A 140 -28.329 6.482 33.520 0.53 20.14 C ANISOU 1088 C AMET A 140 1662 3602 2389 319 195 -120 C ATOM 1089 C BMET A 140 -28.320 6.628 33.474 0.47 19.79 C ANISOU 1089 C BMET A 140 1631 3552 2335 329 198 -136 C ATOM 1090 O AMET A 140 -29.299 6.931 34.132 0.53 18.45 O ANISOU 1090 O AMET A 140 1350 3440 2222 423 390 -49 O ATOM 1091 O BMET A 140 -29.175 7.317 34.031 0.47 18.79 O ANISOU 1091 O BMET A 140 1453 3464 2224 445 392 -108 O ATOM 1092 CB AMET A 140 -29.396 5.638 31.413 0.53 20.40 C ANISOU 1092 CB AMET A 140 1499 3419 2832 292 -199 -47 C ATOM 1093 CB BMET A 140 -29.353 5.442 31.540 0.47 19.82 C ANISOU 1093 CB BMET A 140 1417 3353 2761 277 -199 -30 C ATOM 1094 CG AMET A 140 -29.467 5.653 29.893 0.53 19.08 C ANISOU 1094 CG AMET A 140 1407 3117 2727 326 -471 -126 C ATOM 1095 CG BMET A 140 -29.469 5.224 30.044 0.47 19.63 C ANISOU 1095 CG BMET A 140 1453 3179 2825 296 -499 -95 C ATOM 1096 SD AMET A 140 -30.929 4.814 29.253 0.53 19.70 S ANISOU 1096 SD AMET A 140 1261 3029 3197 266 -776 36 S ATOM 1097 SD BMET A 140 -30.285 6.597 29.213 0.47 21.50 S ANISOU 1097 SD BMET A 140 1655 3369 3144 403 -504 -126 S ATOM 1098 CE AMET A 140 -32.230 5.923 29.787 0.53 21.11 C ANISOU 1098 CE AMET A 140 1155 3284 3581 337 -532 194 C ATOM 1099 CE BMET A 140 -31.911 6.543 29.962 0.47 19.85 C ANISOU 1099 CE BMET A 140 1078 3177 3287 397 -395 116 C ATOM 1100 N ALEU A 141 -27.276 5.949 34.132 0.53 18.57 N ANISOU 1100 N ALEU A 141 1572 3467 2016 238 181 -128 N ATOM 1101 N BLEU A 141 -27.374 5.972 34.139 0.47 18.44 N ANISOU 1101 N BLEU A 141 1546 3451 2011 244 189 -123 N ATOM 1102 CA ALEU A 141 -27.189 5.887 35.587 0.53 19.35 C ANISOU 1102 CA ALEU A 141 1726 3696 1930 247 362 -74 C ATOM 1103 CA BLEU A 141 -27.330 5.962 35.596 0.47 19.14 C ANISOU 1103 CA BLEU A 141 1689 3669 1913 262 380 -72 C ATOM 1104 C ALEU A 141 -26.518 7.131 36.162 0.53 21.34 C ANISOU 1104 C ALEU A 141 2246 3949 1913 295 409 -251 C ATOM 1105 C BLEU A 141 -26.682 7.223 36.159 0.47 21.55 C ANISOU 1105 C BLEU A 141 2265 3973 1950 315 431 -253 C ATOM 1106 O ALEU A 141 -26.378 7.262 37.378 0.53 23.27 O ANISOU 1106 O ALEU A 141 2638 4283 1921 338 523 -261 O ATOM 1107 O BLEU A 141 -26.710 7.454 37.368 0.47 24.11 O ANISOU 1107 O BLEU A 141 2731 4385 2043 386 573 -267 O ATOM 1108 CB ALEU A 141 -26.429 4.635 36.028 0.53 19.12 C ANISOU 1108 CB ALEU A 141 1681 3717 1865 127 275 35 C ATOM 1109 CB BLEU A 141 -26.586 4.721 36.101 0.47 18.87 C ANISOU 1109 CB BLEU A 141 1642 3693 1834 142 303 40 C ATOM 1110 CG ALEU A 141 -26.979 3.295 35.538 0.53 20.20 C ANISOU 1110 CG ALEU A 141 1609 3781 2285 60 147 204 C ATOM 1111 CG BLEU A 141 -27.377 3.415 36.235 0.47 21.08 C ANISOU 1111 CG BLEU A 141 1682 3974 2352 86 289 281 C ATOM 1112 CD1ALEU A 141 -26.166 2.142 36.106 0.53 17.16 C ANISOU 1112 CD1ALEU A 141 1243 3423 1855 -33 67 310 C ATOM 1113 CD1BLEU A 141 -27.900 2.920 34.890 0.47 21.62 C ANISOU 1113 CD1BLEU A 141 1623 3863 2728 53 56 288 C ATOM 1114 CD2ALEU A 141 -28.448 3.152 35.902 0.53 21.75 C ANISOU 1114 CD2ALEU A 141 1561 4012 2690 93 286 413 C ATOM 1115 CD2BLEU A 141 -26.529 2.344 36.907 0.47 18.70 C ANISOU 1115 CD2BLEU A 141 1416 3719 1972 -14 222 387 C ATOM 1116 N GLY A 142 -26.099 8.038 35.285 1.00 16.63 N ANISOU 1116 N GLY A 142 1736 3234 1349 287 289 -377 N ATOM 1117 CA GLY A 142 -25.498 9.287 35.715 1.00 17.50 C ANISOU 1117 CA GLY A 142 2100 3265 1283 297 249 -528 C ATOM 1118 C GLY A 142 -24.190 9.647 35.041 1.00 18.88 C ANISOU 1118 C GLY A 142 2328 3368 1479 150 30 -533 C ATOM 1119 O GLY A 142 -23.758 10.798 35.092 1.00 17.32 O ANISOU 1119 O GLY A 142 2298 3039 1243 121 -75 -618 O ATOM 1120 N TRP A 143 -23.548 8.668 34.415 1.00 17.94 N ANISOU 1120 N TRP A 143 2061 3322 1435 72 -42 -415 N ATOM 1121 CA TRP A 143 -22.294 8.926 33.721 1.00 15.30 C ANISOU 1121 CA TRP A 143 1706 2976 1132 -20 -184 -338 C ATOM 1122 C TRP A 143 -22.596 9.506 32.341 1.00 16.09 C ANISOU 1122 C TRP A 143 1748 3012 1353 55 -191 -324 C ATOM 1123 O TRP A 143 -22.460 8.826 31.326 1.00 13.85 O ANISOU 1123 O TRP A 143 1367 2785 1110 123 -194 -251 O ATOM 1124 CB TRP A 143 -21.460 7.646 33.614 1.00 13.54 C ANISOU 1124 CB TRP A 143 1365 2872 909 -52 -215 -208 C ATOM 1125 CG TRP A 143 -20.006 7.876 33.290 1.00 13.91 C ANISOU 1125 CG TRP A 143 1350 2962 975 -135 -320 -57 C ATOM 1126 CD1 TRP A 143 -19.416 9.055 32.928 1.00 17.63 C ANISOU 1126 CD1 TRP A 143 1825 3367 1506 -215 -409 13 C ATOM 1127 CD2 TRP A 143 -18.962 6.894 33.304 1.00 13.96 C ANISOU 1127 CD2 TRP A 143 1245 3058 1003 -138 -333 100 C ATOM 1128 NE1 TRP A 143 -18.071 8.865 32.713 1.00 16.42 N ANISOU 1128 NE1 TRP A 143 1517 3309 1413 -283 -477 247 N ATOM 1129 CE2 TRP A 143 -17.767 7.547 32.938 1.00 15.03 C ANISOU 1129 CE2 TRP A 143 1276 3229 1206 -214 -411 289 C ATOM 1130 CE3 TRP A 143 -18.922 5.525 33.589 1.00 13.61 C ANISOU 1130 CE3 TRP A 143 1168 3035 967 -80 -287 125 C ATOM 1131 CZ2 TRP A 143 -16.547 6.878 32.850 1.00 16.33 C ANISOU 1131 CZ2 TRP A 143 1297 3471 1438 -200 -394 500 C ATOM 1132 CZ3 TRP A 143 -17.711 4.863 33.502 1.00 17.03 C ANISOU 1132 CZ3 TRP A 143 1501 3527 1444 -61 -297 291 C ATOM 1133 CH2 TRP A 143 -16.539 5.540 33.136 1.00 15.33 C ANISOU 1133 CH2 TRP A 143 1171 3369 1284 -107 -329 477 C ATOM 1134 N ASN A 144 -23.021 10.765 32.318 1.00 17.45 N ANISOU 1134 N ASN A 144 2020 3052 1560 71 -205 -401 N ATOM 1135 CA ASN A 144 -23.414 11.420 31.076 1.00 16.51 C ANISOU 1135 CA ASN A 144 1858 2863 1553 145 -219 -367 C ATOM 1136 C ASN A 144 -23.147 12.923 31.115 1.00 16.08 C ANISOU 1136 C ASN A 144 1925 2630 1555 86 -319 -377 C ATOM 1137 O ASN A 144 -22.733 13.463 32.141 1.00 17.44 O ANISOU 1137 O ASN A 144 2255 2700 1670 -4 -408 -451 O ATOM 1138 CB ASN A 144 -24.893 11.158 30.778 1.00 15.76 C ANISOU 1138 CB ASN A 144 1703 2749 1536 288 -134 -439 C ATOM 1139 CG ASN A 144 -25.808 11.638 31.893 1.00 20.91 C ANISOU 1139 CG ASN A 144 2429 3341 2173 360 -19 -555 C ATOM 1140 OD1 ASN A 144 -25.908 12.835 32.153 1.00 21.17 O ANISOU 1140 OD1 ASN A 144 2608 3232 2203 402 -31 -639 O ATOM 1141 ND2 ASN A 144 -26.492 10.705 32.546 1.00 15.88 N ANISOU 1141 ND2 ASN A 144 1698 2805 1529 404 98 -539 N ATOM 1142 N ASN A 145 -23.390 13.591 29.993 1.00 18.38 N ANISOU 1142 N ASN A 145 2174 2857 1952 140 -343 -299 N ATOM 1143 CA ASN A 145 -23.152 15.025 29.886 1.00 21.06 C ANISOU 1143 CA ASN A 145 2615 2985 2401 74 -471 -264 C ATOM 1144 C ASN A 145 -24.442 15.840 29.919 1.00 22.06 C ANISOU 1144 C ASN A 145 2846 2935 2601 230 -432 -418 C ATOM 1145 O ASN A 145 -24.467 16.987 29.475 1.00 22.93 O ANISOU 1145 O ASN A 145 3023 2850 2841 224 -538 -369 O ATOM 1146 CB ASN A 145 -22.383 15.339 28.601 1.00 23.62 C ANISOU 1146 CB ASN A 145 2802 3363 2809 27 -520 15 C ATOM 1147 CG ASN A 145 -20.989 14.742 28.593 1.00 29.49 C ANISOU 1147 CG ASN A 145 3407 4277 3519 -95 -536 233 C ATOM 1148 OD1 ASN A 145 -20.334 14.649 29.631 1.00 29.70 O ANISOU 1148 OD1 ASN A 145 3472 4273 3540 -244 -635 207 O ATOM 1149 ND2 ASN A 145 -20.527 14.334 27.416 1.00 31.77 N ANISOU 1149 ND2 ASN A 145 3544 4758 3769 0 -439 461 N ATOM 1150 N CYS A 146 -25.510 15.249 30.446 1.00 24.45 N ANISOU 1150 N CYS A 146 3133 3305 2851 378 -277 -560 N ATOM 1151 CA CYS A 146 -26.809 15.917 30.478 1.00 25.64 C ANISOU 1151 CA CYS A 146 3313 3332 3097 576 -191 -656 C ATOM 1152 C CYS A 146 -26.835 17.063 31.484 1.00 27.91 C ANISOU 1152 C CYS A 146 3885 3381 3338 649 -224 -832 C ATOM 1153 O CYS A 146 -27.656 17.974 31.377 1.00 30.32 O ANISOU 1153 O CYS A 146 4264 3510 3746 829 -194 -898 O ATOM 1154 CB CYS A 146 -27.921 14.914 30.797 1.00 25.27 C ANISOU 1154 CB CYS A 146 3099 3448 3053 709 -5 -671 C ATOM 1155 SG CYS A 146 -28.242 13.710 29.481 1.00 30.51 S ANISOU 1155 SG CYS A 146 3506 4269 3819 670 -74 -513 S ATOM 1156 N GLY A 147 -25.932 17.016 32.458 1.00 29.14 N ANISOU 1156 N GLY A 147 4231 3510 3332 528 -316 -915 N ATOM 1157 CA GLY A 147 -25.836 18.063 33.459 1.00 27.67 C ANISOU 1157 CA GLY A 147 4415 3053 3045 600 -430 -1126 C ATOM 1158 C GLY A 147 -25.245 19.344 32.901 1.00 32.67 C ANISOU 1158 C GLY A 147 5181 3361 3873 469 -727 -1078 C ATOM 1159 O GLY A 147 -25.473 20.429 33.435 1.00 34.59 O ANISOU 1159 O GLY A 147 5754 3282 4108 589 -855 -1268 O ATOM 1160 N GLN A 148 -24.483 19.217 31.820 1.00 32.07 N ANISOU 1160 N GLN A 148 4859 3358 3969 246 -837 -803 N ATOM 1161 CA GLN A 148 -23.862 20.370 31.179 1.00 40.88 C ANISOU 1161 CA GLN A 148 6016 4197 5318 84 -1110 -642 C ATOM 1162 C GLN A 148 -24.190 20.409 29.690 1.00 36.27 C ANISOU 1162 C GLN A 148 5158 3726 4897 119 -1014 -391 C ATOM 1163 O GLN A 148 -23.320 20.175 28.852 1.00 37.50 O ANISOU 1163 O GLN A 148 5099 4028 5122 -49 -1056 -90 O ATOM 1164 CB GLN A 148 -22.346 20.343 31.384 1.00 55.46 C ANISOU 1164 CB GLN A 148 7827 6023 7223 -247 -1377 -447 C ATOM 1165 CG GLN A 148 -21.908 20.418 32.839 1.00 68.20 C ANISOU 1165 CG GLN A 148 9765 7477 8670 -316 -1583 -683 C ATOM 1166 CD GLN A 148 -22.115 21.793 33.444 1.00 80.02 C ANISOU 1166 CD GLN A 148 11698 8485 10221 -269 -1883 -912 C ATOM 1167 OE1 GLN A 148 -22.772 21.939 34.474 1.00 85.66 O ANISOU 1167 OE1 GLN A 148 12780 9083 10682 -25 -1835 -1268 O ATOM 1168 NE2 GLN A 148 -21.544 22.810 32.809 1.00 84.23 N ANISOU 1168 NE2 GLN A 148 12208 8718 11077 -481 -2197 -690 N ATOM 1169 N PRO A 149 -25.453 20.712 29.356 1.00 34.13 N ANISOU 1169 N PRO A 149 4894 3401 4673 367 -879 -491 N ATOM 1170 CA PRO A 149 -25.894 20.682 27.959 1.00 31.86 C ANISOU 1170 CA PRO A 149 4381 3228 4496 426 -819 -272 C ATOM 1171 C PRO A 149 -25.305 21.813 27.119 1.00 33.34 C ANISOU 1171 C PRO A 149 4571 3202 4894 292 -1030 -9 C ATOM 1172 O PRO A 149 -24.970 22.876 27.645 1.00 30.95 O ANISOU 1172 O PRO A 149 4478 2547 4734 205 -1249 -53 O ATOM 1173 CB PRO A 149 -27.412 20.829 28.075 1.00 35.53 C ANISOU 1173 CB PRO A 149 4858 3641 5002 717 -670 -443 C ATOM 1174 CG PRO A 149 -27.607 21.614 29.321 1.00 39.73 C ANISOU 1174 CG PRO A 149 5696 3889 5509 832 -701 -706 C ATOM 1175 CD PRO A 149 -26.523 21.167 30.262 1.00 37.64 C ANISOU 1175 CD PRO A 149 5566 3669 5065 637 -784 -787 C ATOM 1176 N LYS A 150 -25.178 21.573 25.818 1.00 33.27 N ANISOU 1176 N LYS A 150 4353 3393 4895 284 -983 276 N ATOM 1177 CA LYS A 150 -24.750 22.609 24.890 1.00 32.88 C ANISOU 1177 CA LYS A 150 4263 3191 5039 189 -1136 605 C ATOM 1178 C LYS A 150 -25.934 23.509 24.560 1.00 36.80 C ANISOU 1178 C LYS A 150 4850 3439 5693 380 -1183 534 C ATOM 1179 O LYS A 150 -26.669 23.265 23.602 1.00 30.54 O ANISOU 1179 O LYS A 150 3941 2802 4859 534 -1101 626 O ATOM 1180 CB LYS A 150 -24.163 21.991 23.620 1.00 34.91 C ANISOU 1180 CB LYS A 150 4296 3800 5167 178 -1026 956 C ATOM 1181 CG LYS A 150 -22.885 21.203 23.860 1.00 39.19 C ANISOU 1181 CG LYS A 150 4712 4583 5596 25 -963 1099 C ATOM 1182 CD LYS A 150 -22.281 20.715 22.556 1.00 43.16 C ANISOU 1182 CD LYS A 150 5027 5430 5940 101 -812 1471 C ATOM 1183 CE LYS A 150 -20.905 20.115 22.780 1.00 46.60 C ANISOU 1183 CE LYS A 150 5290 6087 6329 -28 -737 1697 C ATOM 1184 NZ LYS A 150 -19.961 21.110 23.358 1.00 48.81 N ANISOU 1184 NZ LYS A 150 5494 6118 6934 -339 -962 1945 N ATOM 1185 N GLU A 151 -26.112 24.548 25.369 1.00 40.37 N ANISOU 1185 N GLU A 151 5535 3482 6321 387 -1346 364 N ATOM 1186 CA GLU A 151 -27.283 25.410 25.274 1.00 45.20 C ANISOU 1186 CA GLU A 151 6258 3822 7093 629 -1370 249 C ATOM 1187 C GLU A 151 -27.278 26.252 24.002 1.00 43.07 C ANISOU 1187 C GLU A 151 5891 3441 7031 591 -1506 617 C ATOM 1188 O GLU A 151 -28.335 26.586 23.469 1.00 41.26 O ANISOU 1188 O GLU A 151 5627 3157 6893 810 -1473 624 O ATOM 1189 CB GLU A 151 -27.372 26.319 26.500 1.00 56.57 C ANISOU 1189 CB GLU A 151 8054 4817 8624 699 -1522 -56 C ATOM 1190 CG GLU A 151 -28.782 26.482 27.036 1.00 66.45 C ANISOU 1190 CG GLU A 151 9417 5976 9855 1098 -1338 -359 C ATOM 1191 CD GLU A 151 -29.364 25.174 27.532 1.00 66.40 C ANISOU 1191 CD GLU A 151 9253 6374 9601 1239 -1018 -521 C ATOM 1192 OE1 GLU A 151 -30.467 24.801 27.080 1.00 69.13 O ANISOU 1192 OE1 GLU A 151 9378 6899 9991 1451 -833 -478 O ATOM 1193 OE2 GLU A 151 -28.717 24.519 28.375 1.00 65.29 O ANISOU 1193 OE2 GLU A 151 9197 6359 9252 1122 -983 -658 O ATOM 1194 N GLY A 152 -26.089 26.597 23.523 1.00 43.23 N ANISOU 1194 N GLY A 152 5840 3441 7144 314 -1659 970 N ATOM 1195 CA GLY A 152 -25.964 27.372 22.303 1.00 43.46 C ANISOU 1195 CA GLY A 152 5756 3404 7351 264 -1768 1403 C ATOM 1196 C GLY A 152 -26.440 26.590 21.097 1.00 41.92 C ANISOU 1196 C GLY A 152 5364 3640 6923 425 -1565 1574 C ATOM 1197 O GLY A 152 -27.112 27.127 20.216 1.00 40.27 O ANISOU 1197 O GLY A 152 5131 3372 6798 555 -1616 1748 O ATOM 1198 N LYS A 153 -26.089 25.310 21.062 1.00 40.80 N ANISOU 1198 N LYS A 153 5116 3907 6479 429 -1372 1515 N ATOM 1199 CA LYS A 153 -26.512 24.428 19.985 1.00 39.95 C ANISOU 1199 CA LYS A 153 4906 4178 6095 603 -1234 1606 C ATOM 1200 C LYS A 153 -28.015 24.176 20.061 1.00 36.63 C ANISOU 1200 C LYS A 153 4519 3714 5686 832 -1232 1310 C ATOM 1201 O LYS A 153 -28.706 24.164 19.041 1.00 34.36 O ANISOU 1201 O LYS A 153 4195 3517 5342 977 -1282 1442 O ATOM 1202 CB LYS A 153 -25.743 23.108 20.047 1.00 39.75 C ANISOU 1202 CB LYS A 153 4808 4531 5766 573 -1060 1573 C ATOM 1203 CG LYS A 153 -26.044 22.156 18.906 1.00 40.40 C ANISOU 1203 CG LYS A 153 4871 4966 5514 775 -967 1642 C ATOM 1204 CD LYS A 153 -25.219 20.885 19.021 1.00 42.95 C ANISOU 1204 CD LYS A 153 5159 5607 5552 783 -803 1594 C ATOM 1205 CE LYS A 153 -23.730 21.190 18.990 1.00 47.56 C ANISOU 1205 CE LYS A 153 5615 6291 6163 626 -714 1963 C ATOM 1206 NZ LYS A 153 -22.910 19.950 19.024 1.00 49.41 N ANISOU 1206 NZ LYS A 153 5798 6853 6123 691 -529 1953 N ATOM 1207 N ALA A 154 -28.513 23.987 21.279 1.00 32.59 N ANISOU 1207 N ALA A 154 4065 3070 5249 872 -1180 949 N ATOM 1208 CA ALA A 154 -29.931 23.729 21.501 1.00 34.99 C ANISOU 1208 CA ALA A 154 4324 3352 5619 1093 -1137 729 C ATOM 1209 C ALA A 154 -30.788 24.920 21.083 1.00 36.15 C ANISOU 1209 C ALA A 154 4487 3211 6037 1241 -1261 832 C ATOM 1210 O ALA A 154 -31.841 24.751 20.466 1.00 35.66 O ANISOU 1210 O ALA A 154 4305 3217 6027 1405 -1298 880 O ATOM 1211 CB ALA A 154 -30.182 23.383 22.962 1.00 31.45 C ANISOU 1211 CB ALA A 154 3932 2843 5173 1137 -1000 387 C ATOM 1212 N HIS A 155 -30.336 26.125 21.417 1.00 39.57 N ANISOU 1212 N HIS A 155 5071 3291 6671 1178 -1371 881 N ATOM 1213 CA HIS A 155 -31.075 27.335 21.070 1.00 42.19 C ANISOU 1213 CA HIS A 155 5450 3290 7290 1329 -1505 981 C ATOM 1214 C HIS A 155 -31.099 27.571 19.565 1.00 41.73 C ANISOU 1214 C HIS A 155 5285 3410 7159 1274 -1574 1342 C ATOM 1215 O HIS A 155 -32.115 27.989 19.011 1.00 43.41 O ANISOU 1215 O HIS A 155 5447 3610 7438 1418 -1584 1378 O ATOM 1216 CB HIS A 155 -30.478 28.552 21.780 1.00 48.57 C ANISOU 1216 CB HIS A 155 6500 3659 8295 1230 -1642 924 C ATOM 1217 CG HIS A 155 -30.790 28.609 23.242 1.00 58.59 C ANISOU 1217 CG HIS A 155 7976 4720 9566 1384 -1559 498 C ATOM 1218 ND1 HIS A 155 -32.001 28.203 23.761 1.00 64.08 N ANISOU 1218 ND1 HIS A 155 8604 5539 10203 1684 -1320 256 N ATOM 1219 CD2 HIS A 155 -30.048 29.021 24.297 1.00 64.95 C ANISOU 1219 CD2 HIS A 155 9058 5248 10371 1278 -1667 291 C ATOM 1220 CE1 HIS A 155 -31.992 28.363 25.072 1.00 68.89 C ANISOU 1220 CE1 HIS A 155 9453 5987 10736 1796 -1230 -75 C ATOM 1221 NE2 HIS A 155 -30.818 28.857 25.423 1.00 69.28 N ANISOU 1221 NE2 HIS A 155 9746 5782 10796 1553 -1462 -94 N ATOM 1222 N SER A 156 -29.975 27.302 18.907 1.00 41.15 N ANISOU 1222 N SER A 156 5182 3531 6921 1083 -1596 1622 N ATOM 1223 CA SER A 156 -29.859 27.528 17.472 1.00 47.55 C ANISOU 1223 CA SER A 156 5942 4550 7575 1063 -1612 1959 C ATOM 1224 C SER A 156 -30.793 26.611 16.688 1.00 45.64 C ANISOU 1224 C SER A 156 5647 4617 7078 1244 -1579 1884 C ATOM 1225 O SER A 156 -31.233 26.952 15.591 1.00 43.67 O ANISOU 1225 O SER A 156 5410 4446 6738 1316 -1641 2054 O ATOM 1226 CB SER A 156 -28.413 27.328 17.011 1.00 42.83 C ANISOU 1226 CB SER A 156 5305 4169 6798 869 -1548 2268 C ATOM 1227 OG SER A 156 -27.974 26.006 17.263 1.00 59.06 O ANISOU 1227 OG SER A 156 7323 6531 8588 881 -1423 2158 O ATOM 1228 N GLN A 157 -31.098 25.451 17.260 1.00 43.12 N ANISOU 1228 N GLN A 157 5281 4451 6653 1301 -1516 1626 N ATOM 1229 CA GLN A 157 -32.009 24.508 16.625 1.00 46.23 C ANISOU 1229 CA GLN A 157 5629 5088 6847 1424 -1545 1529 C ATOM 1230 C GLN A 157 -33.435 24.708 17.122 1.00 45.79 C ANISOU 1230 C GLN A 157 5459 4884 7055 1538 -1558 1353 C ATOM 1231 O GLN A 157 -34.352 24.003 16.704 1.00 48.82 O ANISOU 1231 O GLN A 157 5759 5422 7370 1596 -1615 1299 O ATOM 1232 CB GLN A 157 -31.559 23.071 16.878 1.00 48.95 C ANISOU 1232 CB GLN A 157 5972 5688 6937 1399 -1484 1380 C ATOM 1233 CG GLN A 157 -30.172 22.766 16.348 1.00 58.14 C ANISOU 1233 CG GLN A 157 7231 7062 7796 1336 -1414 1573 C ATOM 1234 CD GLN A 157 -29.835 21.294 16.425 1.00 63.60 C ANISOU 1234 CD GLN A 157 7957 8012 8195 1366 -1368 1413 C ATOM 1235 OE1 GLN A 157 -28.689 20.895 16.220 1.00 69.93 O ANISOU 1235 OE1 GLN A 157 8812 9004 8754 1319 -1232 1511 O ATOM 1236 NE2 GLN A 157 -30.837 20.475 16.719 1.00 64.07 N ANISOU 1236 NE2 GLN A 157 7955 8085 8305 1394 -1427 1169 N ATOM 1237 N GLY A 158 -33.612 25.671 18.019 1.00 44.41 N ANISOU 1237 N GLY A 158 5290 4406 7177 1577 -1506 1278 N ATOM 1238 CA GLY A 158 -34.927 26.006 18.532 1.00 43.64 C ANISOU 1238 CA GLY A 158 5085 4187 7308 1747 -1450 1151 C ATOM 1239 C GLY A 158 -35.504 24.952 19.457 1.00 43.15 C ANISOU 1239 C GLY A 158 4884 4265 7246 1804 -1304 931 C ATOM 1240 O GLY A 158 -36.716 24.751 19.497 1.00 45.01 O ANISOU 1240 O GLY A 158 4949 4567 7587 1915 -1271 923 O ATOM 1241 N CYS A 159 -34.636 24.277 20.206 1.00 37.43 N ANISOU 1241 N CYS A 159 4213 3592 6416 1718 -1222 787 N ATOM 1242 CA CYS A 159 -35.079 23.263 21.157 1.00 37.92 C ANISOU 1242 CA CYS A 159 4146 3793 6467 1758 -1063 598 C ATOM 1243 C CYS A 159 -35.808 23.893 22.339 1.00 43.34 C ANISOU 1243 C CYS A 159 4819 4316 7334 1973 -848 457 C ATOM 1244 O CYS A 159 -35.575 25.052 22.678 1.00 43.51 O ANISOU 1244 O CYS A 159 5025 4054 7453 2066 -834 409 O ATOM 1245 CB CYS A 159 -33.891 22.436 21.655 1.00 34.83 C ANISOU 1245 CB CYS A 159 3837 3495 5901 1628 -1040 478 C ATOM 1246 SG CYS A 159 -33.091 21.443 20.377 1.00 38.59 S ANISOU 1246 SG CYS A 159 4355 4247 6060 1464 -1212 626 S ATOM 1247 N GLY A 160 -36.693 23.123 22.963 1.00 44.92 N ANISOU 1247 N GLY A 160 4824 4693 7552 2063 -682 407 N ATOM 1248 CA GLY A 160 -37.427 23.596 24.122 1.00 48.06 C ANISOU 1248 CA GLY A 160 5216 5020 8026 2336 -419 297 C ATOM 1249 C GLY A 160 -36.605 23.456 25.387 1.00 49.57 C ANISOU 1249 C GLY A 160 5604 5144 8087 2366 -225 62 C ATOM 1250 O GLY A 160 -35.465 22.996 25.344 1.00 44.23 O ANISOU 1250 O GLY A 160 5036 4473 7297 2152 -340 -26 O ATOM 1251 N GLU A 161 -37.182 23.850 26.518 1.00 56.58 N ANISOU 1251 N GLU A 161 6568 5989 8941 2657 52 -53 N ATOM 1252 CA GLU A 161 -36.482 23.773 27.794 1.00 61.43 C ANISOU 1252 CA GLU A 161 7363 6486 9492 2616 236 -319 C ATOM 1253 C GLU A 161 -36.291 22.325 28.230 1.00 57.88 C ANISOU 1253 C GLU A 161 6738 6357 8895 2470 311 -348 C ATOM 1254 O GLU A 161 -37.221 21.520 28.178 1.00 59.26 O ANISOU 1254 O GLU A 161 6585 6804 9128 2486 318 -258 O ATOM 1255 CB GLU A 161 -37.238 24.554 28.872 1.00 76.51 C ANISOU 1255 CB GLU A 161 9347 8271 11451 2889 437 -515 C ATOM 1256 CG GLU A 161 -37.265 26.058 28.644 1.00 86.78 C ANISOU 1256 CG GLU A 161 10902 9183 12887 3034 362 -543 C ATOM 1257 CD GLU A 161 -37.971 26.803 29.761 1.00100.13 C ANISOU 1257 CD GLU A 161 12725 10771 14548 3353 571 -756 C ATOM 1258 OE1 GLU A 161 -38.564 26.140 30.638 1.00103.51 O ANISOU 1258 OE1 GLU A 161 13014 11485 14830 3485 814 -809 O ATOM 1259 OE2 GLU A 161 -37.930 28.052 29.763 1.00106.33 O ANISOU 1259 OE2 GLU A 161 13784 11204 15414 3488 503 -836 O ATOM 1260 N GLY A 162 -35.074 21.999 28.654 1.00 50.03 N ANISOU 1260 N GLY A 162 5305 6140 7565 2142 159 -527 N ATOM 1261 CA GLY A 162 -34.744 20.648 29.067 1.00 44.91 C ANISOU 1261 CA GLY A 162 4606 5702 6757 2020 245 -512 C ATOM 1262 C GLY A 162 -34.301 19.795 27.895 1.00 42.66 C ANISOU 1262 C GLY A 162 4296 5456 6458 1850 95 -372 C ATOM 1263 O GLY A 162 -33.832 18.670 28.073 1.00 43.98 O ANISOU 1263 O GLY A 162 4459 5754 6499 1695 139 -339 O ATOM 1264 N GLN A 163 -34.448 20.335 26.690 1.00 40.04 N ANISOU 1264 N GLN A 163 3979 5002 6232 1867 -76 -268 N ATOM 1265 CA GLN A 163 -34.078 19.611 25.481 1.00 37.42 C ANISOU 1265 CA GLN A 163 3672 4714 5833 1725 -226 -129 C ATOM 1266 C GLN A 163 -32.684 19.977 24.992 1.00 33.92 C ANISOU 1266 C GLN A 163 3462 4143 5284 1617 -273 -78 C ATOM 1267 O GLN A 163 -32.210 21.094 25.197 1.00 35.45 O ANISOU 1267 O GLN A 163 3771 4140 5558 1670 -260 -108 O ATOM 1268 CB GLN A 163 -35.091 19.874 24.367 1.00 31.19 C ANISOU 1268 CB GLN A 163 2764 3914 5171 1849 -398 -23 C ATOM 1269 CG GLN A 163 -36.449 19.247 24.597 1.00 33.42 C ANISOU 1269 CG GLN A 163 2795 4330 5573 1852 -361 -12 C ATOM 1270 CD GLN A 163 -37.343 19.371 23.384 1.00 39.58 C ANISOU 1270 CD GLN A 163 3503 5122 6415 1907 -559 94 C ATOM 1271 OE1 GLN A 163 -37.149 20.251 22.545 1.00 42.78 O ANISOU 1271 OE1 GLN A 163 4045 5422 6789 1999 -674 173 O ATOM 1272 NE2 GLN A 163 -38.323 18.484 23.278 1.00 45.59 N ANISOU 1272 NE2 GLN A 163 4051 6008 7263 1856 -602 102 N ATOM 1273 N VAL A 164 -32.036 19.016 24.344 1.00 26.73 N ANISOU 1273 N VAL A 164 2599 3328 4228 1471 -327 -1 N ATOM 1274 CA VAL A 164 -30.746 19.237 23.708 1.00 29.99 C ANISOU 1274 CA VAL A 164 3196 3649 4550 1379 -348 96 C ATOM 1275 C VAL A 164 -30.805 18.776 22.259 1.00 29.53 C ANISOU 1275 C VAL A 164 3171 3674 4375 1404 -481 252 C ATOM 1276 O VAL A 164 -31.714 18.040 21.875 1.00 26.73 O ANISOU 1276 O VAL A 164 2694 3456 4007 1447 -592 229 O ATOM 1277 CB VAL A 164 -29.610 18.482 24.430 1.00 27.52 C ANISOU 1277 CB VAL A 164 2947 3390 4121 1203 -257 18 C ATOM 1278 CG1 VAL A 164 -29.531 18.907 25.884 1.00 30.87 C ANISOU 1278 CG1 VAL A 164 3369 3764 4596 1225 -157 -163 C ATOM 1279 CG2 VAL A 164 -29.816 16.973 24.320 1.00 26.18 C ANISOU 1279 CG2 VAL A 164 2693 3424 3831 1112 -274 11 C ATOM 1280 N ALA A 165 -29.846 19.217 21.453 1.00 26.25 N ANISOU 1280 N ALA A 165 2912 3174 3889 1397 -475 410 N ATOM 1281 CA ALA A 165 -29.656 18.627 20.137 1.00 33.26 C ANISOU 1281 CA ALA A 165 3879 4188 4571 1445 -571 546 C ATOM 1282 C ALA A 165 -29.112 17.217 20.338 1.00 31.46 C ANISOU 1282 C ALA A 165 3640 4115 4197 1291 -560 442 C ATOM 1283 O ALA A 165 -28.060 17.030 20.954 1.00 26.52 O ANISOU 1283 O ALA A 165 3060 3453 3565 1145 -433 416 O ATOM 1284 CB ALA A 165 -28.713 19.467 19.290 1.00 33.19 C ANISOU 1284 CB ALA A 165 4032 4059 4520 1498 -500 790 C ATOM 1285 N CYS A 166 -29.836 16.221 19.843 1.00 24.61 N ANISOU 1285 N CYS A 166 2698 3401 3250 1328 -714 370 N ATOM 1286 CA CYS A 166 -29.478 14.840 20.133 1.00 23.00 C ANISOU 1286 CA CYS A 166 2454 3307 2978 1185 -716 254 C ATOM 1287 C CYS A 166 -28.327 14.357 19.260 1.00 27.43 C ANISOU 1287 C CYS A 166 3187 3932 3303 1178 -707 330 C ATOM 1288 O CYS A 166 -28.517 13.982 18.103 1.00 27.24 O ANISOU 1288 O CYS A 166 3235 4010 3105 1315 -862 350 O ATOM 1289 CB CYS A 166 -30.684 13.919 19.964 1.00 27.62 C ANISOU 1289 CB CYS A 166 2859 3982 3653 1212 -903 131 C ATOM 1290 SG CYS A 166 -30.388 12.261 20.612 1.00 29.10 S ANISOU 1290 SG CYS A 166 2946 4231 3878 1015 -877 2 S ATOM 1291 N LEU A 167 -27.131 14.378 19.834 1.00 21.17 N ANISOU 1291 N LEU A 167 2456 3087 2500 1043 -532 362 N ATOM 1292 CA LEU A 167 -25.927 13.917 19.161 1.00 20.86 C ANISOU 1292 CA LEU A 167 2547 3104 2273 1029 -471 445 C ATOM 1293 C LEU A 167 -25.153 13.039 20.128 1.00 18.84 C ANISOU 1293 C LEU A 167 2245 2859 2053 839 -381 337 C ATOM 1294 O LEU A 167 -25.024 13.380 21.304 1.00 18.89 O ANISOU 1294 O LEU A 167 2188 2781 2208 732 -296 281 O ATOM 1295 CB LEU A 167 -25.074 15.098 18.694 1.00 21.97 C ANISOU 1295 CB LEU A 167 2797 3136 2416 1083 -328 674 C ATOM 1296 CG LEU A 167 -25.734 16.054 17.699 1.00 29.56 C ANISOU 1296 CG LEU A 167 3826 4076 3329 1298 -389 846 C ATOM 1297 CD1 LEU A 167 -24.923 17.333 17.559 1.00 31.18 C ANISOU 1297 CD1 LEU A 167 4087 4094 3667 1307 -208 1098 C ATOM 1298 CD2 LEU A 167 -25.911 15.374 16.349 1.00 32.17 C ANISOU 1298 CD2 LEU A 167 4275 4606 3342 1497 -514 886 C ATOM 1299 N PHE A 168 -24.648 11.913 19.628 1.00 18.43 N ANISOU 1299 N PHE A 168 2238 2913 1850 829 -416 297 N ATOM 1300 CA PHE A 168 -23.980 10.915 20.460 1.00 16.76 C ANISOU 1300 CA PHE A 168 1980 2717 1670 672 -356 201 C ATOM 1301 C PHE A 168 -22.890 11.518 21.340 1.00 15.89 C ANISOU 1301 C PHE A 168 1875 2515 1647 556 -192 254 C ATOM 1302 O PHE A 168 -22.916 11.362 22.560 1.00 18.75 O ANISOU 1302 O PHE A 168 2165 2849 2111 455 -160 162 O ATOM 1303 CB PHE A 168 -23.384 9.809 19.584 1.00 18.27 C ANISOU 1303 CB PHE A 168 2251 3011 1680 718 -404 172 C ATOM 1304 CG PHE A 168 -22.917 8.605 20.355 1.00 17.22 C ANISOU 1304 CG PHE A 168 2056 2884 1601 580 -383 66 C ATOM 1305 CD1 PHE A 168 -21.645 8.566 20.908 1.00 17.63 C ANISOU 1305 CD1 PHE A 168 2127 2914 1657 483 -235 117 C ATOM 1306 CD2 PHE A 168 -23.747 7.507 20.519 1.00 17.52 C ANISOU 1306 CD2 PHE A 168 1998 2932 1727 549 -523 -73 C ATOM 1307 CE1 PHE A 168 -21.213 7.458 21.615 1.00 17.15 C ANISOU 1307 CE1 PHE A 168 2018 2862 1638 380 -224 38 C ATOM 1308 CE2 PHE A 168 -23.321 6.393 21.223 1.00 15.31 C ANISOU 1308 CE2 PHE A 168 1661 2635 1520 432 -491 -132 C ATOM 1309 CZ PHE A 168 -22.052 6.369 21.773 1.00 14.99 C ANISOU 1309 CZ PHE A 168 1667 2593 1434 358 -341 -74 C ATOM 1310 N GLU A 169 -21.942 12.217 20.722 1.00 16.66 N ANISOU 1310 N GLU A 169 2048 2564 1717 589 -94 410 N ATOM 1311 CA GLU A 169 -20.790 12.742 21.453 1.00 19.85 C ANISOU 1311 CA GLU A 169 2423 2852 2266 469 22 447 C ATOM 1312 C GLU A 169 -21.137 13.896 22.390 1.00 20.33 C ANISOU 1312 C GLU A 169 2435 2755 2535 434 14 396 C ATOM 1313 O GLU A 169 -20.321 14.282 23.224 1.00 22.76 O ANISOU 1313 O GLU A 169 2703 2954 2989 336 45 347 O ATOM 1314 CB GLU A 169 -19.697 13.189 20.477 1.00 22.87 C ANISOU 1314 CB GLU A 169 2854 3202 2634 512 154 667 C ATOM 1315 CG GLU A 169 -19.026 12.037 19.755 1.00 24.52 C ANISOU 1315 CG GLU A 169 3113 3566 2637 557 196 690 C ATOM 1316 CD GLU A 169 -17.805 12.460 18.961 1.00 26.80 C ANISOU 1316 CD GLU A 169 3416 3833 2933 603 390 934 C ATOM 1317 OE1 GLU A 169 -17.138 13.441 19.354 1.00 27.00 O ANISOU 1317 OE1 GLU A 169 3355 3680 3224 508 487 1051 O ATOM 1318 OE2 GLU A 169 -17.513 11.808 17.938 1.00 27.65 O ANISOU 1318 OE2 GLU A 169 3613 4094 2799 748 446 1006 O ATOM 1319 N ASP A 170 -22.338 14.448 22.255 1.00 20.63 N ANISOU 1319 N ASP A 170 2470 2774 2594 531 -49 384 N ATOM 1320 CA ASP A 170 -22.760 15.531 23.137 1.00 23.04 C ANISOU 1320 CA ASP A 170 2738 2930 3086 536 -60 307 C ATOM 1321 C ASP A 170 -23.337 15.013 24.454 1.00 21.76 C ANISOU 1321 C ASP A 170 2517 2841 2910 507 -85 102 C ATOM 1322 O ASP A 170 -23.313 15.715 25.463 1.00 21.75 O ANISOU 1322 O ASP A 170 2506 2743 3016 512 -85 -17 O ATOM 1323 CB ASP A 170 -23.787 16.428 22.441 1.00 22.57 C ANISOU 1323 CB ASP A 170 2693 2810 3074 681 -102 399 C ATOM 1324 CG ASP A 170 -23.156 17.355 21.416 1.00 30.78 C ANISOU 1324 CG ASP A 170 3795 3716 4185 734 -37 643 C ATOM 1325 OD1 ASP A 170 -21.912 17.368 21.313 1.00 33.81 O ANISOU 1325 OD1 ASP A 170 4183 4037 4626 643 58 738 O ATOM 1326 OD2 ASP A 170 -23.901 18.082 20.723 1.00 31.07 O ANISOU 1326 OD2 ASP A 170 3861 3705 4240 877 -68 764 O ATOM 1327 N VAL A 171 -23.853 13.788 24.452 1.00 18.02 N ANISOU 1327 N VAL A 171 2005 2531 2312 496 -105 64 N ATOM 1328 CA VAL A 171 -24.505 13.259 25.648 1.00 17.51 C ANISOU 1328 CA VAL A 171 1866 2545 2242 492 -80 -59 C ATOM 1329 C VAL A 171 -23.736 12.098 26.280 1.00 18.84 C ANISOU 1329 C VAL A 171 2035 2803 2320 394 -43 -94 C ATOM 1330 O VAL A 171 -23.788 11.904 27.494 1.00 17.15 O ANISOU 1330 O VAL A 171 1804 2636 2078 402 8 -173 O ATOM 1331 CB VAL A 171 -25.956 12.811 25.343 1.00 19.04 C ANISOU 1331 CB VAL A 171 1953 2817 2466 561 -120 -51 C ATOM 1332 CG1 VAL A 171 -26.811 14.017 24.967 1.00 22.10 C ANISOU 1332 CG1 VAL A 171 2324 3119 2953 685 -158 -30 C ATOM 1333 CG2 VAL A 171 -25.985 11.767 24.235 1.00 19.67 C ANISOU 1333 CG2 VAL A 171 2023 2966 2483 534 -212 -3 C ATOM 1334 N VAL A 172 -23.021 11.332 25.462 1.00 13.90 N ANISOU 1334 N VAL A 172 1440 2211 1631 333 -65 -30 N ATOM 1335 CA VAL A 172 -22.239 10.209 25.969 1.00 14.61 C ANISOU 1335 CA VAL A 172 1529 2367 1656 252 -39 -52 C ATOM 1336 C VAL A 172 -20.800 10.652 26.200 1.00 14.06 C ANISOU 1336 C VAL A 172 1509 2233 1599 196 -20 -53 C ATOM 1337 O VAL A 172 -20.135 11.102 25.269 1.00 16.37 O ANISOU 1337 O VAL A 172 1832 2465 1923 189 -10 34 O ATOM 1338 CB VAL A 172 -22.257 9.008 24.999 1.00 16.04 C ANISOU 1338 CB VAL A 172 1702 2608 1783 235 -87 -17 C ATOM 1339 CG1 VAL A 172 -21.520 7.822 25.610 1.00 14.11 C ANISOU 1339 CG1 VAL A 172 1446 2408 1507 161 -58 -34 C ATOM 1340 CG2 VAL A 172 -23.688 8.630 24.632 1.00 15.29 C ANISOU 1340 CG2 VAL A 172 1521 2538 1751 284 -161 -35 C ATOM 1341 N PRO A 173 -20.314 10.534 27.448 1.00 16.65 N ANISOU 1341 N PRO A 173 1837 2579 1912 173 -15 -141 N ATOM 1342 CA PRO A 173 -18.951 10.967 27.778 1.00 16.14 C ANISOU 1342 CA PRO A 173 1783 2438 1913 119 -46 -177 C ATOM 1343 C PRO A 173 -17.910 10.136 27.044 1.00 13.86 C ANISOU 1343 C PRO A 173 1479 2176 1611 51 -21 -85 C ATOM 1344 O PRO A 173 -18.064 8.921 26.922 1.00 11.67 O ANISOU 1344 O PRO A 173 1201 2000 1232 47 -5 -63 O ATOM 1345 CB PRO A 173 -18.856 10.740 29.292 1.00 19.17 C ANISOU 1345 CB PRO A 173 2183 2889 2213 158 -79 -310 C ATOM 1346 CG PRO A 173 -20.266 10.609 29.762 1.00 17.83 C ANISOU 1346 CG PRO A 173 2012 2804 1957 252 -19 -322 C ATOM 1347 CD PRO A 173 -21.016 9.991 28.622 1.00 17.24 C ANISOU 1347 CD PRO A 173 1890 2753 1909 221 19 -200 C ATOM 1348 N AMET A 174 -16.855 10.778 26.561 0.79 14.15 N ANISOU 1348 N AMET A 174 1486 2107 1783 6 -9 -26 N ATOM 1349 N BMET A 174 -16.861 10.793 26.561 0.21 13.62 N ANISOU 1349 N BMET A 174 1420 2039 1717 6 -9 -26 N ATOM 1350 CA AMET A 174 -15.841 10.054 25.808 0.79 13.42 C ANISOU 1350 CA AMET A 174 1367 2052 1680 -28 51 78 C ATOM 1351 CA BMET A 174 -15.807 10.110 25.821 0.21 13.62 C ANISOU 1351 CA BMET A 174 1389 2070 1715 -30 51 78 C ATOM 1352 C AMET A 174 -14.967 9.199 26.727 0.79 14.86 C ANISOU 1352 C AMET A 174 1511 2289 1848 -72 3 -1 C ATOM 1353 C BMET A 174 -14.972 9.213 26.725 0.21 14.05 C ANISOU 1353 C BMET A 174 1407 2184 1746 -72 3 -1 C ATOM 1354 O AMET A 174 -14.434 8.175 26.300 0.79 13.52 O ANISOU 1354 O AMET A 174 1331 2192 1615 -73 45 51 O ATOM 1355 O BMET A 174 -14.467 8.181 26.283 0.21 13.70 O ANISOU 1355 O BMET A 174 1356 2215 1636 -72 46 51 O ATOM 1356 CB AMET A 174 -14.977 11.021 24.996 0.79 14.38 C ANISOU 1356 CB AMET A 174 1433 2043 1988 -52 127 222 C ATOM 1357 CB BMET A 174 -14.908 11.124 25.115 0.21 14.60 C ANISOU 1357 CB BMET A 174 1452 2054 2042 -61 118 211 C ATOM 1358 CG AMET A 174 -14.181 10.341 23.895 0.79 15.41 C ANISOU 1358 CG AMET A 174 1552 2248 2056 -24 252 376 C ATOM 1359 CG BMET A 174 -15.580 11.830 23.954 0.21 15.21 C ANISOU 1359 CG BMET A 174 1581 2096 2101 16 198 364 C ATOM 1360 SD AMET A 174 -15.237 9.464 22.719 0.79 21.69 S ANISOU 1360 SD AMET A 174 2481 3207 2552 114 276 410 S ATOM 1361 SD BMET A 174 -16.080 10.686 22.653 0.21 24.35 S ANISOU 1361 SD BMET A 174 2840 3449 2962 137 255 445 S ATOM 1362 CE AMET A 174 -15.826 10.818 21.703 0.79 24.06 C ANISOU 1362 CE AMET A 174 2832 3434 2875 208 342 582 C ATOM 1363 CE BMET A 174 -14.493 10.014 22.171 0.21 25.28 C ANISOU 1363 CE BMET A 174 2900 3612 3095 124 382 553 C ATOM 1364 N ASN A 175 -14.825 9.602 27.987 1.00 13.11 N ANISOU 1364 N ASN A 175 1277 2036 1667 -78 -98 -138 N ATOM 1365 CA ASN A 175 -14.049 8.793 28.921 1.00 13.30 C ANISOU 1365 CA ASN A 175 1281 2132 1641 -82 -168 -209 C ATOM 1366 C ASN A 175 -14.775 7.476 29.206 1.00 12.04 C ANISOU 1366 C ASN A 175 1179 2116 1278 -35 -125 -182 C ATOM 1367 O ASN A 175 -14.135 6.439 29.366 1.00 14.07 O ANISOU 1367 O ASN A 175 1418 2431 1497 -40 -128 -151 O ATOM 1368 CB ASN A 175 -13.718 9.551 30.223 1.00 14.51 C ANISOU 1368 CB ASN A 175 1432 2237 1843 -52 -325 -390 C ATOM 1369 CG ASN A 175 -14.925 10.217 30.868 1.00 17.04 C ANISOU 1369 CG ASN A 175 1842 2571 2062 40 -343 -496 C ATOM 1370 OD1 ASN A 175 -16.072 9.842 30.635 1.00 17.63 O ANISOU 1370 OD1 ASN A 175 1964 2727 2007 82 -238 -426 O ATOM 1371 ND2 ASN A 175 -14.656 11.211 31.708 1.00 20.03 N ANISOU 1371 ND2 ASN A 175 2229 2860 2523 86 -493 -684 N ATOM 1372 N TYR A 176 -16.107 7.509 29.226 1.00 11.71 N ANISOU 1372 N TYR A 176 1183 2110 1156 9 -81 -176 N ATOM 1373 CA TYR A 176 -16.889 6.273 29.282 1.00 11.60 C ANISOU 1373 CA TYR A 176 1176 2182 1051 30 -26 -114 C ATOM 1374 C TYR A 176 -16.622 5.406 28.049 1.00 11.40 C ANISOU 1374 C TYR A 176 1132 2142 1056 -8 -3 -45 C ATOM 1375 O TYR A 176 -16.390 4.198 28.157 1.00 10.31 O ANISOU 1375 O TYR A 176 983 2033 903 -12 1 -14 O ATOM 1376 CB TYR A 176 -18.395 6.566 29.387 1.00 11.30 C ANISOU 1376 CB TYR A 176 1137 2162 996 77 20 -109 C ATOM 1377 CG TYR A 176 -19.246 5.350 29.076 1.00 11.08 C ANISOU 1377 CG TYR A 176 1059 2161 991 65 63 -29 C ATOM 1378 CD1 TYR A 176 -19.543 4.415 30.062 1.00 13.51 C ANISOU 1378 CD1 TYR A 176 1338 2525 1269 91 126 39 C ATOM 1379 CD2 TYR A 176 -19.728 5.121 27.789 1.00 10.82 C ANISOU 1379 CD2 TYR A 176 1001 2082 1027 42 29 -17 C ATOM 1380 CE1 TYR A 176 -20.301 3.292 29.777 1.00 14.37 C ANISOU 1380 CE1 TYR A 176 1364 2603 1494 59 158 124 C ATOM 1381 CE2 TYR A 176 -20.481 4.001 27.496 1.00 11.09 C ANISOU 1381 CE2 TYR A 176 968 2100 1147 25 15 14 C ATOM 1382 CZ TYR A 176 -20.766 3.091 28.492 1.00 16.43 C ANISOU 1382 CZ TYR A 176 1583 2789 1869 16 82 89 C ATOM 1383 OH TYR A 176 -21.518 1.977 28.202 1.00 16.82 O ANISOU 1383 OH TYR A 176 1528 2769 2093 -20 63 131 O ATOM 1384 N MET A 177 -16.674 6.030 26.876 1.00 12.48 N ANISOU 1384 N MET A 177 1279 2235 1226 -7 10 -20 N ATOM 1385 CA MET A 177 -16.545 5.301 25.619 1.00 10.45 C ANISOU 1385 CA MET A 177 1041 1993 937 19 23 18 C ATOM 1386 C MET A 177 -15.168 4.671 25.461 1.00 12.58 C ANISOU 1386 C MET A 177 1290 2274 1214 11 53 42 C ATOM 1387 O MET A 177 -15.041 3.583 24.903 1.00 10.87 O ANISOU 1387 O MET A 177 1091 2081 959 48 48 31 O ATOM 1388 CB MET A 177 -16.836 6.221 24.431 1.00 11.38 C ANISOU 1388 CB MET A 177 1198 2092 1035 72 45 67 C ATOM 1389 CG MET A 177 -18.315 6.534 24.245 1.00 11.46 C ANISOU 1389 CG MET A 177 1220 2102 1034 111 -10 39 C ATOM 1390 SD MET A 177 -19.322 5.040 24.090 1.00 16.17 S ANISOU 1390 SD MET A 177 1784 2726 1635 123 -102 -35 S ATOM 1391 CE MET A 177 -18.739 4.383 22.526 1.00 11.89 C ANISOU 1391 CE MET A 177 1327 2222 969 227 -145 -58 C ATOM 1392 N VAL A 178 -14.139 5.350 25.957 1.00 10.90 N ANISOU 1392 N VAL A 178 1027 2029 1085 -29 66 58 N ATOM 1393 CA VAL A 178 -12.775 4.865 25.779 1.00 11.70 C ANISOU 1393 CA VAL A 178 1069 2137 1241 -33 101 95 C ATOM 1394 C VAL A 178 -12.359 3.904 26.891 1.00 13.74 C ANISOU 1394 C VAL A 178 1302 2426 1492 -44 31 46 C ATOM 1395 O VAL A 178 -11.963 2.771 26.622 1.00 11.27 O ANISOU 1395 O VAL A 178 986 2138 1158 -10 46 60 O ATOM 1396 CB VAL A 178 -11.764 6.031 25.707 1.00 14.24 C ANISOU 1396 CB VAL A 178 1294 2380 1738 -78 137 151 C ATOM 1397 CG1 VAL A 178 -10.337 5.505 25.743 1.00 13.14 C ANISOU 1397 CG1 VAL A 178 1041 2245 1706 -87 163 187 C ATOM 1398 CG2 VAL A 178 -11.993 6.855 24.447 1.00 13.12 C ANISOU 1398 CG2 VAL A 178 1175 2208 1603 -39 255 274 C ATOM 1399 N TYR A 179 -12.455 4.352 28.139 1.00 13.16 N ANISOU 1399 N TYR A 179 1224 2353 1422 -62 -52 -14 N ATOM 1400 CA TYR A 179 -11.967 3.560 29.265 1.00 15.35 C ANISOU 1400 CA TYR A 179 1492 2681 1658 -34 -125 -37 C ATOM 1401 C TYR A 179 -12.909 2.417 29.629 1.00 17.16 C ANISOU 1401 C TYR A 179 1782 2955 1783 5 -94 10 C ATOM 1402 O TYR A 179 -12.480 1.276 29.788 1.00 13.99 O ANISOU 1402 O TYR A 179 1369 2562 1385 30 -96 58 O ATOM 1403 CB TYR A 179 -11.750 4.451 30.491 1.00 15.10 C ANISOU 1403 CB TYR A 179 1462 2657 1620 -15 -246 -138 C ATOM 1404 CG TYR A 179 -10.577 5.400 30.372 1.00 16.18 C ANISOU 1404 CG TYR A 179 1485 2704 1960 -68 -327 -195 C ATOM 1405 CD1 TYR A 179 -9.379 4.992 29.797 1.00 16.79 C ANISOU 1405 CD1 TYR A 179 1442 2753 2186 -100 -302 -131 C ATOM 1406 CD2 TYR A 179 -10.668 6.705 30.837 1.00 17.72 C ANISOU 1406 CD2 TYR A 179 1671 2820 2242 -80 -428 -312 C ATOM 1407 CE1 TYR A 179 -8.305 5.862 29.688 1.00 17.71 C ANISOU 1407 CE1 TYR A 179 1400 2762 2566 -162 -361 -152 C ATOM 1408 CE2 TYR A 179 -9.603 7.580 30.733 1.00 18.20 C ANISOU 1408 CE2 TYR A 179 1588 2747 2582 -148 -519 -360 C ATOM 1409 CZ TYR A 179 -8.425 7.154 30.160 1.00 21.67 C ANISOU 1409 CZ TYR A 179 1878 3157 3200 -198 -478 -264 C ATOM 1410 OH TYR A 179 -7.367 8.028 30.057 1.00 24.54 O ANISOU 1410 OH TYR A 179 2047 3363 3915 -279 -552 -282 O ATOM 1411 N PHE A 180 -14.193 2.729 29.764 1.00 14.30 N ANISOU 1411 N PHE A 180 1462 2602 1371 10 -59 11 N ATOM 1412 CA PHE A 180 -15.160 1.759 30.257 1.00 12.09 C ANISOU 1412 CA PHE A 180 1192 2341 1059 38 -9 88 C ATOM 1413 C PHE A 180 -15.674 0.851 29.148 1.00 14.66 C ANISOU 1413 C PHE A 180 1491 2592 1488 3 10 112 C ATOM 1414 O PHE A 180 -15.606 -0.371 29.257 1.00 17.10 O ANISOU 1414 O PHE A 180 1777 2858 1861 8 14 170 O ATOM 1415 CB PHE A 180 -16.332 2.475 30.932 1.00 12.70 C ANISOU 1415 CB PHE A 180 1291 2463 1072 76 36 87 C ATOM 1416 CG PHE A 180 -17.242 1.563 31.715 1.00 16.41 C ANISOU 1416 CG PHE A 180 1739 2966 1530 121 132 219 C ATOM 1417 CD1 PHE A 180 -18.315 0.929 31.102 1.00 12.67 C ANISOU 1417 CD1 PHE A 180 1187 2415 1212 70 183 286 C ATOM 1418 CD2 PHE A 180 -17.039 1.361 33.071 1.00 19.18 C ANISOU 1418 CD2 PHE A 180 2138 3421 1728 231 168 287 C ATOM 1419 CE1 PHE A 180 -19.162 0.102 31.827 1.00 14.61 C ANISOU 1419 CE1 PHE A 180 1366 2658 1528 97 298 449 C ATOM 1420 CE2 PHE A 180 -17.879 0.536 33.801 1.00 20.85 C ANISOU 1420 CE2 PHE A 180 2319 3665 1937 292 309 473 C ATOM 1421 CZ PHE A 180 -18.942 -0.095 33.177 1.00 20.30 C ANISOU 1421 CZ PHE A 180 2134 3488 2090 209 389 570 C ATOM 1422 N ASN A 181 -16.195 1.442 28.081 1.00 14.34 N ANISOU 1422 N ASN A 181 1457 2524 1469 -14 0 59 N ATOM 1423 CA ASN A 181 -16.782 0.633 27.027 1.00 14.79 C ANISOU 1423 CA ASN A 181 1501 2516 1602 -13 -37 30 C ATOM 1424 C ASN A 181 -15.720 -0.086 26.197 1.00 19.84 C ANISOU 1424 C ASN A 181 2166 3136 2236 23 -60 -9 C ATOM 1425 O ASN A 181 -15.742 -1.310 26.085 1.00 23.86 O ANISOU 1425 O ASN A 181 2657 3574 2834 35 -98 -24 O ATOM 1426 CB ASN A 181 -17.675 1.482 26.122 1.00 12.72 C ANISOU 1426 CB ASN A 181 1254 2255 1325 2 -67 -20 C ATOM 1427 CG ASN A 181 -18.497 0.636 25.170 1.00 20.63 C ANISOU 1427 CG ASN A 181 2234 3191 2413 24 -166 -90 C ATOM 1428 OD1 ASN A 181 -18.140 0.469 24.004 1.00 21.06 O ANISOU 1428 OD1 ASN A 181 2353 3252 2398 96 -225 -168 O ATOM 1429 ND2 ASN A 181 -19.595 0.080 25.670 1.00 22.34 N ANISOU 1429 ND2 ASN A 181 2352 3341 2794 -19 -188 -64 N ATOM 1430 N PHE A 182 -14.781 0.667 25.633 1.00 15.77 N ANISOU 1430 N PHE A 182 1677 2668 1645 51 -23 -16 N ATOM 1431 CA PHE A 182 -13.782 0.077 24.748 1.00 13.40 C ANISOU 1431 CA PHE A 182 1395 2375 1322 122 -2 -39 C ATOM 1432 C PHE A 182 -12.760 -0.779 25.495 1.00 13.32 C ANISOU 1432 C PHE A 182 1336 2350 1376 119 3 -10 C ATOM 1433 O PHE A 182 -12.690 -1.986 25.279 1.00 15.15 O ANISOU 1433 O PHE A 182 1574 2525 1659 163 -32 -46 O ATOM 1434 CB PHE A 182 -13.062 1.167 23.949 1.00 13.59 C ANISOU 1434 CB PHE A 182 1428 2454 1281 162 89 7 C ATOM 1435 CG PHE A 182 -12.067 0.633 22.955 1.00 15.04 C ANISOU 1435 CG PHE A 182 1625 2676 1413 277 163 10 C ATOM 1436 CD1 PHE A 182 -12.323 -0.539 22.260 1.00 15.93 C ANISOU 1436 CD1 PHE A 182 1805 2778 1470 382 103 -98 C ATOM 1437 CD2 PHE A 182 -10.882 1.309 22.707 1.00 13.20 C ANISOU 1437 CD2 PHE A 182 1323 2477 1214 294 295 116 C ATOM 1438 CE1 PHE A 182 -11.416 -1.030 21.342 1.00 17.20 C ANISOU 1438 CE1 PHE A 182 1996 2991 1549 533 182 -117 C ATOM 1439 CE2 PHE A 182 -9.969 0.823 21.789 1.00 17.76 C ANISOU 1439 CE2 PHE A 182 1899 3111 1737 429 408 143 C ATOM 1440 CZ PHE A 182 -10.237 -0.349 21.106 1.00 23.07 C ANISOU 1440 CZ PHE A 182 2672 3802 2293 566 357 18 C ATOM 1441 N PHE A 183 -11.966 -0.160 26.364 1.00 13.05 N ANISOU 1441 N PHE A 183 1248 2350 1360 80 19 41 N ATOM 1442 CA PHE A 183 -10.877 -0.880 27.020 1.00 15.26 C ANISOU 1442 CA PHE A 183 1472 2631 1695 101 0 69 C ATOM 1443 C PHE A 183 -11.393 -2.036 27.879 1.00 17.33 C ANISOU 1443 C PHE A 183 1752 2850 1981 109 -47 106 C ATOM 1444 O PHE A 183 -10.989 -3.185 27.697 1.00 17.92 O ANISOU 1444 O PHE A 183 1816 2867 2125 159 -58 112 O ATOM 1445 CB PHE A 183 -10.032 0.071 27.874 1.00 14.03 C ANISOU 1445 CB PHE A 183 1245 2512 1573 66 -35 83 C ATOM 1446 CG PHE A 183 -9.140 0.987 27.071 1.00 18.91 C ANISOU 1446 CG PHE A 183 1780 3127 2278 53 31 98 C ATOM 1447 CD1 PHE A 183 -9.049 0.867 25.694 1.00 21.16 C ANISOU 1447 CD1 PHE A 183 2082 3419 2538 110 152 128 C ATOM 1448 CD2 PHE A 183 -8.384 1.962 27.702 1.00 22.91 C ANISOU 1448 CD2 PHE A 183 2183 3615 2906 0 -29 89 C ATOM 1449 CE1 PHE A 183 -8.228 1.706 24.960 1.00 25.73 C ANISOU 1449 CE1 PHE A 183 2572 4001 3205 118 268 207 C ATOM 1450 CE2 PHE A 183 -7.560 2.804 26.974 1.00 25.83 C ANISOU 1450 CE2 PHE A 183 2432 3943 3439 -28 56 147 C ATOM 1451 CZ PHE A 183 -7.483 2.675 25.601 1.00 25.45 C ANISOU 1451 CZ PHE A 183 2396 3915 3358 32 233 236 C ATOM 1452 N ALA A 184 -12.303 -1.731 28.796 1.00 14.50 N ANISOU 1452 N ALA A 184 1417 2512 1582 77 -56 148 N ATOM 1453 CA ALA A 184 -12.765 -2.719 29.764 1.00 16.87 C ANISOU 1453 CA ALA A 184 1720 2782 1909 99 -51 254 C ATOM 1454 C ALA A 184 -13.758 -3.726 29.179 1.00 18.70 C ANISOU 1454 C ALA A 184 1935 2881 2289 75 -40 269 C ATOM 1455 O ALA A 184 -13.613 -4.930 29.379 1.00 18.55 O ANISOU 1455 O ALA A 184 1891 2762 2394 98 -48 338 O ATOM 1456 CB ALA A 184 -13.384 -2.015 30.968 1.00 15.55 C ANISOU 1456 CB ALA A 184 1581 2706 1620 115 -28 312 C ATOM 1457 N CYS A 185 -14.759 -3.237 28.454 1.00 14.44 N ANISOU 1457 N CYS A 185 1395 2320 1770 32 -45 200 N ATOM 1458 CA CYS A 185 -15.886 -4.084 28.072 1.00 17.26 C ANISOU 1458 CA CYS A 185 1700 2537 2320 -1 -75 200 C ATOM 1459 C CYS A 185 -15.790 -4.664 26.662 1.00 13.69 C ANISOU 1459 C CYS A 185 1268 1989 1946 32 -184 29 C ATOM 1460 O CYS A 185 -16.549 -5.569 26.311 1.00 14.92 O ANISOU 1460 O CYS A 185 1368 1983 2318 13 -267 -16 O ATOM 1461 CB CYS A 185 -17.193 -3.302 28.222 1.00 16.58 C ANISOU 1461 CB CYS A 185 1577 2480 2244 -45 -45 220 C ATOM 1462 SG CYS A 185 -17.578 -2.863 29.937 1.00 24.21 S ANISOU 1462 SG CYS A 185 2527 3557 3116 -26 100 415 S ATOM 1463 N VAL A 186 -14.864 -4.155 25.856 1.00 13.15 N ANISOU 1463 N VAL A 186 1271 2011 1715 98 -184 -66 N ATOM 1464 CA VAL A 186 -14.699 -4.661 24.496 1.00 19.19 C ANISOU 1464 CA VAL A 186 2089 2731 2470 194 -268 -234 C ATOM 1465 C VAL A 186 -13.322 -5.284 24.272 1.00 14.52 C ANISOU 1465 C VAL A 186 1521 2148 1849 289 -233 -256 C ATOM 1466 O VAL A 186 -13.218 -6.439 23.862 1.00 15.84 O ANISOU 1466 O VAL A 186 1697 2189 2134 358 -312 -356 O ATOM 1467 CB VAL A 186 -14.924 -3.549 23.446 1.00 15.20 C ANISOU 1467 CB VAL A 186 1658 2345 1773 253 -267 -310 C ATOM 1468 CG1 VAL A 186 -14.548 -4.044 22.056 1.00 15.14 C ANISOU 1468 CG1 VAL A 186 1743 2347 1662 421 -329 -476 C ATOM 1469 CG2 VAL A 186 -16.369 -3.077 23.470 1.00 16.79 C ANISOU 1469 CG2 VAL A 186 1827 2519 2034 189 -338 -324 C ATOM 1470 N ALEU A 187 -12.272 -4.526 24.565 0.60 13.21 N ANISOU 1470 N ALEU A 187 1286 1782 1951 -101 107 144 N ATOM 1471 N BLEU A 187 -12.269 -4.514 24.538 0.40 14.51 N ANISOU 1471 N BLEU A 187 1450 1945 2118 -102 111 145 N ATOM 1472 CA ALEU A 187 -10.909 -4.966 24.287 0.60 15.49 C ANISOU 1472 CA ALEU A 187 1421 2028 2435 -125 106 67 C ATOM 1473 CA BLEU A 187 -10.901 -4.972 24.300 0.40 15.72 C ANISOU 1473 CA BLEU A 187 1450 2058 2466 -124 104 66 C ATOM 1474 C ALEU A 187 -10.489 -6.165 25.140 0.60 19.00 C ANISOU 1474 C ALEU A 187 1856 2558 2806 -37 -76 7 C ATOM 1475 C BLEU A 187 -10.538 -6.194 25.133 0.40 18.66 C ANISOU 1475 C BLEU A 187 1820 2517 2753 -36 -75 13 C ATOM 1476 O ALEU A 187 -9.915 -7.126 24.628 0.60 20.54 O ANISOU 1476 O ALEU A 187 2010 2765 3028 -21 -58 24 O ATOM 1477 O BLEU A 187 -10.045 -7.190 24.603 0.40 20.70 O ANISOU 1477 O BLEU A 187 2049 2791 3024 -19 -53 40 O ATOM 1478 CB ALEU A 187 -9.930 -3.808 24.494 0.60 17.60 C ANISOU 1478 CB ALEU A 187 1527 2175 2985 -193 122 -81 C ATOM 1479 CB BLEU A 187 -9.898 -3.854 24.587 0.40 17.44 C ANISOU 1479 CB BLEU A 187 1503 2160 2962 -187 104 -92 C ATOM 1480 CG ALEU A 187 -8.501 -4.049 24.011 0.60 18.70 C ANISOU 1480 CG ALEU A 187 1473 2267 3365 -242 169 -176 C ATOM 1481 CG BLEU A 187 -9.484 -2.989 23.397 0.40 18.46 C ANISOU 1481 CG BLEU A 187 1566 2151 3297 -291 347 -36 C ATOM 1482 CD1ALEU A 187 -8.513 -4.635 22.608 0.60 23.13 C ANISOU 1482 CD1ALEU A 187 2061 2839 3888 -263 356 -17 C ATOM 1483 CD1BLEU A 187 -8.252 -2.164 23.735 0.40 19.06 C ANISOU 1483 CD1BLEU A 187 1432 2103 3707 -376 349 -233 C ATOM 1484 CD2ALEU A 187 -7.707 -2.754 24.044 0.60 19.92 C ANISOU 1484 CD2ALEU A 187 1465 2272 3832 -348 249 -318 C ATOM 1485 CD2BLEU A 187 -9.242 -3.850 22.166 0.40 22.23 C ANISOU 1485 CD2BLEU A 187 2038 2673 3736 -290 486 87 C ATOM 1486 N VAL A 188 -10.771 -6.108 26.437 1.00 17.86 N ANISOU 1486 N VAL A 188 1755 2474 2557 41 -249 -60 N ATOM 1487 CA VAL A 188 -10.407 -7.195 27.342 1.00 17.92 C ANISOU 1487 CA VAL A 188 1782 2564 2463 167 -415 -93 C ATOM 1488 C VAL A 188 -11.137 -8.504 27.003 1.00 17.72 C ANISOU 1488 C VAL A 188 1909 2568 2255 193 -361 76 C ATOM 1489 O VAL A 188 -10.496 -9.552 26.938 1.00 19.04 O ANISOU 1489 O VAL A 188 2062 2733 2441 254 -397 80 O ATOM 1490 CB VAL A 188 -10.660 -6.810 28.824 1.00 19.68 C ANISOU 1490 CB VAL A 188 2033 2874 2569 276 -599 -185 C ATOM 1491 CG1 VAL A 188 -10.560 -8.035 29.728 1.00 20.65 C ANISOU 1491 CG1 VAL A 188 2242 3093 2512 442 -735 -146 C ATOM 1492 CG2 VAL A 188 -9.679 -5.736 29.260 1.00 17.46 C ANISOU 1492 CG2 VAL A 188 1554 2570 2510 270 -688 -421 C ATOM 1493 N PRO A 189 -12.466 -8.458 26.768 1.00 16.93 N ANISOU 1493 N PRO A 189 1945 2491 1995 148 -270 195 N ATOM 1494 CA PRO A 189 -13.102 -9.715 26.355 1.00 18.95 C ANISOU 1494 CA PRO A 189 2309 2758 2132 148 -199 314 C ATOM 1495 C PRO A 189 -12.594 -10.249 25.013 1.00 15.77 C ANISOU 1495 C PRO A 189 1834 2308 1849 98 -81 327 C ATOM 1496 O PRO A 189 -12.496 -11.464 24.847 1.00 20.21 O ANISOU 1496 O PRO A 189 2433 2852 2394 129 -77 363 O ATOM 1497 CB PRO A 189 -14.585 -9.340 26.259 1.00 20.32 C ANISOU 1497 CB PRO A 189 2592 2987 2143 98 -117 387 C ATOM 1498 CG PRO A 189 -14.742 -8.192 27.181 1.00 17.08 C ANISOU 1498 CG PRO A 189 2177 2611 1700 127 -211 323 C ATOM 1499 CD PRO A 189 -13.473 -7.412 27.035 1.00 18.12 C ANISOU 1499 CD PRO A 189 2156 2673 2055 118 -249 205 C ATOM 1500 N LEU A 190 -12.277 -9.361 24.075 1.00 15.10 N ANISOU 1500 N LEU A 190 1653 2200 1886 32 22 302 N ATOM 1501 CA LEU A 190 -11.746 -9.791 22.783 1.00 17.16 C ANISOU 1501 CA LEU A 190 1833 2445 2243 4 141 312 C ATOM 1502 C LEU A 190 -10.368 -10.425 22.937 1.00 18.60 C ANISOU 1502 C LEU A 190 1901 2594 2572 48 57 228 C ATOM 1503 O LEU A 190 -10.043 -11.390 22.245 1.00 18.06 O ANISOU 1503 O LEU A 190 1806 2528 2528 68 95 235 O ATOM 1504 CB LEU A 190 -11.676 -8.620 21.802 1.00 17.54 C ANISOU 1504 CB LEU A 190 1816 2474 2376 -55 294 331 C ATOM 1505 CG LEU A 190 -13.006 -8.148 21.208 1.00 21.00 C ANISOU 1505 CG LEU A 190 2358 2971 2651 -61 408 419 C ATOM 1506 CD1 LEU A 190 -12.793 -6.941 20.302 1.00 22.53 C ANISOU 1506 CD1 LEU A 190 2508 3124 2930 -83 570 463 C ATOM 1507 CD2 LEU A 190 -13.697 -9.278 20.458 1.00 24.10 C ANISOU 1507 CD2 LEU A 190 2793 3449 2914 -37 463 450 C ATOM 1508 N LEU A 191 -9.560 -9.883 23.844 1.00 16.33 N ANISOU 1508 N LEU A 191 1532 2291 2382 77 -66 122 N ATOM 1509 CA LEU A 191 -8.241 -10.446 24.109 1.00 18.03 C ANISOU 1509 CA LEU A 191 1623 2506 2722 148 -171 8 C ATOM 1510 C LEU A 191 -8.357 -11.788 24.832 1.00 17.67 C ANISOU 1510 C LEU A 191 1696 2479 2540 278 -294 48 C ATOM 1511 O LEU A 191 -7.584 -12.707 24.569 1.00 22.27 O ANISOU 1511 O LEU A 191 2229 3052 3179 346 -326 14 O ATOM 1512 CB LEU A 191 -7.388 -9.468 24.919 1.00 16.81 C ANISOU 1512 CB LEU A 191 1324 2352 2710 156 -279 -161 C ATOM 1513 CG LEU A 191 -6.925 -8.216 24.168 1.00 21.84 C ANISOU 1513 CG LEU A 191 1812 2922 3566 19 -132 -221 C ATOM 1514 CD1 LEU A 191 -6.133 -7.291 25.080 1.00 25.16 C ANISOU 1514 CD1 LEU A 191 2072 3330 4156 17 -246 -431 C ATOM 1515 CD2 LEU A 191 -6.108 -8.594 22.940 1.00 25.80 C ANISOU 1515 CD2 LEU A 191 2190 3409 4204 -28 5 -218 C ATOM 1516 N LEU A 192 -9.325 -11.897 25.740 1.00 16.42 N ANISOU 1516 N LEU A 192 1697 2340 2203 321 -349 128 N ATOM 1517 CA LEU A 192 -9.614 -13.169 26.401 1.00 21.38 C ANISOU 1517 CA LEU A 192 2475 2957 2693 437 -412 215 C ATOM 1518 C LEU A 192 -10.032 -14.201 25.368 1.00 19.69 C ANISOU 1518 C LEU A 192 2316 2679 2486 382 -280 298 C ATOM 1519 O LEU A 192 -9.624 -15.360 25.425 1.00 22.42 O ANISOU 1519 O LEU A 192 2706 2970 2843 472 -312 318 O ATOM 1520 CB LEU A 192 -10.712 -13.005 27.452 1.00 20.34 C ANISOU 1520 CB LEU A 192 2501 2862 2364 468 -445 303 C ATOM 1521 CG LEU A 192 -10.346 -12.279 28.746 1.00 27.12 C ANISOU 1521 CG LEU A 192 3331 3808 3167 584 -614 213 C ATOM 1522 CD1 LEU A 192 -11.587 -12.076 29.602 1.00 33.20 C ANISOU 1522 CD1 LEU A 192 4256 4633 3727 598 -612 313 C ATOM 1523 CD2 LEU A 192 -9.282 -13.048 29.515 1.00 28.60 C ANISOU 1523 CD2 LEU A 192 3502 4024 3341 790 -771 159 C ATOM 1524 N AMET A 193 -10.869 -13.773 24.425 0.70 19.19 N ANISOU 1524 N AMET A 193 2250 2627 2413 252 -135 333 N ATOM 1525 N BMET A 193 -10.846 -13.755 24.422 0.30 19.65 N ANISOU 1525 N BMET A 193 2305 2686 2474 252 -136 331 N ATOM 1526 CA AMET A 193 -11.300 -14.631 23.324 0.70 21.58 C ANISOU 1526 CA AMET A 193 2567 2903 2728 203 -11 363 C ATOM 1527 CA BMET A 193 -11.311 -14.585 23.325 0.30 22.01 C ANISOU 1527 CA BMET A 193 2620 2960 2781 200 -10 362 C ATOM 1528 C AMET A 193 -10.114 -15.162 22.537 0.70 21.83 C ANISOU 1528 C AMET A 193 2471 2916 2909 241 -13 287 C ATOM 1529 C BMET A 193 -10.157 -15.130 22.491 0.30 21.89 C ANISOU 1529 C BMET A 193 2478 2926 2915 236 -6 288 C ATOM 1530 O AMET A 193 -10.057 -16.346 22.206 0.70 22.96 O ANISOU 1530 O AMET A 193 2646 3004 3075 279 2 289 O ATOM 1531 O BMET A 193 -10.156 -16.296 22.099 0.30 22.34 O ANISOU 1531 O BMET A 193 2564 2931 2992 267 18 290 O ATOM 1532 CB AMET A 193 -12.228 -13.880 22.373 0.70 23.74 C ANISOU 1532 CB AMET A 193 2823 3243 2956 99 128 377 C ATOM 1533 CB BMET A 193 -12.255 -13.772 22.453 0.30 24.55 C ANISOU 1533 CB BMET A 193 2927 3348 3052 98 123 379 C ATOM 1534 CG AMET A 193 -13.684 -13.853 22.777 0.70 25.80 C ANISOU 1534 CG AMET A 193 3211 3535 3057 55 169 439 C ATOM 1535 CG BMET A 193 -12.801 -14.483 21.251 0.30 22.99 C ANISOU 1535 CG BMET A 193 2716 3174 2847 62 247 370 C ATOM 1536 SD AMET A 193 -14.667 -13.033 21.506 0.70 32.54 S ANISOU 1536 SD AMET A 193 4023 4499 3841 -12 320 427 S ATOM 1537 SD BMET A 193 -14.056 -13.411 20.549 0.30 48.61 S ANISOU 1537 SD BMET A 193 5971 6536 5964 1 369 389 S ATOM 1538 CE AMET A 193 -15.535 -11.813 22.488 0.70 31.19 C ANISOU 1538 CE AMET A 193 3936 4375 3540 -28 279 465 C ATOM 1539 CE BMET A 193 -15.042 -13.088 22.004 0.30 30.92 C ANISOU 1539 CE BMET A 193 3871 4290 3586 -17 296 445 C ATOM 1540 N LEU A 194 -9.178 -14.272 22.224 1.00 21.67 N ANISOU 1540 N LEU A 194 2297 2933 3004 226 -19 210 N ATOM 1541 CA LEU A 194 -7.988 -14.654 21.481 1.00 25.01 C ANISOU 1541 CA LEU A 194 2569 3361 3571 258 -12 123 C ATOM 1542 C LEU A 194 -7.201 -15.702 22.256 1.00 23.20 C ANISOU 1542 C LEU A 194 2361 3091 3363 399 -164 78 C ATOM 1543 O LEU A 194 -6.714 -16.673 21.680 1.00 23.51 O ANISOU 1543 O LEU A 194 2365 3107 3459 454 -159 44 O ATOM 1544 CB LEU A 194 -7.117 -13.428 21.200 1.00 23.82 C ANISOU 1544 CB LEU A 194 2244 3245 3561 202 23 44 C ATOM 1545 CG LEU A 194 -5.783 -13.673 20.492 1.00 24.63 C ANISOU 1545 CG LEU A 194 2156 3373 3828 224 42 -64 C ATOM 1546 CD1 LEU A 194 -6.009 -14.268 19.112 1.00 21.42 C ANISOU 1546 CD1 LEU A 194 1732 3003 3405 210 184 -25 C ATOM 1547 CD2 LEU A 194 -4.987 -12.380 20.401 1.00 25.77 C ANISOU 1547 CD2 LEU A 194 2127 3524 4139 141 98 -145 C ATOM 1548 N GLY A 195 -7.099 -15.508 23.567 1.00 19.20 N ANISOU 1548 N GLY A 195 1916 2585 2795 482 -303 75 N ATOM 1549 CA GLY A 195 -6.424 -16.461 24.429 1.00 24.24 C ANISOU 1549 CA GLY A 195 2604 3199 3407 665 -454 53 C ATOM 1550 C GLY A 195 -7.088 -17.825 24.427 1.00 27.27 C ANISOU 1550 C GLY A 195 3175 3475 3713 717 -412 176 C ATOM 1551 O GLY A 195 -6.412 -18.854 24.430 1.00 28.30 O ANISOU 1551 O GLY A 195 3319 3550 3884 848 -470 154 O ATOM 1552 N VAL A 196 -8.417 -17.834 24.419 1.00 22.47 N ANISOU 1552 N VAL A 196 2703 2827 3007 614 -305 293 N ATOM 1553 CA VAL A 196 -9.168 -19.083 24.414 1.00 19.20 C ANISOU 1553 CA VAL A 196 2455 2287 2555 624 -230 395 C ATOM 1554 C VAL A 196 -8.940 -19.846 23.110 1.00 18.03 C ANISOU 1554 C VAL A 196 2223 2092 2536 582 -147 324 C ATOM 1555 O VAL A 196 -8.681 -21.051 23.125 1.00 18.97 O ANISOU 1555 O VAL A 196 2412 2089 2706 673 -156 337 O ATOM 1556 CB VAL A 196 -10.680 -18.838 24.619 1.00 19.09 C ANISOU 1556 CB VAL A 196 2563 2266 2426 497 -119 496 C ATOM 1557 CG1 VAL A 196 -11.466 -20.121 24.416 1.00 17.84 C ANISOU 1557 CG1 VAL A 196 2532 1961 2285 463 -3 563 C ATOM 1558 CG2 VAL A 196 -10.940 -18.278 26.009 1.00 20.90 C ANISOU 1558 CG2 VAL A 196 2894 2541 2507 569 -205 573 C ATOM 1559 N TYR A 197 -9.019 -19.142 21.984 1.00 19.46 N ANISOU 1559 N TYR A 197 2256 2371 2766 466 -62 250 N ATOM 1560 CA TYR A 197 -8.828 -19.780 20.686 1.00 24.17 C ANISOU 1560 CA TYR A 197 2754 2970 3460 445 17 165 C ATOM 1561 C TYR A 197 -7.401 -20.289 20.508 1.00 24.65 C ANISOU 1561 C TYR A 197 2707 3025 3634 571 -76 72 C ATOM 1562 O TYR A 197 -7.188 -21.325 19.882 1.00 23.60 O ANISOU 1562 O TYR A 197 2557 2833 3576 618 -57 15 O ATOM 1563 CB TYR A 197 -9.204 -18.824 19.550 1.00 22.17 C ANISOU 1563 CB TYR A 197 2375 2855 3193 334 135 125 C ATOM 1564 CG TYR A 197 -10.695 -18.774 19.314 1.00 21.79 C ANISOU 1564 CG TYR A 197 2412 2824 3045 236 242 164 C ATOM 1565 CD1 TYR A 197 -11.380 -19.898 18.867 1.00 22.41 C ANISOU 1565 CD1 TYR A 197 2530 2839 3147 218 305 120 C ATOM 1566 CD2 TYR A 197 -11.422 -17.614 19.551 1.00 21.83 C ANISOU 1566 CD2 TYR A 197 2444 2907 2943 166 277 221 C ATOM 1567 CE1 TYR A 197 -12.743 -19.868 18.661 1.00 23.90 C ANISOU 1567 CE1 TYR A 197 2764 3062 3256 127 400 115 C ATOM 1568 CE2 TYR A 197 -12.789 -17.575 19.345 1.00 18.69 C ANISOU 1568 CE2 TYR A 197 2108 2550 2444 93 365 233 C ATOM 1569 CZ TYR A 197 -13.443 -18.704 18.902 1.00 24.03 C ANISOU 1569 CZ TYR A 197 2803 3182 3145 71 426 172 C ATOM 1570 OH TYR A 197 -14.802 -18.670 18.698 1.00 26.17 O ANISOU 1570 OH TYR A 197 3103 3513 3328 -5 512 144 O ATOM 1571 N LEU A 198 -6.429 -19.574 21.064 1.00 21.55 N ANISOU 1571 N LEU A 198 2226 2699 3262 631 -181 31 N ATOM 1572 CA LEU A 198 -5.049 -20.050 21.042 1.00 26.13 C ANISOU 1572 CA LEU A 198 2691 3296 3942 769 -289 -81 C ATOM 1573 C LEU A 198 -4.929 -21.368 21.801 1.00 25.16 C ANISOU 1573 C LEU A 198 2732 3035 3791 941 -384 -34 C ATOM 1574 O LEU A 198 -4.248 -22.292 21.356 1.00 23.57 O ANISOU 1574 O LEU A 198 2490 2793 3672 1045 -416 -108 O ATOM 1575 CB LEU A 198 -4.098 -19.010 21.637 1.00 29.47 C ANISOU 1575 CB LEU A 198 2973 3822 4401 798 -390 -168 C ATOM 1576 CG LEU A 198 -3.834 -17.757 20.798 1.00 36.12 C ANISOU 1576 CG LEU A 198 3622 4769 5333 647 -278 -231 C ATOM 1577 CD1 LEU A 198 -2.864 -16.828 21.512 1.00 36.53 C ANISOU 1577 CD1 LEU A 198 3524 4890 5466 669 -379 -353 C ATOM 1578 CD2 LEU A 198 -3.310 -18.134 19.421 1.00 39.03 C ANISOU 1578 CD2 LEU A 198 3844 5188 5797 626 -176 -302 C ATOM 1579 N ARG A 199 -5.602 -21.450 22.944 1.00 24.82 N ANISOU 1579 N ARG A 199 2884 2919 3629 982 -417 97 N ATOM 1580 CA ARG A 199 -5.591 -22.663 23.753 1.00 29.25 C ANISOU 1580 CA ARG A 199 3642 3326 4145 1159 -473 191 C ATOM 1581 C ARG A 199 -6.334 -23.800 23.056 1.00 22.68 C ANISOU 1581 C ARG A 199 2912 2319 3385 1093 -337 235 C ATOM 1582 O ARG A 199 -5.974 -24.966 23.205 1.00 28.78 O ANISOU 1582 O ARG A 199 3786 2941 4209 1238 -363 256 O ATOM 1583 CB ARG A 199 -6.200 -22.394 25.131 1.00 33.28 C ANISOU 1583 CB ARG A 199 4336 3820 4488 1219 -512 338 C ATOM 1584 CG ARG A 199 -5.357 -21.479 26.007 1.00 38.74 C ANISOU 1584 CG ARG A 199 4931 4678 5110 1346 -683 258 C ATOM 1585 CD ARG A 199 -6.064 -21.153 27.314 1.00 43.93 C ANISOU 1585 CD ARG A 199 5760 5352 5579 1410 -716 394 C ATOM 1586 NE ARG A 199 -6.339 -22.349 28.104 1.00 56.73 N ANISOU 1586 NE ARG A 199 7632 6825 7097 1585 -702 570 N ATOM 1587 CZ ARG A 199 -5.503 -22.859 29.003 1.00 67.68 C ANISOU 1587 CZ ARG A 199 9052 8250 8414 1759 -797 554 C ATOM 1588 NH1 ARG A 199 -4.333 -22.276 29.229 1.00 71.36 N ANISOU 1588 NH1 ARG A 199 9335 8893 8887 1850 -949 365 N ATOM 1589 NH2 ARG A 199 -5.836 -23.952 29.677 1.00 70.13 N ANISOU 1589 NH2 ARG A 199 9574 8423 8651 1839 -725 717 N ATOM 1590 N ILE A 200 -7.367 -23.457 22.292 1.00 21.12 N ANISOU 1590 N ILE A 200 2682 2142 3200 886 -193 233 N ATOM 1591 CA ILE A 200 -8.123 -24.452 21.538 1.00 25.99 C ANISOU 1591 CA ILE A 200 3347 2621 3907 804 -62 215 C ATOM 1592 C ILE A 200 -7.263 -25.102 20.458 1.00 23.57 C ANISOU 1592 C ILE A 200 2893 2321 3740 867 -83 56 C ATOM 1593 O ILE A 200 -7.177 -26.326 20.373 1.00 25.98 O ANISOU 1593 O ILE A 200 3280 2447 4145 945 -71 41 O ATOM 1594 CB ILE A 200 -9.373 -23.837 20.877 1.00 26.03 C ANISOU 1594 CB ILE A 200 3305 2709 3876 595 76 197 C ATOM 1595 CG1 ILE A 200 -10.411 -23.461 21.937 1.00 25.31 C ANISOU 1595 CG1 ILE A 200 3378 2582 3657 529 118 348 C ATOM 1596 CG2 ILE A 200 -9.978 -24.808 19.881 1.00 20.08 C ANISOU 1596 CG2 ILE A 200 2522 1866 3240 522 191 93 C ATOM 1597 CD1 ILE A 200 -11.651 -22.798 21.367 1.00 25.27 C ANISOU 1597 CD1 ILE A 200 3322 2682 3597 347 238 316 C ATOM 1598 N PHE A 201 -6.624 -24.276 19.638 1.00 24.31 N ANISOU 1598 N PHE A 201 2773 2616 3847 837 -103 -59 N ATOM 1599 CA PHE A 201 -5.813 -24.775 18.537 1.00 28.85 C ANISOU 1599 CA PHE A 201 3182 3245 4534 895 -112 -217 C ATOM 1600 C PHE A 201 -4.563 -25.496 19.034 1.00 28.52 C ANISOU 1600 C PHE A 201 3149 3138 4551 1105 -257 -257 C ATOM 1601 O PHE A 201 -4.095 -26.443 18.402 1.00 27.94 O ANISOU 1601 O PHE A 201 3027 3009 4581 1193 -270 -364 O ATOM 1602 CB PHE A 201 -5.437 -23.626 17.601 1.00 30.76 C ANISOU 1602 CB PHE A 201 3203 3723 4762 815 -66 -297 C ATOM 1603 CG PHE A 201 -6.613 -23.038 16.875 1.00 30.00 C ANISOU 1603 CG PHE A 201 3089 3712 4597 659 78 -280 C ATOM 1604 CD1 PHE A 201 -7.526 -23.860 16.234 1.00 31.65 C ANISOU 1604 CD1 PHE A 201 3329 3864 4831 617 162 -340 C ATOM 1605 CD2 PHE A 201 -6.816 -21.670 16.848 1.00 31.27 C ANISOU 1605 CD2 PHE A 201 3198 4009 4676 568 127 -223 C ATOM 1606 CE1 PHE A 201 -8.613 -23.327 15.568 1.00 33.25 C ANISOU 1606 CE1 PHE A 201 3500 4182 4953 506 278 -354 C ATOM 1607 CE2 PHE A 201 -7.904 -21.130 16.186 1.00 30.54 C ANISOU 1607 CE2 PHE A 201 3100 4007 4497 464 251 -206 C ATOM 1608 CZ PHE A 201 -8.803 -21.960 15.546 1.00 29.60 C ANISOU 1608 CZ PHE A 201 3001 3867 4378 442 320 -277 C ATOM 1609 N ALA A 202 -4.031 -25.054 20.169 1.00 25.13 N ANISOU 1609 N ALA A 202 2772 2729 4047 1206 -374 -190 N ATOM 1610 CA ALA A 202 -2.877 -25.715 20.767 1.00 30.44 C ANISOU 1610 CA ALA A 202 3462 3364 4740 1448 -531 -233 C ATOM 1611 C ALA A 202 -3.276 -27.081 21.318 1.00 31.88 C ANISOU 1611 C ALA A 202 3897 3283 4934 1577 -522 -120 C ATOM 1612 O ALA A 202 -2.507 -28.041 21.246 1.00 31.66 O ANISOU 1612 O ALA A 202 3884 3169 4975 1765 -598 -182 O ATOM 1613 CB ALA A 202 -2.270 -24.849 21.865 1.00 28.62 C ANISOU 1613 CB ALA A 202 3207 3255 4411 1542 -666 -220 C ATOM 1614 N ALA A 203 -4.487 -27.163 21.863 1.00 30.19 N ANISOU 1614 N ALA A 203 3881 2929 4660 1475 -416 47 N ATOM 1615 CA ALA A 203 -5.006 -28.422 22.388 1.00 33.54 C ANISOU 1615 CA ALA A 203 4559 3065 5118 1559 -352 181 C ATOM 1616 C ALA A 203 -5.249 -29.416 21.258 1.00 34.35 C ANISOU 1616 C ALA A 203 4619 3023 5410 1490 -252 63 C ATOM 1617 O ALA A 203 -4.993 -30.611 21.404 1.00 36.80 O ANISOU 1617 O ALA A 203 5061 3104 5816 1637 -253 84 O ATOM 1618 CB ALA A 203 -6.288 -28.185 23.175 1.00 34.00 C ANISOU 1618 CB ALA A 203 4807 3033 5079 1433 -232 374 C ATOM 1619 N ALA A 204 -5.742 -28.911 20.132 1.00 32.62 N ANISOU 1619 N ALA A 204 4213 2942 5238 1286 -167 -69 N ATOM 1620 CA ALA A 204 -5.985 -29.734 18.953 1.00 31.19 C ANISOU 1620 CA ALA A 204 3942 2687 5223 1225 -85 -234 C ATOM 1621 C ALA A 204 -4.686 -30.298 18.393 1.00 31.47 C ANISOU 1621 C ALA A 204 3852 2761 5346 1412 -204 -389 C ATOM 1622 O ALA A 204 -4.595 -31.482 18.074 1.00 35.61 O ANISOU 1622 O ALA A 204 4426 3086 6017 1492 -188 -464 O ATOM 1623 CB ALA A 204 -6.704 -28.928 17.890 1.00 28.07 C ANISOU 1623 CB ALA A 204 3360 2503 4804 1019 10 -347 C ATOM 1624 N ARG A 205 -3.687 -29.432 18.271 1.00 33.90 N ANISOU 1624 N ARG A 205 3985 3320 5576 1475 -314 -451 N ATOM 1625 CA ARG A 205 -2.389 -29.815 17.729 1.00 42.26 C ANISOU 1625 CA ARG A 205 4884 4471 6703 1647 -428 -618 C ATOM 1626 C ARG A 205 -1.712 -30.870 18.598 1.00 40.15 C ANISOU 1626 C ARG A 205 4803 4027 6426 1855 -517 -541 C ATOM 1627 O ARG A 205 -1.058 -31.783 18.090 1.00 43.41 O ANISOU 1627 O ARG A 205 5181 4410 6902 1938 -540 -642 O ATOM 1628 CB ARG A 205 -1.494 -28.580 17.595 1.00 50.05 C ANISOU 1628 CB ARG A 205 5657 5763 7595 1620 -491 -672 C ATOM 1629 CG ARG A 205 -0.096 -28.862 17.079 1.00 63.04 C ANISOU 1629 CG ARG A 205 7153 7564 9234 1692 -563 -804 C ATOM 1630 CD ARG A 205 0.775 -27.624 17.201 1.00 71.10 C ANISOU 1630 CD ARG A 205 8004 8829 10181 1634 -603 -838 C ATOM 1631 NE ARG A 205 0.709 -27.061 18.547 1.00 78.75 N ANISOU 1631 NE ARG A 205 9078 9769 11076 1689 -684 -730 N ATOM 1632 CZ ARG A 205 1.371 -25.979 18.941 1.00 85.82 C ANISOU 1632 CZ ARG A 205 9851 10834 11924 1644 -730 -767 C ATOM 1633 NH1 ARG A 205 2.160 -25.335 18.092 1.00 89.21 N ANISOU 1633 NH1 ARG A 205 10065 11444 12386 1533 -680 -886 N ATOM 1634 NH2 ARG A 205 1.246 -25.541 20.186 1.00 87.79 N ANISOU 1634 NH2 ARG A 205 10202 11064 12092 1705 -812 -685 N ATOM 1635 N ARG A 206 -1.880 -30.745 19.911 1.00 37.32 N ANISOU 1635 N ARG A 206 4644 3571 5964 1936 -554 -352 N ATOM 1636 CA ARG A 206 -1.278 -31.683 20.849 1.00 35.49 C ANISOU 1636 CA ARG A 206 4595 3204 5685 2134 -610 -241 C ATOM 1637 C ARG A 206 -1.946 -33.053 20.779 1.00 40.27 C ANISOU 1637 C ARG A 206 5405 3464 6431 2152 -484 -167 C ATOM 1638 O ARG A 206 -1.275 -34.082 20.846 1.00 42.38 O ANISOU 1638 O ARG A 206 5729 3626 6748 2299 -508 -176 O ATOM 1639 CB ARG A 206 -1.352 -31.138 22.277 1.00 45.73 C ANISOU 1639 CB ARG A 206 6035 4534 6807 2202 -663 -56 C ATOM 1640 CG ARG A 206 -0.639 -32.008 23.299 1.00 57.64 C ANISOU 1640 CG ARG A 206 7698 5965 8238 2420 -732 47 C ATOM 1641 CD ARG A 206 -0.691 -31.403 24.692 1.00 68.89 C ANISOU 1641 CD ARG A 206 9231 7485 9459 2488 -794 193 C ATOM 1642 NE ARG A 206 0.073 -32.197 25.651 1.00 80.11 N ANISOU 1642 NE ARG A 206 10781 8879 10779 2723 -874 263 N ATOM 1643 CZ ARG A 206 0.189 -31.903 26.942 1.00 85.92 C ANISOU 1643 CZ ARG A 206 11622 9710 11312 2841 -939 368 C ATOM 1644 NH1 ARG A 206 -0.411 -30.829 27.436 1.00 86.63 N ANISOU 1644 NH1 ARG A 206 11700 9922 11294 2732 -933 415 N ATOM 1645 NH2 ARG A 206 0.906 -32.683 27.739 1.00 90.39 N ANISOU 1645 NH2 ARG A 206 12308 10260 11776 3080 -1009 416 N ATOM 1646 N GLN A 207 -3.267 -33.064 20.644 1.00 38.70 N ANISOU 1646 N GLN A 207 5309 3082 6312 1991 -340 -107 N ATOM 1647 CA GLN A 207 -4.009 -34.318 20.596 1.00 41.69 C ANISOU 1647 CA GLN A 207 5877 3107 6855 1959 -181 -50 C ATOM 1648 C GLN A 207 -3.771 -35.057 19.284 1.00 39.01 C ANISOU 1648 C GLN A 207 5391 2757 6673 1927 -167 -297 C ATOM 1649 O GLN A 207 -3.728 -36.286 19.257 1.00 41.32 O ANISOU 1649 O GLN A 207 5823 2806 7072 1999 -98 -291 O ATOM 1650 CB GLN A 207 -5.501 -34.065 20.802 1.00 39.63 C ANISOU 1650 CB GLN A 207 5742 2685 6632 1749 -31 47 C ATOM 1651 CG GLN A 207 -5.844 -33.583 22.199 1.00 42.59 C ANISOU 1651 CG GLN A 207 6291 3071 6821 1754 -36 311 C ATOM 1652 CD GLN A 207 -7.310 -33.239 22.353 1.00 47.32 C ANISOU 1652 CD GLN A 207 6972 3602 7405 1500 156 407 C ATOM 1653 OE1 GLN A 207 -8.160 -33.755 21.628 1.00 51.62 O ANISOU 1653 OE1 GLN A 207 7482 4007 8125 1307 310 302 O ATOM 1654 NE2 GLN A 207 -7.614 -32.357 23.298 1.00 41.83 N ANISOU 1654 NE2 GLN A 207 6348 3042 6502 1484 140 577 N ATOM 1655 N LEU A 208 -3.614 -34.306 18.199 1.00 40.91 N ANISOU 1655 N LEU A 208 5346 3277 6921 1821 -219 -507 N ATOM 1656 CA LEU A 208 -3.289 -34.902 16.908 1.00 42.78 C ANISOU 1656 CA LEU A 208 5398 3589 7266 1797 -219 -747 C ATOM 1657 C LEU A 208 -1.883 -35.488 16.940 1.00 44.91 C ANISOU 1657 C LEU A 208 5646 3920 7499 2010 -344 -785 C ATOM 1658 O LEU A 208 -1.610 -36.514 16.314 1.00 48.05 O ANISOU 1658 O LEU A 208 6028 4225 8005 2059 -336 -908 O ATOM 1659 CB LEU A 208 -3.410 -33.868 15.786 1.00 48.57 C ANISOU 1659 CB LEU A 208 5838 4656 7962 1651 -220 -922 C ATOM 1660 CG LEU A 208 -4.827 -33.452 15.388 1.00 53.97 C ANISOU 1660 CG LEU A 208 6481 5322 8704 1433 -76 -961 C ATOM 1661 CD1 LEU A 208 -4.801 -32.176 14.556 1.00 56.15 C ANISOU 1661 CD1 LEU A 208 6507 5970 8859 1342 -76 -1053 C ATOM 1662 CD2 LEU A 208 -5.515 -34.574 14.626 1.00 56.52 C ANISOU 1662 CD2 LEU A 208 6796 5487 9191 1345 22 -1121 C ATOM 1663 N ALA A1001 -0.996 -34.831 17.681 1.00 63.60 N ANISOU 1663 N ALA A1001 7454 4290 12422 2174 88 -782 N ATOM 1664 CA ALA A1001 0.374 -35.301 17.843 1.00 64.86 C ANISOU 1664 CA ALA A1001 7182 4301 13161 1910 261 -635 C ATOM 1665 C ALA A1001 0.418 -36.567 18.691 1.00 61.94 C ANISOU 1665 C ALA A1001 6481 4285 12770 1820 171 -706 C ATOM 1666 O ALA A1001 1.200 -37.477 18.422 1.00 63.68 O ANISOU 1666 O ALA A1001 6469 4520 13205 1708 411 -567 O ATOM 1667 CB ALA A1001 1.238 -34.214 18.465 1.00 68.22 C ANISOU 1667 CB ALA A1001 7372 4370 14178 1712 137 -642 C ATOM 1668 N ASP A1002 -0.429 -36.617 19.715 1.00 60.62 N ANISOU 1668 N ASP A1002 6324 4387 12323 1885 -135 -896 N ATOM 1669 CA ASP A1002 -0.503 -37.780 20.593 1.00 59.78 C ANISOU 1669 CA ASP A1002 6005 4590 12118 1850 -180 -931 C ATOM 1670 C ASP A1002 -1.019 -39.010 19.850 1.00 58.87 C ANISOU 1670 C ASP A1002 5995 4684 11689 1902 76 -875 C ATOM 1671 O ASP A1002 -0.558 -40.126 20.090 1.00 54.86 O ANISOU 1671 O ASP A1002 5299 4289 11257 1820 211 -797 O ATOM 1672 CB ASP A1002 -1.393 -37.486 21.803 1.00 59.41 C ANISOU 1672 CB ASP A1002 6008 4759 11806 1948 -493 -1110 C ATOM 1673 CG ASP A1002 -0.776 -36.472 22.748 1.00 68.52 C ANISOU 1673 CG ASP A1002 6999 5747 13287 1909 -827 -1230 C ATOM 1674 OD1 ASP A1002 0.468 -36.367 22.780 1.00 74.56 O ANISOU 1674 OD1 ASP A1002 7482 6285 14561 1771 -823 -1184 O ATOM 1675 OD2 ASP A1002 -1.535 -35.782 23.460 1.00 72.68 O ANISOU 1675 OD2 ASP A1002 7651 6365 13599 2013 -1106 -1395 O ATOM 1676 N LEU A1003 -1.977 -38.801 18.952 1.00 55.18 N ANISOU 1676 N LEU A1003 5837 4256 10872 2061 122 -937 N ATOM 1677 CA LEU A1003 -2.514 -39.889 18.142 1.00 54.02 C ANISOU 1677 CA LEU A1003 5780 4281 10465 2133 305 -954 C ATOM 1678 C LEU A1003 -1.441 -40.476 17.236 1.00 64.80 C ANISOU 1678 C LEU A1003 7061 5505 12056 2066 579 -790 C ATOM 1679 O LEU A1003 -1.356 -41.691 17.061 1.00 54.29 O ANISOU 1679 O LEU A1003 5620 4306 10701 2010 724 -771 O ATOM 1680 CB LEU A1003 -3.696 -39.406 17.299 1.00 55.45 C ANISOU 1680 CB LEU A1003 6306 4512 10252 2375 269 -1080 C ATOM 1681 CG LEU A1003 -4.993 -39.084 18.040 1.00 56.19 C ANISOU 1681 CG LEU A1003 6432 4792 10124 2412 76 -1243 C ATOM 1682 CD1 LEU A1003 -6.030 -38.541 17.073 1.00 59.14 C ANISOU 1682 CD1 LEU A1003 7093 5174 10205 2626 84 -1349 C ATOM 1683 CD2 LEU A1003 -5.519 -40.317 18.756 1.00 55.72 C ANISOU 1683 CD2 LEU A1003 6151 4974 10046 2297 103 -1305 C ATOM 1684 N GLU A1004 -0.621 -39.603 16.663 1.00 65.79 N ANISOU 1684 N GLU A1004 7236 5329 12432 2062 687 -654 N ATOM 1685 CA GLU A1004 0.429 -40.035 15.752 1.00 72.31 C ANISOU 1685 CA GLU A1004 7977 5987 13512 2000 1030 -446 C ATOM 1686 C GLU A1004 1.569 -40.706 16.511 1.00 67.13 C ANISOU 1686 C GLU A1004 6887 5318 13302 1736 1136 -308 C ATOM 1687 O GLU A1004 2.160 -41.668 16.026 1.00 67.32 O ANISOU 1687 O GLU A1004 6800 5367 13412 1678 1397 -180 O ATOM 1688 CB GLU A1004 0.955 -38.852 14.937 1.00 83.59 C ANISOU 1688 CB GLU A1004 9592 7046 15122 2067 1207 -283 C ATOM 1689 CG GLU A1004 1.889 -39.251 13.805 1.00 93.43 C ANISOU 1689 CG GLU A1004 10827 8121 16552 2067 1662 -24 C ATOM 1690 CD GLU A1004 1.218 -40.154 12.784 1.00 98.78 C ANISOU 1690 CD GLU A1004 11767 9017 16747 2328 1713 -132 C ATOM 1691 OE1 GLU A1004 1.906 -41.032 12.222 1.00100.46 O ANISOU 1691 OE1 GLU A1004 11862 9241 17067 2283 2017 16 O ATOM 1692 OE2 GLU A1004 0.004 -39.982 12.540 1.00101.05 O ANISOU 1692 OE2 GLU A1004 12363 9468 16563 2598 1428 -393 O ATOM 1693 N ASP A1005 1.870 -40.197 17.702 1.00 63.85 N ANISOU 1693 N ASP A1005 6248 4866 13146 1620 904 -357 N ATOM 1694 CA ASP A1005 2.929 -40.766 18.528 1.00 65.69 C ANISOU 1694 CA ASP A1005 6092 5100 13767 1450 919 -279 C ATOM 1695 C ASP A1005 2.572 -42.173 18.996 1.00 63.87 C ANISOU 1695 C ASP A1005 5860 5178 13229 1476 926 -307 C ATOM 1696 O ASP A1005 3.431 -43.053 19.046 1.00 58.11 O ANISOU 1696 O ASP A1005 4942 4456 12681 1393 1102 -174 O ATOM 1697 CB ASP A1005 3.220 -39.866 19.730 1.00 72.26 C ANISOU 1697 CB ASP A1005 6724 5844 14886 1404 574 -406 C ATOM 1698 CG ASP A1005 4.011 -38.629 19.351 1.00 83.14 C ANISOU 1698 CG ASP A1005 7955 6813 16822 1291 627 -348 C ATOM 1699 OD1 ASP A1005 4.809 -38.706 18.394 1.00 88.10 O ANISOU 1699 OD1 ASP A1005 8486 7219 17768 1200 1021 -127 O ATOM 1700 OD2 ASP A1005 3.837 -37.581 20.009 1.00 87.09 O ANISOU 1700 OD2 ASP A1005 8439 7195 17458 1294 307 -515 O ATOM 1701 N ASN A1006 1.305 -42.383 19.337 1.00 59.86 N ANISOU 1701 N ASN A1006 5566 4898 12281 1595 764 -467 N ATOM 1702 CA ASN A1006 0.838 -43.711 19.713 1.00 58.54 C ANISOU 1702 CA ASN A1006 5415 4961 11865 1613 833 -481 C ATOM 1703 C ASN A1006 0.910 -44.669 18.531 1.00 57.71 C ANISOU 1703 C ASN A1006 5366 4849 11713 1583 1111 -418 C ATOM 1704 O ASN A1006 1.385 -45.796 18.663 1.00 53.47 O ANISOU 1704 O ASN A1006 4727 4354 11235 1517 1272 -321 O ATOM 1705 CB ASN A1006 -0.590 -43.651 20.256 1.00 60.68 C ANISOU 1705 CB ASN A1006 5860 5426 11769 1731 658 -655 C ATOM 1706 CG ASN A1006 -0.652 -43.123 21.675 1.00 64.33 C ANISOU 1706 CG ASN A1006 6270 5965 12208 1807 422 -697 C ATOM 1707 OD1 ASN A1006 0.293 -43.278 22.449 1.00 67.28 O ANISOU 1707 OD1 ASN A1006 6472 6327 12763 1807 383 -615 O ATOM 1708 ND2 ASN A1006 -1.770 -42.500 22.026 1.00 63.83 N ANISOU 1708 ND2 ASN A1006 6360 5992 11899 1912 254 -834 N ATOM 1709 N TRP A1007 0.446 -44.206 17.375 1.00 53.95 N ANISOU 1709 N TRP A1007 5086 4313 11098 1680 1152 -483 N ATOM 1710 CA TRP A1007 0.485 -44.996 16.150 1.00 54.48 C ANISOU 1710 CA TRP A1007 5248 4379 11074 1732 1374 -467 C ATOM 1711 C TRP A1007 1.916 -45.379 15.778 1.00 61.56 C ANISOU 1711 C TRP A1007 5967 5116 12306 1613 1666 -216 C ATOM 1712 O TRP A1007 2.176 -46.509 15.362 1.00 56.13 O ANISOU 1712 O TRP A1007 5253 4472 11601 1587 1847 -168 O ATOM 1713 CB TRP A1007 -0.173 -44.227 15.003 1.00 55.53 C ANISOU 1713 CB TRP A1007 5682 4469 10947 1969 1330 -585 C ATOM 1714 CG TRP A1007 -0.095 -44.924 13.679 1.00 58.90 C ANISOU 1714 CG TRP A1007 6245 4899 11235 2118 1518 -603 C ATOM 1715 CD1 TRP A1007 0.693 -44.582 12.619 1.00 62.03 C ANISOU 1715 CD1 TRP A1007 6749 5111 11710 2225 1761 -441 C ATOM 1716 CD2 TRP A1007 -0.828 -46.088 13.275 1.00 56.40 C ANISOU 1716 CD2 TRP A1007 5971 4761 10697 2197 1494 -797 C ATOM 1717 NE1 TRP A1007 0.492 -45.457 11.579 1.00 65.32 N ANISOU 1717 NE1 TRP A1007 7296 5617 11906 2410 1846 -549 N ATOM 1718 CE2 TRP A1007 -0.437 -46.391 11.956 1.00 63.18 C ANISOU 1718 CE2 TRP A1007 6975 5566 11463 2393 1661 -790 C ATOM 1719 CE3 TRP A1007 -1.780 -46.901 13.900 1.00 54.93 C ANISOU 1719 CE3 TRP A1007 5701 4741 10427 2120 1378 -968 C ATOM 1720 CZ2 TRP A1007 -0.962 -47.473 11.251 1.00 65.71 C ANISOU 1720 CZ2 TRP A1007 7360 6019 11586 2539 1649 -997 C ATOM 1721 CZ3 TRP A1007 -2.301 -47.973 13.198 1.00 55.93 C ANISOU 1721 CZ3 TRP A1007 5846 4935 10469 2197 1433 -1141 C ATOM 1722 CH2 TRP A1007 -1.891 -48.249 11.887 1.00 63.00 C ANISOU 1722 CH2 TRP A1007 6904 5811 11222 2424 1532 -1169 C ATOM 1723 N GLU A1008 2.840 -44.438 15.935 1.00 57.79 N ANISOU 1723 N GLU A1008 5348 4433 12177 1538 1722 -60 N ATOM 1724 CA GLU A1008 4.246 -44.696 15.641 1.00 66.20 C ANISOU 1724 CA GLU A1008 6184 5322 13647 1415 2028 196 C ATOM 1725 C GLU A1008 4.853 -45.672 16.643 1.00 62.32 C ANISOU 1725 C GLU A1008 5462 4932 13286 1299 1991 245 C ATOM 1726 O GLU A1008 5.627 -46.551 16.268 1.00 60.17 O ANISOU 1726 O GLU A1008 5109 4630 13123 1256 2234 398 O ATOM 1727 CB GLU A1008 5.043 -43.390 15.630 1.00 69.32 C ANISOU 1727 CB GLU A1008 6419 5423 14496 1342 2104 328 C ATOM 1728 CG GLU A1008 4.755 -42.502 14.430 1.00 77.03 C ANISOU 1728 CG GLU A1008 7686 6218 15365 1495 2294 392 C ATOM 1729 CD GLU A1008 5.444 -41.155 14.522 1.00 88.10 C ANISOU 1729 CD GLU A1008 8941 7272 17262 1400 2388 524 C ATOM 1730 OE1 GLU A1008 6.294 -40.981 15.420 1.00 92.77 O ANISOU 1730 OE1 GLU A1008 9115 7754 18380 1196 2309 543 O ATOM 1731 OE2 GLU A1008 5.132 -40.270 13.698 1.00 91.90 O ANISOU 1731 OE2 GLU A1008 9736 7568 17613 1547 2525 588 O ATOM 1732 N THR A1009 4.497 -45.515 17.915 1.00 58.16 N ANISOU 1732 N THR A1009 4875 4526 12696 1305 1687 119 N ATOM 1733 CA THR A1009 4.986 -46.399 18.969 1.00 60.91 C ANISOU 1733 CA THR A1009 5087 4999 13058 1305 1627 156 C ATOM 1734 C THR A1009 4.533 -47.834 18.714 1.00 59.77 C ANISOU 1734 C THR A1009 5087 4990 12633 1330 1786 170 C ATOM 1735 O THR A1009 5.262 -48.788 18.990 1.00 57.43 O ANISOU 1735 O THR A1009 4705 4716 12401 1330 1908 291 O ATOM 1736 CB THR A1009 4.501 -45.939 20.359 1.00 60.29 C ANISOU 1736 CB THR A1009 4999 5062 12846 1407 1283 8 C ATOM 1737 OG1 THR A1009 4.927 -44.590 20.593 1.00 63.89 O ANISOU 1737 OG1 THR A1009 5301 5353 13622 1372 1093 -49 O ATOM 1738 CG2 THR A1009 5.061 -46.836 21.454 1.00 60.39 C ANISOU 1738 CG2 THR A1009 4914 5232 12801 1519 1239 61 C ATOM 1739 N ALEU A1010 3.330 -47.977 18.169 0.50 55.15 N ANISOU 1739 N ALEU A1010 4709 4478 11766 1367 1770 23 N ATOM 1740 N BLEU A1010 3.319 -47.976 18.191 0.50 55.13 N ANISOU 1740 N BLEU A1010 4707 4478 11761 1368 1766 22 N ATOM 1741 CA ALEU A1010 2.777 -49.288 17.853 0.50 54.84 C ANISOU 1741 CA ALEU A1010 4769 4515 11551 1369 1902 -20 C ATOM 1742 CA BLEU A1010 2.775 -49.283 17.839 0.50 54.87 C ANISOU 1742 CA BLEU A1010 4775 4519 11555 1369 1903 -20 C ATOM 1743 C ALEU A1010 3.554 -49.977 16.732 0.50 55.70 C ANISOU 1743 C ALEU A1010 4873 4522 11769 1340 2175 103 C ATOM 1744 C BLEU A1010 3.605 -49.958 16.755 0.50 55.74 C ANISOU 1744 C BLEU A1010 4871 4524 11785 1338 2176 112 C ATOM 1745 O ALEU A1010 3.901 -51.152 16.840 0.50 56.06 O ANISOU 1745 O ALEU A1010 4892 4568 11841 1313 2321 183 O ATOM 1746 O BLEU A1010 4.035 -51.101 16.908 0.50 56.16 O ANISOU 1746 O BLEU A1010 4887 4575 11878 1310 2322 205 O ATOM 1747 CB ALEU A1010 1.302 -49.158 17.469 0.50 53.29 C ANISOU 1747 CB ALEU A1010 4742 4409 11095 1432 1779 -261 C ATOM 1748 CB BLEU A1010 1.324 -49.153 17.370 0.50 53.90 C ANISOU 1748 CB BLEU A1010 4824 4482 11174 1433 1788 -261 C ATOM 1749 CG ALEU A1010 0.570 -50.442 17.074 0.50 54.84 C ANISOU 1749 CG ALEU A1010 4966 4608 11264 1404 1918 -369 C ATOM 1750 CG BLEU A1010 0.224 -49.524 18.365 0.50 52.63 C ANISOU 1750 CG BLEU A1010 4664 4411 10923 1434 1690 -382 C ATOM 1751 CD1ALEU A1010 0.637 -51.463 18.195 0.50 55.57 C ANISOU 1751 CD1ALEU A1010 4958 4675 11481 1332 2034 -263 C ATOM 1752 CD1BLEU A1010 0.423 -50.945 18.866 0.50 57.45 C ANISOU 1752 CD1BLEU A1010 5192 4970 11667 1365 1909 -275 C ATOM 1753 CD2ALEU A1010 -0.873 -50.136 16.713 0.50 54.11 C ANISOU 1753 CD2ALEU A1010 4968 4584 11008 1477 1768 -648 C ATOM 1754 CD2BLEU A1010 0.179 -48.539 19.518 0.50 58.60 C ANISOU 1754 CD2BLEU A1010 5405 5244 11616 1500 1463 -378 C ATOM 1755 N ASN A1011 3.828 -49.240 15.659 1.00 56.77 N ANISOU 1755 N ASN A1011 5056 4558 11955 1380 2267 133 N ATOM 1756 CA ASN A1011 4.539 -49.794 14.511 1.00 61.32 C ANISOU 1756 CA ASN A1011 5662 5045 12592 1413 2553 259 C ATOM 1757 C ASN A1011 6.035 -49.979 14.750 1.00 64.36 C ANISOU 1757 C ASN A1011 5837 5301 13316 1319 2758 535 C ATOM 1758 O ASN A1011 6.634 -50.934 14.251 1.00 61.19 O ANISOU 1758 O ASN A1011 5437 4870 12943 1330 2972 646 O ATOM 1759 CB ASN A1011 4.319 -48.908 13.285 1.00 63.24 C ANISOU 1759 CB ASN A1011 6078 5218 12732 1569 2629 226 C ATOM 1760 CG ASN A1011 2.875 -48.898 12.829 1.00 67.16 C ANISOU 1760 CG ASN A1011 6810 5862 12846 1748 2401 -94 C ATOM 1761 OD1 ASN A1011 2.174 -49.905 12.932 1.00 66.68 O ANISOU 1761 OD1 ASN A1011 6768 5923 12646 1750 2316 -274 O ATOM 1762 ND2 ASN A1011 2.419 -47.757 12.324 1.00 72.14 N ANISOU 1762 ND2 ASN A1011 7618 6457 13334 1917 2307 -171 N ATOM 1763 N ASP A1012 6.637 -49.068 15.508 1.00 60.86 N ANISOU 1763 N ASP A1012 5200 4776 13147 1246 2667 617 N ATOM 1764 CA ASP A1012 8.066 -49.145 15.793 1.00 63.16 C ANISOU 1764 CA ASP A1012 5239 4940 13819 1179 2804 827 C ATOM 1765 C ASP A1012 8.400 -50.370 16.636 1.00 63.25 C ANISOU 1765 C ASP A1012 5206 5089 13739 1212 2743 843 C ATOM 1766 O ASP A1012 9.337 -51.107 16.330 1.00 64.42 O ANISOU 1766 O ASP A1012 5284 5186 14008 1224 2944 998 O ATOM 1767 CB ASP A1012 8.545 -47.877 16.501 1.00 68.84 C ANISOU 1767 CB ASP A1012 5714 5535 14906 1110 2640 824 C ATOM 1768 CG ASP A1012 8.556 -46.670 15.587 1.00 73.42 C ANISOU 1768 CG ASP A1012 6297 5885 15714 1076 2823 897 C ATOM 1769 OD1 ASP A1012 8.736 -46.854 14.365 1.00 78.43 O ANISOU 1769 OD1 ASP A1012 7062 6426 16311 1128 3176 1051 O ATOM 1770 OD2 ASP A1012 8.383 -45.539 16.089 1.00 70.99 O ANISOU 1770 OD2 ASP A1012 5884 5486 15604 1034 2628 806 O ATOM 1771 N ASN A1013 7.628 -50.584 17.696 1.00 61.00 N ANISOU 1771 N ASN A1013 4978 4974 13224 1262 2494 697 N ATOM 1772 CA ASN A1013 7.867 -51.707 18.594 1.00 64.11 C ANISOU 1772 CA ASN A1013 5359 5499 13502 1355 2472 733 C ATOM 1773 C ASN A1013 7.601 -53.057 17.935 1.00 63.71 C ANISOU 1773 C ASN A1013 5467 5433 13307 1350 2702 774 C ATOM 1774 O ASN A1013 8.142 -54.075 18.362 1.00 62.37 O ANISOU 1774 O ASN A1013 5272 5297 13130 1425 2793 874 O ATOM 1775 CB ASN A1013 7.017 -51.565 19.855 1.00 61.97 C ANISOU 1775 CB ASN A1013 5141 5396 13008 1458 2216 597 C ATOM 1776 CG ASN A1013 7.676 -50.692 20.904 1.00 63.02 C ANISOU 1776 CG ASN A1013 5071 5603 13271 1567 1956 562 C ATOM 1777 OD1 ASN A1013 8.893 -50.733 21.085 1.00 68.56 O ANISOU 1777 OD1 ASN A1013 5554 6293 14202 1616 1960 643 O ATOM 1778 ND2 ASN A1013 6.874 -49.898 21.604 1.00 63.16 N ANISOU 1778 ND2 ASN A1013 5141 5706 13150 1630 1707 413 N ATOM 1779 N LEU A1014 6.771 -53.063 16.897 1.00 64.01 N ANISOU 1779 N LEU A1014 5661 5426 13233 1298 2778 669 N ATOM 1780 CA LEU A1014 6.544 -54.276 16.117 1.00 63.59 C ANISOU 1780 CA LEU A1014 5727 5337 13097 1305 2973 653 C ATOM 1781 C LEU A1014 7.812 -54.675 15.370 1.00 64.21 C ANISOU 1781 C LEU A1014 5747 5320 13329 1332 3211 848 C ATOM 1782 O LEU A1014 8.136 -55.858 15.267 1.00 65.52 O ANISOU 1782 O LEU A1014 5939 5454 13502 1364 3368 915 O ATOM 1783 CB LEU A1014 5.390 -54.084 15.132 1.00 63.92 C ANISOU 1783 CB LEU A1014 5915 5389 12982 1316 2942 428 C ATOM 1784 CG LEU A1014 3.980 -54.219 15.706 1.00 67.58 C ANISOU 1784 CG LEU A1014 6421 5893 13362 1284 2802 218 C ATOM 1785 CD1 LEU A1014 2.936 -53.906 14.645 1.00 67.17 C ANISOU 1785 CD1 LEU A1014 6487 5885 13148 1357 2714 -53 C ATOM 1786 CD2 LEU A1014 3.770 -55.616 16.272 1.00 72.08 C ANISOU 1786 CD2 LEU A1014 6967 6375 14045 1235 2969 257 C ATOM 1787 N LYS A1015 8.525 -53.680 14.853 1.00 63.32 N ANISOU 1787 N LYS A1015 5545 5124 13390 1320 3279 956 N ATOM 1788 CA LYS A1015 9.782 -53.917 14.152 1.00 69.57 C ANISOU 1788 CA LYS A1015 6255 5800 14378 1351 3545 1173 C ATOM 1789 C LYS A1015 10.859 -54.394 15.120 1.00 70.27 C ANISOU 1789 C LYS A1015 6146 5915 14640 1374 3517 1303 C ATOM 1790 O LYS A1015 11.718 -55.199 14.761 1.00 72.95 O ANISOU 1790 O LYS A1015 6452 6219 15046 1437 3708 1440 O ATOM 1791 CB LYS A1015 10.246 -52.648 13.433 1.00 73.44 C ANISOU 1791 CB LYS A1015 6674 6139 15089 1330 3688 1291 C ATOM 1792 CG LYS A1015 9.289 -52.147 12.363 1.00 74.52 C ANISOU 1792 CG LYS A1015 7037 6284 14994 1410 3744 1174 C ATOM 1793 CD LYS A1015 9.819 -50.879 11.707 1.00 82.11 C ANISOU 1793 CD LYS A1015 7948 7052 16198 1421 3976 1360 C ATOM 1794 CE LYS A1015 8.884 -50.384 10.614 1.00 85.39 C ANISOU 1794 CE LYS A1015 8653 7505 16288 1606 4032 1244 C ATOM 1795 NZ LYS A1015 8.733 -51.380 9.518 1.00 88.53 N ANISOU 1795 NZ LYS A1015 9276 7987 16376 1812 4175 1185 N ATOM 1796 N VAL A1016 10.804 -53.888 16.348 1.00 66.71 N ANISOU 1796 N VAL A1016 5561 5556 14228 1374 3259 1236 N ATOM 1797 CA VAL A1016 11.751 -54.271 17.389 1.00 69.79 C ANISOU 1797 CA VAL A1016 5749 6053 14715 1484 3162 1293 C ATOM 1798 C VAL A1016 11.615 -55.752 17.742 1.00 70.98 C ANISOU 1798 C VAL A1016 6032 6299 14640 1601 3240 1323 C ATOM 1799 O VAL A1016 12.612 -56.465 17.864 1.00 70.55 O ANISOU 1799 O VAL A1016 5869 6278 14657 1716 3338 1437 O ATOM 1800 CB VAL A1016 11.554 -53.422 18.662 1.00 68.26 C ANISOU 1800 CB VAL A1016 5415 5991 14530 1537 2828 1158 C ATOM 1801 CG1 VAL A1016 12.443 -53.924 19.787 1.00 70.63 C ANISOU 1801 CG1 VAL A1016 5518 6485 14832 1756 2690 1163 C ATOM 1802 CG2 VAL A1016 11.831 -51.956 18.370 1.00 69.23 C ANISOU 1802 CG2 VAL A1016 5357 5962 14987 1409 2761 1131 C ATOM 1803 N ILE A1017 10.375 -56.205 17.896 1.00 66.17 N ANISOU 1803 N ILE A1017 5634 5705 13801 1573 3219 1221 N ATOM 1804 CA ILE A1017 10.094 -57.591 18.255 1.00 71.04 C ANISOU 1804 CA ILE A1017 6356 6286 14350 1647 3388 1290 C ATOM 1805 C ILE A1017 10.557 -58.563 17.171 1.00 70.69 C ANISOU 1805 C ILE A1017 6377 6108 14375 1633 3669 1386 C ATOM 1806 O ILE A1017 11.117 -59.619 17.469 1.00 70.18 O ANISOU 1806 O ILE A1017 6304 6026 14336 1750 3821 1516 O ATOM 1807 CB ILE A1017 8.588 -57.798 18.523 1.00 65.29 C ANISOU 1807 CB ILE A1017 5786 5513 13509 1571 3380 1164 C ATOM 1808 CG1 ILE A1017 8.145 -56.944 19.711 1.00 64.38 C ANISOU 1808 CG1 ILE A1017 5625 5548 13290 1642 3118 1085 C ATOM 1809 CG2 ILE A1017 8.278 -59.265 18.784 1.00 66.71 C ANISOU 1809 CG2 ILE A1017 6065 5577 13706 1613 3632 1252 C ATOM 1810 CD1 ILE A1017 6.652 -56.921 19.926 1.00 62.89 C ANISOU 1810 CD1 ILE A1017 5562 5320 13012 1560 3100 948 C ATOM 1811 N GLU A1018 10.331 -58.195 15.913 1.00 68.70 N ANISOU 1811 N GLU A1018 6199 5780 14123 1539 3736 1316 N ATOM 1812 CA GLU A1018 10.716 -59.037 14.785 1.00 73.88 C ANISOU 1812 CA GLU A1018 6932 6338 14800 1574 3984 1369 C ATOM 1813 C GLU A1018 12.226 -59.223 14.697 1.00 77.80 C ANISOU 1813 C GLU A1018 7286 6848 15427 1677 4100 1572 C ATOM 1814 O GLU A1018 12.708 -60.293 14.326 1.00 79.74 O ANISOU 1814 O GLU A1018 7570 7036 15693 1763 4303 1663 O ATOM 1815 CB GLU A1018 10.194 -58.445 13.476 1.00 76.60 C ANISOU 1815 CB GLU A1018 7388 6666 15051 1545 4006 1233 C ATOM 1816 CG GLU A1018 8.683 -58.425 13.363 1.00 82.39 C ANISOU 1816 CG GLU A1018 8240 7409 15656 1488 3888 971 C ATOM 1817 CD GLU A1018 8.205 -57.780 12.079 1.00 90.39 C ANISOU 1817 CD GLU A1018 9366 8469 16510 1560 3866 803 C ATOM 1818 OE1 GLU A1018 9.058 -57.339 11.280 1.00 95.18 O ANISOU 1818 OE1 GLU A1018 9978 9064 17122 1646 4005 942 O ATOM 1819 OE2 GLU A1018 6.976 -57.714 11.868 1.00 90.11 O ANISOU 1819 OE2 GLU A1018 9410 8471 16357 1564 3731 536 O ATOM 1820 N LYS A1019 12.969 -58.177 15.042 1.00 77.02 N ANISOU 1820 N LYS A1019 6995 6813 15457 1672 3976 1625 N ATOM 1821 CA LYS A1019 14.422 -58.206 14.934 1.00 79.27 C ANISOU 1821 CA LYS A1019 7066 7093 15961 1759 4093 1793 C ATOM 1822 C LYS A1019 15.093 -58.452 16.282 1.00 80.64 C ANISOU 1822 C LYS A1019 7026 7440 16172 1897 3915 1798 C ATOM 1823 O LYS A1019 16.301 -58.263 16.426 1.00 81.60 O ANISOU 1823 O LYS A1019 6876 7615 16512 1981 3922 1868 O ATOM 1824 CB LYS A1019 14.931 -56.900 14.321 1.00 80.90 C ANISOU 1824 CB LYS A1019 7123 7180 16435 1673 4157 1862 C ATOM 1825 CG LYS A1019 14.446 -56.668 12.900 1.00 83.61 C ANISOU 1825 CG LYS A1019 7682 7383 16702 1640 4389 1892 C ATOM 1826 CD LYS A1019 15.091 -55.443 12.279 1.00 89.98 C ANISOU 1826 CD LYS A1019 8351 8014 17822 1595 4565 2042 C ATOM 1827 CE LYS A1019 14.696 -55.302 10.818 1.00 92.26 C ANISOU 1827 CE LYS A1019 8890 8202 17962 1665 4857 2107 C ATOM 1828 NZ LYS A1019 15.052 -56.519 10.034 1.00 94.02 N ANISOU 1828 NZ LYS A1019 9246 8463 18014 1819 5069 2165 N ATOM 1829 N ALA A1020 14.306 -58.875 17.265 1.00 74.99 N ANISOU 1829 N ALA A1020 6415 6817 15261 1955 3776 1719 N ATOM 1830 CA ALA A1020 14.845 -59.213 18.576 1.00 86.42 C ANISOU 1830 CA ALA A1020 7707 8461 16669 2186 3626 1721 C ATOM 1831 C ALA A1020 15.584 -60.546 18.515 1.00 86.93 C ANISOU 1831 C ALA A1020 7780 8523 16728 2367 3846 1868 C ATOM 1832 O ALA A1020 15.378 -61.335 17.593 1.00 81.91 O ANISOU 1832 O ALA A1020 7324 7708 16090 2290 4112 1957 O ATOM 1833 CB ALA A1020 13.735 -59.262 19.614 1.00 75.28 C ANISOU 1833 CB ALA A1020 6437 7109 15058 2237 3491 1644 C ATOM 1834 N ASP A1021 16.447 -60.794 19.496 1.00 94.30 N ANISOU 1834 N ASP A1021 8512 9672 17645 2647 3713 1863 N ATOM 1835 CA ASP A1021 17.218 -62.032 19.529 1.00106.37 C ANISOU 1835 CA ASP A1021 10036 11225 19156 2871 3904 1998 C ATOM 1836 C ASP A1021 16.976 -62.813 20.818 1.00108.29 C ANISOU 1836 C ASP A1021 10376 11586 19185 3182 3860 2026 C ATOM 1837 O ASP A1021 17.234 -64.015 20.881 1.00110.42 O ANISOU 1837 O ASP A1021 10760 11800 19396 3356 4088 2176 O ATOM 1838 CB ASP A1021 18.712 -61.740 19.364 1.00116.74 C ANISOU 1838 CB ASP A1021 10987 12703 20666 3000 3828 1967 C ATOM 1839 CG ASP A1021 19.286 -60.953 20.525 1.00125.28 C ANISOU 1839 CG ASP A1021 11738 14094 21768 3229 3435 1759 C ATOM 1840 OD1 ASP A1021 18.549 -60.134 21.113 1.00125.99 O ANISOU 1840 OD1 ASP A1021 11860 14229 21781 3176 3205 1631 O ATOM 1841 OD2 ASP A1021 20.475 -61.154 20.850 1.00132.15 O ANISOU 1841 OD2 ASP A1021 12300 15175 22736 3492 3340 1698 O ATOM 1842 N ASN A1022 16.480 -62.126 21.843 1.00 77.89 N ANISOU 1842 N ASN A1022 7368 10203 12023 2153 2047 4427 N ATOM 1843 CA ASN A1022 16.167 -62.774 23.112 1.00 76.13 C ANISOU 1843 CA ASN A1022 7237 10316 11372 2425 2028 4203 C ATOM 1844 C ASN A1022 14.771 -62.412 23.610 1.00 71.12 C ANISOU 1844 C ASN A1022 6681 9421 10921 2302 1762 3579 C ATOM 1845 O ASN A1022 14.156 -61.460 23.129 1.00 68.66 O ANISOU 1845 O ASN A1022 6224 8719 11146 1985 1452 3302 O ATOM 1846 CB ASN A1022 17.212 -62.414 24.171 1.00 79.85 C ANISOU 1846 CB ASN A1022 7072 11395 11873 2493 1644 4219 C ATOM 1847 CG ASN A1022 17.354 -60.919 24.366 1.00 81.84 C ANISOU 1847 CG ASN A1022 6644 11613 12837 2050 973 3859 C ATOM 1848 OD1 ASN A1022 16.588 -60.303 25.105 1.00 80.32 O ANISOU 1848 OD1 ASN A1022 6261 11393 12864 1872 563 3279 O ATOM 1849 ND2 ASN A1022 18.341 -60.327 23.705 1.00 85.41 N ANISOU 1849 ND2 ASN A1022 6761 12050 13640 1854 899 4203 N ATOM 1850 N ALA A1023 14.280 -63.178 24.580 1.00 69.92 N ANISOU 1850 N ALA A1023 6771 9493 10302 2570 1935 3363 N ATOM 1851 CA ALA A1023 12.927 -63.001 25.095 1.00 66.50 C ANISOU 1851 CA ALA A1023 6542 8845 9879 2373 1785 2701 C ATOM 1852 C ALA A1023 12.775 -61.701 25.879 1.00 67.57 C ANISOU 1852 C ALA A1023 6113 9094 10465 2043 1081 2136 C ATOM 1853 O ALA A1023 11.678 -61.150 25.969 1.00 65.34 O ANISOU 1853 O ALA A1023 5937 8515 10375 1758 853 1593 O ATOM 1854 CB ALA A1023 12.539 -64.186 25.965 1.00 65.77 C ANISOU 1854 CB ALA A1023 6929 8959 9102 2702 2216 2616 C ATOM 1855 N ALA A1024 13.876 -61.218 26.446 1.00 68.76 N ANISOU 1855 N ALA A1024 5672 9688 10764 2083 745 2266 N ATOM 1856 CA ALA A1024 13.849 -59.991 27.235 1.00 69.24 C ANISOU 1856 CA ALA A1024 5247 9848 11212 1746 72 1722 C ATOM 1857 C ALA A1024 13.537 -58.783 26.358 1.00 66.04 C ANISOU 1857 C ALA A1024 4699 8906 11488 1288 -232 1560 C ATOM 1858 O ALA A1024 12.761 -57.910 26.747 1.00 66.49 O ANISOU 1858 O ALA A1024 4745 8727 11790 1013 -607 974 O ATOM 1859 CB ALA A1024 15.172 -59.797 27.960 1.00 75.73 C ANISOU 1859 CB ALA A1024 5448 11305 12021 1843 -230 1919 C ATOM 1860 N GLN A1025 14.142 -58.742 25.174 1.00 63.25 N ANISOU 1860 N GLN A1025 4277 8346 11408 1264 -26 2108 N ATOM 1861 CA GLN A1025 13.914 -57.652 24.231 1.00 59.69 C ANISOU 1861 CA GLN A1025 3751 7358 11572 905 -225 2051 C ATOM 1862 C GLN A1025 12.475 -57.644 23.731 1.00 54.04 C ANISOU 1862 C GLN A1025 3562 6156 10816 850 -122 1704 C ATOM 1863 O GLN A1025 11.884 -56.584 23.531 1.00 53.44 O ANISOU 1863 O GLN A1025 3444 5711 11151 578 -436 1340 O ATOM 1864 CB GLN A1025 14.876 -57.753 23.047 1.00 61.58 C ANISOU 1864 CB GLN A1025 3954 7484 11959 948 75 2742 C ATOM 1865 CG GLN A1025 16.331 -57.511 23.408 1.00 71.11 C ANISOU 1865 CG GLN A1025 4677 9139 13203 872 -71 3010 C ATOM 1866 CD GLN A1025 17.244 -57.558 22.201 1.00 78.58 C ANISOU 1866 CD GLN A1025 5648 9924 14283 896 264 3677 C ATOM 1867 OE1 GLN A1025 16.803 -57.830 21.085 1.00 78.54 O ANISOU 1867 OE1 GLN A1025 6072 9484 14285 990 626 3948 O ATOM 1868 NE2 GLN A1025 18.527 -57.291 22.419 1.00 85.96 N ANISOU 1868 NE2 GLN A1025 6122 11234 15305 808 148 3930 N ATOM 1869 N VAL A1026 11.920 -58.834 23.525 1.00 54.03 N ANISOU 1869 N VAL A1026 4059 6166 10304 1109 332 1827 N ATOM 1870 CA VAL A1026 10.529 -58.969 23.115 1.00 50.45 C ANISOU 1870 CA VAL A1026 4051 5365 9751 1032 430 1486 C ATOM 1871 C VAL A1026 9.611 -58.446 24.211 1.00 51.63 C ANISOU 1871 C VAL A1026 4114 5590 9913 898 85 787 C ATOM 1872 O VAL A1026 8.627 -57.759 23.936 1.00 56.41 O ANISOU 1872 O VAL A1026 4782 5898 10754 731 -110 420 O ATOM 1873 CB VAL A1026 10.171 -60.434 22.796 1.00 50.60 C ANISOU 1873 CB VAL A1026 4639 5404 9183 1267 1007 1724 C ATOM 1874 CG1 VAL A1026 8.711 -60.552 22.384 1.00 41.81 C ANISOU 1874 CG1 VAL A1026 3899 3999 7989 1103 1056 1333 C ATOM 1875 CG2 VAL A1026 11.084 -60.979 21.707 1.00 48.66 C ANISOU 1875 CG2 VAL A1026 4567 5054 8867 1466 1395 2437 C ATOM 1876 N LYS A1027 9.951 -58.764 25.457 1.00 54.99 N ANISOU 1876 N LYS A1027 4403 6437 10054 1028 23 629 N ATOM 1877 CA LYS A1027 9.149 -58.356 26.606 1.00 60.35 C ANISOU 1877 CA LYS A1027 5049 7217 10666 973 -254 -7 C ATOM 1878 C LYS A1027 9.079 -56.838 26.752 1.00 63.75 C ANISOU 1878 C LYS A1027 5163 7423 11635 694 -805 -385 C ATOM 1879 O LYS A1027 7.997 -56.276 26.912 1.00 61.44 O ANISOU 1879 O LYS A1027 4984 6909 11452 610 -954 -844 O ATOM 1880 CB LYS A1027 9.705 -58.972 27.892 1.00 63.12 C ANISOU 1880 CB LYS A1027 5329 8084 10571 1227 -220 -43 C ATOM 1881 CG LYS A1027 8.957 -58.552 29.147 1.00 63.36 C ANISOU 1881 CG LYS A1027 5361 8227 10485 1225 -491 -683 C ATOM 1882 CD LYS A1027 9.605 -59.122 30.396 1.00 66.37 C ANISOU 1882 CD LYS A1027 5681 9145 10390 1529 -483 -690 C ATOM 1883 CE LYS A1027 8.848 -58.711 31.647 1.00 70.20 C ANISOU 1883 CE LYS A1027 6236 9719 10719 1574 -725 -1322 C ATOM 1884 NZ LYS A1027 9.460 -59.285 32.877 1.00 75.51 N ANISOU 1884 NZ LYS A1027 6894 10934 10861 1932 -718 -1330 N ATOM 1885 N ASP A1028 10.236 -56.184 26.697 1.00 69.96 N ANISOU 1885 N ASP A1028 5562 8269 12751 550 -1076 -181 N ATOM 1886 CA ASP A1028 10.311 -54.733 26.852 1.00 75.78 C ANISOU 1886 CA ASP A1028 6050 8739 14003 232 -1566 -528 C ATOM 1887 C ASP A1028 9.495 -53.999 25.793 1.00 69.49 C ANISOU 1887 C ASP A1028 5449 7368 13587 108 -1554 -587 C ATOM 1888 O ASP A1028 8.832 -53.005 26.089 1.00 73.36 O ANISOU 1888 O ASP A1028 5985 7582 14306 -15 -1837 -1051 O ATOM 1889 CB ASP A1028 11.766 -54.261 26.799 1.00 88.49 C ANISOU 1889 CB ASP A1028 7186 10506 15929 26 -1789 -219 C ATOM 1890 CG ASP A1028 12.504 -54.498 28.101 1.00 99.59 C ANISOU 1890 CG ASP A1028 8295 12508 17037 82 -2040 -370 C ATOM 1891 OD1 ASP A1028 12.418 -53.633 28.998 1.00105.56 O ANISOU 1891 OD1 ASP A1028 8942 13263 17904 -130 -2496 -906 O ATOM 1892 OD2 ASP A1028 13.173 -55.545 28.227 1.00101.90 O ANISOU 1892 OD2 ASP A1028 8497 13272 16948 372 -1777 50 O ATOM 1893 N ALA A1029 9.547 -54.491 24.561 1.00 62.92 N ANISOU 1893 N ALA A1029 4767 6360 12779 190 -1214 -103 N ATOM 1894 CA ALA A1029 8.815 -53.867 23.467 1.00 58.03 C ANISOU 1894 CA ALA A1029 4345 5247 12456 144 -1191 -100 C ATOM 1895 C ALA A1029 7.312 -54.069 23.634 1.00 52.53 C ANISOU 1895 C ALA A1029 3930 4519 11510 263 -1147 -524 C ATOM 1896 O ALA A1029 6.521 -53.185 23.310 1.00 53.16 O ANISOU 1896 O ALA A1029 4078 4284 11837 238 -1313 -782 O ATOM 1897 CB ALA A1029 9.282 -54.418 22.131 1.00 49.92 C ANISOU 1897 CB ALA A1029 3450 4077 11440 241 -835 529 C ATOM 1898 N LEU A1030 6.926 -55.233 24.146 1.00 47.05 N ANISOU 1898 N LEU A1030 3392 4163 10321 406 -894 -575 N ATOM 1899 CA LEU A1030 5.517 -55.550 24.359 1.00 47.22 C ANISOU 1899 CA LEU A1030 3621 4225 10096 475 -802 -955 C ATOM 1900 C LEU A1030 4.915 -54.742 25.505 1.00 49.73 C ANISOU 1900 C LEU A1030 3823 4587 10485 473 -1113 -1534 C ATOM 1901 O LEU A1030 3.743 -54.366 25.458 1.00 47.02 O ANISOU 1901 O LEU A1030 3545 4146 10176 518 -1163 -1855 O ATOM 1902 CB LEU A1030 5.343 -57.045 24.630 1.00 46.47 C ANISOU 1902 CB LEU A1030 3765 4431 9459 585 -379 -835 C ATOM 1903 CG LEU A1030 5.455 -57.997 23.440 1.00 45.40 C ANISOU 1903 CG LEU A1030 3926 4194 9129 608 11 -370 C ATOM 1904 CD1 LEU A1030 5.584 -59.428 23.929 1.00 45.70 C ANISOU 1904 CD1 LEU A1030 4247 4497 8620 725 460 -229 C ATOM 1905 CD2 LEU A1030 4.251 -57.851 22.523 1.00 43.54 C ANISOU 1905 CD2 LEU A1030 3840 3752 8950 524 7 -525 C ATOM 1906 N ATHR A1031 5.714 -54.481 26.536 0.52 53.29 N ANISOU 1906 N ATHR A1031 4105 5214 10929 447 -1322 -1659 N ATOM 1907 N BTHR A1031 5.722 -54.487 26.531 0.48 53.29 N ANISOU 1907 N BTHR A1031 4104 5214 10928 447 -1320 -1655 N ATOM 1908 CA ATHR A1031 5.252 -53.697 27.678 0.52 56.95 C ANISOU 1908 CA ATHR A1031 4531 5692 11414 462 -1623 -2214 C ATOM 1909 CA BTHR A1031 5.291 -53.701 27.680 0.48 57.18 C ANISOU 1909 CA BTHR A1031 4556 5725 11445 459 -1626 -2206 C ATOM 1910 C ATHR A1031 4.957 -52.259 27.269 0.52 59.67 C ANISOU 1910 C ATHR A1031 4857 5580 12235 350 -1925 -2421 C ATOM 1911 C BTHR A1031 4.957 -52.274 27.259 0.48 59.62 C ANISOU 1911 C BTHR A1031 4851 5576 12226 351 -1921 -2416 C ATOM 1912 O ATHR A1031 3.995 -51.654 27.743 0.52 61.10 O ANISOU 1912 O ATHR A1031 5140 5653 12422 454 -2036 -2849 O ATOM 1913 O BTHR A1031 3.967 -51.695 27.709 0.48 60.92 O ANISOU 1913 O BTHR A1031 5120 5636 12391 459 -2021 -2837 O ATOM 1914 CB ATHR A1031 6.282 -53.693 28.823 0.52 61.10 C ANISOU 1914 CB ATHR A1031 4892 6521 11801 439 -1841 -2308 C ATOM 1915 CB BTHR A1031 6.372 -53.673 28.780 0.48 61.37 C ANISOU 1915 CB BTHR A1031 4910 6550 11856 425 -1851 -2280 C ATOM 1916 OG1ATHR A1031 7.558 -53.276 28.322 0.52 65.06 O ANISOU 1916 OG1ATHR A1031 5138 6951 12632 226 -2013 -1967 O ATOM 1917 OG1BTHR A1031 6.695 -55.013 29.170 0.48 60.30 O ANISOU 1917 OG1BTHR A1031 4831 6845 11234 618 -1528 -2041 O ATOM 1918 CG2ATHR A1031 6.407 -55.080 29.435 0.52 60.18 C ANISOU 1918 CG2ATHR A1031 4871 6866 11128 667 -1508 -2165 C ATOM 1919 CG2BTHR A1031 5.885 -52.899 29.995 0.48 62.90 C ANISOU 1919 CG2BTHR A1031 5158 6742 12001 461 -2159 -2883 C ATOM 1920 N LYS A1032 5.790 -51.716 26.387 1.00 59.94 N ANISOU 1920 N LYS A1032 4787 5332 12657 172 -2009 -2090 N ATOM 1921 CA LYS A1032 5.575 -50.371 25.870 1.00 60.05 C ANISOU 1921 CA LYS A1032 4855 4837 13125 82 -2213 -2214 C ATOM 1922 C LYS A1032 4.353 -50.343 24.961 1.00 57.46 C ANISOU 1922 C LYS A1032 4710 4334 12788 296 -2040 -2193 C ATOM 1923 O LYS A1032 3.633 -49.347 24.902 1.00 60.52 O ANISOU 1923 O LYS A1032 5208 4551 13235 411 -2129 -2383 O ATOM 1924 CB LYS A1032 6.810 -49.876 25.118 1.00 60.09 C ANISOU 1924 CB LYS A1032 4722 4596 13513 -155 -2254 -1796 C ATOM 1925 CG LYS A1032 8.040 -49.705 25.994 1.00 63.61 C ANISOU 1925 CG LYS A1032 4962 5274 13933 -380 -2450 -1809 C ATOM 1926 CD LYS A1032 9.215 -49.169 25.195 1.00 67.89 C ANISOU 1926 CD LYS A1032 5355 5604 14838 -620 -2430 -1371 C ATOM 1927 CE LYS A1032 10.435 -48.969 26.078 1.00 76.23 C ANISOU 1927 CE LYS A1032 6156 6966 15842 -890 -2652 -1407 C ATOM 1928 NZ LYS A1032 11.597 -48.449 25.306 1.00 81.84 N ANISOU 1928 NZ LYS A1032 6669 7511 16914 -1157 -2603 -979 N ATOM 1929 N MET A1033 4.118 -51.445 24.255 1.00 51.73 N ANISOU 1929 N MET A1033 4027 3817 11812 383 -1745 -1876 N ATOM 1930 CA MET A1033 2.945 -51.553 23.398 1.00 55.34 C ANISOU 1930 CA MET A1033 4612 4221 12195 554 -1617 -1873 C ATOM 1931 C MET A1033 1.669 -51.618 24.224 1.00 55.39 C ANISOU 1931 C MET A1033 4619 4484 11942 697 -1628 -2336 C ATOM 1932 O MET A1033 0.680 -50.967 23.896 1.00 55.68 O ANISOU 1932 O MET A1033 4694 4525 11935 802 -1679 -2443 O ATOM 1933 CB MET A1033 3.043 -52.781 22.493 1.00 53.00 C ANISOU 1933 CB MET A1033 4413 4086 11640 549 -1305 -1460 C ATOM 1934 CG MET A1033 4.066 -52.647 21.386 1.00 54.95 C ANISOU 1934 CG MET A1033 4714 4100 12065 471 -1223 -926 C ATOM 1935 SD MET A1033 4.218 -54.136 20.381 1.00 64.14 S ANISOU 1935 SD MET A1033 6115 5409 12845 507 -821 -453 S ATOM 1936 CE MET A1033 2.620 -54.155 19.579 1.00 47.56 C ANISOU 1936 CE MET A1033 4175 3373 10521 590 -829 -660 C ATOM 1937 N ARG A1034 1.691 -52.402 25.297 1.00 54.96 N ANISOU 1937 N ARG A1034 4536 4758 11587 687 -1533 -2524 N ATOM 1938 CA ARG A1034 0.506 -52.571 26.129 1.00 54.15 C ANISOU 1938 CA ARG A1034 4427 4904 11242 838 -1471 -2935 C ATOM 1939 C ARG A1034 0.080 -51.249 26.765 1.00 55.53 C ANISOU 1939 C ARG A1034 4615 4939 11543 947 -1729 -3264 C ATOM 1940 O ARG A1034 -1.112 -50.968 26.889 1.00 55.39 O ANISOU 1940 O ARG A1034 4595 5067 11383 1093 -1690 -3434 O ATOM 1941 CB ARG A1034 0.750 -53.618 27.214 1.00 56.00 C ANISOU 1941 CB ARG A1034 4695 5500 11084 823 -1275 -3017 C ATOM 1942 CG ARG A1034 -0.529 -54.142 27.839 1.00 58.66 C ANISOU 1942 CG ARG A1034 5036 6123 11129 947 -1055 -3324 C ATOM 1943 CD ARG A1034 -0.250 -55.116 28.967 1.00 59.56 C ANISOU 1943 CD ARG A1034 5250 6539 10841 984 -818 -3393 C ATOM 1944 NE ARG A1034 -1.468 -55.801 29.389 1.00 63.65 N ANISOU 1944 NE ARG A1034 5785 7315 11085 1042 -496 -3598 N ATOM 1945 CZ ARG A1034 -2.358 -55.291 30.233 1.00 68.67 C ANISOU 1945 CZ ARG A1034 6406 8083 11601 1152 -546 -3849 C ATOM 1946 NH1 ARG A1034 -2.169 -54.085 30.751 1.00 71.24 N ANISOU 1946 NH1 ARG A1034 6731 8254 12083 1279 -889 -4034 N ATOM 1947 NH2 ARG A1034 -3.439 -55.987 30.558 1.00 72.46 N ANISOU 1947 NH2 ARG A1034 6888 8826 11817 1129 -225 -3905 N ATOM 1948 N ALA A1035 1.060 -50.442 27.158 1.00 57.43 N ANISOU 1948 N ALA A1035 4881 4929 12009 856 -1972 -3306 N ATOM 1949 CA ALA A1035 0.788 -49.135 27.747 1.00 59.59 C ANISOU 1949 CA ALA A1035 5261 5042 12337 938 -2172 -3549 C ATOM 1950 C ALA A1035 0.274 -48.157 26.694 1.00 65.22 C ANISOU 1950 C ALA A1035 6055 5490 13237 1012 -2185 -3378 C ATOM 1951 O ALA A1035 -0.611 -47.347 26.967 1.00 63.43 O ANISOU 1951 O ALA A1035 5950 5217 12933 1209 -2209 -3569 O ATOM 1952 CB ALA A1035 2.038 -48.584 28.418 1.00 62.39 C ANISOU 1952 CB ALA A1035 5647 5225 12833 747 -2410 -3628 C ATOM 1953 N ALA A1036 0.834 -48.239 25.492 1.00 61.89 N ANISOU 1953 N ALA A1036 5601 4893 13020 889 -2140 -2994 N ATOM 1954 CA ALA A1036 0.419 -47.377 24.390 1.00 64.64 C ANISOU 1954 CA ALA A1036 6073 5009 13480 985 -2114 -2786 C ATOM 1955 C ALA A1036 -0.977 -47.747 23.899 1.00 65.43 C ANISOU 1955 C ALA A1036 6152 5373 13334 1213 -1993 -2813 C ATOM 1956 O ALA A1036 -1.739 -46.885 23.458 1.00 67.33 O ANISOU 1956 O ALA A1036 6510 5512 13561 1436 -1997 -2815 O ATOM 1957 CB ALA A1036 1.420 -47.456 23.248 1.00 63.73 C ANISOU 1957 CB ALA A1036 5954 4689 13572 810 -2050 -2333 C ATOM 1958 N ALA A1037 -1.304 -49.034 23.976 1.00 61.25 N ANISOU 1958 N ALA A1037 5484 5184 12605 1169 -1866 -2834 N ATOM 1959 CA ALA A1037 -2.615 -49.522 23.561 1.00 55.96 C ANISOU 1959 CA ALA A1037 4730 4818 11715 1325 -1758 -2896 C ATOM 1960 C ALA A1037 -3.706 -49.016 24.495 1.00 60.32 C ANISOU 1960 C ALA A1037 5238 5552 12130 1556 -1778 -3250 C ATOM 1961 O ALA A1037 -4.772 -48.592 24.048 1.00 62.05 O ANISOU 1961 O ALA A1037 5413 5887 12275 1796 -1770 -3270 O ATOM 1962 CB ALA A1037 -2.626 -51.044 23.510 1.00 56.20 C ANISOU 1962 CB ALA A1037 4653 5131 11568 1175 -1566 -2858 C ATOM 1963 N LEU A1038 -3.434 -49.065 25.795 1.00 62.17 N ANISOU 1963 N LEU A1038 5488 5836 12299 1523 -1791 -3504 N ATOM 1964 CA LEU A1038 -4.393 -48.613 26.795 1.00 66.44 C ANISOU 1964 CA LEU A1038 6040 6537 12666 1761 -1767 -3808 C ATOM 1965 C LEU A1038 -4.484 -47.092 26.809 1.00 74.86 C ANISOU 1965 C LEU A1038 7326 7254 13863 1978 -1899 -3848 C ATOM 1966 O LEU A1038 -5.531 -46.527 27.124 1.00 79.47 O ANISOU 1966 O LEU A1038 7945 7931 14318 2288 -1840 -3982 O ATOM 1967 CB LEU A1038 -4.011 -49.134 28.181 1.00 66.05 C ANISOU 1967 CB LEU A1038 6017 6638 12440 1690 -1722 -4036 C ATOM 1968 CG LEU A1038 -3.993 -50.655 28.344 1.00 67.39 C ANISOU 1968 CG LEU A1038 6053 7150 12404 1525 -1493 -4005 C ATOM 1969 CD1 LEU A1038 -3.633 -51.040 29.772 1.00 67.83 C ANISOU 1969 CD1 LEU A1038 6202 7352 12218 1538 -1430 -4204 C ATOM 1970 CD2 LEU A1038 -5.330 -51.260 27.940 1.00 69.73 C ANISOU 1970 CD2 LEU A1038 6160 7786 12547 1585 -1282 -4022 C ATOM 1971 N ASP A1039 -3.381 -46.434 26.465 1.00 79.35 N ANISOU 1971 N ASP A1039 8057 7414 14679 1823 -2034 -3710 N ATOM 1972 CA ASP A1039 -3.348 -44.979 26.395 1.00 86.92 C ANISOU 1972 CA ASP A1039 9308 7954 15765 1979 -2100 -3725 C ATOM 1973 C ASP A1039 -4.141 -44.483 25.191 1.00 85.82 C ANISOU 1973 C ASP A1039 9209 7768 15631 2249 -2009 -3495 C ATOM 1974 O ASP A1039 -4.734 -43.405 25.226 1.00 89.80 O ANISOU 1974 O ASP A1039 9946 8074 16099 2569 -1958 -3542 O ATOM 1975 CB ASP A1039 -1.905 -44.475 26.326 1.00 92.91 C ANISOU 1975 CB ASP A1039 10204 8301 16795 1669 -2230 -3627 C ATOM 1976 CG ASP A1039 -1.816 -42.962 26.309 1.00106.27 C ANISOU 1976 CG ASP A1039 12278 9495 18605 1767 -2244 -3669 C ATOM 1977 OD1 ASP A1039 -1.791 -42.354 27.400 1.00112.38 O ANISOU 1977 OD1 ASP A1039 13281 10121 19298 1792 -2308 -3974 O ATOM 1978 OD2 ASP A1039 -1.768 -42.380 25.205 1.00110.89 O ANISOU 1978 OD2 ASP A1039 12992 9817 19326 1828 -2158 -3394 O ATOM 1979 N ALA A1040 -4.149 -45.278 24.125 1.00 81.83 N ANISOU 1979 N ALA A1040 8516 7446 15129 2155 -1969 -3235 N ATOM 1980 CA ALA A1040 -4.899 -44.937 22.922 1.00 81.68 C ANISOU 1980 CA ALA A1040 8517 7467 15052 2433 -1903 -3002 C ATOM 1981 C ALA A1040 -6.362 -45.339 23.067 1.00 86.81 C ANISOU 1981 C ALA A1040 8917 8612 15454 2723 -1842 -3147 C ATOM 1982 O ALA A1040 -7.231 -44.824 22.362 1.00 87.42 O ANISOU 1982 O ALA A1040 8983 8797 15437 3083 -1803 -3024 O ATOM 1983 CB ALA A1040 -4.282 -45.603 21.703 1.00 74.33 C ANISOU 1983 CB ALA A1040 7536 6526 14180 2223 -1888 -2659 C ATOM 1984 N GLN A1041 -6.625 -46.261 23.986 1.00 87.20 N ANISOU 1984 N GLN A1041 8751 8996 15385 2579 -1810 -3387 N ATOM 1985 CA GLN A1041 -7.981 -46.736 24.233 1.00 92.10 C ANISOU 1985 CA GLN A1041 9079 10134 15781 2780 -1710 -3528 C ATOM 1986 C GLN A1041 -8.797 -45.681 24.976 1.00 95.00 C ANISOU 1986 C GLN A1041 9547 10489 16058 3203 -1650 -3672 C ATOM 1987 O GLN A1041 -10.020 -45.626 24.851 1.00100.01 O ANISOU 1987 O GLN A1041 9950 11510 16538 3514 -1563 -3669 O ATOM 1988 CB GLN A1041 -7.951 -48.047 25.025 1.00 92.10 C ANISOU 1988 CB GLN A1041 8879 10451 15665 2481 -1609 -3713 C ATOM 1989 CG GLN A1041 -9.295 -48.749 25.132 1.00 95.59 C ANISOU 1989 CG GLN A1041 8961 11465 15893 2565 -1461 -3819 C ATOM 1990 CD GLN A1041 -9.186 -50.124 25.763 1.00 94.74 C ANISOU 1990 CD GLN A1041 8714 11618 15666 2226 -1285 -3956 C ATOM 1991 OE1 GLN A1041 -8.109 -50.541 26.189 1.00 91.93 O ANISOU 1991 OE1 GLN A1041 8539 11035 15355 1993 -1274 -3965 O ATOM 1992 NE2 GLN A1041 -10.305 -50.838 25.822 1.00 97.74 N ANISOU 1992 NE2 GLN A1041 8763 12494 15878 2198 -1118 -4040 N ATOM 1993 N LYS A1042 -8.110 -44.841 25.744 1.00 92.53 N ANISOU 1993 N LYS A1042 9581 9740 15835 3217 -1686 -3787 N ATOM 1994 CA LYS A1042 -8.765 -43.771 26.487 1.00 94.15 C ANISOU 1994 CA LYS A1042 10007 9823 15941 3634 -1592 -3920 C ATOM 1995 C LYS A1042 -9.199 -42.642 25.556 1.00 95.72 C ANISOU 1995 C LYS A1042 10390 9803 16176 4042 -1537 -3691 C ATOM 1996 O LYS A1042 -10.288 -42.087 25.701 1.00 97.68 O ANISOU 1996 O LYS A1042 10615 10223 16277 4516 -1390 -3680 O ATOM 1997 CB LYS A1042 -7.838 -43.225 27.575 1.00 96.86 C ANISOU 1997 CB LYS A1042 10727 9734 16340 3483 -1656 -4137 C ATOM 1998 CG LYS A1042 -7.424 -44.253 28.617 1.00 97.34 C ANISOU 1998 CG LYS A1042 10651 10033 16301 3177 -1686 -4347 C ATOM 1999 CD LYS A1042 -6.528 -43.634 29.678 1.00101.83 C ANISOU 1999 CD LYS A1042 11592 10219 16880 3059 -1792 -4565 C ATOM 2000 CE LYS A1042 -6.108 -44.661 30.719 1.00101.63 C ANISOU 2000 CE LYS A1042 11446 10475 16695 2827 -1810 -4739 C ATOM 2001 NZ LYS A1042 -5.243 -44.066 31.776 1.00105.18 N ANISOU 2001 NZ LYS A1042 12247 10614 17103 2723 -1955 -4966 N ATOM 2002 N MET A1058 -18.651 -47.727 19.627 1.00125.37 N ANISOU 2002 N MET A1058 11208 15846 20582 4640 -336 1367 N ATOM 2003 CA MET A1058 -17.959 -47.982 20.885 1.00124.51 C ANISOU 2003 CA MET A1058 11017 16013 20278 4544 130 1252 C ATOM 2004 C MET A1058 -17.901 -49.475 21.190 1.00119.62 C ANISOU 2004 C MET A1058 9993 15845 19614 3887 316 1716 C ATOM 2005 O MET A1058 -17.196 -49.906 22.103 1.00118.79 O ANISOU 2005 O MET A1058 9896 15943 19296 3694 660 1746 O ATOM 2006 CB MET A1058 -18.641 -47.237 22.034 1.00133.51 C ANISOU 2006 CB MET A1058 11725 17730 21271 5139 419 778 C ATOM 2007 CG MET A1058 -18.575 -45.723 21.916 1.00138.22 C ANISOU 2007 CG MET A1058 12787 17812 21918 5820 205 241 C ATOM 2008 SD MET A1058 -16.882 -45.103 21.902 1.00142.20 S ANISOU 2008 SD MET A1058 14306 17429 22293 5713 231 77 S ATOM 2009 CE MET A1058 -16.286 -45.710 23.478 1.00106.59 C ANISOU 2009 CE MET A1058 9464 13536 17499 5529 799 -114 C ATOM 2010 N LYS A1059 -18.647 -50.260 20.420 1.00117.05 N ANISOU 2010 N LYS A1059 9350 15656 19468 3541 52 2065 N ATOM 2011 CA LYS A1059 -18.673 -51.706 20.598 1.00111.44 C ANISOU 2011 CA LYS A1059 8317 15263 18762 2861 126 2518 C ATOM 2012 C LYS A1059 -17.650 -52.378 19.689 1.00106.24 C ANISOU 2012 C LYS A1059 8206 13938 18222 2370 -196 2743 C ATOM 2013 O LYS A1059 -16.963 -53.314 20.098 1.00102.10 O ANISOU 2013 O LYS A1059 7729 13427 17637 1917 -91 2975 O ATOM 2014 CB LYS A1059 -20.075 -52.252 20.326 1.00112.73 C ANISOU 2014 CB LYS A1059 7828 15942 19063 2703 6 2706 C ATOM 2015 CG LYS A1059 -21.145 -51.633 21.211 1.00117.64 C ANISOU 2015 CG LYS A1059 7837 17303 19558 3176 311 2420 C ATOM 2016 CD LYS A1059 -22.532 -52.129 20.849 1.00120.70 C ANISOU 2016 CD LYS A1059 7562 18179 20120 3015 164 2553 C ATOM 2017 CE LYS A1059 -23.586 -51.464 21.717 1.00126.87 C ANISOU 2017 CE LYS A1059 7700 19702 20803 3508 460 2183 C ATOM 2018 NZ LYS A1059 -24.958 -51.914 21.365 1.00133.68 N ANISOU 2018 NZ LYS A1059 7861 21063 21870 3355 322 2262 N ATOM 2019 N ASP A1060 -17.554 -51.893 18.456 1.00107.92 N ANISOU 2019 N ASP A1060 8851 13601 18552 2471 -604 2651 N ATOM 2020 CA ASP A1060 -16.538 -52.368 17.524 1.00106.57 C ANISOU 2020 CA ASP A1060 9263 12836 18392 2063 -907 2746 C ATOM 2021 C ASP A1060 -15.183 -51.788 17.909 1.00102.20 C ANISOU 2021 C ASP A1060 9292 11865 17676 2167 -724 2511 C ATOM 2022 O ASP A1060 -14.136 -52.376 17.633 1.00 98.88 O ANISOU 2022 O ASP A1060 9309 11146 17115 1748 -801 2518 O ATOM 2023 CB ASP A1060 -16.896 -51.984 16.088 1.00111.81 C ANISOU 2023 CB ASP A1060 10224 13161 19097 2126 -1351 2709 C ATOM 2024 CG ASP A1060 -18.293 -52.425 15.697 1.00120.37 C ANISOU 2024 CG ASP A1060 10723 14663 20348 2103 -1547 2856 C ATOM 2025 OD1 ASP A1060 -18.738 -53.489 16.176 1.00122.61 O ANISOU 2025 OD1 ASP A1060 10512 15340 20736 1724 -1454 3081 O ATOM 2026 OD2 ASP A1060 -18.947 -51.706 14.913 1.00124.62 O ANISOU 2026 OD2 ASP A1060 11319 15134 20898 2449 -1802 2750 O ATOM 2027 N PHE A1061 -15.220 -50.623 18.548 1.00104.13 N ANISOU 2027 N PHE A1061 9607 12114 17844 2691 -482 2197 N ATOM 2028 CA PHE A1061 -14.019 -49.957 19.037 1.00 96.64 C ANISOU 2028 CA PHE A1061 9251 10816 16652 2753 -274 1848 C ATOM 2029 C PHE A1061 -13.399 -50.726 20.197 1.00 86.87 C ANISOU 2029 C PHE A1061 7921 9953 15131 2469 77 1822 C ATOM 2030 O PHE A1061 -12.194 -50.981 20.213 1.00 80.88 O ANISOU 2030 O PHE A1061 7637 8910 14185 2160 91 1710 O ATOM 2031 CB PHE A1061 -14.348 -48.522 19.462 1.00102.99 C ANISOU 2031 CB PHE A1061 10114 11512 17506 3426 -162 1479 C ATOM 2032 CG PHE A1061 -13.410 -47.959 20.495 1.00103.73 C ANISOU 2032 CG PHE A1061 10534 11533 17347 3542 164 1058 C ATOM 2033 CD1 PHE A1061 -12.163 -47.480 20.133 1.00100.81 C ANISOU 2033 CD1 PHE A1061 10878 10528 16896 3339 88 860 C ATOM 2034 CD2 PHE A1061 -13.784 -47.895 21.829 1.00108.39 C ANISOU 2034 CD2 PHE A1061 10682 12745 17755 3849 547 841 C ATOM 2035 CE1 PHE A1061 -11.303 -46.958 21.082 1.00101.44 C ANISOU 2035 CE1 PHE A1061 11223 10550 16769 3429 350 429 C ATOM 2036 CE2 PHE A1061 -12.927 -47.375 22.781 1.00108.29 C ANISOU 2036 CE2 PHE A1061 10963 12697 17485 3983 807 403 C ATOM 2037 CZ PHE A1061 -11.686 -46.905 22.406 1.00104.29 C ANISOU 2037 CZ PHE A1061 11165 11508 16951 3771 690 183 C ATOM 2038 N ARG A1062 -14.231 -51.093 21.166 1.00 88.03 N ANISOU 2038 N ARG A1062 7435 10788 15223 2580 357 1936 N ATOM 2039 CA ARG A1062 -13.766 -51.809 22.346 1.00 88.44 C ANISOU 2039 CA ARG A1062 7376 11274 14955 2347 694 1984 C ATOM 2040 C ARG A1062 -13.288 -53.213 21.992 1.00 79.02 C ANISOU 2040 C ARG A1062 6283 9965 13777 1695 499 2364 C ATOM 2041 O ARG A1062 -12.278 -53.681 22.516 1.00 71.70 O ANISOU 2041 O ARG A1062 5670 8980 12594 1464 591 2309 O ATOM 2042 CB ARG A1062 -14.871 -51.874 23.404 1.00100.60 C ANISOU 2042 CB ARG A1062 8167 13665 16392 2593 1054 2084 C ATOM 2043 CG ARG A1062 -14.555 -52.788 24.578 1.00107.24 C ANISOU 2043 CG ARG A1062 8838 15041 16866 2278 1382 2300 C ATOM 2044 CD ARG A1062 -15.356 -52.411 25.814 1.00118.60 C ANISOU 2044 CD ARG A1062 9672 17364 18025 2677 1849 2202 C ATOM 2045 NE ARG A1062 -14.952 -51.112 26.345 1.00121.80 N ANISOU 2045 NE ARG A1062 10343 17705 18231 3305 2019 1550 N ATOM 2046 CZ ARG A1062 -13.934 -50.931 27.181 1.00119.87 C ANISOU 2046 CZ ARG A1062 10486 17465 17595 3362 2207 1241 C ATOM 2047 NH1 ARG A1062 -13.211 -51.967 27.585 1.00116.02 N ANISOU 2047 NH1 ARG A1062 10173 17059 16850 2867 2248 1548 N ATOM 2048 NH2 ARG A1062 -13.637 -49.713 27.613 1.00121.54 N ANISOU 2048 NH2 ARG A1062 10918 17573 17689 3931 2309 602 N ATOM 2049 N HIS A1063 -14.013 -53.876 21.096 1.00 75.82 N ANISOU 2049 N HIS A1063 5611 9510 13686 1433 185 2710 N ATOM 2050 CA HIS A1063 -13.657 -55.227 20.677 1.00 71.59 C ANISOU 2050 CA HIS A1063 5163 8798 13239 845 -81 3030 C ATOM 2051 C HIS A1063 -12.308 -55.244 19.968 1.00 64.88 C ANISOU 2051 C HIS A1063 5023 7334 12293 690 -317 2779 C ATOM 2052 O HIS A1063 -11.514 -56.164 20.155 1.00 56.81 O ANISOU 2052 O HIS A1063 4219 6200 11165 346 -392 2843 O ATOM 2053 CB HIS A1063 -14.736 -55.815 19.765 1.00 76.22 C ANISOU 2053 CB HIS A1063 5322 9421 14219 631 -429 3356 C ATOM 2054 CG HIS A1063 -14.500 -57.248 19.399 1.00 76.15 C ANISOU 2054 CG HIS A1063 5355 9217 14362 36 -742 3660 C ATOM 2055 ND1 HIS A1063 -14.463 -58.258 20.335 1.00 78.04 N ANISOU 2055 ND1 HIS A1063 5408 9713 14532 -332 -588 3987 N ATOM 2056 CD2 HIS A1063 -14.287 -57.839 18.199 1.00 74.41 C ANISOU 2056 CD2 HIS A1063 5365 8552 14356 -234 -1233 3672 C ATOM 2057 CE1 HIS A1063 -14.239 -59.410 19.729 1.00 76.77 C ANISOU 2057 CE1 HIS A1063 5381 9193 14596 -799 -1000 4180 C ATOM 2058 NE2 HIS A1063 -14.128 -59.184 18.432 1.00 75.23 N ANISOU 2058 NE2 HIS A1063 5423 8595 14565 -733 -1392 3952 N ATOM 2059 N GLY A1064 -12.054 -54.221 19.158 1.00 58.12 N ANISOU 2059 N GLY A1064 4515 6100 11467 950 -441 2504 N ATOM 2060 CA GLY A1064 -10.793 -54.102 18.450 1.00 53.56 C ANISOU 2060 CA GLY A1064 4560 5031 10761 793 -610 2260 C ATOM 2061 C GLY A1064 -9.614 -53.974 19.395 1.00 52.60 C ANISOU 2061 C GLY A1064 4744 4916 10324 784 -329 1967 C ATOM 2062 O GLY A1064 -8.566 -54.582 19.180 1.00 49.15 O ANISOU 2062 O GLY A1064 4621 4293 9761 499 -450 1862 O ATOM 2063 N PHE A1065 -9.787 -53.183 20.450 1.00 53.50 N ANISOU 2063 N PHE A1065 4742 5284 10303 1132 23 1786 N ATOM 2064 CA PHE A1065 -8.736 -53.003 21.444 1.00 55.74 C ANISOU 2064 CA PHE A1065 5271 5641 10266 1169 280 1465 C ATOM 2065 C PHE A1065 -8.673 -54.176 22.418 1.00 54.05 C ANISOU 2065 C PHE A1065 4817 5852 9868 959 395 1706 C ATOM 2066 O PHE A1065 -7.612 -54.474 22.965 1.00 50.89 O ANISOU 2066 O PHE A1065 4677 5450 9209 859 449 1517 O ATOM 2067 CB PHE A1065 -8.936 -51.692 22.207 1.00 59.24 C ANISOU 2067 CB PHE A1065 5699 6190 10618 1655 572 1111 C ATOM 2068 CG PHE A1065 -8.358 -50.494 21.509 1.00 60.78 C ANISOU 2068 CG PHE A1065 6376 5812 10904 1783 470 768 C ATOM 2069 CD1 PHE A1065 -9.125 -49.748 20.630 1.00 66.18 C ANISOU 2069 CD1 PHE A1065 7078 6203 11866 2000 287 857 C ATOM 2070 CD2 PHE A1065 -7.043 -50.117 21.730 1.00 58.09 C ANISOU 2070 CD2 PHE A1065 6470 5227 10375 1662 535 382 C ATOM 2071 CE1 PHE A1065 -8.591 -48.645 19.985 1.00 67.46 C ANISOU 2071 CE1 PHE A1065 7738 5785 12109 2071 174 627 C ATOM 2072 CE2 PHE A1065 -6.504 -49.017 21.090 1.00 59.54 C ANISOU 2072 CE2 PHE A1065 7097 4866 10661 1686 449 123 C ATOM 2073 CZ PHE A1065 -7.279 -48.279 20.216 1.00 62.70 C ANISOU 2073 CZ PHE A1065 7566 4924 11332 1877 270 278 C ATOM 2074 N ASP A1066 -9.806 -54.838 22.634 1.00 57.78 N ANISOU 2074 N ASP A1066 4790 6691 10473 879 416 2143 N ATOM 2075 CA ASP A1066 -9.830 -56.044 23.456 1.00 61.64 C ANISOU 2075 CA ASP A1066 5075 7523 10823 590 479 2510 C ATOM 2076 C ASP A1066 -8.983 -57.134 22.814 1.00 55.16 C ANISOU 2076 C ASP A1066 4592 6275 10091 181 94 2601 C ATOM 2077 O ASP A1066 -8.292 -57.885 23.501 1.00 57.43 O ANISOU 2077 O ASP A1066 5026 6627 10166 31 93 2671 O ATOM 2078 CB ASP A1066 -11.262 -56.543 23.664 1.00 72.12 C ANISOU 2078 CB ASP A1066 5765 9302 12335 482 555 3006 C ATOM 2079 CG ASP A1066 -12.000 -55.767 24.737 1.00 84.04 C ANISOU 2079 CG ASP A1066 6849 11471 13613 885 1019 2931 C ATOM 2080 OD1 ASP A1066 -11.332 -55.136 25.583 1.00 86.55 O ANISOU 2080 OD1 ASP A1066 7380 11941 13563 1184 1282 2562 O ATOM 2081 OD2 ASP A1066 -13.249 -55.794 24.737 1.00 92.58 O ANISOU 2081 OD2 ASP A1066 7347 12961 14870 916 1109 3200 O ATOM 2082 N ILE A1067 -9.042 -57.211 21.489 1.00 51.25 N ANISOU 2082 N ILE A1067 4222 5363 9888 47 -259 2575 N ATOM 2083 CA ILE A1067 -8.223 -58.155 20.741 1.00 52.49 C ANISOU 2083 CA ILE A1067 4696 5124 10125 -264 -654 2540 C ATOM 2084 C ILE A1067 -6.749 -57.776 20.846 1.00 46.78 C ANISOU 2084 C ILE A1067 4443 4225 9107 -172 -605 2058 C ATOM 2085 O ILE A1067 -5.892 -58.631 21.073 1.00 45.13 O ANISOU 2085 O ILE A1067 4427 3930 8792 -323 -764 2001 O ATOM 2086 CB ILE A1067 -8.638 -58.213 19.255 1.00 49.84 C ANISOU 2086 CB ILE A1067 4371 4472 10094 -377 -1031 2557 C ATOM 2087 CG1 ILE A1067 -10.061 -58.758 19.119 1.00 53.76 C ANISOU 2087 CG1 ILE A1067 4352 5149 10925 -529 -1154 3014 C ATOM 2088 CG2 ILE A1067 -7.680 -59.084 18.463 1.00 47.39 C ANISOU 2088 CG2 ILE A1067 4401 3832 9773 -613 -1420 2363 C ATOM 2089 CD1 ILE A1067 -10.610 -58.694 17.708 1.00 53.76 C ANISOU 2089 CD1 ILE A1067 4309 4920 11199 -571 -1533 3009 C ATOM 2090 N LEU A1068 -6.466 -56.486 20.700 1.00 43.62 N ANISOU 2090 N LEU A1068 4212 3764 8599 78 -406 1706 N ATOM 2091 CA LEU A1068 -5.095 -55.990 20.697 1.00 40.82 C ANISOU 2091 CA LEU A1068 4257 3247 8004 109 -352 1226 C ATOM 2092 C LEU A1068 -4.379 -56.251 22.019 1.00 41.03 C ANISOU 2092 C LEU A1068 4317 3547 7724 185 -158 1079 C ATOM 2093 O LEU A1068 -3.286 -56.814 22.037 1.00 41.95 O ANISOU 2093 O LEU A1068 4651 3588 7699 68 -308 863 O ATOM 2094 CB LEU A1068 -5.072 -54.493 20.386 1.00 41.64 C ANISOU 2094 CB LEU A1068 4527 3189 8105 324 -175 945 C ATOM 2095 CG LEU A1068 -3.681 -53.917 20.123 1.00 41.48 C ANISOU 2095 CG LEU A1068 4907 2952 7902 239 -148 474 C ATOM 2096 CD1 LEU A1068 -3.111 -54.496 18.838 1.00 40.66 C ANISOU 2096 CD1 LEU A1068 4983 2633 7833 -57 -459 455 C ATOM 2097 CD2 LEU A1068 -3.716 -52.398 20.068 1.00 40.44 C ANISOU 2097 CD2 LEU A1068 4954 2609 7801 434 38 242 C ATOM 2098 N VAL A1069 -4.999 -55.837 23.120 1.00 43.97 N ANISOU 2098 N VAL A1069 4454 4287 7965 420 159 1170 N ATOM 2099 CA VAL A1069 -4.413 -56.015 24.445 1.00 45.04 C ANISOU 2099 CA VAL A1069 4608 4770 7734 539 354 1046 C ATOM 2100 C VAL A1069 -4.243 -57.497 24.771 1.00 51.10 C ANISOU 2100 C VAL A1069 5349 5612 8454 299 135 1422 C ATOM 2101 O VAL A1069 -3.221 -57.908 25.321 1.00 44.67 O ANISOU 2101 O VAL A1069 4741 4846 7384 311 63 1229 O ATOM 2102 CB VAL A1069 -5.272 -55.341 25.535 1.00 51.24 C ANISOU 2102 CB VAL A1069 5088 6039 8343 860 742 1094 C ATOM 2103 CG1 VAL A1069 -4.675 -55.579 26.914 1.00 50.89 C ANISOU 2103 CG1 VAL A1069 5066 6430 7838 992 926 983 C ATOM 2104 CG2 VAL A1069 -5.400 -53.851 25.258 1.00 50.63 C ANISOU 2104 CG2 VAL A1069 5090 5791 8356 1157 893 670 C ATOM 2105 N GLY A1070 -5.246 -58.294 24.417 1.00 47.14 N ANISOU 2105 N GLY A1070 4597 5088 8225 80 -12 1951 N ATOM 2106 CA GLY A1070 -5.197 -59.727 24.635 1.00 48.43 C ANISOU 2106 CA GLY A1070 4766 5195 8441 -197 -285 2371 C ATOM 2107 C GLY A1070 -4.067 -60.391 23.871 1.00 47.53 C ANISOU 2107 C GLY A1070 5015 4631 8415 -319 -711 2090 C ATOM 2108 O GLY A1070 -3.370 -61.255 24.404 1.00 46.48 O ANISOU 2108 O GLY A1070 5055 4463 8141 -356 -901 2139 O ATOM 2109 N GLN A1071 -3.888 -59.986 22.618 1.00 42.29 N ANISOU 2109 N GLN A1071 4460 3655 7955 -355 -873 1791 N ATOM 2110 CA GLN A1071 -2.830 -60.539 21.779 1.00 39.70 C ANISOU 2110 CA GLN A1071 4418 2996 7672 -442 -1248 1447 C ATOM 2111 C GLN A1071 -1.452 -60.143 22.297 1.00 42.25 C ANISOU 2111 C GLN A1071 4975 3435 7644 -261 -1140 923 C ATOM 2112 O GLN A1071 -0.491 -60.901 22.169 1.00 37.30 O ANISOU 2112 O GLN A1071 4523 2686 6963 -271 -1439 689 O ATOM 2113 CB GLN A1071 -3.004 -60.086 20.327 1.00 37.82 C ANISOU 2113 CB GLN A1071 4216 2517 7637 -519 -1387 1267 C ATOM 2114 CG GLN A1071 -4.121 -60.807 19.586 1.00 49.44 C ANISOU 2114 CG GLN A1071 5467 3998 9320 -675 -1625 1582 C ATOM 2115 CD GLN A1071 -4.344 -60.265 18.187 1.00 43.65 C ANISOU 2115 CD GLN A1071 4755 3269 8561 -652 -1703 1359 C ATOM 2116 OE1 GLN A1071 -4.097 -59.090 17.916 1.00 43.83 O ANISOU 2116 OE1 GLN A1071 4897 3260 8495 -552 -1486 1166 O ATOM 2117 NE2 GLN A1071 -4.814 -61.123 17.288 1.00 40.59 N ANISOU 2117 NE2 GLN A1071 4272 2890 8260 -739 -2036 1413 N ATOM 2118 N ILE A1072 -1.361 -58.953 22.882 1.00 37.87 N ANISOU 2118 N ILE A1072 4402 3117 6870 -77 -744 696 N ATOM 2119 CA ILE A1072 -0.124 -58.504 23.509 1.00 37.04 C ANISOU 2119 CA ILE A1072 4464 3170 6438 78 -628 184 C ATOM 2120 C ILE A1072 0.159 -59.342 24.754 1.00 39.75 C ANISOU 2120 C ILE A1072 4808 3765 6532 189 -684 352 C ATOM 2121 O ILE A1072 1.296 -59.750 24.997 1.00 39.78 O ANISOU 2121 O ILE A1072 4967 3793 6353 263 -871 18 O ATOM 2122 CB ILE A1072 -0.186 -57.006 23.880 1.00 37.33 C ANISOU 2122 CB ILE A1072 4490 3344 6348 245 -230 -111 C ATOM 2123 CG1 ILE A1072 -0.253 -56.150 22.614 1.00 36.35 C ANISOU 2123 CG1 ILE A1072 4464 2907 6442 123 -226 -275 C ATOM 2124 CG2 ILE A1072 1.021 -56.603 24.711 1.00 40.92 C ANISOU 2124 CG2 ILE A1072 5070 4008 6471 389 -127 -638 C ATOM 2125 CD1 ILE A1072 -0.360 -54.663 22.879 1.00 36.75 C ANISOU 2125 CD1 ILE A1072 4565 2941 6457 277 90 -539 C ATOM 2126 N ASP A1073 -0.886 -59.612 25.531 1.00 42.28 N ANISOU 2126 N ASP A1073 4934 4307 6822 201 -531 888 N ATOM 2127 CA ASP A1073 -0.757 -60.426 26.735 1.00 47.17 C ANISOU 2127 CA ASP A1073 5567 5196 7158 271 -569 1190 C ATOM 2128 C ASP A1073 -0.333 -61.857 26.408 1.00 45.86 C ANISOU 2128 C ASP A1073 5577 4684 7163 114 -1079 1407 C ATOM 2129 O ASP A1073 0.431 -62.470 27.154 1.00 47.48 O ANISOU 2129 O ASP A1073 5952 4974 7116 242 -1259 1380 O ATOM 2130 CB ASP A1073 -2.071 -60.433 27.520 1.00 51.48 C ANISOU 2130 CB ASP A1073 5817 6110 7633 243 -265 1787 C ATOM 2131 CG ASP A1073 -2.410 -59.074 28.103 1.00 59.13 C ANISOU 2131 CG ASP A1073 6617 7492 8359 521 213 1496 C ATOM 2132 OD1 ASP A1073 -1.475 -58.286 28.362 1.00 59.16 O ANISOU 2132 OD1 ASP A1073 6787 7557 8133 743 301 889 O ATOM 2133 OD2 ASP A1073 -3.611 -58.793 28.304 1.00 62.83 O ANISOU 2133 OD2 ASP A1073 6765 8225 8884 525 479 1839 O ATOM 2134 N ASP A1074 -0.833 -62.386 25.294 1.00 44.95 N ANISOU 2134 N ASP A1074 5432 4166 7481 -129 -1352 1593 N ATOM 2135 CA ASP A1074 -0.452 -63.723 24.850 1.00 45.80 C ANISOU 2135 CA ASP A1074 5722 3856 7823 -251 -1901 1707 C ATOM 2136 C ASP A1074 1.035 -63.777 24.523 1.00 43.49 C ANISOU 2136 C ASP A1074 5661 3472 7391 -41 -2148 1015 C ATOM 2137 O ASP A1074 1.737 -64.705 24.926 1.00 45.38 O ANISOU 2137 O ASP A1074 6087 3591 7565 74 -2511 996 O ATOM 2138 CB ASP A1074 -1.272 -64.148 23.629 1.00 48.47 C ANISOU 2138 CB ASP A1074 5961 3809 8647 -527 -2156 1912 C ATOM 2139 CG ASP A1074 -2.744 -64.323 23.944 1.00 54.25 C ANISOU 2139 CG ASP A1074 6402 4638 9574 -778 -1994 2620 C ATOM 2140 OD1 ASP A1074 -3.089 -64.430 25.139 1.00 57.79 O ANISOU 2140 OD1 ASP A1074 6759 5415 9783 -778 -1752 3044 O ATOM 2141 OD2 ASP A1074 -3.555 -64.362 22.994 1.00 54.10 O ANISOU 2141 OD2 ASP A1074 6189 4562 9805 -945 -2052 2622 O ATOM 2142 N ALA A1075 1.509 -62.774 23.790 1.00 40.05 N ANISOU 2142 N ALA A1075 5200 3107 6910 4 -1961 460 N ATOM 2143 CA ALA A1075 2.917 -62.697 23.422 1.00 41.99 C ANISOU 2143 CA ALA A1075 5572 3378 7004 152 -2121 -236 C ATOM 2144 C ALA A1075 3.785 -62.446 24.651 1.00 43.79 C ANISOU 2144 C ALA A1075 5851 3959 6828 407 -1995 -495 C ATOM 2145 O ALA A1075 4.899 -62.962 24.750 1.00 44.74 O ANISOU 2145 O ALA A1075 6067 4106 6825 585 -2291 -897 O ATOM 2146 CB ALA A1075 3.135 -61.607 22.382 1.00 35.52 C ANISOU 2146 CB ALA A1075 4702 2586 6209 51 -1894 -664 C ATOM 2147 N ALEU A1076 3.263 -61.659 25.587 0.43 44.08 N ANISOU 2147 N ALEU A1076 5799 4301 6647 461 -1580 -305 N ATOM 2148 N BLEU A1076 3.271 -61.645 25.580 0.57 43.93 N ANISOU 2148 N BLEU A1076 5779 4283 6628 462 -1577 -312 N ATOM 2149 CA ALEU A1076 3.982 -61.333 26.813 0.43 41.92 C ANISOU 2149 CA ALEU A1076 5558 4425 5945 719 -1446 -563 C ATOM 2150 CA BLEU A1076 3.981 -61.339 26.818 0.57 41.94 C ANISOU 2150 CA BLEU A1076 5561 4428 5947 720 -1447 -560 C ATOM 2151 C ALEU A1076 4.180 -62.568 27.688 0.43 45.47 C ANISOU 2151 C ALEU A1076 6141 4900 6234 865 -1788 -203 C ATOM 2152 C BLEU A1076 4.194 -62.587 27.663 0.57 45.43 C ANISOU 2152 C BLEU A1076 6139 4885 6237 863 -1799 -208 C ATOM 2153 O ALEU A1076 5.225 -62.730 28.319 0.43 46.72 O ANISOU 2153 O ALEU A1076 6392 5265 6094 1119 -1951 -567 O ATOM 2154 O BLEU A1076 5.259 -62.775 28.251 0.57 46.62 O ANISOU 2154 O BLEU A1076 6384 5227 6102 1115 -1978 -580 O ATOM 2155 CB ALEU A1076 3.237 -60.248 27.594 0.43 42.89 C ANISOU 2155 CB ALEU A1076 5545 4882 5868 779 -944 -446 C ATOM 2156 CB BLEU A1076 3.220 -60.289 27.628 0.57 43.02 C ANISOU 2156 CB BLEU A1076 5562 4903 5879 782 -950 -424 C ATOM 2157 CG ALEU A1076 3.912 -59.724 28.863 0.43 47.38 C ANISOU 2157 CG ALEU A1076 6128 5920 5956 1066 -773 -800 C ATOM 2158 CG BLEU A1076 3.628 -58.833 27.407 0.57 41.13 C ANISOU 2158 CG BLEU A1076 5282 4757 5587 813 -630 -1034 C ATOM 2159 CD1ALEU A1076 5.280 -59.140 28.542 0.43 44.04 C ANISOU 2159 CD1ALEU A1076 5751 5516 5467 1121 -844 -1618 C ATOM 2160 CD1BLEU A1076 2.689 -57.898 28.150 0.57 43.00 C ANISOU 2160 CD1BLEU A1076 5386 5259 5693 931 -204 -881 C ATOM 2161 CD2ALEU A1076 3.031 -58.690 29.548 0.43 46.58 C ANISOU 2161 CD2ALEU A1076 5874 6134 5689 1161 -301 -710 C ATOM 2162 CD2BLEU A1076 5.066 -58.619 27.856 0.57 42.44 C ANISOU 2162 CD2BLEU A1076 5517 5141 5469 974 -726 -1705 C ATOM 2163 N LYS A1077 3.172 -63.434 27.720 1.00 47.68 N ANISOU 2163 N LYS A1077 6433 4960 6723 687 -1920 529 N ATOM 2164 CA LYS A1077 3.249 -64.673 28.485 1.00 51.99 C ANISOU 2164 CA LYS A1077 7163 5418 7173 753 -2285 1012 C ATOM 2165 C LYS A1077 4.300 -65.603 27.892 1.00 51.90 C ANISOU 2165 C LYS A1077 7361 5015 7345 891 -2886 642 C ATOM 2166 O LYS A1077 5.057 -66.245 28.619 1.00 54.91 O ANISOU 2166 O LYS A1077 7930 5439 7494 1155 -3206 610 O ATOM 2167 CB LYS A1077 1.889 -65.372 28.525 1.00 54.99 C ANISOU 2167 CB LYS A1077 7481 5595 7816 423 -2294 1899 C ATOM 2168 CG LYS A1077 1.911 -66.708 29.250 1.00 60.40 C ANISOU 2168 CG LYS A1077 8410 6078 8462 401 -2709 2514 C ATOM 2169 CD LYS A1077 0.550 -67.379 29.226 1.00 64.85 C ANISOU 2169 CD LYS A1077 8872 6429 9339 -35 -2706 3406 C ATOM 2170 CE LYS A1077 0.602 -68.743 29.891 1.00 71.62 C ANISOU 2170 CE LYS A1077 10019 7001 10193 -124 -3127 4019 C ATOM 2171 NZ LYS A1077 1.548 -69.662 29.200 1.00 73.48 N ANISOU 2171 NZ LYS A1077 10503 6725 10691 17 -3642 3448 N ATOM 2172 N LEU A1078 4.342 -65.664 26.565 1.00 48.98 N ANISOU 2172 N LEU A1078 6949 4299 7364 754 -3054 336 N ATOM 2173 CA LEU A1078 5.322 -66.483 25.864 1.00 50.87 C ANISOU 2173 CA LEU A1078 7327 4225 7777 925 -3608 -135 C ATOM 2174 C LEU A1078 6.726 -65.918 26.049 1.00 53.78 C ANISOU 2174 C LEU A1078 7646 4984 7804 1240 -3569 -954 C ATOM 2175 O LEU A1078 7.700 -66.666 26.146 1.00 53.35 O ANISOU 2175 O LEU A1078 7704 4863 7704 1541 -4031 -1299 O ATOM 2176 CB LEU A1078 4.976 -66.575 24.377 1.00 47.20 C ANISOU 2176 CB LEU A1078 6786 3419 7728 706 -3738 -305 C ATOM 2177 CG LEU A1078 3.678 -67.314 24.045 1.00 49.39 C ANISOU 2177 CG LEU A1078 7067 3312 8387 361 -3863 384 C ATOM 2178 CD1 LEU A1078 3.287 -67.104 22.589 1.00 46.02 C ANISOU 2178 CD1 LEU A1078 6454 2864 8167 136 -3817 128 C ATOM 2179 CD2 LEU A1078 3.814 -68.798 24.359 1.00 53.51 C ANISOU 2179 CD2 LEU A1078 7761 3597 8972 320 -4261 570 C ATOM 2180 N ALA A1079 6.818 -64.593 26.105 1.00 48.35 N ANISOU 2180 N ALA A1079 6777 4689 6903 1170 -3044 -1278 N ATOM 2181 CA ALA A1079 8.095 -63.916 26.295 1.00 49.81 C ANISOU 2181 CA ALA A1079 6861 5274 6790 1373 -2953 -2057 C ATOM 2182 C ALA A1079 8.664 -64.184 27.687 1.00 55.39 C ANISOU 2182 C ALA A1079 7656 6287 7102 1711 -3083 -2059 C ATOM 2183 O ALA A1079 9.868 -64.390 27.844 1.00 60.35 O ANISOU 2183 O ALA A1079 8242 7108 7582 1986 -3302 -2598 O ATOM 2184 CB ALA A1079 7.939 -62.419 26.064 1.00 46.49 C ANISOU 2184 CB ALA A1079 6274 5095 6296 1162 -2388 -2322 C ATOM 2185 N ASN A1080 7.794 -64.186 28.692 1.00 54.84 N ANISOU 2185 N ASN A1080 7665 6319 6852 1695 -2889 -1411 N ATOM 2186 CA ASN A1080 8.212 -64.436 30.068 1.00 58.06 C ANISOU 2186 CA ASN A1080 8182 7078 6802 2014 -2994 -1314 C ATOM 2187 C ASN A1080 8.616 -65.890 30.299 1.00 61.43 C ANISOU 2187 C ASN A1080 8867 7200 7275 2250 -3646 -1045 C ATOM 2188 O ASN A1080 9.216 -66.221 31.321 1.00 61.72 O ANISOU 2188 O ASN A1080 9029 7498 6923 2587 -3870 -1053 O ATOM 2189 CB ASN A1080 7.099 -64.047 31.043 1.00 63.39 C ANISOU 2189 CB ASN A1080 8845 8028 7214 1919 -2569 -663 C ATOM 2190 CG ASN A1080 6.844 -62.552 31.074 1.00 63.63 C ANISOU 2190 CG ASN A1080 8652 8395 7130 1832 -1987 -1038 C ATOM 2191 OD1 ASN A1080 7.742 -61.752 30.811 1.00 66.27 O ANISOU 2191 OD1 ASN A1080 8883 8876 7419 1898 -1909 -1805 O ATOM 2192 ND2 ASN A1080 5.616 -62.167 31.401 1.00 60.53 N ANISOU 2192 ND2 ASN A1080 8170 8120 6708 1681 -1591 -508 N ATOM 2193 N GLU A1081 8.281 -66.755 29.348 1.00 61.68 N ANISOU 2193 N GLU A1081 8996 6655 7784 2095 -3991 -819 N ATOM 2194 CA GLU A1081 8.651 -68.162 29.425 1.00 69.67 C ANISOU 2194 CA GLU A1081 10284 7234 8952 2294 -4634 -615 C ATOM 2195 C GLU A1081 9.934 -68.427 28.647 1.00 71.46 C ANISOU 2195 C GLU A1081 10439 7393 9321 2481 -4783 -1514 C ATOM 2196 O GLU A1081 10.432 -69.552 28.615 1.00 76.10 O ANISOU 2196 O GLU A1081 11228 7637 10051 2615 -5135 -1566 O ATOM 2197 CB GLU A1081 7.520 -69.047 28.895 1.00 73.50 C ANISOU 2197 CB GLU A1081 10895 7127 9906 1884 -4719 100 C ATOM 2198 CG GLU A1081 6.265 -69.026 29.749 1.00 80.91 C ANISOU 2198 CG GLU A1081 11892 8124 10728 1639 -4498 1098 C ATOM 2199 CD GLU A1081 5.099 -69.734 29.087 1.00 89.08 C ANISOU 2199 CD GLU A1081 12903 8684 12258 1134 -4456 1662 C ATOM 2200 OE1 GLU A1081 5.204 -70.063 27.887 1.00 89.08 O ANISOU 2200 OE1 GLU A1081 12846 8344 12655 998 -4613 1232 O ATOM 2201 OE2 GLU A1081 4.076 -69.961 29.767 1.00 95.69 O ANISOU 2201 OE2 GLU A1081 13747 9571 13038 862 -4255 2489 O ATOM 2202 N GLY A1082 10.462 -67.384 28.016 1.00 58.63 N ANISOU 2202 N GLY A1082 6167 5648 10463 2142 760 979 N ATOM 2203 CA GLY A1082 11.695 -67.496 27.260 1.00 63.58 C ANISOU 2203 CA GLY A1082 6691 6318 11147 2231 957 1211 C ATOM 2204 C GLY A1082 11.495 -68.073 25.871 1.00 65.36 C ANISOU 2204 C GLY A1082 7202 6329 11301 2249 1294 1231 C ATOM 2205 O GLY A1082 12.460 -68.411 25.186 1.00 71.17 O ANISOU 2205 O GLY A1082 7924 7124 11995 2408 1545 1440 O ATOM 2206 N LYS A1083 10.238 -68.187 25.455 1.00 59.16 N ANISOU 2206 N LYS A1083 6684 5321 10475 2111 1288 1000 N ATOM 2207 CA LYS A1083 9.916 -68.713 24.133 1.00 55.30 C ANISOU 2207 CA LYS A1083 6540 4606 9865 2127 1537 930 C ATOM 2208 C LYS A1083 9.899 -67.590 23.102 1.00 52.23 C ANISOU 2208 C LYS A1083 6057 4270 9519 2012 1410 936 C ATOM 2209 O LYS A1083 8.835 -67.093 22.733 1.00 50.52 O ANISOU 2209 O LYS A1083 5956 4006 9235 1796 1208 690 O ATOM 2210 CB LYS A1083 8.569 -69.437 24.158 1.00 53.28 C ANISOU 2210 CB LYS A1083 6623 4114 9507 1961 1544 645 C ATOM 2211 CG LYS A1083 8.485 -70.549 25.192 1.00 52.18 C ANISOU 2211 CG LYS A1083 6604 3890 9331 2033 1685 684 C ATOM 2212 CD LYS A1083 7.089 -71.145 25.256 1.00 53.68 C ANISOU 2212 CD LYS A1083 7044 3850 9501 1777 1672 452 C ATOM 2213 CE LYS A1083 7.015 -72.267 26.279 1.00 55.24 C ANISOU 2213 CE LYS A1083 7378 3897 9712 1859 1873 569 C ATOM 2214 NZ LYS A1083 5.635 -72.813 26.401 1.00 54.31 N ANISOU 2214 NZ LYS A1083 7423 3606 9606 1515 1843 398 N ATOM 2215 N VAL A1084 11.084 -67.204 22.638 1.00 51.36 N ANISOU 2215 N VAL A1084 5723 4297 9496 2160 1537 1244 N ATOM 2216 CA VAL A1084 11.243 -66.050 21.756 1.00 53.33 C ANISOU 2216 CA VAL A1084 5834 4620 9809 2040 1433 1353 C ATOM 2217 C VAL A1084 10.505 -66.199 20.428 1.00 52.00 C ANISOU 2217 C VAL A1084 6061 4322 9375 2056 1553 1178 C ATOM 2218 O VAL A1084 9.692 -65.349 20.066 1.00 51.66 O ANISOU 2218 O VAL A1084 6068 4256 9304 1860 1309 1008 O ATOM 2219 CB VAL A1084 12.728 -65.780 21.456 1.00 60.53 C ANISOU 2219 CB VAL A1084 6394 5731 10875 2203 1631 1800 C ATOM 2220 CG1 VAL A1084 12.893 -64.429 20.771 1.00 55.34 C ANISOU 2220 CG1 VAL A1084 5532 5126 10370 2000 1479 1976 C ATOM 2221 CG2 VAL A1084 13.544 -65.835 22.735 1.00 62.18 C ANISOU 2221 CG2 VAL A1084 6217 6095 11315 2248 1517 1951 C ATOM 2222 N LYS A1085 10.803 -67.275 19.705 1.00 54.48 N ANISOU 2222 N LYS A1085 6681 4556 9464 2339 1906 1207 N ATOM 2223 CA LYS A1085 10.192 -67.532 18.402 1.00 55.22 C ANISOU 2223 CA LYS A1085 7195 4527 9259 2434 2005 1014 C ATOM 2224 C LYS A1085 8.670 -67.572 18.484 1.00 53.20 C ANISOU 2224 C LYS A1085 7179 4112 8922 2151 1714 563 C ATOM 2225 O LYS A1085 7.976 -67.035 17.620 1.00 53.16 O ANISOU 2225 O LYS A1085 7323 4110 8764 2092 1584 390 O ATOM 2226 CB LYS A1085 10.713 -68.849 17.822 1.00 60.62 C ANISOU 2226 CB LYS A1085 8246 5096 9691 2832 2378 1049 C ATOM 2227 CG LYS A1085 12.166 -68.811 17.381 1.00 62.16 C ANISOU 2227 CG LYS A1085 8226 5537 9856 3207 2722 1512 C ATOM 2228 CD LYS A1085 12.339 -67.976 16.124 1.00 64.75 C ANISOU 2228 CD LYS A1085 8537 6015 10050 3325 2819 1691 C ATOM 2229 CE LYS A1085 13.764 -68.050 15.604 1.00 71.05 C ANISOU 2229 CE LYS A1085 9106 7108 10782 3735 3226 2202 C ATOM 2230 NZ LYS A1085 13.918 -67.332 14.310 1.00 78.94 N ANISOU 2230 NZ LYS A1085 10131 8261 11603 3915 3394 2429 N ATOM 2231 N GLU A1086 8.161 -68.210 19.532 1.00 51.97 N ANISOU 2231 N GLU A1086 7034 3853 8861 1998 1624 403 N ATOM 2232 CA GLU A1086 6.725 -68.343 19.733 1.00 58.17 C ANISOU 2232 CA GLU A1086 7958 4541 9602 1710 1377 30 C ATOM 2233 C GLU A1086 6.106 -66.994 20.089 1.00 57.46 C ANISOU 2233 C GLU A1086 7574 4654 9606 1494 1027 -37 C ATOM 2234 O GLU A1086 4.953 -66.720 19.754 1.00 47.75 O ANISOU 2234 O GLU A1086 6435 3445 8263 1327 812 -322 O ATOM 2235 CB GLU A1086 6.436 -69.375 20.827 1.00 62.23 C ANISOU 2235 CB GLU A1086 8519 4914 10210 1620 1432 -20 C ATOM 2236 CG GLU A1086 4.994 -69.849 20.883 1.00 69.16 C ANISOU 2236 CG GLU A1086 9564 5664 11048 1316 1266 -356 C ATOM 2237 CD GLU A1086 4.810 -71.046 21.797 1.00 76.35 C ANISOU 2237 CD GLU A1086 10591 6365 12053 1239 1409 -329 C ATOM 2238 OE1 GLU A1086 5.823 -71.682 22.160 1.00 81.34 O ANISOU 2238 OE1 GLU A1086 11302 6894 12710 1497 1666 -97 O ATOM 2239 OE2 GLU A1086 3.653 -71.351 22.155 1.00 78.86 O ANISOU 2239 OE2 GLU A1086 10907 6637 12418 932 1276 -511 O ATOM 2240 N ALA A1087 6.886 -66.153 20.762 1.00 47.32 N ANISOU 2240 N ALA A1087 5945 3517 8519 1518 945 217 N ATOM 2241 CA ALA A1087 6.439 -64.817 21.138 1.00 54.86 C ANISOU 2241 CA ALA A1087 6677 4607 9561 1366 584 163 C ATOM 2242 C ALA A1087 6.374 -63.908 19.916 1.00 46.31 C ANISOU 2242 C ALA A1087 5689 3536 8372 1384 531 183 C ATOM 2243 O ALA A1087 5.427 -63.139 19.752 1.00 45.39 O ANISOU 2243 O ALA A1087 5614 3471 8162 1285 258 -25 O ATOM 2244 CB ALA A1087 7.362 -64.223 22.194 1.00 45.27 C ANISOU 2244 CB ALA A1087 5111 3486 8605 1385 460 403 C ATOM 2245 N GLN A1088 7.388 -64.005 19.061 1.00 48.36 N ANISOU 2245 N GLN A1088 5981 3776 8617 1558 816 462 N ATOM 2246 CA GLN A1088 7.452 -63.208 17.842 1.00 49.74 C ANISOU 2246 CA GLN A1088 6259 3973 8668 1634 847 568 C ATOM 2247 C GLN A1088 6.325 -63.560 16.877 1.00 50.06 C ANISOU 2247 C GLN A1088 6682 3975 8365 1694 819 213 C ATOM 2248 O GLN A1088 5.734 -62.678 16.255 1.00 54.14 O ANISOU 2248 O GLN A1088 7284 4536 8750 1687 644 124 O ATOM 2249 CB GLN A1088 8.805 -63.393 17.154 1.00 52.59 C ANISOU 2249 CB GLN A1088 6545 4383 9053 1866 1229 996 C ATOM 2250 CG GLN A1088 9.976 -62.804 17.921 1.00 53.23 C ANISOU 2250 CG GLN A1088 6169 4549 9506 1772 1210 1389 C ATOM 2251 CD GLN A1088 11.305 -63.066 17.243 1.00 56.69 C ANISOU 2251 CD GLN A1088 6455 5120 9963 2017 1626 1854 C ATOM 2252 OE1 GLN A1088 11.651 -64.210 16.950 1.00 57.98 O ANISOU 2252 OE1 GLN A1088 6787 5313 9928 2310 1952 1868 O ATOM 2253 NE2 GLN A1088 12.057 -62.002 16.985 1.00 58.76 N ANISOU 2253 NE2 GLN A1088 6403 5462 10463 1909 1619 2258 N ATOM 2254 N ALA A1089 6.033 -64.851 16.754 1.00 51.19 N ANISOU 2254 N ALA A1089 7069 4016 8363 1759 967 3 N ATOM 2255 CA ALA A1089 4.959 -65.309 15.881 1.00 51.78 C ANISOU 2255 CA ALA A1089 7500 4034 8140 1781 881 -383 C ATOM 2256 C ALA A1089 3.608 -64.807 16.379 1.00 55.41 C ANISOU 2256 C ALA A1089 7859 4588 8608 1510 498 -705 C ATOM 2257 O ALA A1089 2.746 -64.425 15.587 1.00 56.25 O ANISOU 2257 O ALA A1089 8118 4769 8484 1534 320 -949 O ATOM 2258 CB ALA A1089 4.960 -66.825 15.785 1.00 53.56 C ANISOU 2258 CB ALA A1089 8022 4054 8275 1853 1065 -544 C ATOM 2259 N ALA A1090 3.432 -64.809 17.696 1.00 48.58 N ANISOU 2259 N ALA A1090 6727 3760 7972 1308 378 -693 N ATOM 2260 CA ALA A1090 2.203 -64.318 18.306 1.00 48.92 C ANISOU 2260 CA ALA A1090 6619 3962 8005 1114 45 -943 C ATOM 2261 C ALA A1090 2.078 -62.809 18.135 1.00 48.01 C ANISOU 2261 C ALA A1090 6406 3988 7849 1178 -198 -892 C ATOM 2262 O ALA A1090 0.977 -62.277 17.985 1.00 48.10 O ANISOU 2262 O ALA A1090 6423 4157 7696 1148 -462 -1141 O ATOM 2263 CB ALA A1090 2.156 -64.691 19.780 1.00 48.54 C ANISOU 2263 CB ALA A1090 6327 3947 8168 977 21 -887 C ATOM 2264 N ALA A1091 3.217 -62.123 18.157 1.00 47.93 N ANISOU 2264 N ALA A1091 6302 3915 7996 1267 -115 -553 N ATOM 2265 CA ALA A1091 3.242 -60.675 18.001 1.00 49.17 C ANISOU 2265 CA ALA A1091 6411 4104 8168 1301 -345 -451 C ATOM 2266 C ALA A1091 2.972 -60.274 16.555 1.00 55.49 C ANISOU 2266 C ALA A1091 7479 4911 8693 1464 -294 -481 C ATOM 2267 O ALA A1091 2.607 -59.133 16.276 1.00 56.84 O ANISOU 2267 O ALA A1091 7705 5109 8781 1518 -513 -483 O ATOM 2268 CB ALA A1091 4.577 -60.113 18.466 1.00 47.91 C ANISOU 2268 CB ALA A1091 6038 3843 8324 1277 -291 -55 C ATOM 2269 N GLU A1092 3.151 -61.218 15.637 1.00 59.05 N ANISOU 2269 N GLU A1092 8141 5327 8969 1592 -16 -511 N ATOM 2270 CA GLU A1092 2.927 -60.950 14.223 1.00 67.21 C ANISOU 2270 CA GLU A1092 9466 6394 9678 1830 51 -549 C ATOM 2271 C GLU A1092 1.432 -60.876 13.926 1.00 63.25 C ANISOU 2271 C GLU A1092 9097 6040 8896 1822 -259 -1010 C ATOM 2272 O GLU A1092 1.010 -60.249 12.954 1.00 64.57 O ANISOU 2272 O GLU A1092 9465 6290 8778 2029 -340 -1079 O ATOM 2273 CB GLU A1092 3.593 -62.023 13.359 1.00 77.98 C ANISOU 2273 CB GLU A1092 11054 7686 10888 2051 418 -471 C ATOM 2274 CG GLU A1092 3.780 -61.624 11.902 1.00 89.46 C ANISOU 2274 CG GLU A1092 12789 9193 12008 2404 576 -352 C ATOM 2275 CD GLU A1092 4.764 -60.480 11.728 1.00 97.54 C ANISOU 2275 CD GLU A1092 13648 10219 13192 2466 731 184 C ATOM 2276 OE1 GLU A1092 5.650 -60.313 12.594 1.00 98.91 O ANISOU 2276 OE1 GLU A1092 13499 10335 13747 2275 804 500 O ATOM 2277 OE2 GLU A1092 4.651 -59.744 10.725 1.00101.60 O ANISOU 2277 OE2 GLU A1092 14352 10791 13459 2699 769 301 O ATOM 2278 N GLN A1093 0.635 -61.510 14.781 1.00 57.35 N ANISOU 2278 N GLN A1093 8209 5353 8227 1596 -424 -1294 N ATOM 2279 CA GLN A1093 -0.816 -61.494 14.639 1.00 56.70 C ANISOU 2279 CA GLN A1093 8136 5479 7927 1540 -729 -1709 C ATOM 2280 C GLN A1093 -1.385 -60.109 14.934 1.00 56.58 C ANISOU 2280 C GLN A1093 8010 5645 7841 1613 -1026 -1719 C ATOM 2281 O GLN A1093 -2.506 -59.791 14.537 1.00 56.10 O ANISOU 2281 O GLN A1093 7985 5816 7516 1691 -1276 -2012 O ATOM 2282 CB GLN A1093 -1.454 -62.532 15.564 1.00 55.15 C ANISOU 2282 CB GLN A1093 7754 5315 7886 1245 -783 -1914 C ATOM 2283 CG GLN A1093 -0.885 -63.935 15.406 1.00 60.68 C ANISOU 2283 CG GLN A1093 8619 5757 8678 1172 -509 -1902 C ATOM 2284 CD GLN A1093 -1.116 -64.511 14.021 1.00 69.17 C ANISOU 2284 CD GLN A1093 10064 6754 9462 1328 -494 -2149 C ATOM 2285 OE1 GLN A1093 -2.070 -64.146 13.334 1.00 72.80 O ANISOU 2285 OE1 GLN A1093 10589 7401 9670 1383 -750 -2440 O ATOM 2286 NE2 GLN A1093 -0.238 -65.417 13.604 1.00 74.59 N ANISOU 2286 NE2 GLN A1093 11013 7182 10146 1454 -211 -2050 N ATOM 2287 N LEU A1094 -0.601 -59.292 15.632 1.00 55.98 N ANISOU 2287 N LEU A1094 8516 3966 8786 2057 254 318 N ATOM 2288 CA LEU A1094 -1.001 -57.933 15.979 1.00 51.48 C ANISOU 2288 CA LEU A1094 7749 3651 8159 1744 508 595 C ATOM 2289 C LEU A1094 -1.211 -57.068 14.741 1.00 53.35 C ANISOU 2289 C LEU A1094 8187 4098 7986 1895 599 527 C ATOM 2290 O LEU A1094 -2.003 -56.125 14.762 1.00 53.23 O ANISOU 2290 O LEU A1094 8111 4111 8003 1706 632 722 O ATOM 2291 CB LEU A1094 0.046 -57.289 16.892 1.00 50.94 C ANISOU 2291 CB LEU A1094 7382 3910 8062 1583 955 845 C ATOM 2292 CG LEU A1094 0.189 -57.893 18.290 1.00 55.56 C ANISOU 2292 CG LEU A1094 7707 4382 9021 1282 874 1048 C ATOM 2293 CD1 LEU A1094 1.525 -57.518 18.902 1.00 57.38 C ANISOU 2293 CD1 LEU A1094 7661 5040 9099 1215 1265 1254 C ATOM 2294 CD2 LEU A1094 -0.947 -57.430 19.181 1.00 53.82 C ANISOU 2294 CD2 LEU A1094 7337 4066 9046 752 817 1203 C ATOM 2295 N LYS A1095 -0.500 -57.389 13.665 1.00 54.74 N ANISOU 2295 N LYS A1095 8596 4420 7781 2233 644 257 N ATOM 2296 CA LYS A1095 -0.616 -56.630 12.425 1.00 57.73 C ANISOU 2296 CA LYS A1095 9201 5048 7684 2315 701 210 C ATOM 2297 C LYS A1095 -1.995 -56.793 11.795 1.00 57.91 C ANISOU 2297 C LYS A1095 9398 4872 7732 2227 236 184 C ATOM 2298 O LYS A1095 -2.506 -55.872 11.162 1.00 60.31 O ANISOU 2298 O LYS A1095 9766 5336 7814 2168 208 371 O ATOM 2299 CB LYS A1095 0.469 -57.051 11.433 1.00 63.18 C ANISOU 2299 CB LYS A1095 10089 5991 7924 2634 874 -138 C ATOM 2300 CG LYS A1095 1.865 -56.604 11.829 1.00 65.42 C ANISOU 2300 CG LYS A1095 10141 6669 8047 2705 1373 -64 C ATOM 2301 CD LYS A1095 2.868 -56.890 10.728 1.00 73.99 C ANISOU 2301 CD LYS A1095 11376 8100 8635 3008 1589 -438 C ATOM 2302 CE LYS A1095 4.221 -56.280 11.048 1.00 77.43 C ANISOU 2302 CE LYS A1095 11525 9068 8827 3013 2098 -325 C ATOM 2303 NZ LYS A1095 5.215 -56.546 9.972 1.00 85.62 N ANISOU 2303 NZ LYS A1095 12644 10525 9362 3298 2356 -727 N ATOM 2304 N THR A1096 -2.595 -57.965 11.975 1.00 57.89 N ANISOU 2304 N THR A1096 9470 4531 7994 2193 -149 -13 N ATOM 2305 CA THR A1096 -3.937 -58.219 11.464 1.00 59.65 C ANISOU 2305 CA THR A1096 9807 4629 8228 2026 -624 -33 C ATOM 2306 C THR A1096 -4.962 -57.363 12.202 1.00 56.37 C ANISOU 2306 C THR A1096 9049 4212 8156 1778 -680 356 C ATOM 2307 O THR A1096 -5.862 -56.787 11.590 1.00 56.96 O ANISOU 2307 O THR A1096 9100 4414 8129 1730 -893 522 O ATOM 2308 CB THR A1096 -4.319 -59.705 11.592 1.00 62.29 C ANISOU 2308 CB THR A1096 10334 4575 8758 1957 -1001 -341 C ATOM 2309 OG1 THR A1096 -3.378 -60.505 10.866 1.00 68.27 O ANISOU 2309 OG1 THR A1096 11429 5267 9242 2248 -896 -760 O ATOM 2310 CG2 THR A1096 -5.715 -59.949 11.040 1.00 63.35 C ANISOU 2310 CG2 THR A1096 10563 4682 8826 1689 -1499 -355 C ATOM 2311 N THR A1097 -4.814 -57.280 13.520 1.00 52.17 N ANISOU 2311 N THR A1097 8232 3558 8031 1620 -478 505 N ATOM 2312 CA THR A1097 -5.694 -56.465 14.350 1.00 51.94 C ANISOU 2312 CA THR A1097 7855 3521 8359 1373 -413 799 C ATOM 2313 C THR A1097 -5.513 -54.982 14.039 1.00 51.56 C ANISOU 2313 C THR A1097 7759 3673 8157 1483 -51 1054 C ATOM 2314 O THR A1097 -6.477 -54.213 14.016 1.00 49.35 O ANISOU 2314 O THR A1097 7303 3386 8060 1450 -108 1272 O ATOM 2315 CB THR A1097 -5.431 -56.704 15.849 1.00 48.75 C ANISOU 2315 CB THR A1097 7195 2993 8336 1089 -216 868 C ATOM 2316 OG1 THR A1097 -5.489 -58.108 16.128 1.00 52.22 O ANISOU 2316 OG1 THR A1097 7746 3185 8909 994 -568 678 O ATOM 2317 CG2 THR A1097 -6.459 -55.975 16.700 1.00 47.42 C ANISOU 2317 CG2 THR A1097 6665 2815 8537 787 -131 1069 C ATOM 2318 N ARG A1098 -4.266 -54.594 13.798 1.00 50.76 N ANISOU 2318 N ARG A1098 7812 3745 7730 1618 324 1034 N ATOM 2319 CA ARG A1098 -3.925 -53.211 13.495 1.00 52.21 C ANISOU 2319 CA ARG A1098 8047 4090 7699 1661 698 1274 C ATOM 2320 C ARG A1098 -4.603 -52.721 12.219 1.00 54.26 C ANISOU 2320 C ARG A1098 8496 4426 7696 1829 417 1402 C ATOM 2321 O ARG A1098 -5.148 -51.619 12.178 1.00 52.09 O ANISOU 2321 O ARG A1098 8158 4094 7539 1843 512 1712 O ATOM 2322 CB ARG A1098 -2.409 -53.059 13.367 1.00 47.15 C ANISOU 2322 CB ARG A1098 7542 3713 6659 1714 1104 1190 C ATOM 2323 CG ARG A1098 -1.955 -51.669 12.968 1.00 49.38 C ANISOU 2323 CG ARG A1098 7969 4175 6619 1682 1490 1425 C ATOM 2324 CD ARG A1098 -0.518 -51.691 12.484 1.00 50.59 C ANISOU 2324 CD ARG A1098 8271 4711 6238 1736 1792 1283 C ATOM 2325 NE ARG A1098 -0.358 -52.539 11.307 1.00 58.52 N ANISOU 2325 NE ARG A1098 9490 5859 6887 1987 1498 992 N ATOM 2326 CZ ARG A1098 0.809 -52.800 10.728 1.00 64.95 C ANISOU 2326 CZ ARG A1098 10405 7034 7239 2100 1715 761 C ATOM 2327 NH1 ARG A1098 1.925 -52.278 11.219 1.00 65.43 N ANISOU 2327 NH1 ARG A1098 10336 7399 7126 1977 2188 836 N ATOM 2328 NH2 ARG A1098 0.861 -53.584 9.660 1.00 68.52 N ANISOU 2328 NH2 ARG A1098 11072 7581 7381 2300 1483 431 N ATOM 2329 N ASN A1099 -4.569 -53.550 11.180 1.00 54.49 N ANISOU 2329 N ASN A1099 8766 4569 7370 1945 71 1170 N ATOM 2330 CA ASN A1099 -5.105 -53.166 9.880 1.00 65.04 C ANISOU 2330 CA ASN A1099 10306 6075 8333 2024 -234 1302 C ATOM 2331 C ASN A1099 -6.627 -53.230 9.816 1.00 65.97 C ANISOU 2331 C ASN A1099 10208 6096 8760 1972 -720 1492 C ATOM 2332 O ASN A1099 -7.248 -52.564 8.989 1.00 70.34 O ANISOU 2332 O ASN A1099 10795 6785 9145 2034 -959 1794 O ATOM 2333 CB ASN A1099 -4.510 -54.052 8.783 1.00 66.60 C ANISOU 2333 CB ASN A1099 10852 6479 7973 2080 -387 925 C ATOM 2334 CG ASN A1099 -2.995 -54.028 8.773 1.00 66.29 C ANISOU 2334 CG ASN A1099 10944 6625 7618 2172 100 713 C ATOM 2335 OD1 ASN A1099 -2.374 -53.070 9.231 1.00 63.62 O ANISOU 2335 OD1 ASN A1099 10523 6372 7276 2141 520 938 O ATOM 2336 ND2 ASN A1099 -2.390 -55.088 8.248 1.00 69.01 N ANISOU 2336 ND2 ASN A1099 11487 7041 7691 2273 67 260 N ATOM 2337 N ALA A1100 -7.226 -54.030 10.692 1.00 62.73 N ANISOU 2337 N ALA A1100 9553 5492 8788 1835 -885 1351 N ATOM 2338 CA ALA A1100 -8.668 -54.247 10.653 1.00 64.63 C ANISOU 2338 CA ALA A1100 9534 5731 9291 1730 -1362 1480 C ATOM 2339 C ALA A1100 -9.425 -53.333 11.611 1.00 65.65 C ANISOU 2339 C ALA A1100 9210 5741 9994 1732 -1178 1790 C ATOM 2340 O ALA A1100 -10.566 -52.956 11.344 1.00 67.51 O ANISOU 2340 O ALA A1100 9168 6065 10417 1782 -1481 2048 O ATOM 2341 CB ALA A1100 -8.986 -55.702 10.959 1.00 63.53 C ANISOU 2341 CB ALA A1100 9425 5473 9239 1501 -1687 1128 C ATOM 2342 N TYR A1101 -8.792 -52.976 12.724 1.00 64.20 N ANISOU 2342 N TYR A1101 8928 5384 10082 1666 -667 1756 N ATOM 2343 CA TYR A1101 -9.471 -52.207 13.762 1.00 60.05 C ANISOU 2343 CA TYR A1101 7992 4716 10108 1599 -403 1935 C ATOM 2344 C TYR A1101 -8.754 -50.909 14.120 1.00 54.80 C ANISOU 2344 C TYR A1101 7410 3955 9457 1670 204 2090 C ATOM 2345 O TYR A1101 -9.314 -49.823 13.973 1.00 55.53 O ANISOU 2345 O TYR A1101 7394 4046 9657 1798 298 2284 O ATOM 2346 CB TYR A1101 -9.634 -53.057 15.025 1.00 56.85 C ANISOU 2346 CB TYR A1101 7347 4214 10038 1245 -364 1702 C ATOM 2347 CG TYR A1101 -10.489 -54.290 14.841 1.00 59.79 C ANISOU 2347 CG TYR A1101 7639 4649 10428 1064 -947 1541 C ATOM 2348 CD1 TYR A1101 -11.871 -54.225 14.963 1.00 62.66 C ANISOU 2348 CD1 TYR A1101 7584 5118 11106 975 -1232 1651 C ATOM 2349 CD2 TYR A1101 -9.913 -55.522 14.556 1.00 58.64 C ANISOU 2349 CD2 TYR A1101 7835 4455 9992 970 -1194 1267 C ATOM 2350 CE1 TYR A1101 -12.657 -55.352 14.801 1.00 64.29 C ANISOU 2350 CE1 TYR A1101 7732 5428 11267 710 -1767 1504 C ATOM 2351 CE2 TYR A1101 -10.691 -56.653 14.391 1.00 59.78 C ANISOU 2351 CE2 TYR A1101 7992 4597 10126 736 -1709 1101 C ATOM 2352 CZ TYR A1101 -12.062 -56.562 14.515 1.00 63.71 C ANISOU 2352 CZ TYR A1101 8090 5247 10870 562 -2004 1226 C ATOM 2353 OH TYR A1101 -12.840 -57.686 14.352 1.00 69.28 O ANISOU 2353 OH TYR A1101 8822 5996 11505 235 -2519 1062 O ATOM 2354 N ILE A1102 -7.517 -51.035 14.592 1.00 54.77 N ANISOU 2354 N ILE A1102 7993 4908 7911 2621 725 -197 N ATOM 2355 CA ILE A1102 -6.779 -49.911 15.166 1.00 55.78 C ANISOU 2355 CA ILE A1102 8301 5087 7805 2752 628 -285 C ATOM 2356 C ILE A1102 -6.606 -48.742 14.198 1.00 53.95 C ANISOU 2356 C ILE A1102 8637 4523 7337 2785 519 -609 C ATOM 2357 O ILE A1102 -6.805 -47.586 14.572 1.00 54.38 O ANISOU 2357 O ILE A1102 8921 4701 7040 3006 227 -782 O ATOM 2358 CB ILE A1102 -5.386 -50.356 15.653 1.00 57.78 C ANISOU 2358 CB ILE A1102 8353 5162 8438 2552 805 -31 C ATOM 2359 CG1 ILE A1102 -5.509 -51.571 16.576 1.00 54.81 C ANISOU 2359 CG1 ILE A1102 7395 5088 8344 2488 911 328 C ATOM 2360 CG2 ILE A1102 -4.673 -49.210 16.357 1.00 54.67 C ANISOU 2360 CG2 ILE A1102 8133 4785 7856 2655 551 -67 C ATOM 2361 CD1 ILE A1102 -6.399 -51.341 17.780 1.00 55.99 C ANISOU 2361 CD1 ILE A1102 7243 5889 8140 2790 711 452 C ATOM 2362 N GLN A1103 -6.240 -49.046 12.957 1.00 56.40 N ANISOU 2362 N GLN A1103 9193 4416 7822 2608 730 -680 N ATOM 2363 CA GLN A1103 -6.020 -48.010 11.954 1.00 59.25 C ANISOU 2363 CA GLN A1103 9982 4541 7988 2571 656 -878 C ATOM 2364 C GLN A1103 -7.310 -47.250 11.649 1.00 57.95 C ANISOU 2364 C GLN A1103 9982 4613 7423 2680 371 -1131 C ATOM 2365 O GLN A1103 -7.286 -46.047 11.382 1.00 54.81 O ANISOU 2365 O GLN A1103 9793 4230 6802 2659 153 -1237 O ATOM 2366 CB GLN A1103 -5.448 -48.620 10.674 1.00 63.80 C ANISOU 2366 CB GLN A1103 10616 4881 8743 2345 938 -839 C ATOM 2367 CG GLN A1103 -5.056 -47.596 9.623 1.00 68.18 C ANISOU 2367 CG GLN A1103 11442 5342 9123 2267 904 -886 C ATOM 2368 CD GLN A1103 -4.382 -48.225 8.422 1.00 72.48 C ANISOU 2368 CD GLN A1103 12071 5732 9735 2214 1229 -801 C ATOM 2369 OE1 GLN A1103 -4.097 -49.423 8.412 1.00 74.23 O ANISOU 2369 OE1 GLN A1103 12153 5899 10153 2211 1441 -733 O ATOM 2370 NE2 GLN A1103 -4.123 -47.419 7.400 1.00 75.24 N ANISOU 2370 NE2 GLN A1103 12686 6010 9890 2230 1266 -791 N ATOM 2371 N LYS A1104 -8.435 -47.957 11.697 1.00 59.09 N ANISOU 2371 N LYS A1104 10025 4904 7523 2818 352 -1166 N ATOM 2372 CA LYS A1104 -9.734 -47.337 11.472 1.00 61.94 C ANISOU 2372 CA LYS A1104 10495 5503 7537 2979 101 -1329 C ATOM 2373 C LYS A1104 -10.075 -46.359 12.590 1.00 63.56 C ANISOU 2373 C LYS A1104 10659 6098 7394 3333 -145 -1371 C ATOM 2374 O LYS A1104 -10.646 -45.298 12.341 1.00 55.46 O ANISOU 2374 O LYS A1104 9821 5207 6046 3395 -379 -1516 O ATOM 2375 CB LYS A1104 -10.828 -48.399 11.353 1.00 66.73 C ANISOU 2375 CB LYS A1104 10882 6201 8271 3015 77 -1218 C ATOM 2376 CG LYS A1104 -10.717 -49.267 10.114 1.00 72.13 C ANISOU 2376 CG LYS A1104 11806 6403 9199 2767 163 -1299 C ATOM 2377 CD LYS A1104 -11.883 -50.234 10.014 1.00 76.78 C ANISOU 2377 CD LYS A1104 12121 7070 9982 2672 -50 -1118 C ATOM 2378 CE LYS A1104 -11.776 -51.097 8.768 1.00 79.29 C ANISOU 2378 CE LYS A1104 12811 6815 10500 2483 -90 -1278 C ATOM 2379 NZ LYS A1104 -10.533 -51.917 8.766 1.00 82.22 N ANISOU 2379 NZ LYS A1104 13196 6879 11164 2396 198 -1244 N ATOM 2380 N TYR A1105 -9.724 -46.719 13.821 1.00 55.40 N ANISOU 2380 N TYR A1105 9318 5316 6414 3509 -109 -1190 N ATOM 2381 CA TYR A1105 -9.953 -45.837 14.959 1.00 64.18 C ANISOU 2381 CA TYR A1105 10447 6820 7117 3942 -367 -1259 C ATOM 2382 C TYR A1105 -9.065 -44.601 14.870 1.00 57.10 C ANISOU 2382 C TYR A1105 9954 5616 6125 3804 -648 -1441 C ATOM 2383 O TYR A1105 -9.483 -43.501 15.227 1.00 58.77 O ANISOU 2383 O TYR A1105 10376 6015 5938 4034 -996 -1598 O ATOM 2384 CB TYR A1105 -9.705 -46.571 16.278 1.00 65.16 C ANISOU 2384 CB TYR A1105 10078 7368 7312 4043 -266 -938 C ATOM 2385 CG TYR A1105 -9.728 -45.661 17.487 1.00 74.98 C ANISOU 2385 CG TYR A1105 11451 8973 8066 4563 -559 -1054 C ATOM 2386 CD1 TYR A1105 -10.916 -45.093 17.929 1.00 82.39 C ANISOU 2386 CD1 TYR A1105 12403 10445 8455 5146 -699 -1139 C ATOM 2387 CD2 TYR A1105 -8.563 -45.367 18.183 1.00 78.51 C ANISOU 2387 CD2 TYR A1105 12033 9220 8579 4520 -732 -1068 C ATOM 2388 CE1 TYR A1105 -10.943 -44.256 19.031 1.00 87.70 C ANISOU 2388 CE1 TYR A1105 13262 11475 8585 5579 -992 -1261 C ATOM 2389 CE2 TYR A1105 -8.580 -44.533 19.287 1.00 82.42 C ANISOU 2389 CE2 TYR A1105 12759 9979 8579 5047 -1105 -1233 C ATOM 2390 CZ TYR A1105 -9.772 -43.981 19.707 1.00 88.47 C ANISOU 2390 CZ TYR A1105 13578 11309 8727 5561 -1224 -1351 C ATOM 2391 OH TYR A1105 -9.795 -43.150 20.805 1.00 95.36 O ANISOU 2391 OH TYR A1105 14742 12481 9009 6041 -1603 -1533 O ATOM 2392 N LEU A1106 -7.842 -44.797 14.389 1.00 56.06 N ANISOU 2392 N LEU A1106 9888 5023 6389 3432 -517 -1346 N ATOM 2393 CA LEU A1106 -6.882 -43.711 14.219 1.00 60.63 C ANISOU 2393 CA LEU A1106 10755 5264 7019 3257 -799 -1375 C ATOM 2394 C LEU A1106 -7.398 -42.639 13.264 1.00 57.28 C ANISOU 2394 C LEU A1106 10584 4800 6379 3151 -1000 -1519 C ATOM 2395 O LEU A1106 -7.363 -41.448 13.574 1.00 59.46 O ANISOU 2395 O LEU A1106 11106 5045 6441 3265 -1448 -1626 O ATOM 2396 CB LEU A1106 -5.547 -44.259 13.709 1.00 60.55 C ANISOU 2396 CB LEU A1106 10681 4808 7517 2921 -521 -1118 C ATOM 2397 CG LEU A1106 -4.541 -43.232 13.181 1.00 67.34 C ANISOU 2397 CG LEU A1106 11778 5256 8553 2695 -753 -1003 C ATOM 2398 CD1 LEU A1106 -4.019 -42.348 14.305 1.00 72.13 C ANISOU 2398 CD1 LEU A1106 12532 5751 9122 2810 -1332 -1004 C ATOM 2399 CD2 LEU A1106 -3.397 -43.921 12.452 1.00 65.93 C ANISOU 2399 CD2 LEU A1106 11478 4731 8841 2437 -330 -646 C ATOM 2400 N GLU A 219 -7.877 -43.073 12.104 1.00 58.89 N ANISOU 2400 N GLU A 219 10064 3907 8406 2226 -1308 -630 N ATOM 2401 CA GLU A 219 -8.355 -42.157 11.076 1.00 56.78 C ANISOU 2401 CA GLU A 219 9879 3724 7970 2159 -1134 -693 C ATOM 2402 C GLU A 219 -9.633 -41.446 11.507 1.00 52.39 C ANISOU 2402 C GLU A 219 9348 3315 7242 1918 -1291 -536 C ATOM 2403 O GLU A 219 -9.807 -40.258 11.239 1.00 50.42 O ANISOU 2403 O GLU A 219 9009 3214 6934 1872 -1155 -537 O ATOM 2404 CB GLU A 219 -8.582 -42.907 9.762 1.00 61.95 C ANISOU 2404 CB GLU A 219 10857 4206 8477 2182 -1086 -823 C ATOM 2405 CG GLU A 219 -7.326 -43.561 9.206 1.00 69.15 C ANISOU 2405 CG GLU A 219 11743 4961 9570 2421 -877 -1003 C ATOM 2406 CD GLU A 219 -7.591 -44.366 7.948 1.00 77.79 C ANISOU 2406 CD GLU A 219 13193 5874 10490 2436 -844 -1131 C ATOM 2407 OE1 GLU A 219 -8.699 -44.245 7.384 1.00 83.63 O ANISOU 2407 OE1 GLU A 219 14193 6626 10956 2262 -963 -1083 O ATOM 2408 OE2 GLU A 219 -6.692 -45.122 7.524 1.00 77.58 O ANISOU 2408 OE2 GLU A 219 13185 5683 10608 2621 -706 -1277 O ATOM 2409 N ARG A 220 -10.523 -42.170 12.177 1.00 52.61 N ANISOU 2409 N ARG A 220 9489 3299 7203 1760 -1565 -403 N ATOM 2410 CA ARG A 220 -11.770 -41.582 12.652 1.00 52.37 C ANISOU 2410 CA ARG A 220 9450 3396 7052 1517 -1699 -251 C ATOM 2411 C ARG A 220 -11.518 -40.559 13.755 1.00 49.14 C ANISOU 2411 C ARG A 220 8751 3177 6743 1499 -1653 -153 C ATOM 2412 O ARG A 220 -12.146 -39.500 13.782 1.00 45.66 O ANISOU 2412 O ARG A 220 8231 2882 6234 1380 -1606 -93 O ATOM 2413 CB ARG A 220 -12.726 -42.669 13.147 1.00 56.73 C ANISOU 2413 CB ARG A 220 10165 3850 7539 1342 -1972 -139 C ATOM 2414 CG ARG A 220 -13.407 -43.443 12.031 1.00 68.98 C ANISOU 2414 CG ARG A 220 12018 5251 8942 1279 -2064 -198 C ATOM 2415 CD ARG A 220 -14.371 -44.476 12.589 1.00 81.38 C ANISOU 2415 CD ARG A 220 13715 6734 10471 1088 -2336 -78 C ATOM 2416 NE ARG A 220 -15.056 -45.218 11.534 1.00 88.48 N ANISOU 2416 NE ARG A 220 14900 7489 11229 1017 -2455 -127 N ATOM 2417 CZ ARG A 220 -15.905 -46.217 11.755 1.00 94.32 C ANISOU 2417 CZ ARG A 220 15787 8125 11926 855 -2694 -46 C ATOM 2418 NH1 ARG A 220 -16.173 -46.598 12.997 1.00 96.81 N ANISOU 2418 NH1 ARG A 220 15999 8463 12320 744 -2817 85 N ATOM 2419 NH2 ARG A 220 -16.484 -46.837 10.736 1.00 97.04 N ANISOU 2419 NH2 ARG A 220 16393 8338 12140 798 -2813 -94 N ATOM 2420 N ALA A 221 -10.598 -40.877 14.660 1.00 46.93 N ANISOU 2420 N ALA A 221 8320 2887 6623 1616 -1678 -137 N ATOM 2421 CA ALA A 221 -10.226 -39.952 15.726 1.00 48.01 C ANISOU 2421 CA ALA A 221 8198 3195 6849 1610 -1649 -51 C ATOM 2422 C ALA A 221 -9.569 -38.706 15.144 1.00 44.56 C ANISOU 2422 C ALA A 221 7579 2884 6468 1727 -1395 -144 C ATOM 2423 O ALA A 221 -9.791 -37.591 15.620 1.00 41.58 O ANISOU 2423 O ALA A 221 7047 2679 6074 1653 -1351 -71 O ATOM 2424 CB ALA A 221 -9.297 -40.626 16.721 1.00 46.82 C ANISOU 2424 CB ALA A 221 7952 2985 6854 1715 -1756 -25 C ATOM 2425 N ARG A 222 -8.759 -38.908 14.111 1.00 45.64 N ANISOU 2425 N ARG A 222 7740 2929 6671 1904 -1214 -308 N ATOM 2426 CA ARG A 222 -8.099 -37.810 13.419 1.00 48.98 C ANISOU 2426 CA ARG A 222 8011 3455 7146 2007 -935 -418 C ATOM 2427 C ARG A 222 -9.125 -36.951 12.694 1.00 48.03 C ANISOU 2427 C ARG A 222 8020 3418 6811 1863 -885 -410 C ATOM 2428 O ARG A 222 -9.024 -35.725 12.676 1.00 47.55 O ANISOU 2428 O ARG A 222 7806 3514 6748 1853 -749 -409 O ATOM 2429 CB ARG A 222 -7.064 -38.349 12.430 1.00 55.19 C ANISOU 2429 CB ARG A 222 8820 4103 8048 2204 -722 -603 C ATOM 2430 CG ARG A 222 -6.235 -37.283 11.733 1.00 58.38 C ANISOU 2430 CG ARG A 222 9038 4607 8537 2302 -393 -729 C ATOM 2431 CD ARG A 222 -5.323 -37.911 10.692 1.00 64.10 C ANISOU 2431 CD ARG A 222 9805 5175 9374 2466 -158 -924 C ATOM 2432 NE ARG A 222 -4.524 -38.996 11.254 1.00 71.69 N ANISOU 2432 NE ARG A 222 10683 5991 10565 2609 -230 -925 N ATOM 2433 CZ ARG A 222 -3.797 -39.843 10.532 1.00 80.42 C ANISOU 2433 CZ ARG A 222 11842 6914 11799 2759 -77 -1078 C ATOM 2434 NH1 ARG A 222 -3.767 -39.736 9.211 1.00 83.37 N ANISOU 2434 NH1 ARG A 222 12360 7240 12077 2773 151 -1256 N ATOM 2435 NH2 ARG A 222 -3.101 -40.801 11.131 1.00 84.29 N ANISOU 2435 NH2 ARG A 222 12258 7272 12495 2894 -163 -1056 N ATOM 2436 N SER A 223 -10.117 -37.609 12.104 1.00 47.82 N ANISOU 2436 N SER A 223 8279 3282 6609 1745 -1014 -399 N ATOM 2437 CA SER A 223 -11.168 -36.925 11.363 1.00 46.73 C ANISOU 2437 CA SER A 223 8293 3193 6268 1591 -1014 -382 C ATOM 2438 C SER A 223 -12.030 -36.063 12.279 1.00 44.21 C ANISOU 2438 C SER A 223 7831 3034 5933 1420 -1124 -216 C ATOM 2439 O SER A 223 -12.445 -34.967 11.905 1.00 42.53 O ANISOU 2439 O SER A 223 7593 2929 5639 1354 -1043 -209 O ATOM 2440 CB SER A 223 -12.043 -37.940 10.625 1.00 50.30 C ANISOU 2440 CB SER A 223 9066 3483 6563 1487 -1176 -390 C ATOM 2441 OG SER A 223 -13.096 -37.297 9.931 1.00 56.46 O ANISOU 2441 OG SER A 223 9983 4305 7164 1322 -1216 -360 O ATOM 2442 N THR A 224 -12.295 -36.566 13.480 1.00 44.41 N ANISOU 2442 N THR A 224 7774 3071 6030 1342 -1299 -85 N ATOM 2443 CA THR A 224 -13.123 -35.849 14.443 1.00 42.25 C ANISOU 2443 CA THR A 224 7364 2945 5744 1166 -1380 76 C ATOM 2444 C THR A 224 -12.427 -34.580 14.931 1.00 36.69 C ANISOU 2444 C THR A 224 6408 2414 5119 1252 -1229 80 C ATOM 2445 O THR A 224 -13.055 -33.528 15.068 1.00 34.32 O ANISOU 2445 O THR A 224 6024 2247 4770 1145 -1198 149 O ATOM 2446 CB THR A 224 -13.478 -36.744 15.648 1.00 44.00 C ANISOU 2446 CB THR A 224 7584 3132 6003 1058 -1567 206 C ATOM 2447 OG1 THR A 224 -14.213 -37.885 15.191 1.00 44.44 O ANISOU 2447 OG1 THR A 224 7865 3033 5986 960 -1716 208 O ATOM 2448 CG2 THR A 224 -14.321 -35.982 16.658 1.00 48.01 C ANISOU 2448 CG2 THR A 224 7954 3794 6492 872 -1597 365 C ATOM 2449 N LEU A 225 -11.126 -34.682 15.183 1.00 36.24 N ANISOU 2449 N LEU A 225 6215 2354 5202 1440 -1142 5 N ATOM 2450 CA LEU A 225 -10.341 -33.533 15.620 1.00 34.81 C ANISOU 2450 CA LEU A 225 5774 2335 5117 1526 -1006 -3 C ATOM 2451 C LEU A 225 -10.256 -32.467 14.533 1.00 40.64 C ANISOU 2451 C LEU A 225 6500 3144 5796 1572 -794 -108 C ATOM 2452 O LEU A 225 -10.378 -31.275 14.817 1.00 40.83 O ANISOU 2452 O LEU A 225 6379 3328 5808 1534 -730 -65 O ATOM 2453 CB LEU A 225 -8.937 -33.972 16.040 1.00 48.16 C ANISOU 2453 CB LEU A 225 7304 3991 7004 1705 -969 -63 C ATOM 2454 CG LEU A 225 -8.824 -34.551 17.452 1.00 49.71 C ANISOU 2454 CG LEU A 225 7451 4181 7257 1656 -1175 63 C ATOM 2455 CD1 LEU A 225 -7.441 -35.135 17.697 1.00 50.25 C ANISOU 2455 CD1 LEU A 225 7393 4175 7526 1839 -1167 -6 C ATOM 2456 CD2 LEU A 225 -9.143 -33.480 18.484 1.00 48.37 C ANISOU 2456 CD2 LEU A 225 7136 4195 7048 1539 -1206 186 C ATOM 2457 N GLN A 226 -10.055 -32.893 13.291 1.00 41.55 N ANISOU 2457 N GLN A 226 6791 3139 5856 1646 -679 -249 N ATOM 2458 CA GLN A 226 -9.977 -31.954 12.176 1.00 43.01 C ANISOU 2458 CA GLN A 226 7025 3378 5938 1670 -460 -357 C ATOM 2459 C GLN A 226 -11.290 -31.201 11.995 1.00 39.58 C ANISOU 2459 C GLN A 226 6708 3002 5328 1488 -551 -264 C ATOM 2460 O GLN A 226 -11.295 -30.043 11.583 1.00 31.81 O ANISOU 2460 O GLN A 226 5681 2126 4278 1481 -407 -293 O ATOM 2461 CB GLN A 226 -9.604 -32.678 10.883 1.00 49.47 C ANISOU 2461 CB GLN A 226 8065 4044 6689 1749 -326 -517 C ATOM 2462 CG GLN A 226 -8.179 -33.204 10.860 1.00 62.72 C ANISOU 2462 CG GLN A 226 9579 5670 8583 1940 -162 -636 C ATOM 2463 CD GLN A 226 -7.855 -33.949 9.581 1.00 75.77 C ANISOU 2463 CD GLN A 226 11459 7166 10163 2010 -16 -797 C ATOM 2464 OE1 GLN A 226 -8.724 -34.154 8.733 1.00 80.47 O ANISOU 2464 OE1 GLN A 226 12369 7686 10520 1908 -71 -808 O ATOM 2465 NE2 GLN A 226 -6.600 -34.359 9.436 1.00 79.65 N ANISOU 2465 NE2 GLN A 226 11789 7602 10872 2174 162 -922 N ATOM 2466 N LYS A 227 -12.401 -31.861 12.309 1.00 38.83 N ANISOU 2466 N LYS A 227 6742 2836 5175 1328 -787 -149 N ATOM 2467 CA LYS A 227 -13.709 -31.221 12.234 1.00 35.22 C ANISOU 2467 CA LYS A 227 6337 2432 4614 1129 -897 -42 C ATOM 2468 C LYS A 227 -13.878 -30.191 13.346 1.00 32.21 C ANISOU 2468 C LYS A 227 5671 2263 4303 1061 -884 82 C ATOM 2469 O LYS A 227 -14.466 -29.130 13.133 1.00 31.00 O ANISOU 2469 O LYS A 227 5433 2259 4085 947 -831 116 O ATOM 2470 CB LYS A 227 -14.827 -32.262 12.303 1.00 40.72 C ANISOU 2470 CB LYS A 227 7182 3021 5270 953 -1129 46 C ATOM 2471 CG LYS A 227 -14.959 -33.108 11.049 1.00 50.21 C ANISOU 2471 CG LYS A 227 8679 4049 6349 960 -1165 -64 C ATOM 2472 CD LYS A 227 -16.097 -34.107 11.175 1.00 59.57 C ANISOU 2472 CD LYS A 227 9978 5143 7512 777 -1411 29 C ATOM 2473 CE LYS A 227 -16.257 -34.924 9.905 1.00 68.68 C ANISOU 2473 CE LYS A 227 11443 6127 8524 781 -1474 -77 C ATOM 2474 NZ LYS A 227 -17.372 -35.904 10.016 1.00 74.98 N ANISOU 2474 NZ LYS A 227 12338 6838 9314 599 -1730 12 N ATOM 2475 N GLU A 228 -13.364 -30.507 14.532 1.00 30.75 N ANISOU 2475 N GLU A 228 5340 2103 4240 1118 -936 147 N ATOM 2476 CA GLU A 228 -13.400 -29.573 15.653 1.00 31.84 C ANISOU 2476 CA GLU A 228 5221 2453 4422 1050 -909 253 C ATOM 2477 C GLU A 228 -12.540 -28.348 15.369 1.00 30.10 C ANISOU 2477 C GLU A 228 4809 2406 4221 1145 -693 164 C ATOM 2478 O GLU A 228 -12.913 -27.226 15.710 1.00 31.24 O ANISOU 2478 O GLU A 228 4800 2737 4334 1048 -635 223 O ATOM 2479 CB GLU A 228 -12.930 -30.245 16.944 1.00 35.81 C ANISOU 2479 CB GLU A 228 5658 2925 5023 1083 -1023 331 C ATOM 2480 CG GLU A 228 -13.874 -31.301 17.487 1.00 47.13 C ANISOU 2480 CG GLU A 228 7220 4272 6416 915 -1188 443 C ATOM 2481 CD GLU A 228 -13.467 -31.781 18.867 1.00 54.81 C ANISOU 2481 CD GLU A 228 8131 5259 7435 903 -1270 526 C ATOM 2482 OE1 GLU A 228 -13.000 -32.933 18.984 1.00 56.90 O ANISOU 2482 OE1 GLU A 228 8491 5389 7740 962 -1360 496 O ATOM 2483 OE2 GLU A 228 -13.614 -31.004 19.835 1.00 55.96 O ANISOU 2483 OE2 GLU A 228 8155 5542 7567 832 -1250 620 O ATOM 2484 N VAL A 229 -11.384 -28.575 14.753 1.00 31.01 N ANISOU 2484 N VAL A 229 4930 2451 4403 1335 -566 22 N ATOM 2485 CA VAL A 229 -10.508 -27.483 14.343 1.00 30.29 C ANISOU 2485 CA VAL A 229 4665 2499 4343 1418 -335 -71 C ATOM 2486 C VAL A 229 -11.229 -26.583 13.351 1.00 27.25 C ANISOU 2486 C VAL A 229 4373 2194 3788 1298 -230 -93 C ATOM 2487 O VAL A 229 -11.205 -25.359 13.474 1.00 25.27 O ANISOU 2487 O VAL A 229 3959 2122 3519 1243 -131 -71 O ATOM 2488 CB VAL A 229 -9.205 -28.002 13.705 1.00 33.64 C ANISOU 2488 CB VAL A 229 5092 2803 4887 1639 -179 -234 C ATOM 2489 CG1 VAL A 229 -8.403 -26.850 13.117 1.00 33.17 C ANISOU 2489 CG1 VAL A 229 4872 2880 4850 1691 97 -329 C ATOM 2490 CG2 VAL A 229 -8.382 -28.760 14.724 1.00 36.62 C ANISOU 2490 CG2 VAL A 229 5314 3129 5471 1735 -293 -204 C ATOM 2491 N HIS A 230 -11.880 -27.203 12.373 1.00 31.80 N ANISOU 2491 N HIS A 230 5231 2615 4237 1254 -281 -135 N ATOM 2492 CA HIS A 230 -12.597 -26.471 11.337 1.00 31.99 C ANISOU 2492 CA HIS A 230 5402 2664 4090 1140 -235 -156 C ATOM 2493 C HIS A 230 -13.750 -25.663 11.929 1.00 28.56 C ANISOU 2493 C HIS A 230 4841 2373 3636 954 -363 -12 C ATOM 2494 O HIS A 230 -13.988 -24.521 11.535 1.00 25.70 O ANISOU 2494 O HIS A 230 4432 2129 3205 888 -285 -13 O ATOM 2495 CB HIS A 230 -13.114 -27.435 10.267 1.00 40.78 C ANISOU 2495 CB HIS A 230 6878 3544 5072 1121 -328 -218 C ATOM 2496 CG HIS A 230 -13.653 -26.754 9.048 1.00 52.43 C ANISOU 2496 CG HIS A 230 8569 4998 6355 1027 -290 -263 C ATOM 2497 ND1 HIS A 230 -14.996 -26.504 8.867 1.00 55.81 N ANISOU 2497 ND1 HIS A 230 9081 5414 6712 841 -506 -164 N ATOM 2498 CD2 HIS A 230 -13.029 -26.271 7.947 1.00 57.44 C ANISOU 2498 CD2 HIS A 230 9363 5605 6855 1087 -69 -392 C ATOM 2499 CE1 HIS A 230 -15.177 -25.896 7.708 1.00 58.57 C ANISOU 2499 CE1 HIS A 230 9647 5720 6887 795 -457 -228 C ATOM 2500 NE2 HIS A 230 -13.999 -25.742 7.131 1.00 59.48 N ANISOU 2500 NE2 HIS A 230 9834 5827 6939 936 -181 -365 N ATOM 2501 N ALA A 231 -14.459 -26.261 12.881 1.00 26.74 N ANISOU 2501 N ALA A 231 4561 2123 3476 870 -548 110 N ATOM 2502 CA ALA A 231 -15.571 -25.586 13.541 1.00 29.29 C ANISOU 2502 CA ALA A 231 4744 2571 3812 701 -638 242 C ATOM 2503 C ALA A 231 -15.072 -24.441 14.420 1.00 27.68 C ANISOU 2503 C ALA A 231 4271 2583 3662 724 -511 273 C ATOM 2504 O ALA A 231 -15.721 -23.400 14.527 1.00 27.22 O ANISOU 2504 O ALA A 231 4103 2653 3585 625 -492 322 O ATOM 2505 CB ALA A 231 -16.379 -26.578 14.365 1.00 29.67 C ANISOU 2505 CB ALA A 231 4818 2532 3924 600 -823 363 C ATOM 2506 N ALA A 232 -13.917 -24.638 15.049 1.00 26.97 N ANISOU 2506 N ALA A 232 4080 2516 3651 857 -445 242 N ATOM 2507 CA ALA A 232 -13.324 -23.602 15.885 1.00 26.20 C ANISOU 2507 CA ALA A 232 3749 2598 3607 883 -352 264 C ATOM 2508 C ALA A 232 -12.844 -22.436 15.026 1.00 28.38 C ANISOU 2508 C ALA A 232 3970 2973 3839 915 -174 175 C ATOM 2509 O ALA A 232 -12.930 -21.277 15.434 1.00 26.52 O ANISOU 2509 O ALA A 232 3583 2893 3599 863 -121 211 O ATOM 2510 CB ALA A 232 -12.176 -24.169 16.708 1.00 23.99 C ANISOU 2510 CB ALA A 232 3384 2282 3448 1019 -374 253 C ATOM 2511 N LYS A 233 -12.345 -22.749 13.834 1.00 25.80 N ANISOU 2511 N LYS A 233 3791 2544 3469 995 -74 58 N ATOM 2512 CA LYS A 233 -11.891 -21.718 12.908 1.00 29.66 C ANISOU 2512 CA LYS A 233 4280 3100 3889 1008 115 -27 C ATOM 2513 C LYS A 233 -13.055 -20.861 12.421 1.00 26.67 C ANISOU 2513 C LYS A 233 3980 2771 3383 855 58 24 C ATOM 2514 O LYS A 233 -12.930 -19.642 12.315 1.00 25.57 O ANISOU 2514 O LYS A 233 3745 2756 3215 821 154 22 O ATOM 2515 CB LYS A 233 -11.162 -22.342 11.716 1.00 34.27 C ANISOU 2515 CB LYS A 233 5057 3536 4427 1118 261 -167 C ATOM 2516 CG LYS A 233 -9.760 -22.838 12.038 1.00 46.13 C ANISOU 2516 CG LYS A 233 6413 5010 6106 1298 386 -247 C ATOM 2517 CD LYS A 233 -9.043 -23.318 10.785 1.00 51.89 C ANISOU 2517 CD LYS A 233 7329 5596 6791 1410 597 -404 C ATOM 2518 CE LYS A 233 -7.596 -23.679 11.080 1.00 54.60 C ANISOU 2518 CE LYS A 233 7462 5916 7369 1599 750 -493 C ATOM 2519 NZ LYS A 233 -6.866 -24.080 9.846 1.00 59.31 N ANISOU 2519 NZ LYS A 233 8181 6424 7930 1640 967 -648 N ATOM 2520 N SER A 234 -14.185 -21.499 12.131 1.00 25.57 N ANISOU 2520 N SER A 234 4008 2520 3187 763 -118 71 N ATOM 2521 CA SER A 234 -15.381 -20.777 11.704 1.00 26.63 C ANISOU 2521 CA SER A 234 4195 2674 3250 621 -223 126 C ATOM 2522 C SER A 234 -15.846 -19.803 12.783 1.00 24.89 C ANISOU 2522 C SER A 234 3713 2630 3114 553 -237 223 C ATOM 2523 O SER A 234 -16.232 -18.672 12.488 1.00 26.60 O ANISOU 2523 O SER A 234 3888 2923 3294 494 -220 232 O ATOM 2524 CB SER A 234 -16.507 -21.753 11.359 1.00 30.34 C ANISOU 2524 CB SER A 234 4845 2978 3703 528 -442 172 C ATOM 2525 OG SER A 234 -16.119 -22.631 10.318 1.00 33.05 O ANISOU 2525 OG SER A 234 5476 3137 3943 589 -437 73 O ATOM 2526 N ALA A 235 -15.802 -20.247 14.033 1.00 25.30 N ANISOU 2526 N ALA A 235 3616 2729 3266 563 -270 292 N ATOM 2527 CA ALA A 235 -16.207 -19.411 15.154 1.00 25.59 C ANISOU 2527 CA ALA A 235 3443 2918 3363 504 -262 376 C ATOM 2528 C ALA A 235 -15.233 -18.251 15.363 1.00 25.42 C ANISOU 2528 C ALA A 235 3286 3037 3336 570 -113 331 C ATOM 2529 O ALA A 235 -15.643 -17.136 15.692 1.00 22.44 O ANISOU 2529 O ALA A 235 2796 2771 2959 514 -88 364 O ATOM 2530 CB ALA A 235 -16.319 -20.244 16.415 1.00 27.34 C ANISOU 2530 CB ALA A 235 3606 3128 3653 491 -326 459 C ATOM 2531 N ALA A 236 -13.946 -18.516 15.162 1.00 21.99 N ANISOU 2531 N ALA A 236 2854 2583 2918 688 -15 253 N ATOM 2532 CA ALA A 236 -12.918 -17.492 15.326 1.00 20.69 C ANISOU 2532 CA ALA A 236 2544 2535 2782 744 122 210 C ATOM 2533 C ALA A 236 -13.018 -16.421 14.243 1.00 19.80 C ANISOU 2533 C ALA A 236 2493 2454 2576 701 219 161 C ATOM 2534 O ALA A 236 -12.753 -15.245 14.497 1.00 23.32 O ANISOU 2534 O ALA A 236 2818 3015 3027 681 285 167 O ATOM 2535 CB ALA A 236 -11.533 -18.124 15.319 1.00 19.92 C ANISOU 2535 CB ALA A 236 2404 2388 2776 882 202 137 C ATOM 2536 N ILE A 237 -13.390 -16.837 13.035 1.00 16.74 N ANISOU 2536 N ILE A 237 2324 1947 2090 682 211 114 N ATOM 2537 CA ILE A 237 -13.592 -15.912 11.922 1.00 17.86 C ANISOU 2537 CA ILE A 237 2597 2081 2108 624 269 76 C ATOM 2538 C ILE A 237 -14.699 -14.908 12.243 1.00 20.08 C ANISOU 2538 C ILE A 237 2805 2437 2388 519 152 157 C ATOM 2539 O ILE A 237 -14.553 -13.709 12.002 1.00 18.60 O ANISOU 2539 O ILE A 237 2587 2320 2159 489 217 148 O ATOM 2540 CB ILE A 237 -13.938 -16.670 10.623 1.00 21.08 C ANISOU 2540 CB ILE A 237 3314 2310 2384 610 231 21 C ATOM 2541 CG1 ILE A 237 -12.699 -17.390 10.084 1.00 27.72 C ANISOU 2541 CG1 ILE A 237 4246 3074 3212 729 422 -90 C ATOM 2542 CG2 ILE A 237 -14.489 -15.723 9.568 1.00 20.94 C ANISOU 2542 CG2 ILE A 237 3480 2258 2219 517 207 13 C ATOM 2543 CD1 ILE A 237 -12.981 -18.287 8.893 1.00 31.19 C ANISOU 2543 CD1 ILE A 237 5031 3314 3505 728 393 -157 C ATOM 2544 N AILE A 238 -15.798 -15.396 12.803 0.53 18.76 N ANISOU 2544 N AILE A 238 2600 2246 2281 462 -12 234 N ATOM 2545 N BILE A 238 -15.805 -15.421 12.776 0.47 18.81 N ANISOU 2545 N BILE A 238 2613 2249 2286 462 -14 233 N ATOM 2546 CA AILE A 238 -16.907 -14.527 13.181 0.53 19.60 C ANISOU 2546 CA AILE A 238 2601 2414 2434 375 -108 305 C ATOM 2547 CA BILE A 238 -16.922 -14.596 13.229 0.47 20.24 C ANISOU 2547 CA BILE A 238 2678 2492 2519 376 -111 307 C ATOM 2548 C AILE A 238 -16.498 -13.563 14.295 0.53 18.64 C ANISOU 2548 C AILE A 238 2263 2452 2369 397 -12 328 C ATOM 2549 C BILE A 238 -16.458 -13.573 14.258 0.47 18.64 C ANISOU 2549 C BILE A 238 2268 2450 2366 399 -9 325 C ATOM 2550 O AILE A 238 -16.901 -12.397 14.306 0.53 16.85 O ANISOU 2550 O AILE A 238 1973 2286 2143 359 -15 342 O ATOM 2551 O BILE A 238 -16.787 -12.387 14.178 0.47 17.61 O ANISOU 2551 O BILE A 238 2087 2376 2227 363 -5 333 O ATOM 2552 CB AILE A 238 -18.121 -15.356 13.620 0.53 23.79 C ANISOU 2552 CB AILE A 238 3104 2880 3056 306 -266 382 C ATOM 2553 CB BILE A 238 -18.040 -15.458 13.851 0.47 23.49 C ANISOU 2553 CB BILE A 238 3040 2856 3031 314 -254 388 C ATOM 2554 CG1AILE A 238 -18.554 -16.271 12.474 0.53 27.93 C ANISOU 2554 CG1AILE A 238 3865 3224 3522 273 -399 359 C ATOM 2555 CG1BILE A 238 -18.671 -16.368 12.797 0.47 27.53 C ANISOU 2555 CG1BILE A 238 3764 3190 3505 267 -405 379 C ATOM 2556 CG2AILE A 238 -19.267 -14.456 14.051 0.53 23.81 C ANISOU 2556 CG2AILE A 238 2953 2940 3152 229 -333 446 C ATOM 2557 CG2BILE A 238 -19.107 -14.578 14.483 0.47 23.54 C ANISOU 2557 CG2BILE A 238 2872 2937 3134 242 -299 456 C ATOM 2558 CD1AILE A 238 -19.686 -17.181 12.824 0.53 30.48 C ANISOU 2558 CD1AILE A 238 4163 3463 3954 191 -565 437 C ATOM 2559 CD1BILE A 238 -19.621 -15.649 11.871 0.47 24.93 C ANISOU 2559 CD1BILE A 238 3517 2794 3160 186 -545 388 C ATOM 2560 N ALA A 239 -15.684 -14.053 15.224 1.00 17.22 N ANISOU 2560 N ALA A 239 1987 2320 2234 460 51 331 N ATOM 2561 CA ALA A 239 -15.148 -13.217 16.286 1.00 18.63 C ANISOU 2561 CA ALA A 239 2003 2627 2450 482 119 348 C ATOM 2562 C ALA A 239 -14.206 -12.155 15.729 1.00 18.92 C ANISOU 2562 C ALA A 239 2022 2716 2449 509 231 286 C ATOM 2563 O ALA A 239 -14.231 -11.000 16.154 1.00 19.31 O ANISOU 2563 O ALA A 239 1982 2853 2501 483 254 299 O ATOM 2564 CB ALA A 239 -14.431 -14.075 17.300 1.00 21.97 C ANISOU 2564 CB ALA A 239 2370 3052 2926 541 114 367 C ATOM 2565 N GLY A 240 -13.376 -12.557 14.773 1.00 18.81 N ANISOU 2565 N GLY A 240 2104 2640 2404 556 315 216 N ATOM 2566 CA GLY A 240 -12.446 -11.642 14.139 1.00 19.96 C ANISOU 2566 CA GLY A 240 2244 2821 2519 565 457 158 C ATOM 2567 C GLY A 240 -13.157 -10.569 13.338 1.00 18.05 C ANISOU 2567 C GLY A 240 2112 2574 2174 481 437 163 C ATOM 2568 O GLY A 240 -12.753 -9.407 13.348 1.00 17.34 O ANISOU 2568 O GLY A 240 1964 2550 2073 455 504 157 O ATOM 2569 N LEU A 241 -14.220 -10.961 12.641 1.00 13.21 N ANISOU 2569 N LEU A 241 1663 1863 1495 434 320 178 N ATOM 2570 CA LEU A 241 -15.000 -10.022 11.842 1.00 17.10 C ANISOU 2570 CA LEU A 241 2280 2314 1903 355 244 191 C ATOM 2571 C LEU A 241 -15.689 -8.972 12.712 1.00 16.96 C ANISOU 2571 C LEU A 241 2092 2388 1963 324 169 247 C ATOM 2572 O LEU A 241 -15.802 -7.813 12.316 1.00 16.48 O ANISOU 2572 O LEU A 241 2070 2334 1858 284 161 246 O ATOM 2573 CB LEU A 241 -16.039 -10.765 11.002 1.00 20.61 C ANISOU 2573 CB LEU A 241 2925 2613 2294 310 79 202 C ATOM 2574 CG LEU A 241 -15.507 -11.445 9.740 1.00 29.75 C ANISOU 2574 CG LEU A 241 4364 3638 3303 319 146 131 C ATOM 2575 CD1 LEU A 241 -16.624 -12.179 9.017 1.00 33.49 C ANISOU 2575 CD1 LEU A 241 5048 3950 3728 263 -71 151 C ATOM 2576 CD2 LEU A 241 -14.849 -10.422 8.825 1.00 33.71 C ANISOU 2576 CD2 LEU A 241 5018 4128 3661 286 281 86 C ATOM 2577 N PHE A 242 -16.154 -9.384 13.887 1.00 16.10 N ANISOU 2577 N PHE A 242 1818 2334 1964 341 123 294 N ATOM 2578 CA PHE A 242 -16.736 -8.446 14.840 1.00 15.67 C ANISOU 2578 CA PHE A 242 1608 2364 1981 326 98 333 C ATOM 2579 C PHE A 242 -15.699 -7.391 15.211 1.00 12.69 C ANISOU 2579 C PHE A 242 1165 2079 1579 346 207 306 C ATOM 2580 O PHE A 242 -15.987 -6.194 15.213 1.00 15.40 O ANISOU 2580 O PHE A 242 1488 2447 1917 321 191 309 O ATOM 2581 CB PHE A 242 -17.237 -9.170 16.097 1.00 13.01 C ANISOU 2581 CB PHE A 242 1144 2065 1736 334 81 384 C ATOM 2582 CG PHE A 242 -17.877 -8.255 17.108 1.00 16.84 C ANISOU 2582 CG PHE A 242 1494 2624 2282 322 94 413 C ATOM 2583 CD1 PHE A 242 -17.111 -7.621 18.076 1.00 18.56 C ANISOU 2583 CD1 PHE A 242 1722 2874 2457 315 159 370 C ATOM 2584 CD2 PHE A 242 -19.243 -8.022 17.084 1.00 14.71 C ANISOU 2584 CD2 PHE A 242 1168 2316 2106 281 20 445 C ATOM 2585 CE1 PHE A 242 -17.697 -6.768 19.001 1.00 18.23 C ANISOU 2585 CE1 PHE A 242 1675 2825 2428 280 165 351 C ATOM 2586 CE2 PHE A 242 -19.835 -7.174 18.006 1.00 17.15 C ANISOU 2586 CE2 PHE A 242 1439 2630 2449 254 61 414 C ATOM 2587 CZ PHE A 242 -19.059 -6.547 18.966 1.00 17.37 C ANISOU 2587 CZ PHE A 242 1513 2688 2397 257 137 366 C ATOM 2588 N ALA A 243 -14.490 -7.847 15.520 1.00 14.61 N ANISOU 2588 N ALA A 243 1367 2358 1828 393 303 280 N ATOM 2589 CA ALA A 243 -13.404 -6.947 15.882 1.00 16.15 C ANISOU 2589 CA ALA A 243 1506 2598 2031 384 370 247 C ATOM 2590 C ALA A 243 -13.085 -5.984 14.743 1.00 14.65 C ANISOU 2590 C ALA A 243 1390 2411 1766 358 453 225 C ATOM 2591 O ALA A 243 -12.989 -4.779 14.955 1.00 15.82 O ANISOU 2591 O ALA A 243 1517 2583 1910 316 442 224 O ATOM 2592 CB ALA A 243 -12.163 -7.741 16.274 1.00 14.93 C ANISOU 2592 CB ALA A 243 1323 2412 1938 408 401 203 C ATOM 2593 N ALEU A 244 -12.934 -6.523 13.537 0.52 14.79 N ANISOU 2593 N ALEU A 244 1568 2344 1709 349 502 190 N ATOM 2594 N BLEU A 244 -12.930 -6.518 13.535 0.48 14.78 N ANISOU 2594 N BLEU A 244 1566 2343 1708 349 503 190 N ATOM 2595 CA ALEU A 244 -12.601 -5.719 12.366 0.52 15.15 C ANISOU 2595 CA ALEU A 244 1771 2341 1645 289 581 161 C ATOM 2596 CA BLEU A 244 -12.592 -5.698 12.375 0.48 15.10 C ANISOU 2596 CA BLEU A 244 1763 2336 1639 289 582 162 C ATOM 2597 C ALEU A 244 -13.651 -4.647 12.079 0.52 16.22 C ANISOU 2597 C ALEU A 244 1995 2443 1724 226 444 197 C ATOM 2598 C BLEU A 244 -13.654 -4.643 12.069 0.48 16.19 C ANISOU 2598 C BLEU A 244 1993 2438 1719 225 444 197 C ATOM 2599 O ALEU A 244 -13.316 -3.529 11.685 0.52 17.58 O ANISOU 2599 O ALEU A 244 2226 2613 1839 172 485 194 O ATOM 2600 O BLEU A 244 -13.329 -3.532 11.648 0.48 17.53 O ANISOU 2600 O BLEU A 244 2227 2604 1830 171 485 194 O ATOM 2601 CB ALEU A 244 -12.429 -6.618 11.137 0.52 16.84 C ANISOU 2601 CB ALEU A 244 2203 2443 1754 289 652 115 C ATOM 2602 CB BLEU A 244 -12.376 -6.579 11.143 0.48 17.34 C ANISOU 2602 CB BLEU A 244 2262 2509 1819 289 660 114 C ATOM 2603 CG ALEU A 244 -12.087 -5.920 9.818 0.52 16.83 C ANISOU 2603 CG ALEU A 244 2440 2363 1592 214 759 84 C ATOM 2604 CG BLEU A 244 -11.045 -7.328 11.059 0.48 21.16 C ANISOU 2604 CG BLEU A 244 2682 3002 2357 352 863 53 C ATOM 2605 CD1ALEU A 244 -10.727 -5.246 9.902 0.52 17.10 C ANISOU 2605 CD1ALEU A 244 2357 2468 1671 202 980 55 C ATOM 2606 CD1BLEU A 244 -10.965 -8.125 9.769 0.48 19.33 C ANISOU 2606 CD1BLEU A 244 2716 2639 1991 353 955 -5 C ATOM 2607 CD2ALEU A 244 -12.137 -6.899 8.652 0.52 17.70 C ANISOU 2607 CD2ALEU A 244 2824 2336 1564 214 806 36 C ATOM 2608 CD2BLEU A 244 -9.879 -6.358 11.165 0.48 28.06 C ANISOU 2608 CD2BLEU A 244 3429 3937 3295 306 979 26 C ATOM 2609 N CYS A 245 -14.919 -4.988 12.283 1.00 11.78 N ANISOU 2609 N CYS A 245 1431 1843 1200 230 276 233 N ATOM 2610 CA CYS A 245 -16.013 -4.069 11.976 1.00 11.69 C ANISOU 2610 CA CYS A 245 1481 1776 1185 186 119 263 C ATOM 2611 C CYS A 245 -16.208 -2.975 13.029 1.00 12.58 C ANISOU 2611 C CYS A 245 1417 1975 1387 201 105 282 C ATOM 2612 O CYS A 245 -16.647 -1.871 12.704 1.00 12.02 O ANISOU 2612 O CYS A 245 1403 1862 1302 170 23 291 O ATOM 2613 CB CYS A 245 -17.319 -4.847 11.792 1.00 15.25 C ANISOU 2613 CB CYS A 245 1958 2141 1696 182 -60 294 C ATOM 2614 SG CYS A 245 -17.391 -5.827 10.267 1.00 24.69 S ANISOU 2614 SG CYS A 245 3464 3171 2745 141 -125 272 S ATOM 2615 N TRP A 246 -15.876 -3.271 14.281 1.00 12.12 N ANISOU 2615 N TRP A 246 1175 2021 1410 249 174 286 N ATOM 2616 CA TRP A 246 -16.121 -2.327 15.371 1.00 14.59 C ANISOU 2616 CA TRP A 246 1356 2401 1787 267 165 296 C ATOM 2617 C TRP A 246 -14.902 -1.507 15.789 1.00 15.09 C ANISOU 2617 C TRP A 246 1381 2530 1821 259 258 275 C ATOM 2618 O TRP A 246 -15.048 -0.425 16.357 1.00 12.67 O ANISOU 2618 O TRP A 246 1037 2247 1531 257 234 275 O ATOM 2619 CB TRP A 246 -16.666 -3.069 16.594 1.00 9.28 C ANISOU 2619 CB TRP A 246 575 1755 1197 295 161 308 C ATOM 2620 CG TRP A 246 -18.123 -3.385 16.482 1.00 11.53 C ANISOU 2620 CG TRP A 246 813 1995 1572 299 70 341 C ATOM 2621 CD1 TRP A 246 -18.680 -4.564 16.085 1.00 13.94 C ANISOU 2621 CD1 TRP A 246 1131 2251 1914 290 14 368 C ATOM 2622 CD2 TRP A 246 -19.212 -2.497 16.754 1.00 14.17 C ANISOU 2622 CD2 TRP A 246 1111 2280 1992 291 11 327 C ATOM 2623 NE1 TRP A 246 -20.051 -4.468 16.101 1.00 14.74 N ANISOU 2623 NE1 TRP A 246 1158 2298 2144 278 -83 394 N ATOM 2624 CE2 TRP A 246 -20.403 -3.207 16.507 1.00 13.95 C ANISOU 2624 CE2 TRP A 246 1036 2189 2076 280 -75 353 C ATOM 2625 CE3 TRP A 246 -19.295 -1.170 17.186 1.00 13.65 C ANISOU 2625 CE3 TRP A 246 1041 2210 1935 298 19 292 C ATOM 2626 CZ2 TRP A 246 -21.662 -2.636 16.680 1.00 14.76 C ANISOU 2626 CZ2 TRP A 246 1077 2229 2303 279 -135 328 C ATOM 2627 CZ3 TRP A 246 -20.545 -0.604 17.356 1.00 10.71 C ANISOU 2627 CZ3 TRP A 246 611 1776 1682 310 -39 271 C ATOM 2628 CH2 TRP A 246 -21.711 -1.335 17.101 1.00 11.30 C ANISOU 2628 CH2 TRP A 246 629 1796 1870 303 -109 282 C ATOM 2629 N ALEU A 247 -13.707 -2.023 15.518 0.80 16.34 N ANISOU 2629 N ALEU A 247 1554 2695 1958 251 352 251 N ATOM 2630 N BLEU A 247 -13.712 -2.026 15.505 0.20 16.12 N ANISOU 2630 N BLEU A 247 1527 2668 1930 251 352 251 N ATOM 2631 CA ALEU A 247 -12.473 -1.343 15.919 0.80 17.26 C ANISOU 2631 CA ALEU A 247 1660 2795 2104 210 384 211 C ATOM 2632 CA BLEU A 247 -12.467 -1.370 15.899 0.20 16.87 C ANISOU 2632 CA BLEU A 247 1611 2745 2054 210 386 211 C ATOM 2633 C ALEU A 247 -12.288 0.067 15.339 0.80 16.27 C ANISOU 2633 C ALEU A 247 1563 2701 1919 163 426 228 C ATOM 2634 C BLEU A 247 -12.284 0.051 15.336 0.20 16.59 C ANISOU 2634 C BLEU A 247 1603 2740 1959 163 426 228 C ATOM 2635 O ALEU A 247 -11.811 0.950 16.051 0.80 16.56 O ANISOU 2635 O ALEU A 247 1558 2743 1992 141 400 218 O ATOM 2636 O BLEU A 247 -11.811 0.926 16.060 0.20 16.37 O ANISOU 2636 O BLEU A 247 1532 2718 1968 141 399 217 O ATOM 2637 CB ALEU A 247 -11.250 -2.197 15.562 0.80 17.80 C ANISOU 2637 CB ALEU A 247 1721 2831 2211 204 472 167 C ATOM 2638 CB BLEU A 247 -11.268 -2.240 15.502 0.20 17.64 C ANISOU 2638 CB BLEU A 247 1705 2811 2188 205 475 167 C ATOM 2639 CG ALEU A 247 -10.840 -3.252 16.595 0.80 17.69 C ANISOU 2639 CG ALEU A 247 1648 2793 2280 236 421 148 C ATOM 2640 CG BLEU A 247 -9.925 -1.905 16.154 0.20 16.39 C ANISOU 2640 CG BLEU A 247 1467 2638 2122 177 492 126 C ATOM 2641 CD1ALEU A 247 -9.657 -4.073 16.094 0.80 18.81 C ANISOU 2641 CD1ALEU A 247 1750 2915 2483 246 513 97 C ATOM 2642 CD1BLEU A 247 -10.067 -1.826 17.666 0.20 16.27 C ANISOU 2642 CD1BLEU A 247 1411 2626 2146 198 378 141 C ATOM 2643 CD2ALEU A 247 -10.528 -2.609 17.939 0.80 17.94 C ANISOU 2643 CD2ALEU A 247 1635 2829 2351 226 346 150 C ATOM 2644 CD2BLEU A 247 -8.872 -2.932 15.770 0.20 18.97 C ANISOU 2644 CD2BLEU A 247 1747 2943 2517 189 577 72 C ATOM 2645 N PRO A 248 -12.641 0.290 14.055 1.00 16.55 N ANISOU 2645 N PRO A 248 1755 2679 1855 120 440 237 N ATOM 2646 CA PRO A 248 -12.496 1.666 13.555 1.00 15.40 C ANISOU 2646 CA PRO A 248 1714 2489 1647 44 427 244 C ATOM 2647 C PRO A 248 -13.244 2.728 14.369 1.00 12.98 C ANISOU 2647 C PRO A 248 1361 2186 1384 64 296 256 C ATOM 2648 O PRO A 248 -12.656 3.771 14.650 1.00 15.89 O ANISOU 2648 O PRO A 248 1719 2566 1753 21 309 256 O ATOM 2649 CB PRO A 248 -13.065 1.578 12.138 1.00 15.70 C ANISOU 2649 CB PRO A 248 1995 2408 1561 -5 388 250 C ATOM 2650 CG PRO A 248 -12.753 0.198 11.718 1.00 15.35 C ANISOU 2650 CG PRO A 248 1971 2362 1498 23 483 227 C ATOM 2651 CD PRO A 248 -12.992 -0.629 12.951 1.00 15.39 C ANISOU 2651 CD PRO A 248 1761 2453 1633 114 448 230 C ATOM 2652 N LEU A 249 -14.491 2.463 14.750 1.00 12.11 N ANISOU 2652 N LEU A 249 1217 2059 1324 125 185 263 N ATOM 2653 CA LEU A 249 -15.238 3.383 15.607 1.00 11.42 C ANISOU 2653 CA LEU A 249 1068 1971 1300 165 99 260 C ATOM 2654 C LEU A 249 -14.505 3.638 16.922 1.00 14.03 C ANISOU 2654 C LEU A 249 1281 2391 1659 186 162 246 C ATOM 2655 O LEU A 249 -14.374 4.780 17.361 1.00 13.13 O ANISOU 2655 O LEU A 249 1182 2264 1541 175 130 234 O ATOM 2656 CB LEU A 249 -16.639 2.838 15.899 1.00 13.32 C ANISOU 2656 CB LEU A 249 1240 2188 1632 231 19 267 C ATOM 2657 CG LEU A 249 -17.767 3.169 14.919 1.00 14.88 C ANISOU 2657 CG LEU A 249 1532 2261 1862 224 -137 280 C ATOM 2658 CD1 LEU A 249 -19.024 2.398 15.286 1.00 13.37 C ANISOU 2658 CD1 LEU A 249 1213 2056 1812 280 -194 290 C ATOM 2659 CD2 LEU A 249 -18.042 4.659 14.920 1.00 13.90 C ANISOU 2659 CD2 LEU A 249 1455 2071 1754 226 -223 270 C ATOM 2660 N HIS A 250 -14.022 2.568 17.545 1.00 10.74 N ANISOU 2660 N HIS A 250 770 2045 1267 214 227 248 N ATOM 2661 CA HIS A 250 -13.351 2.685 18.835 1.00 14.16 C ANISOU 2661 CA HIS A 250 1197 2464 1720 208 216 219 C ATOM 2662 C HIS A 250 -12.025 3.433 18.713 1.00 15.70 C ANISOU 2662 C HIS A 250 1359 2694 1913 156 246 222 C ATOM 2663 O HIS A 250 -11.667 4.229 19.582 1.00 13.34 O ANISOU 2663 O HIS A 250 1024 2430 1616 152 214 222 O ATOM 2664 CB HIS A 250 -13.122 1.302 19.443 1.00 9.06 C ANISOU 2664 CB HIS A 250 564 1779 1101 216 215 206 C ATOM 2665 CG HIS A 250 -14.377 0.635 19.916 1.00 13.71 C ANISOU 2665 CG HIS A 250 1170 2339 1700 244 198 208 C ATOM 2666 ND1 HIS A 250 -15.164 1.156 20.919 1.00 12.61 N ANISOU 2666 ND1 HIS A 250 1027 2202 1562 267 196 202 N ATOM 2667 CD2 HIS A 250 -14.975 -0.518 19.529 1.00 12.43 C ANISOU 2667 CD2 HIS A 250 1014 2150 1557 249 197 217 C ATOM 2668 CE1 HIS A 250 -16.197 0.358 21.127 1.00 16.47 C ANISOU 2668 CE1 HIS A 250 1513 2659 2085 275 206 204 C ATOM 2669 NE2 HIS A 250 -16.105 -0.665 20.297 1.00 13.46 N ANISOU 2669 NE2 HIS A 250 1137 2263 1716 262 195 217 N ATOM 2670 N ILE A 251 -11.298 3.175 17.632 1.00 10.16 N ANISOU 2670 N ILE A 251 666 1985 1210 108 320 225 N ATOM 2671 CA ILE A 251 -10.024 3.845 17.395 1.00 12.24 C ANISOU 2671 CA ILE A 251 889 2260 1501 33 378 227 C ATOM 2672 C ILE A 251 -10.236 5.343 17.175 1.00 13.46 C ANISOU 2672 C ILE A 251 1122 2392 1601 -30 335 243 C ATOM 2673 O ILE A 251 -9.493 6.171 17.707 1.00 13.65 O ANISOU 2673 O ILE A 251 1108 2418 1661 -80 306 244 O ATOM 2674 CB ILE A 251 -9.285 3.226 16.190 1.00 16.17 C ANISOU 2674 CB ILE A 251 1420 2714 2008 -11 506 209 C ATOM 2675 CG1 ILE A 251 -8.782 1.823 16.544 1.00 18.40 C ANISOU 2675 CG1 ILE A 251 1654 2955 2383 40 509 161 C ATOM 2676 CG2 ILE A 251 -8.120 4.105 15.748 1.00 15.25 C ANISOU 2676 CG2 ILE A 251 1274 2594 1926 -113 602 214 C ATOM 2677 CD1 ILE A 251 -8.080 1.116 15.399 1.00 25.76 C ANISOU 2677 CD1 ILE A 251 2607 3853 3328 9 654 118 C ATOM 2678 N ILE A 252 -11.258 5.687 16.400 1.00 12.52 N ANISOU 2678 N ILE A 252 1144 2206 1407 -30 292 247 N ATOM 2679 CA ILE A 252 -11.605 7.087 16.189 1.00 14.92 C ANISOU 2679 CA ILE A 252 1568 2433 1668 -75 206 252 C ATOM 2680 C ILE A 252 -11.883 7.783 17.525 1.00 15.36 C ANISOU 2680 C ILE A 252 1573 2501 1761 -22 117 231 C ATOM 2681 O ILE A 252 -11.418 8.899 17.756 1.00 15.81 O ANISOU 2681 O ILE A 252 1675 2520 1811 -78 71 229 O ATOM 2682 CB ILE A 252 -12.821 7.229 15.256 1.00 16.47 C ANISOU 2682 CB ILE A 252 1914 2536 1808 -59 121 261 C ATOM 2683 CG1 ILE A 252 -12.440 6.835 13.824 1.00 17.43 C ANISOU 2683 CG1 ILE A 252 2179 2607 1836 -142 199 281 C ATOM 2684 CG2 ILE A 252 -13.358 8.651 15.281 1.00 14.50 C ANISOU 2684 CG2 ILE A 252 1770 2193 1545 -70 -8 260 C ATOM 2685 CD1 ILE A 252 -13.630 6.690 12.895 1.00 14.06 C ANISOU 2685 CD1 ILE A 252 1916 2073 1352 -126 76 295 C ATOM 2686 N ASN A 253 -12.620 7.117 18.410 1.00 13.56 N ANISOU 2686 N ASN A 253 1271 2316 1565 77 102 214 N ATOM 2687 CA ASN A 253 -12.901 7.680 19.728 1.00 14.36 C ANISOU 2687 CA ASN A 253 1362 2421 1674 131 53 185 C ATOM 2688 C ASN A 253 -11.624 7.897 20.537 1.00 14.06 C ANISOU 2688 C ASN A 253 1285 2416 1640 80 40 185 C ATOM 2689 O ASN A 253 -11.511 8.875 21.276 1.00 14.26 O ANISOU 2689 O ASN A 253 1373 2402 1644 72 -29 164 O ATOM 2690 CB ASN A 253 -13.874 6.788 20.507 1.00 12.42 C ANISOU 2690 CB ASN A 253 1056 2213 1451 229 84 172 C ATOM 2691 CG ASN A 253 -15.311 6.953 20.043 1.00 16.21 C ANISOU 2691 CG ASN A 253 1551 2633 1975 288 58 161 C ATOM 2692 OD1 ASN A 253 -15.651 7.943 19.398 1.00 20.04 O ANISOU 2692 OD1 ASN A 253 2113 3036 2467 275 -16 154 O ATOM 2693 ND2 ASN A 253 -16.162 5.988 20.378 1.00 11.98 N ANISOU 2693 ND2 ASN A 253 936 2126 1488 348 104 163 N ATOM 2694 N CYS A 254 -10.661 6.993 20.389 1.00 11.10 N ANISOU 2694 N CYS A 254 810 2098 1310 48 93 207 N ATOM 2695 CA CYS A 254 -9.376 7.152 21.058 1.00 12.89 C ANISOU 2695 CA CYS A 254 965 2340 1591 -6 50 214 C ATOM 2696 C CYS A 254 -8.652 8.405 20.561 1.00 14.37 C ANISOU 2696 C CYS A 254 1189 2473 1797 -118 24 223 C ATOM 2697 O CYS A 254 -8.042 9.123 21.350 1.00 16.56 O ANISOU 2697 O CYS A 254 1473 2722 2097 -161 -76 219 O ATOM 2698 CB CYS A 254 -8.498 5.912 20.859 1.00 12.97 C ANISOU 2698 CB CYS A 254 830 2405 1693 -5 113 232 C ATOM 2699 SG CYS A 254 -9.062 4.441 21.765 1.00 16.79 S ANISOU 2699 SG CYS A 254 1290 2928 2162 105 100 232 S ATOM 2700 N PHE A 255 -8.731 8.675 19.260 1.00 14.60 N ANISOU 2700 N PHE A 255 1270 2473 1804 -176 103 238 N ATOM 2701 CA PHE A 255 -8.105 9.873 18.701 1.00 14.50 C ANISOU 2701 CA PHE A 255 1321 2397 1793 -301 94 256 C ATOM 2702 C PHE A 255 -8.796 11.140 19.199 1.00 15.74 C ANISOU 2702 C PHE A 255 1625 2472 1883 -289 -41 238 C ATOM 2703 O PHE A 255 -8.138 12.113 19.564 1.00 17.09 O ANISOU 2703 O PHE A 255 1822 2594 2076 -371 -118 243 O ATOM 2704 CB PHE A 255 -8.111 9.830 17.170 1.00 16.27 C ANISOU 2704 CB PHE A 255 1627 2588 1967 -372 218 280 C ATOM 2705 CG PHE A 255 -6.914 9.135 16.581 1.00 16.15 C ANISOU 2705 CG PHE A 255 1481 2616 2039 -443 386 293 C ATOM 2706 CD1 PHE A 255 -5.733 9.827 16.363 1.00 16.91 C ANISOU 2706 CD1 PHE A 255 1516 2689 2220 -581 445 316 C ATOM 2707 CD2 PHE A 255 -6.966 7.786 16.260 1.00 18.39 C ANISOU 2707 CD2 PHE A 255 1693 2955 2340 -371 492 280 C ATOM 2708 CE1 PHE A 255 -4.628 9.191 15.829 1.00 20.91 C ANISOU 2708 CE1 PHE A 255 1868 3231 2847 -638 633 321 C ATOM 2709 CE2 PHE A 255 -5.863 7.142 15.725 1.00 19.05 C ANISOU 2709 CE2 PHE A 255 1648 3066 2523 -417 668 279 C ATOM 2710 CZ PHE A 255 -4.693 7.845 15.509 1.00 19.47 C ANISOU 2710 CZ PHE A 255 1617 3100 2680 -547 751 296 C ATOM 2711 N THR A 256 -10.124 11.117 19.215 1.00 13.35 N ANISOU 2711 N THR A 256 1407 2146 1521 -184 -73 213 N ATOM 2712 CA THR A 256 -10.911 12.238 19.716 1.00 15.74 C ANISOU 2712 CA THR A 256 1835 2362 1784 -139 -184 180 C ATOM 2713 C THR A 256 -10.583 12.526 21.177 1.00 18.20 C ANISOU 2713 C THR A 256 2141 2679 2094 -109 -251 145 C ATOM 2714 O THR A 256 -10.441 13.679 21.584 1.00 20.51 O ANISOU 2714 O THR A 256 2543 2888 2363 -141 -348 126 O ATOM 2715 CB THR A 256 -12.424 11.961 19.580 1.00 15.82 C ANISOU 2715 CB THR A 256 1873 2349 1787 -12 -189 154 C ATOM 2716 OG1 THR A 256 -12.749 11.743 18.202 1.00 20.06 O ANISOU 2716 OG1 THR A 256 2460 2852 2311 -48 -175 188 O ATOM 2717 CG2 THR A 256 -13.244 13.127 20.118 1.00 17.88 C ANISOU 2717 CG2 THR A 256 2242 2509 2044 57 -284 105 C ATOM 2718 N PHE A 257 -10.447 11.458 21.956 1.00 13.30 N ANISOU 2718 N PHE A 257 1423 2142 1487 -55 -213 140 N ATOM 2719 CA PHE A 257 -10.233 11.560 23.394 1.00 17.04 C ANISOU 2719 CA PHE A 257 1940 2610 1926 -23 -286 109 C ATOM 2720 C PHE A 257 -8.795 11.911 23.764 1.00 19.46 C ANISOU 2720 C PHE A 257 2212 2899 2282 -137 -390 134 C ATOM 2721 O PHE A 257 -8.555 12.869 24.499 1.00 21.28 O ANISOU 2721 O PHE A 257 2562 3050 2472 -168 -511 110 O ATOM 2722 CB PHE A 257 -10.631 10.246 24.067 1.00 13.16 C ANISOU 2722 CB PHE A 257 1387 2195 1418 65 -221 106 C ATOM 2723 CG PHE A 257 -10.564 10.282 25.567 1.00 18.29 C ANISOU 2723 CG PHE A 257 2143 2820 1986 98 -287 76 C ATOM 2724 CD1 PHE A 257 -11.430 11.084 26.294 1.00 16.38 C ANISOU 2724 CD1 PHE A 257 2065 2507 1651 164 -283 15 C ATOM 2725 CD2 PHE A 257 -9.653 9.496 26.251 1.00 15.15 C ANISOU 2725 CD2 PHE A 257 1702 2454 1602 69 -354 105 C ATOM 2726 CE1 PHE A 257 -11.378 11.112 27.675 1.00 16.03 C ANISOU 2726 CE1 PHE A 257 2174 2424 1492 188 -325 -18 C ATOM 2727 CE2 PHE A 257 -9.596 9.519 27.633 1.00 21.71 C ANISOU 2727 CE2 PHE A 257 2686 3238 2324 89 -439 82 C ATOM 2728 CZ PHE A 257 -10.460 10.328 28.346 1.00 21.17 C ANISOU 2728 CZ PHE A 257 2817 3101 2127 143 -413 20 C ATOM 2729 N PHE A 258 -7.845 11.133 23.255 1.00 15.21 N ANISOU 2729 N PHE A 258 1507 2423 1849 -198 -347 178 N ATOM 2730 CA PHE A 258 -6.448 11.261 23.663 1.00 17.10 C ANISOU 2730 CA PHE A 258 1650 2649 2200 -299 -451 205 C ATOM 2731 C PHE A 258 -5.697 12.382 22.949 1.00 20.98 C ANISOU 2731 C PHE A 258 2132 3078 2760 -443 -472 230 C ATOM 2732 O PHE A 258 -4.632 12.805 23.400 1.00 21.55 O ANISOU 2732 O PHE A 258 2142 3109 2938 -541 -593 250 O ATOM 2733 CB PHE A 258 -5.707 9.939 23.437 1.00 17.09 C ANISOU 2733 CB PHE A 258 1438 2726 2328 -292 -385 235 C ATOM 2734 CG PHE A 258 -6.121 8.839 24.373 1.00 19.70 C ANISOU 2734 CG PHE A 258 1781 3097 2609 -180 -417 224 C ATOM 2735 CD1 PHE A 258 -5.945 8.973 25.742 1.00 22.51 C ANISOU 2735 CD1 PHE A 258 2240 3402 2910 -167 -590 213 C ATOM 2736 CD2 PHE A 258 -6.668 7.662 23.884 1.00 14.31 C ANISOU 2736 CD2 PHE A 258 1035 2482 1919 -101 -284 228 C ATOM 2737 CE1 PHE A 258 -6.318 7.960 26.607 1.00 21.29 C ANISOU 2737 CE1 PHE A 258 2137 3268 2685 -82 -614 212 C ATOM 2738 CE2 PHE A 258 -7.042 6.644 24.742 1.00 16.61 C ANISOU 2738 CE2 PHE A 258 1351 2798 2163 -16 -312 227 C ATOM 2739 CZ PHE A 258 -6.868 6.793 26.106 1.00 19.50 C ANISOU 2739 CZ PHE A 258 1830 3116 2465 -8 -470 222 C ATOM 2740 N CYS A 259 -6.243 12.861 21.835 1.00 21.25 N ANISOU 2740 N CYS A 259 2239 3092 2743 -468 -369 237 N ATOM 2741 CA CYS A 259 -5.559 13.883 21.047 1.00 25.05 C ANISOU 2741 CA CYS A 259 2742 3506 3271 -623 -364 272 C ATOM 2742 C CYS A 259 -6.467 15.070 20.733 1.00 26.35 C ANISOU 2742 C CYS A 259 3135 3568 3310 -621 -420 256 C ATOM 2743 O CYS A 259 -6.961 15.199 19.612 1.00 25.87 O ANISOU 2743 O CYS A 259 3151 3485 3194 -638 -332 274 O ATOM 2744 CB CYS A 259 -5.019 13.278 19.748 1.00 27.16 C ANISOU 2744 CB CYS A 259 2886 3824 3610 -697 -164 311 C ATOM 2745 SG CYS A 259 -3.918 14.367 18.811 1.00 41.99 S ANISOU 2745 SG CYS A 259 4760 5624 5569 -924 -100 366 S ATOM 2746 N PRO A 260 -6.684 15.948 21.724 1.00 31.61 N ANISOU 2746 N PRO A 260 4513 2992 4504 358 -1225 304 N ATOM 2747 CA PRO A 260 -7.524 17.137 21.537 1.00 34.44 C ANISOU 2747 CA PRO A 260 4996 3229 4860 103 -1189 496 C ATOM 2748 C PRO A 260 -6.889 18.166 20.601 1.00 42.75 C ANISOU 2748 C PRO A 260 5697 4584 5962 -244 -1239 699 C ATOM 2749 O PRO A 260 -7.583 19.063 20.123 1.00 41.37 O ANISOU 2749 O PRO A 260 5605 4311 5804 -480 -1275 877 O ATOM 2750 CB PRO A 260 -7.656 17.698 22.955 1.00 35.21 C ANISOU 2750 CB PRO A 260 5418 2951 5008 120 -1421 480 C ATOM 2751 CG PRO A 260 -6.436 17.215 23.662 1.00 37.01 C ANISOU 2751 CG PRO A 260 5575 3202 5286 256 -1623 407 C ATOM 2752 CD PRO A 260 -6.157 15.855 23.097 1.00 32.53 C ANISOU 2752 CD PRO A 260 4863 2820 4677 482 -1518 247 C ATOM 2753 N ASP A 261 -5.589 18.036 20.350 1.00 34.86 N ANISOU 2753 N ASP A 261 4315 3949 4980 -308 -1286 647 N ATOM 2754 CA ASP A 261 -4.890 18.927 19.427 1.00 41.83 C ANISOU 2754 CA ASP A 261 4845 5235 5814 -759 -1316 826 C ATOM 2755 C ASP A 261 -5.071 18.476 17.980 1.00 41.37 C ANISOU 2755 C ASP A 261 4494 5645 5579 -953 -1027 805 C ATOM 2756 O ASP A 261 -4.744 19.207 17.046 1.00 40.50 O ANISOU 2756 O ASP A 261 4158 5898 5334 -1456 -1030 999 O ATOM 2757 CB ASP A 261 -3.401 19.001 19.768 1.00 49.06 C ANISOU 2757 CB ASP A 261 5410 6443 6787 -806 -1461 703 C ATOM 2758 CG ASP A 261 -3.142 19.636 21.120 1.00 58.40 C ANISOU 2758 CG ASP A 261 6867 7197 8126 -706 -1768 776 C ATOM 2759 OD1 ASP A 261 -3.967 20.466 21.558 1.00 59.18 O ANISOU 2759 OD1 ASP A 261 7327 6884 8275 -784 -1902 973 O ATOM 2760 OD2 ASP A 261 -2.113 19.305 21.746 1.00 65.79 O ANISOU 2760 OD2 ASP A 261 7633 8212 9153 -540 -1903 590 O ATOM 2761 N CYS A 262 -5.586 17.264 17.802 1.00 36.41 N ANISOU 2761 N CYS A 262 3891 5018 4925 -603 -803 577 N ATOM 2762 CA CYS A 262 -5.882 16.742 16.474 1.00 36.73 C ANISOU 2762 CA CYS A 262 3674 5479 4802 -739 -508 519 C ATOM 2763 C CYS A 262 -7.281 17.151 16.044 1.00 36.30 C ANISOU 2763 C CYS A 262 3977 5128 4686 -857 -440 771 C ATOM 2764 O CYS A 262 -8.203 17.177 16.859 1.00 31.38 O ANISOU 2764 O CYS A 262 3777 3985 4160 -604 -513 788 O ATOM 2765 CB CYS A 262 -5.764 15.214 16.446 1.00 36.48 C ANISOU 2765 CB CYS A 262 3487 5566 4809 -283 -353 122 C ATOM 2766 SG CYS A 262 -4.120 14.560 16.799 1.00 58.06 S ANISOU 2766 SG CYS A 262 5709 8652 7699 -60 -514 -323 S ATOM 2767 N ASER A 263 -7.438 17.479 14.766 0.55 35.41 N ANISOU 2767 N ASER A 263 3681 5375 4400 -1279 -318 933 N ATOM 2768 N BSER A 263 -7.434 17.475 14.765 0.45 35.42 N ANISOU 2768 N BSER A 263 3680 5378 4401 -1278 -317 931 N ATOM 2769 CA ASER A 263 -8.755 17.783 14.222 0.55 33.39 C ANISOU 2769 CA ASER A 263 3731 4845 4110 -1376 -291 1137 C ATOM 2770 CA BSER A 263 -8.747 17.771 14.206 0.45 33.41 C ANISOU 2770 CA BSER A 263 3727 4857 4110 -1378 -286 1135 C ATOM 2771 C ASER A 263 -9.654 16.558 14.336 0.55 32.40 C ANISOU 2771 C ASER A 263 3755 4560 3995 -895 -20 892 C ATOM 2772 C BSER A 263 -9.653 16.552 14.342 0.45 32.18 C ANISOU 2772 C BSER A 263 3727 4532 3967 -892 -19 890 C ATOM 2773 O ASER A 263 -9.197 15.429 14.169 0.55 30.44 O ANISOU 2773 O ASER A 263 3254 4611 3699 -655 189 614 O ATOM 2774 O BSER A 263 -9.198 15.419 14.196 0.45 30.40 O ANISOU 2774 O BSER A 263 3255 4598 3697 -646 187 611 O ATOM 2775 CB ASER A 263 -8.654 18.239 12.765 0.55 36.05 C ANISOU 2775 CB ASER A 263 3846 5642 4209 -1980 -237 1367 C ATOM 2776 CB BSER A 263 -8.627 18.188 12.738 0.45 36.09 C ANISOU 2776 CB BSER A 263 3832 5674 4207 -1976 -220 1354 C ATOM 2777 OG ASER A 263 -8.008 19.496 12.669 0.55 39.34 O ANISOU 2777 OG ASER A 263 4246 6120 4581 -2528 -569 1674 O ATOM 2778 OG BSER A 263 -9.903 18.372 12.151 0.45 37.65 O ANISOU 2778 OG BSER A 263 4321 5590 4393 -2038 -227 1529 O ATOM 2779 N HIS A 264 -10.929 16.785 14.635 1.00 27.51 N ANISOU 2779 N HIS A 264 3531 3470 3453 -759 -63 950 N ATOM 2780 CA HIS A 264 -11.882 15.691 14.781 1.00 24.62 C ANISOU 2780 CA HIS A 264 3351 2950 3052 -378 186 736 C ATOM 2781 C HIS A 264 -12.023 14.946 13.460 1.00 25.10 C ANISOU 2781 C HIS A 264 3163 3426 2948 -454 488 704 C ATOM 2782 O HIS A 264 -11.976 15.560 12.393 1.00 26.36 O ANISOU 2782 O HIS A 264 3162 3845 3009 -871 481 915 O ATOM 2783 CB HIS A 264 -13.242 16.216 15.243 1.00 26.92 C ANISOU 2783 CB HIS A 264 4031 2757 3439 -301 91 739 C ATOM 2784 CG HIS A 264 -14.144 15.156 15.796 1.00 27.10 C ANISOU 2784 CG HIS A 264 4297 2609 3392 48 312 481 C ATOM 2785 ND1 HIS A 264 -14.731 14.190 15.008 1.00 28.01 N ANISOU 2785 ND1 HIS A 264 4383 2885 3374 154 609 406 N ATOM 2786 CD2 HIS A 264 -14.563 14.914 17.061 1.00 25.48 C ANISOU 2786 CD2 HIS A 264 4381 2116 3184 243 271 287 C ATOM 2787 CE1 HIS A 264 -15.470 13.397 15.763 1.00 27.97 C ANISOU 2787 CE1 HIS A 264 4659 2677 3290 397 723 196 C ATOM 2788 NE2 HIS A 264 -15.386 13.816 17.013 1.00 26.76 N ANISOU 2788 NE2 HIS A 264 4706 2273 3189 421 527 120 N ATOM 2789 N ALA A 265 -12.162 13.624 13.531 1.00 23.44 N ANISOU 2789 N ALA A 265 2934 3279 2693 -96 709 444 N ATOM 2790 CA ALA A 265 -12.416 12.824 12.340 1.00 25.01 C ANISOU 2790 CA ALA A 265 2906 3841 2755 -108 1004 355 C ATOM 2791 C ALA A 265 -13.613 13.405 11.598 1.00 23.01 C ANISOU 2791 C ALA A 265 2850 3454 2439 -331 1068 575 C ATOM 2792 O ALA A 265 -14.621 13.743 12.218 1.00 24.31 O ANISOU 2792 O ALA A 265 3389 3154 2692 -205 976 602 O ATOM 2793 CB ALA A 265 -12.662 11.367 12.706 1.00 21.93 C ANISOU 2793 CB ALA A 265 2608 3351 2372 353 1134 61 C ATOM 2794 N PRO A 266 -13.494 13.548 10.270 1.00 20.59 N ANISOU 2794 N PRO A 266 3437 3000 1386 -628 -39 549 N ATOM 2795 CA PRO A 266 -14.547 14.183 9.469 1.00 27.69 C ANISOU 2795 CA PRO A 266 4489 3693 2339 -594 -215 679 C ATOM 2796 C PRO A 266 -15.859 13.409 9.532 1.00 25.94 C ANISOU 2796 C PRO A 266 4130 3425 2300 -362 -281 676 C ATOM 2797 O PRO A 266 -15.855 12.211 9.816 1.00 21.64 O ANISOU 2797 O PRO A 266 3414 3045 1765 -282 -183 588 O ATOM 2798 CB PRO A 266 -13.964 14.175 8.052 1.00 26.09 C ANISOU 2798 CB PRO A 266 4427 3586 1901 -837 -247 761 C ATOM 2799 CG PRO A 266 -12.960 13.073 8.060 1.00 25.68 C ANISOU 2799 CG PRO A 266 4179 3800 1777 -884 -48 621 C ATOM 2800 CD PRO A 266 -12.379 13.066 9.438 1.00 20.93 C ANISOU 2800 CD PRO A 266 3446 3258 1247 -826 54 529 C ATOM 2801 N LEU A 267 -16.965 14.098 9.273 1.00 23.97 N ANISOU 2801 N LEU A 267 3947 2940 2221 -257 -456 775 N ATOM 2802 CA LEU A 267 -18.291 13.506 9.395 1.00 29.13 C ANISOU 2802 CA LEU A 267 4429 3528 3111 -40 -526 773 C ATOM 2803 C LEU A 267 -18.481 12.298 8.480 1.00 26.74 C ANISOU 2803 C LEU A 267 4062 3397 2701 -85 -583 798 C ATOM 2804 O LEU A 267 -19.089 11.304 8.877 1.00 20.70 O ANISOU 2804 O LEU A 267 3107 2704 2054 49 -526 726 O ATOM 2805 CB LEU A 267 -19.365 14.556 9.102 1.00 33.21 C ANISOU 2805 CB LEU A 267 5005 3742 3871 70 -747 893 C ATOM 2806 CG LEU A 267 -20.816 14.099 9.256 1.00 36.75 C ANISOU 2806 CG LEU A 267 5220 4097 4646 301 -830 891 C ATOM 2807 CD1 LEU A 267 -21.072 13.609 10.674 1.00 37.58 C ANISOU 2807 CD1 LEU A 267 5126 4250 4904 459 -556 701 C ATOM 2808 CD2 LEU A 267 -21.775 15.221 8.884 1.00 37.04 C ANISOU 2808 CD2 LEU A 267 5291 3809 4974 418 -1084 1023 C ATOM 2809 N TRP A 268 -17.955 12.382 7.261 1.00 22.80 N ANISOU 2809 N TRP A 268 3750 2955 1958 -299 -679 892 N ATOM 2810 CA TRP A 268 -18.106 11.292 6.302 1.00 25.73 C ANISOU 2810 CA TRP A 268 4123 3468 2186 -379 -724 901 C ATOM 2811 C TRP A 268 -17.418 10.019 6.794 1.00 22.39 C ANISOU 2811 C TRP A 268 3535 3277 1695 -354 -473 730 C ATOM 2812 O TRP A 268 -17.879 8.912 6.519 1.00 20.51 O ANISOU 2812 O TRP A 268 3212 3117 1464 -310 -478 690 O ATOM 2813 CB TRP A 268 -17.561 11.697 4.926 1.00 26.45 C ANISOU 2813 CB TRP A 268 4465 3563 2022 -642 -798 978 C ATOM 2814 CG TRP A 268 -16.075 11.910 4.872 1.00 29.67 C ANISOU 2814 CG TRP A 268 4912 4097 2265 -811 -552 867 C ATOM 2815 CD1 TRP A 268 -15.411 13.097 4.993 1.00 33.06 C ANISOU 2815 CD1 TRP A 268 5462 4442 2656 -927 -536 903 C ATOM 2816 CD2 TRP A 268 -15.071 10.908 4.666 1.00 32.67 C ANISOU 2816 CD2 TRP A 268 5182 4683 2548 -874 -304 700 C ATOM 2817 NE1 TRP A 268 -14.056 12.895 4.881 1.00 31.48 N ANISOU 2817 NE1 TRP A 268 5208 4405 2347 -1070 -300 772 N ATOM 2818 CE2 TRP A 268 -13.821 11.560 4.680 1.00 32.70 C ANISOU 2818 CE2 TRP A 268 5210 4728 2485 -1023 -158 648 C ATOM 2819 CE3 TRP A 268 -15.107 9.523 4.474 1.00 29.31 C ANISOU 2819 CE3 TRP A 268 4637 4385 2114 -813 -203 591 C ATOM 2820 CZ2 TRP A 268 -12.621 10.875 4.511 1.00 35.56 C ANISOU 2820 CZ2 TRP A 268 5449 5255 2807 -1095 72 497 C ATOM 2821 CZ3 TRP A 268 -13.914 8.845 4.308 1.00 30.87 C ANISOU 2821 CZ3 TRP A 268 4741 4723 2267 -871 33 438 C ATOM 2822 CH2 TRP A 268 -12.688 9.522 4.326 1.00 35.11 C ANISOU 2822 CH2 TRP A 268 5272 5298 2769 -1004 164 395 C ATOM 2823 N LEU A 269 -16.322 10.179 7.528 1.00 21.39 N ANISOU 2823 N LEU A 269 3367 3242 1519 -385 -279 635 N ATOM 2824 CA LEU A 269 -15.601 9.030 8.066 1.00 19.67 C ANISOU 2824 CA LEU A 269 2981 3212 1280 -343 -82 490 C ATOM 2825 C LEU A 269 -16.356 8.420 9.244 1.00 19.70 C ANISOU 2825 C LEU A 269 2810 3181 1494 -122 -54 431 C ATOM 2826 O LEU A 269 -16.349 7.202 9.431 1.00 18.60 O ANISOU 2826 O LEU A 269 2556 3143 1369 -57 20 353 O ATOM 2827 CB LEU A 269 -14.185 9.423 8.493 1.00 20.40 C ANISOU 2827 CB LEU A 269 3058 3405 1287 -457 67 426 C ATOM 2828 CG LEU A 269 -13.329 8.267 9.020 1.00 22.61 C ANISOU 2828 CG LEU A 269 3140 3839 1610 -396 225 287 C ATOM 2829 CD1 LEU A 269 -13.100 7.232 7.926 1.00 22.72 C ANISOU 2829 CD1 LEU A 269 3137 3903 1594 -428 288 217 C ATOM 2830 CD2 LEU A 269 -12.008 8.768 9.584 1.00 17.55 C ANISOU 2830 CD2 LEU A 269 2434 3253 980 -484 308 237 C ATOM 2831 N MET A 270 -16.999 9.272 10.038 1.00 18.78 N ANISOU 2831 N MET A 270 2693 2906 1535 -22 -96 459 N ATOM 2832 CA MET A 270 -17.841 8.805 11.132 1.00 20.18 C ANISOU 2832 CA MET A 270 2733 3035 1901 154 -36 396 C ATOM 2833 C MET A 270 -18.966 7.943 10.579 1.00 18.95 C ANISOU 2833 C MET A 270 2480 2872 1848 229 -123 423 C ATOM 2834 O MET A 270 -19.223 6.850 11.080 1.00 18.95 O ANISOU 2834 O MET A 270 2367 2943 1890 296 -39 353 O ATOM 2835 CB MET A 270 -18.421 9.977 11.927 1.00 20.81 C ANISOU 2835 CB MET A 270 2846 2917 2145 237 -33 398 C ATOM 2836 CG MET A 270 -17.387 10.909 12.530 1.00 23.31 C ANISOU 2836 CG MET A 270 3288 3211 2356 139 35 369 C ATOM 2837 SD MET A 270 -16.277 10.071 13.674 1.00 30.78 S ANISOU 2837 SD MET A 270 4180 4339 3175 95 186 257 S ATOM 2838 CE MET A 270 -17.445 9.293 14.788 1.00 31.29 C ANISOU 2838 CE MET A 270 4147 4350 3391 259 292 178 C ATOM 2839 N TYR A 271 -19.627 8.441 9.538 1.00 17.74 N ANISOU 2839 N TYR A 271 2389 2621 1730 197 -318 537 N ATOM 2840 CA TYR A 271 -20.698 7.701 8.882 1.00 18.34 C ANISOU 2840 CA TYR A 271 2381 2686 1901 231 -459 583 C ATOM 2841 C TYR A 271 -20.205 6.361 8.348 1.00 21.59 C ANISOU 2841 C TYR A 271 2810 3273 2120 141 -398 522 C ATOM 2842 O TYR A 271 -20.886 5.345 8.477 1.00 19.61 O ANISOU 2842 O TYR A 271 2443 3050 1958 198 -394 484 O ATOM 2843 CB TYR A 271 -21.304 8.520 7.738 1.00 22.11 C ANISOU 2843 CB TYR A 271 2970 3024 2405 169 -743 745 C ATOM 2844 CG TYR A 271 -22.230 9.628 8.184 1.00 29.10 C ANISOU 2844 CG TYR A 271 3771 3681 3605 321 -853 808 C ATOM 2845 CD1 TYR A 271 -22.770 9.639 9.463 1.00 30.37 C ANISOU 2845 CD1 TYR A 271 3734 3784 4021 500 -674 696 C ATOM 2846 CD2 TYR A 271 -22.573 10.661 7.319 1.00 36.93 C ANISOU 2846 CD2 TYR A 271 4896 4493 4642 278 -1132 974 C ATOM 2847 CE1 TYR A 271 -23.622 10.653 9.871 1.00 33.64 C ANISOU 2847 CE1 TYR A 271 4054 3968 4759 654 -727 717 C ATOM 2848 CE2 TYR A 271 -23.422 11.677 7.717 1.00 42.37 C ANISOU 2848 CE2 TYR A 271 5488 4935 5675 449 -1238 1023 C ATOM 2849 CZ TYR A 271 -23.944 11.668 8.994 1.00 43.01 C ANISOU 2849 CZ TYR A 271 5341 4963 6038 647 -1015 879 C ATOM 2850 OH TYR A 271 -24.790 12.679 9.392 1.00 48.80 O ANISOU 2850 OH TYR A 271 5962 5432 7149 831 -1074 892 O ATOM 2851 N LEU A 272 -19.018 6.368 7.747 1.00 17.38 N ANISOU 2851 N LEU A 272 2419 2844 1341 -7 -331 501 N ATOM 2852 CA LEU A 272 -18.440 5.152 7.186 1.00 19.30 C ANISOU 2852 CA LEU A 272 2684 3230 1418 -87 -234 414 C ATOM 2853 C LEU A 272 -18.131 4.134 8.279 1.00 17.56 C ANISOU 2853 C LEU A 272 2305 3081 1287 41 -62 293 C ATOM 2854 O LEU A 272 -18.356 2.936 8.109 1.00 15.20 O ANISOU 2854 O LEU A 272 1969 2822 985 60 -35 233 O ATOM 2855 CB LEU A 272 -17.173 5.478 6.395 1.00 22.60 C ANISOU 2855 CB LEU A 272 3255 3741 1592 -273 -140 389 C ATOM 2856 CG LEU A 272 -16.508 4.302 5.680 1.00 30.02 C ANISOU 2856 CG LEU A 272 4221 4781 2404 -351 5 261 C ATOM 2857 CD1 LEU A 272 -17.475 3.679 4.687 1.00 34.95 C ANISOU 2857 CD1 LEU A 272 4961 5365 2955 -421 -143 296 C ATOM 2858 CD2 LEU A 272 -15.229 4.747 4.987 1.00 28.73 C ANISOU 2858 CD2 LEU A 272 4136 4621 2158 -485 145 200 C ATOM 2859 N ALA A 273 -17.613 4.618 9.403 1.00 14.63 N ANISOU 2859 N ALA A 273 1871 2706 981 109 33 265 N ATOM 2860 CA ALA A 273 -17.306 3.752 10.537 1.00 20.39 C ANISOU 2860 CA ALA A 273 2492 3479 1777 209 149 181 C ATOM 2861 C ALA A 273 -18.577 3.161 11.139 1.00 13.23 C ANISOU 2861 C ALA A 273 1506 2499 1023 311 129 184 C ATOM 2862 O ALA A 273 -18.582 2.023 11.610 1.00 12.97 O ANISOU 2862 O ALA A 273 1425 2494 1010 355 188 130 O ATOM 2863 CB ALA A 273 -16.527 4.520 11.595 1.00 13.20 C ANISOU 2863 CB ALA A 273 1577 2567 871 216 213 167 C ATOM 2864 N ILE A 274 -19.650 3.944 11.127 1.00 13.91 N ANISOU 2864 N ILE A 274 1569 2477 1241 345 48 246 N ATOM 2865 CA ILE A 274 -20.930 3.490 11.655 1.00 14.85 C ANISOU 2865 CA ILE A 274 1567 2528 1546 426 54 239 C ATOM 2866 C ILE A 274 -21.536 2.416 10.750 1.00 14.55 C ANISOU 2866 C ILE A 274 1500 2522 1507 384 -45 253 C ATOM 2867 O ILE A 274 -21.988 1.375 11.230 1.00 14.47 O ANISOU 2867 O ILE A 274 1423 2522 1553 406 18 207 O ATOM 2868 CB ILE A 274 -21.918 4.665 11.817 1.00 15.74 C ANISOU 2868 CB ILE A 274 1613 2498 1869 493 -3 288 C ATOM 2869 CG1 ILE A 274 -21.466 5.589 12.951 1.00 15.27 C ANISOU 2869 CG1 ILE A 274 1602 2381 1819 531 139 237 C ATOM 2870 CG2 ILE A 274 -23.324 4.158 12.098 1.00 16.31 C ANISOU 2870 CG2 ILE A 274 1503 2512 2181 560 1 276 C ATOM 2871 CD1 ILE A 274 -22.309 6.854 13.088 1.00 16.88 C ANISOU 2871 CD1 ILE A 274 1759 2407 2249 614 108 261 C ATOM 2872 N AVAL A 275 -21.545 2.691 9.449 0.70 15.45 N ANISOU 2872 N AVAL A 275 1699 2638 1532 295 -206 319 N ATOM 2873 N BVAL A 275 -21.531 2.647 9.441 0.30 15.43 N ANISOU 2873 N BVAL A 275 1698 2639 1524 294 -204 317 N ATOM 2874 CA AVAL A 275 -22.033 1.747 8.451 0.70 16.19 C ANISOU 2874 CA AVAL A 275 1826 2757 1569 210 -323 330 C ATOM 2875 CA BVAL A 275 -22.116 1.669 8.530 0.30 16.16 C ANISOU 2875 CA BVAL A 275 1807 2751 1583 218 -319 326 C ATOM 2876 C AVAL A 275 -21.281 0.419 8.541 0.70 15.30 C ANISOU 2876 C AVAL A 275 1760 2730 1325 190 -179 218 C ATOM 2877 C BVAL A 275 -21.272 0.392 8.466 0.30 15.35 C ANISOU 2877 C BVAL A 275 1774 2738 1322 183 -184 218 C ATOM 2878 O AVAL A 275 -21.880 -0.655 8.491 0.70 19.24 O ANISOU 2878 O AVAL A 275 2227 3218 1864 177 -195 187 O ATOM 2879 O BVAL A 275 -21.807 -0.689 8.229 0.30 18.80 O ANISOU 2879 O BVAL A 275 2201 3169 1772 153 -211 186 O ATOM 2880 CB AVAL A 275 -21.897 2.330 7.025 0.70 18.98 C ANISOU 2880 CB AVAL A 275 2352 3102 1757 66 -510 417 C ATOM 2881 CB BVAL A 275 -22.312 2.243 7.105 0.30 20.80 C ANISOU 2881 CB BVAL A 275 2534 3311 2059 87 -547 430 C ATOM 2882 CG1AVAL A 275 -22.030 1.242 5.973 0.70 18.47 C ANISOU 2882 CG1AVAL A 275 2404 3082 1531 -71 -583 389 C ATOM 2883 CG1BVAL A 275 -23.277 3.424 7.134 0.30 19.14 C ANISOU 2883 CG1BVAL A 275 2233 2967 2073 150 -736 555 C ATOM 2884 CG2AVAL A 275 -22.928 3.431 6.801 0.70 19.17 C ANISOU 2884 CG2AVAL A 275 2319 2995 1969 97 -741 558 C ATOM 2885 CG2BVAL A 275 -20.989 2.645 6.487 0.30 17.73 C ANISOU 2885 CG2BVAL A 275 2341 2992 1404 -26 -472 409 C ATOM 2886 N LEU A 276 -19.965 0.507 8.694 1.00 14.95 N ANISOU 2886 N LEU A 276 1777 2752 1152 188 -45 157 N ATOM 2887 CA LEU A 276 -19.111 -0.676 8.772 1.00 14.93 C ANISOU 2887 CA LEU A 276 1792 2803 1077 201 86 47 C ATOM 2888 C LEU A 276 -19.473 -1.537 9.981 1.00 16.20 C ANISOU 2888 C LEU A 276 1862 2923 1371 304 143 20 C ATOM 2889 O LEU A 276 -19.568 -2.760 9.879 1.00 13.79 O ANISOU 2889 O LEU A 276 1579 2597 1065 305 164 -36 O ATOM 2890 CB LEU A 276 -17.636 -0.278 8.838 1.00 14.19 C ANISOU 2890 CB LEU A 276 1710 2784 896 195 207 -6 C ATOM 2891 CG LEU A 276 -16.651 -1.422 9.099 1.00 15.29 C ANISOU 2891 CG LEU A 276 1805 2955 1048 256 335 -122 C ATOM 2892 CD1 LEU A 276 -16.724 -2.461 7.985 1.00 19.14 C ANISOU 2892 CD1 LEU A 276 2386 3435 1450 191 369 -212 C ATOM 2893 CD2 LEU A 276 -15.231 -0.896 9.263 1.00 18.88 C ANISOU 2893 CD2 LEU A 276 2210 3435 1530 242 413 -156 C ATOM 2894 N ALA A 277 -19.678 -0.894 11.124 1.00 12.90 N ANISOU 2894 N ALA A 277 1378 2477 1048 369 176 57 N ATOM 2895 CA ALA A 277 -20.088 -1.608 12.327 1.00 15.59 C ANISOU 2895 CA ALA A 277 1680 2772 1473 421 241 43 C ATOM 2896 C ALA A 277 -21.413 -2.332 12.094 1.00 16.74 C ANISOU 2896 C ALA A 277 1779 2868 1714 387 197 54 C ATOM 2897 O ALA A 277 -21.579 -3.485 12.491 1.00 15.06 O ANISOU 2897 O ALA A 277 1589 2622 1511 379 234 25 O ATOM 2898 CB ALA A 277 -20.200 -0.652 13.498 1.00 12.36 C ANISOU 2898 CB ALA A 277 1249 2333 1116 454 306 65 C ATOM 2899 N HIS A 278 -22.342 -1.651 11.429 1.00 13.98 N ANISOU 2899 N HIS A 278 1362 2500 1450 357 95 106 N ATOM 2900 CA HIS A 278 -23.657 -2.213 11.138 1.00 15.45 C ANISOU 2900 CA HIS A 278 1457 2646 1769 309 16 128 C ATOM 2901 C HIS A 278 -23.605 -3.385 10.156 1.00 15.52 C ANISOU 2901 C HIS A 278 1564 2665 1666 217 -66 98 C ATOM 2902 O HIS A 278 -24.423 -4.300 10.241 1.00 19.24 O ANISOU 2902 O HIS A 278 1995 3100 2214 162 -84 88 O ATOM 2903 CB HIS A 278 -24.587 -1.126 10.592 1.00 16.22 C ANISOU 2903 CB HIS A 278 1436 2704 2024 311 -131 207 C ATOM 2904 CG HIS A 278 -25.068 -0.162 11.631 1.00 20.71 C ANISOU 2904 CG HIS A 278 1868 3215 2785 406 -22 207 C ATOM 2905 ND1 HIS A 278 -25.508 1.108 11.324 1.00 17.52 N ANISOU 2905 ND1 HIS A 278 1382 2743 2531 461 -127 269 N ATOM 2906 CD2 HIS A 278 -25.185 -0.285 12.975 1.00 20.03 C ANISOU 2906 CD2 HIS A 278 1742 3111 2758 444 192 144 C ATOM 2907 CE1 HIS A 278 -25.872 1.726 12.434 1.00 27.38 C ANISOU 2907 CE1 HIS A 278 2528 3929 3946 546 45 221 C ATOM 2908 NE2 HIS A 278 -25.685 0.903 13.450 1.00 20.88 N ANISOU 2908 NE2 HIS A 278 1741 3145 3049 521 250 141 N ATOM 2909 N ATHR A 279 -22.643 -3.346 9.238 0.53 16.29 N ANISOU 2909 N ATHR A 279 1803 2805 1581 181 -91 69 N ATOM 2910 N BTHR A 279 -22.651 -3.359 9.226 0.47 16.44 N ANISOU 2910 N BTHR A 279 1823 2825 1600 180 -92 69 N ATOM 2911 CA ATHR A 279 -22.485 -4.396 8.236 0.53 17.98 C ANISOU 2911 CA ATHR A 279 2155 3016 1661 83 -129 6 C ATOM 2912 CA BTHR A 279 -22.535 -4.432 8.237 0.47 18.03 C ANISOU 2912 CA BTHR A 279 2160 3020 1672 80 -133 7 C ATOM 2913 C ATHR A 279 -22.182 -5.736 8.904 0.53 19.48 C ANISOU 2913 C ATHR A 279 2375 3157 1868 127 -10 -77 C ATOM 2914 C BTHR A 279 -22.156 -5.752 8.893 0.47 19.33 C ANISOU 2914 C BTHR A 279 2360 3139 1847 127 -8 -79 C ATOM 2915 O ATHR A 279 -22.490 -6.797 8.362 0.53 20.48 O ANISOU 2915 O ATHR A 279 2592 3233 1955 47 -43 -129 O ATOM 2916 O BTHR A 279 -22.364 -6.819 8.317 0.47 20.20 O ANISOU 2916 O BTHR A 279 2569 3200 1905 50 -33 -138 O ATOM 2917 CB ATHR A 279 -21.363 -4.045 7.229 0.53 17.95 C ANISOU 2917 CB ATHR A 279 2303 3068 1450 28 -98 -43 C ATOM 2918 CB BTHR A 279 -21.493 -4.116 7.140 0.47 18.32 C ANISOU 2918 CB BTHR A 279 2356 3110 1495 14 -116 -40 C ATOM 2919 OG1ATHR A 279 -21.640 -2.774 6.627 0.53 17.90 O ANISOU 2919 OG1ATHR A 279 2314 3082 1407 -35 -234 60 O ATOM 2920 OG1BTHR A 279 -20.273 -3.667 7.742 0.47 17.70 O ANISOU 2920 OG1BTHR A 279 2247 3078 1399 113 37 -78 O ATOM 2921 CG2ATHR A 279 -21.256 -5.097 6.135 0.53 17.93 C ANISOU 2921 CG2ATHR A 279 2477 3045 1289 -97 -102 -139 C ATOM 2922 CG2BTHR A 279 -22.016 -3.054 6.180 0.47 17.78 C ANISOU 2922 CG2BTHR A 279 2340 3051 1364 -97 -305 65 C ATOM 2923 N ASN A 280 -21.596 -5.682 10.097 1.00 16.69 N ANISOU 2923 N ASN A 280 1971 2799 1570 239 106 -80 N ATOM 2924 CA ASN A 280 -21.256 -6.895 10.831 1.00 17.90 C ANISOU 2924 CA ASN A 280 2177 2878 1746 285 178 -126 C ATOM 2925 C ASN A 280 -22.495 -7.723 11.165 1.00 16.54 C ANISOU 2925 C ASN A 280 1995 2631 1657 204 147 -101 C ATOM 2926 O ASN A 280 -22.417 -8.941 11.302 1.00 17.39 O ANISOU 2926 O ASN A 280 2202 2647 1760 188 163 -142 O ATOM 2927 CB ASN A 280 -20.497 -6.562 12.114 1.00 19.42 C ANISOU 2927 CB ASN A 280 2339 3073 1965 387 250 -100 C ATOM 2928 CG ASN A 280 -20.046 -7.807 12.854 1.00 20.14 C ANISOU 2928 CG ASN A 280 2513 3060 2078 433 270 -118 C ATOM 2929 OD1 ASN A 280 -19.152 -8.521 12.399 1.00 23.10 O ANISOU 2929 OD1 ASN A 280 2936 3393 2448 494 275 -191 O ATOM 2930 ND2 ASN A 280 -20.668 -8.077 13.995 1.00 17.50 N ANISOU 2930 ND2 ASN A 280 2205 2668 1776 398 287 -57 N ATOM 2931 N SER A 281 -23.640 -7.059 11.277 1.00 15.94 N ANISOU 2931 N SER A 281 1789 2583 1685 149 104 -37 N ATOM 2932 CA SER A 281 -24.893 -7.750 11.555 1.00 22.31 C ANISOU 2932 CA SER A 281 2533 3337 2607 46 89 -17 C ATOM 2933 C SER A 281 -25.421 -8.487 10.326 1.00 21.36 C ANISOU 2933 C SER A 281 2472 3191 2454 -82 -55 -40 C ATOM 2934 O SER A 281 -26.415 -9.208 10.407 1.00 24.99 O ANISOU 2934 O SER A 281 2889 3603 3003 -199 -90 -30 O ATOM 2935 CB SER A 281 -25.943 -6.762 12.064 1.00 21.53 C ANISOU 2935 CB SER A 281 2221 3270 2691 42 111 37 C ATOM 2936 OG SER A 281 -25.542 -6.196 13.300 1.00 22.07 O ANISOU 2936 OG SER A 281 2283 3341 2761 122 272 37 O ATOM 2937 N VAL A 282 -24.753 -8.303 9.190 1.00 18.33 N ANISOU 2937 N VAL A 282 2204 2837 1925 -89 -129 -77 N ATOM 2938 CA VAL A 282 -25.146 -8.963 7.948 1.00 19.87 C ANISOU 2938 CA VAL A 282 2523 3001 2024 -243 -266 -113 C ATOM 2939 C VAL A 282 -24.276 -10.189 7.643 1.00 27.83 C ANISOU 2939 C VAL A 282 3753 3923 2897 -245 -171 -243 C ATOM 2940 O VAL A 282 -24.739 -11.150 7.027 1.00 30.71 O ANISOU 2940 O VAL A 282 4247 4210 3211 -382 -238 -295 O ATOM 2941 CB VAL A 282 -25.072 -7.981 6.747 1.00 20.42 C ANISOU 2941 CB VAL A 282 2638 3141 1979 -307 -413 -76 C ATOM 2942 CG1 VAL A 282 -25.555 -8.647 5.465 1.00 22.46 C ANISOU 2942 CG1 VAL A 282 3073 3363 2098 -515 -583 -107 C ATOM 2943 CG2 VAL A 282 -25.885 -6.726 7.027 1.00 20.39 C ANISOU 2943 CG2 VAL A 282 2412 3181 2156 -272 -529 54 C ATOM 2944 N VAL A 283 -23.025 -10.165 8.096 1.00 20.94 N ANISOU 2944 N VAL A 283 2914 3048 1995 -90 -20 -299 N ATOM 2945 CA VAL A 283 -22.023 -11.104 7.588 1.00 24.12 C ANISOU 2945 CA VAL A 283 3490 3366 2307 -54 81 -445 C ATOM 2946 C VAL A 283 -22.094 -12.527 8.153 1.00 26.18 C ANISOU 2946 C VAL A 283 3847 3457 2645 -35 114 -491 C ATOM 2947 O VAL A 283 -21.754 -13.479 7.452 1.00 28.23 O ANISOU 2947 O VAL A 283 4280 3602 2843 -66 156 -623 O ATOM 2948 CB VAL A 283 -20.589 -10.567 7.825 1.00 27.31 C ANISOU 2948 CB VAL A 283 3845 3824 2709 112 216 -492 C ATOM 2949 CG1 VAL A 283 -20.372 -9.274 7.055 1.00 30.31 C ANISOU 2949 CG1 VAL A 283 4198 4347 2973 56 201 -468 C ATOM 2950 CG2 VAL A 283 -20.324 -10.361 9.305 1.00 30.48 C ANISOU 2950 CG2 VAL A 283 4117 4219 3246 253 238 -402 C ATOM 2951 N ASN A 284 -22.531 -12.682 9.400 1.00 23.45 N ANISOU 2951 N ASN A 284 3420 3073 2417 -1 106 -391 N ATOM 2952 CA ASN A 284 -22.535 -14.005 10.028 1.00 31.35 C ANISOU 2952 CA ASN A 284 4547 3888 3476 6 122 -408 C ATOM 2953 C ASN A 284 -23.335 -15.086 9.275 1.00 31.07 C ANISOU 2953 C ASN A 284 4670 3732 3403 -173 61 -472 C ATOM 2954 O ASN A 284 -22.821 -16.188 9.090 1.00 28.45 O ANISOU 2954 O ASN A 284 4518 3221 3072 -137 96 -572 O ATOM 2955 CB ASN A 284 -23.034 -13.906 11.474 1.00 39.03 C ANISOU 2955 CB ASN A 284 5448 4851 4530 0 129 -276 C ATOM 2956 CG ASN A 284 -22.131 -13.052 12.344 1.00 41.60 C ANISOU 2956 CG ASN A 284 5686 5251 4871 159 176 -222 C ATOM 2957 OD1 ASN A 284 -21.014 -12.712 11.953 1.00 36.06 O ANISOU 2957 OD1 ASN A 284 4962 4585 4155 293 199 -282 O ATOM 2958 ND2 ASN A 284 -22.611 -12.701 13.531 1.00 48.13 N ANISOU 2958 ND2 ASN A 284 6470 6099 5720 120 204 -120 N ATOM 2959 N PRO A 285 -24.578 -14.784 8.830 1.00 27.56 N ANISOU 2959 N PRO A 285 4155 3368 2948 -365 -45 -419 N ATOM 2960 CA PRO A 285 -25.316 -15.821 8.092 1.00 28.62 C ANISOU 2960 CA PRO A 285 4451 3388 3037 -567 -132 -479 C ATOM 2961 C PRO A 285 -24.567 -16.361 6.872 1.00 31.59 C ANISOU 2961 C PRO A 285 5064 3678 3260 -578 -101 -652 C ATOM 2962 O PRO A 285 -24.744 -17.526 6.513 1.00 33.58 O ANISOU 2962 O PRO A 285 5528 3755 3477 -685 -111 -745 O ATOM 2963 CB PRO A 285 -26.593 -15.095 7.658 1.00 26.17 C ANISOU 2963 CB PRO A 285 3967 3217 2761 -746 -289 -386 C ATOM 2964 CG PRO A 285 -26.793 -14.060 8.702 1.00 28.80 C ANISOU 2964 CG PRO A 285 4041 3671 3232 -635 -234 -268 C ATOM 2965 CD PRO A 285 -25.411 -13.585 9.045 1.00 27.35 C ANISOU 2965 CD PRO A 285 3892 3509 2990 -408 -106 -301 C ATOM 2966 N PHE A 286 -23.737 -15.527 6.256 1.00 31.43 N ANISOU 2966 N PHE A 286 5025 3771 3145 -487 -41 -706 N ATOM 2967 CA PHE A 286 -22.929 -15.960 5.121 1.00 37.35 C ANISOU 2967 CA PHE A 286 6000 4452 3739 -506 60 -899 C ATOM 2968 C PHE A 286 -21.786 -16.867 5.555 1.00 35.55 C ANISOU 2968 C PHE A 286 5847 4042 3618 -296 239 -1031 C ATOM 2969 O PHE A 286 -21.444 -17.818 4.855 1.00 38.10 O ANISOU 2969 O PHE A 286 6394 4198 3886 -329 329 -1215 O ATOM 2970 CB PHE A 286 -22.386 -14.751 4.362 1.00 40.68 C ANISOU 2970 CB PHE A 286 6381 5053 4021 -504 95 -912 C ATOM 2971 CG PHE A 286 -23.420 -14.054 3.539 1.00 41.18 C ANISOU 2971 CG PHE A 286 6466 5232 3947 -739 -121 -814 C ATOM 2972 CD1 PHE A 286 -23.679 -14.466 2.243 1.00 45.74 C ANISOU 2972 CD1 PHE A 286 7322 5765 4293 -979 -187 -918 C ATOM 2973 CD2 PHE A 286 -24.149 -13.002 4.064 1.00 37.77 C ANISOU 2973 CD2 PHE A 286 5789 4932 3629 -727 -271 -620 C ATOM 2974 CE1 PHE A 286 -24.639 -13.835 1.481 1.00 48.95 C ANISOU 2974 CE1 PHE A 286 7759 6261 4579 -1209 -452 -799 C ATOM 2975 CE2 PHE A 286 -25.110 -12.367 3.307 1.00 40.97 C ANISOU 2975 CE2 PHE A 286 6187 5415 3966 -920 -515 -513 C ATOM 2976 CZ PHE A 286 -25.357 -12.786 2.014 1.00 44.26 C ANISOU 2976 CZ PHE A 286 6880 5790 4148 -1166 -632 -588 C ATOM 2977 N ILE A 287 -21.198 -16.573 6.711 1.00 33.20 N ANISOU 2977 N ILE A 287 5370 3761 3485 -82 278 -940 N ATOM 2978 CA ILE A 287 -20.133 -17.412 7.244 1.00 34.93 C ANISOU 2978 CA ILE A 287 5622 3789 3860 137 381 -1025 C ATOM 2979 C ILE A 287 -20.659 -18.812 7.550 1.00 32.97 C ANISOU 2979 C ILE A 287 5571 3279 3676 77 321 -1039 C ATOM 2980 O ILE A 287 -20.013 -19.809 7.224 1.00 36.16 O ANISOU 2980 O ILE A 287 6130 3459 4151 170 408 -1200 O ATOM 2981 CB ILE A 287 -19.514 -16.808 8.511 1.00 36.54 C ANISOU 2981 CB ILE A 287 5617 4058 4208 334 362 -885 C ATOM 2982 CG1 ILE A 287 -19.058 -15.371 8.244 1.00 34.91 C ANISOU 2982 CG1 ILE A 287 5228 4102 3936 365 411 -861 C ATOM 2983 CG2 ILE A 287 -18.351 -17.664 8.992 1.00 38.71 C ANISOU 2983 CG2 ILE A 287 5907 4121 4679 569 411 -957 C ATOM 2984 CD1 ILE A 287 -18.024 -15.257 7.148 1.00 38.26 C ANISOU 2984 CD1 ILE A 287 5670 4553 4313 416 584 -1059 C ATOM 2985 N TYR A 288 -21.838 -18.880 8.164 1.00 32.10 N ANISOU 2985 N TYR A 288 5453 3187 3556 -85 188 -880 N ATOM 2986 CA TYR A 288 -22.474 -20.161 8.462 1.00 35.25 C ANISOU 2986 CA TYR A 288 6052 3347 3994 -203 124 -873 C ATOM 2987 C TYR A 288 -22.772 -20.932 7.183 1.00 32.98 C ANISOU 2987 C TYR A 288 6003 2937 3590 -372 137 -1055 C ATOM 2988 O TYR A 288 -22.547 -22.139 7.108 1.00 43.24 O ANISOU 2988 O TYR A 288 7529 3958 4941 -356 164 -1162 O ATOM 2989 CB TYR A 288 -23.767 -19.955 9.256 1.00 35.30 C ANISOU 2989 CB TYR A 288 5968 3439 4005 -397 19 -684 C ATOM 2990 CG TYR A 288 -23.567 -19.268 10.585 1.00 32.24 C ANISOU 2990 CG TYR A 288 5409 3147 3693 -278 31 -521 C ATOM 2991 CD1 TYR A 288 -22.625 -19.729 11.493 1.00 35.68 C ANISOU 2991 CD1 TYR A 288 5918 3421 4219 -88 37 -483 C ATOM 2992 CD2 TYR A 288 -24.313 -18.149 10.926 1.00 35.51 C ANISOU 2992 CD2 TYR A 288 5601 3795 4096 -359 23 -409 C ATOM 2993 CE1 TYR A 288 -22.441 -19.101 12.710 1.00 39.37 C ANISOU 2993 CE1 TYR A 288 6279 3969 4709 -21 27 -332 C ATOM 2994 CE2 TYR A 288 -24.131 -17.510 12.135 1.00 34.32 C ANISOU 2994 CE2 TYR A 288 5336 3718 3985 -274 60 -286 C ATOM 2995 CZ TYR A 288 -23.193 -17.987 13.023 1.00 39.04 C ANISOU 2995 CZ TYR A 288 6048 4167 4619 -123 59 -246 C ATOM 2996 OH TYR A 288 -23.016 -17.347 14.230 1.00 41.58 O ANISOU 2996 OH TYR A 288 6303 4558 4936 -79 77 -122 O ATOM 2997 N ALA A 289 -23.272 -20.223 6.176 1.00 35.55 N ANISOU 2997 N ALA A 289 6305 3453 3749 -544 101 -1087 N ATOM 2998 CA ALA A 289 -23.652 -20.845 4.913 1.00 42.67 C ANISOU 2998 CA ALA A 289 7469 4262 4480 -767 82 -1248 C ATOM 2999 C ALA A 289 -22.449 -21.438 4.185 1.00 45.21 C ANISOU 2999 C ALA A 289 7994 4412 4771 -629 293 -1508 C ATOM 3000 O ALA A 289 -22.528 -22.537 3.639 1.00 51.41 O ANISOU 3000 O ALA A 289 9066 4960 5509 -731 330 -1672 O ATOM 3001 CB ALA A 289 -24.362 -19.835 4.021 1.00 34.74 C ANISOU 3001 CB ALA A 289 6403 3501 3295 -980 -46 -1195 C ATOM 3002 N TYR A 290 -21.336 -20.712 4.186 1.00 43.16 N ANISOU 3002 N TYR A 290 7579 4263 4555 -405 447 -1558 N ATOM 3003 CA TYR A 290 -20.152 -21.132 3.444 1.00 45.44 C ANISOU 3003 CA TYR A 290 7995 4422 4848 -272 700 -1829 C ATOM 3004 C TYR A 290 -19.271 -22.127 4.202 1.00 45.80 C ANISOU 3004 C TYR A 290 8030 4181 5190 19 794 -1904 C ATOM 3005 O TYR A 290 -18.470 -22.831 3.589 1.00 45.90 O ANISOU 3005 O TYR A 290 8056 4083 5301 129 940 -2080 O ATOM 3006 CB TYR A 290 -19.314 -19.910 3.049 1.00 48.88 C ANISOU 3006 CB TYR A 290 8238 5112 5224 -185 835 -1852 C ATOM 3007 CG TYR A 290 -19.822 -19.174 1.827 1.00 58.32 C ANISOU 3007 CG TYR A 290 9509 6524 6126 -458 781 -1833 C ATOM 3008 CD1 TYR A 290 -19.575 -19.658 0.548 1.00 66.97 C ANISOU 3008 CD1 TYR A 290 10767 7587 7090 -579 886 -1974 C ATOM 3009 CD2 TYR A 290 -20.537 -17.989 1.951 1.00 60.47 C ANISOU 3009 CD2 TYR A 290 9702 7013 6260 -594 612 -1661 C ATOM 3010 CE1 TYR A 290 -20.034 -18.986 -0.572 1.00 70.83 C ANISOU 3010 CE1 TYR A 290 11365 8240 7309 -838 812 -1923 C ATOM 3011 CE2 TYR A 290 -20.999 -17.311 0.838 1.00 64.80 C ANISOU 3011 CE2 TYR A 290 10323 7724 6574 -830 510 -1604 C ATOM 3012 CZ TYR A 290 -20.745 -17.814 -0.421 1.00 70.54 C ANISOU 3012 CZ TYR A 290 11238 8400 7163 -956 606 -1726 C ATOM 3013 OH TYR A 290 -21.203 -17.143 -1.533 1.00 74.55 O ANISOU 3013 OH TYR A 290 11857 9036 7433 -1203 489 -1644 O ATOM 3014 N ARG A 291 -19.415 -22.194 5.523 1.00 43.26 N ANISOU 3014 N ARG A 291 7559 3822 5057 147 639 -1685 N ATOM 3015 CA ARG A 291 -18.511 -23.015 6.330 1.00 45.94 C ANISOU 3015 CA ARG A 291 7874 3889 5692 437 662 -1705 C ATOM 3016 C ARG A 291 -19.187 -24.166 7.080 1.00 44.07 C ANISOU 3016 C ARG A 291 7841 3366 5539 375 494 -1596 C ATOM 3017 O ARG A 291 -18.515 -25.101 7.517 1.00 43.10 O ANISOU 3017 O ARG A 291 7797 2929 5651 584 491 -1643 O ATOM 3018 CB ARG A 291 -17.761 -22.134 7.334 1.00 46.27 C ANISOU 3018 CB ARG A 291 7598 4090 5892 666 615 -1540 C ATOM 3019 CG ARG A 291 -16.847 -21.099 6.693 1.00 44.61 C ANISOU 3019 CG ARG A 291 7176 4114 5659 760 798 -1657 C ATOM 3020 CD ARG A 291 -15.852 -20.542 7.698 1.00 42.98 C ANISOU 3020 CD ARG A 291 6677 3973 5682 1022 752 -1537 C ATOM 3021 NE ARG A 291 -15.008 -21.590 8.265 1.00 47.37 N ANISOU 3021 NE ARG A 291 7226 4209 6564 1288 720 -1582 N ATOM 3022 CZ ARG A 291 -13.843 -21.972 7.752 1.00 50.64 C ANISOU 3022 CZ ARG A 291 7509 4529 7202 1494 870 -1791 C ATOM 3023 NH1 ARG A 291 -13.378 -21.390 6.656 1.00 51.55 N ANISOU 3023 NH1 ARG A 291 7529 4887 7170 1433 1065 -1939 N ATOM 3024 NH2 ARG A 291 -13.142 -22.936 8.335 1.00 53.58 N ANISOU 3024 NH2 ARG A 291 7877 4629 7853 1742 762 -1760 N ATOM 3025 N ILE A 292 -20.504 -24.103 7.236 1.00 42.46 N ANISOU 3025 N ILE A 292 7712 3254 5165 86 349 -1447 N ATOM 3026 CA ILE A 292 -21.214 -25.133 7.988 1.00 41.24 C ANISOU 3026 CA ILE A 292 7752 2851 5067 -27 206 -1328 C ATOM 3027 C ILE A 292 -22.273 -25.817 7.129 1.00 42.56 C ANISOU 3027 C ILE A 292 8180 2926 5063 -355 174 -1424 C ATOM 3028 O ILE A 292 -23.293 -25.218 6.790 1.00 41.35 O ANISOU 3028 O ILE A 292 7956 3013 4741 -617 98 -1349 O ATOM 3029 CB ILE A 292 -21.874 -24.552 9.254 1.00 42.69 C ANISOU 3029 CB ILE A 292 7775 3201 5246 -104 66 -1038 C ATOM 3030 CG1 ILE A 292 -20.843 -23.778 10.079 1.00 46.00 C ANISOU 3030 CG1 ILE A 292 7957 3728 5792 180 72 -940 C ATOM 3031 CG2 ILE A 292 -22.506 -25.660 10.083 1.00 45.85 C ANISOU 3031 CG2 ILE A 292 8404 3325 5691 -241 -54 -914 C ATOM 3032 CD1 ILE A 292 -21.416 -23.095 11.301 1.00 47.45 C ANISOU 3032 CD1 ILE A 292 8010 4084 5933 95 -24 -687 C ATOM 3033 N ARG A 293 -22.018 -27.078 6.787 1.00 51.90 N ANISOU 3033 N ARG A 293 9155 4754 5811 157 877 -1382 N ATOM 3034 CA ARG A 293 -22.879 -27.838 5.885 1.00 55.73 C ANISOU 3034 CA ARG A 293 9935 5053 6185 -56 814 -1500 C ATOM 3035 C ARG A 293 -24.319 -27.935 6.376 1.00 48.73 C ANISOU 3035 C ARG A 293 9085 4185 5247 -372 624 -1304 C ATOM 3036 O ARG A 293 -25.258 -27.751 5.602 1.00 48.71 O ANISOU 3036 O ARG A 293 9167 4256 5084 -621 574 -1338 O ATOM 3037 CB ARG A 293 -22.320 -29.249 5.678 1.00 58.70 C ANISOU 3037 CB ARG A 293 10589 5032 6681 97 823 -1657 C ATOM 3038 CG ARG A 293 -20.926 -29.295 5.078 1.00 66.01 C ANISOU 3038 CG ARG A 293 11494 5925 7660 419 1026 -1880 C ATOM 3039 CD ARG A 293 -20.510 -30.725 4.760 1.00 72.97 C ANISOU 3039 CD ARG A 293 12682 6390 8655 564 1034 -2063 C ATOM 3040 NE ARG A 293 -19.182 -30.788 4.154 1.00 79.62 N ANISOU 3040 NE ARG A 293 13489 7214 9550 888 1248 -2292 N ATOM 3041 CZ ARG A 293 -18.612 -31.907 3.717 1.00 93.72 C ANISOU 3041 CZ ARG A 293 15513 8662 11433 1082 1309 -2506 C ATOM 3042 NH1 ARG A 293 -19.254 -33.064 3.815 1.00 97.90 N ANISOU 3042 NH1 ARG A 293 16358 8820 12018 971 1157 -2517 N ATOM 3043 NH2 ARG A 293 -17.401 -31.869 3.179 1.00100.01 N ANISOU 3043 NH2 ARG A 293 16149 9557 12293 1363 1488 -2672 N ATOM 3044 N GLU A 294 -24.488 -28.224 7.662 1.00 48.31 N ANISOU 3044 N GLU A 294 8956 4076 5322 -369 517 -1093 N ATOM 3045 CA GLU A 294 -25.818 -28.428 8.227 1.00 50.90 C ANISOU 3045 CA GLU A 294 9309 4419 5611 -664 345 -896 C ATOM 3046 C GLU A 294 -26.663 -27.158 8.139 1.00 45.34 C ANISOU 3046 C GLU A 294 8378 4081 4767 -842 340 -798 C ATOM 3047 O GLU A 294 -27.875 -27.228 7.938 1.00 45.49 O ANISOU 3047 O GLU A 294 8447 4146 4693 -1122 229 -723 O ATOM 3048 CB GLU A 294 -25.717 -28.899 9.679 1.00 52.14 C ANISOU 3048 CB GLU A 294 9407 4484 5920 -612 250 -679 C ATOM 3049 CG GLU A 294 -26.988 -29.549 10.210 1.00 52.17 C ANISOU 3049 CG GLU A 294 9517 4405 5902 -916 70 -496 C ATOM 3050 CD GLU A 294 -27.273 -30.893 9.565 1.00 59.72 C ANISOU 3050 CD GLU A 294 10833 4984 6875 -1031 -20 -604 C ATOM 3051 OE1 GLU A 294 -26.310 -31.570 9.146 1.00 62.66 O ANISOU 3051 OE1 GLU A 294 11380 5087 7341 -808 42 -781 O ATOM 3052 OE2 GLU A 294 -28.460 -31.273 9.476 1.00 62.15 O ANISOU 3052 OE2 GLU A 294 11247 5264 7104 -1343 -154 -515 O ATOM 3053 N PHE A 295 -26.023 -26.001 8.286 1.00 43.10 N ANISOU 3053 N PHE A 295 7844 4052 4479 -680 453 -795 N ATOM 3054 CA PHE A 295 -26.713 -24.723 8.131 1.00 40.76 C ANISOU 3054 CA PHE A 295 7338 4083 4066 -810 457 -721 C ATOM 3055 C PHE A 295 -27.080 -24.478 6.673 1.00 45.41 C ANISOU 3055 C PHE A 295 8037 4720 4498 -940 484 -877 C ATOM 3056 O PHE A 295 -28.223 -24.146 6.355 1.00 40.89 O ANISOU 3056 O PHE A 295 7442 4273 3820 -1180 393 -805 O ATOM 3057 CB PHE A 295 -25.850 -23.568 8.646 1.00 38.52 C ANISOU 3057 CB PHE A 295 6786 4027 3824 -602 564 -687 C ATOM 3058 CG PHE A 295 -26.172 -23.148 10.052 1.00 37.00 C ANISOU 3058 CG PHE A 295 6396 3971 3693 -613 503 -474 C ATOM 3059 CD1 PHE A 295 -27.360 -22.494 10.337 1.00 35.75 C ANISOU 3059 CD1 PHE A 295 6110 4014 3459 -811 433 -341 C ATOM 3060 CD2 PHE A 295 -25.283 -23.392 11.085 1.00 37.03 C ANISOU 3060 CD2 PHE A 295 6335 3911 3824 -422 519 -408 C ATOM 3061 CE1 PHE A 295 -27.661 -22.101 11.631 1.00 34.60 C ANISOU 3061 CE1 PHE A 295 5786 4007 3352 -817 396 -164 C ATOM 3062 CE2 PHE A 295 -25.577 -22.999 12.380 1.00 35.82 C ANISOU 3062 CE2 PHE A 295 6014 3897 3700 -447 466 -219 C ATOM 3063 CZ PHE A 295 -26.768 -22.354 12.651 1.00 34.62 C ANISOU 3063 CZ PHE A 295 5746 3948 3459 -644 414 -106 C ATOM 3064 N ARG A 296 -26.095 -24.646 5.797 1.00 42.37 N ANISOU 3064 N ARG A 296 7761 4246 4092 -780 609 -1086 N ATOM 3065 CA ARG A 296 -26.265 -24.412 4.369 1.00 43.12 C ANISOU 3065 CA ARG A 296 7974 4394 4015 -887 654 -1253 C ATOM 3066 C ARG A 296 -27.383 -25.261 3.774 1.00 45.06 C ANISOU 3066 C ARG A 296 8469 4486 4165 -1167 517 -1278 C ATOM 3067 O ARG A 296 -28.200 -24.768 2.996 1.00 44.83 O ANISOU 3067 O ARG A 296 8444 4607 3983 -1381 462 -1273 O ATOM 3068 CB ARG A 296 -24.953 -24.687 3.633 1.00 47.41 C ANISOU 3068 CB ARG A 296 8616 4837 4560 -654 827 -1486 C ATOM 3069 CG ARG A 296 -25.062 -24.598 2.124 1.00 51.77 C ANISOU 3069 CG ARG A 296 9332 5428 4912 -770 886 -1679 C ATOM 3070 CD ARG A 296 -23.695 -24.600 1.459 1.00 57.45 C ANISOU 3070 CD ARG A 296 10074 6135 5619 -522 1094 -1897 C ATOM 3071 NE ARG A 296 -22.966 -25.849 1.657 1.00 49.54 N ANISOU 3071 NE ARG A 296 9251 4818 4753 -324 1146 -2032 N ATOM 3072 CZ ARG A 296 -21.979 -26.009 2.534 1.00 51.45 C ANISOU 3072 CZ ARG A 296 9359 4997 5191 -48 1211 -1995 C ATOM 3073 NH1 ARG A 296 -21.370 -27.181 2.641 1.00 53.78 N ANISOU 3073 NH1 ARG A 296 9831 4985 5617 135 1245 -2118 N ATOM 3074 NH2 ARG A 296 -21.600 -24.996 3.302 1.00 50.74 N ANISOU 3074 NH2 ARG A 296 8966 5144 5170 45 1234 -1834 N ATOM 3075 N GLN A 297 -27.419 -26.536 4.148 1.00 47.14 N ANISOU 3075 N GLN A 297 8943 4446 4522 -1173 449 -1293 N ATOM 3076 CA GLN A 297 -28.444 -27.445 3.651 1.00 52.41 C ANISOU 3076 CA GLN A 297 9870 4934 5111 -1453 303 -1314 C ATOM 3077 C GLN A 297 -29.812 -27.091 4.222 1.00 48.10 C ANISOU 3077 C GLN A 297 9177 4560 4537 -1726 141 -1068 C ATOM 3078 O GLN A 297 -30.831 -27.238 3.549 1.00 49.08 O ANISOU 3078 O GLN A 297 9405 4707 4535 -2006 26 -1061 O ATOM 3079 CB GLN A 297 -28.088 -28.896 3.986 1.00 57.79 C ANISOU 3079 CB GLN A 297 10818 5219 5921 -1382 262 -1380 C ATOM 3080 CG GLN A 297 -26.868 -29.423 3.242 1.00 64.70 C ANISOU 3080 CG GLN A 297 11880 5887 6815 -1129 418 -1658 C ATOM 3081 CD GLN A 297 -26.562 -30.872 3.572 1.00 73.86 C ANISOU 3081 CD GLN A 297 13317 6623 8123 -1047 363 -1722 C ATOM 3082 OE1 GLN A 297 -27.061 -31.414 4.558 1.00 78.42 O ANISOU 3082 OE1 GLN A 297 13907 7075 8815 -1139 217 -1526 O ATOM 3083 NE2 GLN A 297 -25.739 -31.507 2.745 1.00 73.21 N ANISOU 3083 NE2 GLN A 297 13461 6318 8038 -873 480 -1997 N ATOM 3084 N THR A 298 -29.829 -26.622 5.465 1.00 46.15 N ANISOU 3084 N THR A 298 8683 4447 4403 -1646 133 -870 N ATOM 3085 CA THR A 298 -31.074 -26.205 6.097 1.00 45.04 C ANISOU 3085 CA THR A 298 8363 4506 4243 -1871 9 -640 C ATOM 3086 C THR A 298 -31.577 -24.911 5.465 1.00 45.79 C ANISOU 3086 C THR A 298 8260 4921 4217 -1948 27 -622 C ATOM 3087 O THR A 298 -32.778 -24.745 5.249 1.00 43.48 O ANISOU 3087 O THR A 298 7918 4754 3848 -2203 -93 -514 O ATOM 3088 CB THR A 298 -30.907 -26.009 7.617 1.00 43.60 C ANISOU 3088 CB THR A 298 7973 4397 4196 -1754 14 -448 C ATOM 3089 OG1 THR A 298 -30.299 -27.174 8.187 1.00 45.33 O ANISOU 3089 OG1 THR A 298 8375 4311 4538 -1654 -5 -457 O ATOM 3090 CG2 THR A 298 -32.257 -25.774 8.278 1.00 43.09 C ANISOU 3090 CG2 THR A 298 7748 4520 4106 -2001 -106 -223 C ATOM 3091 N PHE A 299 -30.651 -24.002 5.168 1.00 41.75 N ANISOU 3091 N PHE A 299 7630 4539 3695 -1731 169 -716 N ATOM 3092 CA PHE A 299 -30.987 -22.754 4.487 1.00 45.19 C ANISOU 3092 CA PHE A 299 7902 5249 4020 -1785 186 -706 C ATOM 3093 C PHE A 299 -31.671 -23.027 3.150 1.00 47.51 C ANISOU 3093 C PHE A 299 8385 5518 4148 -2025 105 -797 C ATOM 3094 O PHE A 299 -32.688 -22.413 2.831 1.00 46.02 O ANISOU 3094 O PHE A 299 8083 5520 3881 -2216 5 -689 O ATOM 3095 CB PHE A 299 -29.738 -21.896 4.262 1.00 38.92 C ANISOU 3095 CB PHE A 299 7003 4551 3233 -1527 352 -812 C ATOM 3096 CG PHE A 299 -29.224 -21.223 5.506 1.00 36.84 C ANISOU 3096 CG PHE A 299 6494 4401 3101 -1331 410 -695 C ATOM 3097 CD1 PHE A 299 -29.995 -21.174 6.656 1.00 36.05 C ANISOU 3097 CD1 PHE A 299 6252 4371 3075 -1401 325 -504 C ATOM 3098 CD2 PHE A 299 -27.971 -20.630 5.520 1.00 39.66 C ANISOU 3098 CD2 PHE A 299 6761 4811 3496 -1091 552 -777 C ATOM 3099 CE1 PHE A 299 -29.523 -20.554 7.799 1.00 34.34 C ANISOU 3099 CE1 PHE A 299 5829 4263 2956 -1232 378 -410 C ATOM 3100 CE2 PHE A 299 -27.493 -20.008 6.660 1.00 34.12 C ANISOU 3100 CE2 PHE A 299 5847 4214 2904 -930 591 -672 C ATOM 3101 CZ PHE A 299 -28.271 -19.971 7.800 1.00 34.14 C ANISOU 3101 CZ PHE A 299 5729 4274 2967 -1000 504 -494 C ATOM 3102 N AARG A 300 -31.108 -23.953 2.378 0.54 49.11 N ANISOU 3102 N AARG A 300 8876 5485 4298 -2009 145 -999 N ATOM 3103 N BARG A 300 -31.112 -23.953 2.378 0.46 49.15 N ANISOU 3103 N BARG A 300 8882 5491 4303 -2009 145 -999 N ATOM 3104 CA AARG A 300 -31.655 -24.303 1.071 0.54 52.89 C ANISOU 3104 CA AARG A 300 9579 5920 4596 -2240 73 -1116 C ATOM 3105 CA BARG A 300 -31.661 -24.295 1.069 0.46 52.84 C ANISOU 3105 CA BARG A 300 9572 5916 4589 -2241 73 -1115 C ATOM 3106 C AARG A 300 -33.076 -24.850 1.179 0.54 53.11 C ANISOU 3106 C AARG A 300 9661 5923 4596 -2561 -133 -973 C ATOM 3107 C BARG A 300 -33.078 -24.852 1.177 0.46 53.14 C ANISOU 3107 C BARG A 300 9665 5927 4599 -2562 -134 -973 C ATOM 3108 O AARG A 300 -33.944 -24.500 0.381 0.54 54.13 O ANISOU 3108 O AARG A 300 9789 6193 4585 -2795 -240 -939 O ATOM 3109 O BARG A 300 -33.947 -24.510 0.376 0.46 54.16 O ANISOU 3109 O BARG A 300 9796 6195 4588 -2797 -241 -940 O ATOM 3110 CB AARG A 300 -30.756 -25.322 0.365 0.54 58.38 C ANISOU 3110 CB AARG A 300 10595 6333 5252 -2143 167 -1378 C ATOM 3111 CB BARG A 300 -30.758 -25.302 0.354 0.46 58.36 C ANISOU 3111 CB BARG A 300 10590 6337 5248 -2143 168 -1378 C ATOM 3112 CG AARG A 300 -29.448 -24.744 -0.155 0.54 60.67 C ANISOU 3112 CG AARG A 300 10847 6697 5509 -1882 375 -1549 C ATOM 3113 CG BARG A 300 -29.405 -24.741 -0.054 0.46 60.12 C ANISOU 3113 CG BARG A 300 10762 6624 5456 -1864 379 -1541 C ATOM 3114 CD AARG A 300 -28.819 -25.649 -1.207 0.54 65.10 C ANISOU 3114 CD AARG A 300 11736 7034 5965 -1849 464 -1834 C ATOM 3115 CD BARG A 300 -28.628 -25.734 -0.903 0.46 64.62 C ANISOU 3115 CD BARG A 300 11651 6940 5963 -1782 481 -1822 C ATOM 3116 NE AARG A 300 -28.210 -26.843 -0.628 0.54 66.60 N ANISOU 3116 NE AARG A 300 12095 6895 6315 -1679 499 -1925 N ATOM 3117 NE BARG A 300 -27.361 -25.180 -1.372 0.46 64.90 N ANISOU 3117 NE BARG A 300 11612 7076 5970 -1529 695 -1974 N ATOM 3118 CZ AARG A 300 -26.905 -26.988 -0.418 0.54 66.70 C ANISOU 3118 CZ AARG A 300 12086 6821 6437 -1357 676 -2051 C ATOM 3119 CZ BARG A 300 -27.222 -24.475 -2.491 0.46 63.29 C ANISOU 3119 CZ BARG A 300 11310 7092 5645 -1550 747 -2001 C ATOM 3120 NH1AARG A 300 -26.067 -26.012 -0.743 0.54 65.60 N ANISOU 3120 NH1AARG A 300 11760 6912 6253 -1189 840 -2102 N ATOM 3121 NH1BARG A 300 -26.031 -24.010 -2.840 0.46 63.27 N ANISOU 3121 NH1BARG A 300 11179 7197 5662 -1309 926 -2092 N ATOM 3122 NH2AARG A 300 -26.435 -28.109 0.113 0.54 67.32 N ANISOU 3122 NH2AARG A 300 12322 6582 6675 -1208 681 -2115 N ATOM 3123 NH2BARG A 300 -28.276 -24.234 -3.259 0.46 63.02 N ANISOU 3123 NH2BARG A 300 11296 7173 5477 -1817 609 -1921 N ATOM 3124 N LYS A 301 -33.307 -25.704 2.171 1.00 51.77 N ANISOU 3124 N LYS A 301 9530 5582 4557 -2583 -198 -876 N ATOM 3125 CA LYS A 301 -34.625 -26.296 2.384 1.00 55.53 C ANISOU 3125 CA LYS A 301 10046 6035 5019 -2900 -392 -722 C ATOM 3126 C LYS A 301 -35.670 -25.243 2.744 1.00 53.37 C ANISOU 3126 C LYS A 301 9440 6103 4737 -3025 -468 -496 C ATOM 3127 O LYS A 301 -36.818 -25.322 2.307 1.00 56.78 O ANISOU 3127 O LYS A 301 9868 6621 5083 -3315 -623 -405 O ATOM 3128 CB LYS A 301 -34.563 -27.362 3.479 1.00 59.43 C ANISOU 3128 CB LYS A 301 10630 6287 5662 -2883 -435 -641 C ATOM 3129 CG LYS A 301 -33.783 -28.606 3.091 1.00 67.58 C ANISOU 3129 CG LYS A 301 12029 6930 6717 -2808 -408 -850 C ATOM 3130 CD LYS A 301 -33.784 -29.629 4.215 1.00 70.16 C ANISOU 3130 CD LYS A 301 12441 7013 7202 -2805 -477 -733 C ATOM 3131 CE LYS A 301 -33.034 -30.888 3.814 1.00 72.28 C ANISOU 3131 CE LYS A 301 13088 6861 7515 -2717 -464 -943 C ATOM 3132 NZ LYS A 301 -32.989 -31.878 4.925 1.00 74.72 N ANISOU 3132 NZ LYS A 301 13487 6912 7991 -2707 -546 -810 N ATOM 3133 N ILE A 302 -35.267 -24.261 3.542 1.00 48.02 N ANISOU 3133 N ILE A 302 8479 5614 4151 -2803 -363 -409 N ATOM 3134 CA ILE A 302 -36.159 -23.177 3.938 1.00 48.91 C ANISOU 3134 CA ILE A 302 8266 6043 4274 -2867 -410 -216 C ATOM 3135 C ILE A 302 -36.530 -22.300 2.744 1.00 54.69 C ANISOU 3135 C ILE A 302 8949 6960 4872 -2959 -448 -250 C ATOM 3136 O ILE A 302 -37.699 -21.966 2.544 1.00 55.01 O ANISOU 3136 O ILE A 302 8854 7175 4871 -3171 -581 -110 O ATOM 3137 CB ILE A 302 -35.523 -22.296 5.032 1.00 42.30 C ANISOU 3137 CB ILE A 302 7171 5343 3558 -2590 -279 -149 C ATOM 3138 CG1 ILE A 302 -35.323 -23.099 6.318 1.00 41.40 C ANISOU 3138 CG1 ILE A 302 7074 5091 3567 -2532 -268 -67 C ATOM 3139 CG2 ILE A 302 -36.384 -21.075 5.306 1.00 42.58 C ANISOU 3139 CG2 ILE A 302 6885 5694 3600 -2625 -312 11 C ATOM 3140 CD1 ILE A 302 -34.653 -22.313 7.429 1.00 39.93 C ANISOU 3140 CD1 ILE A 302 6661 5029 3482 -2275 -148 -9 C ATOM 3141 N ILE A 303 -35.526 -21.938 1.952 1.00 53.67 N ANISOU 3141 N ILE A 303 8922 6798 4674 -2804 -334 -427 N ATOM 3142 CA ILE A 303 -35.716 -21.050 0.810 1.00 55.77 C ANISOU 3142 CA ILE A 303 9152 7237 4801 -2877 -360 -457 C ATOM 3143 C ILE A 303 -36.526 -21.707 -0.308 1.00 67.08 C ANISOU 3143 C ILE A 303 10804 8614 6070 -3190 -515 -498 C ATOM 3144 O ILE A 303 -37.479 -21.116 -0.819 1.00 66.94 O ANISOU 3144 O ILE A 303 10666 8789 5978 -3376 -647 -380 O ATOM 3145 CB ILE A 303 -34.361 -20.582 0.247 1.00 51.53 C ANISOU 3145 CB ILE A 303 8684 6680 4216 -2647 -186 -638 C ATOM 3146 CG1 ILE A 303 -33.602 -19.781 1.306 1.00 49.61 C ANISOU 3146 CG1 ILE A 303 8201 6523 4124 -2362 -54 -581 C ATOM 3147 CG2 ILE A 303 -34.558 -19.749 -1.009 1.00 52.67 C ANISOU 3147 CG2 ILE A 303 8827 6994 4192 -2757 -224 -663 C ATOM 3148 CD1 ILE A 303 -32.107 -19.744 1.091 1.00 52.22 C ANISOU 3148 CD1 ILE A 303 8617 6767 4456 -2118 129 -760 C ATOM 3149 N ARG A 304 -36.145 -22.925 -0.682 1.00 78.36 N ANISOU 3149 N ARG A 304 12556 9772 7447 -3247 -507 -666 N ATOM 3150 CA ARG A 304 -36.834 -23.657 -1.743 1.00 89.21 C ANISOU 3150 CA ARG A 304 14136 11060 8700 -3492 -628 -698 C ATOM 3151 C ARG A 304 -38.304 -23.889 -1.406 1.00 91.02 C ANISOU 3151 C ARG A 304 14243 11381 8961 -3758 -824 -468 C ATOM 3152 O ARG A 304 -39.191 -23.524 -2.177 1.00 94.36 O ANISOU 3152 O ARG A 304 14576 11961 9314 -3910 -926 -354 O ATOM 3153 CB ARG A 304 -36.143 -24.996 -2.011 1.00 98.98 C ANISOU 3153 CB ARG A 304 15713 11961 9932 -3442 -566 -901 C ATOM 3154 CG ARG A 304 -34.788 -24.877 -2.692 1.00107.43 C ANISOU 3154 CG ARG A 304 16903 12959 10956 -3189 -366 -1133 C ATOM 3155 CD ARG A 304 -34.058 -26.213 -2.705 1.00116.08 C ANISOU 3155 CD ARG A 304 18298 13712 12094 -3088 -297 -1330 C ATOM 3156 NE ARG A 304 -32.713 -26.099 -3.262 1.00120.95 N ANISOU 3156 NE ARG A 304 18980 14284 12691 -2814 -88 -1546 N ATOM 3157 CZ ARG A 304 -31.832 -27.094 -3.297 1.00125.74 C ANISOU 3157 CZ ARG A 304 19803 14617 13355 -2642 15 -1741 C ATOM 3158 NH1 ARG A 304 -30.630 -26.900 -3.823 1.00126.77 N ANISOU 3158 NH1 ARG A 304 19935 14758 13474 -2387 210 -1919 N ATOM 3159 NH2 ARG A 304 -32.152 -28.283 -2.805 1.00128.59 N ANISOU 3159 NH2 ARG A 304 20360 14698 13799 -2718 -81 -1744 N ATOM 3160 N SER A 305 -38.557 -24.496 -0.252 1.00 91.33 N ANISOU 3160 N SER A 305 14265 11324 9112 -3812 -873 -387 N ATOM 3161 CA SER A 305 -39.922 -24.756 0.187 1.00 94.28 C ANISOU 3161 CA SER A 305 14487 11804 9530 -4045 -1036 -151 C ATOM 3162 C SER A 305 -40.579 -23.483 0.712 1.00 92.57 C ANISOU 3162 C SER A 305 13876 11928 9370 -4034 -1064 44 C ATOM 3163 O SER A 305 -40.759 -23.318 1.919 1.00 92.15 O ANISOU 3163 O SER A 305 13613 11954 9447 -3972 -1038 175 O ATOM 3164 CB SER A 305 -39.945 -25.844 1.262 1.00 96.32 C ANISOU 3164 CB SER A 305 14848 11849 9899 -4101 -1067 -108 C ATOM 3165 OG SER A 305 -39.446 -27.071 0.757 1.00100.70 O ANISOU 3165 OG SER A 305 15769 12073 10420 -4106 -1060 -277 O TER 3166 SER A 305 HETATM 3167 NA NA A2400 -23.589 -8.237 16.597 1.00 44.22 NA ANISOU 3167 NA NA A2400 5225 6977 4599 64 752 -72 NA HETATM 3168 C01 F9Q A2401 -26.221 5.610 17.023 1.00 20.68 C ANISOU 3168 C01 F9Q A2401 1931 4036 1890 347 434 -383 C HETATM 3169 C02 F9Q A2401 -24.784 5.167 16.860 1.00 27.44 C ANISOU 3169 C02 F9Q A2401 2834 4904 2689 259 440 -360 C HETATM 3170 C03 F9Q A2401 -23.645 6.053 17.306 1.00 28.02 C ANISOU 3170 C03 F9Q A2401 2962 4922 2763 235 397 -399 C HETATM 3171 C04 F9Q A2401 -22.254 5.608 17.149 1.00 23.85 C ANISOU 3171 C04 F9Q A2401 2443 4431 2189 153 405 -365 C HETATM 3172 C05 F9Q A2401 -21.969 4.303 16.542 1.00 19.09 C ANISOU 3172 C05 F9Q A2401 1809 3899 1545 117 465 -308 C HETATM 3173 C06 F9Q A2401 -23.113 3.424 16.106 1.00 18.77 C ANISOU 3173 C06 F9Q A2401 1746 3886 1498 139 504 -283 C HETATM 3174 CL7 F9Q A2401 -22.783 1.874 15.401 1.00 24.43 CL ANISOU 3174 CL7 F9Q A2401 2477 4612 2193 92 548 -231 CL HETATM 3175 N08 F9Q A2401 -24.492 3.869 16.269 1.00 21.57 N ANISOU 3175 N08 F9Q A2401 2079 4223 1893 197 486 -300 N HETATM 3176 C09 F9Q A2401 -21.123 6.508 17.591 1.00 25.47 C ANISOU 3176 C09 F9Q A2401 2687 4596 2396 105 348 -390 C HETATM 3177 C10 F9Q A2401 -19.982 6.036 18.420 1.00 20.29 C ANISOU 3177 C10 F9Q A2401 2011 4015 1683 76 363 -399 C HETATM 3178 N11 F9Q A2401 -18.978 6.934 18.772 1.00 21.00 N ANISOU 3178 N11 F9Q A2401 2131 4072 1775 9 293 -413 N HETATM 3179 C12 F9Q A2401 -19.046 8.291 18.353 1.00 21.80 C ANISOU 3179 C12 F9Q A2401 2300 4049 1933 -32 208 -423 C HETATM 3180 N13 F9Q A2401 -18.021 9.190 18.724 1.00 30.02 N ANISOU 3180 N13 F9Q A2401 3384 5049 2974 -122 124 -433 N HETATM 3181 N14 F9Q A2401 -20.159 8.749 17.552 1.00 30.81 N ANISOU 3181 N14 F9Q A2401 3469 5100 3137 11 191 -412 N HETATM 3182 N15 F9Q A2401 -21.172 7.854 17.186 1.00 21.18 N ANISOU 3182 N15 F9Q A2401 2201 3932 1914 80 260 -394 N HETATM 3183 C16 F9Q A2401 -19.825 4.613 18.903 1.00 19.69 C ANISOU 3183 C16 F9Q A2401 1883 4045 1554 105 436 -380 C HETATM 3184 C17 F9Q A2401 -20.992 3.825 19.446 1.00 19.43 C ANISOU 3184 C17 F9Q A2401 1836 4053 1493 177 495 -401 C HETATM 3185 C18 F9Q A2401 -20.786 2.406 19.916 1.00 19.06 C ANISOU 3185 C18 F9Q A2401 1780 4020 1443 181 517 -348 C HETATM 3186 C19 F9Q A2401 -19.408 1.782 19.869 1.00 19.02 C ANISOU 3186 C19 F9Q A2401 1748 4045 1434 151 510 -299 C HETATM 3187 F20 F9Q A2401 -19.228 0.528 20.292 1.00 23.37 F ANISOU 3187 F20 F9Q A2401 2297 4587 1995 169 518 -252 F HETATM 3188 C21 F9Q A2401 -18.234 2.577 19.337 1.00 19.32 C ANISOU 3188 C21 F9Q A2401 1746 4140 1454 100 500 -299 C HETATM 3189 C22 F9Q A2401 -18.449 3.992 18.860 1.00 19.63 C ANISOU 3189 C22 F9Q A2401 1829 4103 1527 59 444 -328 C HETATM 3190 C1 CLR A2402 -38.127 10.932 21.784 1.00 37.69 C ANISOU 3190 C1 CLR A2402 3088 6402 4831 1799 849 -980 C HETATM 3191 C2 CLR A2402 -37.886 12.428 22.084 1.00 39.45 C ANISOU 3191 C2 CLR A2402 3403 6423 5164 2007 827 -1151 C HETATM 3192 C3 CLR A2402 -38.213 12.770 23.512 1.00 44.47 C ANISOU 3192 C3 CLR A2402 4087 7068 5743 2064 975 -1304 C HETATM 3193 C4 CLR A2402 -37.427 11.871 24.484 1.00 39.94 C ANISOU 3193 C4 CLR A2402 3635 6603 4938 1868 1053 -1323 C HETATM 3194 C5 CLR A2402 -37.599 10.403 24.175 1.00 38.11 C ANISOU 3194 C5 CLR A2402 3321 6543 4616 1674 1056 -1146 C HETATM 3195 C6 CLR A2402 -37.880 9.572 25.195 1.00 38.39 C ANISOU 3195 C6 CLR A2402 3355 6710 4521 1565 1160 -1133 C HETATM 3196 C7 CLR A2402 -38.127 8.080 25.060 1.00 37.01 C ANISOU 3196 C7 CLR A2402 3121 6682 4259 1377 1160 -971 C HETATM 3197 C8 CLR A2402 -37.726 7.550 23.686 1.00 36.12 C ANISOU 3197 C8 CLR A2402 2993 6550 4181 1291 1039 -836 C HETATM 3198 C9 CLR A2402 -38.086 8.549 22.579 1.00 35.51 C ANISOU 3198 C9 CLR A2402 2825 6388 4281 1448 960 -836 C HETATM 3199 C10 CLR A2402 -37.448 9.939 22.738 1.00 37.17 C ANISOU 3199 C10 CLR A2402 3138 6431 4555 1610 935 -992 C HETATM 3200 C11 CLR A2402 -37.843 7.911 21.209 1.00 33.68 C ANISOU 3200 C11 CLR A2402 2555 6178 4064 1344 848 -684 C HETATM 3201 C12 CLR A2402 -38.478 6.523 21.042 1.00 33.14 C ANISOU 3201 C12 CLR A2402 2408 6253 3930 1177 861 -543 C HETATM 3202 C13 CLR A2402 -38.176 5.532 22.137 1.00 32.59 C ANISOU 3202 C13 CLR A2402 2434 6243 3706 1040 938 -550 C HETATM 3203 C14 CLR A2402 -38.484 6.260 23.439 1.00 35.57 C ANISOU 3203 C14 CLR A2402 2820 6618 4077 1154 1044 -688 C HETATM 3204 C15 CLR A2402 -38.351 5.173 24.500 1.00 36.84 C ANISOU 3204 C15 CLR A2402 3044 6866 4086 1010 1107 -663 C HETATM 3205 C16 CLR A2402 -38.879 3.937 23.776 1.00 39.05 C ANISOU 3205 C16 CLR A2402 3245 7238 4356 872 1061 -504 C HETATM 3206 C17 CLR A2402 -39.045 4.271 22.292 1.00 32.88 C ANISOU 3206 C17 CLR A2402 2385 6419 3689 909 966 -439 C HETATM 3207 C18 CLR A2402 -36.698 5.065 22.050 1.00 30.36 C ANISOU 3207 C18 CLR A2402 2329 5889 3319 925 893 -544 C HETATM 3208 C19 CLR A2402 -35.928 9.889 22.410 1.00 34.12 C ANISOU 3208 C19 CLR A2402 2914 5970 4081 1520 861 -1005 C HETATM 3209 C20 CLR A2402 -38.792 3.013 21.445 1.00 35.69 C ANISOU 3209 C20 CLR A2402 2767 6807 3987 732 892 -301 C HETATM 3210 C21 CLR A2402 -39.010 3.229 19.946 1.00 32.87 C ANISOU 3210 C21 CLR A2402 2325 6445 3721 739 793 -217 C HETATM 3211 C22 CLR A2402 -39.701 1.858 21.925 1.00 38.95 C ANISOU 3211 C22 CLR A2402 3106 7355 4339 616 932 -218 C HETATM 3212 C23 CLR A2402 -39.577 0.553 21.125 1.00 40.99 C ANISOU 3212 C23 CLR A2402 3391 7643 4540 438 861 -88 C HETATM 3213 C24 CLR A2402 -40.505 -0.517 21.707 1.00 49.27 C ANISOU 3213 C24 CLR A2402 4366 8826 5530 326 898 -11 C HETATM 3214 C25 CLR A2402 -40.222 -1.935 21.189 1.00 51.91 C ANISOU 3214 C25 CLR A2402 4768 9168 5787 138 837 100 C HETATM 3215 C26 CLR A2402 -40.872 -2.995 22.076 1.00 53.56 C ANISOU 3215 C26 CLR A2402 4943 9491 5917 23 879 162 C HETATM 3216 C27 CLR A2402 -40.680 -2.121 19.745 1.00 50.98 C ANISOU 3216 C27 CLR A2402 4570 9079 5721 70 748 196 C HETATM 3217 O1 CLR A2402 -37.878 14.142 23.779 1.00 43.10 O ANISOU 3217 O1 CLR A2402 4037 6680 5658 2239 945 -1476 O HETATM 3218 C1 CLR A2403 -8.368 10.960 13.283 1.00 31.77 C ANISOU 3218 C1 CLR A2403 3003 5947 3121 -1296 30 344 C HETATM 3219 C2 CLR A2403 -8.342 12.500 13.348 1.00 33.31 C ANISOU 3219 C2 CLR A2403 3329 5988 3341 -1477 -141 389 C HETATM 3220 C3 CLR A2403 -6.974 13.065 13.069 1.00 35.81 C ANISOU 3220 C3 CLR A2403 3532 6432 3644 -1700 -186 509 C HETATM 3221 C4 CLR A2403 -6.402 12.532 11.743 1.00 35.34 C ANISOU 3221 C4 CLR A2403 3328 6572 3526 -1760 -42 604 C HETATM 3222 C5 CLR A2403 -6.504 11.031 11.625 1.00 34.67 C ANISOU 3222 C5 CLR A2403 3127 6625 3422 -1553 138 537 C HETATM 3223 C6 CLR A2403 -5.425 10.346 11.199 1.00 38.78 C ANISOU 3223 C6 CLR A2403 3440 7379 3917 -1569 264 585 C HETATM 3224 C7 CLR A2403 -5.388 8.845 10.955 1.00 40.55 C ANISOU 3224 C7 CLR A2403 3566 7709 4134 -1352 439 513 C HETATM 3225 C8 CLR A2403 -6.780 8.228 11.016 1.00 36.47 C ANISOU 3225 C8 CLR A2403 3189 7057 3612 -1187 478 413 C HETATM 3226 C9 CLR A2403 -7.596 8.860 12.151 1.00 31.17 C ANISOU 3226 C9 CLR A2403 2669 6185 2989 -1157 322 362 C HETATM 3227 C10 CLR A2403 -7.818 10.369 11.981 1.00 33.99 C ANISOU 3227 C10 CLR A2403 3159 6403 3351 -1339 170 418 C HETATM 3228 C11 CLR A2403 -8.896 8.089 12.378 1.00 31.46 C ANISOU 3228 C11 CLR A2403 2815 6108 3032 -967 364 261 C HETATM 3229 C12 CLR A2403 -8.710 6.570 12.460 1.00 26.43 C ANISOU 3229 C12 CLR A2403 2071 5577 2394 -797 505 212 C HETATM 3230 C13 CLR A2403 -7.963 5.970 11.301 1.00 33.11 C ANISOU 3230 C13 CLR A2403 2832 6533 3215 -797 626 238 C HETATM 3231 C14 CLR A2403 -6.648 6.736 11.260 1.00 37.35 C ANISOU 3231 C14 CLR A2403 3243 7192 3758 -953 585 330 C HETATM 3232 C15 CLR A2403 -5.779 5.951 10.282 1.00 37.79 C ANISOU 3232 C15 CLR A2403 3238 7299 3820 -880 693 324 C HETATM 3233 C16 CLR A2403 -6.245 4.510 10.478 1.00 34.44 C ANISOU 3233 C16 CLR A2403 2855 6789 3441 -652 770 226 C HETATM 3234 C17 CLR A2403 -7.473 4.513 11.390 1.00 34.42 C ANISOU 3234 C17 CLR A2403 2950 6688 3439 -600 708 182 C HETATM 3235 C18 CLR A2403 -8.794 6.138 9.995 1.00 34.19 C ANISOU 3235 C18 CLR A2403 3097 6602 3291 -843 661 237 C HETATM 3236 C19 CLR A2403 -8.821 10.660 10.828 1.00 29.10 C ANISOU 3236 C19 CLR A2403 2673 5685 2697 -1361 184 438 C HETATM 3237 C20 CLR A2403 -8.401 3.335 11.045 1.00 34.14 C ANISOU 3237 C20 CLR A2403 3031 6524 3417 -441 775 97 C HETATM 3238 C21 CLR A2403 -9.630 3.251 11.951 1.00 30.52 C ANISOU 3238 C21 CLR A2403 2662 5974 2959 -380 721 55 C HETATM 3239 C22 CLR A2403 -7.636 1.995 11.129 1.00 37.45 C ANISOU 3239 C22 CLR A2403 3382 6942 3905 -287 855 65 C HETATM 3240 C23 CLR A2403 -8.521 0.747 11.275 1.00 33.64 C ANISOU 3240 C23 CLR A2403 3004 6324 3453 -139 893 -7 C HETATM 3241 C24 CLR A2403 -7.676 -0.524 11.155 1.00 37.72 C ANISOU 3241 C24 CLR A2403 3451 6842 4037 -7 986 -34 C HETATM 3242 C25 CLR A2403 -8.505 -1.804 10.975 1.00 39.09 C ANISOU 3242 C25 CLR A2403 3742 6879 4231 109 1042 -105 C HETATM 3243 C26 CLR A2403 -9.310 -2.116 12.233 1.00 37.26 C ANISOU 3243 C26 CLR A2403 3553 6587 4019 166 962 -103 C HETATM 3244 C27 CLR A2403 -9.441 -1.720 9.772 1.00 45.36 C ANISOU 3244 C27 CLR A2403 4682 7599 4955 46 1078 -143 C HETATM 3245 O1 CLR A2403 -7.050 14.498 12.986 1.00 37.86 O ANISOU 3245 O1 CLR A2403 3942 6515 3928 -1881 -353 561 O HETATM 3246 C1 CLR A2404 -3.052 8.386 21.303 1.00 33.34 C ANISOU 3246 C1 CLR A2404 2483 6841 3345 -1212 -386 396 C HETATM 3247 C2 CLR A2404 -2.763 9.901 21.226 1.00 34.58 C ANISOU 3247 C2 CLR A2404 2735 6924 3479 -1458 -522 407 C HETATM 3248 C3 CLR A2404 -1.783 10.247 20.136 1.00 35.81 C ANISOU 3248 C3 CLR A2404 2719 7209 3679 -1601 -490 530 C HETATM 3249 C4 CLR A2404 -2.200 9.646 18.780 1.00 34.70 C ANISOU 3249 C4 CLR A2404 2534 7086 3566 -1480 -295 532 C HETATM 3250 C5 CLR A2404 -2.550 8.182 18.872 1.00 33.46 C ANISOU 3250 C5 CLR A2404 2306 6977 3429 -1224 -158 491 C HETATM 3251 C6 CLR A2404 -2.023 7.335 17.964 1.00 33.75 C ANISOU 3251 C6 CLR A2404 2157 7161 3507 -1136 -5 541 C HETATM 3252 C7 CLR A2404 -2.367 5.859 17.853 1.00 34.81 C ANISOU 3252 C7 CLR A2404 2253 7300 3672 -878 138 495 C HETATM 3253 C8 CLR A2404 -3.541 5.487 18.752 1.00 31.11 C ANISOU 3253 C8 CLR A2404 1963 6681 3175 -760 100 402 C HETATM 3254 C9 CLR A2404 -3.449 6.210 20.103 1.00 31.62 C ANISOU 3254 C9 CLR A2404 2104 6708 3202 -867 -86 399 C HETATM 3255 C10 CLR A2404 -3.483 7.741 19.980 1.00 32.20 C ANISOU 3255 C10 CLR A2404 2299 6697 3240 -1086 -198 392 C HETATM 3256 C11 CLR A2404 -4.492 5.660 21.081 1.00 30.36 C ANISOU 3256 C11 CLR A2404 2098 6434 3002 -733 -104 314 C HETATM 3257 C12 CLR A2404 -4.555 4.129 21.145 1.00 34.42 C ANISOU 3257 C12 CLR A2404 2524 6997 3558 -526 -3 329 C HETATM 3258 C13 CLR A2404 -4.671 3.439 19.813 1.00 33.90 C ANISOU 3258 C13 CLR A2404 2398 6941 3540 -421 170 322 C HETATM 3259 C14 CLR A2404 -3.523 3.990 18.979 1.00 30.79 C ANISOU 3259 C14 CLR A2404 1833 6685 3179 -542 191 398 C HETATM 3260 C15 CLR A2404 -3.513 3.115 17.730 1.00 33.10 C ANISOU 3260 C15 CLR A2404 2122 6943 3512 -404 361 373 C HETATM 3261 C16 CLR A2404 -3.954 1.756 18.262 1.00 34.17 C ANISOU 3261 C16 CLR A2404 2285 7015 3682 -198 400 339 C HETATM 3262 C17 CLR A2404 -4.410 1.925 19.712 1.00 37.70 C ANISOU 3262 C17 CLR A2404 2763 7475 4088 -223 271 345 C HETATM 3263 C18 CLR A2404 -6.065 3.737 19.191 1.00 27.71 C ANISOU 3263 C18 CLR A2404 1820 5997 2712 -407 233 226 C HETATM 3264 C19 CLR A2404 -4.912 8.236 19.618 1.00 30.71 C ANISOU 3264 C19 CLR A2404 2351 6298 3020 -1051 -169 285 C HETATM 3265 C20 CLR A2404 -5.509 0.904 20.044 1.00 38.83 C ANISOU 3265 C20 CLR A2404 3039 7495 4219 -66 318 285 C HETATM 3266 C21 CLR A2404 -5.884 0.889 21.525 1.00 28.03 C ANISOU 3266 C21 CLR A2404 1758 6092 2801 -74 188 291 C HETATM 3267 C22 CLR A2404 -5.065 -0.517 19.627 1.00 43.44 C ANISOU 3267 C22 CLR A2404 3538 8075 4891 115 417 307 C HETATM 3268 C23 CLR A2404 -6.082 -1.635 19.905 1.00 42.33 C ANISOU 3268 C23 CLR A2404 3509 7828 4748 256 461 266 C HETATM 3269 C24 CLR A2404 -5.359 -2.974 20.080 1.00 49.09 C ANISOU 3269 C24 CLR A2404 4266 8679 5707 422 482 321 C HETATM 3270 C25 CLR A2404 -5.701 -4.027 19.015 1.00 53.22 C ANISOU 3270 C25 CLR A2404 4876 9060 6284 547 616 251 C HETATM 3271 C26 CLR A2404 -7.118 -4.567 19.188 1.00 50.89 C ANISOU 3271 C26 CLR A2404 4749 8651 5935 585 638 200 C HETATM 3272 C27 CLR A2404 -5.520 -3.501 17.592 1.00 56.92 C ANISOU 3272 C27 CLR A2404 5385 9492 6749 478 710 185 C HETATM 3273 O1 CLR A2404 -1.706 11.673 19.992 1.00 36.89 O ANISOU 3273 O1 CLR A2404 2987 7233 3797 -1834 -621 541 O HETATM 3274 C1 OLA A2405 -36.347 15.296 12.741 1.00 79.14 C ANISOU 3274 C1 OLA A2405 8796 10430 10844 1536 -509 -28 C HETATM 3275 O1 OLA A2405 -35.676 16.307 12.393 1.00 81.21 O ANISOU 3275 O1 OLA A2405 9225 10459 11171 1517 -634 -5 O HETATM 3276 O2 OLA A2405 -37.201 15.445 13.630 1.00 83.02 O ANISOU 3276 O2 OLA A2405 9150 10971 11422 1747 -410 -149 O HETATM 3277 C2 OLA A2405 -36.134 13.934 12.110 1.00 72.46 C ANISOU 3277 C2 OLA A2405 7919 9795 9819 1307 -476 83 C HETATM 3278 C3 OLA A2405 -36.982 12.854 12.786 1.00 66.61 C ANISOU 3278 C3 OLA A2405 6988 9300 9021 1353 -321 30 C HETATM 3279 C4 OLA A2405 -36.226 11.554 13.029 1.00 58.37 C ANISOU 3279 C4 OLA A2405 5999 8416 7764 1166 -200 2 C HETATM 3280 C5 OLA A2405 -36.282 10.591 11.859 1.00 53.57 C ANISOU 3280 C5 OLA A2405 5382 7913 7061 959 -267 165 C HETATM 3281 C6 OLA A2405 -36.982 9.271 12.151 1.00 52.10 C ANISOU 3281 C6 OLA A2405 5055 7953 6788 904 -163 175 C HETATM 3282 C7 OLA A2405 -36.159 8.077 11.672 1.00 49.36 C ANISOU 3282 C7 OLA A2405 4820 7677 6257 680 -131 212 C HETATM 3283 C8 OLA A2405 -36.959 6.811 11.421 1.00 46.86 C ANISOU 3283 C8 OLA A2405 4393 7540 5870 571 -106 285 C HETATM 3284 C9 OLA A2405 -36.070 5.800 10.712 1.00 46.24 C ANISOU 3284 C9 OLA A2405 4463 7477 5629 359 -103 320 C HETATM 3285 C10 OLA A2405 -36.478 4.636 10.155 1.00 47.68 C ANISOU 3285 C10 OLA A2405 4627 7768 5721 206 -113 391 C HETATM 3286 C11 OLA A2405 -37.916 4.161 10.160 1.00 51.59 C ANISOU 3286 C11 OLA A2405 4933 8405 6263 200 -141 469 C HETATM 3287 C12 OLA A2405 -38.020 2.633 9.981 1.00 53.32 C ANISOU 3287 C12 OLA A2405 5181 8730 6347 15 -102 496 C HETATM 3288 C13 OLA A2405 -38.404 1.885 11.274 1.00 55.60 C ANISOU 3288 C13 OLA A2405 5370 9138 6616 55 39 432 C HETATM 3289 C14 OLA A2405 -39.270 0.639 11.024 1.00 58.96 C ANISOU 3289 C14 OLA A2405 5727 9696 6981 -111 20 518 C HETATM 3290 C15 OLA A2405 -39.412 -0.278 12.254 1.00 60.61 C ANISOU 3290 C15 OLA A2405 5886 10010 7134 -120 160 467 C HETATM 3291 C16 OLA A2405 -38.953 -1.724 11.996 1.00 60.61 C ANISOU 3291 C16 OLA A2405 6037 9993 6999 -317 172 480 C HETATM 3292 C17 OLA A2405 -40.088 -2.757 12.085 1.00 60.91 C ANISOU 3292 C17 OLA A2405 5959 10172 7011 -463 154 574 C HETATM 3293 C18 OLA A2405 -39.804 -4.016 11.252 1.00 58.44 C ANISOU 3293 C18 OLA A2405 5824 9796 6586 -684 94 610 C HETATM 3294 C1 OLA A2406 -8.430 14.817 8.462 1.00 72.69 C ANISOU 3294 C1 OLA A2406 8489 10946 8184 -2081 -201 839 C HETATM 3295 O1 OLA A2406 -8.577 15.821 7.712 1.00 74.36 O ANISOU 3295 O1 OLA A2406 8812 11056 8387 -2255 -311 959 O HETATM 3296 O2 OLA A2406 -8.727 14.942 9.662 1.00 74.06 O ANISOU 3296 O2 OLA A2406 8715 10989 8436 -1968 -275 736 O HETATM 3297 C2 OLA A2406 -7.910 13.495 7.934 1.00 68.54 C ANISOU 3297 C2 OLA A2406 7782 10686 7574 -2008 13 818 C HETATM 3298 C3 OLA A2406 -8.795 12.945 6.813 1.00 63.81 C ANISOU 3298 C3 OLA A2406 7245 10100 6901 -1946 104 816 C HETATM 3299 C4 OLA A2406 -9.371 11.569 7.123 1.00 59.52 C ANISOU 3299 C4 OLA A2406 6661 9595 6357 -1698 240 675 C HETATM 3300 C5 OLA A2406 -8.450 10.428 6.740 1.00 59.48 C ANISOU 3300 C5 OLA A2406 6476 9841 6283 -1658 437 649 C HETATM 3301 C6 OLA A2406 -9.127 9.278 6.006 1.00 59.15 C ANISOU 3301 C6 OLA A2406 6486 9789 6200 -1487 549 552 C HETATM 3302 C7 OLA A2406 -8.361 7.968 6.177 1.00 60.57 C ANISOU 3302 C7 OLA A2406 6559 10032 6421 -1291 671 443 C HETATM 3303 C8 OLA A2406 -9.235 6.742 6.375 1.00 60.10 C ANISOU 3303 C8 OLA A2406 6560 9885 6392 -1080 733 323 C HETATM 3304 C9 OLA A2406 -8.811 5.664 5.388 1.00 61.73 C ANISOU 3304 C9 OLA A2406 6762 10114 6579 -987 856 259 C HETATM 3305 C10 OLA A2406 -9.611 5.079 4.468 1.00 60.18 C ANISOU 3305 C10 OLA A2406 6677 9856 6332 -952 899 212 C HETATM 3306 C11 OLA A2406 -11.075 5.426 4.290 1.00 55.28 C ANISOU 3306 C11 OLA A2406 6189 9142 5671 -993 820 227 C HETATM 3307 C12 OLA A2406 -11.778 4.476 3.301 1.00 52.69 C ANISOU 3307 C12 OLA A2406 5963 8761 5294 -936 879 161 C HETATM 3308 C13 OLA A2406 -11.383 4.712 1.829 1.00 55.14 C ANISOU 3308 C13 OLA A2406 6304 9152 5496 -1066 918 198 C HETATM 3309 C1 OLA A2407 -11.275 -12.455 9.241 1.00 68.58 C ANISOU 3309 C1 OLA A2407 8132 9835 8091 968 1630 -738 C HETATM 3310 O1 OLA A2407 -11.161 -13.247 8.265 1.00 69.92 O ANISOU 3310 O1 OLA A2407 8395 9931 8239 1015 1745 -870 O HETATM 3311 O2 OLA A2407 -11.588 -11.278 8.997 1.00 71.10 O ANISOU 3311 O2 OLA A2407 8451 10219 8344 802 1579 -673 O HETATM 3312 C2 OLA A2407 -11.043 -12.902 10.671 1.00 63.55 C ANISOU 3312 C2 OLA A2407 7399 9196 7552 1120 1551 -651 C HETATM 3313 C3 OLA A2407 -9.712 -12.387 11.224 1.00 61.28 C ANISOU 3313 C3 OLA A2407 6897 9015 7372 1175 1529 -572 C HETATM 3314 C4 OLA A2407 -9.667 -10.875 11.414 1.00 57.74 C ANISOU 3314 C4 OLA A2407 6379 8686 6875 995 1448 -482 C HETATM 3315 C5 OLA A2407 -8.500 -10.412 12.265 1.00 57.62 C ANISOU 3315 C5 OLA A2407 6163 8782 6947 1047 1393 -387 C HETATM 3316 C6 OLA A2407 -8.692 -9.072 12.961 1.00 52.87 C ANISOU 3316 C6 OLA A2407 5520 8274 6294 901 1272 -288 C HETATM 3317 C7 OLA A2407 -8.564 -9.198 14.478 1.00 49.67 C ANISOU 3317 C7 OLA A2407 5022 7921 5931 976 1164 -185 C HETATM 3318 C1 OLA A2408 -20.406 -22.042 28.064 1.00 55.00 C ANISOU 3318 C1 OLA A2408 7383 7316 6200 17 -213 1598 C HETATM 3319 O1 OLA A2408 -20.874 -21.644 26.963 1.00 58.60 O ANISOU 3319 O1 OLA A2408 7835 7765 6667 22 -99 1422 O HETATM 3320 O2 OLA A2408 -20.460 -23.258 28.308 1.00 61.27 O ANISOU 3320 O2 OLA A2408 8317 7898 7064 -16 -323 1741 O HETATM 3321 C2 OLA A2408 -19.797 -21.086 29.071 1.00 50.64 C ANISOU 3321 C2 OLA A2408 6684 7010 5545 39 -229 1640 C HETATM 3322 C3 OLA A2408 -20.037 -19.623 28.689 1.00 46.58 C ANISOU 3322 C3 OLA A2408 6037 6725 4937 38 -91 1456 C HETATM 3323 C4 OLA A2408 -19.515 -18.634 29.723 1.00 43.72 C ANISOU 3323 C4 OLA A2408 5553 6601 4456 35 -111 1483 C HETATM 3324 C5 OLA A2408 -20.074 -17.235 29.560 1.00 41.80 C ANISOU 3324 C5 OLA A2408 5214 6578 4091 -14 13 1324 C HETATM 3325 C6 OLA A2408 -19.097 -16.217 28.988 1.00 42.97 C ANISOU 3325 C6 OLA A2408 5248 6772 4305 132 60 1178 C HETATM 3326 C7 OLA A2408 -19.627 -14.791 29.120 1.00 41.57 C ANISOU 3326 C7 OLA A2408 4991 6809 3994 70 151 1051 C HETATM 3327 C1 OLA A2409 -21.657 -8.930 3.068 1.00 76.24 C ANISOU 3327 C1 OLA A2409 10015 10859 8093 -401 1035 -598 C HETATM 3328 O1 OLA A2409 -21.100 -8.975 1.937 1.00 81.12 O ANISOU 3328 O1 OLA A2409 10691 11495 8636 -423 1086 -650 O HETATM 3329 O2 OLA A2409 -22.049 -10.000 3.563 1.00 78.29 O ANISOU 3329 O2 OLA A2409 10345 11053 8349 -388 1052 -652 O HETATM 3330 C2 OLA A2409 -21.852 -7.626 3.815 1.00 67.99 C ANISOU 3330 C2 OLA A2409 8832 9870 7133 -399 956 -480 C HETATM 3331 C3 OLA A2409 -21.934 -6.427 2.866 1.00 62.92 C ANISOU 3331 C3 OLA A2409 8169 9298 6440 -502 902 -422 C HETATM 3332 C4 OLA A2409 -23.220 -5.622 3.013 1.00 55.95 C ANISOU 3332 C4 OLA A2409 7250 8461 5549 -605 778 -331 C HETATM 3333 C5 OLA A2409 -23.153 -4.253 2.364 1.00 52.02 C ANISOU 3333 C5 OLA A2409 6710 8034 5023 -684 719 -255 C HETATM 3334 C6 OLA A2409 -24.428 -3.428 2.466 1.00 50.47 C ANISOU 3334 C6 OLA A2409 6472 7892 4813 -774 595 -157 C HETATM 3335 C7 OLA A2409 -24.164 -1.948 2.199 1.00 49.70 C ANISOU 3335 C7 OLA A2409 6316 7854 4712 -817 542 -71 C HETATM 3336 C1 OLA A2410 -20.451 14.167 3.324 1.00 87.29 C ANISOU 3336 C1 OLA A2410 11092 11920 10153 -1313 -601 966 C HETATM 3337 O1 OLA A2410 -19.496 14.397 2.532 1.00 88.97 O ANISOU 3337 O1 OLA A2410 11330 12224 10251 -1518 -591 1067 O HETATM 3338 O2 OLA A2410 -20.413 14.697 4.447 1.00 88.48 O ANISOU 3338 O2 OLA A2410 11246 11938 10436 -1200 -635 884 O HETATM 3339 C2 OLA A2410 -21.615 13.276 2.936 1.00 83.24 C ANISOU 3339 C2 OLA A2410 10549 11468 9611 -1221 -574 945 C HETATM 3340 C3 OLA A2410 -22.105 12.432 4.116 1.00 77.32 C ANISOU 3340 C3 OLA A2410 9717 10731 8929 -1007 -468 772 C HETATM 3341 C4 OLA A2410 -21.345 11.122 4.281 1.00 70.70 C ANISOU 3341 C4 OLA A2410 8814 10079 7970 -1009 -273 665 C HETATM 3342 C5 OLA A2410 -20.980 10.459 2.968 1.00 65.96 C ANISOU 3342 C5 OLA A2410 8234 9638 7191 -1168 -205 727 C HETATM 3343 C6 OLA A2410 -21.686 9.137 2.699 1.00 60.62 C ANISOU 3343 C6 OLA A2410 7536 9058 6440 -1111 -116 658 C HETATM 3344 C7 OLA A2410 -21.808 8.293 3.965 1.00 56.82 C ANISOU 3344 C7 OLA A2410 6981 8577 6030 -930 -13 508 C HETATM 3345 C8 OLA A2410 -21.004 7.006 3.957 1.00 51.60 C ANISOU 3345 C8 OLA A2410 6287 8055 5265 -927 164 410 C HETATM 3346 C9 OLA A2410 -21.967 5.829 3.912 1.00 49.53 C ANISOU 3346 C9 OLA A2410 6026 7819 4974 -859 207 349 C HETATM 3347 C10 OLA A2410 -21.954 4.833 2.998 1.00 51.56 C ANISOU 3347 C10 OLA A2410 6326 8170 5096 -932 285 325 C HETATM 3348 C11 OLA A2410 -20.953 4.751 1.866 1.00 54.96 C ANISOU 3348 C11 OLA A2410 6799 8713 5369 -1080 362 347 C HETATM 3349 C12 OLA A2410 -21.096 3.442 1.066 1.00 58.04 C ANISOU 3349 C12 OLA A2410 7242 9100 5711 -1071 432 253 C HETATM 3350 C13 OLA A2410 -20.187 2.308 1.583 1.00 62.06 C ANISOU 3350 C13 OLA A2410 7715 9578 6286 -932 570 114 C HETATM 3351 C14 OLA A2410 -20.971 1.128 2.179 1.00 66.44 C ANISOU 3351 C14 OLA A2410 8285 10071 6887 -824 593 34 C HETATM 3352 C15 OLA A2410 -20.123 -0.141 2.394 1.00 68.50 C ANISOU 3352 C15 OLA A2410 8550 10284 7191 -708 714 -78 C HETATM 3353 C16 OLA A2410 -19.797 -0.419 3.873 1.00 66.72 C ANISOU 3353 C16 OLA A2410 8249 10013 7088 -563 741 -113 C HETATM 3354 C1 OLA A2411 -28.165 -20.106 40.202 1.00 81.22 C ANISOU 3354 C1 OLA A2411 10361 12831 7669 -1737 -42 2264 C HETATM 3355 O1 OLA A2411 -27.777 -21.300 40.068 1.00 81.82 O ANISOU 3355 O1 OLA A2411 10553 12723 7810 -1795 -183 2469 O HETATM 3356 O2 OLA A2411 -28.982 -19.864 41.105 1.00 84.39 O ANISOU 3356 O2 OLA A2411 10702 13421 7941 -1845 29 2233 O HETATM 3357 C2 OLA A2411 -27.663 -18.991 39.305 1.00 76.22 C ANISOU 3357 C2 OLA A2411 9667 12181 7112 -1540 35 2064 C HETATM 3358 C3 OLA A2411 -27.560 -17.657 40.051 1.00 72.67 C ANISOU 3358 C3 OLA A2411 9135 11920 6555 -1477 125 1881 C HETATM 3359 C4 OLA A2411 -27.346 -16.459 39.132 1.00 66.46 C ANISOU 3359 C4 OLA A2411 8276 11122 5852 -1302 217 1661 C HETATM 3360 C5 OLA A2411 -25.906 -15.990 39.062 1.00 63.47 C ANISOU 3360 C5 OLA A2411 7927 10692 5497 -1179 141 1641 C HETATM 3361 C6 OLA A2411 -25.680 -14.756 38.197 1.00 64.66 C ANISOU 3361 C6 OLA A2411 8006 10835 5725 -1020 227 1424 C HETATM 3362 C7 OLA A2411 -24.381 -14.035 38.552 1.00 65.69 C ANISOU 3362 C7 OLA A2411 8144 10990 5826 -935 163 1380 C HETATM 3363 C8 OLA A2411 -24.386 -12.539 38.288 1.00 67.59 C ANISOU 3363 C8 OLA A2411 8318 11279 6084 -829 259 1140 C HETATM 3364 C9 OLA A2411 -23.466 -11.859 39.293 1.00 71.31 C ANISOU 3364 C9 OLA A2411 8812 11836 6448 -834 198 1109 C HETATM 3365 C10 OLA A2411 -23.436 -10.538 39.579 1.00 71.15 C ANISOU 3365 C10 OLA A2411 8769 11878 6388 -787 260 918 C HETATM 3366 C11 OLA A2411 -24.337 -9.513 38.924 1.00 68.32 C ANISOU 3366 C11 OLA A2411 8353 11501 6104 -703 396 712 C HETATM 3367 C12 OLA A2411 -24.336 -8.175 39.688 1.00 63.69 C ANISOU 3367 C12 OLA A2411 7780 10992 5427 -685 445 537 C HETATM 3368 C13 OLA A2411 -22.993 -7.420 39.617 1.00 58.80 C ANISOU 3368 C13 OLA A2411 7183 10348 4812 -633 362 485 C HETATM 3369 C14 OLA A2411 -22.620 -6.975 38.194 1.00 55.74 C ANISOU 3369 C14 OLA A2411 6744 9841 4593 -512 370 413 C HETATM 3370 C15 OLA A2411 -22.660 -5.449 37.987 1.00 54.19 C ANISOU 3370 C15 OLA A2411 6546 9619 4425 -437 426 205 C HETATM 3371 C16 OLA A2411 -22.632 -5.028 36.507 1.00 47.90 C ANISOU 3371 C16 OLA A2411 5695 8699 3804 -327 454 134 C HETATM 3372 C17 OLA A2411 -21.754 -3.798 36.230 1.00 44.81 C ANISOU 3372 C17 OLA A2411 5314 8277 3435 -276 420 14 C HETATM 3373 C18 OLA A2411 -22.293 -2.929 35.084 1.00 40.04 C ANISOU 3373 C18 OLA A2411 4676 7562 2975 -179 488 -114 C HETATM 3374 C1 OLA A2412 -40.117 12.961 9.353 1.00 87.20 C ANISOU 3374 C1 OLA A2412 9183 12022 11927 1293 -822 640 C HETATM 3375 O1 OLA A2412 -41.318 13.286 9.140 1.00 90.21 O ANISOU 3375 O1 OLA A2412 9364 12441 12472 1427 -908 731 O HETATM 3376 O2 OLA A2412 -39.318 13.864 9.652 1.00 89.01 O ANISOU 3376 O2 OLA A2412 9573 12048 12199 1361 -831 556 O HETATM 3377 C2 OLA A2412 -39.643 11.524 9.255 1.00 80.47 C ANISOU 3377 C2 OLA A2412 8378 11354 10842 1059 -718 635 C HETATM 3378 C3 OLA A2412 -40.814 10.542 9.156 1.00 77.26 C ANISOU 3378 C3 OLA A2412 7753 11181 10421 1017 -700 712 C HETATM 3379 C4 OLA A2412 -40.378 9.096 8.953 1.00 71.68 C ANISOU 3379 C4 OLA A2412 7118 10625 9494 774 -622 717 C HETATM 3380 C5 OLA A2412 -41.446 8.227 8.317 1.00 69.11 C ANISOU 3380 C5 OLA A2412 6634 10482 9143 650 -693 859 C HETATM 3381 C6 OLA A2412 -41.213 6.728 8.449 1.00 65.40 C ANISOU 3381 C6 OLA A2412 6209 10161 8480 452 -585 828 C HETATM 3382 C7 OLA A2412 -42.163 5.931 7.558 1.00 65.50 C ANISOU 3382 C7 OLA A2412 6115 10319 8453 276 -703 987 C HETATM 3383 C8 OLA A2412 -41.956 4.428 7.589 1.00 65.74 C ANISOU 3383 C8 OLA A2412 6217 10464 8298 65 -618 962 C HETATM 3384 C9 OLA A2412 -43.303 3.745 7.785 1.00 68.84 C ANISOU 3384 C9 OLA A2412 6373 11057 8727 22 -631 1045 C HETATM 3385 C10 OLA A2412 -43.505 2.570 8.422 1.00 69.28 C ANISOU 3385 C10 OLA A2412 6393 11241 8689 -77 -514 1005 C HETATM 3386 C11 OLA A2412 -42.392 1.753 9.043 1.00 67.04 C ANISOU 3386 C11 OLA A2412 6308 10907 8258 -142 -358 870 C HETATM 3387 C12 OLA A2412 -42.687 0.242 8.990 1.00 66.23 C ANISOU 3387 C12 OLA A2412 6228 10912 8024 -366 -338 906 C HETATM 3388 C13 OLA A2412 -43.522 -0.266 10.184 1.00 65.74 C ANISOU 3388 C13 OLA A2412 5963 11024 7993 -327 -218 896 C HETATM 3389 C1 OLA A2413 -36.505 -15.676 5.207 1.00 81.18 C ANISOU 3389 C1 OLA A2413 10882 11408 8556 -2167 -173 182 C HETATM 3390 O1 OLA A2413 -36.702 -14.516 5.664 1.00 80.32 O ANISOU 3390 O1 OLA A2413 10540 11465 8514 -2049 -151 256 O HETATM 3391 O2 OLA A2413 -36.747 -16.639 5.953 1.00 84.94 O ANISOU 3391 O2 OLA A2413 11403 11801 9070 -2229 -183 219 O HETATM 3392 C2 OLA A2413 -35.992 -15.907 3.799 1.00 78.60 C ANISOU 3392 C2 OLA A2413 10784 10981 8098 -2238 -186 47 C HETATM 3393 C3 OLA A2413 -35.071 -14.776 3.332 1.00 75.32 C ANISOU 3393 C3 OLA A2413 10325 10629 7663 -2065 -97 -22 C HETATM 3394 C4 OLA A2413 -33.612 -15.196 3.203 1.00 71.26 C ANISOU 3394 C4 OLA A2413 9986 9960 7130 -1910 48 -193 C HETATM 3395 C5 OLA A2413 -32.931 -14.638 1.970 1.00 65.09 C ANISOU 3395 C5 OLA A2413 9297 9208 6228 -1900 90 -295 C HETATM 3396 C6 OLA A2413 -31.419 -14.502 2.086 1.00 57.93 C ANISOU 3396 C6 OLA A2413 8430 8238 5342 -1681 261 -424 C HETATM 3397 C7 OLA A2413 -31.023 -13.296 2.935 1.00 50.41 C ANISOU 3397 C7 OLA A2413 7244 7406 4503 -1501 314 -344 C HETATM 3398 C8 OLA A2413 -29.565 -13.271 3.355 1.00 49.35 C ANISOU 3398 C8 OLA A2413 7113 7214 4422 -1286 469 -444 C HETATM 3399 C9 OLA A2413 -29.005 -11.877 3.120 1.00 48.38 C ANISOU 3399 C9 OLA A2413 6859 7229 4296 -1202 510 -419 C HETATM 3400 C10 OLA A2413 -28.155 -11.221 3.941 1.00 47.93 C ANISOU 3400 C10 OLA A2413 6671 7206 4336 -1023 590 -409 C HETATM 3401 C1 OLA A2414 -15.147 12.853 0.887 1.00 66.37 C ANISOU 3401 C1 OLA A2414 8250 10091 6877 -2015 -94 1098 C HETATM 3402 O1 OLA A2414 -13.957 13.250 0.749 1.00 68.56 O ANISOU 3402 O1 OLA A2414 8472 10473 7103 -2170 -57 1160 O HETATM 3403 O2 OLA A2414 -16.012 13.702 1.162 1.00 66.44 O ANISOU 3403 O2 OLA A2414 8349 9885 7009 -1976 -275 1151 O HETATM 3404 C2 OLA A2414 -15.525 11.394 0.724 1.00 62.36 C ANISOU 3404 C2 OLA A2414 7698 9706 6289 -1881 70 963 C HETATM 3405 C3 OLA A2414 -16.991 11.135 1.081 1.00 59.07 C ANISOU 3405 C3 OLA A2414 7339 9139 5966 -1712 -14 910 C HETATM 3406 C4 OLA A2414 -17.418 9.684 0.885 1.00 60.59 C ANISOU 3406 C4 OLA A2414 7507 9438 6078 -1606 129 788 C HETATM 3407 C5 OLA A2414 -16.261 8.737 0.632 1.00 59.94 C ANISOU 3407 C5 OLA A2414 7343 9522 5911 -1601 322 686 C HETATM 3408 C6 OLA A2414 -16.599 7.258 0.773 1.00 57.81 C ANISOU 3408 C6 OLA A2414 7054 9251 5660 -1421 435 518 C HETATM 3409 C1 OLA A2415 -34.377 12.114 4.066 1.00 96.65 C ANISOU 3409 C1 OLA A2415 11424 13040 12259 3 -1147 1081 C HETATM 3410 O1 OLA A2415 -33.146 12.376 3.970 1.00 97.27 O ANISOU 3410 O1 OLA A2415 11650 13057 12251 -95 -1110 1052 O HETATM 3411 O2 OLA A2415 -35.120 12.991 4.538 1.00100.44 O ANISOU 3411 O2 OLA A2415 11816 13406 12939 198 -1222 1088 O HETATM 3412 C2 OLA A2415 -34.951 10.781 3.626 1.00 91.14 C ANISOU 3412 C2 OLA A2415 10656 12544 11430 -112 -1105 1106 C HETATM 3413 C3 OLA A2415 -34.542 10.425 2.194 1.00 86.01 C ANISOU 3413 C3 OLA A2415 10131 11956 10594 -370 -1190 1236 C HETATM 3414 C4 OLA A2415 -33.936 9.032 2.065 1.00 78.08 C ANISOU 3414 C4 OLA A2415 9190 11098 9377 -517 -1033 1140 C HETATM 3415 C5 OLA A2415 -34.611 8.173 1.015 1.00 73.43 C ANISOU 3415 C5 OLA A2415 8601 10643 8657 -692 -1108 1237 C HETATM 3416 C6 OLA A2415 -34.777 6.706 1.393 1.00 66.73 C ANISOU 3416 C6 OLA A2415 7723 9923 7707 -730 -965 1122 C HETATM 3417 C7 OLA A2415 -35.534 5.931 0.317 1.00 63.04 C ANISOU 3417 C7 OLA A2415 7267 9571 7113 -919 -1069 1223 C HETATM 3418 C8 OLA A2415 -35.670 4.441 0.574 1.00 60.87 C ANISOU 3418 C8 OLA A2415 6998 9400 6728 -988 -946 1116 C HETATM 3419 C9 OLA A2415 -34.280 3.827 0.666 1.00 57.09 C ANISOU 3419 C9 OLA A2415 6676 8907 6107 -1036 -768 971 C HETATM 3420 C1 OLA A2416 -28.275 -20.744 35.228 1.00 75.53 C ANISOU 3420 C1 OLA A2416 9719 11539 7439 -1486 3 2149 C HETATM 3421 O1 OLA A2416 -27.108 -20.832 34.810 1.00 72.19 O ANISOU 3421 O1 OLA A2416 9364 10983 7083 -1360 -70 2191 O HETATM 3422 O2 OLA A2416 -29.034 -21.740 35.069 1.00 76.24 O ANISOU 3422 O2 OLA A2416 9873 11538 7555 -1638 -41 2267 O HETATM 3423 C2 OLA A2416 -28.750 -19.472 35.906 1.00 76.33 C ANISOU 3423 C2 OLA A2416 9671 11891 7441 -1452 131 1963 C HETATM 3424 C3 OLA A2416 -30.267 -19.293 35.797 1.00 76.81 C ANISOU 3424 C3 OLA A2416 9628 12072 7483 -1551 236 1886 C HETATM 3425 C4 OLA A2416 -30.773 -17.986 36.396 1.00 76.35 C ANISOU 3425 C4 OLA A2416 9430 12228 7350 -1488 361 1696 C HETATM 3426 C5 OLA A2416 -30.951 -16.880 35.374 1.00 74.51 C ANISOU 3426 C5 OLA A2416 9106 11995 7208 -1335 457 1490 C HETATM 3427 C6 OLA A2416 -31.928 -15.781 35.775 1.00 74.77 C ANISOU 3427 C6 OLA A2416 9003 12204 7201 -1299 577 1327 C HETATM 3428 C7 OLA A2416 -31.381 -14.390 35.460 1.00 73.10 C ANISOU 3428 C7 OLA A2416 8750 11989 7037 -1111 633 1126 C HETATM 3429 C8 OLA A2416 -31.138 -13.507 36.672 1.00 73.04 C ANISOU 3429 C8 OLA A2416 8726 12107 6917 -1074 671 1038 C HETATM 3430 C9 OLA A2416 -30.237 -12.347 36.270 1.00 69.08 C ANISOU 3430 C9 OLA A2416 8228 11543 6476 -907 681 880 C HETATM 3431 C10 OLA A2416 -29.288 -11.775 37.046 1.00 65.62 C ANISOU 3431 C10 OLA A2416 7834 11135 5963 -867 654 837 C HETATM 3432 C11 OLA A2416 -28.420 -10.621 36.591 1.00 61.14 C ANISOU 3432 C11 OLA A2416 7269 10503 5460 -721 654 687 C HETATM 3433 C12 OLA A2416 -26.997 -10.694 37.178 1.00 57.20 C ANISOU 3433 C12 OLA A2416 6842 9998 4892 -722 558 746 C HETATM 3434 C1 OLA A2417 -32.134 15.454 7.718 1.00 81.52 C ANISOU 3434 C1 OLA A2417 9752 10509 10711 482 -1005 620 C HETATM 3435 O1 OLA A2417 -31.129 15.805 7.040 1.00 83.35 O ANISOU 3435 O1 OLA A2417 10125 10679 10866 301 -1073 704 O HETATM 3436 O2 OLA A2417 -32.720 16.329 8.377 1.00 82.24 O ANISOU 3436 O2 OLA A2417 9815 10452 10981 688 -1045 553 O HETATM 3437 C2 OLA A2417 -32.627 14.020 7.741 1.00 76.59 C ANISOU 3437 C2 OLA A2417 9001 10131 9970 449 -879 597 C HETATM 3438 C3 OLA A2417 -34.154 13.939 7.813 1.00 75.59 C ANISOU 3438 C3 OLA A2417 8692 10056 9971 609 -916 630 C HETATM 3439 C4 OLA A2417 -34.671 12.620 8.377 1.00 73.60 C ANISOU 3439 C4 OLA A2417 8305 10027 9632 623 -757 551 C HETATM 3440 C5 OLA A2417 -35.157 11.655 7.313 1.00 70.98 C ANISOU 3440 C5 OLA A2417 7921 9851 9196 458 -806 690 C HETATM 3441 C6 OLA A2417 -36.166 10.619 7.793 1.00 68.63 C ANISOU 3441 C6 OLA A2417 7448 9742 8887 506 -712 656 C HETATM 3442 C7 OLA A2417 -35.749 9.202 7.404 1.00 63.84 C ANISOU 3442 C7 OLA A2417 6891 9289 8078 302 -631 660 C HETATM 3443 C8 OLA A2417 -36.891 8.285 7.004 1.00 62.43 C ANISOU 3443 C8 OLA A2417 6574 9272 7875 238 -660 744 C HETATM 3444 C9 OLA A2417 -36.495 7.521 5.748 1.00 60.67 C ANISOU 3444 C9 OLA A2417 6471 9103 7479 -9 -720 837 C HETATM 3445 C10 OLA A2417 -36.967 6.309 5.380 1.00 59.08 C ANISOU 3445 C10 OLA A2417 6240 9041 7168 -147 -704 867 C HETATM 3446 C11 OLA A2417 -37.978 5.525 6.188 1.00 58.70 C ANISOU 3446 C11 OLA A2417 6017 9127 7159 -89 -630 835 C HETATM 3447 C1 OLA A2418 -43.931 -24.190 13.455 1.00 69.15 C ANISOU 3447 C1 OLA A2418 9071 9993 7208 -3833 -726 1543 C HETATM 3448 O1 OLA A2418 -44.554 -24.972 12.686 1.00 73.44 O ANISOU 3448 O1 OLA A2418 9757 10434 7711 -4048 -877 1559 O HETATM 3449 O2 OLA A2418 -43.001 -24.662 14.130 1.00 68.64 O ANISOU 3449 O2 OLA A2418 9163 9747 7169 -3769 -667 1538 O HETATM 3450 C2 OLA A2418 -44.288 -22.721 13.565 1.00 66.18 C ANISOU 3450 C2 OLA A2418 8358 9937 6850 -3643 -626 1533 C HETATM 3451 C3 OLA A2418 -43.393 -21.990 14.570 1.00 64.53 C ANISOU 3451 C3 OLA A2418 8049 9792 6677 -3387 -451 1498 C HETATM 3452 C4 OLA A2418 -43.683 -20.497 14.667 1.00 65.04 C ANISOU 3452 C4 OLA A2418 7808 10134 6769 -3172 -353 1461 C HETATM 3453 C5 OLA A2418 -42.591 -19.710 15.365 1.00 63.89 C ANISOU 3453 C5 OLA A2418 7626 10003 6646 -2908 -191 1382 C HETATM 3454 C6 OLA A2418 -41.229 -20.392 15.398 1.00 64.77 C ANISOU 3454 C6 OLA A2418 8034 9819 6756 -2845 -168 1304 C HETATM 3455 C7 OLA A2418 -40.332 -19.812 16.490 1.00 65.75 C ANISOU 3455 C7 OLA A2418 8096 9990 6897 -2592 -31 1265 C HETATM 3456 C8 OLA A2418 -39.558 -18.570 16.087 1.00 63.69 C ANISOU 3456 C8 OLA A2418 7775 9755 6668 -2316 55 1108 C HETATM 3457 C9 OLA A2418 -38.220 -18.993 15.497 1.00 63.22 C ANISOU 3457 C9 OLA A2418 7986 9402 6632 -2192 48 970 C HETATM 3458 C10 OLA A2418 -37.532 -18.335 14.536 1.00 60.78 C ANISOU 3458 C10 OLA A2418 7731 9024 6340 -2042 71 822 C HETATM 3459 C11 OLA A2418 -38.003 -17.049 13.890 1.00 59.27 C ANISOU 3459 C11 OLA A2418 7353 9017 6151 -1980 85 784 C HETATM 3460 C12 OLA A2418 -37.462 -15.804 14.619 1.00 56.55 C ANISOU 3460 C12 OLA A2418 6841 8807 5837 -1737 202 738 C HETATM 3461 C13 OLA A2418 -37.795 -14.479 13.904 1.00 55.07 C ANISOU 3461 C13 OLA A2418 6499 8755 5671 -1651 205 692 C HETATM 3462 C14 OLA A2418 -37.784 -13.262 14.842 1.00 58.05 C ANISOU 3462 C14 OLA A2418 6663 9311 6082 -1467 303 685 C HETATM 3463 C15 OLA A2418 -38.628 -12.078 14.328 1.00 63.40 C ANISOU 3463 C15 OLA A2418 7139 10155 6797 -1429 282 696 C HETATM 3464 C16 OLA A2418 -38.243 -10.726 14.956 1.00 63.93 C ANISOU 3464 C16 OLA A2418 7069 10314 6909 -1198 375 631 C HETATM 3465 C17 OLA A2418 -38.379 -9.537 13.991 1.00 60.93 C ANISOU 3465 C17 OLA A2418 6616 9956 6579 -1112 332 591 C HETATM 3466 C1 OLA A2419 -9.796 -14.391 17.248 1.00 58.54 C ANISOU 3466 C1 OLA A2419 6422 8495 7327 1507 993 -17 C HETATM 3467 O1 OLA A2419 -8.959 -15.187 16.790 1.00 61.18 O ANISOU 3467 O1 OLA A2419 6706 8756 7782 1690 1061 -62 O HETATM 3468 O2 OLA A2419 -11.015 -14.700 17.147 1.00 59.98 O ANISOU 3468 O2 OLA A2419 6791 8563 7434 1404 975 -42 O HETATM 3469 C2 OLA A2419 -9.349 -13.098 17.902 1.00 54.21 C ANISOU 3469 C2 OLA A2419 5710 8161 6727 1412 931 61 C HETATM 3470 C3 OLA A2419 -10.530 -12.246 18.373 1.00 48.55 C ANISOU 3470 C3 OLA A2419 5091 7490 5866 1212 865 82 C HETATM 3471 C4 OLA A2419 -10.309 -10.752 18.173 1.00 48.95 C ANISOU 3471 C4 OLA A2419 5040 7723 5836 1096 881 60 C HETATM 3472 C5 OLA A2419 -9.009 -10.245 18.766 1.00 50.66 C ANISOU 3472 C5 OLA A2419 5054 8084 6110 1135 828 139 C HETATM 3473 C6 OLA A2419 -8.557 -8.882 18.260 1.00 52.42 C ANISOU 3473 C6 OLA A2419 5171 8470 6278 1031 864 106 C HETATM 3474 C7 OLA A2419 -8.253 -7.924 19.410 1.00 53.22 C ANISOU 3474 C7 OLA A2419 5194 8689 6340 929 730 196 C HETATM 3475 C10 OLC A2420 -6.076 -4.372 27.590 1.00 64.98 C ANISOU 3475 C10 OLC A2420 6487 10784 7418 320 -236 703 C HETATM 3476 C9 OLC A2420 -6.481 -3.175 27.964 1.00 65.79 C ANISOU 3476 C9 OLC A2420 6687 10919 7393 169 -271 621 C HETATM 3477 C8 OLC A2420 -5.775 -1.917 27.592 1.00 67.22 C ANISOU 3477 C8 OLC A2420 6793 11171 7575 51 -301 582 C HETATM 3478 C24 OLC A2420 -4.610 9.767 29.098 1.00 85.22 C ANISOU 3478 C24 OLC A2420 9852 13199 9327 -1417 -1052 -34 C HETATM 3479 C7 OLC A2420 -6.035 -0.888 28.687 1.00 68.50 C ANISOU 3479 C7 OLC A2420 7078 11374 7576 -116 -419 536 C HETATM 3480 C6 OLC A2420 -4.807 -0.098 29.124 1.00 70.47 C ANISOU 3480 C6 OLC A2420 7212 11748 7816 -253 -567 598 C HETATM 3481 C5 OLC A2420 -5.067 1.320 29.553 1.00 68.36 C ANISOU 3481 C5 OLC A2420 7082 11471 7421 -432 -635 489 C HETATM 3482 C4 OLC A2420 -3.882 2.163 29.934 1.00 68.64 C ANISOU 3482 C4 OLC A2420 7021 11618 7442 -599 -793 546 C HETATM 3483 C3 OLC A2420 -4.302 3.609 29.819 1.00 68.38 C ANISOU 3483 C3 OLC A2420 7146 11504 7330 -747 -805 404 C HETATM 3484 C2 OLC A2420 -3.417 4.683 30.426 1.00 74.09 C ANISOU 3484 C2 OLC A2420 7866 12298 7987 -963 -984 417 C HETATM 3485 C21 OLC A2420 -3.574 8.259 31.030 1.00 81.54 C ANISOU 3485 C21 OLC A2420 9220 13037 8725 -1425 -1212 128 C HETATM 3486 C1 OLC A2420 -3.967 6.027 30.005 1.00 77.56 C ANISOU 3486 C1 OLC A2420 8476 12601 8393 -1068 -963 267 C HETATM 3487 C22 OLC A2420 -3.732 9.566 30.285 1.00 82.96 C ANISOU 3487 C22 OLC A2420 9512 13064 8946 -1532 -1213 34 C HETATM 3488 O19 OLC A2420 -5.091 6.118 29.588 1.00 79.77 O ANISOU 3488 O19 OLC A2420 8890 12751 8668 -975 -837 152 O HETATM 3489 O25 OLC A2420 -4.896 11.140 29.306 1.00 88.41 O ANISOU 3489 O25 OLC A2420 10468 13445 9679 -1553 -1138 -165 O HETATM 3490 O23 OLC A2420 -3.046 10.751 30.654 1.00 84.15 O ANISOU 3490 O23 OLC A2420 9737 13191 9047 -1771 -1387 13 O HETATM 3491 O20 OLC A2420 -3.258 7.272 30.049 1.00 79.54 O ANISOU 3491 O20 OLC A2420 8747 12851 8623 -1279 -1095 253 O HETATM 3492 C10 OLC A2421 -30.394 -1.561 38.815 1.00 54.72 C ANISOU 3492 C10 OLC A2421 6422 9856 4514 -155 1167 -489 C HETATM 3493 C9 OLC A2421 -30.794 -0.317 38.979 1.00 53.22 C ANISOU 3493 C9 OLC A2421 6247 9652 4323 -55 1249 -655 C HETATM 3494 C11 OLC A2421 -29.823 -2.115 37.544 1.00 55.97 C ANISOU 3494 C11 OLC A2421 6554 9887 4825 -148 1067 -392 C HETATM 3495 C8 OLC A2421 -30.727 0.713 37.904 1.00 52.99 C ANISOU 3495 C8 OLC A2421 6207 9477 4451 71 1241 -757 C HETATM 3496 C24 OLC A2421 -28.645 10.121 34.968 1.00 65.37 C ANISOU 3496 C24 OLC A2421 8238 10141 6457 777 1147 -1839 C HETATM 3497 C16 OLC A2421 -26.085 -6.274 37.768 1.00 44.63 C ANISOU 3497 C16 OLC A2421 5248 8438 3273 -461 664 195 C HETATM 3498 C12 OLC A2421 -30.037 -3.624 37.429 1.00 56.06 C ANISOU 3498 C12 OLC A2421 6526 9943 4833 -252 1029 -213 C HETATM 3499 C7 OLC A2421 -31.268 2.021 38.469 1.00 55.78 C ANISOU 3499 C7 OLC A2421 6592 9844 4756 171 1351 -945 C HETATM 3500 C15 OLC A2421 -26.987 -5.758 36.652 1.00 42.48 C ANISOU 3500 C15 OLC A2421 4910 8081 3149 -369 739 99 C HETATM 3501 C13 OLC A2421 -29.014 -4.224 36.507 1.00 49.55 C ANISOU 3501 C13 OLC A2421 5721 9003 4103 -258 919 -121 C HETATM 3502 C6 OLC A2421 -32.638 2.424 37.936 1.00 55.64 C ANISOU 3502 C6 OLC A2421 6458 9832 4851 278 1457 -996 C HETATM 3503 C14 OLC A2421 -28.471 -5.562 36.996 1.00 44.27 C ANISOU 3503 C14 OLC A2421 5085 8384 3351 -376 849 47 C HETATM 3504 C5 OLC A2421 -32.722 3.808 37.355 1.00 55.00 C ANISOU 3504 C5 OLC A2421 6394 9627 4876 426 1483 -1151 C HETATM 3505 C4 OLC A2421 -31.490 4.357 36.695 1.00 55.23 C ANISOU 3505 C4 OLC A2421 6512 9507 4965 439 1365 -1181 C HETATM 3506 C3 OLC A2421 -31.812 5.747 36.202 1.00 56.35 C ANISOU 3506 C3 OLC A2421 6664 9538 5207 590 1406 -1341 C HETATM 3507 C2 OLC A2421 -32.598 6.682 37.098 1.00 59.36 C ANISOU 3507 C2 OLC A2421 7074 9960 5520 690 1545 -1515 C HETATM 3508 C21 OLC A2421 -30.676 9.989 36.675 1.00 66.91 C ANISOU 3508 C21 OLC A2421 8376 10519 6529 869 1414 -1933 C HETATM 3509 C1 OLC A2421 -32.270 8.098 36.681 1.00 63.18 C ANISOU 3509 C1 OLC A2421 7639 10284 6081 814 1528 -1684 C HETATM 3510 C22 OLC A2421 -29.218 10.205 36.340 1.00 68.78 C ANISOU 3510 C22 OLC A2421 8725 10664 6743 782 1261 -1929 C HETATM 3511 O19 OLC A2421 -33.149 8.908 36.545 1.00 69.65 O ANISOU 3511 O19 OLC A2421 8414 11066 6982 957 1617 -1796 O HETATM 3512 O25 OLC A2421 -28.054 11.408 34.927 1.00 67.54 O ANISOU 3512 O25 OLC A2421 8656 10269 6737 825 1092 -2016 O HETATM 3513 O23 OLC A2421 -28.243 10.520 37.322 1.00 71.99 O ANISOU 3513 O23 OLC A2421 9303 11077 6974 688 1211 -2013 O HETATM 3514 O20 OLC A2421 -30.960 8.614 36.420 1.00 59.70 O ANISOU 3514 O20 OLC A2421 7328 9725 5630 780 1406 -1728 O HETATM 3515 C9 OLC A2422 -3.473 -1.899 24.774 1.00 56.64 C ANISOU 3515 C9 OLC A2422 4999 9963 6558 167 -114 639 C HETATM 3516 C8 OLC A2422 -4.437 -0.763 24.748 1.00 54.02 C ANISOU 3516 C8 OLC A2422 4862 9558 6105 26 -111 524 C HETATM 3517 C24 OLC A2422 -1.576 12.535 26.606 1.00 47.36 C ANISOU 3517 C24 OLC A2422 4781 8442 4773 -2039 -1302 248 C HETATM 3518 C7 OLC A2422 -3.832 0.388 25.543 1.00 53.20 C ANISOU 3518 C7 OLC A2422 4741 9542 5929 -163 -270 552 C HETATM 3519 C6 OLC A2422 -3.253 1.514 24.695 1.00 47.16 C ANISOU 3519 C6 OLC A2422 3908 8824 5187 -297 -258 535 C HETATM 3520 C5 OLC A2422 -3.121 2.841 25.390 1.00 45.61 C ANISOU 3520 C5 OLC A2422 3798 8638 4895 -507 -405 511 C HETATM 3521 C4 OLC A2422 -3.649 4.062 24.690 1.00 41.68 C ANISOU 3521 C4 OLC A2422 3433 8041 4362 -626 -374 414 C HETATM 3522 C3 OLC A2422 -3.084 5.268 25.405 1.00 36.49 C ANISOU 3522 C3 OLC A2422 2811 7414 3638 -841 -546 420 C HETATM 3523 C2 OLC A2422 -3.020 6.594 24.669 1.00 36.48 C ANISOU 3523 C2 OLC A2422 2873 7350 3639 -1008 -564 383 C HETATM 3524 C21 OLC A2422 -1.893 9.902 26.410 1.00 40.52 C ANISOU 3524 C21 OLC A2422 3634 7789 3972 -1617 -1042 334 C HETATM 3525 C1 OLC A2422 -2.538 7.641 25.648 1.00 40.02 C ANISOU 3525 C1 OLC A2422 3392 7804 4008 -1215 -759 378 C HETATM 3526 C22 OLC A2422 -1.822 11.292 25.822 1.00 45.13 C ANISOU 3526 C22 OLC A2422 4330 8250 4569 -1811 -1106 305 C HETATM 3527 O19 OLC A2422 -2.244 7.324 26.769 1.00 50.19 O ANISOU 3527 O19 OLC A2422 4669 9164 5238 -1229 -864 404 O HETATM 3528 O25 OLC A2422 -1.500 13.435 25.514 1.00 50.55 O ANISOU 3528 O25 OLC A2422 5214 8747 5245 -2158 -1294 274 O HETATM 3529 O23 OLC A2422 -1.984 11.547 24.436 1.00 53.58 O ANISOU 3529 O23 OLC A2422 5368 9269 5722 -1804 -994 334 O HETATM 3530 O20 OLC A2422 -2.380 9.041 25.382 1.00 38.88 O ANISOU 3530 O20 OLC A2422 3347 7578 3846 -1420 -847 346 O HETATM 3531 C24 OLC A2423 -37.211 -25.431 24.525 1.00 99.27 C ANISOU 3531 C24 OLC A2423 13054 13629 11035 -2785 -167 2074 C HETATM 3532 C7 OLC A2423 -37.415 -13.578 23.958 1.00 71.11 C ANISOU 3532 C7 OLC A2423 8030 11406 7581 -1151 649 848 C HETATM 3533 C6 OLC A2423 -37.247 -14.571 22.814 1.00 71.96 C ANISOU 3533 C6 OLC A2423 8258 11389 7696 -1298 582 919 C HETATM 3534 C5 OLC A2423 -37.169 -16.018 23.216 1.00 74.69 C ANISOU 3534 C5 OLC A2423 8733 11659 7987 -1485 530 1062 C HETATM 3535 C4 OLC A2423 -37.991 -17.006 22.437 1.00 76.41 C ANISOU 3535 C4 OLC A2423 8996 11833 8204 -1714 447 1167 C HETATM 3536 C3 OLC A2423 -37.393 -18.372 22.675 1.00 78.01 C ANISOU 3536 C3 OLC A2423 9411 11859 8371 -1857 385 1287 C HETATM 3537 C2 OLC A2423 -38.225 -19.602 22.366 1.00 83.08 C ANISOU 3537 C2 OLC A2423 10135 12427 9005 -2123 281 1421 C HETATM 3538 C21 OLC A2423 -37.335 -22.851 23.890 1.00 92.93 C ANISOU 3538 C21 OLC A2423 11866 13236 10208 -2464 71 1786 C HETATM 3539 C1 OLC A2423 -37.320 -20.809 22.475 1.00 86.68 C ANISOU 3539 C1 OLC A2423 10854 12631 9449 -2213 214 1517 C HETATM 3540 C22 OLC A2423 -37.686 -24.305 23.672 1.00 96.60 C ANISOU 3540 C22 OLC A2423 12535 13475 10695 -2707 -74 1922 C HETATM 3541 O19 OLC A2423 -36.129 -20.687 22.359 1.00 86.64 O ANISOU 3541 O19 OLC A2423 10964 12477 9480 -2040 230 1435 O HETATM 3542 O25 OLC A2423 -38.460 -26.081 24.686 1.00102.30 O ANISOU 3542 O25 OLC A2423 13385 14085 11401 -3011 -244 2163 O HETATM 3543 O23 OLC A2423 -38.521 -24.744 22.612 1.00 98.10 O ANISOU 3543 O23 OLC A2423 12771 13590 10911 -2888 -153 1914 O HETATM 3544 O20 OLC A2423 -37.750 -22.155 22.715 1.00 90.32 O ANISOU 3544 O20 OLC A2423 11453 12960 9904 -2441 102 1668 O HETATM 3545 C8 OLC A2424 -38.649 4.264 29.543 1.00 58.56 C ANISOU 3545 C8 OLC A2424 5936 9908 6407 888 1450 -849 C HETATM 3546 C24 OLC A2424 -35.548 15.932 30.682 1.00 89.13 C ANISOU 3546 C24 OLC A2424 10706 12427 10732 2125 1419 -2352 C HETATM 3547 C7 OLC A2424 -37.392 4.945 29.015 1.00 61.30 C ANISOU 3547 C7 OLC A2424 6418 10089 6786 922 1360 -904 C HETATM 3548 C6 OLC A2424 -37.389 6.461 29.168 1.00 63.40 C ANISOU 3548 C6 OLC A2424 6708 10264 7117 1099 1402 -1072 C HETATM 3549 C5 OLC A2424 -36.210 7.170 28.564 1.00 60.71 C ANISOU 3549 C5 OLC A2424 6489 9767 6811 1130 1305 -1124 C HETATM 3550 C4 OLC A2424 -35.628 8.329 29.325 1.00 65.28 C ANISOU 3550 C4 OLC A2424 7192 10259 7352 1222 1336 -1303 C HETATM 3551 C3 OLC A2424 -36.666 9.426 29.330 1.00 71.67 C ANISOU 3551 C3 OLC A2424 7916 11033 8281 1419 1413 -1421 C HETATM 3552 C2 OLC A2424 -36.588 10.509 30.389 1.00 79.81 C ANISOU 3552 C2 OLC A2424 9051 12006 9266 1531 1497 -1623 C HETATM 3553 C21 OLC A2424 -35.186 13.307 30.925 1.00 87.31 C ANISOU 3553 C21 OLC A2424 10345 12580 10247 1759 1442 -2031 C HETATM 3554 C1 OLC A2424 -36.778 11.841 29.699 1.00 85.53 C ANISOU 3554 C1 OLC A2424 9773 12559 10165 1729 1461 -1735 C HETATM 3555 C22 OLC A2424 -34.709 14.703 30.593 1.00 86.68 C ANISOU 3555 C22 OLC A2424 10399 12263 10271 1896 1364 -2196 C HETATM 3556 O19 OLC A2424 -37.264 11.887 28.599 1.00 87.39 O ANISOU 3556 O19 OLC A2424 9889 12764 10552 1793 1402 -1652 O HETATM 3557 O25 OLC A2424 -34.549 16.874 30.333 1.00 87.96 O ANISOU 3557 O25 OLC A2424 10744 12049 10628 2151 1283 -2463 O HETATM 3558 O23 OLC A2424 -33.387 14.979 30.157 1.00 83.59 O ANISOU 3558 O23 OLC A2424 10158 11748 9855 1818 1220 -2218 O HETATM 3559 O20 OLC A2424 -36.424 13.121 30.238 1.00 88.03 O ANISOU 3559 O20 OLC A2424 10233 12725 10491 1856 1479 -1940 O HETATM 3560 C10 OLC A2425 -42.219 4.121 12.709 1.00 51.79 C ANISOU 3560 C10 OLC A2425 4132 8954 6593 567 39 498 C HETATM 3561 C9 OLC A2425 -41.383 5.109 12.459 1.00 52.75 C ANISOU 3561 C9 OLC A2425 4400 8883 6759 658 -8 443 C HETATM 3562 C11 OLC A2425 -43.000 3.957 13.978 1.00 50.39 C ANISOU 3562 C11 OLC A2425 3815 8895 6437 664 192 422 C HETATM 3563 C8 OLC A2425 -41.101 6.211 13.421 1.00 53.08 C ANISOU 3563 C8 OLC A2425 4444 8836 6889 891 78 297 C HETATM 3564 C24 OLC A2425 -42.028 19.719 14.186 1.00101.82 C ANISOU 3564 C24 OLC A2425 10928 12842 14918 3047 -638 -261 C HETATM 3565 C12 OLC A2425 -44.057 2.859 13.869 1.00 50.95 C ANISOU 3565 C12 OLC A2425 3790 9105 6465 496 181 528 C HETATM 3566 C7 OLC A2425 -41.331 7.535 12.702 1.00 54.41 C ANISOU 3566 C7 OLC A2425 4596 8848 7229 1025 -72 349 C HETATM 3567 C15 OLC A2425 -43.487 -0.992 13.987 1.00 53.70 C ANISOU 3567 C15 OLC A2425 4399 9603 6403 -100 243 635 C HETATM 3568 C13 OLC A2425 -43.398 1.529 13.644 1.00 49.66 C ANISOU 3568 C13 OLC A2425 3768 8974 6127 263 187 563 C HETATM 3569 C6 OLC A2425 -40.682 8.740 13.372 1.00 53.89 C ANISOU 3569 C6 OLC A2425 4633 8602 7239 1217 -31 202 C HETATM 3570 C14 OLC A2425 -44.119 0.368 14.320 1.00 51.78 C ANISOU 3570 C14 OLC A2425 4005 9354 6316 134 261 591 C HETATM 3571 C5 OLC A2425 -41.568 9.942 13.538 1.00 55.76 C ANISOU 3571 C5 OLC A2425 4720 8776 7692 1471 -74 184 C HETATM 3572 C4 OLC A2425 -41.205 11.191 12.786 1.00 58.25 C ANISOU 3572 C4 OLC A2425 5154 8838 8141 1545 -245 229 C HETATM 3573 C3 OLC A2425 -41.866 12.347 13.497 1.00 63.60 C ANISOU 3573 C3 OLC A2425 5718 9430 9017 1848 -214 121 C HETATM 3574 C2 OLC A2425 -40.998 13.461 14.053 1.00 69.36 C ANISOU 3574 C2 OLC A2425 6645 9914 9795 1977 -201 -37 C HETATM 3575 C21 OLC A2425 -41.695 17.231 13.313 1.00 91.63 C ANISOU 3575 C21 OLC A2425 9539 12041 13234 2529 -579 -18 C HETATM 3576 C1 OLC A2425 -41.651 14.779 13.701 1.00 78.24 C ANISOU 3576 C1 OLC A2425 7709 10846 11173 2205 -338 -3 C HETATM 3577 C22 OLC A2425 -41.432 18.357 14.288 1.00 96.30 C ANISOU 3577 C22 OLC A2425 10248 12406 13935 2765 -515 -245 C HETATM 3578 O19 OLC A2425 -42.775 14.803 13.270 1.00 80.37 O ANISOU 3578 O19 OLC A2425 7759 11202 11577 2294 -406 112 O HETATM 3579 O25 OLC A2425 -41.671 20.186 15.475 1.00104.08 O ANISOU 3579 O25 OLC A2425 11321 13044 15182 3203 -469 -545 O HETATM 3580 O23 OLC A2425 -40.580 18.217 15.414 1.00 94.73 O ANISOU 3580 O23 OLC A2425 10200 12215 13577 2739 -340 -469 O HETATM 3581 O20 OLC A2425 -41.045 16.071 13.832 1.00 83.92 O ANISOU 3581 O20 OLC A2425 8614 11265 12005 2332 -413 -92 O HETATM 3582 C18 OLC A2426 -33.431 -16.321 27.096 1.00 53.45 C ANISOU 3582 C18 OLC A2426 6302 8876 5130 -1207 575 1126 C HETATM 3583 C10 OLC A2426 -33.961 -6.926 30.353 1.00 52.55 C ANISOU 3583 C10 OLC A2426 5693 9201 5074 -295 949 167 C HETATM 3584 C9 OLC A2426 -33.233 -6.103 31.080 1.00 51.50 C ANISOU 3584 C9 OLC A2426 5609 9056 4901 -227 962 79 C HETATM 3585 C17 OLC A2426 -33.965 -14.952 26.762 1.00 54.00 C ANISOU 3585 C17 OLC A2426 6223 9044 5251 -1078 640 961 C HETATM 3586 C11 OLC A2426 -33.406 -7.935 29.393 1.00 53.41 C ANISOU 3586 C11 OLC A2426 5856 9211 5228 -354 878 259 C HETATM 3587 C8 OLC A2426 -33.812 -5.110 32.027 1.00 52.59 C ANISOU 3587 C8 OLC A2426 5707 9291 4984 -170 1045 -24 C HETATM 3588 C24 OLC A2426 -33.072 5.827 33.238 1.00 77.10 C ANISOU 3588 C24 OLC A2426 9042 12014 8237 745 1355 -1222 C HETATM 3589 C16 OLC A2426 -33.196 -13.769 27.345 1.00 49.72 C ANISOU 3589 C16 OLC A2426 5647 8532 4711 -895 682 832 C HETATM 3590 C12 OLC A2426 -33.800 -9.365 29.762 1.00 53.71 C ANISOU 3590 C12 OLC A2426 5902 9313 5193 -508 863 407 C HETATM 3591 C7 OLC A2426 -32.748 -4.783 33.068 1.00 54.79 C ANISOU 3591 C7 OLC A2426 6079 9573 5165 -166 1035 -68 C HETATM 3592 C15 OLC A2426 -34.106 -12.607 27.728 1.00 50.59 C ANISOU 3592 C15 OLC A2426 5617 8771 4835 -824 738 725 C HETATM 3593 C13 OLC A2426 -33.548 -10.284 28.602 1.00 51.72 C ANISOU 3593 C13 OLC A2426 5696 8959 4996 -566 808 487 C HETATM 3594 C6 OLC A2426 -31.709 -3.767 32.607 1.00 53.95 C ANISOU 3594 C6 OLC A2426 6035 9342 5122 -68 995 -166 C HETATM 3595 C14 OLC A2426 -33.699 -11.763 28.946 1.00 52.38 C ANISOU 3595 C14 OLC A2426 5827 9065 5010 -730 775 649 C HETATM 3596 C5 OLC A2426 -31.075 -2.938 33.689 1.00 53.55 C ANISOU 3596 C5 OLC A2426 6050 9325 4973 -42 1014 -262 C HETATM 3597 C4 OLC A2426 -30.183 -1.803 33.268 1.00 55.09 C ANISOU 3597 C4 OLC A2426 6298 9412 5223 45 979 -367 C HETATM 3598 C3 OLC A2426 -30.677 -0.557 33.965 1.00 58.93 C ANISOU 3598 C3 OLC A2426 6789 9939 5662 119 1062 -515 C HETATM 3599 C2 OLC A2426 -30.424 0.799 33.332 1.00 61.74 C ANISOU 3599 C2 OLC A2426 7166 10188 6104 230 1059 -641 C HETATM 3600 C21 OLC A2426 -33.040 3.383 32.177 1.00 74.77 C ANISOU 3600 C21 OLC A2426 8641 11780 7988 544 1240 -895 C HETATM 3601 C1 OLC A2426 -31.767 1.438 33.058 1.00 70.52 C ANISOU 3601 C1 OLC A2426 8192 11319 7284 320 1149 -711 C HETATM 3602 C22 OLC A2426 -33.711 4.518 32.920 1.00 77.48 C ANISOU 3602 C22 OLC A2426 8981 12153 8305 659 1351 -1055 C HETATM 3603 O19 OLC A2426 -32.726 0.751 32.824 1.00 76.29 O ANISOU 3603 O19 OLC A2426 8833 12110 8043 296 1181 -635 O HETATM 3604 O25 OLC A2426 -34.229 6.642 33.146 1.00 77.48 O ANISOU 3604 O25 OLC A2426 9007 12065 8366 887 1452 -1320 O HETATM 3605 O23 OLC A2426 -35.048 4.442 33.389 1.00 82.21 O ANISOU 3605 O23 OLC A2426 9472 12870 8894 699 1468 -1071 O HETATM 3606 O20 OLC A2426 -32.041 2.846 33.045 1.00 73.10 O ANISOU 3606 O20 OLC A2426 8528 11600 7647 443 1202 -865 O HETATM 3607 C18 OLC A2427 -41.864 -5.111 14.209 1.00 75.26 C ANISOU 3607 C18 OLC A2427 7582 12279 8733 -677 297 680 C HETATM 3608 C10 OLC A2427 -38.601 3.101 14.778 1.00 53.44 C ANISOU 3608 C10 OLC A2427 4886 8970 6448 492 360 152 C HETATM 3609 C9 OLC A2427 -38.007 4.269 14.902 1.00 47.49 C ANISOU 3609 C9 OLC A2427 4204 8079 5760 626 345 73 C HETATM 3610 C17 OLC A2427 -40.784 -4.595 15.126 1.00 72.86 C ANISOU 3610 C17 OLC A2427 7382 11883 8420 -504 407 549 C HETATM 3611 C11 OLC A2427 -38.755 2.101 15.883 1.00 57.31 C ANISOU 3611 C11 OLC A2427 5338 9599 6837 445 494 116 C HETATM 3612 C8 OLC A2427 -37.405 4.748 16.176 1.00 45.47 C ANISOU 3612 C8 OLC A2427 3998 7798 5480 750 463 -80 C HETATM 3613 C24 OLC A2427 -37.895 16.887 17.799 1.00 83.00 C ANISOU 3613 C24 OLC A2427 9110 10915 11512 2395 43 -869 C HETATM 3614 C16 OLC A2427 -41.241 -3.645 16.229 1.00 71.93 C ANISOU 3614 C16 OLC A2427 7161 11797 8371 -307 486 480 C HETATM 3615 C12 OLC A2427 -39.328 0.776 15.383 1.00 60.52 C ANISOU 3615 C12 OLC A2427 5716 10100 7178 248 459 235 C HETATM 3616 C7 OLC A2427 -37.214 6.255 16.064 1.00 44.28 C ANISOU 3616 C7 OLC A2427 3883 7485 5456 910 400 -141 C HETATM 3617 C15 OLC A2427 -41.059 -2.177 15.857 1.00 72.08 C ANISOU 3617 C15 OLC A2427 7121 11775 8491 -125 471 422 C HETATM 3618 C13 OLC A2427 -40.034 0.066 16.502 1.00 66.35 C ANISOU 3618 C13 OLC A2427 6433 10901 7875 218 540 226 C HETATM 3619 C6 OLC A2427 -37.850 7.058 17.190 1.00 44.56 C ANISOU 3619 C6 OLC A2427 3807 7557 5566 1122 496 -269 C HETATM 3620 C14 OLC A2427 -39.853 -1.448 16.472 1.00 70.21 C ANISOU 3620 C14 OLC A2427 7012 11418 8246 19 539 289 C HETATM 3621 C5 OLC A2427 -37.425 8.496 17.271 1.00 43.46 C ANISOU 3621 C5 OLC A2427 3760 7218 5535 1274 444 -363 C HETATM 3622 C4 OLC A2427 -38.272 9.512 16.559 1.00 47.32 C ANISOU 3622 C4 OLC A2427 4153 7610 6218 1412 328 -306 C HETATM 3623 C3 OLC A2427 -38.081 10.829 17.271 1.00 49.76 C ANISOU 3623 C3 OLC A2427 4525 7757 6623 1615 347 -464 C HETATM 3624 C2 OLC A2427 -38.283 12.116 16.494 1.00 55.56 C ANISOU 3624 C2 OLC A2427 5288 8271 7553 1736 187 -420 C HETATM 3625 C21 OLC A2427 -40.004 15.279 18.013 1.00 76.09 C ANISOU 3625 C21 OLC A2427 7737 10552 10620 2483 242 -777 C HETATM 3626 C1 OLC A2427 -38.947 13.108 17.421 1.00 62.16 C ANISOU 3626 C1 OLC A2427 6047 9052 8520 2009 262 -585 C HETATM 3627 C22 OLC A2427 -39.044 16.314 18.556 1.00 82.31 C ANISOU 3627 C22 OLC A2427 8776 11081 11417 2543 223 -947 C HETATM 3628 O19 OLC A2427 -39.261 12.777 18.533 1.00 63.11 O ANISOU 3628 O19 OLC A2427 6088 9325 8566 2085 435 -719 O HETATM 3629 O25 OLC A2427 -38.397 18.204 17.648 1.00 87.71 O ANISOU 3629 O25 OLC A2427 9722 11262 12342 2623 -61 -909 O HETATM 3630 O23 OLC A2427 -39.152 16.846 19.868 1.00 85.87 O ANISOU 3630 O23 OLC A2427 9254 11515 11856 2733 379 -1201 O HETATM 3631 O20 OLC A2427 -39.260 14.470 17.103 1.00 69.53 O ANISOU 3631 O20 OLC A2427 7001 9754 9665 2201 145 -603 O HETATM 3632 C10 OLC A2428 -33.660 -8.395 24.666 1.00 54.18 C ANISOU 3632 C10 OLC A2428 5945 9044 5598 -358 767 290 C HETATM 3633 C9 OLC A2428 -33.304 -9.662 24.627 1.00 51.78 C ANISOU 3633 C9 OLC A2428 5713 8710 5250 -461 745 385 C HETATM 3634 C17 OLC A2428 -37.434 -0.823 23.658 1.00 72.83 C ANISOU 3634 C17 OLC A2428 7769 11580 8322 299 933 -163 C HETATM 3635 C11 OLC A2428 -34.510 -7.707 23.642 1.00 57.53 C ANISOU 3635 C11 OLC A2428 6282 9489 6089 -329 763 257 C HETATM 3636 C8 OLC A2428 -33.700 -10.604 23.543 1.00 48.51 C ANISOU 3636 C8 OLC A2428 5321 8267 4843 -578 716 462 C HETATM 3637 C24 OLC A2428 -31.874 -23.735 25.067 1.00 69.51 C ANISOU 3637 C24 OLC A2428 9439 9519 7451 -1752 -18 1716 C HETATM 3638 C16 OLC A2428 -36.150 -1.640 23.780 1.00 69.31 C ANISOU 3638 C16 OLC A2428 7477 11046 7811 212 889 -136 C HETATM 3639 C12 OLC A2428 -35.282 -6.532 24.239 1.00 63.76 C ANISOU 3639 C12 OLC A2428 6968 10363 6895 -238 809 187 C HETATM 3640 C7 OLC A2428 -33.121 -11.970 23.895 1.00 47.21 C ANISOU 3640 C7 OLC A2428 5268 8055 4613 -684 696 572 C HETATM 3641 C15 OLC A2428 -36.301 -3.062 23.251 1.00 69.55 C ANISOU 3641 C15 OLC A2428 7515 11103 7809 69 848 -18 C HETATM 3642 C13 OLC A2428 -35.531 -5.489 23.187 1.00 67.36 C ANISOU 3642 C13 OLC A2428 7371 10790 7434 -153 794 130 C HETATM 3643 C6 OLC A2428 -33.160 -12.989 22.764 1.00 48.62 C ANISOU 3643 C6 OLC A2428 5531 8154 4787 -807 664 642 C HETATM 3644 C14 OLC A2428 -35.212 -4.071 23.649 1.00 69.41 C ANISOU 3644 C14 OLC A2428 7629 11019 7726 -11 823 17 C HETATM 3645 C5 OLC A2428 -32.496 -14.304 23.064 1.00 50.15 C ANISOU 3645 C5 OLC A2428 5869 8267 4920 -904 637 760 C HETATM 3646 C4 OLC A2428 -32.786 -15.463 22.152 1.00 49.70 C ANISOU 3646 C4 OLC A2428 5935 8062 4885 -1048 570 825 C HETATM 3647 C3 OLC A2428 -32.070 -16.666 22.718 1.00 48.51 C ANISOU 3647 C3 OLC A2428 5945 7746 4739 -1082 507 918 C HETATM 3648 C2 OLC A2428 -32.880 -17.889 23.108 1.00 56.47 C ANISOU 3648 C2 OLC A2428 7020 8725 5710 -1300 442 1080 C HETATM 3649 C21 OLC A2428 -31.552 -21.279 24.089 1.00 64.79 C ANISOU 3649 C21 OLC A2428 8554 9216 6848 -1447 192 1379 C HETATM 3650 C1 OLC A2428 -31.979 -19.094 22.969 1.00 61.22 C ANISOU 3650 C1 OLC A2428 7839 9041 6381 -1289 353 1119 C HETATM 3651 C22 OLC A2428 -32.392 -22.492 24.426 1.00 68.51 C ANISOU 3651 C22 OLC A2428 9128 9614 7289 -1699 98 1561 C HETATM 3652 O19 OLC A2428 -30.842 -18.952 22.603 1.00 64.64 O ANISOU 3652 O19 OLC A2428 8339 9338 6885 -1114 356 1023 O HETATM 3653 O25 OLC A2428 -33.117 -24.285 25.471 1.00 69.13 O ANISOU 3653 O25 OLC A2428 9377 9574 7316 -2035 -57 1882 O HETATM 3654 O23 OLC A2428 -33.783 -22.559 24.157 1.00 72.66 O ANISOU 3654 O23 OLC A2428 9578 10275 7754 -1922 101 1617 O HETATM 3655 O20 OLC A2428 -32.347 -20.455 23.236 1.00 63.53 O ANISOU 3655 O20 OLC A2428 8273 9194 6673 -1469 258 1269 O HETATM 3656 C10 OLC A2429 -35.880 -9.969 19.640 1.00 61.36 C ANISOU 3656 C10 OLC A2429 6781 9947 6585 -715 633 466 C HETATM 3657 C9 OLC A2429 -35.317 -10.717 18.712 1.00 56.00 C ANISOU 3657 C9 OLC A2429 6225 9175 5879 -803 608 485 C HETATM 3658 C11 OLC A2429 -37.262 -10.173 20.185 1.00 66.66 C ANISOU 3658 C11 OLC A2429 7317 10763 7246 -800 631 542 C HETATM 3659 C8 OLC A2429 -35.995 -11.881 18.075 1.00 55.04 C ANISOU 3659 C8 OLC A2429 6147 9055 5709 -1021 560 588 C HETATM 3660 C24 OLC A2429 -35.275 -24.756 20.499 1.00 79.91 C ANISOU 3660 C24 OLC A2429 10948 10585 8830 -2338 -149 1494 C HETATM 3661 C12 OLC A2429 -37.301 -10.100 21.711 1.00 68.38 C ANISOU 3661 C12 OLC A2429 7509 11037 7435 -745 682 535 C HETATM 3662 C7 OLC A2429 -35.021 -13.052 18.064 1.00 50.13 C ANISOU 3662 C7 OLC A2429 5737 8249 5062 -1068 539 598 C HETATM 3663 C15 OLC A2429 -38.397 -6.370 22.001 1.00 72.11 C ANISOU 3663 C15 OLC A2429 7701 11641 8058 -340 772 306 C HETATM 3664 C13 OLC A2429 -38.081 -8.894 22.149 1.00 69.94 C ANISOU 3664 C13 OLC A2429 7563 11342 7670 -624 723 474 C HETATM 3665 C6 OLC A2429 -35.420 -14.218 18.959 1.00 49.01 C ANISOU 3665 C6 OLC A2429 5633 8116 4874 -1215 522 722 C HETATM 3666 C14 OLC A2429 -37.553 -7.583 21.576 1.00 69.65 C ANISOU 3666 C14 OLC A2429 7526 11236 7702 -462 726 364 C HETATM 3667 C5 OLC A2429 -35.210 -15.586 18.373 1.00 48.47 C ANISOU 3667 C5 OLC A2429 5774 7829 4814 -1346 437 756 C HETATM 3668 C4 OLC A2429 -35.602 -16.773 19.206 1.00 51.99 C ANISOU 3668 C4 OLC A2429 6279 8253 5222 -1510 398 896 C HETATM 3669 C3 OLC A2429 -35.428 -17.998 18.340 1.00 55.89 C ANISOU 3669 C3 OLC A2429 7001 8493 5743 -1629 301 898 C HETATM 3670 C2 OLC A2429 -35.637 -19.371 18.949 1.00 59.70 C ANISOU 3670 C2 OLC A2429 7615 8858 6209 -1801 230 1034 C HETATM 3671 C21 OLC A2429 -34.980 -22.736 18.792 1.00 71.59 C ANISOU 3671 C21 OLC A2429 9701 9712 7789 -2057 -1 1164 C HETATM 3672 C1 OLC A2429 -34.679 -20.329 18.276 1.00 62.51 C ANISOU 3672 C1 OLC A2429 8238 8891 6623 -1762 170 963 C HETATM 3673 C22 OLC A2429 -34.510 -23.610 19.932 1.00 76.50 C ANISOU 3673 C22 OLC A2429 10424 10218 8425 -2071 -43 1299 C HETATM 3674 O19 OLC A2429 -34.261 -20.096 17.173 1.00 65.70 O ANISOU 3674 O19 OLC A2429 8716 9192 7054 -1685 173 828 O HETATM 3675 O25 OLC A2429 -34.180 -25.458 21.060 1.00 81.01 O ANISOU 3675 O25 OLC A2429 11254 10492 9034 -2215 -189 1526 O HETATM 3676 O23 OLC A2429 -33.264 -23.414 20.581 1.00 80.58 O ANISOU 3676 O23 OLC A2429 10954 10680 8983 -1840 1 1269 O HETATM 3677 O20 OLC A2429 -34.187 -21.551 18.839 1.00 64.19 O ANISOU 3677 O20 OLC A2429 8636 8891 6864 -1804 108 1044 O HETATM 3678 O HOH A2501 0.099 -50.410 21.975 1.00 59.22 O HETATM 3679 O HOH A2502 -18.465 13.254 24.009 1.00 45.48 O HETATM 3680 O HOH A2503 -28.182 12.315 38.776 1.00 54.56 O HETATM 3681 O HOH A2504 -21.208 -23.968 30.407 1.00 58.75 O HETATM 3682 O HOH A2505 -28.274 3.277 16.912 1.00 41.44 O HETATM 3683 O HOH A2506 -24.961 13.500 11.581 1.00 52.46 O HETATM 3684 O HOH A2507 22.363 -61.156 19.336 1.00 47.53 O HETATM 3685 O HOH A2508 -31.313 8.681 32.449 1.00 71.11 O HETATM 3686 O HOH A2509 -28.015 3.350 19.659 1.00 22.62 O HETATM 3687 O HOH A2510 -22.966 -28.062 21.925 1.00 46.75 O HETATM 3688 O HOH A2511 3.986 -72.923 24.094 1.00 53.83 O HETATM 3689 O HOH A2512 -4.356 -63.252 26.978 1.00 54.23 O HETATM 3690 O HOH A2513 -13.284 -33.523 21.423 1.00 46.69 O HETATM 3691 O HOH A2514 -22.162 -6.610 15.422 1.00 24.89 O HETATM 3692 O HOH A2515 -16.560 -29.131 11.695 1.00 47.82 O HETATM 3693 O HOH A2516 -16.285 -16.709 19.342 1.00 19.48 O HETATM 3694 O HOH A2517 -22.497 18.087 25.886 1.00 41.10 O HETATM 3695 O HOH A2518 -26.087 7.970 13.020 1.00 21.77 O HETATM 3696 O HOH A2519 -24.909 16.675 1.920 1.00 45.16 O HETATM 3697 O HOH A2520 -44.559 16.468 12.460 1.00 50.68 O HETATM 3698 O HOH A2521 -14.683 -26.874 17.547 1.00 35.87 O HETATM 3699 O HOH A2522 -17.196 -24.913 9.775 1.00 43.21 O HETATM 3700 O HOH A2523 -10.034 -28.766 9.724 1.00 52.57 O HETATM 3701 O HOH A2524 -23.565 -4.701 14.064 1.00 22.00 O HETATM 3702 O HOH A2525 -5.643 -31.443 24.753 1.00 49.62 O HETATM 3703 O HOH A2526 -4.727 -25.737 25.371 1.00 37.54 O HETATM 3704 O HOH A2527 -23.733 15.591 33.287 1.00 43.04 O HETATM 3705 O HOH A2528 0.109 -28.010 21.204 1.00 53.06 O HETATM 3706 O HOH A2529 -26.483 2.027 15.676 1.00 20.02 O HETATM 3707 O HOH A2530 -24.649 23.932 30.020 1.00 44.02 O HETATM 3708 O HOH A2531 -24.187 -10.956 11.769 1.00 38.59 O HETATM 3709 O HOH A2532 -11.319 15.471 23.315 1.00 31.49 O HETATM 3710 O HOH A2533 -40.042 15.564 23.228 1.00 41.76 O HETATM 3711 O HOH A2534 -16.370 0.769 12.871 1.00 15.53 O HETATM 3712 O HOH A2535 -19.524 -35.446 26.861 1.00 49.16 O HETATM 3713 O HOH A2536 -7.579 10.514 31.010 1.00 46.13 O HETATM 3714 O HOH A2537 -25.950 -14.209 24.842 1.00 28.96 O HETATM 3715 O HOH A2538 -11.255 12.187 16.023 1.00 21.54 O HETATM 3716 O HOH A2539 -9.248 -53.284 26.117 1.00 62.60 O HETATM 3717 O HOH A2540 -28.659 -29.602 0.275 1.00 64.18 O HETATM 3718 O HOH A2541 -34.796 9.255 33.380 1.00 50.99 O HETATM 3719 O HOH A2542 -2.035 13.131 22.261 1.00 36.56 O HETATM 3720 O HOH A2543 -25.457 -13.293 13.670 1.00 19.25 O HETATM 3721 O HOH A2544 -26.201 18.570 22.153 1.00 20.86 O HETATM 3722 O HOH A2545 -18.711 10.236 23.133 1.00 38.23 O HETATM 3723 O HOH A2546 -0.655 -62.794 20.095 1.00 39.27 O HETATM 3724 O HOH A2547 -15.137 10.432 18.092 1.00 18.77 O HETATM 3725 O HOH A2548 -25.920 -11.807 21.615 1.00 21.84 O HETATM 3726 O HOH A2549 -10.097 15.023 25.172 1.00 37.56 O HETATM 3727 O HOH A2550 -19.075 -11.189 13.156 1.00 25.09 O HETATM 3728 O HOH A2551 7.375 -60.631 15.464 1.00 48.66 O HETATM 3729 O HOH A2552 -18.084 -17.251 16.946 1.00 28.28 O HETATM 3730 O HOH A2553 -13.897 -27.820 19.881 1.00 48.54 O HETATM 3731 O HOH A2554 -32.591 24.068 25.475 1.00 56.03 O HETATM 3732 O HOH A2555 -21.676 -33.206 22.600 1.00 53.61 O HETATM 3733 O HOH A2556 -20.865 -2.380 24.563 1.00 25.51 O HETATM 3734 O HOH A2557 -6.941 12.440 27.943 1.00 46.98 O HETATM 3735 O HOH A2558 -18.227 -2.467 20.319 1.00 19.27 O HETATM 3736 O HOH A2559 -25.779 17.125 27.015 1.00 41.73 O HETATM 3737 O HOH A2560 -17.578 14.205 29.551 1.00 53.29 O HETATM 3738 O HOH A2561 -19.397 -1.463 22.421 1.00 24.88 O HETATM 3739 O HOH A2562 -36.689 -30.506 17.438 1.00 66.02 O HETATM 3740 O HOH A2563 -26.189 -11.660 25.822 1.00 30.14 O HETATM 3741 O HOH A2564 -28.904 -30.101 27.090 1.00 55.50 O HETATM 3742 O HOH A2565 -9.585 15.367 18.590 1.00 43.30 O HETATM 3743 O HOH A2566 -29.929 18.227 29.718 1.00 50.59 O HETATM 3744 O HOH A2567 -21.222 -27.422 18.296 1.00 61.32 O HETATM 3745 O HOH A2568 -27.670 20.898 22.392 1.00 25.52 O HETATM 3746 O HOH A2569 -10.197 19.643 21.073 1.00 39.15 O HETATM 3747 O HOH A2570 -24.207 11.692 16.813 1.00 17.26 O HETATM 3748 O HOH A2571 -15.124 3.901 22.046 1.00 16.77 O HETATM 3749 O HOH A2572 -16.586 16.929 8.986 1.00 41.24 O HETATM 3750 O HOH A2573 -20.123 11.400 16.448 1.00 31.47 O HETATM 3751 O HOH A2574 -24.822 -6.429 17.629 1.00 43.66 O HETATM 3752 O HOH A2575 -27.603 -11.368 6.963 1.00 33.98 O HETATM 3753 O HOH A2576 -11.029 -33.811 21.909 1.00 50.05 O HETATM 3754 O HOH A2577 6.004 -75.677 26.557 1.00 35.84 O HETATM 3755 O HOH A2578 -25.241 -15.561 14.703 1.00 28.85 O HETATM 3756 O HOH A2579 -39.288 16.895 25.496 1.00 53.83 O HETATM 3757 O HOH A2580 18.769 -58.938 26.433 1.00 57.69 O HETATM 3758 O HOH A2581 -25.475 12.350 14.632 1.00 38.89 O HETATM 3759 O HOH A2582 -22.687 -9.902 15.095 1.00 62.04 O HETATM 3760 O HOH A2583 -20.795 15.214 33.481 1.00 58.09 O HETATM 3761 O HOH A2584 -18.688 -27.979 6.957 1.00 41.39 O HETATM 3762 O HOH A2585 -2.800 -64.339 20.150 1.00 62.33 O HETATM 3763 O HOH A2586 -22.185 -29.246 9.200 1.00 43.06 O HETATM 3764 O HOH A2587 -25.763 18.850 24.813 1.00 23.84 O HETATM 3765 O HOH A2588 -5.173 18.700 12.980 1.00 47.57 O HETATM 3766 O HOH A2589 -20.812 -11.161 15.324 1.00 48.89 O HETATM 3767 O HOH A2590 -22.003 12.812 17.812 1.00 29.05 O HETATM 3768 O HOH A2591 2.358 -29.353 19.484 1.00 62.39 O HETATM 3769 O HOH A2592 -23.474 -28.568 0.560 1.00 54.10 O HETATM 3770 O HOH A2593 -23.510 9.315 16.046 1.00 31.84 O HETATM 3771 O HOH A2594 -4.412 -64.019 17.922 1.00 42.37 O HETATM 3772 O HOH A2595 -15.081 12.529 28.708 1.00 23.57 O HETATM 3773 O HOH A2596 -35.987 18.821 15.900 1.00 56.53 O HETATM 3774 O HOH A2597 -17.138 12.481 32.924 1.00 48.59 O HETATM 3775 O HOH A2598 -17.211 13.816 26.573 1.00 29.46 O HETATM 3776 O HOH A2599 -9.067 13.598 16.645 1.00 26.71 O HETATM 3777 O HOH A2600 -3.237 16.433 21.715 1.00 40.81 O HETATM 3778 O HOH A2601 -28.581 -28.151 34.040 1.00 59.55 O HETATM 3779 O HOH A2602 -17.435 15.251 6.185 1.00 31.31 O HETATM 3780 O HOH A2603 -25.127 -29.384 23.163 1.00 45.66 O HETATM 3781 O HOH A2604 -23.858 -26.815 13.949 1.00 45.12 O HETATM 3782 O HOH A2605 -17.040 15.717 12.736 1.00 61.44 O HETATM 3783 O HOH A2606 -31.061 -30.018 6.624 1.00 54.56 O HETATM 3784 O HOH A2607 -19.947 -28.521 8.746 1.00 49.86 O HETATM 3785 O HOH A2608 -15.885 -39.827 17.121 1.00 62.53 O HETATM 3786 O HOH A2609 -12.064 -35.596 28.432 1.00 52.40 O HETATM 3787 O HOH A2610 -23.014 27.298 1.829 1.00 64.06 O HETATM 3788 O HOH A2611 -43.999 15.268 9.389 1.00 65.35 O HETATM 3789 O HOH A2612 -31.202 21.005 28.389 1.00 48.22 O HETATM 3790 O HOH A2613 -20.984 12.702 34.909 1.00 43.15 O HETATM 3791 O HOH A2614 -19.832 -30.817 21.196 1.00 55.07 O HETATM 3792 O HOH A2615 -19.502 13.072 33.113 1.00 58.06 O HETATM 3793 O HOH A2616 -20.177 -18.388 15.800 1.00 41.20 O HETATM 3794 O HOH A2617 -22.055 17.204 33.290 1.00 43.63 O HETATM 3795 O HOH A2618 -28.485 22.238 33.599 1.00 54.63 O HETATM 3796 O HOH A2619 -27.073 18.907 13.740 1.00 64.71 O HETATM 3797 O HOH A2620 -29.543 15.867 34.469 1.00 58.42 O HETATM 3798 O HOH A2621 -15.696 14.677 22.399 1.00 50.95 O HETATM 3799 O HOH A2622 -40.505 24.861 25.462 1.00 54.11 O HETATM 3800 O HOH A2623 -7.624 -16.577 28.344 1.00 51.21 O HETATM 3801 O HOH A2624 -21.396 -24.238 32.662 1.00 63.11 O HETATM 3802 O HOH A2625 -19.578 -20.695 13.731 1.00 51.38 O HETATM 3803 O HOH A2626 -37.591 17.614 28.129 1.00 57.00 O HETATM 3804 O HOH A2627 -39.973 -28.709 12.930 1.00 62.32 O HETATM 3805 O HOH A2628 -13.151 13.977 24.293 1.00 36.79 O HETATM 3806 O HOH A2629 -18.331 -27.154 11.250 1.00 63.95 O HETATM 3807 O HOH A2630 -18.118 -33.199 22.753 1.00 60.26 O HETATM 3808 O HOH A2631 -24.611 9.812 13.556 1.00 34.23 O HETATM 3809 O HOH A2632 -20.779 -21.981 15.207 1.00 63.47 O HETATM 3810 O HOH A2633 -21.508 15.195 17.418 1.00 46.48 O HETATM 3811 O HOH A2634 -23.335 13.156 13.653 1.00 59.42 O HETATM 3812 O HOH A2635 -21.434 11.151 13.409 1.00 52.27 O HETATM 3813 O HOH A2636 -25.897 21.024 11.939 1.00 56.13 O CONECT 413 3167 CONECT 557 1246 CONECT 573 1155 CONECT 593 1290 CONECT 712 3167 CONECT 1155 573 CONECT 1246 557 CONECT 1290 593 CONECT 2745 2766 CONECT 2766 2745 CONECT 3167 413 712 3691 3751 CONECT 3167 3759 CONECT 3168 3169 CONECT 3169 3168 3170 3175 CONECT 3170 3169 3171 CONECT 3171 3170 3172 3176 CONECT 3172 3171 3173 CONECT 3173 3172 3174 3175 CONECT 3174 3173 CONECT 3175 3169 3173 CONECT 3176 3171 3177 3182 CONECT 3177 3176 3178 3183 CONECT 3178 3177 3179 CONECT 3179 3178 3180 3181 CONECT 3180 3179 CONECT 3181 3179 3182 CONECT 3182 3176 3181 CONECT 3183 3177 3184 3189 CONECT 3184 3183 3185 CONECT 3185 3184 3186 CONECT 3186 3185 3187 3188 CONECT 3187 3186 CONECT 3188 3186 3189 CONECT 3189 3183 3188 CONECT 3190 3191 3199 CONECT 3191 3190 3192 CONECT 3192 3191 3193 3217 CONECT 3193 3192 3194 CONECT 3194 3193 3195 3199 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 3203 CONECT 3198 3197 3199 3200 CONECT 3199 3190 3194 3198 3208 CONECT 3200 3198 3201 CONECT 3201 3200 3202 CONECT 3202 3201 3203 3206 3207 CONECT 3203 3197 3202 3204 CONECT 3204 3203 3205 CONECT 3205 3204 3206 CONECT 3206 3202 3205 3209 CONECT 3207 3202 CONECT 3208 3199 CONECT 3209 3206 3210 3211 CONECT 3210 3209 CONECT 3211 3209 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 3216 CONECT 3215 3214 CONECT 3216 3214 CONECT 3217 3192 CONECT 3218 3219 3227 CONECT 3219 3218 3220 CONECT 3220 3219 3221 3245 CONECT 3221 3220 3222 CONECT 3222 3221 3223 3227 CONECT 3223 3222 3224 CONECT 3224 3223 3225 CONECT 3225 3224 3226 3231 CONECT 3226 3225 3227 3228 CONECT 3227 3218 3222 3226 3236 CONECT 3228 3226 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 3234 3235 CONECT 3231 3225 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3230 3233 3237 CONECT 3235 3230 CONECT 3236 3227 CONECT 3237 3234 3238 3239 CONECT 3238 3237 CONECT 3239 3237 3240 CONECT 3240 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 3244 CONECT 3243 3242 CONECT 3244 3242 CONECT 3245 3220 CONECT 3246 3247 3255 CONECT 3247 3246 3248 CONECT 3248 3247 3249 3273 CONECT 3249 3248 3250 CONECT 3250 3249 3251 3255 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 3259 CONECT 3254 3253 3255 3256 CONECT 3255 3246 3250 3254 3264 CONECT 3256 3254 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 3262 3263 CONECT 3259 3253 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3258 3261 3265 CONECT 3263 3258 CONECT 3264 3255 CONECT 3265 3262 3266 3267 CONECT 3266 3265 CONECT 3267 3265 3268 CONECT 3268 3267 3269 CONECT 3269 3268 3270 CONECT 3270 3269 3271 3272 CONECT 3271 3270 CONECT 3272 3270 CONECT 3273 3248 CONECT 3274 3275 3276 3277 CONECT 3275 3274 CONECT 3276 3274 CONECT 3277 3274 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 3284 CONECT 3284 3283 3285 CONECT 3285 3284 3286 CONECT 3286 3285 3287 CONECT 3287 3286 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 3291 CONECT 3291 3290 3292 CONECT 3292 3291 3293 CONECT 3293 3292 CONECT 3294 3295 3296 3297 CONECT 3295 3294 CONECT 3296 3294 CONECT 3297 3294 3298 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3299 3301 CONECT 3301 3300 3302 CONECT 3302 3301 3303 CONECT 3303 3302 3304 CONECT 3304 3303 3305 CONECT 3305 3304 3306 CONECT 3306 3305 3307 CONECT 3307 3306 3308 CONECT 3308 3307 CONECT 3309 3310 3311 3312 CONECT 3310 3309 CONECT 3311 3309 CONECT 3312 3309 3313 CONECT 3313 3312 3314 CONECT 3314 3313 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 CONECT 3318 3319 3320 3321 CONECT 3319 3318 CONECT 3320 3318 CONECT 3321 3318 3322 CONECT 3322 3321 3323 CONECT 3323 3322 3324 CONECT 3324 3323 3325 CONECT 3325 3324 3326 CONECT 3326 3325 CONECT 3327 3328 3329 3330 CONECT 3328 3327 CONECT 3329 3327 CONECT 3330 3327 3331 CONECT 3331 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 CONECT 3336 3337 3338 3339 CONECT 3337 3336 CONECT 3338 3336 CONECT 3339 3336 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 CONECT 3343 3342 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 CONECT 3354 3355 3356 3357 CONECT 3355 3354 CONECT 3356 3354 CONECT 3357 3354 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 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 CONECT 3374 3375 3376 3377 CONECT 3375 3374 CONECT 3376 3374 CONECT 3377 3374 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 CONECT 3389 3390 3391 3392 CONECT 3390 3389 CONECT 3391 3389 CONECT 3392 3389 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 CONECT 3401 3402 3403 3404 CONECT 3402 3401 CONECT 3403 3401 CONECT 3404 3401 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 CONECT 3409 3410 3411 3412 CONECT 3410 3409 CONECT 3411 3409 CONECT 3412 3409 3413 CONECT 3413 3412 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3419 CONECT 3419 3418 CONECT 3420 3421 3422 3423 CONECT 3421 3420 CONECT 3422 3420 CONECT 3423 3420 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 3430 CONECT 3430 3429 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 CONECT 3434 3435 3436 3437 CONECT 3435 3434 CONECT 3436 3434 CONECT 3437 3434 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 CONECT 3444 3443 3445 CONECT 3445 3444 3446 CONECT 3446 3445 CONECT 3447 3448 3449 3450 CONECT 3448 3447 CONECT 3449 3447 CONECT 3450 3447 3451 CONECT 3451 3450 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3464 CONECT 3464 3463 3465 CONECT 3465 3464 CONECT 3466 3467 3468 3469 CONECT 3467 3466 CONECT 3468 3466 CONECT 3469 3466 3470 CONECT 3470 3469 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 CONECT 3475 3476 CONECT 3476 3475 3477 CONECT 3477 3476 3479 CONECT 3478 3487 3489 CONECT 3479 3477 3480 CONECT 3480 3479 3481 CONECT 3481 3480 3482 CONECT 3482 3481 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3486 CONECT 3485 3487 3491 CONECT 3486 3484 3488 3491 CONECT 3487 3478 3485 3490 CONECT 3488 3486 CONECT 3489 3478 CONECT 3490 3487 CONECT 3491 3485 3486 CONECT 3492 3493 3494 CONECT 3493 3492 3495 CONECT 3494 3492 3498 CONECT 3495 3493 3499 CONECT 3496 3510 3512 CONECT 3497 3500 CONECT 3498 3494 3501 CONECT 3499 3495 3502 CONECT 3500 3497 3503 CONECT 3501 3498 3503 CONECT 3502 3499 3504 CONECT 3503 3500 3501 CONECT 3504 3502 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3509 CONECT 3508 3510 3514 CONECT 3509 3507 3511 3514 CONECT 3510 3496 3508 3513 CONECT 3511 3509 CONECT 3512 3496 CONECT 3513 3510 CONECT 3514 3508 3509 CONECT 3515 3516 CONECT 3516 3515 3518 CONECT 3517 3526 3528 CONECT 3518 3516 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3525 CONECT 3524 3526 3530 CONECT 3525 3523 3527 3530 CONECT 3526 3517 3524 3529 CONECT 3527 3525 CONECT 3528 3517 CONECT 3529 3526 CONECT 3530 3524 3525 CONECT 3531 3540 3542 CONECT 3532 3533 CONECT 3533 3532 3534 CONECT 3534 3533 3535 CONECT 3535 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 3539 CONECT 3538 3540 3544 CONECT 3539 3537 3541 3544 CONECT 3540 3531 3538 3543 CONECT 3541 3539 CONECT 3542 3531 CONECT 3543 3540 CONECT 3544 3538 3539 CONECT 3545 3547 CONECT 3546 3555 3557 CONECT 3547 3545 3548 CONECT 3548 3547 3549 CONECT 3549 3548 3550 CONECT 3550 3549 3551 CONECT 3551 3550 3552 CONECT 3552 3551 3554 CONECT 3553 3555 3559 CONECT 3554 3552 3556 3559 CONECT 3555 3546 3553 3558 CONECT 3556 3554 CONECT 3557 3546 CONECT 3558 3555 CONECT 3559 3553 3554 CONECT 3560 3561 3562 CONECT 3561 3560 3563 CONECT 3562 3560 3565 CONECT 3563 3561 3566 CONECT 3564 3577 3579 CONECT 3565 3562 3568 CONECT 3566 3563 3569 CONECT 3567 3570 CONECT 3568 3565 3570 CONECT 3569 3566 3571 CONECT 3570 3567 3568 CONECT 3571 3569 3572 CONECT 3572 3571 3573 CONECT 3573 3572 3574 CONECT 3574 3573 3576 CONECT 3575 3577 3581 CONECT 3576 3574 3578 3581 CONECT 3577 3564 3575 3580 CONECT 3578 3576 CONECT 3579 3564 CONECT 3580 3577 CONECT 3581 3575 3576 CONECT 3582 3585 CONECT 3583 3584 3586 CONECT 3584 3583 3587 CONECT 3585 3582 3589 CONECT 3586 3583 3590 CONECT 3587 3584 3591 CONECT 3588 3602 3604 CONECT 3589 3585 3592 CONECT 3590 3586 3593 CONECT 3591 3587 3594 CONECT 3592 3589 3595 CONECT 3593 3590 3595 CONECT 3594 3591 3596 CONECT 3595 3592 3593 CONECT 3596 3594 3597 CONECT 3597 3596 3598 CONECT 3598 3597 3599 CONECT 3599 3598 3601 CONECT 3600 3602 3606 CONECT 3601 3599 3603 3606 CONECT 3602 3588 3600 3605 CONECT 3603 3601 CONECT 3604 3588 CONECT 3605 3602 CONECT 3606 3600 3601 CONECT 3607 3610 CONECT 3608 3609 3611 CONECT 3609 3608 3612 CONECT 3610 3607 3614 CONECT 3611 3608 3615 CONECT 3612 3609 3616 CONECT 3613 3627 3629 CONECT 3614 3610 3617 CONECT 3615 3611 3618 CONECT 3616 3612 3619 CONECT 3617 3614 3620 CONECT 3618 3615 3620 CONECT 3619 3616 3621 CONECT 3620 3617 3618 CONECT 3621 3619 3622 CONECT 3622 3621 3623 CONECT 3623 3622 3624 CONECT 3624 3623 3626 CONECT 3625 3627 3631 CONECT 3626 3624 3628 3631 CONECT 3627 3613 3625 3630 CONECT 3628 3626 CONECT 3629 3613 CONECT 3630 3627 CONECT 3631 3625 3626 CONECT 3632 3633 3635 CONECT 3633 3632 3636 CONECT 3634 3638 CONECT 3635 3632 3639 CONECT 3636 3633 3640 CONECT 3637 3651 3653 CONECT 3638 3634 3641 CONECT 3639 3635 3642 CONECT 3640 3636 3643 CONECT 3641 3638 3644 CONECT 3642 3639 3644 CONECT 3643 3640 3645 CONECT 3644 3641 3642 CONECT 3645 3643 3646 CONECT 3646 3645 3647 CONECT 3647 3646 3648 CONECT 3648 3647 3650 CONECT 3649 3651 3655 CONECT 3650 3648 3652 3655 CONECT 3651 3637 3649 3654 CONECT 3652 3650 CONECT 3653 3637 CONECT 3654 3651 CONECT 3655 3649 3650 CONECT 3656 3657 3658 CONECT 3657 3656 3659 CONECT 3658 3656 3661 CONECT 3659 3657 3662 CONECT 3660 3673 3675 CONECT 3661 3658 3664 CONECT 3662 3659 3665 CONECT 3663 3666 CONECT 3664 3661 3666 CONECT 3665 3662 3667 CONECT 3666 3663 3664 CONECT 3667 3665 3668 CONECT 3668 3667 3669 CONECT 3669 3668 3670 CONECT 3670 3669 3672 CONECT 3671 3673 3677 CONECT 3672 3670 3674 3677 CONECT 3673 3660 3671 3676 CONECT 3674 3672 CONECT 3675 3660 CONECT 3676 3673 CONECT 3677 3671 3672 CONECT 3691 3167 CONECT 3751 3167 CONECT 3759 3167 MASTER 743 0 30 19 2 0 51 6 3645 1 525 34 END