HEADER SIGNALING PROTEIN 22-OCT-15 5EE7 TITLE CRYSTAL STRUCTURE OF THE HUMAN GLUCAGON RECEPTOR (GCGR) IN COMPLEX TITLE 2 WITH THE ANTAGONIST MK-0893 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUCAGON RECEPTOR,ENDOLYSIN,GLUCAGON RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: GL-R,LYSIS PROTEIN,LYSOZYME,MURAMIDASE,GL-R; COMPND 5 EC: 3.2.1.17; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: CHIMERIC FUSION OF HUMAN GLUCAGON RECEPTOR AND T4- COMPND 9 LYSOZYME SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: GCGR; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF21 KEYWDS GPCR, SIGNALING PROTEIN, 7TM EXPDTA X-RAY DIFFRACTION AUTHOR A.JAZAYERI,A.S.DORE,D.LAMB,H.KRISHNAMURTHY,S.M.SOUTHALL,A.H.BAIG, AUTHOR 2 A.BORTOLATO,M.KOGLIN,N.J.ROBERTSON,J.C.ERREY,S.P.ANDREWS, AUTHOR 3 A.J.H.BROWN,R.M.COOKE,M.WEIR,F.H.MARSHALL REVDAT 3 18-MAY-16 5EE7 1 JRNL REVDAT 2 11-MAY-16 5EE7 1 JRNL REVDAT 1 20-APR-16 5EE7 0 JRNL AUTH A.JAZAYERI,A.S.DORE,D.LAMB,H.KRISHNAMURTHY,S.M.SOUTHALL, JRNL AUTH 2 A.H.BAIG,A.BORTOLATO,M.KOGLIN,N.J.ROBERTSON,J.C.ERREY, JRNL AUTH 3 S.P.ANDREWS,I.TEOBALD,A.J.BROWN,R.M.COOKE,M.WEIR, JRNL AUTH 4 F.H.MARSHALL JRNL TITL EXTRA-HELICAL BINDING SITE OF A GLUCAGON RECEPTOR JRNL TITL 2 ANTAGONIST. JRNL REF NATURE V. 533 274 2016 JRNL REFN ESSN 1476-4687 JRNL PMID 27111510 JRNL DOI 10.1038/NATURE17414 REMARK 2 REMARK 2 RESOLUTION. 2.50 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8 REMARK 3 NUMBER OF REFLECTIONS : 15996 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.228 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860 REMARK 3 FREE R VALUE TEST SET COUNT : 777 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 19.9715 - 4.5282 0.86 2575 122 0.2153 0.2793 REMARK 3 2 4.5282 - 3.6011 0.90 2556 134 0.1973 0.2287 REMARK 3 3 3.6011 - 3.1479 0.89 2502 123 0.2336 0.2434 REMARK 3 4 3.1479 - 2.8610 0.91 2560 127 0.2446 0.2944 REMARK 3 5 2.8610 - 2.6564 0.92 2537 140 0.2655 0.2683 REMARK 3 6 2.6564 - 2.5001 0.90 2489 131 0.2757 0.3150 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.480 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 35.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 3661 REMARK 3 ANGLE : 0.796 4888 REMARK 3 CHIRALITY : 0.029 531 REMARK 3 PLANARITY : 0.004 594 REMARK 3 DIHEDRAL : 13.545 1344 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 27 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 160 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.8876 14.8775 -54.3628 REMARK 3 T TENSOR REMARK 3 T11: 0.1802 T22: 0.2131 REMARK 3 T33: 0.2355 T12: 0.0184 REMARK 3 T13: -0.0122 T23: -0.0013 REMARK 3 L TENSOR REMARK 3 L11: 0.5334 L22: 1.1018 REMARK 3 L33: -0.0869 L12: 0.6391 REMARK 3 L13: -0.3089 L23: -0.2169 REMARK 3 S TENSOR REMARK 3 S11: 0.0497 S12: 0.0190 S13: -0.0291 REMARK 3 S21: 0.0409 S22: 0.0187 S23: -0.0317 REMARK 3 S31: 0.0340 S32: 0.0522 S33: 0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 172 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.9507 17.2713 -29.6347 REMARK 3 T TENSOR REMARK 3 T11: 0.4200 T22: 0.3210 REMARK 3 T33: 0.2479 T12: 0.0960 REMARK 3 T13: 0.0461 T23: 0.0635 REMARK 3 L TENSOR REMARK 3 L11: 0.0199 L22: 0.1399 REMARK 3 L33: 0.0161 L12: -0.0587 REMARK 3 L13: 0.0570 L23: -0.0268 REMARK 3 S TENSOR REMARK 3 S11: -0.4863 S12: 0.2893 S13: -0.4858 REMARK 3 S21: 0.3944 S22: 0.3852 S23: 0.4384 REMARK 3 S31: -0.7040 S32: 0.9190 S33: 0.0000 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 194 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.9690 12.8960 -46.2249 REMARK 3 T TENSOR REMARK 3 T11: 0.2390 T22: 0.1873 REMARK 3 T33: 0.2806 T12: -0.0017 REMARK 3 T13: -0.0131 T23: 0.0076 REMARK 3 L TENSOR REMARK 3 L11: -1.0840 L22: -0.1881 REMARK 3 L33: -0.4311 L12: -0.7295 REMARK 3 L13: 0.2788 L23: -0.7766 REMARK 3 S TENSOR REMARK 3 S11: -0.1416 S12: 0.0740 S13: 0.1253 REMARK 3 S21: 0.0760 S22: -0.0831 S23: -0.1991 REMARK 3 S31: -0.0689 S32: 0.2283 S33: -0.0000 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 195 THROUGH 200 ) REMARK 3 ORIGIN FOR THE GROUP (A): -15.6218 17.6143 -65.7095 REMARK 3 T TENSOR REMARK 3 T11: 0.4028 T22: 0.5019 REMARK 3 T33: 0.2446 T12: -0.0604 REMARK 3 T13: 0.0753 T23: -0.0391 REMARK 3 L TENSOR REMARK 3 L11: 0.0357 L22: -0.0433 REMARK 3 L33: -0.0517 L12: 0.0076 REMARK 3 L13: 0.0612 L23: -0.0217 REMARK 3 S TENSOR REMARK 3 S11: -0.6143 S12: -0.7292 S13: -0.2783 REMARK 3 S21: 0.3475 S22: -0.3756 S23: -0.1024 REMARK 3 S31: 0.7634 S32: -0.9375 S33: -0.0000 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 226 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0618 17.8410 -68.0404 REMARK 3 T TENSOR REMARK 3 T11: 0.4301 T22: 0.4054 REMARK 3 T33: 0.5568 T12: 0.0064 REMARK 3 T13: 0.0238 T23: 0.0321 REMARK 3 L TENSOR REMARK 3 L11: 0.2429 L22: -0.1555 REMARK 3 L33: 0.1000 L12: -0.2631 REMARK 3 L13: 0.0946 L23: 0.0623 REMARK 3 S TENSOR REMARK 3 S11: -0.1204 S12: 0.2763 S13: -0.4136 REMARK 3 S21: -0.2797 S22: -0.2137 S23: 0.6029 REMARK 3 S31: -0.0506 S32: 0.4991 S33: -0.0000 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 255 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.2630 3.4815 -41.4619 REMARK 3 T TENSOR REMARK 3 T11: 0.1998 T22: 0.1881 REMARK 3 T33: 0.2175 T12: -0.0292 REMARK 3 T13: 0.0126 T23: -0.0029 REMARK 3 L TENSOR REMARK 3 L11: 0.5616 L22: -0.2587 REMARK 3 L33: -0.0686 L12: -0.2704 REMARK 3 L13: -0.1797 L23: -0.6650 REMARK 3 S TENSOR REMARK 3 S11: -0.2150 S12: 0.1290 S13: -0.1264 REMARK 3 S21: -0.0057 S22: -0.1593 S23: -0.2958 REMARK 3 S31: 0.1853 S32: -0.3010 S33: 0.0000 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 259 THROUGH 272 ) REMARK 3 ORIGIN FOR THE GROUP (A): -3.8063 5.2315 -33.0144 REMARK 3 T TENSOR REMARK 3 T11: 0.2014 T22: 0.2584 REMARK 3 T33: 0.4059 T12: 0.0582 REMARK 3 T13: -0.0332 T23: 0.1436 REMARK 3 L TENSOR REMARK 3 L11: 0.2028 L22: 0.3170 REMARK 3 L33: 0.0374 L12: -0.0616 REMARK 3 L13: -0.1986 L23: -0.0129 REMARK 3 S TENSOR REMARK 3 S11: -0.5155 S12: 0.2031 S13: -0.5786 REMARK 3 S21: 0.3436 S22: -0.1151 S23: -0.1466 REMARK 3 S31: 0.4243 S32: 0.8286 S33: -0.0000 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 285 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.5284 3.7386 -53.4429 REMARK 3 T TENSOR REMARK 3 T11: 0.2118 T22: 0.2743 REMARK 3 T33: 0.2895 T12: 0.0063 REMARK 3 T13: -0.0061 T23: 0.0691 REMARK 3 L TENSOR REMARK 3 L11: 0.0884 L22: -0.1118 REMARK 3 L33: -0.0213 L12: 0.1386 REMARK 3 L13: -0.1098 L23: 0.0406 REMARK 3 S TENSOR REMARK 3 S11: -0.1626 S12: -0.4494 S13: -0.0591 REMARK 3 S21: -0.5283 S22: 0.1492 S23: 0.4460 REMARK 3 S31: 0.5631 S32: 0.3669 S33: 0.0000 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 286 THROUGH 305 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.3439 5.6859 -64.0427 REMARK 3 T TENSOR REMARK 3 T11: 0.5292 T22: 0.5821 REMARK 3 T33: 0.4799 T12: -0.0093 REMARK 3 T13: 0.1010 T23: 0.0098 REMARK 3 L TENSOR REMARK 3 L11: 0.3388 L22: 0.1550 REMARK 3 L33: -0.1012 L12: -0.2389 REMARK 3 L13: 0.2737 L23: -0.1573 REMARK 3 S TENSOR REMARK 3 S11: -0.9174 S12: -0.3382 S13: -0.9611 REMARK 3 S21: -0.6808 S22: 0.2638 S23: -0.2431 REMARK 3 S31: 0.4405 S32: -0.3278 S33: -0.0000 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 331 ) REMARK 3 ORIGIN FOR THE GROUP (A): -14.0358 -7.5055 -41.5450 REMARK 3 T TENSOR REMARK 3 T11: 0.1797 T22: 0.1476 REMARK 3 T33: 0.2346 T12: 0.0105 REMARK 3 T13: 0.0215 T23: -0.0329 REMARK 3 L TENSOR REMARK 3 L11: 0.5454 L22: -0.3128 REMARK 3 L33: -0.1716 L12: -0.0440 REMARK 3 L13: 0.1060 L23: -0.6553 REMARK 3 S TENSOR REMARK 3 S11: 0.1588 S12: -0.0158 S13: 0.0868 REMARK 3 S21: 0.0816 S22: 0.0881 S23: -0.1502 REMARK 3 S31: 0.0028 S32: 0.0552 S33: 0.0000 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 343 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.4740 -3.7054 -22.4966 REMARK 3 T TENSOR REMARK 3 T11: 0.7380 T22: 0.2816 REMARK 3 T33: 0.3037 T12: 0.1509 REMARK 3 T13: 0.2224 T23: -0.0575 REMARK 3 L TENSOR REMARK 3 L11: 0.1718 L22: 0.1300 REMARK 3 L33: 0.0075 L12: -0.1734 REMARK 3 L13: -0.4448 L23: 0.0268 REMARK 3 S TENSOR REMARK 3 S11: -0.5714 S12: 0.5308 S13: 0.5773 REMARK 3 S21: 1.6473 S22: 0.4016 S23: 0.5192 REMARK 3 S31: -0.0181 S32: 0.0432 S33: 0.0000 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 344 THROUGH 364 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.0492 -0.8325 -41.4661 REMARK 3 T TENSOR REMARK 3 T11: 0.1928 T22: 0.2757 REMARK 3 T33: 0.1962 T12: -0.0105 REMARK 3 T13: -0.0105 T23: 0.0214 REMARK 3 L TENSOR REMARK 3 L11: -0.4899 L22: 0.1363 REMARK 3 L33: -0.2116 L12: -0.3403 REMARK 3 L13: -0.0490 L23: 0.5193 REMARK 3 S TENSOR REMARK 3 S11: 0.1042 S12: -0.0379 S13: -0.0677 REMARK 3 S21: -0.0854 S22: 0.0350 S23: 0.0406 REMARK 3 S31: -0.2164 S32: -0.3343 S33: 0.0000 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 365 THROUGH 372 ) REMARK 3 ORIGIN FOR THE GROUP (A): -16.7591 -5.5674 -62.4409 REMARK 3 T TENSOR REMARK 3 T11: 0.3666 T22: 0.4391 REMARK 3 T33: 0.3511 T12: -0.0488 REMARK 3 T13: -0.0126 T23: 0.0756 REMARK 3 L TENSOR REMARK 3 L11: 0.0836 L22: 0.1351 REMARK 3 L33: 0.0637 L12: 0.0280 REMARK 3 L13: 0.0357 L23: -0.1161 REMARK 3 S TENSOR REMARK 3 S11: -0.8327 S12: 0.6664 S13: 0.3147 REMARK 3 S21: -0.0129 S22: 0.4026 S23: -0.6611 REMARK 3 S31: -0.7324 S32: 0.7425 S33: -0.0000 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 378 THROUGH 387 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.1710 1.2353 -62.1255 REMARK 3 T TENSOR REMARK 3 T11: 0.3519 T22: 0.4481 REMARK 3 T33: 0.3802 T12: 0.0231 REMARK 3 T13: -0.0330 T23: -0.1347 REMARK 3 L TENSOR REMARK 3 L11: 0.0158 L22: 0.0526 REMARK 3 L33: 0.1596 L12: -0.2065 REMARK 3 L13: -0.0348 L23: -0.1502 REMARK 3 S TENSOR REMARK 3 S11: 0.1179 S12: 0.4590 S13: -0.1543 REMARK 3 S21: 0.5839 S22: -0.3358 S23: 0.7893 REMARK 3 S31: 0.6771 S32: 1.0471 S33: -0.0000 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 388 THROUGH 404 ) REMARK 3 ORIGIN FOR THE GROUP (A): -24.4604 9.6661 -43.1324 REMARK 3 T TENSOR REMARK 3 T11: 0.1644 T22: 0.1865 REMARK 3 T33: 0.2351 T12: 0.0163 REMARK 3 T13: -0.0143 T23: -0.0069 REMARK 3 L TENSOR REMARK 3 L11: -0.1995 L22: -0.2708 REMARK 3 L33: -0.0440 L12: -0.5495 REMARK 3 L13: 0.2346 L23: -0.2980 REMARK 3 S TENSOR REMARK 3 S11: 0.1157 S12: -0.0647 S13: 0.1907 REMARK 3 S21: 0.0787 S22: 0.1675 S23: 0.0418 REMARK 3 S31: 0.0641 S32: 0.0745 S33: -0.0000 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 405 THROUGH 418 ) REMARK 3 ORIGIN FOR THE GROUP (A): -28.4798 20.7096 -26.5461 REMARK 3 T TENSOR REMARK 3 T11: 0.5575 T22: 0.2296 REMARK 3 T33: -0.4902 T12: 0.1172 REMARK 3 T13: 0.1262 T23: -0.2685 REMARK 3 L TENSOR REMARK 3 L11: 0.1422 L22: 0.1446 REMARK 3 L33: -0.0956 L12: 0.2456 REMARK 3 L13: 0.2230 L23: 0.2060 REMARK 3 S TENSOR REMARK 3 S11: -0.2433 S12: -1.3458 S13: -2.2076 REMARK 3 S21: 0.0434 S22: 0.5030 S23: -0.8305 REMARK 3 S31: -0.5357 S32: 0.0100 S33: -0.0000 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1000 THROUGH 1018 ) REMARK 3 ORIGIN FOR THE GROUP (A): -2.1014 -7.1879 -13.5009 REMARK 3 T TENSOR REMARK 3 T11: 0.7137 T22: 0.7151 REMARK 3 T33: 0.5984 T12: -0.0266 REMARK 3 T13: -0.1454 T23: 0.1318 REMARK 3 L TENSOR REMARK 3 L11: -0.1311 L22: 0.0724 REMARK 3 L33: -0.2948 L12: -0.7273 REMARK 3 L13: -0.0877 L23: 0.3286 REMARK 3 S TENSOR REMARK 3 S11: -0.1271 S12: 0.2114 S13: 0.3025 REMARK 3 S21: 0.6224 S22: -0.2444 S23: -0.4119 REMARK 3 S31: 0.0034 S32: 0.1704 S33: -0.0000 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1022 THROUGH 1034 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.4454 -9.1852 -3.1713 REMARK 3 T TENSOR REMARK 3 T11: 1.0895 T22: 0.8254 REMARK 3 T33: 0.5435 T12: 0.2026 REMARK 3 T13: -0.2801 T23: 0.0169 REMARK 3 L TENSOR REMARK 3 L11: 0.0752 L22: 0.1197 REMARK 3 L33: 0.0476 L12: 0.0506 REMARK 3 L13: 0.0033 L23: -0.0114 REMARK 3 S TENSOR REMARK 3 S11: -0.8607 S12: 0.3438 S13: 0.0849 REMARK 3 S21: 1.1400 S22: 1.5557 S23: 0.1411 REMARK 3 S31: 0.8339 S32: -0.5054 S33: 0.0000 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1035 THROUGH 1048 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.4492 -17.4281 0.3288 REMARK 3 T TENSOR REMARK 3 T11: 1.2340 T22: 0.9484 REMARK 3 T33: 0.7129 T12: 0.0960 REMARK 3 T13: -0.1806 T23: 0.1015 REMARK 3 L TENSOR REMARK 3 L11: 0.1127 L22: -0.1470 REMARK 3 L33: 0.0446 L12: 0.0554 REMARK 3 L13: -0.1516 L23: 0.1657 REMARK 3 S TENSOR REMARK 3 S11: -0.8851 S12: -0.8303 S13: 0.0095 REMARK 3 S21: 0.6986 S22: 0.1886 S23: 0.1279 REMARK 3 S31: 0.4721 S32: -0.1933 S33: 0.0000 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1049 THROUGH 1057 ) REMARK 3 ORIGIN FOR THE GROUP (A): 2.8982 -22.8781 -7.5463 REMARK 3 T TENSOR REMARK 3 T11: 0.8825 T22: 0.8348 REMARK 3 T33: 0.7283 T12: 0.0877 REMARK 3 T13: 0.1096 T23: 0.2538 REMARK 3 L TENSOR REMARK 3 L11: -0.0030 L22: 0.0790 REMARK 3 L33: 0.0019 L12: -0.0197 REMARK 3 L13: -0.0333 L23: -0.0038 REMARK 3 S TENSOR REMARK 3 S11: -0.6145 S12: 0.2054 S13: 0.2372 REMARK 3 S21: 1.1426 S22: -0.5138 S23: -0.0106 REMARK 3 S31: 0.7834 S32: 0.1895 S33: -0.0000 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1058 THROUGH 1078 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.6013 -10.7938 -6.6293 REMARK 3 T TENSOR REMARK 3 T11: 1.0178 T22: 0.8983 REMARK 3 T33: 0.8150 T12: -0.1011 REMARK 3 T13: -0.0642 T23: 0.3280 REMARK 3 L TENSOR REMARK 3 L11: 0.7060 L22: 0.1327 REMARK 3 L33: 0.1449 L12: 0.0730 REMARK 3 L13: 0.6693 L23: -0.1820 REMARK 3 S TENSOR REMARK 3 S11: -0.8907 S12: -0.1100 S13: -1.2336 REMARK 3 S21: 0.2137 S22: -0.1837 S23: 1.5596 REMARK 3 S31: -0.3595 S32: 1.2032 S33: -0.0000 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1079 THROUGH 1090 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.1017 5.4733 -2.7434 REMARK 3 T TENSOR REMARK 3 T11: 1.2783 T22: 1.1301 REMARK 3 T33: 0.8988 T12: 0.2040 REMARK 3 T13: -0.0851 T23: 0.0650 REMARK 3 L TENSOR REMARK 3 L11: 0.0620 L22: 0.0090 REMARK 3 L33: -0.0309 L12: -0.1163 REMARK 3 L13: 0.0636 L23: -0.0341 REMARK 3 S TENSOR REMARK 3 S11: 1.0897 S12: 1.4810 S13: 0.4052 REMARK 3 S21: 0.5785 S22: -0.2345 S23: -0.0833 REMARK 3 S31: -0.2657 S32: -0.1818 S33: -0.0000 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1091 THROUGH 1104 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.7242 2.1946 -8.7191 REMARK 3 T TENSOR REMARK 3 T11: 1.0251 T22: 0.8304 REMARK 3 T33: 0.5110 T12: 0.0252 REMARK 3 T13: -0.0614 T23: 0.0872 REMARK 3 L TENSOR REMARK 3 L11: -0.0209 L22: 0.2720 REMARK 3 L33: -0.0113 L12: -0.0225 REMARK 3 L13: 0.1137 L23: 0.0892 REMARK 3 S TENSOR REMARK 3 S11: -0.1491 S12: -0.2727 S13: -0.4528 REMARK 3 S21: 0.7536 S22: -0.2681 S23: 0.2299 REMARK 3 S31: -0.7274 S32: 0.0593 S33: 0.0000 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1105 THROUGH 1122 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.4348 11.1604 -1.8133 REMARK 3 T TENSOR REMARK 3 T11: 1.4701 T22: 1.2234 REMARK 3 T33: 1.2026 T12: 0.2372 REMARK 3 T13: -0.0209 T23: -0.0102 REMARK 3 L TENSOR REMARK 3 L11: -0.0802 L22: 0.0095 REMARK 3 L33: 0.0034 L12: -0.1250 REMARK 3 L13: 0.0904 L23: 0.1574 REMARK 3 S TENSOR REMARK 3 S11: 0.3155 S12: -1.0154 S13: 0.2190 REMARK 3 S21: 0.8377 S22: -0.0952 S23: -0.0421 REMARK 3 S31: 0.5706 S32: -0.0604 S33: 0.0000 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1123 THROUGH 1139 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.5511 14.5094 -7.9817 REMARK 3 T TENSOR REMARK 3 T11: 1.4912 T22: 1.2901 REMARK 3 T33: 1.0375 T12: -0.0884 REMARK 3 T13: -0.1032 T23: 0.1595 REMARK 3 L TENSOR REMARK 3 L11: 0.1171 L22: 0.0867 REMARK 3 L33: 0.1881 L12: 0.1292 REMARK 3 L13: -0.2167 L23: 0.0734 REMARK 3 S TENSOR REMARK 3 S11: 1.1508 S12: -0.0378 S13: 0.0655 REMARK 3 S21: -0.0759 S22: -0.8865 S23: -0.1440 REMARK 3 S31: -1.1559 S32: 0.2682 S33: -0.0000 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1140 THROUGH 1152 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.4307 8.1906 -14.4428 REMARK 3 T TENSOR REMARK 3 T11: 1.0297 T22: 0.7448 REMARK 3 T33: 0.7020 T12: -0.0851 REMARK 3 T13: -0.0804 T23: 0.1096 REMARK 3 L TENSOR REMARK 3 L11: 0.0816 L22: -0.0285 REMARK 3 L33: 0.0935 L12: 0.2342 REMARK 3 L13: -0.2487 L23: 0.0915 REMARK 3 S TENSOR REMARK 3 S11: -0.5157 S12: -0.2709 S13: 1.1365 REMARK 3 S21: 1.1177 S22: -0.1484 S23: -1.1365 REMARK 3 S31: -1.2424 S32: 0.0747 S33: -0.0000 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1153 THROUGH 1159 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.9987 5.8869 -20.6738 REMARK 3 T TENSOR REMARK 3 T11: 1.3320 T22: 0.5681 REMARK 3 T33: 0.4332 T12: -0.1390 REMARK 3 T13: -0.0298 T23: 0.1304 REMARK 3 L TENSOR REMARK 3 L11: 0.0469 L22: 0.0273 REMARK 3 L33: -0.0564 L12: 0.0579 REMARK 3 L13: 0.0318 L23: -0.1141 REMARK 3 S TENSOR REMARK 3 S11: 0.1314 S12: 0.3986 S13: 0.4919 REMARK 3 S21: 0.1810 S22: -1.0881 S23: -0.0906 REMARK 3 S31: -1.2955 S32: -0.7699 S33: 0.0000 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 5EE7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-15. REMARK 100 THE DEPOSITION ID IS D_1000214768. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 - 6.5 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16065 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 32.730 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.15700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.76800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4L6R REMARK 200 REMARK 200 REMARK: OVAL SHAPED REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: ADA BUFFER, SODIUM POTASSIUM TARTRATE, REMARK 280 PEG 400, PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 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 18.79150 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.55400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.73800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.55400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.79150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.73800 REMARK 290 SMTRY3 4 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: 6420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 46.0 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 LYS A 136 REMARK 465 GLY A 137 REMARK 465 ARG A 201 REMARK 465 TYR A 202 REMARK 465 SER A 203 REMARK 465 GLN A 204 REMARK 465 LYS A 205 REMARK 465 ILE A 206 REMARK 465 GLU A 207 REMARK 465 ASP A 208 REMARK 465 ASP A 209 REMARK 465 LEU A 210 REMARK 465 SER A 211 REMARK 465 THR A 1019 REMARK 465 GLU A 1020 REMARK 465 GLY A 1021 REMARK 465 SER A 297 REMARK 465 ASN A 298 REMARK 465 ASP A 299 REMARK 465 ALA A 373 REMARK 465 GLN A 374 REMARK 465 GLY A 375 REMARK 465 THR A 376 REMARK 465 LEU A 377 REMARK 465 ALA A 419 REMARK 465 ALA A 420 REMARK 465 HIS A 421 REMARK 465 HIS A 422 REMARK 465 HIS A 423 REMARK 465 HIS A 424 REMARK 465 HIS A 425 REMARK 465 HIS A 426 REMARK 465 HIS A 427 REMARK 465 HIS A 428 REMARK 465 HIS A 429 REMARK 465 HIS A 430 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 ILE A1027 76.11 -106.32 REMARK 500 LEU A1031 -63.03 -102.65 REMARK 500 SER A1088 59.10 -92.45 REMARK 500 PHE A1112 46.21 -101.83 REMARK 500 GLU A 260 151.59 67.23 REMARK 500 GLN A 293 -111.15 53.68 REMARK 500 CYS A 294 28.08 -140.17 REMARK 500 CYS A 401 -64.13 -125.08 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 1202 REMARK 610 OLA A 1203 REMARK 610 OLA A 1204 REMARK 610 OLA A 1205 REMARK 610 OLA A 1206 REMARK 610 OLA A 1210 REMARK 610 OLA A 1211 REMARK 610 OLA A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 PE5 A 1216 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 5MV A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PE5 A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TLA A 1217 DBREF 5EE7 A 136 254 UNP P47871 GLR_HUMAN 136 254 DBREF 5EE7 A 255 1158 UNP P00720 ENLYS_BPT4 1 160 DBREF 5EE7 A 259 417 UNP P47871 GLR_HUMAN 259 417 SEQADV 5EE7 GLY A 137 UNP P47871 MET 137 ENGINEERED MUTATION SEQADV 5EE7 ALA A 154 UNP P47871 GLY 154 ENGINEERED MUTATION SEQADV 5EE7 ALA A 173 UNP P47871 ARG 173 ENGINEERED MUTATION SEQADV 5EE7 LEU A 182 UNP P47871 ALA 182 ENGINEERED MUTATION SEQADV 5EE7 ALA A 190 UNP P47871 SER 190 ENGINEERED MUTATION SEQADV 5EE7 PHE A 193 UNP P47871 VAL 193 ENGINEERED MUTATION SEQADV 5EE7 GLU A 207 UNP P47871 GLY 207 ENGINEERED MUTATION SEQADV 5EE7 ALA A 223 UNP P47871 GLY 223 ENGINEERED MUTATION SEQADV 5EE7 LEU A 255 UNP P00720 MET 1 LINKER SEQADV 5EE7 GLY A 1010 UNP P00720 ARG 12 ENGINEERED MUTATION SEQADV 5EE7 THR A 1052 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 5EE7 ALA A 1095 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 5EE7 ARG A 1135 UNP P00720 ILE 137 ENGINEERED MUTATION SEQADV 5EE7 TYR A 1159 UNP P00720 LINKER SEQADV 5EE7 ALA A 276 UNP P47871 MET 276 ENGINEERED MUTATION SEQADV 5EE7 ALA A 344 UNP P47871 LYS 344 ENGINEERED MUTATION SEQADV 5EE7 PHE A 362 UNP P47871 GLU 362 ENGINEERED MUTATION SEQADV 5EE7 ALA A 387 UNP P47871 PHE 387 ENGINEERED MUTATION SEQADV 5EE7 ALA A 418 UNP P47871 EXPRESSION TAG SEQADV 5EE7 ALA A 419 UNP P47871 EXPRESSION TAG SEQADV 5EE7 ALA A 420 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 421 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 422 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 423 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 424 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 425 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 426 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 427 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 428 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 429 UNP P47871 EXPRESSION TAG SEQADV 5EE7 HIS A 430 UNP P47871 EXPRESSION TAG SEQRES 1 A 452 LYS GLY TYR SER SER PHE GLN VAL MET TYR THR VAL GLY SEQRES 2 A 452 TYR SER LEU SER LEU ALA ALA LEU LEU LEU ALA LEU ALA SEQRES 3 A 452 ILE LEU GLY GLY LEU SER LYS LEU HIS CYS THR ALA ASN SEQRES 4 A 452 ALA ILE HIS ALA ASN LEU PHE LEU SER PHE VAL LEU LYS SEQRES 5 A 452 ALA SER ALA VAL LEU PHE ILE ASP GLY LEU LEU ARG THR SEQRES 6 A 452 ARG TYR SER GLN LYS ILE GLU ASP ASP LEU SER VAL SER SEQRES 7 A 452 THR TRP LEU SER ASP GLY ALA VAL ALA ALA CYS ARG VAL SEQRES 8 A 452 ALA ALA VAL PHE MET GLN TYR GLY ILE VAL ALA ASN TYR SEQRES 9 A 452 CYS TRP LEU LEU VAL GLU GLY LEU TYR LEU HIS ASN LEU SEQRES 10 A 452 LEU GLY LEU ASN ILE PHE GLU MET LEU ARG ILE ASP GLU SEQRES 11 A 452 GLY LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR SEQRES 12 A 452 TYR THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SEQRES 13 A 452 SER LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE SEQRES 14 A 452 GLY ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA SEQRES 15 A 452 GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG SEQRES 16 A 452 GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SEQRES 17 A 452 SER LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET SEQRES 18 A 452 VAL PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR SEQRES 19 A 452 ASN SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU SEQRES 20 A 452 ALA ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN SEQRES 21 A 452 THR PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG SEQRES 22 A 452 THR GLY THR TRP ASP ALA TYR PRO GLU ARG SER PHE PHE SEQRES 23 A 452 SER LEU TYR LEU GLY ILE GLY TRP GLY ALA PRO ALA LEU SEQRES 24 A 452 PHE VAL VAL PRO TRP ALA VAL VAL LYS CYS LEU PHE GLU SEQRES 25 A 452 ASN VAL GLN CYS TRP THR SER ASN ASP ASN MET GLY PHE SEQRES 26 A 452 TRP TRP ILE LEU ARG PHE PRO VAL PHE LEU ALA ILE LEU SEQRES 27 A 452 ILE ASN PHE PHE ILE PHE VAL ARG ILE VAL GLN LEU LEU SEQRES 28 A 452 VAL ALA LYS LEU ARG ALA ARG GLN MET HIS HIS THR ASP SEQRES 29 A 452 TYR ALA PHE ARG LEU ALA LYS SER THR LEU THR LEU ILE SEQRES 30 A 452 PRO LEU LEU GLY VAL HIS PHE VAL VAL PHE ALA PHE VAL SEQRES 31 A 452 THR ASP GLU HIS ALA GLN GLY THR LEU ARG SER ALA LYS SEQRES 32 A 452 LEU PHE PHE ASP LEU ALA LEU SER SER PHE GLN GLY LEU SEQRES 33 A 452 LEU VAL ALA VAL LEU TYR CYS PHE LEU ASN LYS GLU VAL SEQRES 34 A 452 GLN SER GLU LEU ARG ARG ARG TRP HIS ARG ALA ALA ALA SEQRES 35 A 452 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HET 5MV A1201 41 HET OLA A1202 10 HET OLA A1203 15 HET OLA A1204 15 HET OLA A1205 11 HET OLA A1206 11 HET OLA A1207 20 HET OLA A1208 20 HET OLA A1209 20 HET OLA A1210 17 HET OLA A1211 7 HET OLA A1212 11 HET OLA A1213 7 HET OLA A1214 14 HET OLA A1215 11 HET PE5 A1216 24 HET TLA A1217 10 HETNAM 5MV 3-[[4-[(1~{S})-1-[3-[3,5-BIS(CHLORANYL)PHENYL]-5-(6- HETNAM 2 5MV METHOXYNAPHTHALEN-2-YL)PYRAZOL-1- HETNAM 3 5MV YL]ETHYL]PHENYL]CARBONYLAMINO]PROPANOIC ACID HETNAM OLA OLEIC ACID HETNAM PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL HETNAM TLA L(+)-TARTARIC ACID HETSYN PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}- HETSYN 2 PE5 ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, POLYETHYLENE HETSYN 3 PE5 GLYCOL PEG400 FORMUL 2 5MV C32 H27 CL2 N3 O4 FORMUL 3 OLA 14(C18 H34 O2) FORMUL 17 PE5 C18 H38 O9 FORMUL 18 TLA C4 H6 O6 FORMUL 19 HOH *24(H2 O) HELIX 1 AA1 TYR A 138 LEU A 166 1 29 HELIX 2 AA2 SER A 167 HIS A 170 5 4 HELIX 3 AA3 CYS A 171 ARG A 199 1 29 HELIX 4 AA4 VAL A 212 LEU A 216 5 5 HELIX 5 AA5 SER A 217 GLY A 254 1 38 HELIX 6 AA6 ASN A 1000 GLY A 1010 1 11 HELIX 7 AA7 SER A 1036 GLY A 1049 1 14 HELIX 8 AA8 THR A 1057 ASN A 1079 1 23 HELIX 9 AA9 LEU A 1082 SER A 1088 1 7 HELIX 10 AB1 ASP A 1090 GLY A 1105 1 16 HELIX 11 AB2 GLY A 1105 GLY A 1111 1 7 HELIX 12 AB3 PHE A 1112 GLN A 1121 1 10 HELIX 13 AB4 ARG A 1123 SER A 1134 1 12 HELIX 14 AB5 SER A 1134 THR A 1140 1 7 HELIX 15 AB6 THR A 1140 GLY A 1154 1 15 HELIX 16 AB7 PHE A 263 TRP A 272 1 10 HELIX 17 AB8 TRP A 272 GLU A 290 1 19 HELIX 18 AB9 TRP A 304 ILE A 306 5 3 HELIX 19 AC1 LEU A 307 ALA A 335 1 29 HELIX 20 AC2 ASP A 342 ASP A 370 1 29 HELIX 21 AC3 SER A 379 SER A 390 1 12 HELIX 22 AC4 PHE A 391 CYS A 401 1 11 HELIX 23 AC5 ASN A 404 ALA A 418 1 15 SHEET 1 AA1 3 ARG A1012 TYR A1016 0 SHEET 2 AA1 3 TYR A1023 GLY A1026 -1 O GLY A1026 N ARG A1012 SHEET 3 AA1 3 HIS A1029 THR A1032 -1 O LEU A1031 N TYR A1023 SSBOND 1 CYS A 224 CYS A 294 1555 1555 2.02 CISPEP 1 TYR A 1159 PRO A 259 0 -3.33 SITE 1 AC1 18 GLY A 269 ILE A 270 GLY A 273 ALA A 274 SITE 2 AC1 18 LEU A 277 LEU A 329 PHE A 345 ARG A 346 SITE 3 AC1 18 LYS A 349 SER A 350 THR A 353 LEU A 399 SITE 4 AC1 18 ASN A 404 LYS A 405 OLA A1211 OLA A1212 SITE 5 AC1 18 OLA A1214 HOH A1313 SITE 1 AC2 2 LEU A 268 OLA A1214 SITE 1 AC3 2 PHE A 289 ALA A 380 SITE 1 AC4 4 HIS A 361 ASP A 385 LEU A 388 PHE A 391 SITE 1 AC5 8 THR A 146 SER A 150 PHE A 320 VAL A 323 SITE 2 AC5 8 ARG A 324 GLN A 327 OLA A1206 OLA A1209 SITE 1 AC6 3 ARG A 324 OLA A1205 HOH A1309 SITE 1 AC7 2 SER A 189 VAL A 326 SITE 1 AC8 4 CYS A 171 THR A 172 ASN A 179 PHE A 264 SITE 1 AC9 4 HIS A 250 ILE A 317 ARG A 324 OLA A1205 SITE 1 AD1 3 ASP A 218 ARG A 225 LYS A1058 SITE 1 AD2 2 5MV A1201 OLA A1212 SITE 1 AD3 4 PHE A 345 5MV A1201 OLA A1211 OLA A1213 SITE 1 AD4 3 LEU A 352 OLA A1212 OLA A1215 SITE 1 AD5 4 SER A 265 5MV A1201 OLA A1202 HOH A1301 SITE 1 AD6 3 LEU A 333 ARG A 334 OLA A1213 SITE 1 AD7 13 TYR A 145 TYR A 149 LYS A 187 ILE A 194 SITE 2 AD7 13 ARG A 199 ILE A 235 ASN A 238 TYR A 239 SITE 3 AD7 13 THR A 296 MET A 301 HIS A 361 PHE A 365 SITE 4 AD7 13 GLN A 392 SITE 1 AD8 7 ILE A 315 ASN A 318 PHE A 319 ILE A 355 SITE 2 AD8 7 PRO A 356 GLY A 359 VAL A 360 CRYST1 37.583 71.476 183.108 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.026608 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013991 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005461 0.00000 ATOM 1 N TYR A 138 -26.173 9.248 -69.199 1.00 50.95 N ANISOU 1 N TYR A 138 6449 6567 6343 -238 -116 -108 N ATOM 2 CA TYR A 138 -25.084 9.717 -68.352 1.00 49.20 C ANISOU 2 CA TYR A 138 6185 6335 6175 -173 -81 -133 C ATOM 3 C TYR A 138 -25.388 11.092 -67.765 1.00 51.43 C ANISOU 3 C TYR A 138 6427 6633 6479 -141 -115 -78 C ATOM 4 O TYR A 138 -24.844 11.464 -66.724 1.00 47.86 O ANISOU 4 O TYR A 138 5934 6173 6077 -81 -103 -83 O ATOM 5 CB TYR A 138 -23.772 9.766 -69.139 1.00 55.67 C ANISOU 5 CB TYR A 138 7030 7145 6978 -198 -15 -193 C ATOM 6 CG TYR A 138 -22.554 9.953 -68.263 1.00 58.88 C ANISOU 6 CG TYR A 138 7390 7531 7451 -132 23 -224 C ATOM 7 CD1 TYR A 138 -22.070 11.224 -67.968 1.00 56.53 C ANISOU 7 CD1 TYR A 138 7064 7246 7167 -105 20 -206 C ATOM 8 CD2 TYR A 138 -21.893 8.860 -67.723 1.00 51.54 C ANISOU 8 CD2 TYR A 138 6441 6565 6576 -99 60 -266 C ATOM 9 CE1 TYR A 138 -20.961 11.397 -67.159 1.00 55.51 C ANISOU 9 CE1 TYR A 138 6894 7098 7099 -50 48 -231 C ATOM 10 CE2 TYR A 138 -20.783 9.023 -66.917 1.00 60.29 C ANISOU 10 CE2 TYR A 138 7504 7653 7752 -44 84 -285 C ATOM 11 CZ TYR A 138 -20.321 10.293 -66.637 1.00 55.15 C ANISOU 11 CZ TYR A 138 6830 7017 7107 -21 76 -267 C ATOM 12 OH TYR A 138 -19.215 10.456 -65.834 1.00 50.25 O ANISOU 12 OH TYR A 138 6165 6376 6553 28 93 -282 O ATOM 13 N SER A 139 -26.254 11.843 -68.438 1.00 53.38 N ANISOU 13 N SER A 139 6687 6902 6693 -187 -157 -23 N ATOM 14 CA SER A 139 -26.632 13.170 -67.972 1.00 47.57 C ANISOU 14 CA SER A 139 5910 6177 5989 -164 -183 34 C ATOM 15 C SER A 139 -27.301 13.081 -66.602 1.00 49.14 C ANISOU 15 C SER A 139 6065 6357 6250 -106 -201 61 C ATOM 16 O SER A 139 -26.911 13.774 -65.651 1.00 51.43 O ANISOU 16 O SER A 139 6318 6642 6582 -57 -184 62 O ATOM 17 CB SER A 139 -27.565 13.839 -68.986 1.00 60.16 C ANISOU 17 CB SER A 139 7520 7790 7548 -230 -232 99 C ATOM 18 OG SER A 139 -27.978 15.122 -68.548 1.00 69.86 O ANISOU 18 OG SER A 139 8701 9022 8822 -208 -251 157 O ATOM 19 N SER A 140 -28.287 12.195 -66.502 1.00 49.15 N ANISOU 19 N SER A 140 6074 6346 6254 -115 -231 79 N ATOM 20 CA SER A 140 -29.005 11.985 -65.252 1.00 49.23 C ANISOU 20 CA SER A 140 6052 6333 6321 -67 -244 101 C ATOM 21 C SER A 140 -28.091 11.436 -64.165 1.00 36.80 C ANISOU 21 C SER A 140 4465 4745 4772 -10 -208 50 C ATOM 22 O SER A 140 -28.188 11.829 -63.001 1.00 36.87 O ANISOU 22 O SER A 140 4447 4741 4823 31 -204 63 O ATOM 23 CB SER A 140 -30.179 11.030 -65.472 1.00 49.45 C ANISOU 23 CB SER A 140 6094 6349 6345 -91 -281 125 C ATOM 24 OG SER A 140 -31.054 11.519 -66.471 1.00 56.05 O ANISOU 24 OG SER A 140 6939 7197 7162 -150 -326 183 O ATOM 25 N PHE A 141 -27.186 10.545 -64.562 1.00 37.94 N ANISOU 25 N PHE A 141 4633 4890 4894 -15 -180 -6 N ATOM 26 CA PHE A 141 -26.250 9.932 -63.627 1.00 36.17 C ANISOU 26 CA PHE A 141 4392 4647 4703 33 -152 -47 C ATOM 27 C PHE A 141 -25.295 10.981 -63.074 1.00 37.75 C ANISOU 27 C PHE A 141 4567 4854 4924 61 -133 -53 C ATOM 28 O PHE A 141 -24.990 11.002 -61.872 1.00 34.88 O ANISOU 28 O PHE A 141 4180 4479 4595 102 -133 -53 O ATOM 29 CB PHE A 141 -25.477 8.803 -64.321 1.00 33.01 C ANISOU 29 CB PHE A 141 4015 4238 4290 15 -118 -103 C ATOM 30 CG PHE A 141 -24.313 8.279 -63.530 1.00 35.32 C ANISOU 30 CG PHE A 141 4282 4508 4629 58 -89 -140 C ATOM 31 CD1 PHE A 141 -24.513 7.569 -62.357 1.00 40.71 C ANISOU 31 CD1 PHE A 141 4943 5173 5352 99 -105 -132 C ATOM 32 CD2 PHE A 141 -23.016 8.479 -63.971 1.00 39.44 C ANISOU 32 CD2 PHE A 141 4800 5024 5162 55 -47 -179 C ATOM 33 CE1 PHE A 141 -23.437 7.081 -61.630 1.00 38.14 C ANISOU 33 CE1 PHE A 141 4590 4825 5075 133 -88 -156 C ATOM 34 CE2 PHE A 141 -21.939 7.992 -63.251 1.00 42.09 C ANISOU 34 CE2 PHE A 141 5104 5333 5555 93 -25 -205 C ATOM 35 CZ PHE A 141 -22.152 7.290 -62.078 1.00 37.80 C ANISOU 35 CZ PHE A 141 4537 4775 5051 130 -50 -189 C ATOM 36 N GLN A 142 -24.865 11.881 -63.953 1.00 37.62 N ANISOU 36 N GLN A 142 4557 4855 4881 34 -120 -55 N ATOM 37 CA GLN A 142 -23.956 12.942 -63.558 1.00 38.20 C ANISOU 37 CA GLN A 142 4607 4935 4973 58 -100 -61 C ATOM 38 C GLN A 142 -24.650 13.896 -62.601 1.00 39.32 C ANISOU 38 C GLN A 142 4723 5079 5140 78 -118 -16 C ATOM 39 O GLN A 142 -24.064 14.319 -61.596 1.00 36.54 O ANISOU 39 O GLN A 142 4349 4721 4814 110 -106 -24 O ATOM 40 CB GLN A 142 -23.437 13.697 -64.782 1.00 41.55 C ANISOU 40 CB GLN A 142 5047 5377 5362 21 -79 -71 C ATOM 41 CG GLN A 142 -22.367 14.723 -64.449 1.00 53.62 C ANISOU 41 CG GLN A 142 6551 6910 6912 47 -53 -85 C ATOM 42 CD GLN A 142 -21.864 15.467 -65.667 1.00 59.92 C ANISOU 42 CD GLN A 142 7367 7724 7676 11 -29 -96 C ATOM 43 OE1 GLN A 142 -22.370 15.287 -66.775 1.00 64.02 O ANISOU 43 OE1 GLN A 142 7923 8254 8150 -40 -37 -87 O ATOM 44 NE2 GLN A 142 -20.860 16.313 -65.467 1.00 56.14 N ANISOU 44 NE2 GLN A 142 6866 7246 7217 34 -1 -114 N ATOM 45 N VAL A 143 -25.910 14.207 -62.891 1.00 33.67 N ANISOU 45 N VAL A 143 4007 4365 4420 55 -144 32 N ATOM 46 CA VAL A 143 -26.665 15.086 -62.010 1.00 31.93 C ANISOU 46 CA VAL A 143 3760 4134 4238 69 -148 75 C ATOM 47 C VAL A 143 -26.819 14.442 -60.637 1.00 31.09 C ANISOU 47 C VAL A 143 3650 4004 4159 103 -147 65 C ATOM 48 O VAL A 143 -26.653 15.097 -59.597 1.00 30.46 O ANISOU 48 O VAL A 143 3555 3915 4102 122 -130 69 O ATOM 49 CB VAL A 143 -28.067 15.406 -62.586 1.00 34.17 C ANISOU 49 CB VAL A 143 4038 4413 4533 36 -178 136 C ATOM 50 CG1 VAL A 143 -28.950 16.051 -61.529 1.00 25.36 C ANISOU 50 CG1 VAL A 143 2892 3269 3475 53 -171 176 C ATOM 51 CG2 VAL A 143 -27.952 16.299 -63.811 1.00 39.22 C ANISOU 51 CG2 VAL A 143 4678 5076 5149 -3 -185 159 C ATOM 52 N MET A 144 -27.084 13.140 -60.634 1.00 31.83 N ANISOU 52 N MET A 144 3762 4088 4245 106 -163 51 N ATOM 53 CA MET A 144 -27.356 12.452 -59.384 1.00 31.71 C ANISOU 53 CA MET A 144 3746 4049 4253 134 -166 48 C ATOM 54 C MET A 144 -26.118 12.346 -58.504 1.00 31.79 C ANISOU 54 C MET A 144 3752 4059 4268 160 -152 15 C ATOM 55 O MET A 144 -26.191 12.618 -57.302 1.00 34.75 O ANISOU 55 O MET A 144 4124 4421 4659 173 -149 23 O ATOM 56 CB MET A 144 -27.933 11.064 -59.649 1.00 45.13 C ANISOU 56 CB MET A 144 5463 5738 5947 131 -185 42 C ATOM 57 CG MET A 144 -29.330 10.876 -59.079 1.00 50.50 C ANISOU 57 CG MET A 144 6141 6391 6654 133 -200 79 C ATOM 58 SD MET A 144 -30.051 9.304 -59.566 1.00107.83 S ANISOU 58 SD MET A 144 13422 13643 13907 126 -223 73 S ATOM 59 CE MET A 144 -29.975 9.462 -61.344 1.00 61.62 C ANISOU 59 CE MET A 144 7584 7819 8010 76 -235 73 C ATOM 60 N TYR A 145 -24.975 11.965 -59.072 1.00 26.70 N ANISOU 60 N TYR A 145 3107 3425 3614 163 -144 -21 N ATOM 61 CA TYR A 145 -23.793 11.898 -58.217 1.00 35.59 C ANISOU 61 CA TYR A 145 4219 4545 4757 185 -139 -43 C ATOM 62 C TYR A 145 -23.263 13.294 -57.875 1.00 27.02 C ANISOU 62 C TYR A 145 3122 3473 3672 185 -125 -37 C ATOM 63 O TYR A 145 -22.577 13.458 -56.864 1.00 25.02 O ANISOU 63 O TYR A 145 2860 3214 3431 197 -128 -42 O ATOM 64 CB TYR A 145 -22.686 11.007 -58.823 1.00 30.81 C ANISOU 64 CB TYR A 145 3608 3933 4163 190 -128 -81 C ATOM 65 CG TYR A 145 -21.911 11.523 -60.024 1.00 36.69 C ANISOU 65 CG TYR A 145 4354 4691 4898 173 -99 -106 C ATOM 66 CD1 TYR A 145 -21.065 12.625 -59.928 1.00 34.01 C ANISOU 66 CD1 TYR A 145 3998 4361 4564 179 -85 -111 C ATOM 67 CD2 TYR A 145 -21.965 10.850 -61.239 1.00 38.65 C ANISOU 67 CD2 TYR A 145 4621 4936 5129 148 -81 -129 C ATOM 68 CE1 TYR A 145 -20.346 13.073 -61.018 1.00 37.63 C ANISOU 68 CE1 TYR A 145 4459 4827 5014 164 -55 -135 C ATOM 69 CE2 TYR A 145 -21.247 11.287 -62.332 1.00 37.11 C ANISOU 69 CE2 TYR A 145 4434 4747 4918 126 -48 -155 C ATOM 70 CZ TYR A 145 -20.440 12.399 -62.217 1.00 42.14 C ANISOU 70 CZ TYR A 145 5053 5393 5564 136 -35 -158 C ATOM 71 OH TYR A 145 -19.723 12.833 -63.306 1.00 41.63 O ANISOU 71 OH TYR A 145 5000 5332 5487 114 1 -186 O ATOM 72 N THR A 146 -23.582 14.298 -58.691 1.00 29.13 N ANISOU 72 N THR A 146 3386 3756 3927 168 -111 -25 N ATOM 73 CA THR A 146 -23.189 15.662 -58.338 1.00 26.23 C ANISOU 73 CA THR A 146 3003 3398 3564 168 -91 -18 C ATOM 74 C THR A 146 -23.946 16.097 -57.090 1.00 27.60 C ANISOU 74 C THR A 146 3178 3556 3752 168 -89 6 C ATOM 75 O THR A 146 -23.346 16.580 -56.122 1.00 28.14 O ANISOU 75 O THR A 146 3245 3623 3824 171 -80 -2 O ATOM 76 CB THR A 146 -23.459 16.668 -59.469 1.00 32.61 C ANISOU 76 CB THR A 146 3803 4223 4362 147 -77 -3 C ATOM 77 OG1 THR A 146 -22.688 16.314 -60.623 1.00 30.29 O ANISOU 77 OG1 THR A 146 3519 3942 4050 139 -71 -31 O ATOM 78 CG2 THR A 146 -23.078 18.077 -59.022 1.00 29.62 C ANISOU 78 CG2 THR A 146 3405 3853 3997 150 -51 3 C ATOM 79 N VAL A 147 -25.261 15.881 -57.099 1.00 26.66 N ANISOU 79 N VAL A 147 3065 3422 3642 159 -94 35 N ATOM 80 CA VAL A 147 -26.075 16.206 -55.932 1.00 26.22 C ANISOU 80 CA VAL A 147 3015 3340 3606 154 -80 56 C ATOM 81 C VAL A 147 -25.638 15.384 -54.725 1.00 23.89 C ANISOU 81 C VAL A 147 2742 3034 3302 164 -93 37 C ATOM 82 O VAL A 147 -25.568 15.892 -53.601 1.00 29.40 O ANISOU 82 O VAL A 147 3451 3720 3999 153 -75 37 O ATOM 83 CB VAL A 147 -27.576 15.952 -56.198 1.00 26.32 C ANISOU 83 CB VAL A 147 3027 3330 3644 144 -85 92 C ATOM 84 CG1 VAL A 147 -28.376 16.022 -54.906 1.00 25.98 C ANISOU 84 CG1 VAL A 147 2996 3248 3626 140 -62 104 C ATOM 85 CG2 VAL A 147 -28.121 16.935 -57.225 1.00 25.55 C ANISOU 85 CG2 VAL A 147 2904 3237 3566 126 -77 126 C ATOM 86 N GLY A 148 -25.279 14.128 -54.968 1.00 27.48 N ANISOU 86 N GLY A 148 3202 3491 3748 178 -122 22 N ATOM 87 CA GLY A 148 -24.889 13.244 -53.884 1.00 27.78 C ANISOU 87 CA GLY A 148 3255 3517 3783 186 -142 13 C ATOM 88 C GLY A 148 -23.594 13.651 -53.200 1.00 26.78 C ANISOU 88 C GLY A 148 3124 3400 3650 184 -148 0 C ATOM 89 O GLY A 148 -23.526 13.729 -51.971 1.00 24.41 O ANISOU 89 O GLY A 148 2845 3090 3341 170 -154 6 O ATOM 90 N TYR A 149 -22.564 13.925 -53.990 1.00 22.61 N ANISOU 90 N TYR A 149 2574 2891 3127 192 -146 -18 N ATOM 91 CA TYR A 149 -21.286 14.330 -53.418 1.00 25.42 C ANISOU 91 CA TYR A 149 2919 3253 3486 191 -156 -28 C ATOM 92 C TYR A 149 -21.304 15.739 -52.834 1.00 30.10 C ANISOU 92 C TYR A 149 3518 3853 4064 170 -130 -24 C ATOM 93 O TYR A 149 -20.647 15.992 -51.822 1.00 27.77 O ANISOU 93 O TYR A 149 3233 3557 3761 155 -144 -23 O ATOM 94 CB TYR A 149 -20.173 14.210 -54.458 1.00 22.69 C ANISOU 94 CB TYR A 149 2545 2915 3162 206 -152 -51 C ATOM 95 CG TYR A 149 -19.741 12.781 -54.677 1.00 26.28 C ANISOU 95 CG TYR A 149 2988 3352 3644 221 -173 -60 C ATOM 96 CD1 TYR A 149 -19.155 12.052 -53.651 1.00 24.48 C ANISOU 96 CD1 TYR A 149 2754 3108 3438 224 -210 -48 C ATOM 97 CD2 TYR A 149 -19.932 12.154 -55.899 1.00 29.12 C ANISOU 97 CD2 TYR A 149 3345 3709 4009 227 -155 -77 C ATOM 98 CE1 TYR A 149 -18.767 10.743 -53.836 1.00 28.18 C ANISOU 98 CE1 TYR A 149 3204 3555 3946 239 -224 -52 C ATOM 99 CE2 TYR A 149 -19.545 10.843 -56.097 1.00 32.18 C ANISOU 99 CE2 TYR A 149 3721 4075 4430 238 -163 -89 C ATOM 100 CZ TYR A 149 -18.963 10.143 -55.061 1.00 32.97 C ANISOU 100 CZ TYR A 149 3806 4156 4565 247 -195 -75 C ATOM 101 OH TYR A 149 -18.576 8.837 -55.247 1.00 37.96 O ANISOU 101 OH TYR A 149 4418 4761 5244 258 -198 -82 O ATOM 102 N SER A 150 -22.043 16.659 -53.453 1.00 25.74 N ANISOU 102 N SER A 150 2961 3306 3512 164 -94 -18 N ATOM 103 CA SER A 150 -22.098 18.013 -52.900 1.00 24.91 C ANISOU 103 CA SER A 150 2859 3203 3403 143 -59 -14 C ATOM 104 C SER A 150 -22.883 18.032 -51.585 1.00 28.26 C ANISOU 104 C SER A 150 3317 3603 3817 117 -46 -3 C ATOM 105 O SER A 150 -22.483 18.689 -50.615 1.00 27.47 O ANISOU 105 O SER A 150 3235 3501 3702 90 -32 -9 O ATOM 106 CB SER A 150 -22.710 18.988 -53.904 1.00 25.28 C ANISOU 106 CB SER A 150 2884 3257 3466 143 -23 -3 C ATOM 107 OG SER A 150 -24.076 18.694 -54.130 1.00 42.31 O ANISOU 107 OG SER A 150 5045 5394 5637 139 -17 22 O ATOM 108 N LEU A 151 -23.988 17.290 -51.549 1.00 29.71 N ANISOU 108 N LEU A 151 3514 3765 4009 120 -50 12 N ATOM 109 CA LEU A 151 -24.791 17.191 -50.333 1.00 30.99 C ANISOU 109 CA LEU A 151 3713 3896 4165 93 -32 20 C ATOM 110 C LEU A 151 -24.019 16.469 -49.232 1.00 29.60 C ANISOU 110 C LEU A 151 3569 3722 3957 79 -71 13 C ATOM 111 O LEU A 151 -24.081 16.850 -48.050 1.00 26.48 O ANISOU 111 O LEU A 151 3212 3311 3536 40 -53 12 O ATOM 112 CB LEU A 151 -26.106 16.465 -50.623 1.00 28.89 C ANISOU 112 CB LEU A 151 3451 3605 3922 104 -30 39 C ATOM 113 CG LEU A 151 -27.296 16.682 -49.695 1.00 37.10 C ANISOU 113 CG LEU A 151 4519 4600 4978 77 14 50 C ATOM 114 CD1 LEU A 151 -27.549 18.169 -49.499 1.00 32.08 C ANISOU 114 CD1 LEU A 151 3875 3949 4366 50 79 52 C ATOM 115 CD2 LEU A 151 -28.523 16.002 -50.279 1.00 40.42 C ANISOU 115 CD2 LEU A 151 4928 4996 5434 95 10 72 C ATOM 116 N SER A 152 -23.277 15.438 -49.632 1.00 24.11 N ANISOU 116 N SER A 152 2857 3041 3263 106 -122 11 N ATOM 117 CA SER A 152 -22.452 14.695 -48.691 1.00 23.32 C ANISOU 117 CA SER A 152 2774 2940 3145 94 -171 15 C ATOM 118 C SER A 152 -21.395 15.615 -48.116 1.00 25.81 C ANISOU 118 C SER A 152 3093 3271 3442 66 -175 9 C ATOM 119 O SER A 152 -21.146 15.606 -46.917 1.00 24.52 O ANISOU 119 O SER A 152 2968 3102 3248 26 -194 18 O ATOM 120 CB SER A 152 -21.785 13.491 -49.363 1.00 26.10 C ANISOU 120 CB SER A 152 3093 3298 3524 130 -216 15 C ATOM 121 OG SER A 152 -22.743 12.615 -49.934 1.00 27.32 O ANISOU 121 OG SER A 152 3246 3440 3693 152 -211 18 O ATOM 122 N LEU A 153 -20.809 16.443 -48.973 1.00 22.54 N ANISOU 122 N LEU A 153 2644 2876 3044 82 -156 -4 N ATOM 123 CA LEU A 153 -19.748 17.348 -48.549 1.00 26.86 C ANISOU 123 CA LEU A 153 3188 3438 3579 59 -159 -12 C ATOM 124 C LEU A 153 -20.271 18.396 -47.582 1.00 23.19 C ANISOU 124 C LEU A 153 2765 2965 3081 9 -114 -15 C ATOM 125 O LEU A 153 -19.626 18.700 -46.574 1.00 30.61 O ANISOU 125 O LEU A 153 3733 3908 3989 -33 -132 -14 O ATOM 126 CB LEU A 153 -19.112 18.029 -49.763 1.00 25.00 C ANISOU 126 CB LEU A 153 2907 3221 3372 89 -138 -28 C ATOM 127 CG LEU A 153 -17.926 18.953 -49.491 1.00 28.97 C ANISOU 127 CG LEU A 153 3397 3739 3872 74 -141 -38 C ATOM 128 CD1 LEU A 153 -16.828 18.212 -48.749 1.00 29.63 C ANISOU 128 CD1 LEU A 153 3479 3819 3961 63 -209 -25 C ATOM 129 CD2 LEU A 153 -17.402 19.530 -50.798 1.00 30.01 C ANISOU 129 CD2 LEU A 153 3485 3885 4034 108 -115 -56 C ATOM 130 N ALA A 154 -21.456 18.924 -47.868 1.00 23.27 N ANISOU 130 N ALA A 154 2780 2960 3102 9 -54 -17 N ATOM 131 CA ALA A 154 -22.048 19.913 -46.976 1.00 28.60 C ANISOU 131 CA ALA A 154 3491 3615 3759 -41 7 -24 C ATOM 132 C ALA A 154 -22.316 19.289 -45.613 1.00 27.37 C ANISOU 132 C ALA A 154 3399 3439 3562 -88 -9 -18 C ATOM 133 O ALA A 154 -21.956 19.857 -44.574 1.00 26.37 O ANISOU 133 O ALA A 154 3316 3309 3394 -146 4 -26 O ATOM 134 CB ALA A 154 -23.337 20.477 -47.572 1.00 22.19 C ANISOU 134 CB ALA A 154 2662 2780 2988 -31 74 -18 C ATOM 135 N ALA A 155 -22.914 18.099 -45.625 1.00 29.61 N ANISOU 135 N ALA A 155 3691 3708 3851 -68 -39 -4 N ATOM 136 CA ALA A 155 -23.251 17.420 -44.379 1.00 31.64 C ANISOU 136 CA ALA A 155 4010 3943 4070 -111 -54 4 C ATOM 137 C ALA A 155 -22.006 17.058 -43.571 1.00 33.16 C ANISOU 137 C ALA A 155 4224 4155 4219 -144 -126 15 C ATOM 138 O ALA A 155 -22.018 17.109 -42.338 1.00 32.16 O ANISOU 138 O ALA A 155 4162 4017 4041 -210 -129 18 O ATOM 139 CB ALA A 155 -24.068 16.175 -44.668 1.00 29.24 C ANISOU 139 CB ALA A 155 3701 3621 3787 -75 -75 18 C ATOM 140 N LEU A 156 -20.927 16.715 -44.270 1.00 30.03 N ANISOU 140 N LEU A 156 3775 3787 3848 -104 -184 22 N ATOM 141 CA LEU A 156 -19.694 16.307 -43.607 1.00 31.42 C ANISOU 141 CA LEU A 156 3956 3977 4005 -130 -262 42 C ATOM 142 C LEU A 156 -18.968 17.497 -42.998 1.00 30.24 C ANISOU 142 C LEU A 156 3829 3841 3819 -185 -251 33 C ATOM 143 O LEU A 156 -18.428 17.397 -41.897 1.00 30.81 O ANISOU 143 O LEU A 156 3945 3915 3846 -246 -298 51 O ATOM 144 CB LEU A 156 -18.769 15.574 -44.583 1.00 27.00 C ANISOU 144 CB LEU A 156 3326 3430 3503 -70 -315 52 C ATOM 145 CG LEU A 156 -19.212 14.178 -45.026 1.00 30.18 C ANISOU 145 CG LEU A 156 3708 3819 3940 -25 -341 65 C ATOM 146 CD1 LEU A 156 -18.482 13.792 -46.296 1.00 28.67 C ANISOU 146 CD1 LEU A 156 3447 3636 3811 33 -353 58 C ATOM 147 CD2 LEU A 156 -18.993 13.137 -43.935 1.00 33.05 C ANISOU 147 CD2 LEU A 156 4100 4170 4286 -57 -408 100 C ATOM 148 N LEU A 157 -18.940 18.618 -43.714 1.00 30.79 N ANISOU 148 N LEU A 157 3869 3921 3908 -167 -193 7 N ATOM 149 CA LEU A 157 -18.349 19.827 -43.150 1.00 33.20 C ANISOU 149 CA LEU A 157 4197 4238 4181 -220 -169 -7 C ATOM 150 C LEU A 157 -19.162 20.308 -41.951 1.00 32.48 C ANISOU 150 C LEU A 157 4187 4124 4031 -299 -115 -18 C ATOM 151 O LEU A 157 -18.601 20.775 -40.955 1.00 34.04 O ANISOU 151 O LEU A 157 4433 4326 4174 -373 -129 -19 O ATOM 152 CB LEU A 157 -18.254 20.934 -44.204 1.00 30.24 C ANISOU 152 CB LEU A 157 3770 3875 3844 -181 -109 -32 C ATOM 153 CG LEU A 157 -17.307 20.697 -45.384 1.00 29.62 C ANISOU 153 CG LEU A 157 3619 3817 3818 -115 -148 -30 C ATOM 154 CD1 LEU A 157 -17.351 21.873 -46.345 1.00 26.18 C ANISOU 154 CD1 LEU A 157 3144 3392 3410 -87 -82 -54 C ATOM 155 CD2 LEU A 157 -15.885 20.447 -44.899 1.00 34.03 C ANISOU 155 CD2 LEU A 157 4168 4388 4374 -134 -226 -14 C ATOM 156 N LEU A 158 -20.481 20.153 -42.034 1.00 31.63 N ANISOU 156 N LEU A 158 4096 3986 3935 -290 -54 -26 N ATOM 157 CA LEU A 158 -21.346 20.545 -40.929 1.00 30.63 C ANISOU 157 CA LEU A 158 4048 3825 3764 -366 12 -40 C ATOM 158 C LEU A 158 -21.082 19.674 -39.710 1.00 37.21 C ANISOU 158 C LEU A 158 4952 4655 4532 -428 -54 -19 C ATOM 159 O LEU A 158 -20.970 20.172 -38.584 1.00 38.60 O ANISOU 159 O LEU A 158 5203 4821 4641 -519 -34 -29 O ATOM 160 CB LEU A 158 -22.816 20.447 -41.338 1.00 37.47 C ANISOU 160 CB LEU A 158 4908 4652 4677 -336 87 -46 C ATOM 161 CG LEU A 158 -23.862 20.663 -40.241 1.00 45.70 C ANISOU 161 CG LEU A 158 6029 5643 5691 -409 166 -61 C ATOM 162 CD1 LEU A 158 -23.759 22.064 -39.658 1.00 36.75 C ANISOU 162 CD1 LEU A 158 4931 4497 4536 -480 252 -92 C ATOM 163 CD2 LEU A 158 -25.259 20.402 -40.783 1.00 39.88 C ANISOU 163 CD2 LEU A 158 5268 4863 5020 -366 225 -58 C ATOM 164 N ALA A 159 -20.963 18.371 -39.950 1.00 36.77 N ANISOU 164 N ALA A 159 4873 4605 4494 -383 -132 11 N ATOM 165 CA ALA A 159 -20.707 17.412 -38.887 1.00 30.49 C ANISOU 165 CA ALA A 159 4133 3806 3645 -434 -206 41 C ATOM 166 C ALA A 159 -19.342 17.638 -38.253 1.00 35.33 C ANISOU 166 C ALA A 159 4761 4448 4217 -490 -284 62 C ATOM 167 O ALA A 159 -19.174 17.488 -37.042 1.00 34.65 O ANISOU 167 O ALA A 159 4751 4356 4057 -578 -319 79 O ATOM 168 CB ALA A 159 -20.811 15.997 -39.428 1.00 33.02 C ANISOU 168 CB ALA A 159 4410 4126 4012 -365 -269 69 C ATOM 169 N LEU A 160 -18.370 18.014 -39.079 1.00 36.61 N ANISOU 169 N LEU A 160 4849 4637 4424 -442 -313 63 N ATOM 170 CA LEU A 160 -17.029 18.298 -38.588 1.00 39.21 C ANISOU 170 CA LEU A 160 5178 4990 4730 -489 -388 85 C ATOM 171 C LEU A 160 -17.032 19.545 -37.721 1.00 42.42 C ANISOU 171 C LEU A 160 5657 5398 5064 -583 -334 58 C ATOM 172 O LEU A 160 -16.356 19.598 -36.689 1.00 43.66 O ANISOU 172 O LEU A 160 5869 5564 5157 -671 -394 81 O ATOM 173 CB LEU A 160 -16.052 18.469 -39.749 1.00 30.24 C ANISOU 173 CB LEU A 160 3945 3875 3671 -412 -415 86 C ATOM 174 CG LEU A 160 -15.530 17.181 -40.380 1.00 31.68 C ANISOU 174 CG LEU A 160 4058 4056 3924 -344 -494 122 C ATOM 175 CD1 LEU A 160 -14.740 17.489 -41.640 1.00 34.21 C ANISOU 175 CD1 LEU A 160 4289 4387 4321 -270 -488 108 C ATOM 176 CD2 LEU A 160 -14.678 16.422 -39.381 1.00 26.97 C ANISOU 176 CD2 LEU A 160 3480 3458 3310 -399 -606 178 C ATOM 177 N ALA A 161 -17.806 20.544 -38.140 1.00 31.41 N ANISOU 177 N ALA A 161 4601 4538 2796 -746 -467 122 N ATOM 178 CA ALA A 161 -17.937 21.769 -37.361 1.00 38.09 C ANISOU 178 CA ALA A 161 5819 5232 3424 -811 -524 256 C ATOM 179 C ALA A 161 -18.631 21.484 -36.039 1.00 36.38 C ANISOU 179 C ALA A 161 5740 4690 3394 -482 -348 387 C ATOM 180 O ALA A 161 -18.333 22.112 -35.024 1.00 42.15 O ANISOU 180 O ALA A 161 6716 5370 3929 -466 -355 490 O ATOM 181 CB ALA A 161 -18.695 22.828 -38.148 1.00 37.02 C ANISOU 181 CB ALA A 161 5863 4955 3248 -1008 -643 279 C ATOM 182 N ILE A 162 -19.548 20.524 -36.050 1.00 39.94 N ANISOU 182 N ILE A 162 6030 4922 4225 -216 -189 382 N ATOM 183 CA ILE A 162 -20.258 20.167 -34.830 1.00 37.15 C ANISOU 183 CA ILE A 162 5788 4252 4077 113 -11 502 C ATOM 184 C ILE A 162 -19.350 19.431 -33.853 1.00 41.20 C ANISOU 184 C ILE A 162 6207 4915 4531 268 78 504 C ATOM 185 O ILE A 162 -19.267 19.805 -32.684 1.00 44.93 O ANISOU 185 O ILE A 162 6902 5270 4900 374 125 618 O ATOM 186 CB ILE A 162 -21.492 19.299 -35.122 1.00 39.49 C ANISOU 186 CB ILE A 162 5925 4273 4806 360 137 494 C ATOM 187 CG1 ILE A 162 -22.561 20.127 -35.830 1.00 33.92 C ANISOU 187 CG1 ILE A 162 5375 3340 4173 250 68 527 C ATOM 188 CG2 ILE A 162 -22.059 18.721 -33.831 1.00 44.16 C ANISOU 188 CG2 ILE A 162 6579 4584 5617 717 335 603 C ATOM 189 CD1 ILE A 162 -23.865 19.378 -36.046 1.00 37.88 C ANISOU 189 CD1 ILE A 162 5757 3535 5101 498 214 535 C ATOM 190 N LEU A 163 -18.657 18.401 -34.332 1.00 41.00 N ANISOU 190 N LEU A 163 5857 5154 4566 276 100 377 N ATOM 191 CA LEU A 163 -17.776 17.629 -33.464 1.00 40.44 C ANISOU 191 CA LEU A 163 5674 5239 4452 423 187 369 C ATOM 192 C LEU A 163 -16.616 18.471 -32.946 1.00 45.46 C ANISOU 192 C LEU A 163 6494 6104 4675 224 62 399 C ATOM 193 O LEU A 163 -16.201 18.326 -31.797 1.00 50.94 O ANISOU 193 O LEU A 163 7275 6782 5298 370 136 468 O ATOM 194 CB LEU A 163 -17.220 16.404 -34.200 1.00 38.76 C ANISOU 194 CB LEU A 163 5070 5288 4369 442 217 217 C ATOM 195 CG LEU A 163 -18.174 15.283 -34.620 1.00 37.56 C ANISOU 195 CG LEU A 163 4674 4957 4641 676 362 172 C ATOM 196 CD1 LEU A 163 -17.378 14.119 -35.190 1.00 30.63 C ANISOU 196 CD1 LEU A 163 3425 4384 3828 681 382 25 C ATOM 197 CD2 LEU A 163 -19.038 14.834 -33.449 1.00 39.01 C ANISOU 197 CD2 LEU A 163 4951 4791 5082 1030 556 291 C ATOM 198 N GLY A 164 -16.101 19.359 -33.795 1.00 47.24 N ANISOU 198 N GLY A 164 6781 6540 4630 -111 -128 347 N ATOM 199 CA GLY A 164 -14.979 20.188 -33.399 1.00 45.01 C ANISOU 199 CA GLY A 164 6665 6489 3949 -322 -259 369 C ATOM 200 C GLY A 164 -15.368 21.349 -32.508 1.00 45.03 C ANISOU 200 C GLY A 164 7056 6257 3796 -326 -286 522 C ATOM 201 O GLY A 164 -14.598 21.756 -31.638 1.00 54.34 O ANISOU 201 O GLY A 164 8342 7525 4780 -336 -305 566 O ATOM 202 N GLY A 165 -16.571 21.873 -32.711 1.00 45.71 N ANISOU 202 N GLY A 165 7301 6035 4033 -294 -274 589 N ATOM 203 CA GLY A 165 -17.029 23.026 -31.958 1.00 54.30 C ANISOU 203 CA GLY A 165 8694 6891 5047 -296 -294 710 C ATOM 204 C GLY A 165 -17.638 22.730 -30.599 1.00 49.27 C ANISOU 204 C GLY A 165 8181 5957 4582 21 -125 831 C ATOM 205 O GLY A 165 -17.741 23.619 -29.755 1.00 63.63 O ANISOU 205 O GLY A 165 10059 7682 6434 18 -130 850 O ATOM 206 N LEU A 166 -18.038 21.481 -30.382 1.00 58.82 N ANISOU 206 N LEU A 166 9248 7053 6047 304 44 837 N ATOM 207 CA LEU A 166 -18.633 21.091 -29.110 1.00 53.17 C ANISOU 207 CA LEU A 166 8637 6048 5519 633 223 953 C ATOM 208 C LEU A 166 -17.619 20.314 -28.280 1.00 58.07 C ANISOU 208 C LEU A 166 9137 6861 6066 761 296 936 C ATOM 209 O LEU A 166 -17.367 19.136 -28.534 1.00 60.50 O ANISOU 209 O LEU A 166 9138 7294 6554 880 382 843 O ATOM 210 CB LEU A 166 -19.902 20.264 -29.332 1.00 46.00 C ANISOU 210 CB LEU A 166 7572 4860 5046 880 376 944 C ATOM 211 CG LEU A 166 -21.017 20.903 -30.167 1.00 49.64 C ANISOU 211 CG LEU A 166 8033 5170 5657 747 309 903 C ATOM 212 CD1 LEU A 166 -22.336 20.172 -29.967 1.00 52.52 C ANISOU 212 CD1 LEU A 166 8118 5403 6435 902 424 818 C ATOM 213 CD2 LEU A 166 -21.175 22.377 -29.849 1.00 53.48 C ANISOU 213 CD2 LEU A 166 8672 5667 5982 535 182 897 C ATOM 214 N SER A 167 -17.039 20.988 -27.293 1.00 59.87 N ANISOU 214 N SER A 167 9472 7141 6136 687 245 950 N ATOM 215 CA SER A 167 -15.937 20.435 -26.514 1.00 61.07 C ANISOU 215 CA SER A 167 9553 7494 6158 757 283 942 C ATOM 216 C SER A 167 -16.316 19.213 -25.681 1.00 62.14 C ANISOU 216 C SER A 167 9602 7464 6545 1140 504 988 C ATOM 217 O SER A 167 -15.463 18.375 -25.390 1.00 62.28 O ANISOU 217 O SER A 167 9489 7683 6491 1249 566 976 O ATOM 218 CB SER A 167 -15.354 21.514 -25.598 1.00 58.05 C ANISOU 218 CB SER A 167 9234 7163 5659 581 177 932 C ATOM 219 OG SER A 167 -16.348 22.042 -24.739 1.00 74.36 O ANISOU 219 OG SER A 167 11402 8932 7919 690 237 957 O ATOM 220 N LYS A 168 -17.583 19.103 -25.297 1.00 54.03 N ANISOU 220 N LYS A 168 8550 6135 5845 1289 613 973 N ATOM 221 CA LYS A 168 -18.001 17.988 -24.455 1.00 57.00 C ANISOU 221 CA LYS A 168 8736 6441 6480 1526 801 929 C ATOM 222 C LYS A 168 -18.128 16.705 -25.275 1.00 56.61 C ANISOU 222 C LYS A 168 8416 6444 6651 1652 888 894 C ATOM 223 O LYS A 168 -18.233 15.610 -24.724 1.00 61.46 O ANISOU 223 O LYS A 168 8810 7110 7432 1715 983 840 O ATOM 224 CB LYS A 168 -19.320 18.302 -23.745 1.00 66.83 C ANISOU 224 CB LYS A 168 9939 7545 7909 1463 828 867 C ATOM 225 CG LYS A 168 -19.547 17.455 -22.497 1.00 82.15 C ANISOU 225 CG LYS A 168 11743 9517 9952 1544 941 843 C ATOM 226 CD LYS A 168 -20.866 17.767 -21.808 1.00 84.91 C ANISOU 226 CD LYS A 168 12107 9776 10379 1512 991 830 C ATOM 227 CE LYS A 168 -21.074 16.864 -20.598 1.00 90.87 C ANISOU 227 CE LYS A 168 12816 10569 11141 1629 1170 867 C ATOM 228 NZ LYS A 168 -22.382 17.107 -19.924 1.00 82.93 N ANISOU 228 NZ LYS A 168 11872 9485 10154 1653 1288 897 N ATOM 229 N LEU A 169 -18.117 16.852 -26.596 1.00 53.92 N ANISOU 229 N LEU A 169 8074 6113 6299 1616 814 917 N ATOM 230 CA LEU A 169 -18.172 15.710 -27.503 1.00 48.60 C ANISOU 230 CA LEU A 169 7051 5544 5871 1685 869 799 C ATOM 231 C LEU A 169 -16.779 15.214 -27.886 1.00 53.88 C ANISOU 231 C LEU A 169 7485 6638 6350 1534 793 671 C ATOM 232 O LEU A 169 -16.638 14.349 -28.752 1.00 50.83 O ANISOU 232 O LEU A 169 6791 6409 6114 1524 805 547 O ATOM 233 CB LEU A 169 -18.956 16.069 -28.765 1.00 52.61 C ANISOU 233 CB LEU A 169 7522 5978 6490 1531 789 749 C ATOM 234 CG LEU A 169 -20.426 16.446 -28.579 1.00 54.14 C ANISOU 234 CG LEU A 169 7770 5933 6868 1447 785 743 C ATOM 235 CD1 LEU A 169 -21.038 16.805 -29.919 1.00 45.87 C ANISOU 235 CD1 LEU A 169 6714 4801 5914 1355 715 720 C ATOM 236 CD2 LEU A 169 -21.204 15.319 -27.918 1.00 43.29 C ANISOU 236 CD2 LEU A 169 6144 4581 5725 1422 818 648 C ATOM 237 N HIS A 170 -15.751 15.773 -27.255 1.00 51.36 N ANISOU 237 N HIS A 170 7311 6504 5699 1415 713 701 N ATOM 238 CA HIS A 170 -14.377 15.411 -27.586 1.00 57.24 C ANISOU 238 CA HIS A 170 7857 7659 6233 1253 629 586 C ATOM 239 C HIS A 170 -13.964 14.091 -26.950 1.00 53.25 C ANISOU 239 C HIS A 170 7118 7224 5890 1511 784 552 C ATOM 240 O HIS A 170 -13.310 14.060 -25.910 1.00 58.56 O ANISOU 240 O HIS A 170 7879 7950 6420 1594 820 606 O ATOM 241 CB HIS A 170 -13.413 16.520 -27.165 1.00 56.83 C ANISOU 241 CB HIS A 170 8048 7784 5760 1021 480 630 C ATOM 242 CG HIS A 170 -13.406 17.693 -28.094 1.00 58.99 C ANISOU 242 CG HIS A 170 8462 8136 5816 691 289 611 C ATOM 243 ND1 HIS A 170 -12.549 18.761 -27.941 1.00 58.74 N ANISOU 243 ND1 HIS A 170 8636 8285 5398 438 130 637 N ATOM 244 CD2 HIS A 170 -14.152 17.963 -29.192 1.00 53.08 C ANISOU 244 CD2 HIS A 170 7677 7309 5183 572 230 569 C ATOM 245 CE1 HIS A 170 -12.768 19.640 -28.903 1.00 63.57 C ANISOU 245 CE1 HIS A 170 9331 8926 5896 177 -18 612 C ATOM 246 NE2 HIS A 170 -13.736 19.180 -29.675 1.00 61.25 N ANISOU 246 NE2 HIS A 170 8895 8478 5901 252 39 571 N ATOM 247 N CYS A 171 -14.362 13.000 -27.592 1.00 58.28 N ANISOU 247 N CYS A 171 7456 7857 6831 1637 874 462 N ATOM 248 CA CYS A 171 -13.965 11.664 -27.183 1.00 49.53 C ANISOU 248 CA CYS A 171 6086 6838 5895 1853 1006 409 C ATOM 249 C CYS A 171 -13.136 11.032 -28.295 1.00 48.01 C ANISOU 249 C CYS A 171 5565 7011 5666 1695 935 241 C ATOM 250 O CYS A 171 -12.981 11.619 -29.367 1.00 45.42 O ANISOU 250 O CYS A 171 5222 6831 5204 1420 783 173 O ATOM 251 CB CYS A 171 -15.193 10.810 -26.861 1.00 44.31 C ANISOU 251 CB CYS A 171 5425 5804 5606 1765 976 403 C ATOM 252 SG CYS A 171 -16.410 10.735 -28.189 1.00 95.00 S ANISOU 252 SG CYS A 171 11747 12079 12270 1650 919 319 S ATOM 253 N THR A 172 -12.581 9.852 -28.038 1.00 48.84 N ANISOU 253 N THR A 172 5508 7145 5905 1646 913 165 N ATOM 254 CA THR A 172 -11.805 9.152 -29.054 1.00 48.52 C ANISOU 254 CA THR A 172 5197 7371 5869 1486 841 14 C ATOM 255 C THR A 172 -12.686 8.757 -30.239 1.00 34.05 C ANISOU 255 C THR A 172 3251 5377 4310 1387 814 -69 C ATOM 256 O THR A 172 -12.273 8.849 -31.404 1.00 37.14 O ANISOU 256 O THR A 172 3473 6029 4610 1253 744 -158 O ATOM 257 CB THR A 172 -11.134 7.890 -28.469 1.00 47.51 C ANISOU 257 CB THR A 172 4994 7187 5872 1453 840 -38 C ATOM 258 OG1 THR A 172 -10.332 8.257 -27.341 1.00 54.22 O ANISOU 258 OG1 THR A 172 5950 8175 6475 1549 860 42 O ATOM 259 CG2 THR A 172 -10.255 7.207 -29.511 1.00 32.00 C ANISOU 259 CG2 THR A 172 2815 5449 3894 1295 771 -160 C ATOM 260 N ALA A 173 -13.920 8.366 -29.937 1.00 31.94 N ANISOU 260 N ALA A 173 4354 3210 4571 578 -80 -361 N ATOM 261 CA ALA A 173 -14.839 7.905 -30.965 1.00 29.35 C ANISOU 261 CA ALA A 173 4017 2914 4221 591 -52 -383 C ATOM 262 C ALA A 173 -15.151 9.019 -31.946 1.00 24.25 C ANISOU 262 C ALA A 173 3417 2187 3608 595 -166 -372 C ATOM 263 O ALA A 173 -15.278 8.787 -33.151 1.00 25.08 O ANISOU 263 O ALA A 173 3518 2288 3725 600 -170 -403 O ATOM 264 CB ALA A 173 -16.119 7.382 -30.332 1.00 26.58 C ANISOU 264 CB ALA A 173 3650 2624 3827 592 6 -361 C ATOM 265 N ASN A 174 -15.252 10.238 -31.429 1.00 26.87 N ANISOU 265 N ASN A 174 3797 2465 3949 584 -259 -320 N ATOM 266 CA ASN A 174 -15.537 11.382 -32.280 1.00 26.83 C ANISOU 266 CA ASN A 174 3850 2389 3957 566 -374 -285 C ATOM 267 C ASN A 174 -14.324 11.834 -33.082 1.00 31.32 C ANISOU 267 C ASN A 174 4424 2872 4603 529 -469 -269 C ATOM 268 O ASN A 174 -14.471 12.400 -34.164 1.00 31.94 O ANISOU 268 O ASN A 174 4503 2967 4666 465 -503 -227 O ATOM 269 CB ASN A 174 -16.101 12.534 -31.446 1.00 31.03 C ANISOU 269 CB ASN A 174 4428 2913 4450 559 -438 -225 C ATOM 270 CG ASN A 174 -17.553 12.301 -31.050 1.00 39.67 C ANISOU 270 CG ASN A 174 5514 4072 5486 576 -366 -217 C ATOM 271 OD1 ASN A 174 -18.241 11.466 -31.639 1.00 32.66 O ANISOU 271 OD1 ASN A 174 4602 3221 4587 586 -293 -244 O ATOM 272 ND2 ASN A 174 -18.025 13.043 -30.056 1.00 38.30 N ANISOU 272 ND2 ASN A 174 5356 3915 5279 574 -389 -175 N ATOM 273 N ALA A 175 -13.125 11.586 -32.561 1.00 26.10 N ANISOU 273 N ALA A 175 3730 2197 3990 520 -469 -270 N ATOM 274 CA ALA A 175 -11.918 11.853 -33.338 1.00 25.27 C ANISOU 274 CA ALA A 175 3568 2125 3908 424 -490 -204 C ATOM 275 C ALA A 175 -11.853 10.897 -34.524 1.00 34.50 C ANISOU 275 C ALA A 175 4652 3433 5025 377 -365 -217 C ATOM 276 O ALA A 175 -11.503 11.289 -35.653 1.00 35.23 O ANISOU 276 O ALA A 175 4701 3591 5094 292 -369 -147 O ATOM 277 CB ALA A 175 -10.678 11.718 -32.472 1.00 31.87 C ANISOU 277 CB ALA A 175 4390 2914 4805 425 -508 -195 C ATOM 278 N ILE A 176 -12.232 9.646 -34.270 1.00 27.20 N ANISOU 278 N ILE A 176 3707 2549 4080 442 -259 -306 N ATOM 279 CA ILE A 176 -12.281 8.661 -35.340 1.00 24.02 C ANISOU 279 CA ILE A 176 3239 2271 3617 414 -147 -319 C ATOM 280 C ILE A 176 -13.335 9.045 -36.375 1.00 25.52 C ANISOU 280 C ILE A 176 3449 2482 3766 395 -155 -296 C ATOM 281 O ILE A 176 -13.082 8.995 -37.590 1.00 28.25 O ANISOU 281 O ILE A 176 3750 2906 4077 330 -119 -245 O ATOM 282 CB ILE A 176 -12.585 7.260 -34.796 1.00 29.88 C ANISOU 282 CB ILE A 176 3962 3052 4340 496 -43 -422 C ATOM 283 CG1 ILE A 176 -11.481 6.822 -33.834 1.00 26.11 C ANISOU 283 CG1 ILE A 176 3460 2563 3900 506 -17 -455 C ATOM 284 CG2 ILE A 176 -12.725 6.260 -35.935 1.00 24.30 C ANISOU 284 CG2 ILE A 176 3202 2472 3559 474 60 -425 C ATOM 285 CD1 ILE A 176 -11.731 5.486 -33.209 1.00 19.71 C ANISOU 285 CD1 ILE A 176 2627 1807 3054 576 87 -553 C ATOM 286 N HIS A 177 -14.499 9.476 -35.893 1.00 24.72 N ANISOU 286 N HIS A 177 3420 2302 3670 454 -203 -325 N ATOM 287 CA HIS A 177 -15.568 9.886 -36.797 1.00 25.58 C ANISOU 287 CA HIS A 177 3559 2418 3741 434 -210 -305 C ATOM 288 C HIS A 177 -15.146 11.086 -37.626 1.00 28.29 C ANISOU 288 C HIS A 177 3896 2769 4084 335 -278 -223 C ATOM 289 O HIS A 177 -15.468 11.174 -38.808 1.00 32.90 O ANISOU 289 O HIS A 177 4460 3406 4637 286 -246 -199 O ATOM 290 CB HIS A 177 -16.839 10.228 -36.020 1.00 27.03 C ANISOU 290 CB HIS A 177 3833 2509 3929 516 -258 -335 C ATOM 291 CG HIS A 177 -17.441 9.062 -35.305 1.00 27.68 C ANISOU 291 CG HIS A 177 3905 2610 4001 606 -179 -398 C ATOM 292 ND1 HIS A 177 -18.194 9.200 -34.160 1.00 29.49 N ANISOU 292 ND1 HIS A 177 4137 2871 4199 606 -157 -357 N ATOM 293 CD2 HIS A 177 -17.402 7.736 -35.573 1.00 22.75 C ANISOU 293 CD2 HIS A 177 3220 2072 3352 625 -73 -442 C ATOM 294 CE1 HIS A 177 -18.595 8.009 -33.753 1.00 26.80 C ANISOU 294 CE1 HIS A 177 3738 2613 3832 611 -50 -367 C ATOM 295 NE2 HIS A 177 -18.126 7.103 -34.592 1.00 27.26 N ANISOU 295 NE2 HIS A 177 3765 2709 3886 620 1 -414 N ATOM 296 N ALA A 178 -14.389 11.989 -37.015 1.00 30.33 N ANISOU 296 N ALA A 178 4169 2973 4381 309 -373 -178 N ATOM 297 CA ALA A 178 -13.946 13.183 -37.716 1.00 33.61 C ANISOU 297 CA ALA A 178 4574 3396 4801 221 -451 -98 C ATOM 298 C ALA A 178 -12.972 12.814 -38.823 1.00 34.74 C ANISOU 298 C ALA A 178 4621 3637 4941 154 -391 -50 C ATOM 299 O ALA A 178 -13.050 13.360 -39.931 1.00 30.10 O ANISOU 299 O ALA A 178 4008 3090 4340 95 -396 -7 O ATOM 300 CB ALA A 178 -13.308 14.176 -36.745 1.00 30.58 C ANISOU 300 CB ALA A 178 4232 2928 4461 217 -578 -52 C ATOM 301 N ASN A 179 -12.065 11.877 -38.540 1.00 29.80 N ANISOU 301 N ASN A 179 3945 3049 4327 167 -329 -55 N ATOM 302 CA ASN A 179 -11.133 11.461 -39.585 1.00 26.93 C ANISOU 302 CA ASN A 179 3500 2780 3952 114 -268 7 C ATOM 303 C ASN A 179 -11.827 10.724 -40.735 1.00 30.87 C ANISOU 303 C ASN A 179 3981 3353 4398 123 -171 -16 C ATOM 304 O ASN A 179 -11.462 10.895 -41.911 1.00 38.26 O ANISOU 304 O ASN A 179 4870 4343 5323 78 -153 48 O ATOM 305 CB ASN A 179 -10.023 10.601 -38.989 1.00 36.32 C ANISOU 305 CB ASN A 179 4651 3998 5152 124 -218 11 C ATOM 306 CG ASN A 179 -9.034 11.416 -38.168 1.00 35.34 C ANISOU 306 CG ASN A 179 4533 3805 5091 95 -317 69 C ATOM 307 OD1 ASN A 179 -8.085 11.986 -38.707 1.00 41.05 O ANISOU 307 OD1 ASN A 179 5211 4549 5838 33 -360 172 O ATOM 308 ND2 ASN A 179 -9.260 11.481 -36.862 1.00 29.48 N ANISOU 308 ND2 ASN A 179 3848 2972 4381 149 -360 11 N ATOM 309 N LEU A 180 -12.851 9.941 -40.402 1.00 32.71 N ANISOU 309 N LEU A 180 4251 3576 4600 188 -117 -101 N ATOM 310 CA LEU A 180 -13.648 9.265 -41.425 1.00 25.73 C ANISOU 310 CA LEU A 180 3365 2743 3668 204 -39 -120 C ATOM 311 C LEU A 180 -14.356 10.290 -42.310 1.00 27.11 C ANISOU 311 C LEU A 180 3564 2891 3845 162 -82 -93 C ATOM 312 O LEU A 180 -14.384 10.180 -43.560 1.00 30.69 O ANISOU 312 O LEU A 180 3989 3390 4280 137 -38 -60 O ATOM 313 CB LEU A 180 -14.664 8.336 -40.757 1.00 27.20 C ANISOU 313 CB LEU A 180 3592 2912 3832 287 7 -210 C ATOM 314 CG LEU A 180 -15.693 7.576 -41.593 1.00 26.28 C ANISOU 314 CG LEU A 180 3489 2825 3669 321 75 -236 C ATOM 315 CD1 LEU A 180 -15.009 6.606 -42.534 1.00 27.13 C ANISOU 315 CD1 LEU A 180 3544 3031 3733 312 157 -202 C ATOM 316 CD2 LEU A 180 -16.643 6.842 -40.669 1.00 27.51 C ANISOU 316 CD2 LEU A 180 3684 2947 3819 410 95 -315 C ATOM 317 N PHE A 181 -14.881 11.317 -41.641 1.00 30.35 N ANISOU 317 N PHE A 181 4030 3224 4277 156 -169 -105 N ATOM 318 CA PHE A 181 -15.569 12.406 -42.312 1.00 31.47 C ANISOU 318 CA PHE A 181 4203 3340 4413 110 -216 -88 C ATOM 319 C PHE A 181 -14.615 13.066 -43.276 1.00 32.16 C ANISOU 319 C PHE A 181 4224 3473 4522 38 -238 -14 C ATOM 320 O PHE A 181 -14.974 13.345 -44.414 1.00 30.27 O ANISOU 320 O PHE A 181 3971 3256 4272 7 -212 -3 O ATOM 321 CB PHE A 181 -16.078 13.453 -41.317 1.00 26.60 C ANISOU 321 CB PHE A 181 3662 2640 3805 115 -319 -96 C ATOM 322 CG PHE A 181 -17.187 12.978 -40.430 1.00 22.55 C ANISOU 322 CG PHE A 181 3224 2069 3274 196 -306 -155 C ATOM 323 CD1 PHE A 181 -17.883 11.814 -40.710 1.00 26.11 C ANISOU 323 CD1 PHE A 181 3673 2544 3702 249 -212 -201 C ATOM 324 CD2 PHE A 181 -17.539 13.709 -39.310 1.00 24.97 C ANISOU 324 CD2 PHE A 181 3607 2293 3587 230 -396 -156 C ATOM 325 CE1 PHE A 181 -18.905 11.387 -39.885 1.00 24.14 C ANISOU 325 CE1 PHE A 181 3487 2240 3445 332 -206 -245 C ATOM 326 CE2 PHE A 181 -18.560 13.288 -38.484 1.00 27.60 C ANISOU 326 CE2 PHE A 181 4011 2568 3910 319 -387 -198 C ATOM 327 CZ PHE A 181 -19.244 12.124 -38.772 1.00 26.72 C ANISOU 327 CZ PHE A 181 3886 2483 3782 370 -291 -243 C ATOM 328 N LEU A 182 -13.388 13.295 -42.816 1.00 28.94 N ANISOU 328 N LEU A 182 3774 3073 4148 18 -286 39 N ATOM 329 CA LEU A 182 -12.389 13.948 -43.647 1.00 29.52 C ANISOU 329 CA LEU A 182 3778 3187 4251 -42 -318 125 C ATOM 330 C LEU A 182 -12.060 13.115 -44.873 1.00 34.23 C ANISOU 330 C LEU A 182 4315 3858 4831 -36 -218 156 C ATOM 331 O LEU A 182 -11.886 13.665 -45.966 1.00 30.16 O ANISOU 331 O LEU A 182 3760 3369 4331 -69 -222 203 O ATOM 332 CB LEU A 182 -11.109 14.214 -42.856 1.00 31.01 C ANISOU 332 CB LEU A 182 3937 3362 4482 -58 -385 189 C ATOM 333 CG LEU A 182 -11.062 15.411 -41.910 1.00 38.29 C ANISOU 333 CG LEU A 182 4907 4208 5434 -78 -520 204 C ATOM 334 CD1 LEU A 182 -9.689 15.474 -41.259 1.00 44.82 C ANISOU 334 CD1 LEU A 182 5699 5021 6310 -91 -573 278 C ATOM 335 CD2 LEU A 182 -11.370 16.708 -42.648 1.00 34.35 C ANISOU 335 CD2 LEU A 182 4405 3710 4935 -133 -594 235 C ATOM 336 N SER A 183 -11.990 11.794 -44.709 1.00 30.08 N ANISOU 336 N SER A 183 3788 3368 4274 12 -130 130 N ATOM 337 CA SER A 183 -11.669 10.959 -45.861 1.00 29.64 C ANISOU 337 CA SER A 183 3690 3383 4191 28 -41 171 C ATOM 338 C SER A 183 -12.774 11.080 -46.909 1.00 32.65 C ANISOU 338 C SER A 183 4098 3751 4556 35 -8 139 C ATOM 339 O SER A 183 -12.494 11.204 -48.118 1.00 38.50 O ANISOU 339 O SER A 183 4801 4522 5305 27 18 195 O ATOM 340 CB SER A 183 -11.460 9.499 -45.442 1.00 28.84 C ANISOU 340 CB SER A 183 3589 3327 4040 79 43 144 C ATOM 341 OG SER A 183 -12.645 8.927 -44.924 1.00 33.68 O ANISOU 341 OG SER A 183 4260 3911 4625 127 71 46 O ATOM 342 N PHE A 184 -14.028 11.099 -46.456 1.00 28.82 N ANISOU 342 N PHE A 184 3680 3215 4054 54 -12 56 N ATOM 343 CA PHE A 184 -15.117 11.305 -47.416 1.00 26.63 C ANISOU 343 CA PHE A 184 3437 2915 3768 52 17 28 C ATOM 344 C PHE A 184 -15.132 12.721 -48.002 1.00 28.17 C ANISOU 344 C PHE A 184 3618 3089 3997 -11 -43 50 C ATOM 345 O PHE A 184 -15.562 12.923 -49.137 1.00 34.88 O ANISOU 345 O PHE A 184 4464 3937 4850 -21 -8 50 O ATOM 346 CB PHE A 184 -16.471 10.980 -46.784 1.00 25.24 C ANISOU 346 CB PHE A 184 3340 2687 3564 88 28 -52 C ATOM 347 CG PHE A 184 -16.784 9.513 -46.750 1.00 23.71 C ANISOU 347 CG PHE A 184 3158 2518 3332 157 105 -78 C ATOM 348 CD1 PHE A 184 -17.251 8.867 -47.886 1.00 22.22 C ANISOU 348 CD1 PHE A 184 2979 2342 3121 182 171 -69 C ATOM 349 CD2 PHE A 184 -16.594 8.776 -45.593 1.00 21.70 C ANISOU 349 CD2 PHE A 184 2906 2273 3065 202 110 -112 C ATOM 350 CE1 PHE A 184 -17.530 7.516 -47.868 1.00 21.26 C ANISOU 350 CE1 PHE A 184 2872 2248 2958 248 231 -86 C ATOM 351 CE2 PHE A 184 -16.870 7.421 -45.566 1.00 21.94 C ANISOU 351 CE2 PHE A 184 2943 2338 3055 266 178 -139 C ATOM 352 CZ PHE A 184 -17.341 6.790 -46.706 1.00 24.85 C ANISOU 352 CZ PHE A 184 3323 2725 3394 288 234 -123 C ATOM 353 N VAL A 185 -14.655 13.699 -47.236 1.00 35.90 N ANISOU 353 N VAL A 185 4589 4050 5000 -52 -135 68 N ATOM 354 CA VAL A 185 -14.586 15.081 -47.706 1.00 29.82 C ANISOU 354 CA VAL A 185 3801 3272 4256 -114 -204 90 C ATOM 355 C VAL A 185 -13.576 15.185 -48.834 1.00 30.73 C ANISOU 355 C VAL A 185 3827 3440 4409 -126 -186 167 C ATOM 356 O VAL A 185 -13.785 15.891 -49.826 1.00 33.33 O ANISOU 356 O VAL A 185 4132 3774 4758 -153 -185 170 O ATOM 357 CB VAL A 185 -14.192 16.049 -46.564 1.00 32.82 C ANISOU 357 CB VAL A 185 4198 3622 4652 -145 -322 108 C ATOM 358 CG1 VAL A 185 -13.636 17.368 -47.111 1.00 31.90 C ANISOU 358 CG1 VAL A 185 4031 3522 4567 -207 -403 160 C ATOM 359 CG2 VAL A 185 -15.378 16.297 -45.647 1.00 30.24 C ANISOU 359 CG2 VAL A 185 3971 3232 4286 -132 -353 40 C ATOM 360 N LEU A 186 -12.490 14.438 -48.680 1.00 34.03 N ANISOU 360 N LEU A 186 4197 3896 4836 -100 -165 232 N ATOM 361 CA LEU A 186 -11.425 14.407 -49.664 1.00 36.75 C ANISOU 361 CA LEU A 186 4459 4290 5213 -95 -147 328 C ATOM 362 C LEU A 186 -11.926 13.743 -50.927 1.00 32.91 C ANISOU 362 C LEU A 186 3976 3817 4710 -53 -51 319 C ATOM 363 O LEU A 186 -11.691 14.229 -52.047 1.00 40.30 O ANISOU 363 O LEU A 186 4865 4764 5683 -53 -43 362 O ATOM 364 CB LEU A 186 -10.209 13.664 -49.105 1.00 38.51 C ANISOU 364 CB LEU A 186 4648 4551 5435 -76 -139 403 C ATOM 365 CG LEU A 186 -8.921 13.731 -49.919 1.00 44.24 C ANISOU 365 CG LEU A 186 5289 5324 6195 -71 -138 534 C ATOM 366 CD1 LEU A 186 -8.495 15.177 -50.092 1.00 49.55 C ANISOU 366 CD1 LEU A 186 5911 5982 6933 -121 -242 583 C ATOM 367 CD2 LEU A 186 -7.834 12.928 -49.229 1.00 49.78 C ANISOU 367 CD2 LEU A 186 5974 6059 6881 -59 -121 601 C ATOM 368 N LYS A 187 -12.656 12.645 -50.745 1.00 33.84 N ANISOU 368 N LYS A 187 4151 3928 4777 -9 19 263 N ATOM 369 CA LYS A 187 -13.202 11.956 -51.901 1.00 31.20 C ANISOU 369 CA LYS A 187 3836 3594 4425 39 102 257 C ATOM 370 C LYS A 187 -14.157 12.856 -52.669 1.00 29.74 C ANISOU 370 C LYS A 187 3671 3360 4267 11 98 205 C ATOM 371 O LYS A 187 -13.993 13.050 -53.874 1.00 30.14 O ANISOU 371 O LYS A 187 3689 3412 4348 28 128 240 O ATOM 372 CB LYS A 187 -13.928 10.675 -51.494 1.00 33.37 C ANISOU 372 CB LYS A 187 4174 3865 4639 89 163 204 C ATOM 373 CG LYS A 187 -14.532 9.957 -52.685 1.00 32.36 C ANISOU 373 CG LYS A 187 4078 3726 4493 143 237 206 C ATOM 374 CD LYS A 187 -15.356 8.753 -52.289 1.00 34.48 C ANISOU 374 CD LYS A 187 4411 3987 4702 194 283 154 C ATOM 375 CE LYS A 187 -15.825 8.020 -53.533 1.00 42.19 C ANISOU 375 CE LYS A 187 5423 4947 5661 254 346 177 C ATOM 376 NZ LYS A 187 -16.730 6.887 -53.216 1.00 35.50 N ANISOU 376 NZ LYS A 187 4642 4087 4760 305 380 131 N ATOM 377 N ALA A 188 -15.135 13.426 -51.967 1.00 30.54 N ANISOU 377 N ALA A 188 3829 3418 4356 -29 62 124 N ATOM 378 CA ALA A 188 -16.174 14.215 -52.626 1.00 27.78 C ANISOU 378 CA ALA A 188 3514 3024 4016 -62 68 64 C ATOM 379 C ALA A 188 -15.602 15.465 -53.279 1.00 29.62 C ANISOU 379 C ALA A 188 3680 3275 4300 -109 22 93 C ATOM 380 O ALA A 188 -16.021 15.848 -54.382 1.00 22.22 O ANISOU 380 O ALA A 188 2735 2319 3388 -113 61 70 O ATOM 381 CB ALA A 188 -17.262 14.593 -51.632 1.00 28.56 C ANISOU 381 CB ALA A 188 3693 3078 4080 -92 33 -10 C ATOM 382 N SER A 189 -14.623 16.082 -52.620 1.00 26.30 N ANISOU 382 N SER A 189 3208 2886 3900 -140 -60 144 N ATOM 383 CA SER A 189 -14.004 17.280 -53.172 1.00 29.48 C ANISOU 383 CA SER A 189 3537 3312 4353 -182 -118 181 C ATOM 384 C SER A 189 -13.264 16.933 -54.455 1.00 27.53 C ANISOU 384 C SER A 189 3216 3091 4154 -131 -63 253 C ATOM 385 O SER A 189 -13.356 17.655 -55.461 1.00 31.64 O ANISOU 385 O SER A 189 3696 3610 4717 -139 -54 243 O ATOM 386 CB SER A 189 -13.054 17.916 -52.160 1.00 27.67 C ANISOU 386 CB SER A 189 3271 3102 4138 -217 -227 239 C ATOM 387 OG SER A 189 -13.752 18.347 -51.002 1.00 28.96 O ANISOU 387 OG SER A 189 3513 3233 4260 -253 -287 180 O ATOM 388 N ALA A 190 -12.566 15.801 -54.434 1.00 32.27 N ANISOU 388 N ALA A 190 3804 3714 4743 -71 -21 323 N ATOM 389 CA ALA A 190 -11.838 15.373 -55.622 1.00 36.14 C ANISOU 389 CA ALA A 190 4237 4226 5268 -6 31 411 C ATOM 390 C ALA A 190 -12.801 15.069 -56.766 1.00 33.59 C ANISOU 390 C ALA A 190 3955 3861 4948 35 114 354 C ATOM 391 O ALA A 190 -12.561 15.475 -57.905 1.00 33.57 O ANISOU 391 O ALA A 190 3904 3852 5001 65 134 385 O ATOM 392 CB ALA A 190 -10.969 14.154 -55.312 1.00 30.04 C ANISOU 392 CB ALA A 190 3460 3492 4460 47 64 499 C ATOM 393 N VAL A 191 -13.907 14.396 -56.454 1.00 26.81 N ANISOU 393 N VAL A 191 3186 2964 4035 39 159 273 N ATOM 394 CA VAL A 191 -14.876 14.019 -57.476 1.00 28.07 C ANISOU 394 CA VAL A 191 3400 3069 4198 79 235 225 C ATOM 395 C VAL A 191 -15.491 15.249 -58.123 1.00 28.11 C ANISOU 395 C VAL A 191 3392 3039 4249 29 228 155 C ATOM 396 O VAL A 191 -15.567 15.345 -59.348 1.00 28.50 O ANISOU 396 O VAL A 191 3424 3058 4345 71 277 159 O ATOM 397 CB VAL A 191 -16.017 13.144 -56.902 1.00 31.25 C ANISOU 397 CB VAL A 191 3903 3434 4538 87 271 155 C ATOM 398 CG1 VAL A 191 -17.116 12.957 -57.939 1.00 25.08 C ANISOU 398 CG1 VAL A 191 3183 2580 3768 116 337 103 C ATOM 399 CG2 VAL A 191 -15.486 11.801 -56.440 1.00 31.45 C ANISOU 399 CG2 VAL A 191 3941 3498 4511 148 293 213 C ATOM 400 N LEU A 192 -15.911 16.198 -57.293 1.00 27.28 N ANISOU 400 N LEU A 192 3299 2938 4129 -56 167 91 N ATOM 401 CA LEU A 192 -16.530 17.410 -57.806 1.00 25.76 C ANISOU 401 CA LEU A 192 3100 2724 3962 -116 160 17 C ATOM 402 C LEU A 192 -15.547 18.236 -58.631 1.00 26.71 C ANISOU 402 C LEU A 192 3110 2881 4156 -109 133 68 C ATOM 403 O LEU A 192 -15.923 18.835 -59.648 1.00 28.04 O ANISOU 403 O LEU A 192 3259 3027 4368 -112 171 19 O ATOM 404 CB LEU A 192 -17.096 18.236 -56.649 1.00 25.26 C ANISOU 404 CB LEU A 192 3081 2667 3850 -203 89 -42 C ATOM 405 CG LEU A 192 -18.318 17.572 -56.010 1.00 24.93 C ANISOU 405 CG LEU A 192 3153 2575 3744 -204 123 -101 C ATOM 406 CD1 LEU A 192 -18.728 18.269 -54.730 1.00 20.60 C ANISOU 406 CD1 LEU A 192 2653 2030 3143 -268 45 -133 C ATOM 407 CD2 LEU A 192 -19.472 17.548 -57.000 1.00 24.34 C ANISOU 407 CD2 LEU A 192 3134 2438 3675 -205 206 -171 C ATOM 408 N PHE A 193 -14.278 18.229 -58.229 1.00 29.16 N ANISOU 408 N PHE A 193 3348 3246 4487 -93 73 170 N ATOM 409 CA PHE A 193 -13.280 18.993 -58.970 1.00 31.03 C ANISOU 409 CA PHE A 193 3473 3518 4799 -77 39 238 C ATOM 410 C PHE A 193 -12.979 18.364 -60.326 1.00 33.97 C ANISOU 410 C PHE A 193 3816 3867 5225 26 121 291 C ATOM 411 O PHE A 193 -12.948 19.056 -61.347 1.00 39.19 O ANISOU 411 O PHE A 193 4420 4518 5953 45 138 276 O ATOM 412 CB PHE A 193 -11.990 19.128 -58.168 1.00 35.93 C ANISOU 412 CB PHE A 193 4028 4192 5430 -85 -51 350 C ATOM 413 CG PHE A 193 -10.959 19.989 -58.835 1.00 42.60 C ANISOU 413 CG PHE A 193 4754 5074 6357 -69 -103 434 C ATOM 414 CD1 PHE A 193 -11.049 21.369 -58.774 1.00 40.91 C ANISOU 414 CD1 PHE A 193 4494 4881 6168 -139 -180 388 C ATOM 415 CD2 PHE A 193 -9.902 19.420 -59.527 1.00 44.49 C ANISOU 415 CD2 PHE A 193 4930 5329 6645 21 -77 565 C ATOM 416 CE1 PHE A 193 -10.103 22.167 -59.386 1.00 42.63 C ANISOU 416 CE1 PHE A 193 4596 5136 6468 -119 -234 467 C ATOM 417 CE2 PHE A 193 -8.952 20.215 -60.142 1.00 48.77 C ANISOU 417 CE2 PHE A 193 5358 5901 7270 46 -128 654 C ATOM 418 CZ PHE A 193 -9.055 21.591 -60.070 1.00 45.55 C ANISOU 418 CZ PHE A 193 4896 5515 6897 -23 -208 602 C ATOM 419 N ILE A 194 -12.766 17.051 -60.331 1.00 29.42 N ANISOU 419 N ILE A 194 3281 3282 4615 98 171 355 N ATOM 420 CA ILE A 194 -12.489 16.326 -61.566 1.00 33.47 C ANISOU 420 CA ILE A 194 3788 3767 5163 211 245 421 C ATOM 421 C ILE A 194 -13.664 16.457 -62.525 1.00 35.15 C ANISOU 421 C ILE A 194 4053 3902 5399 225 316 315 C ATOM 422 O ILE A 194 -13.488 16.633 -63.737 1.00 37.57 O ANISOU 422 O ILE A 194 4324 4176 5776 298 356 338 O ATOM 423 CB ILE A 194 -12.226 14.823 -61.289 1.00 36.94 C ANISOU 423 CB ILE A 194 4288 4215 5535 278 284 496 C ATOM 424 CG1 ILE A 194 -10.899 14.633 -60.554 1.00 38.06 C ANISOU 424 CG1 ILE A 194 4371 4430 5662 277 230 619 C ATOM 425 CG2 ILE A 194 -12.241 14.018 -62.578 1.00 36.86 C ANISOU 425 CG2 ILE A 194 4305 4157 5541 399 361 552 C ATOM 426 CD1 ILE A 194 -10.587 13.188 -60.232 1.00 39.77 C ANISOU 426 CD1 ILE A 194 4642 4670 5800 334 271 687 C ATOM 427 N ASP A 195 -14.866 16.398 -61.962 1.00 39.53 N ANISOU 427 N ASP A 195 5437 6359 3224 -548 981 126 N ATOM 428 CA ASP A 195 -16.080 16.528 -62.746 1.00 49.65 C ANISOU 428 CA ASP A 195 6585 7834 4445 -720 1032 -218 C ATOM 429 C ASP A 195 -16.173 17.919 -63.354 1.00 47.80 C ANISOU 429 C ASP A 195 6143 7711 4308 -530 659 -447 C ATOM 430 O ASP A 195 -16.601 18.081 -64.497 1.00 48.53 O ANISOU 430 O ASP A 195 6175 7773 4491 -608 660 -625 O ATOM 431 CB ASP A 195 -17.306 16.248 -61.878 1.00 49.61 C ANISOU 431 CB ASP A 195 6496 8191 4161 -893 1168 -432 C ATOM 432 CG ASP A 195 -18.424 15.586 -62.649 1.00 54.87 C ANISOU 432 CG ASP A 195 7152 8916 4781 -1170 1420 -644 C ATOM 433 OD1 ASP A 195 -18.140 14.643 -63.416 1.00 58.14 O ANISOU 433 OD1 ASP A 195 7722 9006 5361 -1280 1632 -481 O ATOM 434 OD2 ASP A 195 -19.587 16.011 -62.491 1.00 70.88 O ANISOU 434 OD2 ASP A 195 8998 11172 6762 -1197 1299 -921 O ATOM 435 N GLY A 196 -15.734 18.921 -62.598 1.00 43.20 N ANISOU 435 N GLY A 196 5454 7247 3713 -275 338 -434 N ATOM 436 CA GLY A 196 -15.774 20.282 -63.095 1.00 38.32 C ANISOU 436 CA GLY A 196 4636 6738 3185 -78 -32 -641 C ATOM 437 C GLY A 196 -14.757 20.475 -64.198 1.00 40.16 C ANISOU 437 C GLY A 196 4945 6617 3697 43 -129 -476 C ATOM 438 O GLY A 196 -14.962 21.260 -65.124 1.00 40.21 O ANISOU 438 O GLY A 196 4820 6646 3811 105 -320 -670 O ATOM 439 N LEU A 197 -13.656 19.740 -64.098 1.00 39.38 N ANISOU 439 N LEU A 197 5061 6188 3714 74 10 -114 N ATOM 440 CA LEU A 197 -12.556 19.879 -65.042 1.00 37.36 C ANISOU 440 CA LEU A 197 4895 5574 3725 204 -80 85 C ATOM 441 C LEU A 197 -12.746 19.086 -66.336 1.00 44.84 C ANISOU 441 C LEU A 197 5944 6302 4790 -6 177 78 C ATOM 442 O LEU A 197 -12.136 19.408 -67.356 1.00 50.28 O ANISOU 442 O LEU A 197 6649 6760 5695 86 67 133 O ATOM 443 CB LEU A 197 -11.249 19.454 -64.372 1.00 40.11 C ANISOU 443 CB LEU A 197 5432 5656 4154 336 -51 484 C ATOM 444 CG LEU A 197 -9.958 19.992 -64.983 1.00 42.16 C ANISOU 444 CG LEU A 197 5742 5604 4674 572 -270 696 C ATOM 445 CD1 LEU A 197 -9.959 21.511 -64.969 1.00 43.03 C ANISOU 445 CD1 LEU A 197 5630 5901 4819 822 -698 504 C ATOM 446 CD2 LEU A 197 -8.765 19.460 -64.223 1.00 50.05 C ANISOU 446 CD2 LEU A 197 6934 6360 5723 675 -206 1085 C ATOM 447 N LEU A 198 -13.590 18.058 -66.306 1.00 42.45 N ANISOU 447 N LEU A 198 5709 6074 4347 -286 516 8 N ATOM 448 CA LEU A 198 -13.697 17.165 -67.459 1.00 44.06 C ANISOU 448 CA LEU A 198 6036 6045 4659 -494 793 39 C ATOM 449 C LEU A 198 -15.095 17.024 -68.058 1.00 51.00 C ANISOU 449 C LEU A 198 6802 7152 5425 -728 928 -305 C ATOM 450 O LEU A 198 -15.232 16.608 -69.210 1.00 53.31 O ANISOU 450 O LEU A 198 7145 7277 5833 -862 1074 -341 O ATOM 451 CB LEU A 198 -13.185 15.773 -67.083 1.00 49.01 C ANISOU 451 CB LEU A 198 6913 6434 5274 -638 1145 356 C ATOM 452 CG LEU A 198 -11.675 15.622 -66.897 1.00 50.17 C ANISOU 452 CG LEU A 198 7229 6240 5595 -454 1092 744 C ATOM 453 CD1 LEU A 198 -11.329 14.195 -66.497 1.00 42.57 C ANISOU 453 CD1 LEU A 198 6505 5075 4594 -626 1463 1027 C ATOM 454 CD2 LEU A 198 -10.937 16.024 -68.166 1.00 50.50 C ANISOU 454 CD2 LEU A 198 7289 5997 5901 -342 957 808 C ATOM 455 N ARG A 199 -16.130 17.355 -67.292 1.00 48.87 N ANISOU 455 N ARG A 199 6380 7258 4929 -780 885 -556 N ATOM 456 CA ARG A 199 -17.490 17.059 -67.733 1.00 46.76 C ANISOU 456 CA ARG A 199 6027 7211 4530 -1028 1059 -864 C ATOM 457 C ARG A 199 -18.478 18.217 -67.616 1.00 52.64 C ANISOU 457 C ARG A 199 6507 8337 5157 -967 793 -1241 C ATOM 458 O ARG A 199 -19.679 18.024 -67.805 1.00 61.68 O ANISOU 458 O ARG A 199 7554 9621 6262 -1130 871 -1439 O ATOM 459 CB ARG A 199 -18.037 15.868 -66.948 1.00 52.18 C ANISOU 459 CB ARG A 199 6830 7979 5016 -1263 1411 -804 C ATOM 460 CG ARG A 199 -17.270 14.576 -67.147 1.00 58.88 C ANISOU 460 CG ARG A 199 7931 8448 5993 -1353 1692 -459 C ATOM 461 CD ARG A 199 -17.946 13.430 -66.417 1.00 60.29 C ANISOU 461 CD ARG A 199 8155 8631 6120 -1459 1845 -405 C ATOM 462 NE ARG A 199 -17.281 12.157 -66.667 1.00 61.43 N ANISOU 462 NE ARG A 199 8473 8429 6437 -1467 1992 -120 N ATOM 463 CZ ARG A 199 -16.240 11.715 -65.973 1.00 69.60 C ANISOU 463 CZ ARG A 199 9623 9311 7511 -1365 2023 182 C ATOM 464 NH1 ARG A 199 -15.693 10.544 -66.267 1.00 68.73 N ANISOU 464 NH1 ARG A 199 9603 8943 7569 -1351 2084 383 N ATOM 465 NH2 ARG A 199 -15.744 12.447 -64.984 1.00 67.14 N ANISOU 465 NH2 ARG A 199 9316 9130 7063 -1264 1954 263 N ATOM 466 N THR A 200 -17.985 19.413 -67.315 1.00 49.92 N ANISOU 466 N THR A 200 6035 8064 4869 -693 422 -1262 N ATOM 467 CA THR A 200 -18.874 20.553 -67.117 1.00 51.32 C ANISOU 467 CA THR A 200 5955 8508 5038 -592 150 -1518 C ATOM 468 C THR A 200 -18.961 21.438 -68.356 1.00 55.02 C ANISOU 468 C THR A 200 6299 8814 5792 -473 -30 -1562 C ATOM 469 O THR A 200 -18.218 21.253 -69.317 1.00 55.84 O ANISOU 469 O THR A 200 6501 8717 5997 -474 -26 -1520 O ATOM 470 CB THR A 200 -18.429 21.410 -65.922 1.00 44.14 C ANISOU 470 CB THR A 200 4965 7720 4085 -344 -117 -1447 C ATOM 471 OG1 THR A 200 -18.490 20.627 -64.725 1.00 52.17 O ANISOU 471 OG1 THR A 200 6083 8908 4833 -446 65 -1384 O ATOM 472 CG2 THR A 200 -19.340 22.612 -65.771 1.00 42.73 C ANISOU 472 CG2 THR A 200 4567 7584 4086 -212 -275 -1528 C ATOM 473 N VAL A 212 -11.398 15.454 -74.892 1.00 99.13 N ANISOU 473 N VAL A 212 12192 10924 14547 486 -594 -945 N ATOM 474 CA VAL A 212 -11.265 16.315 -73.724 1.00 96.18 C ANISOU 474 CA VAL A 212 11845 10571 14127 377 -531 -795 C ATOM 475 C VAL A 212 -9.911 16.117 -73.052 1.00 98.16 C ANISOU 475 C VAL A 212 12080 11039 14177 363 -384 -615 C ATOM 476 O VAL A 212 -9.010 16.941 -73.200 1.00 98.77 O ANISOU 476 O VAL A 212 12224 11326 13978 287 -420 -494 O ATOM 477 CB VAL A 212 -12.381 16.051 -72.697 1.00 97.10 C ANISOU 477 CB VAL A 212 11904 10433 14558 383 -457 -841 C ATOM 478 CG1 VAL A 212 -12.274 17.031 -71.536 1.00 81.63 C ANISOU 478 CG1 VAL A 212 9975 8499 12542 269 -407 -690 C ATOM 479 CG2 VAL A 212 -13.745 16.150 -73.360 1.00101.70 C ANISOU 479 CG2 VAL A 212 12496 10794 15352 404 -595 -1028 C ATOM 480 N SER A 213 -9.775 15.009 -72.328 1.00 91.97 N ANISOU 480 N SER A 213 11207 10203 13534 440 -219 -601 N ATOM 481 CA SER A 213 -8.547 14.695 -71.604 1.00 95.69 C ANISOU 481 CA SER A 213 11653 10864 13842 439 -62 -438 C ATOM 482 C SER A 213 -7.393 14.411 -72.562 1.00101.56 C ANISOU 482 C SER A 213 12420 11845 14323 478 -89 -412 C ATOM 483 O SER A 213 -6.225 14.429 -72.169 1.00 98.18 O ANISOU 483 O SER A 213 11997 11623 13684 456 6 -266 O ATOM 484 CB SER A 213 -8.767 13.504 -70.669 1.00 95.77 C ANISOU 484 CB SER A 213 11558 10744 14086 523 117 -446 C ATOM 485 OG SER A 213 -9.262 12.382 -71.378 1.00104.29 O ANISOU 485 OG SER A 213 12580 11702 15343 641 102 -606 O ATOM 486 N THR A 214 -7.731 14.127 -73.816 1.00101.65 N ANISOU 486 N THR A 214 12443 11828 14353 538 -218 -557 N ATOM 487 CA THR A 214 -6.734 13.894 -74.851 1.00103.07 C ANISOU 487 CA THR A 214 12646 12226 14289 579 -267 -548 C ATOM 488 C THR A 214 -5.905 15.144 -75.165 1.00 99.73 C ANISOU 488 C THR A 214 12320 12029 13544 469 -353 -422 C ATOM 489 O THR A 214 -4.772 15.032 -75.634 1.00103.08 O ANISOU 489 O THR A 214 12763 12684 13721 482 -345 -349 O ATOM 490 CB THR A 214 -7.392 13.392 -76.152 1.00102.08 C ANISOU 490 CB THR A 214 12513 12007 14267 668 -400 -742 C ATOM 491 OG1 THR A 214 -8.223 14.421 -76.701 1.00102.23 O ANISOU 491 OG1 THR A 214 12599 11938 14305 602 -569 -814 O ATOM 492 CG2 THR A 214 -8.237 12.157 -75.879 1.00102.09 C ANISOU 492 CG2 THR A 214 12417 11779 14593 776 -321 -872 C ATOM 493 N TRP A 215 -6.461 16.327 -74.910 1.00 92.33 N ANISOU 493 N TRP A 215 11443 11027 12609 362 -437 -397 N ATOM 494 CA TRP A 215 -5.771 17.572 -75.257 1.00 94.30 C ANISOU 494 CA TRP A 215 11787 11474 12568 255 -534 -286 C ATOM 495 C TRP A 215 -5.612 18.562 -74.099 1.00 94.25 C ANISOU 495 C TRP A 215 11814 11492 12504 134 -479 -134 C ATOM 496 O TRP A 215 -5.499 19.768 -74.321 1.00 90.22 O ANISOU 496 O TRP A 215 11386 11062 11834 31 -588 -75 O ATOM 497 CB TRP A 215 -6.489 18.266 -76.422 1.00 94.80 C ANISOU 497 CB TRP A 215 11915 11480 12626 234 -739 -407 C ATOM 498 CG TRP A 215 -7.980 18.370 -76.274 1.00 99.11 C ANISOU 498 CG TRP A 215 12449 11744 13465 236 -799 -545 C ATOM 499 CD1 TRP A 215 -8.911 17.495 -76.754 1.00104.28 C ANISOU 499 CD1 TRP A 215 13050 12206 14365 338 -826 -724 C ATOM 500 CD2 TRP A 215 -8.714 19.414 -75.617 1.00 99.26 C ANISOU 500 CD2 TRP A 215 12510 11643 13560 132 -842 -517 C ATOM 501 NE1 TRP A 215 -10.176 17.925 -76.434 1.00104.50 N ANISOU 501 NE1 TRP A 215 13086 12005 14616 303 -881 -809 N ATOM 502 CE2 TRP A 215 -10.082 19.100 -75.735 1.00100.72 C ANISOU 502 CE2 TRP A 215 12666 11567 14038 178 -892 -684 C ATOM 503 CE3 TRP A 215 -8.347 20.580 -74.939 1.00102.22 C ANISOU 503 CE3 TRP A 215 12946 12109 13786 7 -844 -368 C ATOM 504 CZ2 TRP A 215 -11.083 19.909 -75.199 1.00101.30 C ANISOU 504 CZ2 TRP A 215 12769 11470 14253 103 -945 -706 C ATOM 505 CZ3 TRP A 215 -9.343 21.382 -74.407 1.00 90.03 C ANISOU 505 CZ3 TRP A 215 11429 10393 12385 -67 -898 -390 C ATOM 506 CH2 TRP A 215 -10.693 21.043 -74.541 1.00 89.11 C ANISOU 506 CH2 TRP A 215 11283 10020 12554 -19 -948 -557 C ATOM 507 N LEU A 216 -5.585 18.053 -72.871 1.00 93.90 N ANISOU 507 N LEU A 216 11705 11384 12587 148 -311 -69 N ATOM 508 CA LEU A 216 -5.464 18.898 -71.683 1.00 89.99 C ANISOU 508 CA LEU A 216 11230 10904 12060 45 -246 72 C ATOM 509 C LEU A 216 -4.120 19.637 -71.596 1.00 83.70 C ANISOU 509 C LEU A 216 10489 10385 10928 -36 -230 249 C ATOM 510 O LEU A 216 -3.080 19.112 -71.994 1.00 87.33 O ANISOU 510 O LEU A 216 10941 11034 11208 9 -182 297 O ATOM 511 CB LEU A 216 -5.678 18.058 -70.423 1.00 79.79 C ANISOU 511 CB LEU A 216 9847 9492 10978 94 -59 100 C ATOM 512 CG LEU A 216 -6.933 18.337 -69.596 1.00 69.88 C ANISOU 512 CG LEU A 216 8568 7987 9995 65 -55 51 C ATOM 513 CD1 LEU A 216 -8.174 18.265 -70.463 1.00 79.66 C ANISOU 513 CD1 LEU A 216 9816 9022 11429 100 -199 -138 C ATOM 514 CD2 LEU A 216 -7.031 17.359 -68.438 1.00 67.27 C ANISOU 514 CD2 LEU A 216 8140 7559 9861 130 138 80 C ATOM 515 N SER A 217 -4.161 20.859 -71.067 1.00 79.98 N ANISOU 515 N SER A 217 10076 9936 10378 -154 -272 344 N ATOM 516 CA SER A 217 -2.980 21.718 -70.943 1.00 82.91 C ANISOU 516 CA SER A 217 10505 10555 10440 -245 -270 512 C ATOM 517 C SER A 217 -2.150 21.402 -69.700 1.00 80.37 C ANISOU 517 C SER A 217 10135 10333 10068 -248 -77 661 C ATOM 518 O SER A 217 -2.535 20.571 -68.882 1.00 79.90 O ANISOU 518 O SER A 217 9997 10142 10219 -185 56 638 O ATOM 519 CB SER A 217 -3.394 23.190 -70.920 1.00 90.80 C ANISOU 519 CB SER A 217 11587 11532 11379 -371 -405 548 C ATOM 520 OG SER A 217 -4.067 23.513 -69.714 1.00 75.97 O ANISOU 520 OG SER A 217 9685 9500 9680 -414 -341 579 O ATOM 521 N ASP A 218 -1.004 22.068 -69.574 1.00 83.09 N ANISOU 521 N ASP A 218 10527 10914 10132 -321 -61 814 N ATOM 522 CA ASP A 218 -0.043 21.771 -68.512 1.00 81.29 C ANISOU 522 CA ASP A 218 10257 10818 9811 -322 121 961 C ATOM 523 C ASP A 218 -0.571 21.972 -67.089 1.00 76.15 C ANISOU 523 C ASP A 218 9564 10029 9340 -354 227 1014 C ATOM 524 O ASP A 218 -0.259 21.183 -66.198 1.00 71.76 O ANISOU 524 O ASP A 218 8937 9475 8855 -298 400 1063 O ATOM 525 CB ASP A 218 1.214 22.625 -68.702 1.00 88.38 C ANISOU 525 CB ASP A 218 11222 11990 10368 -408 95 1111 C ATOM 526 CG ASP A 218 0.922 24.117 -68.643 1.00 92.52 C ANISOU 526 CG ASP A 218 11826 12510 10817 -539 -34 1162 C ATOM 527 OD1 ASP A 218 -0.219 24.515 -68.958 1.00 87.59 O ANISOU 527 OD1 ASP A 218 11224 11697 10359 -557 -156 1053 O ATOM 528 OD2 ASP A 218 1.834 24.890 -68.282 1.00 93.84 O ANISOU 528 OD2 ASP A 218 12032 12862 10759 -623 -15 1311 O ATOM 529 N GLY A 219 -1.368 23.013 -66.863 1.00 70.62 N ANISOU 529 N GLY A 219 8908 9212 8714 -440 125 1004 N ATOM 530 CA GLY A 219 -1.949 23.225 -65.549 1.00 65.07 C ANISOU 530 CA GLY A 219 8163 8369 8190 -468 212 1045 C ATOM 531 C GLY A 219 -3.118 22.290 -65.305 1.00 65.42 C ANISOU 531 C GLY A 219 8134 8156 8567 -377 256 908 C ATOM 532 O GLY A 219 -3.350 21.822 -64.180 1.00 60.46 O ANISOU 532 O GLY A 219 7434 7436 8102 -345 399 940 O ATOM 533 N ALA A 220 -3.833 21.993 -66.387 1.00 67.22 N ANISOU 533 N ALA A 220 8376 8272 8892 -332 134 753 N ATOM 534 CA ALA A 220 -5.030 21.174 -66.324 1.00 57.30 C ANISOU 534 CA ALA A 220 7057 6761 7954 -251 148 605 C ATOM 535 C ALA A 220 -4.697 19.736 -65.967 1.00 56.92 C ANISOU 535 C ALA A 220 6915 6706 8007 -133 320 594 C ATOM 536 O ALA A 220 -5.318 19.164 -65.077 1.00 56.12 O ANISOU 536 O ALA A 220 6740 6441 8142 -89 428 572 O ATOM 537 CB ALA A 220 -5.776 21.231 -67.642 1.00 66.35 C ANISOU 537 CB ALA A 220 8245 7812 9154 -230 -29 444 C ATOM 538 N VAL A 221 -3.703 19.165 -66.646 1.00 62.09 N ANISOU 538 N VAL A 221 7571 7541 8479 -84 345 613 N ATOM 539 CA VAL A 221 -3.295 17.790 -66.370 1.00 62.36 C ANISOU 539 CA VAL A 221 7520 7586 8587 28 505 605 C ATOM 540 C VAL A 221 -2.760 17.661 -64.950 1.00 61.40 C ANISOU 540 C VAL A 221 7348 7518 8463 18 693 749 C ATOM 541 O VAL A 221 -2.938 16.631 -64.304 1.00 62.51 O ANISOU 541 O VAL A 221 7403 7564 8784 102 837 731 O ATOM 542 CB VAL A 221 -2.212 17.281 -67.359 1.00 66.67 C ANISOU 542 CB VAL A 221 8084 8346 8902 78 494 613 C ATOM 543 CG1 VAL A 221 -2.786 17.118 -68.751 1.00 74.76 C ANISOU 543 CG1 VAL A 221 9136 9301 9968 119 330 452 C ATOM 544 CG2 VAL A 221 -0.999 18.206 -67.377 1.00 71.22 C ANISOU 544 CG2 VAL A 221 8730 9189 9143 -14 478 770 C ATOM 545 N ALA A 222 -2.121 18.718 -64.461 1.00 60.10 N ANISOU 545 N ALA A 222 7235 7502 8099 -84 691 892 N ATOM 546 CA ALA A 222 -1.543 18.692 -63.129 1.00 54.36 C ANISOU 546 CA ALA A 222 6464 6846 7345 -98 864 1035 C ATOM 547 C ALA A 222 -2.640 18.696 -62.072 1.00 46.39 C ANISOU 547 C ALA A 222 5399 5605 6621 -97 919 1009 C ATOM 548 O ALA A 222 -2.677 17.817 -61.203 1.00 42.68 O ANISOU 548 O ALA A 222 4844 5071 6301 -26 1083 1028 O ATOM 549 CB ALA A 222 -0.604 19.875 -62.932 1.00 49.75 C ANISOU 549 CB ALA A 222 5951 6478 6473 -210 834 1187 C ATOM 550 N ALA A 223 -3.558 19.655 -62.168 1.00 48.98 N ANISOU 550 N ALA A 223 5774 5805 7030 -171 780 962 N ATOM 551 CA ALA A 223 -4.623 19.739 -61.175 1.00 51.96 C ANISOU 551 CA ALA A 223 6104 5967 7672 -175 821 939 C ATOM 552 C ALA A 223 -5.489 18.483 -61.228 1.00 48.38 C ANISOU 552 C ALA A 223 5569 5304 7511 -61 878 802 C ATOM 553 O ALA A 223 -5.926 17.958 -60.195 1.00 45.13 O ANISOU 553 O ALA A 223 5078 4767 7303 -18 1008 815 O ATOM 554 CB ALA A 223 -5.466 20.988 -61.398 1.00 57.79 C ANISOU 554 CB ALA A 223 6913 6608 8435 -273 646 900 C ATOM 555 N CYS A 224 -5.675 17.968 -62.440 1.00 45.52 N ANISOU 555 N CYS A 224 5222 4913 7159 -8 785 675 N ATOM 556 CA CYS A 224 -6.492 16.792 -62.645 1.00 45.09 C ANISOU 556 CA CYS A 224 5096 4663 7374 100 820 534 C ATOM 557 C CYS A 224 -5.851 15.546 -62.030 1.00 54.21 C ANISOU 557 C CYS A 224 6162 5865 8571 197 1021 583 C ATOM 558 O CYS A 224 -6.520 14.750 -61.378 1.00 47.99 O ANISOU 558 O CYS A 224 5291 4903 8041 264 1123 538 O ATOM 559 CB CYS A 224 -6.699 16.609 -64.145 1.00 54.20 C ANISOU 559 CB CYS A 224 6293 5808 8493 131 666 395 C ATOM 560 SG CYS A 224 -8.030 15.497 -64.606 1.00 65.23 S ANISOU 560 SG CYS A 224 7622 6921 10241 242 642 187 S ATOM 561 N ARG A 225 -4.545 15.380 -62.233 1.00 55.04 N ANISOU 561 N ARG A 225 6284 6210 8420 203 1080 679 N ATOM 562 CA ARG A 225 -3.823 14.246 -61.654 1.00 46.32 C ANISOU 562 CA ARG A 225 5102 5174 7323 291 1273 736 C ATOM 563 C ARG A 225 -3.745 14.312 -60.129 1.00 45.82 C ANISOU 563 C ARG A 225 4983 5094 7334 277 1437 859 C ATOM 564 O ARG A 225 -3.858 13.287 -59.445 1.00 42.92 O ANISOU 564 O ARG A 225 4526 4643 7137 362 1592 856 O ATOM 565 CB ARG A 225 -2.409 14.168 -62.228 1.00 53.59 C ANISOU 565 CB ARG A 225 6062 6371 7929 293 1289 817 C ATOM 566 CG ARG A 225 -2.305 13.489 -63.579 1.00 58.84 C ANISOU 566 CG ARG A 225 6739 7061 8555 362 1201 697 C ATOM 567 CD ARG A 225 -1.111 14.021 -64.358 1.00 62.54 C ANISOU 567 CD ARG A 225 7285 7802 8676 316 1132 772 C ATOM 568 NE ARG A 225 -0.791 13.216 -65.534 1.00 78.38 N ANISOU 568 NE ARG A 225 9290 9868 10621 398 1081 678 N ATOM 569 CZ ARG A 225 -1.518 13.185 -66.647 1.00 81.57 C ANISOU 569 CZ ARG A 225 9719 10168 11107 421 925 530 C ATOM 570 NH1 ARG A 225 -2.629 13.903 -66.740 1.00 82.26 N ANISOU 570 NH1 ARG A 225 9835 10078 11343 368 805 455 N ATOM 571 NH2 ARG A 225 -1.140 12.425 -67.667 1.00 81.17 N ANISOU 571 NH2 ARG A 225 9662 10189 10990 501 888 453 N ATOM 572 N VAL A 226 -3.567 15.519 -59.595 1.00 46.10 N ANISOU 572 N VAL A 226 5068 5204 7244 171 1403 965 N ATOM 573 CA VAL A 226 -3.513 15.685 -58.147 1.00 42.54 C ANISOU 573 CA VAL A 226 4566 4740 6857 153 1548 1082 C ATOM 574 C VAL A 226 -4.864 15.313 -57.546 1.00 43.23 C ANISOU 574 C VAL A 226 4586 4551 7290 193 1573 994 C ATOM 575 O VAL A 226 -4.944 14.607 -56.526 1.00 38.54 O ANISOU 575 O VAL A 226 3904 3891 6847 253 1739 1034 O ATOM 576 CB VAL A 226 -3.146 17.130 -57.750 1.00 36.49 C ANISOU 576 CB VAL A 226 3870 4097 5898 28 1485 1202 C ATOM 577 CG1 VAL A 226 -3.236 17.310 -56.249 1.00 39.24 C ANISOU 577 CG1 VAL A 226 4160 4409 6341 16 1625 1308 C ATOM 578 CG2 VAL A 226 -1.754 17.478 -58.240 1.00 41.10 C ANISOU 578 CG2 VAL A 226 4514 4962 6139 -11 1477 1302 C ATOM 579 N ALA A 227 -5.928 15.752 -58.215 1.00 44.25 N ANISOU 579 N ALA A 227 4720 6018 6073 517 -138 434 N ATOM 580 CA ALA A 227 -7.273 15.418 -57.771 1.00 39.45 C ANISOU 580 CA ALA A 227 4076 5489 5425 480 -134 317 C ATOM 581 C ALA A 227 -7.527 13.915 -57.873 1.00 32.49 C ANISOU 581 C ALA A 227 3138 4678 4530 473 -35 333 C ATOM 582 O ALA A 227 -8.214 13.340 -57.031 1.00 30.39 O ANISOU 582 O ALA A 227 2836 4478 4231 447 -10 318 O ATOM 583 CB ALA A 227 -8.306 16.188 -58.578 1.00 35.16 C ANISOU 583 CB ALA A 227 3489 5052 4820 453 -105 278 C ATOM 584 N ALA A 228 -6.960 13.276 -58.893 1.00 27.56 N ANISOU 584 N ALA A 228 2500 4053 3918 494 36 365 N ATOM 585 CA ALA A 228 -7.129 11.832 -59.050 1.00 33.20 C ANISOU 585 CA ALA A 228 3166 4833 4617 487 167 371 C ATOM 586 C ALA A 228 -6.454 11.074 -57.907 1.00 35.41 C ANISOU 586 C ALA A 228 3472 4995 4988 509 177 478 C ATOM 587 O ALA A 228 -7.019 10.117 -57.348 1.00 35.63 O ANISOU 587 O ALA A 228 3512 5051 4975 447 269 422 O ATOM 588 CB ALA A 228 -6.578 11.373 -60.394 1.00 27.92 C ANISOU 588 CB ALA A 228 2496 4162 3952 510 237 383 C ATOM 589 N VAL A 229 -5.259 11.526 -57.535 1.00 35.77 N ANISOU 589 N VAL A 229 3607 4869 5115 541 85 580 N ATOM 590 CA VAL A 229 -4.552 10.894 -56.430 1.00 39.67 C ANISOU 590 CA VAL A 229 4160 5206 5704 543 79 681 C ATOM 591 C VAL A 229 -5.340 11.071 -55.139 1.00 33.40 C ANISOU 591 C VAL A 229 3353 4432 4904 518 20 647 C ATOM 592 O VAL A 229 -5.510 10.122 -54.366 1.00 32.27 O ANISOU 592 O VAL A 229 3277 4225 4759 460 74 626 O ATOM 593 CB VAL A 229 -3.133 11.472 -56.245 1.00 39.20 C ANISOU 593 CB VAL A 229 4217 5002 5675 531 4 742 C ATOM 594 CG1 VAL A 229 -2.457 10.838 -55.039 1.00 37.79 C ANISOU 594 CG1 VAL A 229 4113 4681 5565 503 -1 811 C ATOM 595 CG2 VAL A 229 -2.302 11.254 -57.494 1.00 37.48 C ANISOU 595 CG2 VAL A 229 4006 4774 5460 547 59 779 C ATOM 596 N PHE A 230 -5.854 12.278 -54.921 1.00 36.56 N ANISOU 596 N PHE A 230 3762 4897 5230 503 -82 569 N ATOM 597 CA PHE A 230 -6.626 12.526 -53.707 1.00 39.24 C ANISOU 597 CA PHE A 230 4099 5265 5547 477 -150 532 C ATOM 598 C PHE A 230 -7.906 11.699 -53.672 1.00 32.59 C ANISOU 598 C PHE A 230 3231 4564 4590 396 -54 412 C ATOM 599 O PHE A 230 -8.357 11.283 -52.604 1.00 35.10 O ANISOU 599 O PHE A 230 3641 4841 4855 323 -65 352 O ATOM 600 CB PHE A 230 -6.960 14.010 -53.572 1.00 37.16 C ANISOU 600 CB PHE A 230 3876 5030 5212 474 -247 442 C ATOM 601 CG PHE A 230 -5.785 14.859 -53.201 1.00 39.15 C ANISOU 601 CG PHE A 230 4242 5153 5480 491 -307 463 C ATOM 602 CD1 PHE A 230 -4.663 14.294 -52.618 1.00 52.69 C ANISOU 602 CD1 PHE A 230 6025 6735 7257 482 -300 551 C ATOM 603 CD2 PHE A 230 -5.799 16.221 -53.430 1.00 43.89 C ANISOU 603 CD2 PHE A 230 4846 5775 6054 496 -343 436 C ATOM 604 CE1 PHE A 230 -3.577 15.074 -52.273 1.00 61.69 C ANISOU 604 CE1 PHE A 230 7213 7792 8436 464 -325 606 C ATOM 605 CE2 PHE A 230 -4.719 17.006 -53.086 1.00 51.65 C ANISOU 605 CE2 PHE A 230 5862 6663 7097 483 -363 527 C ATOM 606 CZ PHE A 230 -3.605 16.431 -52.508 1.00 53.75 C ANISOU 606 CZ PHE A 230 6175 6815 7431 460 -356 607 C ATOM 607 N MET A 231 -8.481 11.447 -54.843 1.00 32.61 N ANISOU 607 N MET A 231 3177 4709 4504 372 49 331 N ATOM 608 CA MET A 231 -9.688 10.639 -54.918 1.00 33.62 C ANISOU 608 CA MET A 231 3358 4948 4467 251 154 163 C ATOM 609 C MET A 231 -9.394 9.197 -54.530 1.00 34.62 C ANISOU 609 C MET A 231 3616 4944 4593 175 253 135 C ATOM 610 O MET A 231 -10.117 8.611 -53.712 1.00 33.21 O ANISOU 610 O MET A 231 3523 4764 4332 83 275 41 O ATOM 611 CB MET A 231 -10.297 10.690 -56.321 1.00 36.00 C ANISOU 611 CB MET A 231 3565 5433 4679 244 244 89 C ATOM 612 CG MET A 231 -11.617 9.932 -56.447 1.00 29.73 C ANISOU 612 CG MET A 231 2819 4768 3707 116 347 -85 C ATOM 613 SD MET A 231 -12.361 10.065 -58.085 1.00 45.01 S ANISOU 613 SD MET A 231 4686 6876 5541 100 427 -163 S ATOM 614 CE MET A 231 -11.127 9.242 -59.088 1.00 53.03 C ANISOU 614 CE MET A 231 5691 7801 6657 154 526 -96 C ATOM 615 N GLN A 232 -8.329 8.629 -55.098 1.00 30.51 N ANISOU 615 N GLN A 232 3110 4313 4169 216 314 222 N ATOM 616 CA GLN A 232 -7.984 7.245 -54.769 1.00 35.31 C ANISOU 616 CA GLN A 232 3838 4791 4786 146 419 204 C ATOM 617 C GLN A 232 -7.665 7.118 -53.283 1.00 31.75 C ANISOU 617 C GLN A 232 3472 4198 4393 128 348 255 C ATOM 618 O GLN A 232 -8.119 6.183 -52.594 1.00 32.39 O ANISOU 618 O GLN A 232 3644 4243 4419 34 410 175 O ATOM 619 CB GLN A 232 -6.792 6.765 -55.599 1.00 36.37 C ANISOU 619 CB GLN A 232 3972 4822 5025 209 487 313 C ATOM 620 CG GLN A 232 -6.926 6.994 -57.091 1.00 38.05 C ANISOU 620 CG GLN A 232 4086 5170 5201 252 544 289 C ATOM 621 CD GLN A 232 -8.092 6.249 -57.700 1.00 44.71 C ANISOU 621 CD GLN A 232 4945 6157 5886 146 666 105 C ATOM 622 OE1 GLN A 232 -8.569 5.254 -57.152 1.00 51.89 O ANISOU 622 OE1 GLN A 232 5956 7027 6732 40 738 10 O ATOM 623 NE2 GLN A 232 -8.560 6.727 -58.843 1.00 51.34 N ANISOU 623 NE2 GLN A 232 5677 7167 6662 173 690 58 N ATOM 624 N TYR A 233 -6.927 8.107 -52.788 1.00 34.51 N ANISOU 624 N TYR A 233 3783 4476 4853 219 215 386 N ATOM 625 CA TYR A 233 -6.500 8.124 -51.398 1.00 37.63 C ANISOU 625 CA TYR A 233 4246 4738 5315 216 134 452 C ATOM 626 C TYR A 233 -7.692 8.195 -50.465 1.00 35.14 C ANISOU 626 C TYR A 233 3963 4504 4884 142 97 327 C ATOM 627 O TYR A 233 -7.728 7.518 -49.431 1.00 33.16 O ANISOU 627 O TYR A 233 3797 4171 4631 87 110 311 O ATOM 628 CB TYR A 233 -5.572 9.309 -51.147 1.00 28.46 C ANISOU 628 CB TYR A 233 3024 3505 4286 331 -13 608 C ATOM 629 CG TYR A 233 -5.046 9.382 -49.741 1.00 25.63 C ANISOU 629 CG TYR A 233 2729 3008 4001 333 -103 684 C ATOM 630 CD1 TYR A 233 -4.029 8.536 -49.320 1.00 33.07 C ANISOU 630 CD1 TYR A 233 3746 3781 5036 326 -53 786 C ATOM 631 CD2 TYR A 233 -5.559 10.296 -48.833 1.00 25.32 C ANISOU 631 CD2 TYR A 233 2672 3010 3938 344 -234 658 C ATOM 632 CE1 TYR A 233 -3.537 8.594 -48.033 1.00 30.37 C ANISOU 632 CE1 TYR A 233 3458 3325 4757 325 -130 855 C ATOM 633 CE2 TYR A 233 -5.075 10.364 -47.541 1.00 30.53 C ANISOU 633 CE2 TYR A 233 3388 3550 4663 349 -317 725 C ATOM 634 CZ TYR A 233 -4.061 9.510 -47.146 1.00 35.04 C ANISOU 634 CZ TYR A 233 4036 3974 5301 326 -256 802 C ATOM 635 OH TYR A 233 -3.563 9.563 -45.863 1.00 31.85 O ANISOU 635 OH TYR A 233 3705 3519 4876 290 -299 787 O ATOM 636 N GLY A 234 -8.691 8.981 -50.853 1.00 32.62 N ANISOU 636 N GLY A 234 3574 4355 4467 141 59 241 N ATOM 637 CA GLY A 234 -9.878 9.134 -50.039 1.00 28.19 C ANISOU 637 CA GLY A 234 3040 3885 3786 79 21 130 C ATOM 638 C GLY A 234 -10.694 7.860 -50.046 1.00 30.19 C ANISOU 638 C GLY A 234 3366 4177 3927 -36 152 1 C ATOM 639 O GLY A 234 -11.240 7.459 -49.018 1.00 29.35 O ANISOU 639 O GLY A 234 3326 4056 3770 -92 140 -53 O ATOM 640 N ILE A 235 -10.737 7.192 -51.196 1.00 30.89 N ANISOU 640 N ILE A 235 3444 4311 3983 -66 277 -46 N ATOM 641 CA ILE A 235 -11.521 5.970 -51.289 1.00 31.06 C ANISOU 641 CA ILE A 235 3532 4370 3900 -178 404 -174 C ATOM 642 C ILE A 235 -10.930 4.878 -50.403 1.00 35.34 C ANISOU 642 C ILE A 235 4172 4742 4513 -216 452 -140 C ATOM 643 O ILE A 235 -11.655 4.254 -49.628 1.00 37.06 O ANISOU 643 O ILE A 235 4448 4969 4663 -292 476 -220 O ATOM 644 CB ILE A 235 -11.631 5.465 -52.738 1.00 31.23 C ANISOU 644 CB ILE A 235 3520 4469 3875 -201 529 -232 C ATOM 645 CG1 ILE A 235 -12.521 6.399 -53.558 1.00 31.12 C ANISOU 645 CG1 ILE A 235 3407 4658 3758 -189 502 -294 C ATOM 646 CG2 ILE A 235 -12.201 4.054 -52.769 1.00 29.28 C ANISOU 646 CG2 ILE A 235 3356 4218 3552 -315 665 -349 C ATOM 647 CD1 ILE A 235 -12.743 5.947 -54.986 1.00 33.88 C ANISOU 647 CD1 ILE A 235 3715 5110 4047 -214 623 -363 C ATOM 648 N VAL A 236 -9.623 4.646 -50.497 1.00 35.93 N ANISOU 648 N VAL A 236 4261 4666 4724 -162 468 -15 N ATOM 649 CA VAL A 236 -9.015 3.633 -49.630 1.00 28.89 C ANISOU 649 CA VAL A 236 3456 3615 3907 -198 520 31 C ATOM 650 C VAL A 236 -9.084 4.034 -48.146 1.00 28.30 C ANISOU 650 C VAL A 236 3406 3493 3855 -189 406 66 C ATOM 651 O VAL A 236 -9.277 3.188 -47.251 1.00 27.59 O ANISOU 651 O VAL A 236 3378 3346 3758 -250 448 37 O ATOM 652 CB VAL A 236 -7.545 3.366 -50.020 1.00 31.55 C ANISOU 652 CB VAL A 236 3802 3797 4387 -137 558 179 C ATOM 653 CG1 VAL A 236 -7.000 2.175 -49.249 1.00 33.20 C ANISOU 653 CG1 VAL A 236 4100 3856 4661 -188 644 217 C ATOM 654 CG2 VAL A 236 -7.425 3.127 -51.516 1.00 22.87 C ANISOU 654 CG2 VAL A 236 2669 2752 3268 -125 655 155 C ATOM 655 N ALA A 237 -8.957 5.334 -47.889 1.00 31.82 N ANISOU 655 N ALA A 237 3796 3968 4327 -111 261 127 N ATOM 656 CA ALA A 237 -9.000 5.835 -46.520 1.00 25.39 C ANISOU 656 CA ALA A 237 2999 3114 3533 -93 140 160 C ATOM 657 C ALA A 237 -10.379 5.634 -45.899 1.00 26.63 C ANISOU 657 C ALA A 237 3181 3386 3551 -164 138 24 C ATOM 658 O ALA A 237 -10.498 5.471 -44.679 1.00 25.83 O ANISOU 658 O ALA A 237 3120 3239 3454 -177 91 29 O ATOM 659 CB ALA A 237 -8.605 7.306 -46.473 1.00 22.05 C ANISOU 659 CB ALA A 237 2508 2702 3166 6 -13 247 C ATOM 660 N ASN A 238 -11.416 5.637 -46.736 1.00 22.73 N ANISOU 660 N ASN A 238 2661 3044 2933 -208 190 -92 N ATOM 661 CA ASN A 238 -12.767 5.398 -46.244 1.00 28.89 C ANISOU 661 CA ASN A 238 3465 3938 3573 -278 195 -216 C ATOM 662 C ASN A 238 -12.868 4.039 -45.568 1.00 30.10 C ANISOU 662 C ASN A 238 3694 4016 3729 -353 288 -252 C ATOM 663 O ASN A 238 -13.288 3.932 -44.413 1.00 34.43 O ANISOU 663 O ASN A 238 4272 4557 4252 -367 238 -266 O ATOM 664 CB ASN A 238 -13.790 5.475 -47.382 1.00 30.10 C ANISOU 664 CB ASN A 238 3579 4262 3594 -323 258 -327 C ATOM 665 CG ASN A 238 -13.939 6.872 -47.946 1.00 27.76 C ANISOU 665 CG ASN A 238 3197 4073 3278 -254 166 -302 C ATOM 666 OD1 ASN A 238 -14.135 7.046 -49.146 1.00 30.93 O ANISOU 666 OD1 ASN A 238 3541 4571 3639 -256 221 -335 O ATOM 667 ND2 ASN A 238 -13.844 7.877 -47.085 1.00 28.19 N ANISOU 667 ND2 ASN A 238 3234 4112 3363 -192 27 -244 N ATOM 668 N TYR A 239 -12.468 3.002 -46.294 1.00 27.17 N ANISOU 668 N TYR A 239 3346 3588 3389 -397 425 -265 N ATOM 669 CA TYR A 239 -12.526 1.644 -45.773 1.00 30.82 C ANISOU 669 CA TYR A 239 3872 3975 3864 -471 531 -299 C ATOM 670 C TYR A 239 -11.534 1.400 -44.640 1.00 29.91 C ANISOU 670 C TYR A 239 3787 3700 3877 -438 500 -183 C ATOM 671 O TYR A 239 -11.825 0.646 -43.705 1.00 28.64 O ANISOU 671 O TYR A 239 3661 3506 3714 -483 530 -207 O ATOM 672 CB TYR A 239 -12.311 0.651 -46.913 1.00 28.27 C ANISOU 672 CB TYR A 239 3565 3629 3546 -523 688 -341 C ATOM 673 CG TYR A 239 -13.459 0.685 -47.892 1.00 28.36 C ANISOU 673 CG TYR A 239 3552 3808 3414 -576 732 -474 C ATOM 674 CD1 TYR A 239 -14.630 -0.018 -47.636 1.00 33.15 C ANISOU 674 CD1 TYR A 239 4189 4495 3911 -665 783 -595 C ATOM 675 CD2 TYR A 239 -13.393 1.454 -49.046 1.00 28.19 C ANISOU 675 CD2 TYR A 239 3471 3872 3366 -534 718 -473 C ATOM 676 CE1 TYR A 239 -15.695 0.023 -48.515 1.00 34.66 C ANISOU 676 CE1 TYR A 239 4358 4845 3966 -718 822 -711 C ATOM 677 CE2 TYR A 239 -14.452 1.502 -49.931 1.00 29.93 C ANISOU 677 CE2 TYR A 239 3663 4257 3452 -585 761 -591 C ATOM 678 CZ TYR A 239 -15.601 0.784 -49.661 1.00 37.32 C ANISOU 678 CZ TYR A 239 4636 5268 4276 -680 813 -710 C ATOM 679 OH TYR A 239 -16.661 0.828 -50.537 1.00 38.37 O ANISOU 679 OH TYR A 239 4742 5568 4271 -736 856 -822 O ATOM 680 N CYS A 240 -10.372 2.045 -44.700 1.00 27.24 N ANISOU 680 N CYS A 240 3428 3268 3652 -359 440 -53 N ATOM 681 CA CYS A 240 -9.430 1.896 -43.593 1.00 29.71 C ANISOU 681 CA CYS A 240 3766 3438 4083 -328 402 65 C ATOM 682 C CYS A 240 -9.951 2.531 -42.301 1.00 27.73 C ANISOU 682 C CYS A 240 3511 3228 3798 -306 270 57 C ATOM 683 O CYS A 240 -9.712 2.015 -41.203 1.00 26.61 O ANISOU 683 O CYS A 240 3396 3012 3704 -318 272 95 O ATOM 684 CB CYS A 240 -8.070 2.483 -43.967 1.00 31.53 C ANISOU 684 CB CYS A 240 3976 3561 4441 -247 360 215 C ATOM 685 SG CYS A 240 -7.197 1.501 -45.204 1.00 32.25 S ANISOU 685 SG CYS A 240 4089 3563 4601 -265 527 260 S ATOM 686 N TRP A 241 -10.685 3.634 -42.427 1.00 28.96 N ANISOU 686 N TRP A 241 3630 3506 3870 -273 160 8 N ATOM 687 CA TRP A 241 -11.235 4.289 -41.240 1.00 28.04 C ANISOU 687 CA TRP A 241 3511 3433 3709 -247 32 -4 C ATOM 688 C TRP A 241 -12.495 3.583 -40.755 1.00 28.22 C ANISOU 688 C TRP A 241 3560 3548 3613 -318 77 -122 C ATOM 689 O TRP A 241 -12.819 3.621 -39.568 1.00 20.92 O ANISOU 689 O TRP A 241 2649 2627 2672 -308 10 -122 O ATOM 690 CB TRP A 241 -11.511 5.773 -41.506 1.00 21.40 C ANISOU 690 CB TRP A 241 2621 2681 2829 -180 -103 -1 C ATOM 691 CG TRP A 241 -10.276 6.599 -41.326 1.00 25.62 C ANISOU 691 CG TRP A 241 3132 3107 3497 -95 -202 136 C ATOM 692 CD1 TRP A 241 -9.504 7.145 -42.309 1.00 26.99 C ANISOU 692 CD1 TRP A 241 3263 3249 3742 -45 -210 208 C ATOM 693 CD2 TRP A 241 -9.640 6.934 -40.085 1.00 25.23 C ANISOU 693 CD2 TRP A 241 3097 2963 3528 -49 -305 223 C ATOM 694 NE1 TRP A 241 -8.438 7.814 -41.757 1.00 26.26 N ANISOU 694 NE1 TRP A 241 3160 3046 3773 29 -316 338 N ATOM 695 CE2 TRP A 241 -8.498 7.699 -40.394 1.00 25.69 C ANISOU 695 CE2 TRP A 241 3123 2932 3705 24 -375 346 C ATOM 696 CE3 TRP A 241 -9.932 6.670 -38.743 1.00 23.63 C ANISOU 696 CE3 TRP A 241 2925 2746 3307 -60 -348 210 C ATOM 697 CZ2 TRP A 241 -7.645 8.198 -39.412 1.00 24.62 C ANISOU 697 CZ2 TRP A 241 2993 2693 3669 79 -486 454 C ATOM 698 CZ3 TRP A 241 -9.085 7.171 -37.767 1.00 28.36 C ANISOU 698 CZ3 TRP A 241 3525 3248 4001 -3 -456 314 C ATOM 699 CH2 TRP A 241 -7.954 7.926 -38.108 1.00 27.88 C ANISOU 699 CH2 TRP A 241 3438 3098 4057 63 -523 433 C ATOM 700 N LEU A 242 -13.210 2.940 -41.669 1.00 28.28 N ANISOU 700 N LEU A 242 3574 3634 3537 -386 189 -221 N ATOM 701 CA LEU A 242 -14.307 2.076 -41.256 1.00 34.35 C ANISOU 701 CA LEU A 242 4370 4472 4210 -460 249 -322 C ATOM 702 C LEU A 242 -13.737 0.902 -40.464 1.00 29.86 C ANISOU 702 C LEU A 242 3833 3776 3734 -490 328 -280 C ATOM 703 O LEU A 242 -14.334 0.437 -39.482 1.00 26.75 O ANISOU 703 O LEU A 242 3453 3404 3308 -512 320 -311 O ATOM 704 CB LEU A 242 -15.099 1.590 -42.472 1.00 35.92 C ANISOU 704 CB LEU A 242 4568 4771 4308 -532 358 -432 C ATOM 705 CG LEU A 242 -16.342 0.755 -42.181 1.00 34.88 C ANISOU 705 CG LEU A 242 4461 4726 4066 -612 416 -541 C ATOM 706 CD1 LEU A 242 -17.289 1.516 -41.262 1.00 29.39 C ANISOU 706 CD1 LEU A 242 3760 4134 3275 -583 289 -561 C ATOM 707 CD2 LEU A 242 -17.030 0.378 -43.482 1.00 30.03 C ANISOU 707 CD2 LEU A 242 3843 4210 3356 -681 517 -643 C ATOM 708 N LEU A 243 -12.550 0.458 -40.873 1.00 26.06 N ANISOU 708 N LEU A 243 3361 3167 3374 -483 403 -199 N ATOM 709 CA LEU A 243 -11.862 -0.612 -40.163 1.00 30.20 C ANISOU 709 CA LEU A 243 3909 3563 4002 -508 487 -139 C ATOM 710 C LEU A 243 -11.452 -0.145 -38.774 1.00 29.32 C ANISOU 710 C LEU A 243 3789 3401 3949 -450 374 -52 C ATOM 711 O LEU A 243 -11.614 -0.874 -37.792 1.00 29.96 O ANISOU 711 O LEU A 243 3876 3457 4049 -474 404 -51 O ATOM 712 CB LEU A 243 -10.636 -1.083 -40.948 1.00 33.45 C ANISOU 712 CB LEU A 243 4333 3848 4528 -507 589 -56 C ATOM 713 CG LEU A 243 -9.784 -2.171 -40.294 1.00 37.67 C ANISOU 713 CG LEU A 243 4891 4241 5181 -531 690 26 C ATOM 714 CD1 LEU A 243 -10.582 -3.451 -40.128 1.00 46.79 C ANISOU 714 CD1 LEU A 243 6062 5421 6293 -618 815 -74 C ATOM 715 CD2 LEU A 243 -8.525 -2.429 -41.105 1.00 33.91 C ANISOU 715 CD2 LEU A 243 4429 3642 4812 -515 773 128 C ATOM 716 N VAL A 244 -10.946 1.085 -38.685 1.00 28.03 N ANISOU 716 N VAL A 244 3606 3230 3815 -373 240 19 N ATOM 717 CA VAL A 244 -10.583 1.648 -37.386 1.00 27.40 C ANISOU 717 CA VAL A 244 3517 3110 3782 -315 118 95 C ATOM 718 C VAL A 244 -11.824 1.780 -36.506 1.00 25.70 C ANISOU 718 C VAL A 244 3299 3010 3454 -321 49 7 C ATOM 719 O VAL A 244 -11.778 1.572 -35.294 1.00 25.11 O ANISOU 719 O VAL A 244 3224 2912 3407 -305 11 39 O ATOM 720 CB VAL A 244 -9.907 3.035 -37.531 1.00 24.99 C ANISOU 720 CB VAL A 244 3190 2783 3523 -231 -23 177 C ATOM 721 CG1 VAL A 244 -9.855 3.761 -36.192 1.00 20.37 C ANISOU 721 CG1 VAL A 244 2597 2194 2951 -174 -169 220 C ATOM 722 CG2 VAL A 244 -8.512 2.891 -38.113 1.00 23.62 C ANISOU 722 CG2 VAL A 244 3018 2474 3483 -210 29 300 C ATOM 723 N GLU A 245 -12.947 2.089 -37.137 1.00 27.62 N ANISOU 723 N GLU A 245 3540 3387 3569 -344 40 -101 N ATOM 724 CA GLU A 245 -14.206 2.210 -36.424 1.00 34.13 C ANISOU 724 CA GLU A 245 4365 4330 4271 -350 -19 -182 C ATOM 725 C GLU A 245 -14.602 0.863 -35.810 1.00 30.84 C ANISOU 725 C GLU A 245 3961 3901 3856 -408 84 -216 C ATOM 726 O GLU A 245 -15.029 0.780 -34.640 1.00 27.22 O ANISOU 726 O GLU A 245 3497 3469 3375 -387 26 -214 O ATOM 727 CB GLU A 245 -15.293 2.706 -37.373 1.00 26.93 C ANISOU 727 CB GLU A 245 3449 3562 3222 -374 -26 -281 C ATOM 728 CG GLU A 245 -16.462 3.334 -36.673 1.00 36.80 C ANISOU 728 CG GLU A 245 4697 4938 4345 -352 -132 -335 C ATOM 729 CD GLU A 245 -16.209 4.777 -36.308 1.00 36.70 C ANISOU 729 CD GLU A 245 4668 4939 4339 -266 -290 -284 C ATOM 730 OE1 GLU A 245 -15.967 5.590 -37.226 1.00 32.04 O ANISOU 730 OE1 GLU A 245 4055 4369 3751 -244 -315 -275 O ATOM 731 OE2 GLU A 245 -16.251 5.097 -35.101 1.00 40.81 O ANISOU 731 OE2 GLU A 245 5193 5451 4864 -217 -389 -253 O ATOM 732 N GLY A 246 -14.404 -0.199 -36.587 1.00 31.94 N ANISOU 732 N GLY A 246 4113 3994 4029 -477 237 -240 N ATOM 733 CA GLY A 246 -14.709 -1.529 -36.097 1.00 25.90 C ANISOU 733 CA GLY A 246 3353 3207 3282 -535 347 -269 C ATOM 734 C GLY A 246 -13.773 -1.923 -34.975 1.00 25.69 C ANISOU 734 C GLY A 246 3313 3065 3382 -505 349 -163 C ATOM 735 O GLY A 246 -14.203 -2.527 -33.988 1.00 26.16 O ANISOU 735 O GLY A 246 3358 3142 3441 -512 359 -170 O ATOM 736 N LEU A 247 -12.504 -1.537 -35.099 1.00 27.34 N ANISOU 736 N LEU A 247 3522 3164 3700 -466 334 -56 N ATOM 737 CA LEU A 247 -11.512 -1.839 -34.068 1.00 27.52 C ANISOU 737 CA LEU A 247 3531 3077 3847 -437 335 59 C ATOM 738 C LEU A 247 -11.818 -1.135 -32.755 1.00 28.66 C ANISOU 738 C LEU A 247 3653 3272 3963 -373 187 80 C ATOM 739 O LEU A 247 -11.713 -1.728 -31.677 1.00 25.48 O ANISOU 739 O LEU A 247 3227 2846 3608 -369 205 118 O ATOM 740 CB LEU A 247 -10.113 -1.433 -34.523 1.00 27.17 C ANISOU 740 CB LEU A 247 3495 2912 3916 -405 334 178 C ATOM 741 CG LEU A 247 -9.363 -2.273 -35.550 1.00 31.20 C ANISOU 741 CG LEU A 247 4026 3326 4501 -453 492 211 C ATOM 742 CD1 LEU A 247 -8.121 -1.519 -35.976 1.00 27.49 C ANISOU 742 CD1 LEU A 247 3561 2762 4120 -398 442 333 C ATOM 743 CD2 LEU A 247 -8.988 -3.622 -34.969 1.00 39.70 C ANISOU 743 CD2 LEU A 247 5099 4321 5664 -502 634 252 C ATOM 744 N TYR A 248 -12.204 0.133 -32.849 1.00 27.95 N ANISOU 744 N TYR A 248 3566 3256 3796 -321 42 54 N ATOM 745 CA TYR A 248 -12.509 0.895 -31.656 1.00 25.55 C ANISOU 745 CA TYR A 248 3247 3002 3458 -255 -107 68 C ATOM 746 C TYR A 248 -13.745 0.354 -30.972 1.00 28.43 C ANISOU 746 C TYR A 248 3603 3473 3727 -272 -100 -13 C ATOM 747 O TYR A 248 -13.767 0.240 -29.749 1.00 30.74 O ANISOU 747 O TYR A 248 3872 3769 4038 -235 -150 21 O ATOM 748 CB TYR A 248 -12.716 2.376 -31.972 1.00 29.13 C ANISOU 748 CB TYR A 248 3706 3514 3846 -197 -256 53 C ATOM 749 CG TYR A 248 -13.261 3.132 -30.782 1.00 26.66 C ANISOU 749 CG TYR A 248 3385 3271 3473 -132 -406 44 C ATOM 750 CD1 TYR A 248 -12.413 3.604 -29.792 1.00 24.00 C ANISOU 750 CD1 TYR A 248 3035 2864 3220 -71 -502 136 C ATOM 751 CD2 TYR A 248 -14.628 3.345 -30.634 1.00 26.03 C ANISOU 751 CD2 TYR A 248 3312 3330 3251 -132 -451 -51 C ATOM 752 CE1 TYR A 248 -12.908 4.281 -28.694 1.00 32.39 C ANISOU 752 CE1 TYR A 248 4090 3991 4224 -8 -639 124 C ATOM 753 CE2 TYR A 248 -15.131 4.017 -29.539 1.00 31.99 C ANISOU 753 CE2 TYR A 248 4061 4147 3945 -67 -586 -56 C ATOM 754 CZ TYR A 248 -14.268 4.485 -28.573 1.00 33.12 C ANISOU 754 CZ TYR A 248 4192 4219 4174 -4 -680 28 C ATOM 755 OH TYR A 248 -14.768 5.157 -27.482 1.00 27.99 O ANISOU 755 OH TYR A 248 3538 3634 3461 64 -816 19 O ATOM 756 N LEU A 249 -14.779 0.036 -31.747 1.00 28.89 N ANISOU 756 N LEU A 249 3676 3621 3682 -325 -42 -116 N ATOM 757 CA LEU A 249 -15.988 -0.486 -31.126 1.00 24.29 C ANISOU 757 CA LEU A 249 3083 3139 3006 -340 -38 -185 C ATOM 758 C LEU A 249 -15.705 -1.834 -30.473 1.00 25.70 C ANISOU 758 C LEU A 249 3235 3254 3276 -373 78 -153 C ATOM 759 O LEU A 249 -16.154 -2.109 -29.351 1.00 26.62 O ANISOU 759 O LEU A 249 3322 3413 3380 -343 42 -145 O ATOM 760 CB LEU A 249 -17.112 -0.615 -32.153 1.00 30.04 C ANISOU 760 CB LEU A 249 3833 3972 3608 -399 10 -294 C ATOM 761 CG LEU A 249 -18.420 -1.216 -31.635 1.00 28.46 C ANISOU 761 CG LEU A 249 3627 3880 3309 -421 21 -362 C ATOM 762 CD1 LEU A 249 -19.005 -0.378 -30.512 1.00 20.35 C ANISOU 762 CD1 LEU A 249 2590 2934 2207 -339 -134 -348 C ATOM 763 CD2 LEU A 249 -19.412 -1.363 -32.772 1.00 29.00 C ANISOU 763 CD2 LEU A 249 3718 4042 3260 -489 79 -462 C ATOM 764 N HIS A 250 -14.906 -2.650 -31.157 1.00 23.57 N ANISOU 764 N HIS A 250 2970 2881 3104 -429 219 -125 N ATOM 765 CA HIS A 250 -14.571 -3.972 -30.642 1.00 35.33 C ANISOU 765 CA HIS A 250 4430 4302 4692 -468 350 -90 C ATOM 766 C HIS A 250 -13.784 -3.890 -29.339 1.00 36.50 C ANISOU 766 C HIS A 250 4539 4394 4936 -408 298 19 C ATOM 767 O HIS A 250 -14.042 -4.649 -28.403 1.00 36.61 O ANISOU 767 O HIS A 250 4508 4424 4980 -406 335 32 O ATOM 768 CB HIS A 250 -13.770 -4.765 -31.677 1.00 35.17 C ANISOU 768 CB HIS A 250 4429 4173 4760 -535 509 -73 C ATOM 769 CG HIS A 250 -13.146 -6.011 -31.129 1.00 38.01 C ANISOU 769 CG HIS A 250 4757 4440 5247 -567 646 -9 C ATOM 770 ND1 HIS A 250 -11.858 -6.044 -30.640 1.00 40.94 N ANISOU 770 ND1 HIS A 250 5112 4698 5747 -540 665 119 N ATOM 771 CD2 HIS A 250 -13.635 -7.265 -30.985 1.00 37.61 C ANISOU 771 CD2 HIS A 250 4681 4394 5216 -624 773 -50 C ATOM 772 CE1 HIS A 250 -11.580 -7.265 -30.222 1.00 39.80 C ANISOU 772 CE1 HIS A 250 4932 4495 5695 -580 804 156 C ATOM 773 NE2 HIS A 250 -12.641 -8.026 -30.420 1.00 40.80 N ANISOU 773 NE2 HIS A 250 5052 4690 5762 -630 871 52 N ATOM 774 N ASN A 251 -12.822 -2.976 -29.279 1.00 28.73 N ANISOU 774 N ASN A 251 3565 3347 4004 -358 212 99 N ATOM 775 CA ASN A 251 -12.066 -2.791 -28.051 1.00 35.16 C ANISOU 775 CA ASN A 251 4343 4114 4901 -300 150 202 C ATOM 776 C ASN A 251 -12.900 -2.164 -26.935 1.00 36.17 C ANISOU 776 C ASN A 251 4448 4352 4942 -232 3 172 C ATOM 777 O ASN A 251 -12.699 -2.468 -25.760 1.00 36.92 O ANISOU 777 O ASN A 251 4496 4445 5087 -197 -13 228 O ATOM 778 CB ASN A 251 -10.814 -1.955 -28.323 1.00 42.24 C ANISOU 778 CB ASN A 251 5261 4912 5877 -267 92 299 C ATOM 779 CG ASN A 251 -9.737 -2.745 -29.052 1.00 55.93 C ANISOU 779 CG ASN A 251 7006 6517 7729 -321 246 373 C ATOM 780 OD1 ASN A 251 -9.623 -3.962 -28.881 1.00 59.03 O ANISOU 780 OD1 ASN A 251 7376 6872 8183 -371 392 389 O ATOM 781 ND2 ASN A 251 -8.943 -2.059 -29.868 1.00 51.26 N ANISOU 781 ND2 ASN A 251 6447 5859 7172 -307 217 424 N ATOM 782 N LEU A 252 -13.839 -1.296 -27.302 1.00 34.00 N ANISOU 782 N LEU A 252 4204 4177 4536 -210 -101 88 N ATOM 783 CA LEU A 252 -14.709 -0.660 -26.316 1.00 35.39 C ANISOU 783 CA LEU A 252 4367 4463 4616 -142 -242 58 C ATOM 784 C LEU A 252 -15.642 -1.665 -25.650 1.00 35.50 C ANISOU 784 C LEU A 252 4343 4553 4594 -155 -184 19 C ATOM 785 O LEU A 252 -15.925 -1.567 -24.456 1.00 36.51 O ANISOU 785 O LEU A 252 4434 4732 4706 -92 -263 42 O ATOM 786 CB LEU A 252 -15.535 0.452 -26.965 1.00 29.84 C ANISOU 786 CB LEU A 252 3708 3853 3779 -123 -349 -19 C ATOM 787 CG LEU A 252 -16.546 1.173 -26.073 1.00 34.73 C ANISOU 787 CG LEU A 252 4324 4592 4278 -53 -493 -56 C ATOM 788 CD1 LEU A 252 -15.834 2.010 -25.021 1.00 36.87 C ANISOU 788 CD1 LEU A 252 4581 4828 4599 32 -628 17 C ATOM 789 CD2 LEU A 252 -17.483 2.034 -26.905 1.00 31.45 C ANISOU 789 CD2 LEU A 252 3950 4274 3725 -57 -554 -136 C ATOM 790 N LEU A 253 -16.119 -2.634 -26.426 1.00 34.28 N ANISOU 790 N LEU A 253 4194 4404 4427 -234 -47 -38 N ATOM 791 CA LEU A 253 -17.005 -3.658 -25.877 1.00 37.10 C ANISOU 791 CA LEU A 253 4510 4827 4761 -251 16 -72 C ATOM 792 C LEU A 253 -16.295 -4.563 -24.874 1.00 42.33 C ANISOU 792 C LEU A 253 5102 5424 5556 -239 90 13 C ATOM 793 O LEU A 253 -16.920 -5.110 -23.965 1.00 42.41 O ANISOU 793 O LEU A 253 5057 5500 5556 -212 89 14 O ATOM 794 CB LEU A 253 -17.602 -4.501 -27.001 1.00 34.66 C ANISOU 794 CB LEU A 253 4223 4528 4417 -345 150 -153 C ATOM 795 CG LEU A 253 -18.560 -3.743 -27.919 1.00 33.46 C ANISOU 795 CG LEU A 253 4127 4472 4115 -360 87 -245 C ATOM 796 CD1 LEU A 253 -19.001 -4.630 -29.061 1.00 32.09 C ANISOU 796 CD1 LEU A 253 3973 4298 3921 -459 229 -321 C ATOM 797 CD2 LEU A 253 -19.757 -3.241 -27.130 1.00 42.69 C ANISOU 797 CD2 LEU A 253 5289 5777 5156 -300 -38 -275 C ATOM 798 N GLY A 254 -14.985 -4.714 -25.043 1.00 43.98 N ANISOU 798 N GLY A 254 5309 5509 5892 -258 155 94 N ATOM 799 CA GLY A 254 -14.203 -5.575 -24.178 1.00 39.39 C ANISOU 799 CA GLY A 254 4659 4861 5445 -255 242 187 C ATOM 800 C GLY A 254 -13.738 -4.903 -22.902 1.00 45.65 C ANISOU 800 C GLY A 254 5411 5668 6264 -166 116 266 C ATOM 801 O GLY A 254 -13.119 -5.540 -22.052 1.00 54.76 O ANISOU 801 O GLY A 254 6498 6785 7525 -155 177 350 O ATOM 802 N LEU A 255 -14.042 -3.619 -22.755 1.00 46.20 N ANISOU 802 N LEU A 255 5520 5795 6239 -103 -56 240 N ATOM 803 CA LEU A 255 -13.548 -2.863 -21.612 1.00 54.59 C ANISOU 803 CA LEU A 255 6554 6864 7322 -18 -188 309 C ATOM 804 C LEU A 255 -14.496 -2.903 -20.418 1.00 58.94 C ANISOU 804 C LEU A 255 7052 7539 7804 53 -269 286 C ATOM 805 O LEU A 255 -15.703 -2.697 -20.547 1.00 57.87 O ANISOU 805 O LEU A 255 6938 7507 7543 68 -324 202 O ATOM 806 CB LEU A 255 -13.270 -1.411 -22.011 1.00 51.92 C ANISOU 806 CB LEU A 255 6282 6514 6933 20 -336 301 C ATOM 807 CG LEU A 255 -12.000 -1.217 -22.843 1.00 51.90 C ANISOU 807 CG LEU A 255 6312 6377 7029 -20 -286 368 C ATOM 808 CD1 LEU A 255 -11.654 0.254 -22.994 1.00 55.94 C ANISOU 808 CD1 LEU A 255 6869 6877 7509 33 -449 377 C ATOM 809 CD2 LEU A 255 -10.837 -1.981 -22.228 1.00 54.50 C ANISOU 809 CD2 LEU A 255 6590 6612 7508 -33 -190 487 C ATOM 810 N ASN A1000 -13.918 -3.181 -19.256 1.00 59.79 N ANISOU 810 N ASN A1000 7755 8605 6356 -169 -113 213 N ATOM 811 CA ASN A1000 -14.631 -3.179 -17.989 1.00 52.46 C ANISOU 811 CA ASN A1000 7090 7525 5318 -240 -138 81 C ATOM 812 C ASN A1000 -13.622 -3.014 -16.859 1.00 58.68 C ANISOU 812 C ASN A1000 7981 8174 6140 -304 -346 200 C ATOM 813 O ASN A1000 -12.447 -2.742 -17.112 1.00 56.75 O ANISOU 813 O ASN A1000 7598 7955 6011 -301 -471 377 O ATOM 814 CB ASN A1000 -15.444 -4.464 -17.814 1.00 49.70 C ANISOU 814 CB ASN A1000 6851 7173 4862 -197 47 -88 C ATOM 815 CG ASN A1000 -14.613 -5.718 -18.023 1.00 51.33 C ANISOU 815 CG ASN A1000 6976 7429 5099 -137 86 -13 C ATOM 816 OD1 ASN A1000 -13.384 -5.682 -17.983 1.00 58.92 O ANISOU 816 OD1 ASN A1000 7852 8390 6147 -144 -50 160 O ATOM 817 ND2 ASN A1000 -15.287 -6.839 -18.245 1.00 60.62 N ANISOU 817 ND2 ASN A1000 8178 8648 6206 -78 274 -148 N ATOM 818 N ILE A1001 -14.075 -3.178 -15.620 1.00 61.67 N ANISOU 818 N ILE A1001 8602 8405 6425 -355 -381 101 N ATOM 819 CA ILE A1001 -13.183 -3.076 -14.471 1.00 56.15 C ANISOU 819 CA ILE A1001 8020 7564 5749 -402 -573 194 C ATOM 820 C ILE A1001 -12.098 -4.147 -14.552 1.00 57.13 C ANISOU 820 C ILE A1001 8071 7717 5919 -354 -581 295 C ATOM 821 O ILE A1001 -10.932 -3.905 -14.209 1.00 57.80 O ANISOU 821 O ILE A1001 8118 7755 6089 -373 -752 442 O ATOM 822 CB ILE A1001 -13.971 -3.212 -13.146 1.00 58.51 C ANISOU 822 CB ILE A1001 8605 7702 5925 -445 -582 52 C ATOM 823 CG1 ILE A1001 -13.024 -3.376 -11.955 1.00 65.58 C ANISOU 823 CG1 ILE A1001 9628 8454 6835 -468 -758 135 C ATOM 824 CG2 ILE A1001 -14.946 -4.380 -13.216 1.00 51.96 C ANISOU 824 CG2 ILE A1001 7865 6894 4985 -399 -359 -121 C ATOM 825 CD1 ILE A1001 -12.254 -2.129 -11.612 1.00 68.04 C ANISOU 825 CD1 ILE A1001 9902 8705 7245 -521 -989 271 C ATOM 826 N PHE A1002 -12.479 -5.310 -15.071 1.00 55.11 N ANISOU 826 N PHE A1002 7783 7546 5611 -291 -393 215 N ATOM 827 CA PHE A1002 -11.568 -6.438 -15.176 1.00 61.31 C ANISOU 827 CA PHE A1002 8505 8369 6420 -244 -379 293 C ATOM 828 C PHE A1002 -10.458 -6.153 -16.176 1.00 65.88 C ANISOU 828 C PHE A1002 8829 9066 7137 -216 -452 481 C ATOM 829 O PHE A1002 -9.284 -6.345 -15.876 1.00 69.23 O ANISOU 829 O PHE A1002 9224 9459 7623 -222 -582 614 O ATOM 830 CB PHE A1002 -12.323 -7.704 -15.585 1.00 62.72 C ANISOU 830 CB PHE A1002 8694 8623 6516 -179 -151 158 C ATOM 831 CG PHE A1002 -13.442 -8.074 -14.650 1.00 68.39 C ANISOU 831 CG PHE A1002 9657 9224 7103 -198 -58 -33 C ATOM 832 CD1 PHE A1002 -13.193 -8.834 -13.518 1.00 65.08 C ANISOU 832 CD1 PHE A1002 9429 8679 6618 -207 -86 -62 C ATOM 833 CD2 PHE A1002 -14.743 -7.667 -14.906 1.00 65.99 C ANISOU 833 CD2 PHE A1002 9396 8933 6742 -203 62 -185 C ATOM 834 CE1 PHE A1002 -14.217 -9.177 -12.655 1.00 61.26 C ANISOU 834 CE1 PHE A1002 9174 8081 6020 -218 5 -234 C ATOM 835 CE2 PHE A1002 -15.773 -8.006 -14.048 1.00 61.39 C ANISOU 835 CE2 PHE A1002 9042 8238 6046 -221 150 -359 C ATOM 836 CZ PHE A1002 -15.510 -8.763 -12.921 1.00 67.78 C ANISOU 836 CZ PHE A1002 10038 8919 6795 -227 123 -381 C ATOM 837 N GLU A1003 -10.838 -5.683 -17.363 1.00 59.73 N ANISOU 837 N GLU A1003 7870 8420 6405 -180 -366 489 N ATOM 838 CA GLU A1003 -9.856 -5.346 -18.387 1.00 63.99 C ANISOU 838 CA GLU A1003 8161 9074 7079 -145 -423 667 C ATOM 839 C GLU A1003 -9.002 -4.144 -17.999 1.00 63.00 C ANISOU 839 C GLU A1003 8010 8869 7057 -208 -641 810 C ATOM 840 O GLU A1003 -7.823 -4.077 -18.345 1.00 64.40 O ANISOU 840 O GLU A1003 8042 9078 7348 -195 -743 978 O ATOM 841 CB GLU A1003 -10.551 -5.072 -19.722 1.00 54.91 C ANISOU 841 CB GLU A1003 6836 8078 5949 -81 -273 628 C ATOM 842 CG GLU A1003 -10.317 -6.153 -20.764 1.00 63.93 C ANISOU 842 CG GLU A1003 7807 9371 7111 18 -135 656 C ATOM 843 CD GLU A1003 -8.847 -6.352 -21.079 1.00 69.07 C ANISOU 843 CD GLU A1003 8305 10063 7877 35 -252 864 C ATOM 844 OE1 GLU A1003 -8.254 -7.320 -20.556 1.00 68.24 O ANISOU 844 OE1 GLU A1003 8261 9922 7744 33 -278 891 O ATOM 845 OE2 GLU A1003 -8.287 -5.545 -21.850 1.00 64.55 O ANISOU 845 OE2 GLU A1003 7552 9555 7420 53 -316 999 O ATOM 846 N MET A1004 -9.591 -3.209 -17.266 1.00 59.63 N ANISOU 846 N MET A1004 7727 8336 6594 -275 -715 742 N ATOM 847 CA MET A1004 -8.871 -2.012 -16.849 1.00 63.09 C ANISOU 847 CA MET A1004 8147 8692 7131 -335 -923 865 C ATOM 848 C MET A1004 -7.779 -2.361 -15.843 1.00 67.68 C ANISOU 848 C MET A1004 8817 9153 7745 -361 -1088 951 C ATOM 849 O MET A1004 -6.621 -1.949 -15.990 1.00 69.23 O ANISOU 849 O MET A1004 8888 9346 8071 -366 -1230 1113 O ATOM 850 CB MET A1004 -9.839 -0.989 -16.254 1.00 62.66 C ANISOU 850 CB MET A1004 8238 8553 7016 -399 -960 759 C ATOM 851 CG MET A1004 -9.168 0.219 -15.637 1.00 68.63 C ANISOU 851 CG MET A1004 9005 9207 7864 -464 -1184 869 C ATOM 852 SD MET A1004 -10.354 1.434 -15.041 1.00 64.16 S ANISOU 852 SD MET A1004 8596 8561 7221 -538 -1222 748 S ATOM 853 CE MET A1004 -11.351 0.414 -13.967 1.00 64.96 C ANISOU 853 CE MET A1004 8982 8561 7141 -546 -1126 551 C ATOM 854 N LEU A1005 -8.146 -3.145 -14.832 1.00 70.67 N ANISOU 854 N LEU A1005 9412 9433 8007 -371 -1064 838 N ATOM 855 CA LEU A1005 -7.163 -3.615 -13.867 1.00 73.88 C ANISOU 855 CA LEU A1005 9917 9728 8426 -382 -1201 900 C ATOM 856 C LEU A1005 -6.151 -4.536 -14.541 1.00 74.41 C ANISOU 856 C LEU A1005 9826 9892 8553 -328 -1174 1012 C ATOM 857 O LEU A1005 -4.979 -4.563 -14.170 1.00 79.23 O ANISOU 857 O LEU A1005 10413 10450 9240 -336 -1324 1130 O ATOM 858 CB LEU A1005 -7.848 -4.339 -12.708 1.00 75.45 C ANISOU 858 CB LEU A1005 10382 9806 8478 -389 -1153 746 C ATOM 859 CG LEU A1005 -8.677 -3.473 -11.762 1.00 79.74 C ANISOU 859 CG LEU A1005 11120 10219 8960 -445 -1221 648 C ATOM 860 CD1 LEU A1005 -9.327 -4.339 -10.699 1.00 80.41 C ANISOU 860 CD1 LEU A1005 11459 10191 8900 -436 -1150 500 C ATOM 861 CD2 LEU A1005 -7.811 -2.396 -11.128 1.00 80.42 C ANISOU 861 CD2 LEU A1005 11207 10200 9148 -489 -1465 765 C ATOM 862 N ARG A1006 -6.613 -5.281 -15.541 1.00 69.75 N ANISOU 862 N ARG A1006 9125 9446 7929 -272 -985 971 N ATOM 863 CA ARG A1006 -5.753 -6.203 -16.276 1.00 74.48 C ANISOU 863 CA ARG A1006 9567 10156 8576 -216 -943 1073 C ATOM 864 C ARG A1006 -4.700 -5.456 -17.084 1.00 71.26 C ANISOU 864 C ARG A1006 8929 9815 8333 -210 -1057 1263 C ATOM 865 O ARG A1006 -3.603 -5.963 -17.316 1.00 71.51 O ANISOU 865 O ARG A1006 8860 9881 8431 -188 -1116 1387 O ATOM 866 CB ARG A1006 -6.590 -7.087 -17.198 1.00 76.93 C ANISOU 866 CB ARG A1006 9804 10609 8818 -149 -713 978 C ATOM 867 CG ARG A1006 -5.897 -8.353 -17.663 1.00 76.79 C ANISOU 867 CG ARG A1006 9691 10685 8801 -92 -651 1038 C ATOM 868 CD ARG A1006 -6.909 -9.302 -18.276 1.00 88.00 C ANISOU 868 CD ARG A1006 11095 12212 10129 -28 -421 903 C ATOM 869 NE ARG A1006 -7.980 -9.620 -17.335 1.00 90.08 N ANISOU 869 NE ARG A1006 11597 12370 10261 -53 -338 714 N ATOM 870 CZ ARG A1006 -9.226 -9.918 -17.690 1.00 88.30 C ANISOU 870 CZ ARG A1006 11397 12193 9958 -20 -152 555 C ATOM 871 NH1 ARG A1006 -9.569 -9.935 -18.971 1.00 84.55 N ANISOU 871 NH1 ARG A1006 10726 11874 9524 45 -31 557 N ATOM 872 NH2 ARG A1006 -10.133 -10.194 -16.763 1.00 86.34 N ANISOU 872 NH2 ARG A1006 11374 11833 9596 -46 -87 391 N ATOM 873 N ILE A1007 -5.044 -4.248 -17.517 1.00 75.26 N ANISOU 873 N ILE A1007 9353 10337 8904 -230 -1085 1285 N ATOM 874 CA ILE A1007 -4.105 -3.404 -18.241 1.00 77.69 C ANISOU 874 CA ILE A1007 9449 10693 9375 -226 -1191 1463 C ATOM 875 C ILE A1007 -3.154 -2.707 -17.271 1.00 76.68 C ANISOU 875 C ILE A1007 9387 10417 9332 -287 -1422 1554 C ATOM 876 O ILE A1007 -1.953 -2.606 -17.532 1.00 81.09 O ANISOU 876 O ILE A1007 9810 10983 10016 -279 -1532 1710 O ATOM 877 CB ILE A1007 -4.841 -2.352 -19.101 1.00 76.17 C ANISOU 877 CB ILE A1007 9142 10577 9221 -217 -1125 1449 C ATOM 878 CG1 ILE A1007 -5.594 -3.034 -20.243 1.00 67.77 C ANISOU 878 CG1 ILE A1007 7970 9676 8104 -135 -905 1380 C ATOM 879 CG2 ILE A1007 -3.866 -1.332 -19.669 1.00 71.81 C ANISOU 879 CG2 ILE A1007 8395 10044 8844 -219 -1252 1631 C ATOM 880 CD1 ILE A1007 -6.484 -2.100 -21.034 1.00 66.74 C ANISOU 880 CD1 ILE A1007 7757 9620 7982 -117 -817 1331 C ATOM 881 N ASP A1008 -3.686 -2.243 -16.144 1.00 73.00 N ANISOU 881 N ASP A1008 9126 9813 8798 -344 -1496 1455 N ATOM 882 CA ASP A1008 -2.868 -1.495 -15.191 1.00 80.70 C ANISOU 882 CA ASP A1008 10166 10641 9855 -395 -1720 1529 C ATOM 883 C ASP A1008 -1.975 -2.366 -14.301 1.00 83.28 C ANISOU 883 C ASP A1008 10604 10877 10164 -390 -1815 1551 C ATOM 884 O ASP A1008 -1.060 -1.857 -13.656 1.00 87.15 O ANISOU 884 O ASP A1008 11108 11259 10745 -416 -2005 1633 O ATOM 885 CB ASP A1008 -3.763 -0.622 -14.312 1.00 85.28 C ANISOU 885 CB ASP A1008 10924 11109 10372 -451 -1775 1420 C ATOM 886 CG ASP A1008 -4.562 0.382 -15.117 1.00 80.98 C ANISOU 886 CG ASP A1008 10276 10645 9850 -463 -1707 1404 C ATOM 887 OD1 ASP A1008 -4.193 0.638 -16.282 1.00 76.64 O ANISOU 887 OD1 ASP A1008 9502 10216 9401 -429 -1661 1507 O ATOM 888 OD2 ASP A1008 -5.558 0.916 -14.585 1.00 75.37 O ANISOU 888 OD2 ASP A1008 9710 9875 9053 -503 -1698 1287 O ATOM 889 N GLU A1009 -2.230 -3.670 -14.268 1.00 80.89 N ANISOU 889 N GLU A1009 10375 10615 9744 -353 -1683 1474 N ATOM 890 CA GLU A1009 -1.473 -4.562 -13.391 1.00 77.87 C ANISOU 890 CA GLU A1009 10117 10146 9322 -345 -1756 1476 C ATOM 891 C GLU A1009 -0.721 -5.647 -14.157 1.00 75.66 C ANISOU 891 C GLU A1009 9699 9986 9060 -295 -1686 1557 C ATOM 892 O GLU A1009 0.299 -6.150 -13.689 1.00 85.48 O ANISOU 892 O GLU A1009 10971 11179 10327 -290 -1789 1619 O ATOM 893 CB GLU A1009 -2.402 -5.211 -12.361 1.00 82.52 C ANISOU 893 CB GLU A1009 10970 10644 9741 -347 -1680 1300 C ATOM 894 CG GLU A1009 -2.927 -4.259 -11.295 1.00 84.16 C ANISOU 894 CG GLU A1009 11356 10699 9923 -394 -1792 1228 C ATOM 895 CD GLU A1009 -1.867 -3.866 -10.279 1.00 99.71 C ANISOU 895 CD GLU A1009 13401 12520 11964 -409 -2021 1298 C ATOM 896 OE1 GLU A1009 -0.774 -4.472 -10.284 1.00100.66 O ANISOU 896 OE1 GLU A1009 13469 12647 12132 -384 -2081 1383 O ATOM 897 OE2 GLU A1009 -2.130 -2.949 -9.472 1.00105.93 O ANISOU 897 OE2 GLU A1009 14301 13186 12760 -443 -2143 1266 O ATOM 898 N GLY A1010 -1.235 -6.013 -15.325 1.00 69.94 N ANISOU 898 N GLY A1010 8829 9421 8323 -256 -1513 1553 N ATOM 899 CA GLY A1010 -0.620 -7.051 -16.131 1.00 67.07 C ANISOU 899 CA GLY A1010 8327 9186 7972 -204 -1436 1628 C ATOM 900 C GLY A1010 -0.848 -8.426 -15.536 1.00 77.09 C ANISOU 900 C GLY A1010 9759 10439 9094 -182 -1343 1520 C ATOM 901 O GLY A1010 -1.693 -8.596 -14.659 1.00 77.87 O ANISOU 901 O GLY A1010 10067 10444 9075 -199 -1296 1373 O ATOM 902 N LEU A1011 -0.087 -9.409 -16.005 1.00 85.13 N ANISOU 902 N LEU A1011 10681 11547 10118 -144 -1314 1596 N ATOM 903 CA LEU A1011 -0.201 -10.769 -15.489 1.00 91.71 C ANISOU 903 CA LEU A1011 11656 12375 10815 -121 -1224 1505 C ATOM 904 C LEU A1011 1.167 -11.435 -15.379 1.00 88.89 C ANISOU 904 C LEU A1011 11257 12024 10493 -112 -1330 1622 C ATOM 905 O LEU A1011 1.799 -11.753 -16.387 1.00 94.04 O ANISOU 905 O LEU A1011 11708 12809 11214 -81 -1312 1741 O ATOM 906 CB LEU A1011 -1.130 -11.603 -16.377 1.00 92.68 C ANISOU 906 CB LEU A1011 11707 12646 10861 -67 -995 1423 C ATOM 907 CG LEU A1011 -1.404 -13.046 -15.941 1.00 87.77 C ANISOU 907 CG LEU A1011 11219 12032 10097 -37 -871 1316 C ATOM 908 CD1 LEU A1011 -2.890 -13.357 -16.019 1.00 92.91 C ANISOU 908 CD1 LEU A1011 11952 12706 10644 -15 -671 1139 C ATOM 909 CD2 LEU A1011 -0.613 -14.025 -16.792 1.00 84.18 C ANISOU 909 CD2 LEU A1011 10596 11724 9663 9 -831 1420 C ATOM 910 N ARG A1012 1.617 -11.640 -14.146 1.00 88.10 N ANISOU 910 N ARG A1012 11352 11780 10343 -135 -1442 1585 N ATOM 911 CA ARG A1012 2.896 -12.287 -13.887 1.00 88.70 C ANISOU 911 CA ARG A1012 11422 11843 10436 -129 -1548 1675 C ATOM 912 C ARG A1012 2.685 -13.624 -13.190 1.00 84.10 C ANISOU 912 C ARG A1012 11024 11238 9689 -104 -1452 1560 C ATOM 913 O ARG A1012 2.203 -13.672 -12.059 1.00 85.91 O ANISOU 913 O ARG A1012 11484 11331 9826 -112 -1459 1437 O ATOM 914 CB ARG A1012 3.790 -11.386 -13.034 1.00 95.36 C ANISOU 914 CB ARG A1012 12327 12533 11374 -166 -1779 1737 C ATOM 915 CG ARG A1012 3.997 -9.994 -13.602 1.00 95.66 C ANISOU 915 CG ARG A1012 12196 12573 11579 -193 -1881 1845 C ATOM 916 CD ARG A1012 5.116 -9.977 -14.619 1.00 98.91 C ANISOU 916 CD ARG A1012 12365 13092 12126 -180 -1938 2023 C ATOM 917 NE ARG A1012 6.433 -10.097 -13.999 1.00109.53 N ANISOU 917 NE ARG A1012 13742 14348 13526 -191 -2117 2098 N ATOM 918 CZ ARG A1012 7.206 -9.063 -13.679 1.00104.12 C ANISOU 918 CZ ARG A1012 13017 13559 12984 -218 -2306 2181 C ATOM 919 NH1 ARG A1012 6.795 -7.825 -13.919 1.00100.86 N ANISOU 919 NH1 ARG A1012 12529 13121 12671 -242 -2340 2204 N ATOM 920 NH2 ARG A1012 8.391 -9.265 -13.118 1.00102.37 N ANISOU 920 NH2 ARG A1012 12829 13259 12807 -221 -2461 2236 N ATOM 921 N LEU A1013 3.044 -14.709 -13.866 1.00 84.43 N ANISOU 921 N LEU A1013 10967 11416 9698 -69 -1362 1602 N ATOM 922 CA LEU A1013 2.885 -16.041 -13.295 1.00 80.75 C ANISOU 922 CA LEU A1013 10659 10945 9078 -42 -1260 1501 C ATOM 923 C LEU A1013 3.939 -16.334 -12.229 1.00 83.50 C ANISOU 923 C LEU A1013 11156 11171 9399 -52 -1415 1520 C ATOM 924 O LEU A1013 3.784 -17.263 -11.436 1.00 84.67 O ANISOU 924 O LEU A1013 11492 11265 9413 -31 -1354 1416 O ATOM 925 CB LEU A1013 2.939 -17.099 -14.397 1.00 81.70 C ANISOU 925 CB LEU A1013 10614 11257 9172 0 -1117 1543 C ATOM 926 CG LEU A1013 1.849 -16.997 -15.467 1.00 81.28 C ANISOU 926 CG LEU A1013 10419 11333 9130 29 -943 1505 C ATOM 927 CD1 LEU A1013 1.979 -18.123 -16.480 1.00 80.10 C ANISOU 927 CD1 LEU A1013 10112 11368 8953 81 -814 1546 C ATOM 928 CD2 LEU A1013 0.465 -16.996 -14.832 1.00 78.73 C ANISOU 928 CD2 LEU A1013 10283 10929 8703 29 -812 1316 C ATOM 929 N LYS A1014 5.011 -15.547 -12.217 1.00 88.57 N ANISOU 929 N LYS A1014 11714 11767 10172 -77 -1611 1647 N ATOM 930 CA LYS A1014 6.024 -15.653 -11.171 1.00 94.38 C ANISOU 930 CA LYS A1014 12590 12371 10899 -83 -1778 1659 C ATOM 931 C LYS A1014 5.960 -14.439 -10.241 1.00 93.46 C ANISOU 931 C LYS A1014 12590 12075 10844 -109 -1931 1628 C ATOM 932 O LYS A1014 5.527 -13.359 -10.645 1.00 92.18 O ANISOU 932 O LYS A1014 12330 11913 10780 -134 -1954 1659 O ATOM 933 CB LYS A1014 7.425 -15.794 -11.777 1.00 91.87 C ANISOU 933 CB LYS A1014 12096 12127 10682 -86 -1897 1823 C ATOM 934 CG LYS A1014 8.481 -16.256 -10.779 1.00 99.27 C ANISOU 934 CG LYS A1014 13182 12957 11579 -80 -2036 1818 C ATOM 935 CD LYS A1014 9.866 -16.345 -11.399 1.00101.82 C ANISOU 935 CD LYS A1014 13328 13350 12009 -88 -2159 1978 C ATOM 936 CE LYS A1014 10.897 -16.761 -10.358 1.00107.48 C ANISOU 936 CE LYS A1014 14204 13951 12683 -79 -2301 1958 C ATOM 937 NZ LYS A1014 12.268 -16.874 -10.930 1.00117.98 N ANISOU 937 NZ LYS A1014 15370 15343 14114 -89 -2424 2109 N ATOM 938 N ILE A1015 6.384 -14.626 -8.995 1.00 94.24 N ANISOU 938 N ILE A1015 12899 12023 10884 -97 -2035 1565 N ATOM 939 CA ILE A1015 6.397 -13.547 -8.012 1.00 96.37 C ANISOU 939 CA ILE A1015 13293 12115 11210 -110 -2195 1532 C ATOM 940 C ILE A1015 7.371 -12.432 -8.393 1.00 94.65 C ANISOU 940 C ILE A1015 12895 11880 11188 -140 -2388 1679 C ATOM 941 O ILE A1015 8.429 -12.686 -8.969 1.00 90.46 O ANISOU 941 O ILE A1015 12216 11422 10734 -141 -2451 1797 O ATOM 942 CB ILE A1015 6.752 -14.076 -6.611 1.00 99.92 C ANISOU 942 CB ILE A1015 14002 12409 11554 -73 -2269 1436 C ATOM 943 CG1 ILE A1015 7.997 -14.962 -6.677 1.00104.39 C ANISOU 943 CG1 ILE A1015 14535 13019 12109 -53 -2325 1502 C ATOM 944 CG2 ILE A1015 5.585 -14.856 -6.028 1.00 95.85 C ANISOU 944 CG2 ILE A1015 13696 11865 10860 -43 -2088 1274 C ATOM 945 CD1 ILE A1015 8.234 -15.774 -5.424 1.00103.66 C ANISOU 945 CD1 ILE A1015 14702 12806 11877 -3 -2344 1390 C ATOM 946 N TYR A1016 6.997 -11.198 -8.070 1.00 97.31 N ANISOU 946 N TYR A1016 13246 12121 11607 -165 -2479 1670 N ATOM 947 CA TYR A1016 7.799 -10.025 -8.408 1.00 96.19 C ANISOU 947 CA TYR A1016 12934 11953 11661 -193 -2654 1801 C ATOM 948 C TYR A1016 7.536 -8.891 -7.423 1.00100.78 C ANISOU 948 C TYR A1016 13639 12363 12290 -206 -2796 1748 C ATOM 949 O TYR A1016 6.520 -8.890 -6.726 1.00 98.21 O ANISOU 949 O TYR A1016 13498 11966 11850 -199 -2731 1620 O ATOM 950 CB TYR A1016 7.491 -9.556 -9.833 1.00 95.82 C ANISOU 950 CB TYR A1016 12633 12063 11711 -218 -2564 1901 C ATOM 951 CG TYR A1016 6.101 -8.976 -9.989 1.00 99.58 C ANISOU 951 CG TYR A1016 13138 12553 12146 -235 -2448 1819 C ATOM 952 CD1 TYR A1016 4.992 -9.801 -10.119 1.00 98.09 C ANISOU 952 CD1 TYR A1016 13036 12434 11801 -218 -2243 1704 C ATOM 953 CD2 TYR A1016 5.897 -7.602 -10.004 1.00100.69 C ANISOU 953 CD2 TYR A1016 13217 12636 12404 -268 -2545 1852 C ATOM 954 CE1 TYR A1016 3.721 -9.276 -10.252 1.00 94.94 C ANISOU 954 CE1 TYR A1016 12668 12044 11363 -234 -2139 1620 C ATOM 955 CE2 TYR A1016 4.629 -7.069 -10.140 1.00 94.72 C ANISOU 955 CE2 TYR A1016 12493 11895 11602 -286 -2442 1773 C ATOM 956 CZ TYR A1016 3.546 -7.911 -10.267 1.00 92.97 C ANISOU 956 CZ TYR A1016 12361 11739 11222 -269 -2240 1656 C ATOM 957 OH TYR A1016 2.280 -7.390 -10.405 1.00 95.92 O ANISOU 957 OH TYR A1016 12769 12126 11549 -287 -2138 1569 O ATOM 958 N LYS A1017 8.455 -7.932 -7.354 1.00105.35 N ANISOU 958 N LYS A1017 14118 12872 13040 -221 -2990 1846 N ATOM 959 CA LYS A1017 8.235 -6.736 -6.548 1.00105.91 C ANISOU 959 CA LYS A1017 14268 12793 13179 -233 -3134 1813 C ATOM 960 C LYS A1017 7.389 -5.718 -7.313 1.00101.90 C ANISOU 960 C LYS A1017 13625 12352 12742 -277 -3077 1846 C ATOM 961 O LYS A1017 7.582 -5.513 -8.511 1.00102.52 O ANISOU 961 O LYS A1017 13477 12562 12916 -296 -3023 1956 O ATOM 962 CB LYS A1017 9.570 -6.115 -6.123 1.00109.74 C ANISOU 962 CB LYS A1017 14700 13170 13827 -226 -3370 1896 C ATOM 963 CG LYS A1017 10.523 -5.808 -7.269 1.00115.34 C ANISOU 963 CG LYS A1017 15133 13980 14711 -249 -3412 2062 C ATOM 964 CD LYS A1017 11.785 -5.123 -6.766 1.00115.32 C ANISOU 964 CD LYS A1017 15087 13850 14878 -241 -3648 2129 C ATOM 965 CE LYS A1017 12.713 -4.753 -7.912 1.00118.69 C ANISOU 965 CE LYS A1017 15237 14369 15491 -263 -3688 2298 C ATOM 966 NZ LYS A1017 13.944 -4.069 -7.427 1.00133.70 N ANISOU 966 NZ LYS A1017 17090 16139 17570 -254 -3916 2358 N ATOM 967 N ASP A1018 6.465 -5.068 -6.613 1.00102.46 N ANISOU 967 N ASP A1018 13838 12329 12764 -288 -3090 1750 N ATOM 968 CA ASP A1018 5.578 -4.097 -7.246 1.00103.72 C ANISOU 968 CA ASP A1018 13895 12545 12970 -331 -3034 1763 C ATOM 969 C ASP A1018 6.161 -2.690 -7.172 1.00106.07 C ANISOU 969 C ASP A1018 14079 12765 13457 -358 -3230 1855 C ATOM 970 O ASP A1018 7.321 -2.508 -6.802 1.00106.76 O ANISOU 970 O ASP A1018 14134 12773 13659 -343 -3400 1922 O ATOM 971 CB ASP A1018 4.191 -4.129 -6.596 1.00103.99 C ANISOU 971 CB ASP A1018 14137 12528 12845 -334 -2935 1610 C ATOM 972 CG ASP A1018 4.205 -3.640 -5.159 1.00109.79 C ANISOU 972 CG ASP A1018 15083 13069 13561 -320 -3099 1536 C ATOM 973 OD1 ASP A1018 5.247 -3.788 -4.485 1.00111.96 O ANISOU 973 OD1 ASP A1018 15407 13247 13887 -287 -3251 1562 O ATOM 974 OD2 ASP A1018 3.172 -3.109 -4.702 1.00111.74 O ANISOU 974 OD2 ASP A1018 15451 13262 13745 -337 -3078 1449 O ATOM 975 N TYR A1022 7.123 -4.661 -2.571 1.00 81.66 N ANISOU 975 N TYR A1022 12550 10122 8356 3194 -3575 -1380 N ATOM 976 CA TYR A1022 6.353 -5.759 -1.995 1.00 89.56 C ANISOU 976 CA TYR A1022 13935 11023 9071 3308 -3520 -1174 C ATOM 977 C TYR A1022 6.170 -6.887 -3.005 1.00 86.82 C ANISOU 977 C TYR A1022 13549 10839 8599 2831 -3590 -1156 C ATOM 978 O TYR A1022 5.909 -6.639 -4.182 1.00 84.22 O ANISOU 978 O TYR A1022 12799 10812 8389 2327 -3588 -1023 O ATOM 979 CB TYR A1022 4.986 -5.265 -1.512 1.00 90.21 C ANISOU 979 CB TYR A1022 13996 11206 9074 3396 -3325 -626 C ATOM 980 CG TYR A1022 5.051 -4.179 -0.461 1.00 91.23 C ANISOU 980 CG TYR A1022 14145 11185 9334 3770 -3166 -642 C ATOM 981 CD1 TYR A1022 6.147 -4.064 0.384 1.00 92.17 C ANISOU 981 CD1 TYR A1022 14511 11027 9483 4106 -3193 -1118 C ATOM 982 CD2 TYR A1022 4.013 -3.267 -0.314 1.00 93.59 C ANISOU 982 CD2 TYR A1022 14213 11643 9706 3726 -2972 -199 C ATOM 983 CE1 TYR A1022 6.208 -3.071 1.346 1.00 92.85 C ANISOU 983 CE1 TYR A1022 14614 11052 9611 4319 -3036 -1159 C ATOM 984 CE2 TYR A1022 4.065 -2.272 0.643 1.00 95.47 C ANISOU 984 CE2 TYR A1022 14452 11776 10047 3976 -2808 -238 C ATOM 985 CZ TYR A1022 5.164 -2.179 1.470 1.00 89.82 C ANISOU 985 CZ TYR A1022 13986 10830 9313 4248 -2842 -719 C ATOM 986 OH TYR A1022 5.220 -1.190 2.425 1.00 86.14 O ANISOU 986 OH TYR A1022 13521 10326 8882 4401 -2691 -754 O ATOM 987 N TYR A1023 6.318 -8.125 -2.544 1.00 90.47 N ANISOU 987 N TYR A1023 14415 11081 8879 2940 -3574 -1295 N ATOM 988 CA TYR A1023 6.135 -9.281 -3.415 1.00 85.26 C ANISOU 988 CA TYR A1023 13719 10527 8148 2452 -3538 -1282 C ATOM 989 C TYR A1023 4.693 -9.390 -3.899 1.00 86.05 C ANISOU 989 C TYR A1023 13587 10868 8242 2028 -3260 -716 C ATOM 990 O TYR A1023 3.748 -9.164 -3.141 1.00 81.59 O ANISOU 990 O TYR A1023 13137 10256 7607 2230 -3060 -342 O ATOM 991 CB TYR A1023 6.559 -10.566 -2.701 1.00 86.53 C ANISOU 991 CB TYR A1023 14366 10374 8139 2688 -3537 -1524 C ATOM 992 CG TYR A1023 8.055 -10.680 -2.520 1.00 82.38 C ANISOU 992 CG TYR A1023 13790 9597 7913 2861 -3554 -1948 C ATOM 993 CD1 TYR A1023 8.890 -10.879 -3.612 1.00 78.79 C ANISOU 993 CD1 TYR A1023 12970 9265 7700 2455 -3553 -2118 C ATOM 994 CD2 TYR A1023 8.634 -10.589 -1.262 1.00 83.97 C ANISOU 994 CD2 TYR A1023 14263 9471 8172 3424 -3551 -2065 C ATOM 995 CE1 TYR A1023 10.259 -10.980 -3.457 1.00 77.60 C ANISOU 995 CE1 TYR A1023 12720 8951 7816 2605 -3536 -2337 C ATOM 996 CE2 TYR A1023 10.003 -10.692 -1.097 1.00 85.91 C ANISOU 996 CE2 TYR A1023 14365 9584 8694 3555 -3592 -2250 C ATOM 997 CZ TYR A1023 10.811 -10.888 -2.199 1.00 80.45 C ANISOU 997 CZ TYR A1023 13308 9042 8215 3145 -3574 -2375 C ATOM 998 OH TYR A1023 12.174 -10.992 -2.042 1.00 78.96 O ANISOU 998 OH TYR A1023 12964 8787 8249 3250 -3596 -2478 O ATOM 999 N THR A1024 4.539 -9.756 -5.167 1.00 87.15 N ANISOU 999 N THR A1024 13402 11259 8450 1438 -3249 -659 N ATOM 1000 CA THR A1024 3.241 -9.779 -5.828 1.00 83.71 C ANISOU 1000 CA THR A1024 12673 11094 8038 968 -3007 -141 C ATOM 1001 C THR A1024 3.262 -10.841 -6.925 1.00 77.18 C ANISOU 1001 C THR A1024 11731 10405 7188 414 -3006 -198 C ATOM 1002 O THR A1024 4.321 -11.163 -7.458 1.00 76.23 O ANISOU 1002 O THR A1024 11593 10263 7107 315 -3218 -626 O ATOM 1003 CB THR A1024 2.895 -8.388 -6.427 1.00 84.13 C ANISOU 1003 CB THR A1024 12235 11432 8300 787 -2994 89 C ATOM 1004 OG1 THR A1024 2.999 -7.385 -5.409 1.00 84.09 O ANISOU 1004 OG1 THR A1024 12343 11286 8321 1321 -3019 93 O ATOM 1005 CG2 THR A1024 1.487 -8.359 -7.008 1.00 76.60 C ANISOU 1005 CG2 THR A1024 10992 10746 7366 339 -2731 653 C ATOM 1006 N ILE A1025 2.099 -11.395 -7.253 1.00 77.62 N ANISOU 1006 N ILE A1025 11713 10600 7178 56 -2768 231 N ATOM 1007 CA ILE A1025 2.003 -12.388 -8.315 1.00 79.05 C ANISOU 1007 CA ILE A1025 11768 10930 7338 -495 -2746 223 C ATOM 1008 C ILE A1025 0.633 -12.310 -8.983 1.00 78.25 C ANISOU 1008 C ILE A1025 11345 11117 7271 -971 -2495 777 C ATOM 1009 O ILE A1025 -0.289 -11.688 -8.453 1.00 71.76 O ANISOU 1009 O ILE A1025 10486 10330 6450 -826 -2318 1170 O ATOM 1010 CB ILE A1025 2.248 -13.817 -7.783 1.00 78.32 C ANISOU 1010 CB ILE A1025 12147 10574 7038 -360 -2739 32 C ATOM 1011 CG1 ILE A1025 2.783 -14.721 -8.897 1.00 76.79 C ANISOU 1011 CG1 ILE A1025 11840 10483 6855 -833 -2844 -219 C ATOM 1012 CG2 ILE A1025 0.982 -14.384 -7.155 1.00 77.31 C ANISOU 1012 CG2 ILE A1025 12230 10390 6753 -329 -2457 487 C ATOM 1013 CD1 ILE A1025 3.106 -16.121 -8.448 1.00 84.76 C ANISOU 1013 CD1 ILE A1025 13295 11238 7670 -718 -2855 -438 C ATOM 1014 N GLY A1026 0.508 -12.934 -10.151 1.00 76.58 N ANISOU 1014 N GLY A1026 10897 11112 7088 -1539 -2480 805 N ATOM 1015 CA GLY A1026 -0.728 -12.896 -10.908 1.00 69.94 C ANISOU 1015 CA GLY A1026 9726 10560 6287 -2038 -2258 1305 C ATOM 1016 C GLY A1026 -1.045 -11.496 -11.389 1.00 72.64 C ANISOU 1016 C GLY A1026 9611 11160 6828 -2164 -2250 1523 C ATOM 1017 O GLY A1026 -0.205 -10.833 -11.998 1.00 71.86 O ANISOU 1017 O GLY A1026 9256 11163 6882 -2241 -2450 1242 O ATOM 1018 N ILE A1027 -2.267 -11.050 -11.123 1.00 75.09 N ANISOU 1018 N ILE A1027 9818 11577 7137 -2190 -2017 2029 N ATOM 1019 CA ILE A1027 -2.703 -9.721 -11.531 1.00 67.16 C ANISOU 1019 CA ILE A1027 8384 10818 6314 -2309 -1982 2289 C ATOM 1020 C ILE A1027 -2.785 -8.768 -10.339 1.00 73.29 C ANISOU 1020 C ILE A1027 9319 11431 7095 -1730 -1963 2362 C ATOM 1021 O ILE A1027 -3.870 -8.488 -9.827 1.00 70.79 O ANISOU 1021 O ILE A1027 9017 11140 6740 -1647 -1745 2799 O ATOM 1022 CB ILE A1027 -4.073 -9.782 -12.238 1.00 75.32 C ANISOU 1022 CB ILE A1027 9111 12136 7372 -2815 -1731 2837 C ATOM 1023 CG1 ILE A1027 -4.081 -10.908 -13.275 1.00 71.47 C ANISOU 1023 CG1 ILE A1027 8541 11772 6844 -3357 -1723 2786 C ATOM 1024 CG2 ILE A1027 -4.410 -8.444 -12.890 1.00 75.28 C ANISOU 1024 CG2 ILE A1027 8608 12419 7575 -3022 -1723 3064 C ATOM 1025 CD1 ILE A1027 -5.414 -11.108 -13.950 1.00 82.37 C ANISOU 1025 CD1 ILE A1027 9656 13414 8229 -3856 -1475 3311 C ATOM 1026 N GLY A1028 -1.630 -8.300 -9.874 1.00 76.28 N ANISOU 1026 N GLY A1028 9833 11636 7516 -1323 -2192 1928 N ATOM 1027 CA GLY A1028 -1.593 -7.249 -8.873 1.00 79.48 C ANISOU 1027 CA GLY A1028 10329 11915 7955 -801 -2204 1962 C ATOM 1028 C GLY A1028 -1.966 -7.703 -7.475 1.00 79.30 C ANISOU 1028 C GLY A1028 10794 11592 7742 -303 -2080 2059 C ATOM 1029 O GLY A1028 -2.278 -6.879 -6.615 1.00 77.04 O ANISOU 1029 O GLY A1028 10578 11226 7468 89 -2020 2218 O ATOM 1030 N HIS A1029 -1.948 -9.012 -7.247 1.00 75.83 N ANISOU 1030 N HIS A1029 10694 10990 7129 -320 -2039 1969 N ATOM 1031 CA HIS A1029 -2.355 -9.561 -5.959 1.00 79.56 C ANISOU 1031 CA HIS A1029 11640 11182 7409 116 -1909 2076 C ATOM 1032 C HIS A1029 -1.227 -9.505 -4.934 1.00 82.95 C ANISOU 1032 C HIS A1029 12455 11283 7778 719 -2107 1620 C ATOM 1033 O HIS A1029 -0.215 -10.190 -5.078 1.00 82.86 O ANISOU 1033 O HIS A1029 12618 11141 7725 745 -2291 1182 O ATOM 1034 CB HIS A1029 -2.832 -11.004 -6.128 1.00 84.98 C ANISOU 1034 CB HIS A1029 12533 11827 7930 -153 -1776 2179 C ATOM 1035 CG HIS A1029 -3.283 -11.645 -4.853 1.00 89.17 C ANISOU 1035 CG HIS A1029 13548 12076 8257 263 -1635 2298 C ATOM 1036 ND1 HIS A1029 -4.392 -11.215 -4.156 1.00 92.84 N ANISOU 1036 ND1 HIS A1029 14051 12542 8681 434 -1409 2750 N ATOM 1037 CD2 HIS A1029 -2.776 -12.684 -4.148 1.00 85.65 C ANISOU 1037 CD2 HIS A1029 13569 11338 7637 542 -1687 2025 C ATOM 1038 CE1 HIS A1029 -4.548 -11.961 -3.077 1.00 90.44 C ANISOU 1038 CE1 HIS A1029 14218 11960 8186 800 -1328 2750 C ATOM 1039 NE2 HIS A1029 -3.581 -12.860 -3.049 1.00 88.05 N ANISOU 1039 NE2 HIS A1029 14183 11475 7799 873 -1493 2315 N ATOM 1040 N LEU A1030 -1.416 -8.699 -3.893 1.00 82.43 N ANISOU 1040 N LEU A1030 12527 11085 7706 1202 -2066 1726 N ATOM 1041 CA LEU A1030 -0.433 -8.582 -2.824 1.00 79.70 C ANISOU 1041 CA LEU A1030 12560 10424 7300 1807 -2237 1330 C ATOM 1042 C LEU A1030 -0.296 -9.903 -2.073 1.00 86.51 C ANISOU 1042 C LEU A1030 13932 10997 7941 2026 -2207 1186 C ATOM 1043 O LEU A1030 -1.292 -10.562 -1.771 1.00 91.01 O ANISOU 1043 O LEU A1030 14653 11547 8381 1950 -1982 1534 O ATOM 1044 CB LEU A1030 -0.827 -7.460 -1.857 1.00 82.05 C ANISOU 1044 CB LEU A1030 12893 10652 7629 2257 -2165 1537 C ATOM 1045 CG LEU A1030 0.112 -7.163 -0.686 1.00 83.96 C ANISOU 1045 CG LEU A1030 13505 10576 7820 2913 -2331 1168 C ATOM 1046 CD1 LEU A1030 1.454 -6.658 -1.190 1.00 89.25 C ANISOU 1046 CD1 LEU A1030 14020 11261 8630 2940 -2627 679 C ATOM 1047 CD2 LEU A1030 -0.520 -6.160 0.266 1.00 91.46 C ANISOU 1047 CD2 LEU A1030 14493 11473 8783 3311 -2208 1460 C ATOM 1048 N LEU A1031 0.940 -10.287 -1.774 1.00 85.31 N ANISOU 1048 N LEU A1031 14044 10624 7748 2298 -2435 673 N ATOM 1049 CA LEU A1031 1.197 -11.483 -0.980 1.00 85.79 C ANISOU 1049 CA LEU A1031 14610 10385 7601 2565 -2432 490 C ATOM 1050 C LEU A1031 1.551 -11.082 0.445 1.00 89.62 C ANISOU 1050 C LEU A1031 15476 10566 8008 3251 -2479 354 C ATOM 1051 O LEU A1031 0.838 -11.414 1.391 1.00 97.20 O ANISOU 1051 O LEU A1031 16740 11368 8821 3516 -2304 600 O ATOM 1052 CB LEU A1031 2.321 -12.320 -1.596 1.00 88.88 C ANISOU 1052 CB LEU A1031 15069 10719 7982 2395 -2648 7 C ATOM 1053 CG LEU A1031 2.040 -13.017 -2.930 1.00 81.89 C ANISOU 1053 CG LEU A1031 13897 10085 7132 1730 -2604 95 C ATOM 1054 CD1 LEU A1031 3.277 -13.755 -3.413 1.00 75.08 C ANISOU 1054 CD1 LEU A1031 13131 9135 6262 1642 -2840 -429 C ATOM 1055 CD2 LEU A1031 0.864 -13.972 -2.806 1.00 81.75 C ANISOU 1055 CD2 LEU A1031 14024 10077 6961 1526 -2339 498 C ATOM 1056 N THR A1032 2.660 -10.363 0.587 1.00 86.75 N ANISOU 1056 N THR A1032 15093 10123 7744 3536 -2718 -41 N ATOM 1057 CA THR A1032 3.061 -9.820 1.876 1.00 91.36 C ANISOU 1057 CA THR A1032 15945 10442 8324 4135 -2737 -206 C ATOM 1058 C THR A1032 4.003 -8.636 1.699 1.00 93.69 C ANISOU 1058 C THR A1032 15967 10784 8847 4234 -2898 -526 C ATOM 1059 O THR A1032 4.691 -8.516 0.684 1.00 93.46 O ANISOU 1059 O THR A1032 15715 10903 8892 3996 -3131 -741 O ATOM 1060 CB THR A1032 3.746 -10.882 2.756 1.00 98.56 C ANISOU 1060 CB THR A1032 17334 11013 9102 4445 -2764 -579 C ATOM 1061 OG1 THR A1032 4.031 -10.324 4.044 1.00101.92 O ANISOU 1061 OG1 THR A1032 17885 11275 9565 4815 -2636 -782 O ATOM 1062 CG2 THR A1032 5.040 -11.353 2.114 1.00 95.40 C ANISOU 1062 CG2 THR A1032 16976 10558 8713 4383 -3067 -1071 C ATOM 1063 N LYS A1033 4.011 -7.751 2.689 1.00 96.05 N ANISOU 1063 N LYS A1033 16255 10995 9245 4510 -2743 -572 N ATOM 1064 CA LYS A1033 4.914 -6.609 2.695 1.00 97.07 C ANISOU 1064 CA LYS A1033 16171 11162 9549 4592 -2846 -889 C ATOM 1065 C LYS A1033 6.259 -6.976 3.322 1.00 92.35 C ANISOU 1065 C LYS A1033 15877 10378 8835 4811 -2996 -1467 C ATOM 1066 O LYS A1033 7.178 -6.158 3.365 1.00 90.84 O ANISOU 1066 O LYS A1033 15559 10263 8692 4819 -3118 -1765 O ATOM 1067 CB LYS A1033 4.265 -5.434 3.424 1.00 99.81 C ANISOU 1067 CB LYS A1033 16341 11596 9986 4664 -2612 -645 C ATOM 1068 CG LYS A1033 2.981 -4.972 2.750 1.00 98.57 C ANISOU 1068 CG LYS A1033 15849 11678 9926 4408 -2486 -75 C ATOM 1069 CD LYS A1033 2.163 -4.045 3.626 1.00110.62 C ANISOU 1069 CD LYS A1033 17267 13238 11526 4498 -2225 197 C ATOM 1070 CE LYS A1033 0.835 -3.718 2.958 1.00111.33 C ANISOU 1070 CE LYS A1033 17049 13567 11682 4219 -2095 776 C ATOM 1071 NZ LYS A1033 -0.054 -2.906 3.832 1.00124.15 N ANISOU 1071 NZ LYS A1033 18579 15205 13390 4295 -1844 1047 N ATOM 1072 N SER A1034 6.361 -8.210 3.807 1.00 88.73 N ANISOU 1072 N SER A1034 15808 9760 8146 4916 -3011 -1576 N ATOM 1073 CA SER A1034 7.601 -8.714 4.384 1.00 90.29 C ANISOU 1073 CA SER A1034 16013 9979 8316 4880 -3154 -1769 C ATOM 1074 C SER A1034 8.678 -8.880 3.312 1.00 89.52 C ANISOU 1074 C SER A1034 15569 9918 8525 4682 -3385 -1860 C ATOM 1075 O SER A1034 8.426 -9.459 2.255 1.00 90.85 O ANISOU 1075 O SER A1034 15750 9938 8832 4642 -3451 -1872 O ATOM 1076 CB SER A1034 7.359 -10.045 5.099 1.00 88.43 C ANISOU 1076 CB SER A1034 16113 9610 7875 4963 -3090 -1669 C ATOM 1077 OG SER A1034 8.570 -10.581 5.604 1.00 92.91 O ANISOU 1077 OG SER A1034 16572 10192 8538 4925 -3224 -1712 O ATOM 1078 N PRO A1035 9.894 -8.383 3.596 1.00 88.24 N ANISOU 1078 N PRO A1035 13193 11709 8627 2243 -4674 135 N ATOM 1079 CA PRO A1035 11.052 -8.486 2.700 1.00 88.16 C ANISOU 1079 CA PRO A1035 13127 11553 8818 2106 -4659 236 C ATOM 1080 C PRO A1035 11.421 -9.934 2.382 1.00 86.72 C ANISOU 1080 C PRO A1035 13187 11261 8501 2125 -4534 485 C ATOM 1081 O PRO A1035 11.938 -10.205 1.299 1.00 80.78 O ANISOU 1081 O PRO A1035 12410 10355 7929 1947 -4524 564 O ATOM 1082 CB PRO A1035 12.167 -7.806 3.494 1.00 93.98 C ANISOU 1082 CB PRO A1035 13763 12370 9574 2223 -4665 213 C ATOM 1083 CG PRO A1035 11.459 -6.855 4.392 1.00 89.72 C ANISOU 1083 CG PRO A1035 13125 11979 8986 2315 -4732 33 C ATOM 1084 CD PRO A1035 10.195 -7.564 4.781 1.00 89.73 C ANISOU 1084 CD PRO A1035 13288 12048 8757 2408 -4704 36 C ATOM 1085 N SER A1036 11.171 -10.843 3.316 1.00 91.47 N ANISOU 1085 N SER A1036 13977 11936 8843 2289 -4322 605 N ATOM 1086 CA SER A1036 11.504 -12.249 3.119 1.00 91.30 C ANISOU 1086 CA SER A1036 14115 11807 8769 2236 -3991 842 C ATOM 1087 C SER A1036 10.760 -12.834 1.924 1.00 89.91 C ANISOU 1087 C SER A1036 13905 11475 8781 1931 -3777 872 C ATOM 1088 O SER A1036 9.552 -12.647 1.779 1.00 88.39 O ANISOU 1088 O SER A1036 13637 11307 8641 1810 -3688 747 O ATOM 1089 CB SER A1036 11.182 -13.058 4.376 1.00 90.35 C ANISOU 1089 CB SER A1036 14145 11801 8381 2419 -3704 934 C ATOM 1090 OG SER A1036 11.403 -14.444 4.174 1.00 85.73 O ANISOU 1090 OG SER A1036 13714 11111 7749 2357 -3363 1159 O ATOM 1091 N LEU A1037 11.495 -13.548 1.076 1.00 85.29 N ANISOU 1091 N LEU A1037 13377 10732 8297 1809 -3695 1038 N ATOM 1092 CA LEU A1037 10.934 -14.156 -0.123 1.00 79.46 C ANISOU 1092 CA LEU A1037 12610 9835 7745 1516 -3495 1085 C ATOM 1093 C LEU A1037 10.134 -15.406 0.220 1.00 83.91 C ANISOU 1093 C LEU A1037 13301 10393 8186 1474 -3052 1204 C ATOM 1094 O LEU A1037 9.048 -15.642 -0.322 1.00 87.23 O ANISOU 1094 O LEU A1037 13672 10769 8703 1275 -2870 1150 O ATOM 1095 CB LEU A1037 12.054 -14.495 -1.107 1.00 86.22 C ANISOU 1095 CB LEU A1037 13486 10529 8745 1409 -3565 1227 C ATOM 1096 CG LEU A1037 11.674 -15.254 -2.376 1.00 80.43 C ANISOU 1096 CG LEU A1037 12740 9618 8201 1111 -3347 1310 C ATOM 1097 CD1 LEU A1037 10.670 -14.453 -3.177 1.00 77.55 C ANISOU 1097 CD1 LEU A1037 12196 9233 8036 905 -3462 1113 C ATOM 1098 CD2 LEU A1037 12.912 -15.553 -3.206 1.00 80.12 C ANISOU 1098 CD2 LEU A1037 12729 9434 8280 1042 -3439 1453 C ATOM 1099 N ASN A1038 10.681 -16.203 1.132 1.00 90.40 N ANISOU 1099 N ASN A1038 14290 11264 8793 1666 -2879 1366 N ATOM 1100 CA ASN A1038 10.015 -17.411 1.597 1.00 85.78 C ANISOU 1100 CA ASN A1038 13843 10685 8065 1660 -2457 1489 C ATOM 1101 C ASN A1038 8.700 -17.105 2.304 1.00 84.99 C ANISOU 1101 C ASN A1038 13704 10719 7870 1694 -2364 1333 C ATOM 1102 O ASN A1038 7.754 -17.888 2.236 1.00 84.78 O ANISOU 1102 O ASN A1038 13724 10667 7820 1577 -2037 1368 O ATOM 1103 CB ASN A1038 10.935 -18.195 2.533 1.00 91.84 C ANISOU 1103 CB ASN A1038 14791 11494 8608 1889 -2332 1681 C ATOM 1104 CG ASN A1038 12.009 -18.966 1.790 1.00 87.13 C ANISOU 1104 CG ASN A1038 14276 10741 8090 1813 -2270 1885 C ATOM 1105 OD1 ASN A1038 12.343 -18.648 0.651 1.00 79.81 O ANISOU 1105 OD1 ASN A1038 13253 9688 7382 1632 -2427 1865 O ATOM 1106 ND2 ASN A1038 12.554 -19.991 2.438 1.00 91.18 N ANISOU 1106 ND2 ASN A1038 14964 11258 8422 1950 -2040 2083 N ATOM 1107 N ALA A1039 8.648 -15.966 2.987 1.00 87.27 N ANISOU 1107 N ALA A1039 13905 11151 8102 1855 -2652 1160 N ATOM 1108 CA ALA A1039 7.428 -15.538 3.659 1.00 88.81 C ANISOU 1108 CA ALA A1039 14048 11480 8216 1893 -2606 992 C ATOM 1109 C ALA A1039 6.321 -15.249 2.650 1.00 98.31 C ANISOU 1109 C ALA A1039 15114 12611 9626 1621 -2576 857 C ATOM 1110 O ALA A1039 5.143 -15.453 2.936 1.00102.29 O ANISOU 1110 O ALA A1039 15616 13170 10079 1570 -2373 784 O ATOM 1111 CB ALA A1039 7.697 -14.313 4.521 1.00 88.81 C ANISOU 1111 CB ALA A1039 13971 11642 8132 2115 -2950 832 C ATOM 1112 N ALA A1040 6.707 -14.774 1.469 1.00 94.22 N ANISOU 1112 N ALA A1040 14485 11973 9343 1448 -2780 823 N ATOM 1113 CA ALA A1040 5.748 -14.497 0.404 1.00 87.48 C ANISOU 1113 CA ALA A1040 13497 11039 8703 1179 -2765 703 C ATOM 1114 C ALA A1040 5.317 -15.787 -0.277 1.00 88.26 C ANISOU 1114 C ALA A1040 13678 11005 8851 973 -2376 854 C ATOM 1115 O ALA A1040 4.128 -16.001 -0.556 1.00 87.41 O ANISOU 1115 O ALA A1040 13531 10891 8790 816 -2179 782 O ATOM 1116 CB ALA A1040 6.343 -13.535 -0.609 1.00 83.27 C ANISOU 1116 CB ALA A1040 12816 10424 8400 1071 -3123 616 C ATOM 1117 N LYS A1041 6.293 -16.654 -0.530 1.00 88.38 N ANISOU 1117 N LYS A1041 13810 10917 8855 976 -2263 1065 N ATOM 1118 CA LYS A1041 6.021 -17.938 -1.160 1.00 87.59 C ANISOU 1118 CA LYS A1041 13799 10685 8797 791 -1891 1229 C ATOM 1119 C LYS A1041 5.120 -18.804 -0.288 1.00 90.64 C ANISOU 1119 C LYS A1041 14305 11149 8985 853 -1521 1275 C ATOM 1120 O LYS A1041 4.326 -19.592 -0.799 1.00 86.39 O ANISOU 1120 O LYS A1041 13789 10536 8499 664 -1216 1319 O ATOM 1121 CB LYS A1041 7.329 -18.673 -1.456 1.00 83.02 C ANISOU 1121 CB LYS A1041 13331 9994 8219 817 -1856 1450 C ATOM 1122 CG LYS A1041 8.232 -17.947 -2.438 1.00 81.45 C ANISOU 1122 CG LYS A1041 13021 9697 8228 729 -2191 1422 C ATOM 1123 CD LYS A1041 9.587 -18.629 -2.595 1.00 86.60 C ANISOU 1123 CD LYS A1041 13790 10255 8860 785 -2174 1635 C ATOM 1124 CE LYS A1041 9.514 -19.861 -3.487 1.00 82.73 C ANISOU 1124 CE LYS A1041 13369 9601 8464 565 -1847 1809 C ATOM 1125 NZ LYS A1041 8.918 -21.047 -2.809 1.00 98.37 N ANISOU 1125 NZ LYS A1041 15502 11611 10263 606 -1428 1932 N ATOM 1126 N SER A1042 5.239 -18.650 1.027 1.00 94.63 N ANISOU 1126 N SER A1042 14885 11807 9264 1115 -1549 1261 N ATOM 1127 CA SER A1042 4.406 -19.407 1.954 1.00100.13 C ANISOU 1127 CA SER A1042 15696 12590 9757 1195 -1216 1296 C ATOM 1128 C SER A1042 2.948 -18.980 1.852 1.00 99.47 C ANISOU 1128 C SER A1042 15505 12562 9727 1069 -1159 1103 C ATOM 1129 O SER A1042 2.045 -19.818 1.833 1.00 94.13 O ANISOU 1129 O SER A1042 14889 11866 9012 962 -816 1141 O ATOM 1130 CB SER A1042 4.904 -19.234 3.391 1.00102.59 C ANISOU 1130 CB SER A1042 16101 13060 9819 1512 -1293 1314 C ATOM 1131 OG SER A1042 4.825 -17.880 3.802 1.00106.24 O ANISOU 1131 OG SER A1042 16434 13647 10287 1626 -1649 1109 O ATOM 1132 N GLU A1043 2.725 -17.670 1.782 1.00103.16 N ANISOU 1132 N GLU A1043 15813 13100 10284 1080 -1497 893 N ATOM 1133 CA GLU A1043 1.376 -17.145 1.637 1.00101.92 C ANISOU 1133 CA GLU A1043 15539 12997 10191 959 -1482 694 C ATOM 1134 C GLU A1043 0.792 -17.518 0.281 1.00 97.16 C ANISOU 1134 C GLU A1043 14866 12242 9809 647 -1336 697 C ATOM 1135 O GLU A1043 -0.410 -17.760 0.162 1.00 93.79 O ANISOU 1135 O GLU A1043 14414 11828 9394 517 -1124 620 O ATOM 1136 CB GLU A1043 1.365 -15.626 1.822 1.00102.35 C ANISOU 1136 CB GLU A1043 15434 13153 10302 1043 -1897 474 C ATOM 1137 CG GLU A1043 1.959 -15.165 3.142 1.00111.87 C ANISOU 1137 CG GLU A1043 16694 14515 11299 1351 -2066 458 C ATOM 1138 CD GLU A1043 1.168 -14.040 3.779 1.00121.59 C ANISOU 1138 CD GLU A1043 17807 15901 12490 1439 -2267 221 C ATOM 1139 OE1 GLU A1043 0.155 -13.612 3.188 1.00115.85 O ANISOU 1139 OE1 GLU A1043 16958 15159 11899 1260 -2277 69 O ATOM 1140 OE2 GLU A1043 1.556 -13.587 4.877 1.00129.98 O ANISOU 1140 OE2 GLU A1043 18899 17102 13384 1687 -2413 187 O ATOM 1141 N LEU A1044 1.648 -17.592 -0.734 1.00 92.67 N ANISOU 1141 N LEU A1044 14269 11531 9412 526 -1441 789 N ATOM 1142 CA LEU A1044 1.183 -17.986 -2.060 1.00 89.85 C ANISOU 1142 CA LEU A1044 13846 11023 9269 226 -1302 805 C ATOM 1143 C LEU A1044 0.762 -19.452 -2.084 1.00 91.49 C ANISOU 1143 C LEU A1044 14198 11165 9400 136 -841 975 C ATOM 1144 O LEU A1044 -0.330 -19.790 -2.556 1.00 91.40 O ANISOU 1144 O LEU A1044 14150 11123 9456 -53 -620 922 O ATOM 1145 CB LEU A1044 2.267 -17.741 -3.108 1.00 88.33 C ANISOU 1145 CB LEU A1044 13595 10694 9271 127 -1526 871 C ATOM 1146 CG LEU A1044 1.947 -18.268 -4.509 1.00 79.26 C ANISOU 1146 CG LEU A1044 12392 9379 8343 -181 -1369 920 C ATOM 1147 CD1 LEU A1044 0.741 -17.549 -5.089 1.00 77.39 C ANISOU 1147 CD1 LEU A1044 11991 9160 8254 -360 -1432 709 C ATOM 1148 CD2 LEU A1044 3.149 -18.132 -5.424 1.00 79.72 C ANISOU 1148 CD2 LEU A1044 12417 9306 8567 -253 -1576 1010 C ATOM 1149 N ASP A1045 1.624 -20.317 -1.559 1.00 93.74 N ANISOU 1149 N ASP A1045 14647 11432 9539 274 -694 1178 N ATOM 1150 CA ASP A1045 1.350 -21.749 -1.540 1.00 92.64 C ANISOU 1150 CA ASP A1045 14656 11226 9317 205 -257 1357 C ATOM 1151 C ASP A1045 0.146 -22.070 -0.664 1.00 94.24 C ANISOU 1151 C ASP A1045 14912 11545 9350 260 1 1289 C ATOM 1152 O ASP A1045 -0.626 -22.980 -0.964 1.00 86.88 O ANISOU 1152 O ASP A1045 14031 10557 8422 108 350 1345 O ATOM 1153 CB ASP A1045 2.573 -22.527 -1.051 1.00 95.91 C ANISOU 1153 CB ASP A1045 15235 11610 9596 371 -181 1582 C ATOM 1154 CG ASP A1045 3.786 -22.335 -1.942 1.00 99.14 C ANISOU 1154 CG ASP A1045 15605 11894 10170 308 -406 1666 C ATOM 1155 OD1 ASP A1045 3.603 -22.042 -3.143 1.00 96.63 O ANISOU 1155 OD1 ASP A1045 15162 11468 10084 75 -490 1607 O ATOM 1156 OD2 ASP A1045 4.922 -22.476 -1.441 1.00100.80 O ANISOU 1156 OD2 ASP A1045 15908 12114 10276 492 -498 1789 O ATOM 1157 N LYS A1046 -0.010 -21.317 0.422 1.00 98.62 N ANISOU 1157 N LYS A1046 15454 12262 9754 476 -171 1165 N ATOM 1158 CA LYS A1046 -1.155 -21.496 1.302 1.00 98.75 C ANISOU 1158 CA LYS A1046 15511 12402 9608 539 38 1080 C ATOM 1159 C LYS A1046 -2.436 -21.041 0.614 1.00 96.83 C ANISOU 1159 C LYS A1046 15124 12152 9515 320 55 892 C ATOM 1160 O LYS A1046 -3.477 -21.689 0.728 1.00 97.65 O ANISOU 1160 O LYS A1046 15271 12268 9563 232 370 882 O ATOM 1161 CB LYS A1046 -0.951 -20.730 2.612 1.00103.91 C ANISOU 1161 CB LYS A1046 16175 13232 10072 825 -177 989 C ATOM 1162 CG LYS A1046 -2.051 -20.937 3.641 1.00110.15 C ANISOU 1162 CG LYS A1046 17021 14159 10672 916 35 910 C ATOM 1163 CD LYS A1046 -1.780 -20.130 4.902 1.00116.27 C ANISOU 1163 CD LYS A1046 17797 15109 11271 1198 -201 819 C ATOM 1164 CE LYS A1046 -2.890 -20.306 5.926 1.00113.77 C ANISOU 1164 CE LYS A1046 17531 14930 10767 1286 2 734 C ATOM 1165 NZ LYS A1046 -2.644 -19.492 7.150 1.00105.47 N ANISOU 1165 NZ LYS A1046 16472 14053 9548 1556 -233 639 N ATOM 1166 N ALA A1047 -2.354 -19.926 -0.105 1.00 97.10 N ANISOU 1166 N ALA A1047 14986 12167 9741 232 -283 744 N ATOM 1167 CA ALA A1047 -3.512 -19.391 -0.815 1.00 96.40 C ANISOU 1167 CA ALA A1047 14746 12071 9810 25 -304 557 C ATOM 1168 C ALA A1047 -3.968 -20.289 -1.962 1.00 90.53 C ANISOU 1168 C ALA A1047 14004 11176 9217 -257 -15 642 C ATOM 1169 O ALA A1047 -5.159 -20.366 -2.261 1.00 87.30 O ANISOU 1169 O ALA A1047 13539 10776 8857 -412 150 535 O ATOM 1170 CB ALA A1047 -3.210 -17.995 -1.337 1.00 90.79 C ANISOU 1170 CB ALA A1047 13855 11369 9271 2 -744 391 C ATOM 1171 N ILE A1048 -3.021 -20.966 -2.606 1.00 93.51 N ANISOU 1171 N ILE A1048 14444 11417 9670 -324 47 830 N ATOM 1172 CA ILE A1048 -3.354 -21.816 -3.746 1.00 88.16 C ANISOU 1172 CA ILE A1048 13762 10589 9147 -594 310 919 C ATOM 1173 C ILE A1048 -3.525 -23.283 -3.333 1.00 90.85 C ANISOU 1173 C ILE A1048 14287 10899 9331 -585 757 1107 C ATOM 1174 O ILE A1048 -4.156 -24.073 -4.039 1.00 91.15 O ANISOU 1174 O ILE A1048 14335 10847 9451 -797 1051 1155 O ATOM 1175 CB ILE A1048 -2.283 -21.678 -4.855 1.00 90.67 C ANISOU 1175 CB ILE A1048 14021 10760 9669 -711 115 1005 C ATOM 1176 CG1 ILE A1048 -2.152 -20.206 -5.253 1.00 86.88 C ANISOU 1176 CG1 ILE A1048 13358 10312 9342 -720 -326 812 C ATOM 1177 CG2 ILE A1048 -2.627 -22.520 -6.079 1.00 87.05 C ANISOU 1177 CG2 ILE A1048 13548 10146 9382 -1000 376 1091 C ATOM 1178 CD1 ILE A1048 -1.532 -19.984 -6.606 1.00 84.51 C ANISOU 1178 CD1 ILE A1048 12955 9861 9292 -916 -493 843 C ATOM 1179 N GLY A1049 -3.005 -23.636 -2.161 1.00 92.15 N ANISOU 1179 N GLY A1049 14205 10582 10226 192 2502 598 N ATOM 1180 CA GLY A1049 -3.149 -24.991 -1.659 1.00 91.88 C ANISOU 1180 CA GLY A1049 14605 10364 9942 227 2944 487 C ATOM 1181 C GLY A1049 -2.227 -26.013 -2.298 1.00 92.34 C ANISOU 1181 C GLY A1049 14670 10514 9900 376 3070 740 C ATOM 1182 O GLY A1049 -2.540 -27.203 -2.326 1.00 90.96 O ANISOU 1182 O GLY A1049 14743 10255 9562 373 3496 608 O ATOM 1183 N ARG A1050 -1.101 -25.551 -2.835 1.00 97.86 N ANISOU 1183 N ARG A1050 15090 11391 10702 504 2704 1101 N ATOM 1184 CA ARG A1050 -0.097 -26.450 -3.399 1.00 99.18 C ANISOU 1184 CA ARG A1050 15258 11648 10778 661 2777 1380 C ATOM 1185 C ARG A1050 1.289 -25.807 -3.418 1.00 93.95 C ANISOU 1185 C ARG A1050 14424 11091 10183 829 2304 1801 C ATOM 1186 O ARG A1050 1.417 -24.586 -3.334 1.00 91.78 O ANISOU 1186 O ARG A1050 13914 10883 10074 807 1905 1878 O ATOM 1187 CB ARG A1050 -0.492 -26.874 -4.815 1.00 96.43 C ANISOU 1187 CB ARG A1050 14596 11512 10531 595 2987 1309 C ATOM 1188 CG ARG A1050 -0.495 -25.741 -5.826 1.00 95.42 C ANISOU 1188 CG ARG A1050 13936 11640 10679 539 2643 1391 C ATOM 1189 CD ARG A1050 -0.714 -26.271 -7.232 1.00 92.74 C ANISOU 1189 CD ARG A1050 13304 11512 10419 501 2849 1367 C ATOM 1190 NE ARG A1050 -0.624 -25.220 -8.242 1.00 91.11 N ANISOU 1190 NE ARG A1050 12583 11559 10474 461 2512 1473 N ATOM 1191 CZ ARG A1050 0.508 -24.839 -8.824 1.00 85.43 C ANISOU 1191 CZ ARG A1050 11589 11019 9851 593 2171 1835 C ATOM 1192 NH1 ARG A1050 1.654 -25.419 -8.495 1.00 85.95 N ANISOU 1192 NH1 ARG A1050 11846 11038 9773 774 2119 2129 N ATOM 1193 NH2 ARG A1050 0.496 -23.875 -9.735 1.00 83.39 N ANISOU 1193 NH2 ARG A1050 10865 10986 9833 543 1881 1904 N ATOM 1194 N ASN A1051 2.325 -26.634 -3.529 1.00 90.85 N ANISOU 1194 N ASN A1051 14148 10711 9660 996 2348 2073 N ATOM 1195 CA ASN A1051 3.687 -26.129 -3.671 1.00101.56 C ANISOU 1195 CA ASN A1051 15325 12184 11078 1163 1922 2487 C ATOM 1196 C ASN A1051 3.904 -25.553 -5.066 1.00 99.73 C ANISOU 1196 C ASN A1051 14562 12252 11080 1148 1705 2628 C ATOM 1197 O ASN A1051 4.213 -26.281 -6.009 1.00 93.18 O ANISOU 1197 O ASN A1051 13604 11559 10241 1197 1867 2730 O ATOM 1198 CB ASN A1051 4.714 -27.231 -3.395 1.00103.96 C ANISOU 1198 CB ASN A1051 15917 12413 11171 1345 2052 2731 C ATOM 1199 CG ASN A1051 5.039 -27.373 -1.920 1.00102.08 C ANISOU 1199 CG ASN A1051 16131 11913 10744 1422 2027 2758 C ATOM 1200 OD1 ASN A1051 4.906 -26.423 -1.149 1.00 98.58 O ANISOU 1200 OD1 ASN A1051 15716 11384 10357 1386 1762 2721 O ATOM 1201 ND2 ASN A1051 5.479 -28.562 -1.523 1.00104.52 N ANISOU 1201 ND2 ASN A1051 16794 12093 10825 1530 2301 2825 N ATOM 1202 N THR A1052 3.714 -24.243 -5.192 1.00 99.21 N ANISOU 1202 N THR A1052 14189 12283 11223 1076 1344 2625 N ATOM 1203 CA THR A1052 3.841 -23.564 -6.476 1.00 96.17 C ANISOU 1203 CA THR A1052 13285 12179 11075 1048 1115 2739 C ATOM 1204 C THR A1052 5.280 -23.204 -6.840 1.00100.57 C ANISOU 1204 C THR A1052 13628 12886 11698 1226 719 3180 C ATOM 1205 O THR A1052 5.575 -22.921 -8.002 1.00 96.54 O ANISOU 1205 O THR A1052 12714 12616 11350 1237 577 3323 O ATOM 1206 CB THR A1052 3.004 -22.274 -6.493 1.00 91.26 C ANISOU 1206 CB THR A1052 12408 11606 10661 890 889 2546 C ATOM 1207 OG1 THR A1052 3.515 -21.362 -5.513 1.00 94.54 O ANISOU 1207 OG1 THR A1052 12904 11925 11093 947 508 2685 O ATOM 1208 CG2 THR A1052 1.550 -22.581 -6.181 1.00 89.75 C ANISOU 1208 CG2 THR A1052 12405 11276 10419 707 1273 2106 C ATOM 1209 N ASN A1053 6.165 -23.221 -5.845 1.00104.50 N ANISOU 1209 N ASN A1053 14397 13242 12068 1365 545 3392 N ATOM 1210 CA ASN A1053 7.555 -22.788 -6.007 1.00101.58 C ANISOU 1210 CA ASN A1053 13856 12987 11753 1538 135 3812 C ATOM 1211 C ASN A1053 7.652 -21.384 -6.615 1.00 98.19 C ANISOU 1211 C ASN A1053 12953 12761 11595 1494 -309 3915 C ATOM 1212 O ASN A1053 8.593 -21.073 -7.345 1.00101.26 O ANISOU 1212 O ASN A1053 13042 13341 12093 1600 -589 4226 O ATOM 1213 CB ASN A1053 8.336 -23.790 -6.865 1.00107.96 C ANISOU 1213 CB ASN A1053 14606 13919 12494 1663 287 4036 C ATOM 1214 CG ASN A1053 9.840 -23.664 -6.690 1.00119.34 C ANISOU 1214 CG ASN A1053 16031 15395 13917 1850 -55 4425 C ATOM 1215 OD1 ASN A1053 10.318 -23.143 -5.683 1.00118.06 O ANISOU 1215 OD1 ASN A1053 16028 15086 13745 1848 -318 4396 O ATOM 1216 ND2 ASN A1053 10.593 -24.141 -7.676 1.00125.14 N ANISOU 1216 ND2 ASN A1053 16546 16275 14726 1855 -64 4445 N ATOM 1217 N GLY A1054 6.667 -20.544 -6.314 1.00 94.69 N ANISOU 1217 N GLY A1054 12444 12275 11260 1337 -369 3650 N ATOM 1218 CA GLY A1054 6.664 -19.166 -6.770 1.00 94.46 C ANISOU 1218 CA GLY A1054 11993 12415 11482 1283 -785 3717 C ATOM 1219 C GLY A1054 6.145 -18.990 -8.185 1.00 86.55 C ANISOU 1219 C GLY A1054 10557 11658 10671 1182 -731 3633 C ATOM 1220 O GLY A1054 6.080 -17.870 -8.692 1.00 83.52 O ANISOU 1220 O GLY A1054 9793 11433 10508 1127 -1056 3676 O ATOM 1221 N VAL A1055 5.765 -20.094 -8.819 1.00 84.47 N ANISOU 1221 N VAL A1055 10351 11422 10321 1155 -318 3512 N ATOM 1222 CA VAL A1055 5.267 -20.061 -10.191 1.00 83.21 C ANISOU 1222 CA VAL A1055 9799 11490 10325 1063 -226 3427 C ATOM 1223 C VAL A1055 3.860 -20.647 -10.276 1.00 83.42 C ANISOU 1223 C VAL A1055 9957 11436 10301 888 232 3007 C ATOM 1224 O VAL A1055 3.603 -21.739 -9.770 1.00 88.12 O ANISOU 1224 O VAL A1055 10935 11860 10687 897 614 2873 O ATOM 1225 CB VAL A1055 6.200 -20.830 -11.147 1.00 84.78 C ANISOU 1225 CB VAL A1055 9863 11853 10499 1199 -175 3707 C ATOM 1226 CG1 VAL A1055 5.608 -20.880 -12.546 1.00 80.52 C ANISOU 1226 CG1 VAL A1055 8944 11536 10114 1096 -39 3594 C ATOM 1227 CG2 VAL A1055 7.582 -20.191 -11.171 1.00 82.72 C ANISOU 1227 CG2 VAL A1055 9428 11694 10310 1367 -643 4127 C ATOM 1228 N ILE A1056 2.955 -19.919 -10.925 1.00 80.86 N ANISOU 1228 N ILE A1056 9314 11237 10171 729 193 2800 N ATOM 1229 CA ILE A1056 1.552 -20.320 -11.007 1.00 80.01 C ANISOU 1229 CA ILE A1056 9300 11060 10042 549 593 2387 C ATOM 1230 C ILE A1056 1.047 -20.337 -12.448 1.00 76.64 C ANISOU 1230 C ILE A1056 8472 10869 9778 456 701 2301 C ATOM 1231 O ILE A1056 1.736 -19.890 -13.363 1.00 78.02 O ANISOU 1231 O ILE A1056 8273 11266 10103 521 430 2553 O ATOM 1232 CB ILE A1056 0.648 -19.383 -10.179 1.00 75.91 C ANISOU 1232 CB ILE A1056 8843 10411 9587 409 487 2128 C ATOM 1233 CG1 ILE A1056 0.517 -18.023 -10.865 1.00 63.64 C ANISOU 1233 CG1 ILE A1056 6809 9063 8309 335 102 2168 C ATOM 1234 CG2 ILE A1056 1.187 -19.226 -8.767 1.00 82.26 C ANISOU 1234 CG2 ILE A1056 10011 10993 10250 502 330 2230 C ATOM 1235 CD1 ILE A1056 -0.334 -17.035 -10.104 1.00 74.51 C ANISOU 1235 CD1 ILE A1056 8219 10329 9765 199 -29 1929 C ATOM 1236 N THR A1057 -0.153 -20.876 -12.642 1.00 80.25 N ANISOU 1236 N THR A1057 9014 11276 10201 307 1102 1946 N ATOM 1237 CA THR A1057 -0.800 -20.883 -13.951 1.00 75.99 C ANISOU 1237 CA THR A1057 8113 10945 9816 196 1234 1814 C ATOM 1238 C THR A1057 -1.728 -19.679 -14.111 1.00 75.63 C ANISOU 1238 C THR A1057 7789 10965 9981 28 1053 1598 C ATOM 1239 O THR A1057 -2.081 -19.027 -13.127 1.00 82.49 O ANISOU 1239 O THR A1057 8813 11684 10847 -25 924 1481 O ATOM 1240 CB THR A1057 -1.600 -22.177 -14.180 1.00 71.34 C ANISOU 1240 CB THR A1057 7747 10281 9078 125 1785 1547 C ATOM 1241 OG1 THR A1057 -2.650 -22.272 -13.210 1.00 78.08 O ANISOU 1241 OG1 THR A1057 8923 10908 9835 1 2021 1203 O ATOM 1242 CG2 THR A1057 -0.693 -23.391 -14.055 1.00 65.55 C ANISOU 1242 CG2 THR A1057 7284 9485 8135 291 1975 1759 C ATOM 1243 N LYS A1058 -2.109 -19.378 -15.350 1.00 92.67 N ANISOU 1243 N LYS A1058 10773 15352 9086 -663 -481 3356 N ATOM 1244 CA LYS A1058 -2.984 -18.239 -15.628 1.00100.02 C ANISOU 1244 CA LYS A1058 11930 16006 10068 -909 -891 3127 C ATOM 1245 C LYS A1058 -4.373 -18.397 -15.006 1.00100.68 C ANISOU 1245 C LYS A1058 11975 15369 10910 -730 -633 2976 C ATOM 1246 O LYS A1058 -4.978 -17.417 -14.548 1.00 97.47 O ANISOU 1246 O LYS A1058 11799 14769 10467 -872 -805 2967 O ATOM 1247 CB LYS A1058 -3.116 -18.031 -17.139 1.00 98.10 C ANISOU 1247 CB LYS A1058 11652 15791 9830 -1114 -1357 2751 C ATOM 1248 CG LYS A1058 -4.002 -16.858 -17.529 1.00100.58 C ANISOU 1248 CG LYS A1058 12192 15825 10197 -1385 -1814 2496 C ATOM 1249 CD LYS A1058 -3.970 -16.597 -19.026 1.00104.76 C ANISOU 1249 CD LYS A1058 12701 16473 10629 -1617 -2301 2164 C ATOM 1250 CE LYS A1058 -4.542 -17.764 -19.814 1.00110.97 C ANISOU 1250 CE LYS A1058 13173 16877 12114 -1396 -2117 1834 C ATOM 1251 NZ LYS A1058 -4.522 -17.500 -21.281 1.00112.55 N ANISOU 1251 NZ LYS A1058 13353 17195 12216 -1624 -2596 1505 N ATOM 1252 N ASP A1059 -4.867 -19.633 -14.967 1.00 97.72 N ANISOU 1252 N ASP A1059 11307 14605 11218 -414 -218 2866 N ATOM 1253 CA ASP A1059 -6.183 -19.897 -14.400 1.00 95.64 C ANISOU 1253 CA ASP A1059 10974 13654 11711 -223 54 2726 C ATOM 1254 C ASP A1059 -6.207 -19.584 -12.911 1.00 95.97 C ANISOU 1254 C ASP A1059 11153 13679 11633 -136 356 3074 C ATOM 1255 O ASP A1059 -7.160 -18.990 -12.411 1.00 96.01 O ANISOU 1255 O ASP A1059 11289 13287 11905 -163 334 2997 O ATOM 1256 CB ASP A1059 -6.595 -21.352 -14.636 1.00102.52 C ANISOU 1256 CB ASP A1059 11489 14155 13308 107 450 2573 C ATOM 1257 CG ASP A1059 -7.064 -21.603 -16.055 1.00114.32 C ANISOU 1257 CG ASP A1059 12852 15434 15149 44 159 2137 C ATOM 1258 OD1 ASP A1059 -6.543 -20.944 -16.980 1.00111.80 O ANISOU 1258 OD1 ASP A1059 12655 15483 14339 -232 -304 2029 O ATOM 1259 OD2 ASP A1059 -7.958 -22.456 -16.245 1.00124.86 O ANISOU 1259 OD2 ASP A1059 13960 16233 17246 269 390 1905 O ATOM 1260 N GLU A1060 -5.146 -19.971 -12.208 1.00 92.40 N ANISOU 1260 N GLU A1060 10673 13668 10767 -34 633 3457 N ATOM 1261 CA GLU A1060 -5.042 -19.689 -10.783 1.00 92.27 C ANISOU 1261 CA GLU A1060 10787 13698 10575 45 924 3816 C ATOM 1262 C GLU A1060 -4.941 -18.185 -10.529 1.00 88.25 C ANISOU 1262 C GLU A1060 10641 13408 9483 -267 516 3901 C ATOM 1263 O GLU A1060 -5.512 -17.666 -9.564 1.00 84.68 O ANISOU 1263 O GLU A1060 10332 12724 9117 -245 628 4005 O ATOM 1264 CB GLU A1060 -3.836 -20.421 -10.185 1.00 93.71 C ANISOU 1264 CB GLU A1060 10861 14346 10397 200 1274 4206 C ATOM 1265 CG GLU A1060 -3.929 -21.943 -10.282 1.00 98.46 C ANISOU 1265 CG GLU A1060 11100 14722 11591 531 1716 4157 C ATOM 1266 CD GLU A1060 -2.644 -22.645 -9.877 1.00 96.59 C ANISOU 1266 CD GLU A1060 10753 14992 10953 654 1997 4514 C ATOM 1267 OE1 GLU A1060 -1.623 -21.956 -9.675 1.00 96.96 O ANISOU 1267 OE1 GLU A1060 11003 15601 10238 464 1813 4778 O ATOM 1268 OE2 GLU A1060 -2.654 -23.890 -9.761 1.00101.31 O ANISOU 1268 OE2 GLU A1060 11061 15426 12006 940 2399 4533 O ATOM 1269 N ALA A1061 -4.253 -17.486 -11.428 1.00 90.34 N ANISOU 1269 N ALA A1061 11048 14105 9174 -558 30 3842 N ATOM 1270 CA ALA A1061 -4.032 -16.052 -11.277 1.00 88.44 C ANISOU 1270 CA ALA A1061 11150 14129 8324 -874 -401 3933 C ATOM 1271 C ALA A1061 -5.330 -15.280 -11.441 1.00 84.86 C ANISOU 1271 C ALA A1061 10826 13150 8267 -989 -656 3618 C ATOM 1272 O ALA A1061 -5.650 -14.397 -10.639 1.00 88.42 O ANISOU 1272 O ALA A1061 11506 13527 8564 -1074 -721 3732 O ATOM 1273 CB ALA A1061 -3.002 -15.565 -12.281 1.00 83.42 C ANISOU 1273 CB ALA A1061 10607 14073 7016 -1153 -863 3932 C ATOM 1274 N GLU A1062 -6.077 -15.615 -12.487 1.00 85.89 N ANISOU 1274 N GLU A1062 10809 12915 8910 -989 -802 3219 N ATOM 1275 CA GLU A1062 -7.368 -14.979 -12.712 1.00 91.21 C ANISOU 1275 CA GLU A1062 11578 13048 10028 -1083 -1030 2894 C ATOM 1276 C GLU A1062 -8.389 -15.393 -11.647 1.00 89.59 C ANISOU 1276 C GLU A1062 11295 12287 10460 -809 -574 2916 C ATOM 1277 O GLU A1062 -9.284 -14.611 -11.287 1.00 88.29 O ANISOU 1277 O GLU A1062 11293 11777 10476 -889 -704 2804 O ATOM 1278 CB GLU A1062 -7.863 -15.304 -14.122 1.00 90.64 C ANISOU 1278 CB GLU A1062 11354 12738 10345 -1144 -1287 2469 C ATOM 1279 CG GLU A1062 -6.896 -14.790 -15.185 1.00 95.91 C ANISOU 1279 CG GLU A1062 12115 13964 10362 -1439 -1774 2439 C ATOM 1280 CD GLU A1062 -7.361 -15.034 -16.604 1.00102.40 C ANISOU 1280 CD GLU A1062 12802 14580 11526 -1522 -2061 2018 C ATOM 1281 OE1 GLU A1062 -7.878 -16.134 -16.884 1.00108.80 O ANISOU 1281 OE1 GLU A1062 13339 15021 12978 -1271 -1760 1833 O ATOM 1282 OE2 GLU A1062 -7.203 -14.121 -17.443 1.00105.19 O ANISOU 1282 OE2 GLU A1062 13322 15145 11502 -1843 -2596 1874 O ATOM 1283 N LYS A1063 -8.227 -16.604 -11.117 1.00 91.37 N ANISOU 1283 N LYS A1063 11270 12442 11005 -491 -43 3073 N ATOM 1284 CA LYS A1063 -9.051 -17.047 -10.000 1.00 89.90 C ANISOU 1284 CA LYS A1063 10999 11798 11359 -222 427 3158 C ATOM 1285 C LYS A1063 -8.802 -16.166 -8.782 1.00 87.68 C ANISOU 1285 C LYS A1063 10977 11720 10617 -292 465 3482 C ATOM 1286 O LYS A1063 -9.738 -15.816 -8.070 1.00 92.31 O ANISOU 1286 O LYS A1063 11637 11903 11534 -231 575 3442 O ATOM 1287 CB LYS A1063 -8.772 -18.516 -9.657 1.00 88.98 C ANISOU 1287 CB LYS A1063 10566 11640 11602 119 976 3305 C ATOM 1288 CG LYS A1063 -9.557 -19.520 -10.492 1.00 96.51 C ANISOU 1288 CG LYS A1063 11229 12117 13325 294 1089 2956 C ATOM 1289 CD LYS A1063 -9.135 -20.951 -10.187 1.00101.97 C ANISOU 1289 CD LYS A1063 11613 12832 14300 615 1596 3123 C ATOM 1290 CE LYS A1063 -9.778 -21.936 -11.155 1.00104.35 C ANISOU 1290 CE LYS A1063 11628 12721 15299 767 1652 2770 C ATOM 1291 NZ LYS A1063 -9.335 -23.338 -10.915 1.00104.27 N ANISOU 1291 NZ LYS A1063 11312 12743 15562 1075 2120 2923 N ATOM 1292 N LEU A1064 -7.545 -15.787 -8.557 1.00 86.30 N ANISOU 1292 N LEU A1064 10943 12172 9673 -423 360 3797 N ATOM 1293 CA LEU A1064 -7.238 -14.830 -7.495 1.00 88.71 C ANISOU 1293 CA LEU A1064 11524 12713 9468 -528 323 4095 C ATOM 1294 C LEU A1064 -7.827 -13.460 -7.827 1.00 87.09 C ANISOU 1294 C LEU A1064 11598 12387 9105 -823 -201 3882 C ATOM 1295 O LEU A1064 -8.307 -12.726 -6.944 1.00 89.47 O ANISOU 1295 O LEU A1064 12086 12535 9375 -847 -191 3964 O ATOM 1296 CB LEU A1064 -5.724 -14.713 -7.286 1.00 88.49 C ANISOU 1296 CB LEU A1064 11588 13399 8636 -621 288 4470 C ATOM 1297 CG LEU A1064 -4.942 -15.984 -6.941 1.00 90.75 C ANISOU 1297 CG LEU A1064 11622 13901 8956 -358 770 4725 C ATOM 1298 CD1 LEU A1064 -3.449 -15.695 -6.871 1.00 78.46 C ANISOU 1298 CD1 LEU A1064 10199 12744 6868 -455 586 4567 C ATOM 1299 CD2 LEU A1064 -5.435 -16.593 -5.638 1.00 94.79 C ANISOU 1299 CD2 LEU A1064 12029 14100 9889 -58 1334 4921 C ATOM 1300 N PHE A1065 -7.824 -13.144 -9.119 1.00 86.89 N ANISOU 1300 N PHE A1065 11591 12414 9009 -1042 -656 3594 N ATOM 1301 CA PHE A1065 -8.241 -11.831 -9.590 1.00 85.18 C ANISOU 1301 CA PHE A1065 11638 12149 8579 -1358 -1213 3391 C ATOM 1302 C PHE A1065 -9.718 -11.559 -9.298 1.00 86.63 C ANISOU 1302 C PHE A1065 11842 11662 9411 -1292 -1174 3127 C ATOM 1303 O PHE A1065 -10.072 -10.488 -8.775 1.00 82.70 O ANISOU 1303 O PHE A1065 11594 11104 8723 -1437 -1387 3151 O ATOM 1304 CB PHE A1065 -7.953 -11.712 -11.089 1.00 85.09 C ANISOU 1304 CB PHE A1065 11596 12312 8421 -1583 -1670 3127 C ATOM 1305 CG PHE A1065 -8.237 -10.357 -11.661 1.00 85.49 C ANISOU 1305 CG PHE A1065 11916 12382 8185 -1936 -2282 2937 C ATOM 1306 CD1 PHE A1065 -7.627 -9.230 -11.138 1.00 83.95 C ANISOU 1306 CD1 PHE A1065 11990 12546 7360 -2127 -2514 3130 C ATOM 1307 CD2 PHE A1065 -9.097 -10.212 -12.737 1.00 85.70 C ANISOU 1307 CD2 PHE A1065 11897 12036 8628 -2052 -2594 2514 C ATOM 1308 CE1 PHE A1065 -7.881 -7.981 -11.666 1.00 79.94 C ANISOU 1308 CE1 PHE A1065 11585 11890 6898 -2302 -2839 2735 C ATOM 1309 CE2 PHE A1065 -9.355 -8.965 -13.271 1.00 83.29 C ANISOU 1309 CE2 PHE A1065 11836 11747 8064 -2384 -3167 2342 C ATOM 1310 CZ PHE A1065 -8.746 -7.849 -12.734 1.00 83.69 C ANISOU 1310 CZ PHE A1065 12095 12094 7609 -2508 -3267 2471 C ATOM 1311 N ASN A1066 -10.572 -12.542 -9.585 1.00 86.52 N ANISOU 1311 N ASN A1066 11563 11147 10164 -1062 -888 2888 N ATOM 1312 CA ASN A1066 -12.005 -12.367 -9.347 1.00 87.44 C ANISOU 1312 CA ASN A1066 11674 10608 10939 -985 -832 2629 C ATOM 1313 C ASN A1066 -12.308 -12.135 -7.870 1.00 91.53 C ANISOU 1313 C ASN A1066 12288 11006 11483 -836 -498 2882 C ATOM 1314 O ASN A1066 -13.140 -11.286 -7.508 1.00 94.06 O ANISOU 1314 O ASN A1066 12780 11029 11929 -920 -656 2765 O ATOM 1315 CB ASN A1066 -12.788 -13.585 -9.845 1.00 90.53 C ANISOU 1315 CB ASN A1066 11742 10505 12150 -735 -533 2370 C ATOM 1316 CG ASN A1066 -12.640 -13.807 -11.334 1.00 87.33 C ANISOU 1316 CG ASN A1066 11237 10154 11791 -874 -870 2074 C ATOM 1317 OD1 ASN A1066 -12.379 -12.872 -12.091 1.00 88.18 O ANISOU 1317 OD1 ASN A1066 11535 10493 11476 -1187 -1396 1953 O ATOM 1318 ND2 ASN A1066 -12.811 -15.051 -11.765 1.00 85.79 N ANISOU 1318 ND2 ASN A1066 10739 9745 12114 -642 -572 1956 N ATOM 1319 N GLN A1067 -11.584 -12.858 -7.021 1.00 92.57 N ANISOU 1319 N GLN A1067 12315 11397 11460 -626 -50 3237 N ATOM 1320 CA GLN A1067 -11.754 -12.735 -5.583 1.00 92.77 C ANISOU 1320 CA GLN A1067 12412 11361 11476 -469 306 3514 C ATOM 1321 C GLN A1067 -11.361 -11.344 -5.129 1.00 91.28 C ANISOU 1321 C GLN A1067 12575 11498 10610 -728 -55 3668 C ATOM 1322 O GLN A1067 -12.072 -10.715 -4.344 1.00 91.14 O ANISOU 1322 O GLN A1067 12697 11225 10708 -716 -29 3667 O ATOM 1323 CB GLN A1067 -10.906 -13.768 -4.841 1.00 90.65 C ANISOU 1323 CB GLN A1067 11967 11375 11101 -221 820 3883 C ATOM 1324 CG GLN A1067 -11.083 -15.196 -5.310 1.00 93.74 C ANISOU 1324 CG GLN A1067 12004 11530 12083 32 1168 3770 C ATOM 1325 CD GLN A1067 -9.841 -16.023 -5.055 1.00 94.89 C ANISOU 1325 CD GLN A1067 12018 12153 11882 156 1461 4107 C ATOM 1326 OE1 GLN A1067 -8.812 -15.494 -4.633 1.00 90.53 O ANISOU 1326 OE1 GLN A1067 11647 12129 10621 30 1367 4411 O ATOM 1327 NE2 GLN A1067 -9.924 -17.322 -5.318 1.00 89.42 N ANISOU 1327 NE2 GLN A1067 11010 11277 11688 402 1808 4054 N ATOM 1328 N ASP A1068 -10.234 -10.854 -5.642 1.00 92.97 N ANISOU 1328 N ASP A1068 12930 12278 10117 -964 -404 3795 N ATOM 1329 CA ASP A1068 -9.775 -9.530 -5.234 1.00 96.34 C ANISOU 1329 CA ASP A1068 13693 13048 9864 -1218 -769 3960 C ATOM 1330 C ASP A1068 -10.748 -8.436 -5.672 1.00 93.11 C ANISOU 1330 C ASP A1068 13474 12301 9605 -1439 -1234 3628 C ATOM 1331 O ASP A1068 -10.965 -7.457 -4.943 1.00 93.50 O ANISOU 1331 O ASP A1068 13764 12345 9418 -1535 -1374 3711 O ATOM 1332 CB ASP A1068 -8.379 -9.254 -5.790 1.00 90.70 C ANISOU 1332 CB ASP A1068 13052 12967 8444 -1394 -1042 4062 C ATOM 1333 CG ASP A1068 -7.306 -10.054 -5.080 1.00 95.94 C ANISOU 1333 CG ASP A1068 13569 13877 9008 -1102 -561 4163 C ATOM 1334 OD1 ASP A1068 -7.481 -10.348 -3.878 1.00101.69 O ANISOU 1334 OD1 ASP A1068 14298 14468 9872 -898 -157 4335 O ATOM 1335 OD2 ASP A1068 -6.286 -10.386 -5.721 1.00 93.69 O ANISOU 1335 OD2 ASP A1068 13188 13872 8538 -1092 -610 4035 O ATOM 1336 N VAL A1069 -11.369 -8.616 -6.837 1.00 91.88 N ANISOU 1336 N VAL A1069 13205 11841 9863 -1510 -1464 3246 N ATOM 1337 CA VAL A1069 -12.360 -7.640 -7.285 1.00 88.47 C ANISOU 1337 CA VAL A1069 12934 11045 9634 -1710 -1894 2912 C ATOM 1338 C VAL A1069 -13.586 -7.651 -6.369 1.00 91.98 C ANISOU 1338 C VAL A1069 13359 10925 10664 -1510 -1591 2827 C ATOM 1339 O VAL A1069 -14.075 -6.585 -5.941 1.00 92.05 O ANISOU 1339 O VAL A1069 13601 10813 10561 -1644 -1835 2780 O ATOM 1340 CB VAL A1069 -12.798 -7.901 -8.738 1.00 90.14 C ANISOU 1340 CB VAL A1069 13013 11030 10206 -1817 -2181 2515 C ATOM 1341 CG1 VAL A1069 -13.907 -6.941 -9.139 1.00 91.47 C ANISOU 1341 CG1 VAL A1069 13335 10773 10647 -2006 -2591 2166 C ATOM 1342 CG2 VAL A1069 -11.610 -7.766 -9.678 1.00 81.80 C ANISOU 1342 CG2 VAL A1069 11995 10549 8537 -2044 -2531 2583 C ATOM 1343 N ASP A1070 -14.045 -8.856 -6.027 1.00 93.66 N ANISOU 1343 N ASP A1070 13293 10813 11482 -1185 -1056 2827 N ATOM 1344 CA ASP A1070 -15.190 -8.996 -5.129 1.00 89.96 C ANISOU 1344 CA ASP A1070 12771 9816 11594 -968 -717 2767 C ATOM 1345 C ASP A1070 -14.915 -8.325 -3.789 1.00 91.74 C ANISOU 1345 C ASP A1070 13204 10251 11402 -950 -595 3089 C ATOM 1346 O ASP A1070 -15.734 -7.545 -3.285 1.00 96.16 O ANISOU 1346 O ASP A1070 13917 10524 12096 -988 -698 2986 O ATOM 1347 CB ASP A1070 -15.524 -10.473 -4.902 1.00 99.92 C ANISOU 1347 CB ASP A1070 13689 10783 13494 -615 -132 2788 C ATOM 1348 CG ASP A1070 -16.448 -11.038 -5.962 1.00103.99 C ANISOU 1348 CG ASP A1070 14002 10803 14707 -573 -195 2379 C ATOM 1349 OD1 ASP A1070 -17.680 -10.953 -5.779 1.00108.12 O ANISOU 1349 OD1 ASP A1070 14494 10774 15814 -490 -128 2153 O ATOM 1350 OD2 ASP A1070 -15.946 -11.576 -6.972 1.00 99.84 O ANISOU 1350 OD2 ASP A1070 13346 10438 14150 -619 -309 2284 O ATOM 1351 N ALA A1071 -13.743 -8.617 -3.231 1.00 91.36 N ANISOU 1351 N ALA A1071 13163 10714 10836 -896 -386 3475 N ATOM 1352 CA ALA A1071 -13.357 -8.082 -1.933 1.00 96.80 C ANISOU 1352 CA ALA A1071 14035 11648 11097 -863 -235 3816 C ATOM 1353 C ALA A1071 -13.241 -6.566 -1.960 1.00 94.70 C ANISOU 1353 C ALA A1071 14119 11576 10288 -1177 -785 3787 C ATOM 1354 O ALA A1071 -13.593 -5.893 -0.987 1.00 98.61 O ANISOU 1354 O ALA A1071 14781 11992 10694 -1159 -746 3884 O ATOM 1355 CB ALA A1071 -12.041 -8.699 -1.482 1.00 94.97 C ANISOU 1355 CB ALA A1071 13741 11954 10389 -771 52 4226 C ATOM 1356 N ALA A1072 -12.770 -6.028 -3.082 1.00 91.61 N ANISOU 1356 N ALA A1072 13832 11430 9543 -1465 -1305 3648 N ATOM 1357 CA ALA A1072 -12.655 -4.581 -3.208 1.00 92.82 C ANISOU 1357 CA ALA A1072 14312 11766 9188 -1782 -1871 3607 C ATOM 1358 C ALA A1072 -14.036 -3.938 -3.193 1.00 90.19 C ANISOU 1358 C ALA A1072 14057 10865 9345 -1817 -2045 3270 C ATOM 1359 O ALA A1072 -14.271 -2.956 -2.474 1.00 88.43 O ANISOU 1359 O ALA A1072 14068 10633 8898 -1899 -2202 3327 O ATOM 1360 CB ALA A1072 -11.907 -4.211 -4.478 1.00 85.05 C ANISOU 1360 CB ALA A1072 13272 11126 7918 -1994 -2280 3346 C ATOM 1361 N VAL A1073 -14.961 -4.509 -3.963 1.00 86.53 N ANISOU 1361 N VAL A1073 13395 9921 9561 -1744 -2008 2921 N ATOM 1362 CA VAL A1073 -16.305 -3.940 -4.018 1.00 90.18 C ANISOU 1362 CA VAL A1073 13917 9823 10524 -1777 -2176 2583 C ATOM 1363 C VAL A1073 -17.015 -4.028 -2.663 1.00 94.51 C ANISOU 1363 C VAL A1073 14454 10070 11384 -1524 -1740 2694 C ATOM 1364 O VAL A1073 -17.675 -3.072 -2.236 1.00 93.21 O ANISOU 1364 O VAL A1073 14482 9702 11230 -1609 -1945 2590 O ATOM 1365 CB VAL A1073 -17.165 -4.633 -5.091 1.00 89.20 C ANISOU 1365 CB VAL A1073 13562 9227 11103 -1727 -2182 2196 C ATOM 1366 CG1 VAL A1073 -18.585 -4.091 -5.069 1.00 88.70 C ANISOU 1366 CG1 VAL A1073 13552 8565 11586 -1741 -2315 1860 C ATOM 1367 CG2 VAL A1073 -16.546 -4.444 -6.467 1.00 83.84 C ANISOU 1367 CG2 VAL A1073 12907 8828 10119 -1998 -2656 2054 C ATOM 1368 N ARG A1074 -16.851 -5.153 -1.970 1.00 94.56 N ANISOU 1368 N ARG A1074 14238 10068 11624 -1216 -1145 2915 N ATOM 1369 CA ARG A1074 -17.443 -5.288 -0.641 1.00 92.18 C ANISOU 1369 CA ARG A1074 13912 9526 11584 -969 -705 3055 C ATOM 1370 C ARG A1074 -16.817 -4.305 0.338 1.00 94.80 C ANISOU 1370 C ARG A1074 14528 10252 11239 -1070 -819 3351 C ATOM 1371 O ARG A1074 -17.486 -3.800 1.246 1.00 99.43 O ANISOU 1371 O ARG A1074 15217 10617 11945 -996 -724 3356 O ATOM 1372 CB ARG A1074 -17.290 -6.714 -0.115 1.00 93.81 C ANISOU 1372 CB ARG A1074 13818 9688 12137 -632 -56 3260 C ATOM 1373 CG ARG A1074 -17.991 -7.762 -0.950 1.00 86.95 C ANISOU 1373 CG ARG A1074 12651 8386 12000 -490 113 2979 C ATOM 1374 CD ARG A1074 -18.044 -9.085 -0.215 1.00 88.32 C ANISOU 1374 CD ARG A1074 12538 8435 12586 -133 777 3181 C ATOM 1375 NE ARG A1074 -18.133 -10.212 -1.137 1.00 93.48 N ANISOU 1375 NE ARG A1074 12905 8909 13703 -24 914 3018 N ATOM 1376 CZ ARG A1074 -17.084 -10.910 -1.561 1.00 86.41 C ANISOU 1376 CZ ARG A1074 11894 8400 12539 -9 993 3183 C ATOM 1377 NH1 ARG A1074 -15.865 -10.599 -1.144 1.00 87.60 N ANISOU 1377 NH1 ARG A1074 12190 9135 11959 -99 953 3522 N ATOM 1378 NH2 ARG A1074 -17.255 -11.922 -2.400 1.00 85.46 N ANISOU 1378 NH2 ARG A1074 11511 8078 12883 99 1109 3006 N ATOM 1379 N GLY A1075 -15.533 -4.025 0.137 1.00 94.11 N ANISOU 1379 N GLY A1075 14568 10752 10438 -1241 -1033 3593 N ATOM 1380 CA GLY A1075 -14.816 -3.103 0.995 1.00 96.64 C ANISOU 1380 CA GLY A1075 15162 11490 10065 -1353 -1169 3892 C ATOM 1381 C GLY A1075 -15.339 -1.697 0.811 1.00 97.31 C ANISOU 1381 C GLY A1075 15516 11461 9995 -1605 -1714 3659 C ATOM 1382 O GLY A1075 -15.433 -0.929 1.769 1.00107.60 O ANISOU 1382 O GLY A1075 16868 12852 11165 -1529 -1651 3628 O ATOM 1383 N ILE A1076 -15.692 -1.358 -0.426 1.00 93.93 N ANISOU 1383 N ILE A1076 15118 10870 9702 -1829 -2174 3335 N ATOM 1384 CA ILE A1076 -16.302 -0.061 -0.689 1.00 95.38 C ANISOU 1384 CA ILE A1076 15548 10880 9810 -2077 -2712 3087 C ATOM 1385 C ILE A1076 -17.709 0.024 -0.101 1.00 98.32 C ANISOU 1385 C ILE A1076 15881 10650 10824 -1908 -2518 2862 C ATOM 1386 O ILE A1076 -18.072 1.027 0.516 1.00 99.93 O ANISOU 1386 O ILE A1076 16306 10792 10869 -1986 -2715 2846 O ATOM 1387 CB ILE A1076 -16.374 0.235 -2.198 1.00 86.66 C ANISOU 1387 CB ILE A1076 14455 9733 8739 -2351 -3240 2770 C ATOM 1388 CG1 ILE A1076 -14.976 0.197 -2.814 1.00 83.46 C ANISOU 1388 CG1 ILE A1076 13793 9944 7973 -2401 -3193 2696 C ATOM 1389 CG2 ILE A1076 -17.023 1.588 -2.445 1.00 89.35 C ANISOU 1389 CG2 ILE A1076 14978 9892 9080 -2587 -3735 2449 C ATOM 1390 CD1 ILE A1076 -14.965 0.443 -4.302 1.00 78.29 C ANISOU 1390 CD1 ILE A1076 13091 9249 7406 -2647 -3585 2389 C ATOM 1391 N LEU A1077 -18.497 -1.032 -0.290 1.00 99.42 N ANISOU 1391 N LEU A1077 15737 10350 11688 -1675 -2133 2690 N ATOM 1392 CA LEU A1077 -19.877 -1.033 0.191 1.00104.19 C ANISOU 1392 CA LEU A1077 16277 10360 12951 -1508 -1937 2461 C ATOM 1393 C LEU A1077 -19.982 -0.975 1.715 1.00110.60 C ANISOU 1393 C LEU A1077 17135 11191 13697 -1291 -1530 2727 C ATOM 1394 O LEU A1077 -20.903 -0.362 2.254 1.00113.59 O ANISOU 1394 O LEU A1077 17609 11239 14310 -1262 -1569 2582 O ATOM 1395 CB LEU A1077 -20.614 -2.270 -0.326 1.00103.42 C ANISOU 1395 CB LEU A1077 15849 9816 13632 -1292 -1584 2255 C ATOM 1396 CG LEU A1077 -20.795 -2.347 -1.843 1.00101.45 C ANISOU 1396 CG LEU A1077 15533 9423 13591 -1482 -1969 1921 C ATOM 1397 CD1 LEU A1077 -21.375 -3.692 -2.247 1.00 98.32 C ANISOU 1397 CD1 LEU A1077 14795 8638 13924 -1235 -1561 1776 C ATOM 1398 CD2 LEU A1077 -21.675 -1.209 -2.337 1.00104.01 C ANISOU 1398 CD2 LEU A1077 16048 9431 14041 -1716 -2493 1569 C ATOM 1399 N ARG A1078 -19.040 -1.610 2.404 1.00109.04 N ANISOU 1399 N ARG A1078 16868 11381 13180 -1140 -1144 3113 N ATOM 1400 CA ARG A1078 -19.033 -1.593 3.865 1.00108.13 C ANISOU 1400 CA ARG A1078 16794 11333 12957 -936 -746 3397 C ATOM 1401 C ARG A1078 -18.550 -0.262 4.433 1.00109.01 C ANISOU 1401 C ARG A1078 17249 11784 12385 -1136 -1113 3544 C ATOM 1402 O ARG A1078 -18.969 0.147 5.517 1.00110.88 O ANISOU 1402 O ARG A1078 17580 11924 12627 -1024 -947 3627 O ATOM 1403 CB ARG A1078 -18.166 -2.730 4.408 1.00110.64 C ANISOU 1403 CB ARG A1078 16920 11956 13161 -713 -213 3768 C ATOM 1404 CG ARG A1078 -18.929 -4.018 4.667 1.00111.95 C ANISOU 1404 CG ARG A1078 16751 11698 14087 -385 366 3718 C ATOM 1405 CD ARG A1078 -19.959 -3.831 5.770 1.00107.47 C ANISOU 1405 CD ARG A1078 16184 10761 13888 -194 651 3692 C ATOM 1406 NE ARG A1078 -20.681 -5.065 6.061 1.00112.22 N ANISOU 1406 NE ARG A1078 16461 10967 15210 121 1211 3666 N ATOM 1407 CZ ARG A1078 -21.827 -5.414 5.485 1.00115.23 C ANISOU 1407 CZ ARG A1078 16679 10798 16307 189 1228 3318 C ATOM 1408 NH1 ARG A1078 -22.386 -4.619 4.583 1.00112.23 N ANISOU 1408 NH1 ARG A1078 16430 10195 16017 -38 718 2960 N ATOM 1409 NH2 ARG A1078 -22.415 -6.557 5.811 1.00114.00 N ANISOU 1409 NH2 ARG A1078 16227 10312 16778 481 1749 3331 N ATOM 1410 N ASN A1079 -17.666 0.408 3.700 1.00109.74 N ANISOU 1410 N ASN A1079 17584 11795 12317 283 -2902 -1380 N ATOM 1411 CA ASN A1079 -17.103 1.674 4.154 1.00110.10 C ANISOU 1411 CA ASN A1079 17797 11524 12512 195 -2537 -1148 C ATOM 1412 C ASN A1079 -18.162 2.767 4.254 1.00111.13 C ANISOU 1412 C ASN A1079 17961 11584 12679 259 -2062 -756 C ATOM 1413 O ASN A1079 -18.996 2.918 3.362 1.00109.84 O ANISOU 1413 O ASN A1079 17516 11819 12398 506 -1914 -562 O ATOM 1414 CB ASN A1079 -15.976 2.116 3.220 1.00106.59 C ANISOU 1414 CB ASN A1079 17088 11369 12043 369 -2488 -1092 C ATOM 1415 CG ASN A1079 -15.198 3.296 3.763 1.00111.58 C ANISOU 1415 CG ASN A1079 17915 11642 12839 248 -2175 -912 C ATOM 1416 OD1 ASN A1079 -15.614 4.446 3.623 1.00111.50 O ANISOU 1416 OD1 ASN A1079 17873 11620 12872 338 -1744 -560 O ATOM 1417 ND2 ASN A1079 -14.057 3.018 4.384 1.00117.46 N ANISOU 1417 ND2 ASN A1079 18861 12092 13678 43 -2393 -1155 N ATOM 1418 N ALA A1080 -18.125 3.527 5.344 1.00108.33 N ANISOU 1418 N ALA A1080 17953 10720 12488 36 -1824 -642 N ATOM 1419 CA ALA A1080 -19.090 4.598 5.562 1.00105.07 C ANISOU 1419 CA ALA A1080 17611 10185 12125 68 -1369 -275 C ATOM 1420 C ALA A1080 -18.829 5.810 4.669 1.00109.38 C ANISOU 1420 C ALA A1080 17906 10988 12666 298 -974 71 C ATOM 1421 O ALA A1080 -19.765 6.469 4.215 1.00103.45 O ANISOU 1421 O ALA A1080 17015 10422 11871 466 -651 377 O ATOM 1422 CB ALA A1080 -19.087 5.014 7.026 1.00100.48 C ANISOU 1422 CB ALA A1080 17484 8970 11722 -248 -1250 -272 C ATOM 1423 N LYS A1081 -17.554 6.103 4.428 1.00108.38 N ANISOU 1423 N LYS A1081 17725 10867 12586 302 -1001 23 N ATOM 1424 CA LYS A1081 -17.170 7.292 3.670 1.00113.12 C ANISOU 1424 CA LYS A1081 18115 11664 13201 495 -629 342 C ATOM 1425 C LYS A1081 -16.935 7.011 2.187 1.00117.14 C ANISOU 1425 C LYS A1081 18168 12794 13547 811 -725 351 C ATOM 1426 O LYS A1081 -16.573 7.911 1.430 1.00118.77 O ANISOU 1426 O LYS A1081 18158 13221 13748 997 -447 599 O ATOM 1427 CB LYS A1081 -15.919 7.925 4.283 1.00111.90 C ANISOU 1427 CB LYS A1081 18173 11139 13205 319 -552 324 C ATOM 1428 CG LYS A1081 -16.128 8.450 5.695 1.00107.65 C ANISOU 1428 CG LYS A1081 18073 9990 12840 28 -377 380 C ATOM 1429 CD LYS A1081 -17.286 9.436 5.747 1.00111.47 C ANISOU 1429 CD LYS A1081 18573 10437 13342 104 69 757 C ATOM 1430 CE LYS A1081 -17.511 9.957 7.157 1.00117.29 C ANISOU 1430 CE LYS A1081 19748 10567 14250 -184 244 814 C ATOM 1431 NZ LYS A1081 -16.322 10.690 7.675 1.00124.23 N ANISOU 1431 NZ LYS A1081 20810 11107 15284 -331 359 833 N ATOM 1432 N LEU A1082 -17.132 5.763 1.777 1.00114.22 N ANISOU 1432 N LEU A1082 17652 12702 13045 873 -1119 80 N ATOM 1433 CA LEU A1082 -16.923 5.389 0.381 1.00113.46 C ANISOU 1433 CA LEU A1082 17124 13200 12787 1170 -1246 60 C ATOM 1434 C LEU A1082 -18.222 4.982 -0.308 1.00115.47 C ANISOU 1434 C LEU A1082 17145 13838 12889 1376 -1243 146 C ATOM 1435 O LEU A1082 -18.391 5.213 -1.504 1.00114.03 O ANISOU 1435 O LEU A1082 16597 14139 12589 1666 -1130 309 O ATOM 1436 CB LEU A1082 -15.900 4.252 0.283 1.00110.12 C ANISOU 1436 CB LEU A1082 16667 12852 12321 1108 -1733 -338 C ATOM 1437 CG LEU A1082 -14.441 4.615 0.577 1.00116.41 C ANISOU 1437 CG LEU A1082 17577 13421 13233 984 -1761 -424 C ATOM 1438 CD1 LEU A1082 -13.570 3.369 0.647 1.00117.24 C ANISOU 1438 CD1 LEU A1082 17697 13550 13299 886 -2272 -846 C ATOM 1439 CD2 LEU A1082 -13.910 5.576 -0.473 1.00123.17 C ANISOU 1439 CD2 LEU A1082 18129 14605 14063 1232 -1475 -156 C ATOM 1440 N LYS A1083 -19.128 4.361 0.444 1.00116.74 N ANISOU 1440 N LYS A1083 17517 13787 13053 1225 -1372 31 N ATOM 1441 CA LYS A1083 -20.390 3.875 -0.121 1.00112.72 C ANISOU 1441 CA LYS A1083 16812 13614 12403 1398 -1402 84 C ATOM 1442 C LYS A1083 -21.294 4.950 -0.755 1.00112.79 C ANISOU 1442 C LYS A1083 16632 13847 12377 1621 -937 504 C ATOM 1443 O LYS A1083 -21.749 4.760 -1.883 1.00113.35 O ANISOU 1443 O LYS A1083 16349 14420 12299 1895 -939 584 O ATOM 1444 CB LYS A1083 -21.184 3.114 0.943 1.00110.52 C ANISOU 1444 CB LYS A1083 16837 12999 12157 1167 -1594 -100 C ATOM 1445 CG LYS A1083 -22.501 2.556 0.430 1.00111.31 C ANISOU 1445 CG LYS A1083 16755 13422 12117 1328 -1644 -62 C ATOM 1446 CD LYS A1083 -23.266 1.832 1.520 1.00116.16 C ANISOU 1446 CD LYS A1083 17680 13684 12770 1092 -1827 -239 C ATOM 1447 CE LYS A1083 -24.537 1.207 0.972 1.00109.65 C ANISOU 1447 CE LYS A1083 16662 13199 11803 1257 -1905 -221 C ATOM 1448 NZ LYS A1083 -25.295 0.481 2.026 1.00113.56 N ANISOU 1448 NZ LYS A1083 17457 13357 12335 1029 -2089 -394 N ATOM 1449 N PRO A1084 -21.582 6.063 -0.041 1.00112.29 N ANISOU 1449 N PRO A1084 16801 13418 12445 1506 -541 773 N ATOM 1450 CA PRO A1084 -22.434 7.075 -0.685 1.00111.57 C ANISOU 1450 CA PRO A1084 16519 13558 12316 1725 -103 1172 C ATOM 1451 C PRO A1084 -21.851 7.614 -1.987 1.00117.15 C ANISOU 1451 C PRO A1084 16840 14727 12944 2014 40 1339 C ATOM 1452 O PRO A1084 -22.592 7.932 -2.916 1.00119.42 O ANISOU 1452 O PRO A1084 16839 15412 13125 2273 237 1567 O ATOM 1453 CB PRO A1084 -22.515 8.187 0.366 1.00111.89 C ANISOU 1453 CB PRO A1084 16897 13084 12532 1525 265 1393 C ATOM 1454 CG PRO A1084 -22.215 7.518 1.657 1.00119.88 C ANISOU 1454 CG PRO A1084 18298 13602 13649 1195 -11 1097 C ATOM 1455 CD PRO A1084 -21.192 6.477 1.320 1.00115.97 C ANISOU 1455 CD PRO A1084 17696 13273 13096 1190 -461 741 C ATOM 1456 N VAL A1085 -20.527 7.702 -2.041 1.00115.55 N ANISOU 1456 N VAL A1085 16637 14471 12797 1968 -63 1222 N ATOM 1457 CA VAL A1085 -19.838 8.174 -3.232 1.00115.24 C ANISOU 1457 CA VAL A1085 16245 14849 12692 2226 45 1354 C ATOM 1458 C VAL A1085 -20.005 7.179 -4.374 1.00115.30 C ANISOU 1458 C VAL A1085 15886 15414 12508 2467 -258 1196 C ATOM 1459 O VAL A1085 -20.318 7.555 -5.504 1.00118.28 O ANISOU 1459 O VAL A1085 15919 16245 12779 2756 -81 1407 O ATOM 1460 CB VAL A1085 -18.334 8.397 -2.955 1.00114.80 C ANISOU 1460 CB VAL A1085 16294 14582 12743 2100 -36 1231 C ATOM 1461 CG1 VAL A1085 -17.567 8.594 -4.249 1.00116.29 C ANISOU 1461 CG1 VAL A1085 16096 15250 12841 2370 -27 1293 C ATOM 1462 CG2 VAL A1085 -18.137 9.580 -2.017 1.00119.13 C ANISOU 1462 CG2 VAL A1085 17149 14640 13475 1913 329 1448 C ATOM 1463 N TYR A1086 -19.812 5.902 -4.059 1.00114.53 N ANISOU 1463 N TYR A1086 15870 15276 12370 2345 -715 823 N ATOM 1464 CA TYR A1086 -19.932 4.830 -5.039 1.00108.91 C ANISOU 1464 CA TYR A1086 14840 15058 11482 2544 -1054 627 C ATOM 1465 C TYR A1086 -21.357 4.668 -5.564 1.00107.10 C ANISOU 1465 C TYR A1086 14431 15131 11131 2727 -958 776 C ATOM 1466 O TYR A1086 -21.559 4.327 -6.729 1.00103.94 O ANISOU 1466 O TYR A1086 13666 15248 10578 2998 -1037 791 O ATOM 1467 CB TYR A1086 -19.446 3.516 -4.423 1.00107.38 C ANISOU 1467 CB TYR A1086 14822 14688 11290 2337 -1559 191 C ATOM 1468 CG TYR A1086 -19.637 2.297 -5.296 1.00 98.19 C ANISOU 1468 CG TYR A1086 13369 13989 9949 2511 -1944 -42 C ATOM 1469 CD1 TYR A1086 -18.719 1.978 -6.287 1.00 93.96 C ANISOU 1469 CD1 TYR A1086 12536 13841 9324 2691 -2132 -154 C ATOM 1470 CD2 TYR A1086 -20.726 1.453 -5.116 1.00100.15 C ANISOU 1470 CD2 TYR A1086 13647 14284 10122 2494 -2125 -156 C ATOM 1471 CE1 TYR A1086 -18.886 0.861 -7.082 1.00 94.12 C ANISOU 1471 CE1 TYR A1086 12293 14284 9183 2850 -2487 -370 C ATOM 1472 CE2 TYR A1086 -20.903 0.335 -5.906 1.00 98.02 C ANISOU 1472 CE2 TYR A1086 13115 14434 9692 2652 -2480 -371 C ATOM 1473 CZ TYR A1086 -19.980 0.043 -6.887 1.00 94.62 C ANISOU 1473 CZ TYR A1086 12391 14385 9175 2830 -2660 -478 C ATOM 1474 OH TYR A1086 -20.153 -1.073 -7.675 1.00 92.14 O ANISOU 1474 OH TYR A1086 11816 14492 8702 2989 -3016 -694 O ATOM 1475 N ASP A1087 -22.341 4.919 -4.704 1.00107.92 N ANISOU 1475 N ASP A1087 14791 14911 11301 2581 -785 887 N ATOM 1476 CA ASP A1087 -23.741 4.770 -5.086 1.00109.30 C ANISOU 1476 CA ASP A1087 14831 15326 11371 2729 -689 1027 C ATOM 1477 C ASP A1087 -24.148 5.806 -6.125 1.00114.21 C ANISOU 1477 C ASP A1087 15146 16317 11933 3022 -280 1410 C ATOM 1478 O ASP A1087 -24.858 5.496 -7.081 1.00110.31 O ANISOU 1478 O ASP A1087 14346 16276 11290 3268 -301 1473 O ATOM 1479 CB ASP A1087 -24.650 4.885 -3.859 1.00108.26 C ANISOU 1479 CB ASP A1087 15068 14727 11340 2490 -576 1070 C ATOM 1480 CG ASP A1087 -24.503 3.714 -2.909 1.00110.94 C ANISOU 1480 CG ASP A1087 15681 14759 11713 2227 -1003 687 C ATOM 1481 OD1 ASP A1087 -24.261 2.585 -3.385 1.00112.81 O ANISOU 1481 OD1 ASP A1087 15756 15266 11841 2291 -1406 402 O ATOM 1482 OD2 ASP A1087 -24.632 3.921 -1.684 1.00113.41 O ANISOU 1482 OD2 ASP A1087 16370 14559 12161 1957 -936 670 O ATOM 1483 N SER A1088 -23.676 7.034 -5.937 1.00115.94 N ANISOU 1483 N SER A1088 15447 16340 12267 2994 88 1664 N ATOM 1484 CA SER A1088 -23.998 8.122 -6.850 1.00117.24 C ANISOU 1484 CA SER A1088 15343 16813 12390 3255 504 2043 C ATOM 1485 C SER A1088 -22.937 8.237 -7.934 1.00121.27 C ANISOU 1485 C SER A1088 15533 17708 12838 3463 453 2035 C ATOM 1486 O SER A1088 -22.299 9.280 -8.086 1.00124.74 O ANISOU 1486 O SER A1088 15945 18096 13353 3502 746 2248 O ATOM 1487 CB SER A1088 -24.133 9.445 -6.092 1.00121.94 C ANISOU 1487 CB SER A1088 16188 17001 13142 3125 956 2346 C ATOM 1488 OG SER A1088 -22.925 9.785 -5.434 1.00126.14 O ANISOU 1488 OG SER A1088 16939 17173 13815 2928 938 2259 O ATOM 1489 N LEU A1089 -22.758 7.158 -8.689 1.00116.87 N ANISOU 1489 N LEU A1089 14730 17536 12139 3599 79 1790 N ATOM 1490 CA LEU A1089 -21.784 7.130 -9.771 1.00107.69 C ANISOU 1490 CA LEU A1089 13244 16773 10900 3808 -13 1755 C ATOM 1491 C LEU A1089 -22.223 6.215 -10.909 1.00107.37 C ANISOU 1491 C LEU A1089 12837 17296 10664 4070 -265 1644 C ATOM 1492 O LEU A1089 -22.866 5.188 -10.690 1.00102.60 O ANISOU 1492 O LEU A1089 12278 16712 9993 4016 -555 1430 O ATOM 1493 CB LEU A1089 -20.415 6.681 -9.255 1.00107.01 C ANISOU 1493 CB LEU A1089 13324 16440 10895 3611 -312 1457 C ATOM 1494 CG LEU A1089 -19.475 7.728 -8.657 1.00111.59 C ANISOU 1494 CG LEU A1089 14112 16643 11644 3459 -59 1587 C ATOM 1495 CD1 LEU A1089 -18.154 7.085 -8.264 1.00111.72 C ANISOU 1495 CD1 LEU A1089 14254 16479 11714 3287 -418 1253 C ATOM 1496 CD2 LEU A1089 -19.248 8.870 -9.635 1.00116.25 C ANISOU 1496 CD2 LEU A1089 14418 17538 12214 3714 322 1930 C ATOM 1497 N ASP A1090 -21.859 6.605 -12.125 1.00113.23 N ANISOU 1497 N ASP A1090 13214 18493 11316 4353 -150 1792 N ATOM 1498 CA ASP A1090 -22.077 5.796 -13.317 1.00111.80 C ANISOU 1498 CA ASP A1090 12652 18877 10948 4622 -388 1689 C ATOM 1499 C ASP A1090 -21.101 4.626 -13.312 1.00110.04 C ANISOU 1499 C ASP A1090 12425 18695 10690 4542 -888 1281 C ATOM 1500 O ASP A1090 -20.122 4.641 -12.566 1.00109.19 O ANISOU 1500 O ASP A1090 12558 18230 10701 4320 -992 1130 O ATOM 1501 CB ASP A1090 -21.915 6.638 -14.580 1.00110.50 C ANISOU 1501 CB ASP A1090 12112 19164 10710 4941 -96 1979 C ATOM 1502 CG ASP A1090 -20.603 7.392 -14.610 1.00107.08 C ANISOU 1502 CG ASP A1090 11692 18620 10373 4911 31 2041 C ATOM 1503 OD1 ASP A1090 -20.528 8.482 -14.002 1.00107.23 O ANISOU 1503 OD1 ASP A1090 11912 18299 10531 4795 387 2275 O ATOM 1504 OD2 ASP A1090 -19.647 6.896 -15.241 1.00105.92 O ANISOU 1504 OD2 ASP A1090 11353 18726 10165 5005 -226 1858 O ATOM 1505 N ALA A1091 -21.383 3.601 -14.112 1.00 77.89 N ANISOU 1505 N ALA A1091 11581 9913 8101 1589 254 -811 N ATOM 1506 CA ALA A1091 -20.633 2.349 -14.034 1.00 76.32 C ANISOU 1506 CA ALA A1091 11129 9789 8079 1506 290 -647 C ATOM 1507 C ALA A1091 -19.136 2.524 -14.281 1.00 73.25 C ANISOU 1507 C ALA A1091 10780 9471 7580 1318 70 -489 C ATOM 1508 O ALA A1091 -18.310 1.894 -13.606 1.00 77.38 O ANISOU 1508 O ALA A1091 11273 10042 8087 1204 60 -301 O ATOM 1509 CB ALA A1091 -21.206 1.343 -15.019 1.00 73.74 C ANISOU 1509 CB ALA A1091 10430 9484 8104 1617 417 -745 C ATOM 1510 N VAL A1092 -18.787 3.411 -15.208 1.00 67.24 N ANISOU 1510 N VAL A1092 10102 8714 6734 1283 -106 -564 N ATOM 1511 CA VAL A1092 -17.391 3.613 -15.576 1.00 69.48 C ANISOU 1511 CA VAL A1092 10411 9062 6925 1109 -318 -430 C ATOM 1512 C VAL A1092 -16.593 4.212 -14.420 1.00 74.22 C ANISOU 1512 C VAL A1092 11318 9660 7221 973 -428 -270 C ATOM 1513 O VAL A1092 -15.516 3.715 -14.071 1.00 73.89 O ANISOU 1513 O VAL A1092 11235 9677 7162 833 -499 -85 O ATOM 1514 CB VAL A1092 -17.267 4.531 -16.814 1.00 65.38 C ANISOU 1514 CB VAL A1092 9936 8539 6365 1109 -482 -559 C ATOM 1515 CG1 VAL A1092 -15.805 4.746 -17.183 1.00 61.26 C ANISOU 1515 CG1 VAL A1092 9444 8086 5746 926 -701 -418 C ATOM 1516 CG2 VAL A1092 -18.037 3.943 -17.985 1.00 60.15 C ANISOU 1516 CG2 VAL A1092 8971 7878 6005 1244 -380 -718 C ATOM 1517 N ARG A1093 -17.126 5.274 -13.824 1.00 73.56 N ANISOU 1517 N ARG A1093 11543 9507 6900 1015 -442 -341 N ATOM 1518 CA ARG A1093 -16.466 5.922 -12.694 1.00 80.26 C ANISOU 1518 CA ARG A1093 12703 10344 7447 899 -542 -201 C ATOM 1519 C ARG A1093 -16.471 5.034 -11.447 1.00 79.55 C ANISOU 1519 C ARG A1093 12586 10258 7380 883 -396 -59 C ATOM 1520 O ARG A1093 -15.560 5.113 -10.615 1.00 73.79 O ANISOU 1520 O ARG A1093 12010 9550 6477 748 -486 116 O ATOM 1521 CB ARG A1093 -17.121 7.276 -12.401 1.00 80.72 C ANISOU 1521 CB ARG A1093 13091 10324 7256 960 -586 -326 C ATOM 1522 CG ARG A1093 -16.946 8.290 -13.531 1.00 72.51 C ANISOU 1522 CG ARG A1093 12129 9280 6143 949 -763 -445 C ATOM 1523 CD ARG A1093 -17.336 9.697 -13.102 1.00 79.58 C ANISOU 1523 CD ARG A1093 13388 10105 6744 973 -842 -530 C ATOM 1524 NE ARG A1093 -17.101 10.680 -14.157 1.00 77.95 N ANISOU 1524 NE ARG A1093 13265 9895 6456 952 -1022 -634 N ATOM 1525 CZ ARG A1093 -18.019 11.066 -15.037 1.00 79.91 C ANISOU 1525 CZ ARG A1093 13465 10103 6795 1083 -988 -839 C ATOM 1526 NH1 ARG A1093 -19.240 10.549 -14.994 1.00 80.07 N ANISOU 1526 NH1 ARG A1093 13348 10082 6994 1245 -780 -964 N ATOM 1527 NH2 ARG A1093 -17.718 11.967 -15.963 1.00 81.89 N ANISOU 1527 NH2 ARG A1093 13802 10353 6959 1051 -1162 -920 N ATOM 1528 N ARG A1094 -17.485 4.178 -11.329 1.00 79.52 N ANISOU 1528 N ARG A1094 12385 10234 7593 1019 -174 -132 N ATOM 1529 CA ARG A1094 -17.507 3.194 -10.254 1.00 79.53 C ANISOU 1529 CA ARG A1094 12318 10245 7657 1010 -23 -1 C ATOM 1530 C ARG A1094 -16.314 2.266 -10.418 1.00 79.82 C ANISOU 1530 C ARG A1094 12150 10367 7810 872 -92 179 C ATOM 1531 O ARG A1094 -15.585 1.978 -9.455 1.00 78.57 O ANISOU 1531 O ARG A1094 12080 10229 7543 761 -116 358 O ATOM 1532 CB ARG A1094 -18.814 2.392 -10.259 1.00 71.10 C ANISOU 1532 CB ARG A1094 11041 9144 6831 1185 228 -122 C ATOM 1533 CG ARG A1094 -20.019 3.142 -9.711 1.00 80.70 C ANISOU 1533 CG ARG A1094 12471 10269 7921 1318 334 -266 C ATOM 1534 CD ARG A1094 -21.233 2.233 -9.551 1.00 77.36 C ANISOU 1534 CD ARG A1094 11839 9816 7738 1478 593 -358 C ATOM 1535 NE ARG A1094 -22.373 2.942 -8.974 1.00 84.06 N ANISOU 1535 NE ARG A1094 12898 10578 8463 1602 698 -491 N ATOM 1536 CZ ARG A1094 -23.533 2.372 -8.664 1.00 83.76 C ANISOU 1536 CZ ARG A1094 12748 10498 8582 1748 924 -583 C ATOM 1537 NH1 ARG A1094 -23.716 1.075 -8.873 1.00 72.97 N ANISOU 1537 NH1 ARG A1094 11057 9166 7501 1790 1070 -556 N ATOM 1538 NH2 ARG A1094 -24.513 3.099 -8.142 1.00 83.72 N ANISOU 1538 NH2 ARG A1094 12952 10413 8446 1852 1005 -703 N ATOM 1539 N ALA A1095 -16.079 1.849 -11.659 1.00 74.60 N ANISOU 1539 N ALA A1095 11228 9756 7361 874 -135 130 N ATOM 1540 CA ALA A1095 -14.919 1.020 -11.945 1.00 70.79 C ANISOU 1540 CA ALA A1095 10545 9357 6994 742 -215 289 C ATOM 1541 C ALA A1095 -13.642 1.798 -11.634 1.00 71.94 C ANISOU 1541 C ALA A1095 10934 9527 6873 563 -444 430 C ATOM 1542 O ALA A1095 -12.659 1.230 -11.147 1.00 74.50 O ANISOU 1542 O ALA A1095 11219 9900 7186 433 -495 614 O ATOM 1543 CB ALA A1095 -14.937 0.551 -13.391 1.00 67.82 C ANISOU 1543 CB ALA A1095 9862 9025 6880 782 -229 195 C ATOM 1544 N ALA A1096 -13.673 3.105 -11.879 1.00 75.22 N ANISOU 1544 N ALA A1096 11606 9904 7071 557 -580 343 N ATOM 1545 CA ALA A1096 -12.511 3.946 -11.606 1.00 80.08 C ANISOU 1545 CA ALA A1096 12470 10535 7420 393 -802 465 C ATOM 1546 C ALA A1096 -12.186 4.018 -10.111 1.00 85.17 C ANISOU 1546 C ALA A1096 13347 11158 7855 320 -791 619 C ATOM 1547 O ALA A1096 -11.017 4.091 -9.729 1.00 86.74 O ANISOU 1547 O ALA A1096 13639 11393 7924 163 -935 787 O ATOM 1548 CB ALA A1096 -12.725 5.347 -12.168 1.00 77.15 C ANISOU 1548 CB ALA A1096 12329 10122 6861 416 -939 327 C ATOM 1549 N LEU A1097 -13.215 3.992 -9.266 1.00 85.21 N ANISOU 1549 N LEU A1097 13446 11102 7828 434 -620 563 N ATOM 1550 CA LEU A1097 -12.996 3.989 -7.820 1.00 81.87 C ANISOU 1550 CA LEU A1097 13233 10654 7219 377 -589 704 C ATOM 1551 C LEU A1097 -12.470 2.628 -7.367 1.00 81.68 C ANISOU 1551 C LEU A1097 12984 10684 7367 314 -504 869 C ATOM 1552 O LEU A1097 -11.544 2.527 -6.533 1.00 86.98 O ANISOU 1552 O LEU A1097 13773 11374 7901 181 -583 1050 O ATOM 1553 CB LEU A1097 -14.291 4.338 -7.084 1.00 76.93 C ANISOU 1553 CB LEU A1097 12763 9947 6519 522 -422 589 C ATOM 1554 CG LEU A1097 -14.214 4.658 -5.590 1.00 80.46 C ANISOU 1554 CG LEU A1097 13499 10351 6720 479 -402 701 C ATOM 1555 CD1 LEU A1097 -13.260 5.812 -5.339 1.00 78.08 C ANISOU 1555 CD1 LEU A1097 13510 10046 6111 343 -636 782 C ATOM 1556 CD2 LEU A1097 -15.600 4.980 -5.051 1.00 84.36 C ANISOU 1556 CD2 LEU A1097 14112 10765 7175 639 -227 559 C ATOM 1557 N ILE A1098 -13.045 1.578 -7.948 1.00 75.92 N ANISOU 1557 N ILE A1098 11926 9979 6942 410 -347 804 N ATOM 1558 CA ILE A1098 -12.641 0.219 -7.611 1.00 80.88 C ANISOU 1558 CA ILE A1098 12310 10659 7763 365 -253 944 C ATOM 1559 C ILE A1098 -11.179 -0.027 -7.986 1.00 81.81 C ANISOU 1559 C ILE A1098 12348 10852 7884 190 -439 1100 C ATOM 1560 O ILE A1098 -10.487 -0.808 -7.335 1.00 85.28 O ANISOU 1560 O ILE A1098 12724 11328 8353 96 -430 1270 O ATOM 1561 CB ILE A1098 -13.544 -0.819 -8.308 1.00 75.62 C ANISOU 1561 CB ILE A1098 11293 10005 7433 505 -61 831 C ATOM 1562 CG1 ILE A1098 -14.996 -0.633 -7.870 1.00 71.95 C ANISOU 1562 CG1 ILE A1098 10902 9463 6973 678 132 683 C ATOM 1563 CG2 ILE A1098 -13.095 -2.236 -7.991 1.00 74.69 C ANISOU 1563 CG2 ILE A1098 10916 9943 7518 456 29 978 C ATOM 1564 CD1 ILE A1098 -15.978 -1.481 -8.647 1.00 69.70 C ANISOU 1564 CD1 ILE A1098 10295 9182 7007 829 312 544 C ATOM 1565 N ASN A1099 -10.705 0.661 -9.024 1.00 79.61 N ANISOU 1565 N ASN A1099 12081 10597 7571 145 -610 1042 N ATOM 1566 CA ASN A1099 -9.301 0.562 -9.417 1.00 80.52 C ANISOU 1566 CA ASN A1099 12144 10780 7669 -24 -800 1182 C ATOM 1567 C ASN A1099 -8.383 0.995 -8.275 1.00 85.27 C ANISOU 1567 C ASN A1099 13024 11374 8000 -169 -920 1359 C ATOM 1568 O ASN A1099 -7.453 0.269 -7.884 1.00 83.99 O ANISOU 1568 O ASN A1099 12775 11261 7876 -287 -958 1532 O ATOM 1569 CB ASN A1099 -9.040 1.419 -10.661 1.00 76.18 C ANISOU 1569 CB ASN A1099 11611 10244 7088 -41 -965 1074 C ATOM 1570 CG ASN A1099 -7.734 1.070 -11.358 1.00 75.26 C ANISOU 1570 CG ASN A1099 11341 10208 7045 -190 -1127 1189 C ATOM 1571 OD1 ASN A1099 -6.736 0.734 -10.719 1.00 83.52 O ANISOU 1571 OD1 ASN A1099 12421 11288 8025 -326 -1201 1372 O ATOM 1572 ND2 ASN A1099 -7.739 1.152 -12.683 1.00 67.28 N ANISOU 1572 ND2 ASN A1099 10161 9226 6174 -163 -1183 1081 N ATOM 1573 N MET A1100 -8.668 2.171 -7.726 1.00 89.00 N ANISOU 1573 N MET A1100 13832 11784 8201 -155 -976 1314 N ATOM 1574 CA MET A1100 -7.886 2.697 -6.620 1.00 97.30 C ANISOU 1574 CA MET A1100 15176 12819 8976 -281 -1091 1469 C ATOM 1575 C MET A1100 -7.990 1.812 -5.387 1.00 97.38 C ANISOU 1575 C MET A1100 15169 12818 9011 -284 -944 1595 C ATOM 1576 O MET A1100 -7.002 1.618 -4.678 1.00 97.06 O ANISOU 1576 O MET A1100 15210 12799 8868 -420 -1032 1775 O ATOM 1577 CB MET A1100 -8.338 4.115 -6.272 1.00105.28 C ANISOU 1577 CB MET A1100 16542 13758 9702 -244 -1158 1378 C ATOM 1578 CG MET A1100 -8.131 5.131 -7.378 1.00109.32 C ANISOU 1578 CG MET A1100 17121 14275 10142 -259 -1327 1268 C ATOM 1579 SD MET A1100 -8.600 6.787 -6.846 1.00226.31 S ANISOU 1579 SD MET A1100 32373 29008 24608 -226 -1413 1177 S ATOM 1580 CE MET A1100 -7.527 7.000 -5.427 1.00130.19 C ANISOU 1580 CE MET A1100 20472 16829 12164 -388 -1524 1408 C ATOM 1581 N VAL A1101 -9.177 1.263 -5.130 1.00 94.94 N ANISOU 1581 N VAL A1101 14756 12476 8842 -134 -721 1501 N ATOM 1582 CA VAL A1101 -9.307 0.377 -3.973 1.00 92.90 C ANISOU 1582 CA VAL A1101 14472 12207 8618 -133 -573 1618 C ATOM 1583 C VAL A1101 -8.466 -0.885 -4.162 1.00 92.55 C ANISOU 1583 C VAL A1101 14138 12239 8787 -224 -573 1760 C ATOM 1584 O VAL A1101 -7.836 -1.376 -3.221 1.00 96.19 O ANISOU 1584 O VAL A1101 14646 12711 9192 -318 -576 1930 O ATOM 1585 CB VAL A1101 -10.773 -0.004 -3.708 1.00 91.91 C ANISOU 1585 CB VAL A1101 14274 12032 8617 49 -326 1484 C ATOM 1586 CG1 VAL A1101 -10.864 -1.050 -2.605 1.00 99.24 C ANISOU 1586 CG1 VAL A1101 15136 12957 9612 47 -168 1610 C ATOM 1587 CG2 VAL A1101 -11.569 1.233 -3.333 1.00 91.35 C ANISOU 1587 CG2 VAL A1101 14514 11882 8313 131 -324 1361 C ATOM 1588 N PHE A1102 -8.422 -1.370 -5.398 1.00 88.29 N ANISOU 1588 N PHE A1102 13307 11753 8487 -200 -578 1690 N ATOM 1589 CA PHE A1102 -7.638 -2.549 -5.744 1.00 87.22 C ANISOU 1589 CA PHE A1102 12874 11693 8572 -281 -585 1809 C ATOM 1590 C PHE A1102 -6.145 -2.274 -5.609 1.00 86.20 C ANISOU 1590 C PHE A1102 12854 11606 8293 -475 -808 1979 C ATOM 1591 O PHE A1102 -5.361 -3.182 -5.324 1.00 82.48 O ANISOU 1591 O PHE A1102 12238 11183 7916 -571 -819 2132 O ATOM 1592 CB PHE A1102 -7.973 -3.003 -7.169 1.00 80.50 C ANISOU 1592 CB PHE A1102 11704 10885 7997 -204 -550 1679 C ATOM 1593 CG PHE A1102 -7.273 -4.269 -7.591 1.00 82.68 C ANISOU 1593 CG PHE A1102 11651 11240 8525 -272 -541 1785 C ATOM 1594 CD1 PHE A1102 -7.853 -5.507 -7.365 1.00 84.73 C ANISOU 1594 CD1 PHE A1102 11659 11511 9023 -191 -340 1793 C ATOM 1595 CD2 PHE A1102 -6.045 -4.219 -8.231 1.00 84.67 C ANISOU 1595 CD2 PHE A1102 11841 11554 8776 -414 -734 1873 C ATOM 1596 CE1 PHE A1102 -7.214 -6.669 -7.758 1.00 84.03 C ANISOU 1596 CE1 PHE A1102 11267 11496 9166 -252 -333 1889 C ATOM 1597 CE2 PHE A1102 -5.401 -5.378 -8.624 1.00 83.50 C ANISOU 1597 CE2 PHE A1102 11389 11480 8859 -476 -727 1969 C ATOM 1598 CZ PHE A1102 -5.987 -6.604 -8.387 1.00 81.41 C ANISOU 1598 CZ PHE A1102 10877 11226 8829 -394 -527 1976 C ATOM 1599 N GLN A1103 -5.752 -1.020 -5.810 1.00 88.92 N ANISOU 1599 N GLN A1103 13452 11931 8405 -532 -987 1951 N ATOM 1600 CA GLN A1103 -4.333 -0.672 -5.755 1.00 93.14 C ANISOU 1600 CA GLN A1103 14095 12503 8792 -715 -1210 2102 C ATOM 1601 C GLN A1103 -3.826 -0.355 -4.345 1.00 97.69 C ANISOU 1601 C GLN A1103 14962 13043 9113 -809 -1261 2257 C ATOM 1602 O GLN A1103 -2.813 -0.905 -3.908 1.00 95.77 O ANISOU 1602 O GLN A1103 14680 12837 8870 -940 -1332 2431 O ATOM 1603 CB GLN A1103 -4.049 0.515 -6.672 1.00 90.93 C ANISOU 1603 CB GLN A1103 13945 12222 8383 -745 -1393 2010 C ATOM 1604 CG GLN A1103 -2.575 0.856 -6.791 1.00 92.96 C ANISOU 1604 CG GLN A1103 14283 12522 8515 -932 -1626 2154 C ATOM 1605 CD GLN A1103 -2.326 2.007 -7.740 1.00 97.00 C ANISOU 1605 CD GLN A1103 14913 13033 8909 -957 -1800 2057 C ATOM 1606 OE1 GLN A1103 -3.262 2.676 -8.176 1.00100.59 O ANISOU 1606 OE1 GLN A1103 15438 13447 9336 -837 -1756 1886 O ATOM 1607 NE2 GLN A1103 -1.062 2.243 -8.070 1.00 93.05 N ANISOU 1607 NE2 GLN A1103 14436 12579 8342 -1114 -2001 2165 N ATOM 1608 N MET A1104 -4.528 0.526 -3.639 1.00 97.42 N ANISOU 1608 N MET A1104 15216 12935 8863 -741 -1226 2192 N ATOM 1609 CA MET A1104 -4.042 1.033 -2.357 1.00105.53 C ANISOU 1609 CA MET A1104 16559 13922 9616 -830 -1297 2326 C ATOM 1610 C MET A1104 -4.881 0.581 -1.161 1.00106.10 C ANISOU 1610 C MET A1104 16701 13942 9671 -744 -1097 2344 C ATOM 1611 O MET A1104 -4.702 1.081 -0.050 1.00103.38 O ANISOU 1611 O MET A1104 16642 13552 9087 -790 -1132 2429 O ATOM 1612 CB MET A1104 -3.981 2.562 -2.392 1.00109.79 C ANISOU 1612 CB MET A1104 17430 14418 9869 -849 -1455 2262 C ATOM 1613 CG MET A1104 -5.340 3.233 -2.470 1.00112.83 C ANISOU 1613 CG MET A1104 17926 14739 10206 -683 -1338 2069 C ATOM 1614 SD MET A1104 -5.260 4.944 -3.032 1.00150.37 S ANISOU 1614 SD MET A1104 22972 19459 14701 -697 -1537 1957 S ATOM 1615 CE MET A1104 -4.607 4.721 -4.683 1.00114.66 C ANISOU 1615 CE MET A1104 18164 15015 10385 -748 -1660 1913 C ATOM 1616 N GLY A1105 -5.795 -0.357 -1.388 1.00114.14 N ANISOU 1616 N GLY A1105 18079 13176 12114 2982 -2483 1702 N ATOM 1617 CA GLY A1105 -6.623 -0.873 -0.313 1.00117.97 C ANISOU 1617 CA GLY A1105 18735 13797 12290 2817 -2414 1772 C ATOM 1618 C GLY A1105 -7.827 0.007 -0.044 1.00124.08 C ANISOU 1618 C GLY A1105 19382 14660 13102 2687 -2142 1644 C ATOM 1619 O GLY A1105 -7.998 1.050 -0.676 1.00119.61 O ANISOU 1619 O GLY A1105 18593 14053 12801 2726 -2008 1493 O ATOM 1620 N GLU A1106 -8.664 -0.413 0.899 1.00130.43 N ANISOU 1620 N GLU A1106 20332 15587 13639 2531 -2060 1703 N ATOM 1621 CA GLU A1106 -9.901 0.301 1.198 1.00131.94 C ANISOU 1621 CA GLU A1106 20425 15867 13839 2393 -1802 1602 C ATOM 1622 C GLU A1106 -9.652 1.630 1.912 1.00134.80 C ANISOU 1622 C GLU A1106 20633 16373 14213 2383 -1710 1332 C ATOM 1623 O GLU A1106 -10.142 2.684 1.488 1.00132.50 O ANISOU 1623 O GLU A1106 20132 16076 14138 2376 -1530 1179 O ATOM 1624 CB GLU A1106 -10.824 -0.576 2.051 1.00135.07 C ANISOU 1624 CB GLU A1106 21033 16359 13930 2229 -1752 1747 C ATOM 1625 CG GLU A1106 -11.282 -1.874 1.385 1.00134.25 C ANISOU 1625 CG GLU A1106 21081 16122 13805 2215 -1810 2016 C ATOM 1626 CD GLU A1106 -10.240 -2.981 1.437 1.00133.15 C ANISOU 1626 CD GLU A1106 21133 15930 13528 2305 -2082 2178 C ATOM 1627 OE1 GLU A1106 -9.220 -2.815 2.140 1.00130.86 O ANISOU 1627 OE1 GLU A1106 20884 15722 13116 2360 -2222 2087 O ATOM 1628 OE2 GLU A1106 -10.447 -4.020 0.772 1.00128.39 O ANISOU 1628 OE2 GLU A1106 20641 15202 12939 2320 -2155 2395 O ATOM 1629 N THR A1107 -8.876 1.576 2.990 1.00140.13 N ANISOU 1629 N THR A1107 21411 17174 14657 2387 -1836 1272 N ATOM 1630 CA THR A1107 -8.588 2.758 3.794 1.00140.46 C ANISOU 1630 CA THR A1107 21328 17364 14675 2376 -1766 1023 C ATOM 1631 C THR A1107 -7.744 3.761 3.012 1.00135.93 C ANISOU 1631 C THR A1107 20529 16712 14408 2527 -1791 855 C ATOM 1632 O THR A1107 -7.803 4.967 3.261 1.00139.61 O ANISOU 1632 O THR A1107 20817 17260 14968 2519 -1665 636 O ATOM 1633 CB THR A1107 -7.864 2.387 5.105 1.00149.02 C ANISOU 1633 CB THR A1107 22588 18593 15439 2358 -1917 1009 C ATOM 1634 OG1 THR A1107 -8.496 1.244 5.695 1.00151.35 O ANISOU 1634 OG1 THR A1107 23120 18931 15455 2240 -1936 1203 O ATOM 1635 CG2 THR A1107 -7.906 3.546 6.092 1.00150.93 C ANISOU 1635 CG2 THR A1107 22722 19013 15613 2304 -1802 767 C ATOM 1636 N GLY A1108 -6.967 3.258 2.057 1.00131.24 N ANISOU 1636 N GLY A1108 19941 15956 13968 2665 -1952 959 N ATOM 1637 CA GLY A1108 -6.109 4.108 1.251 1.00131.50 C ANISOU 1637 CA GLY A1108 19771 15900 14293 2816 -1993 817 C ATOM 1638 C GLY A1108 -6.906 5.050 0.371 1.00132.33 C ANISOU 1638 C GLY A1108 19646 15938 14693 2806 -1775 715 C ATOM 1639 O GLY A1108 -6.505 6.193 0.150 1.00134.16 O ANISOU 1639 O GLY A1108 19676 16178 15119 2874 -1721 512 O ATOM 1640 N VAL A1109 -8.037 4.568 -0.134 1.00130.47 N ANISOU 1640 N VAL A1109 19443 15637 14492 2722 -1652 855 N ATOM 1641 CA VAL A1109 -8.953 5.406 -0.898 1.00128.26 C ANISOU 1641 CA VAL A1109 18962 15304 14467 2693 -1428 766 C ATOM 1642 C VAL A1109 -9.871 6.179 0.042 1.00129.85 C ANISOU 1642 C VAL A1109 19112 15679 14546 2543 -1221 617 C ATOM 1643 O VAL A1109 -10.343 7.270 -0.286 1.00127.92 O ANISOU 1643 O VAL A1109 18664 15443 14497 2531 -1044 451 O ATOM 1644 CB VAL A1109 -9.796 4.571 -1.875 1.00123.93 C ANISOU 1644 CB VAL A1109 18465 14605 14017 2669 -1380 976 C ATOM 1645 CG1 VAL A1109 -10.591 5.471 -2.807 1.00124.04 C ANISOU 1645 CG1 VAL A1109 18256 14541 14331 2667 -1168 877 C ATOM 1646 CG2 VAL A1109 -8.898 3.661 -2.674 1.00119.52 C ANISOU 1646 CG2 VAL A1109 17990 13888 13534 2807 -1601 1145 C ATOM 1647 N ALA A1110 -10.098 5.620 1.227 1.00132.91 N ANISOU 1647 N ALA A1110 19685 16208 14606 2432 -1248 673 N ATOM 1648 CA ALA A1110 -10.927 6.284 2.227 1.00131.23 C ANISOU 1648 CA ALA A1110 19443 16173 14245 2286 -1066 538 C ATOM 1649 C ALA A1110 -10.254 7.558 2.738 1.00133.29 C ANISOU 1649 C ALA A1110 19541 16542 14561 2335 -1047 276 C ATOM 1650 O ALA A1110 -10.908 8.429 3.308 1.00135.05 O ANISOU 1650 O ALA A1110 19666 16892 14757 2240 -872 118 O ATOM 1651 CB ALA A1110 -11.231 5.341 3.380 1.00133.27 C ANISOU 1651 CB ALA A1110 19948 16555 14135 2165 -1117 665 C ATOM 1652 N GLY A1111 -8.944 7.662 2.529 1.00129.52 N ANISOU 1652 N GLY A1111 19035 16015 14162 2483 -1230 229 N ATOM 1653 CA GLY A1111 -8.177 8.792 3.024 1.00133.27 C ANISOU 1653 CA GLY A1111 19367 16587 14681 2542 -1238 -11 C ATOM 1654 C GLY A1111 -8.266 10.043 2.167 1.00132.59 C ANISOU 1654 C GLY A1111 19010 16439 14931 2604 -1100 -192 C ATOM 1655 O GLY A1111 -7.734 11.091 2.537 1.00130.31 O ANISOU 1655 O GLY A1111 18581 16232 14699 2646 -1081 -405 O ATOM 1656 N PHE A1112 -8.928 9.937 1.020 1.00133.64 N ANISOU 1656 N PHE A1112 19067 16425 15285 2613 -1005 -108 N ATOM 1657 CA PHE A1112 -9.146 11.091 0.150 1.00132.40 C ANISOU 1657 CA PHE A1112 18655 16200 15451 2663 -857 -270 C ATOM 1658 C PHE A1112 -10.565 11.640 0.289 1.00131.40 C ANISOU 1658 C PHE A1112 18448 16143 15335 2517 -599 -335 C ATOM 1659 O PHE A1112 -11.222 11.912 -0.714 1.00127.93 O ANISOU 1659 O PHE A1112 17886 15590 15132 2523 -470 -328 O ATOM 1660 CB PHE A1112 -8.894 10.730 -1.319 1.00128.31 C ANISOU 1660 CB PHE A1112 18081 15462 15209 2785 -917 -155 C ATOM 1661 CG PHE A1112 -7.477 10.332 -1.626 1.00129.84 C ANISOU 1661 CG PHE A1112 18318 15571 15444 2943 -1161 -111 C ATOM 1662 CD1 PHE A1112 -6.454 11.267 -1.595 1.00124.99 C ANISOU 1662 CD1 PHE A1112 17558 14978 14953 3053 -1221 -305 C ATOM 1663 CD2 PHE A1112 -7.173 9.026 -1.978 1.00132.17 C ANISOU 1663 CD2 PHE A1112 18795 15762 15662 2984 -1330 124 C ATOM 1664 CE1 PHE A1112 -5.152 10.903 -1.889 1.00121.19 C ANISOU 1664 CE1 PHE A1112 17115 14418 14514 3199 -1444 -267 C ATOM 1665 CE2 PHE A1112 -5.873 8.655 -2.274 1.00129.69 C ANISOU 1665 CE2 PHE A1112 18519 15369 15387 3130 -1556 164 C ATOM 1666 CZ PHE A1112 -4.862 9.595 -2.229 1.00125.13 C ANISOU 1666 CZ PHE A1112 17797 14815 14931 3237 -1613 -33 C ATOM 1667 N THR A1113 -11.037 11.800 1.524 1.00134.85 N ANISOU 1667 N THR A1113 18953 16765 15517 2387 -524 -400 N ATOM 1668 CA THR A1113 -12.424 12.205 1.755 1.00133.48 C ANISOU 1668 CA THR A1113 18730 16669 15318 2235 -286 -446 C ATOM 1669 C THR A1113 -12.742 13.574 1.154 1.00127.97 C ANISOU 1669 C THR A1113 17765 15951 14905 2260 -110 -657 C ATOM 1670 O THR A1113 -13.829 13.782 0.599 1.00123.68 O ANISOU 1670 O THR A1113 17145 15363 14486 2191 72 -648 O ATOM 1671 CB THR A1113 -12.752 12.234 3.261 1.00133.56 C ANISOU 1671 CB THR A1113 18850 16894 15003 2100 -247 -501 C ATOM 1672 OG1 THR A1113 -11.652 12.800 3.981 1.00138.80 O ANISOU 1672 OG1 THR A1113 19481 17657 15600 2171 -362 -655 O ATOM 1673 CG2 THR A1113 -13.014 10.830 3.779 1.00131.49 C ANISOU 1673 CG2 THR A1113 18854 16648 14457 2022 -342 -267 C ATOM 1674 N ASN A1114 -11.776 14.485 1.230 1.00128.18 N ANISOU 1674 N ASN A1114 17654 16007 15041 2362 -167 -843 N ATOM 1675 CA ASN A1114 -11.920 15.806 0.628 1.00126.57 C ANISOU 1675 CA ASN A1114 17193 15778 15118 2403 -21 -1049 C ATOM 1676 C ASN A1114 -12.003 15.722 -0.893 1.00128.02 C ANISOU 1676 C ASN A1114 17277 15748 15616 2498 -2 -975 C ATOM 1677 O ASN A1114 -12.622 16.567 -1.538 1.00127.88 O ANISOU 1677 O ASN A1114 17077 15688 15822 2490 170 -1087 O ATOM 1678 CB ASN A1114 -10.763 16.718 1.041 1.00119.85 C ANISOU 1678 CB ASN A1114 16229 14998 14309 2503 -108 -1252 C ATOM 1679 CG ASN A1114 -10.920 17.263 2.450 1.00129.22 C ANISOU 1679 CG ASN A1114 17434 16407 15258 2400 -50 -1397 C ATOM 1680 OD1 ASN A1114 -12.034 17.429 2.945 1.00122.67 O ANISOU 1680 OD1 ASN A1114 16612 15678 14319 2256 120 -1419 O ATOM 1681 ND2 ASN A1114 -9.797 17.551 3.101 1.00137.76 N ANISOU 1681 ND2 ASN A1114 18518 17565 16258 2475 -192 -1500 N ATOM 1682 N SER A1115 -11.360 14.706 -1.461 1.00126.62 N ANISOU 1682 N SER A1115 17220 15438 15454 2591 -183 -789 N ATOM 1683 CA SER A1115 -11.442 14.464 -2.896 1.00122.44 C ANISOU 1683 CA SER A1115 16620 14699 15201 2681 -182 -689 C ATOM 1684 C SER A1115 -12.640 13.582 -3.243 1.00120.21 C ANISOU 1684 C SER A1115 16450 14356 14869 2578 -87 -494 C ATOM 1685 O SER A1115 -13.068 13.531 -4.395 1.00115.89 O ANISOU 1685 O SER A1115 15823 13653 14555 2619 -20 -432 O ATOM 1686 CB SER A1115 -10.150 13.825 -3.408 1.00119.75 C ANISOU 1686 CB SER A1115 16344 14238 14919 2838 -424 -586 C ATOM 1687 OG SER A1115 -10.157 13.726 -4.821 1.00113.10 O ANISOU 1687 OG SER A1115 15410 13194 14368 2937 -420 -514 O ATOM 1688 N LEU A1116 -13.174 12.888 -2.241 1.00122.61 N ANISOU 1688 N LEU A1116 16938 14782 14867 2446 -82 -397 N ATOM 1689 CA LEU A1116 -14.358 12.055 -2.433 1.00118.62 C ANISOU 1689 CA LEU A1116 16547 14238 14285 2334 14 -217 C ATOM 1690 C LEU A1116 -15.613 12.912 -2.547 1.00117.71 C ANISOU 1690 C LEU A1116 16286 14166 14272 2226 277 -341 C ATOM 1691 O LEU A1116 -16.453 12.699 -3.431 1.00119.33 O ANISOU 1691 O LEU A1116 16457 14254 14629 2206 386 -255 O ATOM 1692 CB LEU A1116 -14.508 11.056 -1.282 1.00122.20 C ANISOU 1692 CB LEU A1116 17245 14813 14371 2225 -65 -80 C ATOM 1693 CG LEU A1116 -13.594 9.831 -1.286 1.00125.10 C ANISOU 1693 CG LEU A1116 17809 15113 14611 2304 -314 117 C ATOM 1694 CD1 LEU A1116 -13.597 9.158 0.079 1.00128.20 C ANISOU 1694 CD1 LEU A1116 18415 15666 14629 2199 -386 184 C ATOM 1695 CD2 LEU A1116 -14.023 8.851 -2.367 1.00115.94 C ANISOU 1695 CD2 LEU A1116 16719 13771 13562 2329 -336 342 C ATOM 1696 N ARG A1117 -15.727 13.895 -1.657 1.00118.61 N ANISOU 1696 N ARG A1117 16312 14448 14305 2161 376 -546 N ATOM 1697 CA ARG A1117 -16.895 14.765 -1.652 1.00119.81 C ANISOU 1697 CA ARG A1117 16326 14661 14535 2053 623 -680 C ATOM 1698 C ARG A1117 -16.995 15.579 -2.939 1.00117.94 C ANISOU 1698 C ARG A1117 15868 14278 14666 2146 722 -777 C ATOM 1699 O ARG A1117 -18.094 15.930 -3.369 1.00116.25 O ANISOU 1699 O ARG A1117 15567 14040 14564 2072 916 -807 O ATOM 1700 CB ARG A1117 -16.860 15.699 -0.442 1.00117.15 C ANISOU 1700 CB ARG A1117 15931 14533 14045 1980 691 -890 C ATOM 1701 CG ARG A1117 -15.539 16.413 -0.256 1.00119.55 C ANISOU 1701 CG ARG A1117 16138 14867 14417 2107 563 -1048 C ATOM 1702 CD ARG A1117 -15.628 17.451 0.843 1.00126.06 C ANISOU 1702 CD ARG A1117 16879 15893 15125 2034 657 -1270 C ATOM 1703 NE ARG A1117 -16.556 18.522 0.495 1.00132.83 N ANISOU 1703 NE ARG A1117 17542 16768 16160 1976 887 -1430 N ATOM 1704 CZ ARG A1117 -16.228 19.581 -0.237 1.00136.85 C ANISOU 1704 CZ ARG A1117 17832 17213 16953 2072 940 -1598 C ATOM 1705 NH1 ARG A1117 -14.992 19.711 -0.701 1.00131.03 N ANISOU 1705 NH1 ARG A1117 17041 16388 16355 2229 780 -1627 N ATOM 1706 NH2 ARG A1117 -17.134 20.511 -0.507 1.00137.57 N ANISOU 1706 NH2 ARG A1117 17758 17325 17188 2010 1152 -1739 N ATOM 1707 N MET A1118 -15.853 15.870 -3.556 1.00117.58 N ANISOU 1707 N MET A1118 15732 14135 14808 2306 590 -826 N ATOM 1708 CA MET A1118 -15.843 16.668 -4.779 1.00119.94 C ANISOU 1708 CA MET A1118 15818 14292 15460 2405 672 -925 C ATOM 1709 C MET A1118 -16.489 15.936 -5.950 1.00116.58 C ANISOU 1709 C MET A1118 15421 13682 15191 2422 709 -741 C ATOM 1710 O MET A1118 -17.336 16.495 -6.646 1.00114.13 O ANISOU 1710 O MET A1118 14975 13312 15079 2397 888 -804 O ATOM 1711 CB MET A1118 -14.414 17.071 -5.150 1.00122.29 C ANISOU 1711 CB MET A1118 16028 14528 15911 2576 507 -1008 C ATOM 1712 CG MET A1118 -13.840 18.187 -4.292 1.00128.90 C ANISOU 1712 CG MET A1118 16753 15521 16703 2581 518 -1249 C ATOM 1713 SD MET A1118 -12.334 18.904 -4.977 1.00185.77 S ANISOU 1713 SD MET A1118 23795 22626 24163 2785 375 -1380 S ATOM 1714 CE MET A1118 -11.176 17.564 -4.731 1.00125.04 C ANISOU 1714 CE MET A1118 16330 14893 16289 2868 84 -1175 C ATOM 1715 N LEU A1119 -16.088 14.688 -6.172 1.00116.48 N ANISOU 1715 N LEU A1119 15585 13580 15093 2466 539 -516 N ATOM 1716 CA LEU A1119 -16.695 13.893 -7.233 1.00111.50 C ANISOU 1716 CA LEU A1119 14998 12776 14591 2480 562 -325 C ATOM 1717 C LEU A1119 -18.108 13.466 -6.841 1.00110.56 C ANISOU 1717 C LEU A1119 14973 12721 14315 2309 724 -241 C ATOM 1718 O LEU A1119 -18.936 13.173 -7.705 1.00108.36 O ANISOU 1718 O LEU A1119 14674 12320 14176 2293 824 -146 O ATOM 1719 CB LEU A1119 -15.824 12.678 -7.571 1.00109.81 C ANISOU 1719 CB LEU A1119 14947 12451 14327 2579 325 -109 C ATOM 1720 CG LEU A1119 -15.848 11.430 -6.688 1.00109.91 C ANISOU 1720 CG LEU A1119 15217 12538 14005 2498 205 82 C ATOM 1721 CD1 LEU A1119 -16.792 10.389 -7.266 1.00107.33 C ANISOU 1721 CD1 LEU A1119 15006 12104 13669 2441 249 306 C ATOM 1722 CD2 LEU A1119 -14.447 10.857 -6.541 1.00107.93 C ANISOU 1722 CD2 LEU A1119 15068 12261 13678 2618 -55 153 C ATOM 1723 N GLN A1120 -18.385 13.425 -5.539 1.00110.00 N ANISOU 1723 N GLN A1120 15004 12840 13953 2182 750 -276 N ATOM 1724 CA GLN A1120 -19.753 13.198 -5.083 1.00112.60 C ANISOU 1724 CA GLN A1120 15400 13249 14134 2011 924 -232 C ATOM 1725 C GLN A1120 -20.643 14.386 -5.453 1.00111.18 C ANISOU 1725 C GLN A1120 15010 13082 14152 1963 1163 -421 C ATOM 1726 O GLN A1120 -21.846 14.235 -5.670 1.00107.83 O ANISOU 1726 O GLN A1120 14591 12642 13737 1861 1326 -372 O ATOM 1727 CB GLN A1120 -19.794 12.953 -3.573 1.00116.93 C ANISOU 1727 CB GLN A1120 16098 14003 14328 1889 896 -241 C ATOM 1728 CG GLN A1120 -21.148 12.476 -3.065 1.00113.33 C ANISOU 1728 CG GLN A1120 15751 13625 13684 1712 1046 -154 C ATOM 1729 CD GLN A1120 -21.155 12.207 -1.574 1.00116.98 C ANISOU 1729 CD GLN A1120 16367 14288 13793 1596 1012 -158 C ATOM 1730 OE1 GLN A1120 -20.239 12.608 -0.855 1.00115.85 O ANISOU 1730 OE1 GLN A1120 16216 14246 13555 1638 909 -268 O ATOM 1731 NE2 GLN A1120 -22.190 11.521 -1.101 1.00115.93 N ANISOU 1731 NE2 GLN A1120 16375 14212 13463 1450 1099 -37 N ATOM 1732 N GLN A1121 -20.032 15.566 -5.529 1.00112.09 N ANISOU 1732 N GLN A1121 14938 13224 14425 2040 1181 -639 N ATOM 1733 CA GLN A1121 -20.724 16.795 -5.911 1.00114.43 C ANISOU 1733 CA GLN A1121 15019 13530 14928 2014 1394 -838 C ATOM 1734 C GLN A1121 -20.642 16.991 -7.428 1.00112.11 C ANISOU 1734 C GLN A1121 14588 13023 14985 2141 1413 -823 C ATOM 1735 O GLN A1121 -21.074 18.014 -7.964 1.00112.70 O ANISOU 1735 O GLN A1121 14471 13072 15280 2150 1571 -985 O ATOM 1736 CB GLN A1121 -20.128 17.997 -5.164 1.00118.34 C ANISOU 1736 CB GLN A1121 15384 14174 15407 2027 1407 -1087 C ATOM 1737 CG GLN A1121 -20.952 19.281 -5.228 1.00116.28 C ANISOU 1737 CG GLN A1121 14922 13975 15285 1963 1637 -1307 C ATOM 1738 CD GLN A1121 -22.331 19.130 -4.620 1.00120.60 C ANISOU 1738 CD GLN A1121 15535 14631 15657 1780 1814 -1285 C ATOM 1739 OE1 GLN A1121 -22.499 18.489 -3.584 1.00123.19 O ANISOU 1739 OE1 GLN A1121 16033 15085 15689 1679 1773 -1202 O ATOM 1740 NE2 GLN A1121 -23.330 19.721 -5.268 1.00118.00 N ANISOU 1740 NE2 GLN A1121 15070 14252 15511 1738 2014 -1361 N ATOM 1741 N LYS A1122 -20.075 15.993 -8.102 1.00107.97 N ANISOU 1741 N LYS A1122 14167 12349 14506 2239 1249 -626 N ATOM 1742 CA LYS A1122 -19.883 15.994 -9.553 1.00 99.60 C ANISOU 1742 CA LYS A1122 13003 11076 13764 2372 1234 -578 C ATOM 1743 C LYS A1122 -18.971 17.124 -10.034 1.00100.48 C ANISOU 1743 C LYS A1122 12910 11147 14120 2507 1211 -776 C ATOM 1744 O LYS A1122 -19.080 17.574 -11.175 1.00 98.18 O ANISOU 1744 O LYS A1122 12471 10710 14122 2591 1278 -817 O ATOM 1745 CB LYS A1122 -21.234 16.079 -10.275 1.00 93.10 C ANISOU 1745 CB LYS A1122 12117 10174 13083 2301 1443 -555 C ATOM 1746 CG LYS A1122 -22.215 14.980 -9.903 1.00 93.51 C ANISOU 1746 CG LYS A1122 12361 10252 12917 2168 1481 -358 C ATOM 1747 CD LYS A1122 -21.703 13.617 -10.332 1.00 93.72 C ANISOU 1747 CD LYS A1122 12561 10151 12896 2241 1287 -101 C ATOM 1748 CE LYS A1122 -22.725 12.528 -10.051 1.00 93.27 C ANISOU 1748 CE LYS A1122 12688 10108 12643 2111 1334 97 C ATOM 1749 NZ LYS A1122 -22.261 11.199 -10.539 1.00 92.68 N ANISOU 1749 NZ LYS A1122 12777 9900 12535 2184 1147 351 N ATOM 1750 N ARG A1123 -18.069 17.574 -9.166 1.00125.03 N ANISOU 1750 N ARG A1123 19389 15025 13092 1946 -419 227 N ATOM 1751 CA ARG A1123 -17.036 18.529 -9.558 1.00126.51 C ANISOU 1751 CA ARG A1123 19791 15108 13169 1839 -159 350 C ATOM 1752 C ARG A1123 -15.817 17.788 -10.098 1.00123.87 C ANISOU 1752 C ARG A1123 19225 14925 12915 1813 -314 493 C ATOM 1753 O ARG A1123 -14.772 17.744 -9.450 1.00123.29 O ANISOU 1753 O ARG A1123 19084 14905 12854 1369 -324 597 O ATOM 1754 CB ARG A1123 -16.627 19.414 -8.378 1.00128.40 C ANISOU 1754 CB ARG A1123 20223 15242 13321 1295 44 375 C ATOM 1755 CG ARG A1123 -17.745 20.271 -7.809 1.00132.74 C ANISOU 1755 CG ARG A1123 21031 15624 13781 1284 232 243 C ATOM 1756 CD ARG A1123 -17.204 21.234 -6.763 1.00137.41 C ANISOU 1756 CD ARG A1123 21833 16103 14274 755 463 284 C ATOM 1757 NE ARG A1123 -16.616 20.536 -5.622 1.00136.99 N ANISOU 1757 NE ARG A1123 21553 16189 14310 248 272 328 N ATOM 1758 CZ ARG A1123 -17.183 20.454 -4.423 1.00138.97 C ANISOU 1758 CZ ARG A1123 21782 16438 14581 -70 220 244 C ATOM 1759 NH1 ARG A1123 -18.353 21.037 -4.199 1.00140.51 N ANISOU 1759 NH1 ARG A1123 22174 16499 14716 63 347 109 N ATOM 1760 NH2 ARG A1123 -16.578 19.797 -3.443 1.00137.56 N ANISOU 1760 NH2 ARG A1123 21390 16394 14484 -522 42 294 N ATOM 1761 N TRP A1124 -15.958 17.207 -11.285 1.00117.83 N ANISOU 1761 N TRP A1124 18336 14231 12203 2289 -435 496 N ATOM 1762 CA TRP A1124 -14.943 16.305 -11.822 1.00117.84 C ANISOU 1762 CA TRP A1124 18071 14398 12305 2309 -631 615 C ATOM 1763 C TRP A1124 -13.583 16.973 -12.072 1.00123.68 C ANISOU 1763 C TRP A1124 18935 15089 12970 2094 -440 769 C ATOM 1764 O TRP A1124 -12.533 16.347 -11.875 1.00122.11 O ANISOU 1764 O TRP A1124 18524 15023 12848 1835 -584 880 O ATOM 1765 CB TRP A1124 -15.456 15.666 -13.116 1.00112.73 C ANISOU 1765 CB TRP A1124 17302 13815 11716 2897 -766 578 C ATOM 1766 CG TRP A1124 -16.748 14.903 -12.944 1.00111.98 C ANISOU 1766 CG TRP A1124 17056 13787 11704 3128 -975 431 C ATOM 1767 CD1 TRP A1124 -16.946 13.788 -12.181 1.00106.39 C ANISOU 1767 CD1 TRP A1124 16053 13240 11131 2939 -1265 394 C ATOM 1768 CD2 TRP A1124 -18.013 15.196 -13.557 1.00110.51 C ANISOU 1768 CD2 TRP A1124 17006 13511 11471 3591 -909 301 C ATOM 1769 NE1 TRP A1124 -18.252 13.373 -12.274 1.00102.72 N ANISOU 1769 NE1 TRP A1124 15535 12790 10706 3251 -1382 247 N ATOM 1770 CE2 TRP A1124 -18.929 14.220 -13.113 1.00106.92 C ANISOU 1770 CE2 TRP A1124 16326 13171 11128 3655 -1169 187 C ATOM 1771 CE3 TRP A1124 -18.461 16.190 -14.434 1.00118.72 C ANISOU 1771 CE3 TRP A1124 18337 14386 12385 3958 -655 270 C ATOM 1772 CZ2 TRP A1124 -20.264 14.208 -13.516 1.00107.18 C ANISOU 1772 CZ2 TRP A1124 16412 13161 11150 4069 -1182 43 C ATOM 1773 CZ3 TRP A1124 -19.788 16.176 -14.833 1.00120.64 C ANISOU 1773 CZ3 TRP A1124 18632 14586 12617 4371 -671 129 C ATOM 1774 CH2 TRP A1124 -20.673 15.192 -14.374 1.00112.95 C ANISOU 1774 CH2 TRP A1124 17428 13732 11757 4422 -933 17 C ATOM 1775 N ASP A1125 -13.598 18.237 -12.479 1.00127.40 N ANISOU 1775 N ASP A1125 19745 15369 13290 2192 -119 774 N ATOM 1776 CA ASP A1125 -12.361 18.931 -12.833 1.00127.42 C ANISOU 1776 CA ASP A1125 19887 15314 13212 2037 81 912 C ATOM 1777 C ASP A1125 -11.449 19.167 -11.627 1.00129.77 C ANISOU 1777 C ASP A1125 20184 15626 13496 1411 127 991 C ATOM 1778 O ASP A1125 -10.278 18.764 -11.629 1.00131.25 O ANISOU 1778 O ASP A1125 20216 15921 13733 1188 44 1116 O ATOM 1779 CB ASP A1125 -12.677 20.270 -13.507 1.00135.01 C ANISOU 1779 CB ASP A1125 21229 16057 14010 2290 425 889 C ATOM 1780 CG ASP A1125 -13.331 20.103 -14.869 1.00136.16 C ANISOU 1780 CG ASP A1125 21385 16189 14159 2916 401 842 C ATOM 1781 OD1 ASP A1125 -14.051 19.104 -15.071 1.00137.42 O ANISOU 1781 OD1 ASP A1125 21314 16470 14430 3174 145 768 O ATOM 1782 OD2 ASP A1125 -13.124 20.977 -15.740 1.00138.33 O ANISOU 1782 OD2 ASP A1125 21902 16334 14323 3150 641 879 O ATOM 1783 N GLU A1126 -11.989 19.807 -10.594 1.00130.37 N ANISOU 1783 N GLU A1126 20429 15598 13507 1125 258 916 N ATOM 1784 CA GLU A1126 -11.202 20.105 -9.405 1.00135.95 C ANISOU 1784 CA GLU A1126 21156 16309 14189 525 319 981 C ATOM 1785 C GLU A1126 -10.783 18.831 -8.690 1.00134.41 C ANISOU 1785 C GLU A1126 20593 16328 14148 237 -11 1018 C ATOM 1786 O GLU A1126 -9.696 18.763 -8.109 1.00133.62 O ANISOU 1786 O GLU A1126 20415 16294 14062 -191 -26 1127 O ATOM 1787 CB GLU A1126 -11.979 21.016 -8.456 1.00139.42 C ANISOU 1787 CB GLU A1126 21848 16592 14531 304 518 880 C ATOM 1788 CG GLU A1126 -11.717 22.496 -8.674 1.00142.01 C ANISOU 1788 CG GLU A1126 22560 16710 14687 265 904 908 C ATOM 1789 CD GLU A1126 -10.289 22.892 -8.337 1.00145.85 C ANISOU 1789 CD GLU A1126 23083 17206 15129 -169 1020 1052 C ATOM 1790 OE1 GLU A1126 -10.063 23.410 -7.223 1.00154.35 O ANISOU 1790 OE1 GLU A1126 24262 18232 16153 -643 1134 1056 O ATOM 1791 OE2 GLU A1126 -9.391 22.686 -9.182 1.00143.03 O ANISOU 1791 OE2 GLU A1126 22652 16906 14787 -40 998 1161 O ATOM 1792 N ALA A1127 -11.642 17.818 -8.751 1.00130.61 N ANISOU 1792 N ALA A1127 19885 15958 13783 478 -276 928 N ATOM 1793 CA ALA A1127 -11.306 16.517 -8.197 1.00125.80 C ANISOU 1793 CA ALA A1127 18909 15559 13330 267 -608 960 C ATOM 1794 C ALA A1127 -10.118 15.930 -8.940 1.00123.69 C ANISOU 1794 C ALA A1127 18451 15417 13127 317 -720 1103 C ATOM 1795 O ALA A1127 -9.232 15.331 -8.330 1.00123.16 O ANISOU 1795 O ALA A1127 18175 15483 13137 -54 -870 1194 O ATOM 1796 CB ALA A1127 -12.498 15.577 -8.272 1.00121.43 C ANISOU 1796 CB ALA A1127 18164 15090 12882 576 -855 832 C ATOM 1797 N ALA A1128 -10.086 16.138 -10.255 1.00122.37 N ANISOU 1797 N ALA A1128 18365 15204 12927 770 -637 1124 N ATOM 1798 CA ALA A1128 -8.974 15.651 -11.067 1.00119.41 C ANISOU 1798 CA ALA A1128 17830 14934 12606 853 -722 1257 C ATOM 1799 C ALA A1128 -7.675 16.377 -10.736 1.00123.23 C ANISOU 1799 C ALA A1128 18439 15372 13010 440 -532 1389 C ATOM 1800 O ALA A1128 -6.609 15.757 -10.660 1.00121.33 O ANISOU 1800 O ALA A1128 17986 15268 12847 224 -672 1506 O ATOM 1801 CB ALA A1128 -9.293 15.802 -12.545 1.00118.98 C ANISOU 1801 CB ALA A1128 17861 14826 12522 1435 -655 1241 C ATOM 1802 N VAL A1129 -7.771 17.685 -10.512 1.00127.14 N ANISOU 1802 N VAL A1129 19277 15677 13352 323 -213 1371 N ATOM 1803 CA VAL A1129 -6.590 18.478 -10.180 1.00129.40 C ANISOU 1803 CA VAL A1129 19712 15906 13548 -72 -5 1488 C ATOM 1804 C VAL A1129 -6.025 18.056 -8.827 1.00129.90 C ANISOU 1804 C VAL A1129 19606 16078 13670 -651 -135 1532 C ATOM 1805 O VAL A1129 -4.822 17.782 -8.688 1.00127.96 O ANISOU 1805 O VAL A1129 19230 15931 13460 -933 -190 1660 O ATOM 1806 CB VAL A1129 -6.913 19.987 -10.147 1.00128.95 C ANISOU 1806 CB VAL A1129 20067 15615 13312 -85 370 1446 C ATOM 1807 CG1 VAL A1129 -5.675 20.797 -9.782 1.00126.02 C ANISOU 1807 CG1 VAL A1129 19847 15188 12849 -506 586 1565 C ATOM 1808 CG2 VAL A1129 -7.478 20.437 -11.483 1.00128.01 C ANISOU 1808 CG2 VAL A1129 20123 15383 13130 489 505 1404 C ATOM 1809 N ASN A1130 -6.910 17.974 -7.837 1.00125.73 N ANISOU 1809 N ASN A1130 19075 15538 13156 -821 -191 1426 N ATOM 1810 CA ASN A1130 -6.491 17.602 -6.497 1.00126.12 C ANISOU 1810 CA ASN A1130 18978 15685 13258 -1370 -310 1455 C ATOM 1811 C ASN A1130 -5.948 16.178 -6.455 1.00124.22 C ANISOU 1811 C ASN A1130 18337 15675 13186 -1427 -661 1523 C ATOM 1812 O ASN A1130 -5.012 15.890 -5.709 1.00120.36 O ANISOU 1812 O ASN A1130 17711 15286 12735 -1870 -739 1617 O ATOM 1813 CB ASN A1130 -7.652 17.755 -5.514 1.00129.00 C ANISOU 1813 CB ASN A1130 19415 15989 13609 -1494 -311 1316 C ATOM 1814 CG ASN A1130 -7.228 17.528 -4.077 1.00132.46 C ANISOU 1814 CG ASN A1130 19743 16506 14080 -2088 -396 1344 C ATOM 1815 OD1 ASN A1130 -6.078 17.768 -3.713 1.00134.62 O ANISOU 1815 OD1 ASN A1130 20016 16809 14325 -2464 -329 1463 O ATOM 1816 ND2 ASN A1130 -8.157 17.057 -3.252 1.00137.07 N ANISOU 1816 ND2 ASN A1130 20230 17126 14723 -2175 -546 1235 N ATOM 1817 N LEU A1131 -6.522 15.290 -7.261 1.00120.59 N ANISOU 1817 N LEU A1131 17691 15302 12827 -981 -870 1476 N ATOM 1818 CA LEU A1131 -5.982 13.939 -7.359 1.00115.77 C ANISOU 1818 CA LEU A1131 16704 14906 12378 -992 -1194 1545 C ATOM 1819 C LEU A1131 -4.606 13.944 -8.010 1.00116.51 C ANISOU 1819 C LEU A1131 16747 15051 12472 -1038 -1159 1702 C ATOM 1820 O LEU A1131 -3.743 13.141 -7.655 1.00117.03 O ANISOU 1820 O LEU A1131 16553 15277 12638 -1299 -1354 1798 O ATOM 1821 CB LEU A1131 -6.927 13.026 -8.139 1.00112.15 C ANISOU 1821 CB LEU A1131 16069 14522 12022 -482 -1411 1456 C ATOM 1822 CG LEU A1131 -8.126 12.500 -7.350 1.00107.85 C ANISOU 1822 CG LEU A1131 15429 14011 11540 -498 -1575 1317 C ATOM 1823 CD1 LEU A1131 -8.971 11.593 -8.223 1.00100.97 C ANISOU 1823 CD1 LEU A1131 14380 13218 10768 22 -1784 1237 C ATOM 1824 CD2 LEU A1131 -7.672 11.773 -6.093 1.00111.47 C ANISOU 1824 CD2 LEU A1131 15651 14612 12091 -1002 -1778 1357 C ATOM 1825 N ALA A1132 -4.404 14.850 -8.962 1.00120.10 N ANISOU 1825 N ALA A1132 17449 15368 12814 -783 -908 1728 N ATOM 1826 CA ALA A1132 -3.104 14.967 -9.609 1.00124.53 C ANISOU 1826 CA ALA A1132 17993 15960 13361 -822 -845 1873 C ATOM 1827 C ALA A1132 -2.051 15.468 -8.626 1.00128.01 C ANISOU 1827 C ALA A1132 18491 16398 13748 -1408 -731 1971 C ATOM 1828 O ALA A1132 -0.872 15.131 -8.742 1.00128.70 O ANISOU 1828 O ALA A1132 18435 16588 13879 -1589 -796 2100 O ATOM 1829 CB ALA A1132 -3.188 15.883 -10.823 1.00122.35 C ANISOU 1829 CB ALA A1132 17991 15526 12969 -419 -588 1871 C ATOM 1830 N LYS A1133 -2.477 16.271 -7.656 1.00126.57 N ANISOU 1830 N LYS A1133 18517 16101 13471 -1706 -561 1908 N ATOM 1831 CA LYS A1133 -1.553 16.780 -6.641 1.00129.49 C ANISOU 1831 CA LYS A1133 18951 16466 13783 -2280 -447 1990 C ATOM 1832 C LYS A1133 -1.109 15.711 -5.628 1.00133.28 C ANISOU 1832 C LYS A1133 19103 17143 14395 -2678 -735 2038 C ATOM 1833 O LYS A1133 -0.067 15.849 -4.986 1.00138.46 O ANISOU 1833 O LYS A1133 19727 17848 15036 -3125 -704 2141 O ATOM 1834 CB LYS A1133 -2.179 17.967 -5.898 1.00133.36 C ANISOU 1834 CB LYS A1133 19768 16772 14132 -2479 -175 1905 C ATOM 1835 CG LYS A1133 -1.207 18.714 -4.992 1.00141.51 C ANISOU 1835 CG LYS A1133 20925 17767 15075 -3040 6 1989 C ATOM 1836 CD LYS A1133 -1.902 19.810 -4.202 1.00138.55 C ANISOU 1836 CD LYS A1133 20855 17216 14571 -3239 257 1896 C ATOM 1837 CE LYS A1133 -0.968 20.418 -3.168 1.00133.25 C ANISOU 1837 CE LYS A1133 20271 16532 13826 -3835 401 1975 C ATOM 1838 NZ LYS A1133 -1.643 21.481 -2.375 1.00122.02 N ANISOU 1838 NZ LYS A1133 19144 14938 12280 -4041 648 1883 N ATOM 1839 N SER A1134 -1.889 14.639 -5.504 1.00131.71 N ANISOU 1839 N SER A1134 18661 17058 14325 -2511 -1016 1964 N ATOM 1840 CA SER A1134 -1.680 13.635 -4.457 1.00127.31 C ANISOU 1840 CA SER A1134 17806 16675 13891 -2875 -1291 1986 C ATOM 1841 C SER A1134 -0.400 12.810 -4.631 1.00125.60 C ANISOU 1841 C SER A1134 17311 16636 13776 -3027 -1475 2136 C ATOM 1842 O SER A1134 0.117 12.671 -5.738 1.00128.95 O ANISOU 1842 O SER A1134 17698 17080 14217 -2730 -1473 2203 O ATOM 1843 CB SER A1134 -2.888 12.697 -4.385 1.00124.81 C ANISOU 1843 CB SER A1134 17306 16431 13686 -2611 -1539 1863 C ATOM 1844 OG SER A1134 -4.066 13.410 -4.046 1.00120.70 O ANISOU 1844 OG SER A1134 17023 15758 13079 -2533 -1386 1723 O ATOM 1845 N ARG A1135 0.109 12.285 -3.517 1.00128.04 N ANISOU 1845 N ARG A1135 17430 17069 14150 -3498 -1629 2188 N ATOM 1846 CA ARG A1135 1.337 11.486 -3.498 1.00133.86 C ANISOU 1846 CA ARG A1135 17892 17982 14986 -3706 -1813 2332 C ATOM 1847 C ARG A1135 1.192 10.231 -4.356 1.00135.04 C ANISOU 1847 C ARG A1135 17744 18276 15290 -3306 -2098 2338 C ATOM 1848 O ARG A1135 2.164 9.748 -4.958 1.00132.84 O ANISOU 1848 O ARG A1135 17301 18099 15075 -3260 -2187 2455 O ATOM 1849 CB ARG A1135 1.689 11.106 -2.055 1.00136.52 C ANISOU 1849 CB ARG A1135 18077 18426 15368 -4269 -1943 2365 C ATOM 1850 CG ARG A1135 3.133 10.682 -1.820 1.00139.38 C ANISOU 1850 CG ARG A1135 18243 18932 15784 -4616 -2039 2528 C ATOM 1851 CD ARG A1135 3.356 10.365 -0.344 1.00136.60 C ANISOU 1851 CD ARG A1135 17761 18675 15468 -5168 -2157 2547 C ATOM 1852 NE ARG A1135 4.766 10.174 -0.019 1.00134.38 N ANISOU 1852 NE ARG A1135 17340 18509 15210 -5552 -2200 2704 N ATOM 1853 CZ ARG A1135 5.562 11.133 0.444 1.00136.91 C ANISOU 1853 CZ ARG A1135 17852 18759 15410 -5931 -1968 2772 C ATOM 1854 NH1 ARG A1135 5.086 12.356 0.639 1.00138.89 N ANISOU 1854 NH1 ARG A1135 18443 18820 15507 -5978 -1674 2698 N ATOM 1855 NH2 ARG A1135 6.834 10.871 0.712 1.00133.85 N ANISOU 1855 NH2 ARG A1135 17313 18490 15053 -6262 -2028 2914 N ATOM 1856 N TRP A1136 -0.037 9.726 -4.424 1.00137.22 N ANISOU 1856 N TRP A1136 17956 18556 15624 -3012 -2233 2209 N ATOM 1857 CA TRP A1136 -0.363 8.564 -5.240 1.00133.93 C ANISOU 1857 CA TRP A1136 17275 18265 15349 -2599 -2495 2192 C ATOM 1858 C TRP A1136 -0.077 8.839 -6.710 1.00130.92 C ANISOU 1858 C TRP A1136 16982 17826 14934 -2152 -2383 2232 C ATOM 1859 O TRP A1136 0.278 7.933 -7.465 1.00126.64 O ANISOU 1859 O TRP A1136 16204 17409 14505 -1911 -2575 2286 O ATOM 1860 CB TRP A1136 -1.833 8.174 -5.048 1.00130.26 C ANISOU 1860 CB TRP A1136 16784 17785 14925 -2356 -2611 2031 C ATOM 1861 CG TRP A1136 -2.389 7.322 -6.151 1.00129.97 C ANISOU 1861 CG TRP A1136 16580 17815 14988 -1815 -2789 1985 C ATOM 1862 CD1 TRP A1136 -2.005 6.055 -6.479 1.00126.96 C ANISOU 1862 CD1 TRP A1136 15859 17618 14763 -1712 -3077 2043 C ATOM 1863 CD2 TRP A1136 -3.439 7.671 -7.065 1.00127.02 C ANISOU 1863 CD2 TRP A1136 16370 17327 14565 -1303 -2692 1871 C ATOM 1864 NE1 TRP A1136 -2.744 5.595 -7.542 1.00116.61 N ANISOU 1864 NE1 TRP A1136 14491 16315 13502 -1172 -3163 1971 N ATOM 1865 CE2 TRP A1136 -3.632 6.568 -7.920 1.00120.63 C ANISOU 1865 CE2 TRP A1136 15304 16645 13887 -912 -2932 1865 C ATOM 1866 CE3 TRP A1136 -4.231 8.810 -7.244 1.00128.26 C ANISOU 1866 CE3 TRP A1136 16865 17288 14580 -1139 -2423 1774 C ATOM 1867 CZ2 TRP A1136 -4.583 6.569 -8.938 1.00117.45 C ANISOU 1867 CZ2 TRP A1136 14970 16181 13474 -369 -2913 1765 C ATOM 1868 CZ3 TRP A1136 -5.176 8.809 -8.256 1.00121.76 C ANISOU 1868 CZ3 TRP A1136 16110 16405 13749 -595 -2407 1677 C ATOM 1869 CH2 TRP A1136 -5.343 7.696 -9.089 1.00120.59 C ANISOU 1869 CH2 TRP A1136 15699 16389 13730 -218 -2651 1674 C ATOM 1870 N TYR A1137 -0.233 10.097 -7.113 1.00131.09 N ANISOU 1870 N TYR A1137 17348 17659 14800 -2042 -2069 2204 N ATOM 1871 CA TYR A1137 0.105 10.499 -8.471 1.00129.93 C ANISOU 1871 CA TYR A1137 17320 17443 14604 -1652 -1929 2248 C ATOM 1872 C TYR A1137 1.614 10.494 -8.686 1.00133.71 C ANISOU 1872 C TYR A1137 17724 17990 15090 -1878 -1905 2412 C ATOM 1873 O TYR A1137 2.097 10.056 -9.728 1.00130.29 O ANISOU 1873 O TYR A1137 17176 17617 14713 -1587 -1975 2476 O ATOM 1874 CB TYR A1137 -0.462 11.884 -8.784 1.00126.43 C ANISOU 1874 CB TYR A1137 17275 16774 13988 -1497 -1590 2175 C ATOM 1875 CG TYR A1137 -0.340 12.270 -10.240 1.00127.22 C ANISOU 1875 CG TYR A1137 17505 16795 14039 -1029 -1454 2197 C ATOM 1876 CD1 TYR A1137 -1.334 11.934 -11.149 1.00123.71 C ANISOU 1876 CD1 TYR A1137 17044 16334 13627 -494 -1524 2101 C ATOM 1877 CD2 TYR A1137 0.768 12.965 -10.707 1.00130.55 C ANISOU 1877 CD2 TYR A1137 18065 17161 14378 -1121 -1256 2312 C ATOM 1878 CE1 TYR A1137 -1.230 12.279 -12.481 1.00122.90 C ANISOU 1878 CE1 TYR A1137 17058 16161 13478 -65 -1403 2122 C ATOM 1879 CE2 TYR A1137 0.881 13.315 -12.040 1.00132.57 C ANISOU 1879 CE2 TYR A1137 18440 17344 14588 -694 -1132 2332 C ATOM 1880 CZ TYR A1137 -0.121 12.970 -12.922 1.00128.85 C ANISOU 1880 CZ TYR A1137 17950 16857 14151 -167 -1207 2237 C ATOM 1881 OH TYR A1137 -0.015 13.317 -14.249 1.00120.55 O ANISOU 1881 OH TYR A1137 17018 15735 13052 259 -1084 2257 O ATOM 1882 N ASN A1138 2.356 10.979 -7.694 1.00136.28 N ANISOU 1882 N ASN A1138 18113 18309 15360 -2399 -1806 2480 N ATOM 1883 CA ASN A1138 3.811 11.017 -7.786 1.00136.58 C ANISOU 1883 CA ASN A1138 18085 18412 15399 -2659 -1776 2636 C ATOM 1884 C ASN A1138 4.439 9.629 -7.839 1.00135.16 C ANISOU 1884 C ASN A1138 17509 18453 15394 -2693 -2105 2721 C ATOM 1885 O ASN A1138 5.470 9.435 -8.485 1.00134.78 O ANISOU 1885 O ASN A1138 17369 18465 15375 -2662 -2120 2838 O ATOM 1886 CB ASN A1138 4.398 11.803 -6.610 1.00135.72 C ANISOU 1886 CB ASN A1138 18119 18255 15192 -3232 -1610 2680 C ATOM 1887 CG ASN A1138 4.722 13.239 -6.974 1.00140.66 C ANISOU 1887 CG ASN A1138 19114 18690 15640 -3245 -1240 2697 C ATOM 1888 OD1 ASN A1138 4.279 13.745 -8.005 1.00145.84 O ANISOU 1888 OD1 ASN A1138 19954 19226 16233 -2819 -1092 2651 O ATOM 1889 ND2 ASN A1138 5.501 13.904 -6.127 1.00133.78 N ANISOU 1889 ND2 ASN A1138 18353 17791 14687 -3737 -1089 2764 N ATOM 1890 N GLN A1139 3.821 8.662 -7.167 1.00133.83 N ANISOU 1890 N GLN A1139 17105 18401 15343 -2755 -2366 2663 N ATOM 1891 CA GLN A1139 4.380 7.314 -7.154 1.00129.91 C ANISOU 1891 CA GLN A1139 16227 18116 15018 -2798 -2685 2742 C ATOM 1892 C GLN A1139 4.063 6.526 -8.429 1.00128.05 C ANISOU 1892 C GLN A1139 15835 17939 14880 -2250 -2838 2724 C ATOM 1893 O GLN A1139 4.932 5.839 -8.963 1.00123.25 O ANISOU 1893 O GLN A1139 15013 17452 14364 -2200 -2975 2830 O ATOM 1894 CB GLN A1139 3.893 6.556 -5.919 1.00130.25 C ANISOU 1894 CB GLN A1139 16070 18268 15150 -3094 -2910 2693 C ATOM 1895 CG GLN A1139 4.437 7.139 -4.624 1.00139.65 C ANISOU 1895 CG GLN A1139 17351 19442 16268 -3686 -2804 2738 C ATOM 1896 CD GLN A1139 3.838 6.504 -3.390 1.00143.99 C ANISOU 1896 CD GLN A1139 17742 20078 16891 -3967 -3001 2675 C ATOM 1897 OE1 GLN A1139 3.766 7.129 -2.331 1.00144.34 O ANISOU 1897 OE1 GLN A1139 17926 20061 16854 -4361 -2884 2653 O ATOM 1898 NE2 GLN A1139 3.406 5.255 -3.516 1.00142.05 N ANISOU 1898 NE2 GLN A1139 17201 19972 16798 -3770 -3300 2645 N ATOM 1899 N THR A1140 2.833 6.637 -8.925 1.00140.33 N ANISOU 1899 N THR A1140 19634 16136 17550 -2268 -3195 1272 N ATOM 1900 CA THR A1140 2.443 5.948 -10.157 1.00131.42 C ANISOU 1900 CA THR A1140 18177 15307 16449 -2246 -2734 1491 C ATOM 1901 C THR A1140 1.701 6.876 -11.117 1.00129.29 C ANISOU 1901 C THR A1140 17947 14922 16257 -2162 -2587 1520 C ATOM 1902 O THR A1140 0.490 6.744 -11.295 1.00119.73 O ANISOU 1902 O THR A1140 16849 13890 14753 -1910 -2288 1390 O ATOM 1903 CB THR A1140 1.538 4.731 -9.865 1.00123.91 C ANISOU 1903 CB THR A1140 17231 14768 15083 -2010 -2366 1371 C ATOM 1904 OG1 THR A1140 0.412 5.146 -9.080 1.00128.43 O ANISOU 1904 OG1 THR A1140 18209 15303 15285 -1729 -2388 1035 O ATOM 1905 CG2 THR A1140 2.304 3.656 -9.111 1.00121.76 C ANISOU 1905 CG2 THR A1140 16846 14659 14758 -2108 -2445 1394 C ATOM 1906 N PRO A1141 2.426 7.826 -11.730 1.00131.28 N ANISOU 1906 N PRO A1141 18107 14871 16901 -2374 -2800 1689 N ATOM 1907 CA PRO A1141 1.790 8.801 -12.628 1.00130.68 C ANISOU 1907 CA PRO A1141 18077 14651 16923 -2309 -2695 1722 C ATOM 1908 C PRO A1141 1.058 8.208 -13.837 1.00119.31 C ANISOU 1908 C PRO A1141 16374 13526 15431 -2218 -2194 1886 C ATOM 1909 O PRO A1141 -0.014 8.698 -14.187 1.00115.24 O ANISOU 1909 O PRO A1141 16011 13018 14758 -2016 -2015 1780 O ATOM 1910 CB PRO A1141 2.975 9.648 -13.105 1.00129.30 C ANISOU 1910 CB PRO A1141 17763 14144 17222 -2610 -3002 1932 C ATOM 1911 CG PRO A1141 4.151 8.740 -12.995 1.00129.18 C ANISOU 1911 CG PRO A1141 17459 14242 17383 -2843 -3070 2121 C ATOM 1912 CD PRO A1141 3.895 7.917 -11.767 1.00130.25 C ANISOU 1912 CD PRO A1141 17773 14559 17157 -2695 -3097 1896 C ATOM 1913 N ASN A1142 1.608 7.153 -14.437 1.00114.06 N ANISOU 1913 N ASN A1142 15327 13124 14884 -2361 -1966 2133 N ATOM 1914 CA ASN A1142 1.058 6.622 -15.681 1.00109.72 C ANISOU 1914 CA ASN A1142 14490 12858 14340 -2319 -1502 2325 C ATOM 1915 C ASN A1142 -0.298 5.950 -15.506 1.00104.85 C ANISOU 1915 C ASN A1142 13998 12569 13270 -2004 -1132 2137 C ATOM 1916 O ASN A1142 -1.138 5.980 -16.405 1.00 99.29 O ANISOU 1916 O ASN A1142 13214 12011 12502 -1884 -794 2193 O ATOM 1917 CB ASN A1142 2.049 5.643 -16.317 1.00109.61 C ANISOU 1917 CB ASN A1142 14035 13037 14575 -2564 -1365 2636 C ATOM 1918 CG ASN A1142 3.222 6.348 -16.973 1.00112.33 C ANISOU 1918 CG ASN A1142 14179 13094 15409 -2875 -1612 2886 C ATOM 1919 OD1 ASN A1142 3.457 7.534 -16.736 1.00116.22 O ANISOU 1919 OD1 ASN A1142 14883 13222 16053 -2925 -1950 2809 O ATOM 1920 ND2 ASN A1142 3.962 5.623 -17.802 1.00109.35 N ANISOU 1920 ND2 ASN A1142 13392 12879 15279 -3086 -1440 3184 N ATOM 1921 N ARG A1143 -0.501 5.348 -14.340 1.00107.38 N ANISOU 1921 N ARG A1143 14517 13005 13278 -1872 -1199 1913 N ATOM 1922 CA ARG A1143 -1.763 4.704 -14.010 1.00101.15 C ANISOU 1922 CA ARG A1143 13882 12515 12036 -1568 -883 1702 C ATOM 1923 C ARG A1143 -2.758 5.746 -13.520 1.00100.77 C ANISOU 1923 C ARG A1143 14252 12263 11772 -1336 -1004 1412 C ATOM 1924 O ARG A1143 -3.947 5.733 -13.876 1.00 98.53 O ANISOU 1924 O ARG A1143 14055 12142 11240 -1102 -698 1313 O ATOM 1925 CB ARG A1143 -1.532 3.627 -12.950 1.00 97.10 C ANISOU 1925 CB ARG A1143 13407 12202 11283 -1531 -915 1583 C ATOM 1926 CG ARG A1143 -2.766 2.864 -12.528 1.00 94.42 C ANISOU 1926 CG ARG A1143 13223 12185 10466 -1226 -597 1360 C ATOM 1927 CD ARG A1143 -2.372 1.693 -11.647 1.00 92.20 C ANISOU 1927 CD ARG A1143 12904 12122 10006 -1234 -603 1305 C ATOM 1928 NE ARG A1143 -3.528 0.924 -11.203 1.00 89.07 N ANISOU 1928 NE ARG A1143 12658 12038 9146 -945 -302 1086 N ATOM 1929 CZ ARG A1143 -3.449 -0.218 -10.530 1.00 81.86 C ANISOU 1929 CZ ARG A1143 11711 11383 8008 -899 -210 1023 C ATOM 1930 NH1 ARG A1143 -2.264 -0.730 -10.225 1.00 81.75 N ANISOU 1930 NH1 ARG A1143 11513 11354 8193 -1123 -395 1167 N ATOM 1931 NH2 ARG A1143 -4.555 -0.851 -10.165 1.00 74.98 N ANISOU 1931 NH2 ARG A1143 10990 10788 6713 -629 71 817 N ATOM 1932 N ALA A1144 -2.241 6.667 -12.714 1.00110.67 N ANISOU 1932 N ALA A1144 15760 13154 13135 -1409 -1457 1282 N ATOM 1933 CA ALA A1144 -3.048 7.721 -12.128 1.00114.39 C ANISOU 1933 CA ALA A1144 16645 13389 13428 -1214 -1632 1000 C ATOM 1934 C ALA A1144 -3.634 8.635 -13.194 1.00108.12 C ANISOU 1934 C ALA A1144 15836 12477 12767 -1167 -1493 1082 C ATOM 1935 O ALA A1144 -4.718 9.167 -13.015 1.00104.21 O ANISOU 1935 O ALA A1144 15618 11946 12031 -929 -1426 867 O ATOM 1936 CB ALA A1144 -2.224 8.526 -11.134 1.00122.78 C ANISOU 1936 CB ALA A1144 17942 14076 14632 -1344 -2153 882 C ATOM 1937 N LYS A1145 -2.927 8.814 -14.306 1.00107.96 N ANISOU 1937 N LYS A1145 15492 12400 13129 -1393 -1448 1391 N ATOM 1938 CA LYS A1145 -3.463 9.636 -15.386 1.00103.91 C ANISOU 1938 CA LYS A1145 14939 11791 12752 -1358 -1298 1489 C ATOM 1939 C LYS A1145 -4.684 8.977 -16.007 1.00 97.21 C ANISOU 1939 C LYS A1145 14015 11306 11614 -1124 -802 1473 C ATOM 1940 O LYS A1145 -5.688 9.636 -16.270 1.00 94.68 O ANISOU 1940 O LYS A1145 13879 10937 11159 -931 -690 1354 O ATOM 1941 CB LYS A1145 -2.408 9.889 -16.464 1.00104.16 C ANISOU 1941 CB LYS A1145 14618 11701 13256 -1661 -1342 1835 C ATOM 1942 CG LYS A1145 -1.266 10.789 -16.035 1.00110.11 C ANISOU 1942 CG LYS A1145 15454 12049 14334 -1893 -1831 1862 C ATOM 1943 CD LYS A1145 -0.156 10.771 -17.074 1.00117.08 C ANISOU 1943 CD LYS A1145 15944 12875 15666 -2204 -1840 2217 C ATOM 1944 CE LYS A1145 1.136 11.346 -16.520 1.00124.50 C ANISOU 1944 CE LYS A1145 16921 13476 16906 -2457 -2316 2254 C ATOM 1945 NZ LYS A1145 2.249 11.264 -17.507 1.00123.73 N ANISOU 1945 NZ LYS A1145 16435 13335 17242 -2765 -2323 2598 N ATOM 1946 N ARG A1146 -4.595 7.669 -16.229 1.00 90.52 N ANISOU 1946 N ARG A1146 12898 10825 10670 -1143 -505 1592 N ATOM 1947 CA ARG A1146 -5.693 6.933 -16.842 1.00 85.05 C ANISOU 1947 CA ARG A1146 12103 10506 9706 -938 -15 1593 C ATOM 1948 C ARG A1146 -6.907 6.884 -15.923 1.00 84.95 C ANISOU 1948 C ARG A1146 12464 10586 9225 -611 50 1241 C ATOM 1949 O ARG A1146 -8.045 7.042 -16.377 1.00 79.13 O ANISOU 1949 O ARG A1146 11808 9973 8287 -397 330 1162 O ATOM 1950 CB ARG A1146 -5.247 5.516 -17.213 1.00 82.38 C ANISOU 1950 CB ARG A1146 11393 10532 9374 -1044 270 1796 C ATOM 1951 CG ARG A1146 -4.121 5.476 -18.237 1.00 80.48 C ANISOU 1951 CG ARG A1146 10753 10238 9587 -1361 263 2158 C ATOM 1952 CD ARG A1146 -3.854 4.061 -18.732 1.00 78.05 C ANISOU 1952 CD ARG A1146 10069 10322 9264 -1440 612 2360 C ATOM 1953 NE ARG A1146 -3.199 3.230 -17.725 1.00 80.32 N ANISOU 1953 NE ARG A1146 10365 10692 9462 -1499 459 2295 N ATOM 1954 CZ ARG A1146 -1.887 3.018 -17.669 1.00 85.34 C ANISOU 1954 CZ ARG A1146 10793 11225 10406 -1777 235 2481 C ATOM 1955 NH1 ARG A1146 -1.083 3.576 -18.563 1.00 85.61 N ANISOU 1955 NH1 ARG A1146 10597 11069 10861 -2023 137 2740 N ATOM 1956 NH2 ARG A1146 -1.378 2.245 -16.719 1.00 83.37 N ANISOU 1956 NH2 ARG A1146 10567 11066 10045 -1808 110 2407 N ATOM 1957 N VAL A1147 -6.664 6.697 -14.629 1.00 90.53 N ANISOU 1957 N VAL A1147 13406 11228 9764 -576 -217 1026 N ATOM 1958 CA VAL A1147 -7.767 6.658 -13.671 1.00 89.75 C ANISOU 1958 CA VAL A1147 13677 11202 9222 -276 -184 678 C ATOM 1959 C VAL A1147 -8.406 8.038 -13.488 1.00 91.17 C ANISOU 1959 C VAL A1147 14204 11060 9378 -144 -382 487 C ATOM 1960 O VAL A1147 -9.636 8.171 -13.455 1.00 88.13 O ANISOU 1960 O VAL A1147 14020 10777 8688 123 -176 296 O ATOM 1961 CB VAL A1147 -7.301 6.120 -12.303 1.00 94.69 C ANISOU 1961 CB VAL A1147 14467 11828 9682 -283 -437 498 C ATOM 1962 CG1 VAL A1147 -8.454 6.105 -11.314 1.00 97.17 C ANISOU 1962 CG1 VAL A1147 15172 12210 9539 26 -406 132 C ATOM 1963 CG2 VAL A1147 -6.714 4.727 -12.458 1.00 88.87 C ANISOU 1963 CG2 VAL A1147 13395 11419 8952 -400 -229 680 C ATOM 1964 N ILE A1148 -7.564 9.065 -13.395 1.00 97.79 N ANISOU 1964 N ILE A1148 15105 11510 10543 -334 -776 542 N ATOM 1965 CA ILE A1148 -8.033 10.434 -13.212 1.00 98.34 C ANISOU 1965 CA ILE A1148 15495 11239 10632 -239 -999 376 C ATOM 1966 C ILE A1148 -8.841 10.889 -14.415 1.00 96.10 C ANISOU 1966 C ILE A1148 15119 11004 10390 -142 -697 482 C ATOM 1967 O ILE A1148 -9.893 11.499 -14.262 1.00 96.34 O ANISOU 1967 O ILE A1148 15426 10974 10205 89 -647 275 O ATOM 1968 CB ILE A1148 -6.860 11.416 -12.989 1.00102.65 C ANISOU 1968 CB ILE A1148 16080 11364 11559 -494 -1468 452 C ATOM 1969 CG1 ILE A1148 -6.354 11.335 -11.548 1.00111.79 C ANISOU 1969 CG1 ILE A1148 17482 12391 12602 -519 -1833 239 C ATOM 1970 CG2 ILE A1148 -7.273 12.845 -13.301 1.00110.93 C ANISOU 1970 CG2 ILE A1148 17339 12081 12727 -442 -1612 390 C ATOM 1971 CD1 ILE A1148 -5.124 12.179 -11.293 1.00122.30 C ANISOU 1971 CD1 ILE A1148 18830 13336 14304 -784 -2289 322 C ATOM 1972 N THR A1149 -8.351 10.579 -15.612 1.00 90.72 N ANISOU 1972 N THR A1149 14047 10437 9987 -319 -494 806 N ATOM 1973 CA THR A1149 -9.091 10.892 -16.827 1.00 91.04 C ANISOU 1973 CA THR A1149 13959 10562 10070 -239 -175 933 C ATOM 1974 C THR A1149 -10.362 10.060 -16.925 1.00 84.95 C ANISOU 1974 C THR A1149 13211 10181 8886 40 263 810 C ATOM 1975 O THR A1149 -11.339 10.489 -17.535 1.00 82.72 O ANISOU 1975 O THR A1149 12989 9938 8502 210 485 778 O ATOM 1976 CB THR A1149 -8.241 10.671 -18.091 1.00 89.12 C ANISOU 1976 CB THR A1149 13273 10369 10218 -505 -46 1316 C ATOM 1977 OG1 THR A1149 -7.637 9.374 -18.046 1.00 90.23 O ANISOU 1977 OG1 THR A1149 13137 10798 10349 -622 95 1449 O ATOM 1978 CG2 THR A1149 -7.156 11.734 -18.194 1.00 96.19 C ANISOU 1978 CG2 THR A1149 14164 10847 11537 -760 -455 1439 C ATOM 1979 N THR A1150 -10.344 8.862 -16.346 1.00 79.69 N ANISOU 1979 N THR A1150 12489 9805 7983 86 393 747 N ATOM 1980 CA THR A1150 -11.563 8.062 -16.293 1.00 75.64 C ANISOU 1980 CA THR A1150 12034 9657 7047 362 787 596 C ATOM 1981 C THR A1150 -12.607 8.741 -15.406 1.00 80.69 C ANISOU 1981 C THR A1150 13130 10165 7362 639 673 237 C ATOM 1982 O THR A1150 -13.804 8.683 -15.691 1.00 77.02 O ANISOU 1982 O THR A1150 12757 9881 6626 882 975 124 O ATOM 1983 CB THR A1150 -11.292 6.637 -15.780 1.00 72.21 C ANISOU 1983 CB THR A1150 11462 9552 6424 352 931 592 C ATOM 1984 OG1 THR A1150 -10.258 6.032 -16.567 1.00 81.01 O ANISOU 1984 OG1 THR A1150 12154 10768 7856 81 1014 926 O ATOM 1985 CG2 THR A1150 -12.548 5.788 -15.879 1.00 55.18 C ANISOU 1985 CG2 THR A1150 9327 7791 3849 626 1376 464 C ATOM 1986 N PHE A1151 -12.152 9.404 -14.345 1.00 87.08 N ANISOU 1986 N PHE A1151 14224 10657 8205 599 236 59 N ATOM 1987 CA PHE A1151 -13.060 10.169 -13.491 1.00 97.16 C ANISOU 1987 CA PHE A1151 15943 11761 9212 839 87 -279 C ATOM 1988 C PHE A1151 -13.540 11.449 -14.173 1.00 94.14 C ANISOU 1988 C PHE A1151 15666 11125 8978 889 54 -262 C ATOM 1989 O PHE A1151 -14.708 11.827 -14.072 1.00 94.45 O ANISOU 1989 O PHE A1151 15948 11187 8752 1145 184 -467 O ATOM 1990 CB PHE A1151 -12.385 10.529 -12.163 1.00101.49 C ANISOU 1990 CB PHE A1151 16758 12033 9768 765 -379 -467 C ATOM 1991 CG PHE A1151 -12.389 9.417 -11.152 1.00 96.63 C ANISOU 1991 CG PHE A1151 16207 11657 8851 838 -353 -626 C ATOM 1992 CD1 PHE A1151 -13.573 9.007 -10.560 1.00 91.19 C ANISOU 1992 CD1 PHE A1151 15760 11175 7714 1133 -156 -905 C ATOM 1993 CD2 PHE A1151 -11.208 8.800 -10.775 1.00 91.98 C ANISOU 1993 CD2 PHE A1151 15444 11079 8426 613 -531 -502 C ATOM 1994 CE1 PHE A1151 -13.581 7.990 -9.622 1.00 89.99 C ANISOU 1994 CE1 PHE A1151 15672 11240 7282 1201 -133 -1055 C ATOM 1995 CE2 PHE A1151 -11.209 7.783 -9.837 1.00 93.36 C ANISOU 1995 CE2 PHE A1151 15679 11470 8322 681 -510 -648 C ATOM 1996 CZ PHE A1151 -12.397 7.378 -9.260 1.00 88.14 C ANISOU 1996 CZ PHE A1151 15260 11015 7215 975 -310 -925 C ATOM 1997 N ARG A1152 -12.616 12.102 -14.868 1.00 93.19 N ANISOU 1997 N ARG A1152 15357 10765 9285 639 -121 -15 N ATOM 1998 CA ARG A1152 -12.827 13.422 -15.446 1.00 99.43 C ANISOU 1998 CA ARG A1152 16248 11251 10281 637 -233 19 C ATOM 1999 C ARG A1152 -13.726 13.385 -16.674 1.00 98.20 C ANISOU 1999 C ARG A1152 15926 11303 10085 760 189 146 C ATOM 2000 O ARG A1152 -14.574 14.256 -16.864 1.00 99.87 O ANISOU 2000 O ARG A1152 16343 11381 10222 927 214 31 O ATOM 2001 CB ARG A1152 -11.471 14.041 -15.805 1.00106.25 C ANISOU 2001 CB ARG A1152 16940 11808 11623 313 -549 257 C ATOM 2002 CG ARG A1152 -11.528 15.449 -16.372 1.00113.95 C ANISOU 2002 CG ARG A1152 18011 12433 12850 277 -708 305 C ATOM 2003 CD ARG A1152 -10.125 15.974 -16.658 1.00115.32 C ANISOU 2003 CD ARG A1152 18012 12317 13488 -53 -1028 534 C ATOM 2004 NE ARG A1152 -9.424 15.164 -17.653 1.00120.64 N ANISOU 2004 NE ARG A1152 18236 13208 14394 -260 -810 868 N ATOM 2005 CZ ARG A1152 -9.440 15.408 -18.960 1.00121.29 C ANISOU 2005 CZ ARG A1152 18059 13317 14708 -342 -603 1120 C ATOM 2006 NH1 ARG A1152 -10.123 16.441 -19.434 1.00122.28 N ANISOU 2006 NH1 ARG A1152 18331 13265 14865 -230 -585 1080 N ATOM 2007 NH2 ARG A1152 -8.774 14.620 -19.793 1.00110.70 N ANISOU 2007 NH2 ARG A1152 16313 12179 13571 -536 -413 1413 N ATOM 2008 N THR A1153 -13.531 12.367 -17.504 1.00112.64 N ANISOU 2008 N THR A1153 21551 10746 10499 -848 -1230 932 N ATOM 2009 CA THR A1153 -14.260 12.247 -18.759 1.00107.18 C ANISOU 2009 CA THR A1153 20658 10362 9703 -432 -1169 773 C ATOM 2010 C THR A1153 -15.478 11.334 -18.648 1.00104.24 C ANISOU 2010 C THR A1153 19977 10397 9232 -303 -999 267 C ATOM 2011 O THR A1153 -16.461 11.509 -19.368 1.00106.91 O ANISOU 2011 O THR A1153 20214 10966 9441 94 -980 -7 O ATOM 2012 CB THR A1153 -13.343 11.721 -19.877 1.00103.78 C ANISOU 2012 CB THR A1153 20072 9997 9365 -473 -1108 1161 C ATOM 2013 OG1 THR A1153 -12.857 10.420 -19.525 1.00 99.10 O ANISOU 2013 OG1 THR A1153 19234 9542 8879 -832 -942 1214 O ATOM 2014 CG2 THR A1153 -12.162 12.661 -20.077 1.00110.16 C ANISOU 2014 CG2 THR A1153 20968 10509 10379 -561 -1247 1554 C ATOM 2015 N GLY A1154 -15.412 10.358 -17.748 1.00103.34 N ANISOU 2015 N GLY A1154 19713 10372 9181 -640 -874 145 N ATOM 2016 CA GLY A1154 -16.493 9.400 -17.606 1.00101.82 C ANISOU 2016 CA GLY A1154 19214 10567 8907 -553 -703 -317 C ATOM 2017 C GLY A1154 -16.486 8.395 -18.741 1.00100.90 C ANISOU 2017 C GLY A1154 18751 10788 8799 -449 -543 -285 C ATOM 2018 O GLY A1154 -17.482 7.715 -18.995 1.00101.11 O ANISOU 2018 O GLY A1154 18510 11173 8735 -261 -410 -662 O ATOM 2019 N THR A1155 -15.357 8.316 -19.437 1.00 96.22 N ANISOU 2019 N THR A1155 18166 10078 8316 -568 -558 171 N ATOM 2020 CA THR A1155 -15.224 7.448 -20.598 1.00 89.46 C ANISOU 2020 CA THR A1155 17006 9510 7476 -468 -421 258 C ATOM 2021 C THR A1155 -14.066 6.466 -20.448 1.00 89.47 C ANISOU 2021 C THR A1155 16872 9479 7642 -893 -319 589 C ATOM 2022 O THR A1155 -13.245 6.584 -19.536 1.00 89.52 O ANISOU 2022 O THR A1155 17053 9202 7758 -1257 -377 810 O ATOM 2023 CB THR A1155 -15.013 8.266 -21.888 1.00 90.68 C ANISOU 2023 CB THR A1155 17260 9601 7593 -134 -525 502 C ATOM 2024 OG1 THR A1155 -13.774 8.982 -21.806 1.00 90.54 O ANISOU 2024 OG1 THR A1155 17522 9192 7689 -334 -670 985 O ATOM 2025 CG2 THR A1155 -16.154 9.254 -22.089 1.00 95.79 C ANISOU 2025 CG2 THR A1155 18039 10281 8077 298 -627 183 C ATOM 2026 N TRP A1156 -14.012 5.496 -21.355 1.00 82.51 N ANISOU 2026 N TRP A1156 15678 8893 6779 -843 -168 619 N ATOM 2027 CA TRP A1156 -12.925 4.526 -21.391 1.00 75.51 C ANISOU 2027 CA TRP A1156 14637 8006 6046 -1211 -62 941 C ATOM 2028 C TRP A1156 -11.780 5.020 -22.268 1.00 75.25 C ANISOU 2028 C TRP A1156 14738 7754 6100 -1217 -155 1459 C ATOM 2029 O TRP A1156 -10.901 4.246 -22.633 1.00 76.70 O ANISOU 2029 O TRP A1156 14546 8037 6560 -1383 -68 1637 O ATOM 2030 CB TRP A1156 -13.426 3.173 -21.900 1.00 67.09 C ANISOU 2030 CB TRP A1156 13156 7374 4961 -1171 156 712 C ATOM 2031 CG TRP A1156 -14.370 2.490 -20.971 1.00 64.51 C ANISOU 2031 CG TRP A1156 12670 7264 4579 -1246 267 250 C ATOM 2032 CD1 TRP A1156 -15.728 2.427 -21.081 1.00 70.97 C ANISOU 2032 CD1 TRP A1156 13356 8364 5246 -923 319 -226 C ATOM 2033 CD2 TRP A1156 -14.029 1.765 -19.784 1.00 68.23 C ANISOU 2033 CD2 TRP A1156 13091 7687 5144 -1673 341 219 C ATOM 2034 NE1 TRP A1156 -16.255 1.707 -20.035 1.00 73.44 N ANISOU 2034 NE1 TRP A1156 13541 8809 5553 -1122 420 -552 N ATOM 2035 CE2 TRP A1156 -15.232 1.290 -19.224 1.00 70.23 C ANISOU 2035 CE2 TRP A1156 13183 8205 5297 -1582 435 -289 C ATOM 2036 CE3 TRP A1156 -12.823 1.472 -19.139 1.00 66.99 C ANISOU 2036 CE3 TRP A1156 13014 7290 5151 -2124 335 573 C ATOM 2037 CZ2 TRP A1156 -15.264 0.538 -18.051 1.00 69.30 C ANISOU 2037 CZ2 TRP A1156 12978 8119 5234 -1925 523 -452 C ATOM 2038 CZ3 TRP A1156 -12.857 0.725 -17.975 1.00 57.90 C ANISOU 2038 CZ3 TRP A1156 11776 6170 4054 -2465 423 409 C ATOM 2039 CH2 TRP A1156 -14.069 0.269 -17.442 1.00 62.40 C ANISOU 2039 CH2 TRP A1156 12184 7007 4520 -2364 516 -99 C ATOM 2040 N ASP A1157 -11.791 6.310 -22.592 1.00 71.70 N ANISOU 2040 N ASP A1157 14573 7075 5594 -973 -335 1573 N ATOM 2041 CA ASP A1157 -10.861 6.876 -23.568 1.00 77.48 C ANISOU 2041 CA ASP A1157 15118 7735 6588 -854 -412 1872 C ATOM 2042 C ASP A1157 -9.391 6.725 -23.186 1.00 75.44 C ANISOU 2042 C ASP A1157 14461 7423 6781 -1150 -410 2068 C ATOM 2043 O ASP A1157 -8.526 6.656 -24.058 1.00 73.91 O ANISOU 2043 O ASP A1157 13940 7326 6815 -1089 -382 2277 O ATOM 2044 CB ASP A1157 -11.170 8.356 -23.787 1.00 82.65 C ANISOU 2044 CB ASP A1157 16112 8162 7130 -561 -605 1898 C ATOM 2045 CG ASP A1157 -12.341 8.574 -24.719 1.00 76.14 C ANISOU 2045 CG ASP A1157 15451 7517 5963 -95 -613 1718 C ATOM 2046 OD1 ASP A1157 -13.240 7.708 -24.763 1.00 72.70 O ANISOU 2046 OD1 ASP A1157 14731 7434 5457 0 -458 1341 O ATOM 2047 OD2 ASP A1157 -12.361 9.609 -25.413 1.00 74.77 O ANISOU 2047 OD2 ASP A1157 15446 7217 5745 193 -750 1836 O ATOM 2048 N ALA A1158 -9.107 6.678 -21.889 1.00 77.12 N ANISOU 2048 N ALA A1158 14682 7521 7101 -1423 -433 1978 N ATOM 2049 CA ALA A1158 -7.741 6.478 -21.424 1.00 78.04 C ANISOU 2049 CA ALA A1158 14397 7663 7591 -1617 -419 2099 C ATOM 2050 C ALA A1158 -7.257 5.081 -21.794 1.00 84.93 C ANISOU 2050 C ALA A1158 14835 8800 8632 -1703 -254 2125 C ATOM 2051 O ALA A1158 -6.053 4.827 -21.882 1.00 82.62 O ANISOU 2051 O ALA A1158 14165 8583 8642 -1719 -210 2257 O ATOM 2052 CB ALA A1158 -7.650 6.693 -19.926 1.00 76.68 C ANISOU 2052 CB ALA A1158 14331 7354 7450 -1842 -482 1960 C ATOM 2053 N TYR A1159 -8.207 4.176 -22.003 1.00 79.76 N ANISOU 2053 N TYR A1159 14244 8297 7765 -1725 -144 1978 N ATOM 2054 CA TYR A1159 -7.894 2.784 -22.290 1.00 78.31 C ANISOU 2054 CA TYR A1159 13659 8373 7722 -1810 14 1962 C ATOM 2055 C TYR A1159 -8.283 2.397 -23.717 1.00 80.31 C ANISOU 2055 C TYR A1159 13838 8821 7854 -1597 105 2043 C ATOM 2056 O TYR A1159 -9.294 2.864 -24.241 1.00 77.34 O ANISOU 2056 O TYR A1159 13787 8451 7148 -1402 89 1981 O ATOM 2057 CB TYR A1159 -8.598 1.872 -21.281 1.00 77.50 C ANISOU 2057 CB TYR A1159 13590 8357 7500 -2046 104 1695 C ATOM 2058 CG TYR A1159 -8.152 2.096 -19.851 1.00 73.94 C ANISOU 2058 CG TYR A1159 13150 7762 7183 -2250 19 1606 C ATOM 2059 CD1 TYR A1159 -8.733 3.087 -19.069 1.00 73.89 C ANISOU 2059 CD1 TYR A1159 13565 7522 6988 -2296 -92 1513 C ATOM 2060 CD2 TYR A1159 -7.152 1.317 -19.285 1.00 66.15 C ANISOU 2060 CD2 TYR A1159 11760 6886 6489 -2344 47 1607 C ATOM 2061 CE1 TYR A1159 -8.330 3.298 -17.765 1.00 74.67 C ANISOU 2061 CE1 TYR A1159 13657 7521 7193 -2468 -168 1431 C ATOM 2062 CE2 TYR A1159 -6.742 1.519 -17.982 1.00 72.06 C ANISOU 2062 CE2 TYR A1159 12505 7550 7324 -2474 -27 1524 C ATOM 2063 CZ TYR A1159 -7.332 2.512 -17.226 1.00 79.05 C ANISOU 2063 CZ TYR A1159 13787 8226 8023 -2552 -133 1441 C ATOM 2064 OH TYR A1159 -6.927 2.714 -15.926 1.00 81.31 O ANISOU 2064 OH TYR A1159 14055 8456 8382 -2668 -202 1364 O ATOM 2065 N PRO A 259 -7.469 1.547 -24.356 1.00 88.70 N ANISOU 2065 N PRO A 259 11666 9898 12138 888 155 991 N ATOM 2066 CA PRO A 259 -6.218 1.038 -23.796 1.00 90.45 C ANISOU 2066 CA PRO A 259 11845 10178 12345 1023 161 1124 C ATOM 2067 C PRO A 259 -5.014 1.895 -24.164 1.00 97.32 C ANISOU 2067 C PRO A 259 12626 11214 13138 1026 6 1247 C ATOM 2068 O PRO A 259 -4.746 2.067 -25.349 1.00103.32 O ANISOU 2068 O PRO A 259 13259 12047 13950 1023 37 1279 O ATOM 2069 CB PRO A 259 -6.108 -0.362 -24.416 1.00 92.44 C ANISOU 2069 CB PRO A 259 12040 10382 12700 1137 383 1089 C ATOM 2070 CG PRO A 259 -6.950 -0.305 -25.681 1.00 84.36 C ANISOU 2070 CG PRO A 259 10985 9323 11746 1055 458 967 C ATOM 2071 CD PRO A 259 -7.733 0.984 -25.688 1.00 91.52 C ANISOU 2071 CD PRO A 259 11954 10238 12581 890 275 901 C ATOM 2072 N GLU A 260 -4.327 2.431 -23.154 1.00104.44 N ANISOU 2072 N GLU A 260 13560 12187 13936 1031 -127 1334 N ATOM 2073 CA GLU A 260 -3.040 3.115 -23.327 1.00115.90 C ANISOU 2073 CA GLU A 260 14914 13827 15295 1041 -259 1442 C ATOM 2074 C GLU A 260 -3.118 4.435 -24.107 1.00116.18 C ANISOU 2074 C GLU A 260 14896 13994 15254 909 -381 1417 C ATOM 2075 O GLU A 260 -4.005 4.642 -24.938 1.00109.55 O ANISOU 2075 O GLU A 260 14043 13109 14471 831 -339 1346 O ATOM 2076 CB GLU A 260 -2.044 2.174 -24.020 1.00119.56 C ANISOU 2076 CB GLU A 260 15212 14370 15846 1183 -131 1556 C ATOM 2077 CG GLU A 260 -0.616 2.681 -24.084 1.00119.95 C ANISOU 2077 CG GLU A 260 15137 14630 15807 1201 -251 1678 C ATOM 2078 CD GLU A 260 0.278 1.806 -24.931 1.00122.27 C ANISOU 2078 CD GLU A 260 15263 15017 16177 1333 -120 1780 C ATOM 2079 OE1 GLU A 260 0.046 0.580 -24.971 1.00126.78 O ANISOU 2079 OE1 GLU A 260 15851 15471 16850 1460 85 1772 O ATOM 2080 OE2 GLU A 260 1.209 2.345 -25.566 1.00121.05 O ANISOU 2080 OE2 GLU A 260 14965 15056 15971 1304 -214 1848 O ATOM 2081 N ARG A 261 -2.190 5.338 -23.802 1.00126.95 N ANISOU 2081 N ARG A 261 16187 15531 16516 874 -505 1493 N ATOM 2082 CA ARG A 261 -1.991 6.556 -24.576 1.00126.77 C ANISOU 2082 CA ARG A 261 16040 15685 16443 736 -605 1485 C ATOM 2083 C ARG A 261 -1.306 6.241 -25.905 1.00117.07 C ANISOU 2083 C ARG A 261 14639 14575 15268 754 -595 1530 C ATOM 2084 O ARG A 261 -0.624 5.223 -26.036 1.00121.34 O ANISOU 2084 O ARG A 261 15114 15119 15873 889 -514 1621 O ATOM 2085 CB ARG A 261 -1.163 7.569 -23.788 1.00134.07 C ANISOU 2085 CB ARG A 261 16904 16757 17281 670 -721 1555 C ATOM 2086 CG ARG A 261 -1.756 7.945 -22.443 1.00143.10 C ANISOU 2086 CG ARG A 261 18172 17809 18390 651 -731 1541 C ATOM 2087 CD ARG A 261 -0.747 8.711 -21.611 1.00150.47 C ANISOU 2087 CD ARG A 261 19042 18872 19256 619 -830 1622 C ATOM 2088 NE ARG A 261 -0.166 9.825 -22.353 1.00151.27 N ANISOU 2088 NE ARG A 261 18976 19151 19348 455 -922 1632 N ATOM 2089 CZ ARG A 261 0.826 10.585 -21.903 1.00145.39 C ANISOU 2089 CZ ARG A 261 18149 18531 18560 397 -1004 1700 C ATOM 2090 NH1 ARG A 261 1.352 10.351 -20.709 1.00144.11 N ANISOU 2090 NH1 ARG A 261 18049 18352 18354 498 -1015 1765 N ATOM 2091 NH2 ARG A 261 1.294 11.578 -22.646 1.00146.62 N ANISOU 2091 NH2 ARG A 261 18172 18818 18718 233 -1068 1703 N ATOM 2092 N SER A 262 -1.520 7.108 -26.892 1.00105.97 N ANISOU 2092 N SER A 262 13126 13277 13861 607 -658 1491 N ATOM 2093 CA SER A 262 -0.885 7.006 -28.207 1.00 98.33 C ANISOU 2093 CA SER A 262 11966 12456 12941 589 -666 1546 C ATOM 2094 C SER A 262 -1.233 5.707 -28.930 1.00 87.56 C ANISOU 2094 C SER A 262 10544 10985 11739 721 -507 1593 C ATOM 2095 O SER A 262 -0.579 5.336 -29.907 1.00 78.63 O ANISOU 2095 O SER A 262 9250 9973 10653 766 -472 1651 O ATOM 2096 CB SER A 262 0.637 7.140 -28.083 1.00108.91 C ANISOU 2096 CB SER A 262 13218 13967 14194 631 -723 1615 C ATOM 2097 OG SER A 262 1.002 8.426 -27.613 1.00119.68 O ANISOU 2097 OG SER A 262 14586 15427 15458 493 -833 1587 O ATOM 2098 N PHE A 263 -2.261 5.022 -28.441 1.00 82.46 N ANISOU 2098 N PHE A 263 10042 10107 11180 785 -383 1540 N ATOM 2099 CA PHE A 263 -2.843 3.899 -29.156 1.00 79.75 C ANISOU 2099 CA PHE A 263 9678 9608 11015 889 -178 1510 C ATOM 2100 C PHE A 263 -3.585 4.434 -30.375 1.00 71.01 C ANISOU 2100 C PHE A 263 8481 8502 9997 755 -208 1446 C ATOM 2101 O PHE A 263 -3.810 3.722 -31.354 1.00 63.58 O ANISOU 2101 O PHE A 263 7454 7492 9211 822 -55 1408 O ATOM 2102 CB PHE A 263 -3.779 3.107 -28.242 1.00 94.69 C ANISOU 2102 CB PHE A 263 11776 11252 12951 950 -33 1408 C ATOM 2103 CG PHE A 263 -4.310 1.843 -28.856 1.00 93.34 C ANISOU 2103 CG PHE A 263 11608 10919 12937 1048 221 1316 C ATOM 2104 CD1 PHE A 263 -3.557 0.681 -28.840 1.00 95.90 C ANISOU 2104 CD1 PHE A 263 11885 11249 13303 1219 383 1369 C ATOM 2105 CD2 PHE A 263 -5.567 1.814 -29.437 1.00 68.60 C ANISOU 2105 CD2 PHE A 263 8537 7640 9890 950 303 1148 C ATOM 2106 CE1 PHE A 263 -4.044 -0.486 -29.400 1.00 98.96 C ANISOU 2106 CE1 PHE A 263 12290 11505 13804 1283 622 1249 C ATOM 2107 CE2 PHE A 263 -6.057 0.651 -29.997 1.00 73.13 C ANISOU 2107 CE2 PHE A 263 9125 8091 10572 1008 536 1016 C ATOM 2108 CZ PHE A 263 -5.296 -0.500 -29.979 1.00 85.84 C ANISOU 2108 CZ PHE A 263 10691 9712 12211 1170 694 1065 C ATOM 2109 N PHE A 264 -3.966 5.704 -30.289 1.00 61.44 N ANISOU 2109 N PHE A 264 7291 7364 8688 559 -393 1406 N ATOM 2110 CA PHE A 264 -4.627 6.406 -31.378 1.00 51.38 C ANISOU 2110 CA PHE A 264 5927 6117 7477 385 -477 1342 C ATOM 2111 C PHE A 264 -3.700 6.600 -32.576 1.00 51.20 C ANISOU 2111 C PHE A 264 5678 6339 7436 356 -548 1395 C ATOM 2112 O PHE A 264 -4.160 6.748 -33.708 1.00 48.20 O ANISOU 2112 O PHE A 264 5184 5980 7148 267 -568 1329 O ATOM 2113 CB PHE A 264 -5.148 7.757 -30.889 1.00 50.73 C ANISOU 2113 CB PHE A 264 5927 6083 7266 171 -639 1264 C ATOM 2114 CG PHE A 264 -6.068 8.442 -31.860 1.00 46.82 C ANISOU 2114 CG PHE A 264 5385 5566 6839 -31 -723 1168 C ATOM 2115 CD1 PHE A 264 -7.275 7.866 -32.213 1.00 39.30 C ANISOU 2115 CD1 PHE A 264 4507 4366 6061 -26 -611 1063 C ATOM 2116 CD2 PHE A 264 -5.735 9.671 -32.402 1.00 43.92 C ANISOU 2116 CD2 PHE A 264 4961 5384 6343 -228 -845 1127 C ATOM 2117 CE1 PHE A 264 -8.126 8.493 -33.101 1.00 36.28 C ANISOU 2117 CE1 PHE A 264 4093 3952 5739 -218 -696 950 C ATOM 2118 CE2 PHE A 264 -6.585 10.305 -33.287 1.00 46.21 C ANISOU 2118 CE2 PHE A 264 5282 5625 6653 -400 -880 1025 C ATOM 2119 CZ PHE A 264 -7.781 9.713 -33.639 1.00 35.37 C ANISOU 2119 CZ PHE A 264 3910 4041 5486 -411 -876 967 C ATOM 2120 N SER A 265 -2.393 6.612 -32.323 1.00 53.63 N ANISOU 2120 N SER A 265 5930 6834 7614 420 -580 1476 N ATOM 2121 CA SER A 265 -1.416 6.749 -33.400 1.00 50.25 C ANISOU 2121 CA SER A 265 5324 6634 7133 394 -616 1489 C ATOM 2122 C SER A 265 -1.479 5.551 -34.338 1.00 47.68 C ANISOU 2122 C SER A 265 4854 6273 6988 551 -446 1501 C ATOM 2123 O SER A 265 -1.250 5.681 -35.543 1.00 46.50 O ANISOU 2123 O SER A 265 4555 6271 6841 481 -458 1437 O ATOM 2124 CB SER A 265 -0.003 6.902 -32.839 1.00 58.88 C ANISOU 2124 CB SER A 265 6411 7875 8085 448 -658 1561 C ATOM 2125 OG SER A 265 0.380 5.749 -32.107 1.00 77.95 O ANISOU 2125 OG SER A 265 8852 10205 10561 665 -536 1662 O ATOM 2126 N LEU A 266 -1.797 4.385 -33.784 1.00 51.55 N ANISOU 2126 N LEU A 266 5422 6547 7619 757 -243 1529 N ATOM 2127 CA LEU A 266 -2.008 3.195 -34.598 1.00 48.91 C ANISOU 2127 CA LEU A 266 5020 6106 7458 898 13 1439 C ATOM 2128 C LEU A 266 -3.220 3.387 -35.501 1.00 40.11 C ANISOU 2128 C LEU A 266 3945 4881 6413 717 68 1194 C ATOM 2129 O LEU A 266 -3.217 2.983 -36.668 1.00 44.61 O ANISOU 2129 O LEU A 266 4410 5506 7034 693 180 1061 O ATOM 2130 CB LEU A 266 -2.199 1.964 -33.712 1.00 52.23 C ANISOU 2130 CB LEU A 266 5606 6278 7963 1104 250 1441 C ATOM 2131 CG LEU A 266 -2.445 0.638 -34.432 1.00 61.13 C ANISOU 2131 CG LEU A 266 6726 7268 9234 1227 551 1294 C ATOM 2132 CD1 LEU A 266 -1.158 0.124 -35.064 1.00 62.99 C ANISOU 2132 CD1 LEU A 266 6784 7719 9429 1331 594 1368 C ATOM 2133 CD2 LEU A 266 -3.046 -0.399 -33.489 1.00 69.55 C ANISOU 2133 CD2 LEU A 266 8030 8076 10319 1303 741 1210 C ATOM 2134 N TYR A 267 -4.247 4.034 -34.958 1.00 36.59 N ANISOU 2134 N TYR A 267 3650 4286 5968 586 -17 1138 N ATOM 2135 CA TYR A 267 -5.445 4.341 -35.726 1.00 33.63 C ANISOU 2135 CA TYR A 267 3321 3805 5652 399 10 915 C ATOM 2136 C TYR A 267 -5.127 5.304 -36.856 1.00 34.69 C ANISOU 2136 C TYR A 267 3275 4208 5697 208 -174 878 C ATOM 2137 O TYR A 267 -5.650 5.173 -37.964 1.00 31.05 O ANISOU 2137 O TYR A 267 2765 3740 5292 112 -92 693 O ATOM 2138 CB TYR A 267 -6.522 4.945 -34.825 1.00 30.53 C ANISOU 2138 CB TYR A 267 3122 3214 5264 295 -70 888 C ATOM 2139 CG TYR A 267 -7.121 3.987 -33.826 1.00 33.82 C ANISOU 2139 CG TYR A 267 3738 3324 5790 458 135 876 C ATOM 2140 CD1 TYR A 267 -7.095 2.615 -34.043 1.00 36.78 C ANISOU 2140 CD1 TYR A 267 4129 3560 6286 642 415 805 C ATOM 2141 CD2 TYR A 267 -7.726 4.457 -32.669 1.00 36.73 C ANISOU 2141 CD2 TYR A 267 4287 3589 6081 404 52 893 C ATOM 2142 CE1 TYR A 267 -7.651 1.740 -33.132 1.00 36.98 C ANISOU 2142 CE1 TYR A 267 4354 3452 6245 697 560 718 C ATOM 2143 CE2 TYR A 267 -8.285 3.590 -31.753 1.00 35.63 C ANISOU 2143 CE2 TYR A 267 4341 3326 5872 486 210 786 C ATOM 2144 CZ TYR A 267 -8.247 2.234 -31.989 1.00 39.73 C ANISOU 2144 CZ TYR A 267 4868 3768 6461 621 444 711 C ATOM 2145 OH TYR A 267 -8.807 1.369 -31.075 1.00 46.36 O ANISOU 2145 OH TYR A 267 5865 4529 7222 668 540 628 O ATOM 2146 N LEU A 268 -4.248 6.260 -36.572 1.00 33.90 N ANISOU 2146 N LEU A 268 3076 4347 5458 156 -420 1058 N ATOM 2147 CA LEU A 268 -3.803 7.208 -37.580 1.00 31.68 C ANISOU 2147 CA LEU A 268 2685 4318 5034 -18 -575 1011 C ATOM 2148 C LEU A 268 -3.022 6.508 -38.678 1.00 33.02 C ANISOU 2148 C LEU A 268 2683 4635 5229 64 -460 977 C ATOM 2149 O LEU A 268 -3.151 6.838 -39.858 1.00 35.13 O ANISOU 2149 O LEU A 268 2934 4986 5429 -59 -459 809 O ATOM 2150 CB LEU A 268 -2.934 8.291 -36.940 1.00 43.35 C ANISOU 2150 CB LEU A 268 4295 5920 6257 -75 -714 1084 C ATOM 2151 CG LEU A 268 -3.492 9.708 -36.834 1.00 36.26 C ANISOU 2151 CG LEU A 268 3590 4985 5203 -252 -789 968 C ATOM 2152 CD1 LEU A 268 -4.873 9.695 -36.219 1.00 35.84 C ANISOU 2152 CD1 LEU A 268 3643 4719 5256 -310 -797 941 C ATOM 2153 CD2 LEU A 268 -2.548 10.558 -36.011 1.00 46.75 C ANISOU 2153 CD2 LEU A 268 5000 6380 6385 -253 -833 1031 C ATOM 2154 N GLY A 269 -2.220 5.525 -38.282 1.00 38.88 N ANISOU 2154 N GLY A 269 3341 5387 6045 293 -340 1119 N ATOM 2155 CA GLY A 269 -1.386 4.811 -39.226 1.00 41.73 C ANISOU 2155 CA GLY A 269 3561 5880 6414 386 -215 1094 C ATOM 2156 C GLY A 269 -2.209 3.927 -40.135 1.00 34.44 C ANISOU 2156 C GLY A 269 2639 4804 5643 396 26 877 C ATOM 2157 O GLY A 269 -1.913 3.793 -41.322 1.00 37.10 O ANISOU 2157 O GLY A 269 2833 5279 5985 356 69 790 O ATOM 2158 N ILE A 270 -3.255 3.327 -39.580 1.00 34.33 N ANISOU 2158 N ILE A 270 2814 4494 5737 440 187 771 N ATOM 2159 CA ILE A 270 -4.144 2.503 -40.383 1.00 33.97 C ANISOU 2159 CA ILE A 270 2814 4270 5822 434 421 538 C ATOM 2160 C ILE A 270 -5.005 3.358 -41.303 1.00 28.80 C ANISOU 2160 C ILE A 270 2138 3652 5153 187 316 364 C ATOM 2161 O ILE A 270 -5.114 3.096 -42.499 1.00 27.79 O ANISOU 2161 O ILE A 270 1915 3582 5062 135 403 216 O ATOM 2162 CB ILE A 270 -5.061 1.638 -39.503 1.00 38.98 C ANISOU 2162 CB ILE A 270 3662 4567 6582 548 624 472 C ATOM 2163 CG1 ILE A 270 -4.237 0.664 -38.657 1.00 34.10 C ANISOU 2163 CG1 ILE A 270 3066 3899 5990 806 757 631 C ATOM 2164 CG2 ILE A 270 -6.067 0.885 -40.358 1.00 29.81 C ANISOU 2164 CG2 ILE A 270 2549 3220 5557 519 850 218 C ATOM 2165 CD1 ILE A 270 -5.069 -0.132 -37.670 1.00 44.42 C ANISOU 2165 CD1 ILE A 270 4587 4881 7411 926 943 591 C ATOM 2166 N GLY A 271 -5.599 4.406 -40.749 1.00 32.50 N ANISOU 2166 N GLY A 271 2692 4092 5563 34 125 385 N ATOM 2167 CA GLY A 271 -6.536 5.204 -41.511 1.00 29.75 C ANISOU 2167 CA GLY A 271 2347 3748 5210 -198 32 218 C ATOM 2168 C GLY A 271 -5.927 6.135 -42.540 1.00 30.98 C ANISOU 2168 C GLY A 271 2464 4206 5103 -320 -141 199 C ATOM 2169 O GLY A 271 -6.509 6.342 -43.604 1.00 31.50 O ANISOU 2169 O GLY A 271 2601 4311 5056 -426 -116 37 O ATOM 2170 N TRP A 272 -4.750 6.682 -42.250 1.00 31.85 N ANISOU 2170 N TRP A 272 2527 4512 5065 -278 -284 349 N ATOM 2171 CA TRP A 272 -4.117 7.606 -43.184 1.00 32.10 C ANISOU 2171 CA TRP A 272 2595 4722 4880 -341 -381 251 C ATOM 2172 C TRP A 272 -2.845 7.028 -43.807 1.00 33.61 C ANISOU 2172 C TRP A 272 2620 5061 5092 -242 -346 316 C ATOM 2173 O TRP A 272 -2.620 7.184 -45.005 1.00 37.57 O ANISOU 2173 O TRP A 272 3096 5617 5563 -281 -330 176 O ATOM 2174 CB TRP A 272 -3.810 8.945 -42.498 1.00 32.63 C ANISOU 2174 CB TRP A 272 2828 4791 4778 -366 -532 314 C ATOM 2175 CG TRP A 272 -5.035 9.734 -42.100 1.00 30.89 C ANISOU 2175 CG TRP A 272 2793 4439 4505 -446 -544 232 C ATOM 2176 CD1 TRP A 272 -5.337 10.206 -40.853 1.00 30.57 C ANISOU 2176 CD1 TRP A 272 2873 4309 4435 -450 -606 348 C ATOM 2177 CD2 TRP A 272 -6.120 10.136 -42.952 1.00 29.37 C ANISOU 2177 CD2 TRP A 272 2676 4187 4296 -532 -501 87 C ATOM 2178 NE1 TRP A 272 -6.536 10.880 -40.876 1.00 25.65 N ANISOU 2178 NE1 TRP A 272 2395 3568 3782 -525 -604 291 N ATOM 2179 CE2 TRP A 272 -7.038 10.848 -42.152 1.00 31.68 C ANISOU 2179 CE2 TRP A 272 3133 4356 4549 -567 -539 134 C ATOM 2180 CE3 TRP A 272 -6.403 9.963 -44.312 1.00 28.02 C ANISOU 2180 CE3 TRP A 272 2450 4052 4146 -568 -431 -74 C ATOM 2181 CZ2 TRP A 272 -8.221 11.386 -42.668 1.00 24.52 C ANISOU 2181 CZ2 TRP A 272 2329 3376 3613 -617 -506 35 C ATOM 2182 CZ3 TRP A 272 -7.577 10.499 -44.823 1.00 29.67 C ANISOU 2182 CZ3 TRP A 272 2771 4183 4317 -626 -399 -174 C ATOM 2183 CH2 TRP A 272 -8.470 11.202 -44.002 1.00 26.08 C ANISOU 2183 CH2 TRP A 272 2464 3626 3819 -647 -435 -119 C ATOM 2184 N GLY A 273 -2.018 6.361 -43.005 1.00 33.83 N ANISOU 2184 N GLY A 273 2749 5226 4878 75 257 261 N ATOM 2185 CA GLY A 273 -0.757 5.832 -43.501 1.00 30.72 C ANISOU 2185 CA GLY A 273 2413 4895 4364 158 320 305 C ATOM 2186 C GLY A 273 -0.880 4.633 -44.430 1.00 32.81 C ANISOU 2186 C GLY A 273 2695 5141 4629 198 323 416 C ATOM 2187 O GLY A 273 -0.266 4.596 -45.506 1.00 35.01 O ANISOU 2187 O GLY A 273 2993 5456 4853 232 332 479 O ATOM 2188 N ALA A 274 -1.688 3.657 -44.024 1.00 24.88 N ANISOU 2188 N ALA A 274 1661 4121 3671 215 320 528 N ATOM 2189 CA ALA A 274 -1.877 2.456 -44.824 1.00 30.68 C ANISOU 2189 CA ALA A 274 2388 4838 4431 281 336 755 C ATOM 2190 C ALA A 274 -2.361 2.773 -46.250 1.00 35.84 C ANISOU 2190 C ALA A 274 3020 5364 5233 195 234 838 C ATOM 2191 O ALA A 274 -1.822 2.211 -47.206 1.00 34.90 O ANISOU 2191 O ALA A 274 3021 5185 5052 254 247 925 O ATOM 2192 CB ALA A 274 -2.851 1.497 -44.129 1.00 35.30 C ANISOU 2192 CB ALA A 274 2944 5366 5103 287 332 863 C ATOM 2193 N PRO A 275 -3.386 3.644 -46.400 1.00 31.68 N ANISOU 2193 N PRO A 275 2481 4707 4848 38 105 749 N ATOM 2194 CA PRO A 275 -3.723 4.018 -47.780 1.00 33.67 C ANISOU 2194 CA PRO A 275 2756 4788 5247 -80 -28 801 C ATOM 2195 C PRO A 275 -2.566 4.663 -48.537 1.00 31.79 C ANISOU 2195 C PRO A 275 2550 4641 4886 -47 4 734 C ATOM 2196 O PRO A 275 -2.436 4.438 -49.738 1.00 31.02 O ANISOU 2196 O PRO A 275 2696 4345 4746 -80 -70 739 O ATOM 2197 CB PRO A 275 -4.866 5.031 -47.594 1.00 31.45 C ANISOU 2197 CB PRO A 275 2520 4395 5035 -217 -129 651 C ATOM 2198 CG PRO A 275 -5.449 4.708 -46.274 1.00 33.81 C ANISOU 2198 CG PRO A 275 2789 4756 5302 -178 -74 618 C ATOM 2199 CD PRO A 275 -4.291 4.280 -45.425 1.00 25.86 C ANISOU 2199 CD PRO A 275 1743 3949 4133 -35 70 596 C ATOM 2200 N ALA A 276 -1.732 5.425 -47.850 1.00 35.25 N ANISOU 2200 N ALA A 276 2975 5258 5159 15 101 563 N ATOM 2201 CA ALA A 276 -0.597 6.071 -48.501 1.00 34.94 C ANISOU 2201 CA ALA A 276 2963 5306 5007 49 136 494 C ATOM 2202 C ALA A 276 0.384 5.030 -49.023 1.00 38.18 C ANISOU 2202 C ALA A 276 3424 5807 5275 196 233 637 C ATOM 2203 O ALA A 276 0.966 5.192 -50.102 1.00 43.98 O ANISOU 2203 O ALA A 276 4335 6452 5921 188 198 600 O ATOM 2204 CB ALA A 276 0.102 7.027 -47.539 1.00 30.50 C ANISOU 2204 CB ALA A 276 2435 4792 4362 72 203 291 C ATOM 2205 N LEU A 277 0.511 3.936 -48.273 1.00 36.09 N ANISOU 2205 N LEU A 277 3164 5607 4942 318 334 729 N ATOM 2206 CA LEU A 277 1.421 2.845 -48.626 1.00 37.50 C ANISOU 2206 CA LEU A 277 3549 5773 4926 462 423 793 C ATOM 2207 C LEU A 277 1.084 2.198 -49.965 1.00 35.89 C ANISOU 2207 C LEU A 277 3661 5249 4726 402 307 837 C ATOM 2208 O LEU A 277 1.962 1.662 -50.639 1.00 45.65 O ANISOU 2208 O LEU A 277 5090 6454 5800 488 353 853 O ATOM 2209 CB LEU A 277 1.410 1.769 -47.541 1.00 40.04 C ANISOU 2209 CB LEU A 277 3811 6199 5204 586 538 891 C ATOM 2210 CG LEU A 277 2.534 1.740 -46.507 1.00 54.73 C ANISOU 2210 CG LEU A 277 5713 8198 6883 657 613 793 C ATOM 2211 CD1 LEU A 277 2.448 0.456 -45.694 1.00 44.54 C ANISOU 2211 CD1 LEU A 277 4456 6920 5546 753 678 896 C ATOM 2212 CD2 LEU A 277 3.897 1.876 -47.171 1.00 46.66 C ANISOU 2212 CD2 LEU A 277 4804 7241 5684 734 659 750 C ATOM 2213 N PHE A 278 -0.189 2.223 -50.338 1.00 36.33 N ANISOU 2213 N PHE A 278 3770 5069 4966 255 159 859 N ATOM 2214 CA PHE A 278 -0.620 1.594 -51.580 1.00 38.57 C ANISOU 2214 CA PHE A 278 4347 5040 5269 188 43 905 C ATOM 2215 C PHE A 278 -0.841 2.612 -52.687 1.00 35.40 C ANISOU 2215 C PHE A 278 4011 4497 4941 41 -94 819 C ATOM 2216 O PHE A 278 -0.515 2.363 -53.846 1.00 45.60 O ANISOU 2216 O PHE A 278 5540 5624 6162 26 -145 819 O ATOM 2217 CB PHE A 278 -1.896 0.788 -51.347 1.00 36.47 C ANISOU 2217 CB PHE A 278 4130 4579 5148 127 -32 998 C ATOM 2218 CG PHE A 278 -1.689 -0.438 -50.513 1.00 35.42 C ANISOU 2218 CG PHE A 278 4004 4524 4929 272 90 1098 C ATOM 2219 CD1 PHE A 278 -1.805 -0.383 -49.136 1.00 35.99 C ANISOU 2219 CD1 PHE A 278 3826 4814 5034 329 181 1111 C ATOM 2220 CD2 PHE A 278 -1.372 -1.647 -51.107 1.00 41.42 C ANISOU 2220 CD2 PHE A 278 5021 5141 5576 350 115 1180 C ATOM 2221 CE1 PHE A 278 -1.612 -1.510 -48.366 1.00 31.42 C ANISOU 2221 CE1 PHE A 278 3253 4309 4377 462 293 1204 C ATOM 2222 CE2 PHE A 278 -1.179 -2.777 -50.341 1.00 42.78 C ANISOU 2222 CE2 PHE A 278 5200 5385 5671 484 228 1274 C ATOM 2223 CZ PHE A 278 -1.300 -2.708 -48.969 1.00 39.31 C ANISOU 2223 CZ PHE A 278 4509 5162 5264 540 317 1286 C ATOM 2224 N VAL A 279 -1.394 3.761 -52.323 1.00 30.34 N ANISOU 2224 N VAL A 279 3159 3924 4445 -68 -153 745 N ATOM 2225 CA VAL A 279 -1.701 4.791 -53.300 1.00 34.51 C ANISOU 2225 CA VAL A 279 3727 4323 5064 -216 -288 663 C ATOM 2226 C VAL A 279 -0.444 5.482 -53.834 1.00 38.86 C ANISOU 2226 C VAL A 279 4296 5007 5462 -166 -234 574 C ATOM 2227 O VAL A 279 -0.331 5.696 -55.043 1.00 38.56 O ANISOU 2227 O VAL A 279 4444 4800 5407 -234 -325 543 O ATOM 2228 CB VAL A 279 -2.665 5.845 -52.708 1.00 39.18 C ANISOU 2228 CB VAL A 279 4074 4954 5859 -348 -363 608 C ATOM 2229 CG1 VAL A 279 -2.782 7.053 -53.627 1.00 32.53 C ANISOU 2229 CG1 VAL A 279 3240 4030 5091 -485 -480 510 C ATOM 2230 CG2 VAL A 279 -4.037 5.228 -52.466 1.00 38.35 C ANISOU 2230 CG2 VAL A 279 3992 4656 5923 -430 -453 690 C ATOM 2231 N VAL A 280 0.495 5.833 -52.958 1.00 35.08 N ANISOU 2231 N VAL A 280 3630 4829 4872 -49 -89 532 N ATOM 2232 CA VAL A 280 1.693 6.529 -53.439 1.00 38.60 C ANISOU 2232 CA VAL A 280 4084 5410 5172 -1 -36 443 C ATOM 2233 C VAL A 280 2.508 5.741 -54.484 1.00 43.84 C ANISOU 2233 C VAL A 280 5038 5954 5664 73 -21 474 C ATOM 2234 O VAL A 280 2.784 6.267 -55.568 1.00 42.41 O ANISOU 2234 O VAL A 280 4984 5669 5459 6 -97 414 O ATOM 2235 CB VAL A 280 2.624 6.938 -52.262 1.00 39.98 C ANISOU 2235 CB VAL A 280 4011 5941 5240 127 132 400 C ATOM 2236 CG1 VAL A 280 3.955 7.443 -52.792 1.00 34.76 C ANISOU 2236 CG1 VAL A 280 3394 5412 4401 198 199 320 C ATOM 2237 CG2 VAL A 280 1.960 7.992 -51.394 1.00 35.08 C ANISOU 2237 CG2 VAL A 280 3098 5450 4782 39 111 341 C ATOM 2238 N PRO A 281 2.879 4.470 -54.182 1.00 44.54 N ANISOU 2238 N PRO A 281 5235 6052 5635 206 75 568 N ATOM 2239 CA PRO A 281 3.653 3.734 -55.192 1.00 47.60 C ANISOU 2239 CA PRO A 281 5899 6325 5864 273 89 596 C ATOM 2240 C PRO A 281 2.920 3.579 -56.522 1.00 46.85 C ANISOU 2240 C PRO A 281 6047 5897 5858 135 -78 611 C ATOM 2241 O PRO A 281 3.552 3.600 -57.586 1.00 47.00 O ANISOU 2241 O PRO A 281 6254 5828 5776 134 -105 581 O ATOM 2242 CB PRO A 281 3.868 2.364 -54.538 1.00 44.97 C ANISOU 2242 CB PRO A 281 5621 6029 5436 418 203 707 C ATOM 2243 CG PRO A 281 3.764 2.630 -53.083 1.00 43.63 C ANISOU 2243 CG PRO A 281 5162 6107 5307 471 299 705 C ATOM 2244 CD PRO A 281 2.689 3.659 -52.972 1.00 42.62 C ANISOU 2244 CD PRO A 281 4878 5926 5391 306 177 651 C ATOM 2245 N TRP A 282 1.603 3.430 -56.473 1.00 47.18 N ANISOU 2245 N TRP A 282 6085 5757 6085 19 -189 657 N ATOM 2246 CA TRP A 282 0.867 3.269 -57.713 1.00 46.03 C ANISOU 2246 CA TRP A 282 6166 5296 6027 -115 -348 675 C ATOM 2247 C TRP A 282 0.716 4.590 -58.453 1.00 45.09 C ANISOU 2247 C TRP A 282 6010 5131 5992 -255 -462 569 C ATOM 2248 O TRP A 282 0.584 4.613 -59.679 1.00 42.85 O ANISOU 2248 O TRP A 282 5932 4631 5717 -342 -571 558 O ATOM 2249 CB TRP A 282 -0.503 2.643 -57.488 1.00 51.96 C ANISOU 2249 CB TRP A 282 6941 5853 6946 -196 -434 760 C ATOM 2250 CG TRP A 282 -1.014 2.145 -58.787 1.00 63.80 C ANISOU 2250 CG TRP A 282 8721 7037 8483 -291 -563 797 C ATOM 2251 CD1 TRP A 282 -2.043 2.658 -59.521 1.00 59.40 C ANISOU 2251 CD1 TRP A 282 8217 6260 8093 -467 -730 777 C ATOM 2252 CD2 TRP A 282 -0.458 1.078 -59.561 1.00 58.72 C ANISOU 2252 CD2 TRP A 282 8347 6266 7698 -217 -535 857 C ATOM 2253 NE1 TRP A 282 -2.183 1.950 -60.691 1.00 59.54 N ANISOU 2253 NE1 TRP A 282 8441 6142 8039 -467 -743 757 N ATOM 2254 CE2 TRP A 282 -1.220 0.975 -60.739 1.00 68.82 C ANISOU 2254 CE2 TRP A 282 9782 7310 9056 -339 -655 834 C ATOM 2255 CE3 TRP A 282 0.600 0.184 -59.362 1.00 55.60 C ANISOU 2255 CE3 TRP A 282 8037 5980 7107 -47 -393 901 C ATOM 2256 CZ2 TRP A 282 -0.955 0.017 -61.719 1.00 67.50 C ANISOU 2256 CZ2 TRP A 282 9777 7086 8784 -287 -607 820 C ATOM 2257 CZ3 TRP A 282 0.857 -0.767 -60.332 1.00 60.88 C ANISOU 2257 CZ3 TRP A 282 8989 6457 7684 -22 -410 957 C ATOM 2258 CH2 TRP A 282 0.081 -0.846 -61.494 1.00 61.55 C ANISOU 2258 CH2 TRP A 282 9144 6371 7870 -146 -506 897 C ATOM 2259 N ALA A 283 0.722 5.692 -57.713 1.00 46.47 N ANISOU 2259 N ALA A 283 5921 5507 6230 -281 -438 491 N ATOM 2260 CA ALA A 283 0.781 6.996 -58.351 1.00 44.59 C ANISOU 2260 CA ALA A 283 5631 5265 6044 -393 -524 382 C ATOM 2261 C ALA A 283 2.120 7.128 -59.066 1.00 43.71 C ANISOU 2261 C ALA A 283 5643 5229 5736 -312 -463 329 C ATOM 2262 O ALA A 283 2.208 7.723 -60.142 1.00 41.58 O ANISOU 2262 O ALA A 283 5486 4838 5475 -403 -559 269 O ATOM 2263 CB ALA A 283 0.598 8.111 -57.329 1.00 36.08 C ANISOU 2263 CB ALA A 283 4236 4410 5062 -423 -493 311 C ATOM 2264 N VAL A 284 3.157 6.541 -58.474 1.00 41.36 N ANISOU 2264 N VAL A 284 5327 5127 5260 -139 -304 352 N ATOM 2265 CA VAL A 284 4.474 6.536 -59.095 1.00 39.44 C ANISOU 2265 CA VAL A 284 5208 4960 4816 -46 -234 309 C ATOM 2266 C VAL A 284 4.459 5.723 -60.387 1.00 43.84 C ANISOU 2266 C VAL A 284 6088 5244 5324 -75 -313 358 C ATOM 2267 O VAL A 284 5.007 6.153 -61.405 1.00 42.32 O ANISOU 2267 O VAL A 284 6025 4991 5064 -109 -359 297 O ATOM 2268 CB VAL A 284 5.546 5.967 -58.139 1.00 40.77 C ANISOU 2268 CB VAL A 284 5294 5391 4805 150 -42 335 C ATOM 2269 CG1 VAL A 284 6.872 5.790 -58.855 1.00 48.04 C ANISOU 2269 CG1 VAL A 284 6378 6362 5514 248 26 303 C ATOM 2270 CG2 VAL A 284 5.704 6.860 -56.920 1.00 34.82 C ANISOU 2270 CG2 VAL A 284 4220 4927 4082 180 44 274 C ATOM 2271 N VAL A 285 3.811 4.560 -60.357 1.00 46.52 N ANISOU 2271 N VAL A 285 6557 5417 5702 -64 -332 467 N ATOM 2272 CA VAL A 285 3.704 3.736 -61.562 1.00 55.28 C ANISOU 2272 CA VAL A 285 7973 6256 6777 -98 -409 520 C ATOM 2273 C VAL A 285 2.879 4.435 -62.648 1.00 52.11 C ANISOU 2273 C VAL A 285 7661 5618 6521 -288 -592 477 C ATOM 2274 O VAL A 285 3.192 4.342 -63.839 1.00 55.23 O ANISOU 2274 O VAL A 285 8273 5856 6856 -327 -655 462 O ATOM 2275 CB VAL A 285 3.076 2.357 -61.249 1.00 51.95 C ANISOU 2275 CB VAL A 285 7658 5701 6381 -55 -394 647 C ATOM 2276 CG1 VAL A 285 2.773 1.590 -62.528 1.00 53.92 C ANISOU 2276 CG1 VAL A 285 8215 5646 6626 -118 -493 700 C ATOM 2277 CG2 VAL A 285 3.999 1.548 -60.359 1.00 49.68 C ANISOU 2277 CG2 VAL A 285 7327 5622 5927 139 -213 696 C ATOM 2278 N LYS A 286 1.857 5.174 -62.227 1.00 55.87 N ANISOU 2278 N LYS A 286 6766 7125 7337 724 1807 863 N ATOM 2279 CA LYS A 286 1.012 5.901 -63.165 1.00 62.83 C ANISOU 2279 CA LYS A 286 7827 8072 7973 510 1547 608 C ATOM 2280 C LYS A 286 1.799 7.009 -63.844 1.00 58.02 C ANISOU 2280 C LYS A 286 7364 7450 7231 498 1362 495 C ATOM 2281 O LYS A 286 1.770 7.148 -65.065 1.00 61.09 O ANISOU 2281 O LYS A 286 7990 7682 7542 255 1377 288 O ATOM 2282 CB LYS A 286 -0.210 6.489 -62.453 1.00 63.27 C ANISOU 2282 CB LYS A 286 7737 8465 7838 599 1207 603 C ATOM 2283 CG LYS A 286 -1.398 5.547 -62.350 1.00 63.09 C ANISOU 2283 CG LYS A 286 7673 8436 7860 473 1324 591 C ATOM 2284 CD LYS A 286 -2.090 5.381 -63.693 1.00 70.84 C ANISOU 2284 CD LYS A 286 8911 9256 8750 134 1346 329 C ATOM 2285 CE LYS A 286 -3.362 4.561 -63.562 1.00 70.61 C ANISOU 2285 CE LYS A 286 8834 9248 8744 16 1414 312 C ATOM 2286 NZ LYS A 286 -4.126 4.513 -64.840 1.00 88.62 N ANISOU 2286 NZ LYS A 286 11361 11400 10910 -307 1390 47 N ATOM 2287 N CYS A 287 2.511 7.789 -63.039 1.00 56.80 N ANISOU 2287 N CYS A 287 7063 7462 7055 764 1190 636 N ATOM 2288 CA CYS A 287 3.315 8.888 -63.552 1.00 60.37 C ANISOU 2288 CA CYS A 287 7625 7922 7392 787 998 557 C ATOM 2289 C CYS A 287 4.463 8.398 -64.433 1.00 58.47 C ANISOU 2289 C CYS A 287 7560 7344 7311 666 1314 532 C ATOM 2290 O CYS A 287 4.855 9.072 -65.384 1.00 59.18 O ANISOU 2290 O CYS A 287 7835 7358 7293 544 1216 379 O ATOM 2291 CB CYS A 287 3.863 9.719 -62.388 1.00 53.84 C ANISOU 2291 CB CYS A 287 6582 7336 6540 1121 768 739 C ATOM 2292 SG CYS A 287 4.840 11.152 -62.884 1.00 91.84 S ANISOU 2292 SG CYS A 287 11497 12187 11212 1181 495 663 S ATOM 2293 N LEU A 288 4.988 7.216 -64.122 1.00 60.43 N ANISOU 2293 N LEU A 288 7750 7393 7817 700 1694 684 N ATOM 2294 CA LEU A 288 6.132 6.679 -64.853 1.00 60.74 C ANISOU 2294 CA LEU A 288 7937 7113 8028 609 2016 685 C ATOM 2295 C LEU A 288 5.775 5.997 -66.169 1.00 61.52 C ANISOU 2295 C LEU A 288 8283 6953 8139 278 2226 480 C ATOM 2296 O LEU A 288 6.488 6.150 -67.159 1.00 72.60 O ANISOU 2296 O LEU A 288 9882 8161 9543 147 2316 371 O ATOM 2297 CB LEU A 288 6.901 5.688 -63.975 1.00 56.46 C ANISOU 2297 CB LEU A 288 7230 6456 7767 785 2342 935 C ATOM 2298 CG LEU A 288 7.912 6.295 -63.005 1.00 57.20 C ANISOU 2298 CG LEU A 288 7149 6671 7913 1095 2245 1138 C ATOM 2299 CD1 LEU A 288 8.543 5.220 -62.139 1.00 50.87 C ANISOU 2299 CD1 LEU A 288 6184 5754 7391 1251 2580 1379 C ATOM 2300 CD2 LEU A 288 8.972 7.056 -63.779 1.00 53.73 C ANISOU 2300 CD2 LEU A 288 6868 6117 7431 1067 2193 1065 C ATOM 2301 N PHE A 289 4.677 5.247 -66.186 1.00 62.04 N ANISOU 2301 N PHE A 289 8342 7017 8215 145 2303 427 N ATOM 2302 CA PHE A 289 4.415 4.359 -67.315 1.00 71.56 C ANISOU 2302 CA PHE A 289 9759 7944 9486 -149 2568 267 C ATOM 2303 C PHE A 289 3.073 4.594 -67.997 1.00 76.47 C ANISOU 2303 C PHE A 289 10504 8647 9904 -374 2372 40 C ATOM 2304 O PHE A 289 2.924 4.336 -69.192 1.00 80.07 O ANISOU 2304 O PHE A 289 11190 8903 10330 -634 2478 -154 O ATOM 2305 CB PHE A 289 4.507 2.906 -66.852 1.00 72.57 C ANISOU 2305 CB PHE A 289 9790 7896 9887 -135 2954 420 C ATOM 2306 CG PHE A 289 5.707 2.624 -65.997 1.00 69.46 C ANISOU 2306 CG PHE A 289 9239 7452 9699 109 3139 666 C ATOM 2307 CD1 PHE A 289 6.984 2.679 -66.533 1.00 69.85 C ANISOU 2307 CD1 PHE A 289 9405 7295 9841 106 3303 675 C ATOM 2308 CD2 PHE A 289 5.561 2.310 -64.655 1.00 68.88 C ANISOU 2308 CD2 PHE A 289 8901 7541 9728 343 3146 890 C ATOM 2309 CE1 PHE A 289 8.093 2.426 -65.748 1.00 70.37 C ANISOU 2309 CE1 PHE A 289 9327 7311 10098 329 3471 901 C ATOM 2310 CE2 PHE A 289 6.664 2.052 -63.864 1.00 62.79 C ANISOU 2310 CE2 PHE A 289 7986 6724 9148 568 3314 1116 C ATOM 2311 CZ PHE A 289 7.933 2.110 -64.411 1.00 70.37 C ANISOU 2311 CZ PHE A 289 9065 7472 10200 560 3476 1120 C ATOM 2312 N GLU A 290 2.097 5.077 -67.238 1.00 81.70 N ANISOU 2312 N GLU A 290 11014 9601 10427 -274 2088 66 N ATOM 2313 CA GLU A 290 0.756 5.281 -67.773 1.00 88.44 C ANISOU 2313 CA GLU A 290 11963 10549 11092 -474 1894 -134 C ATOM 2314 C GLU A 290 0.341 6.743 -67.678 1.00 82.40 C ANISOU 2314 C GLU A 290 11182 10077 10047 -406 1438 -224 C ATOM 2315 O GLU A 290 -0.841 7.055 -67.531 1.00 78.87 O ANISOU 2315 O GLU A 290 10700 9826 9441 -453 1204 -306 O ATOM 2316 CB GLU A 290 -0.247 4.393 -67.035 1.00 88.62 C ANISOU 2316 CB GLU A 290 11828 10641 11201 -455 1982 -40 C ATOM 2317 CG GLU A 290 0.199 2.943 -66.925 1.00 91.84 C ANISOU 2317 CG GLU A 290 12207 10784 11904 -480 2424 86 C ATOM 2318 CD GLU A 290 -0.796 2.076 -66.182 1.00103.12 C ANISOU 2318 CD GLU A 290 13471 12286 13422 -459 2505 187 C ATOM 2319 OE1 GLU A 290 -0.357 1.196 -65.411 1.00 98.78 O ANISOU 2319 OE1 GLU A 290 12765 11666 13103 -322 2763 395 O ATOM 2320 OE2 GLU A 290 -2.015 2.270 -66.375 1.00105.70 O ANISOU 2320 OE2 GLU A 290 13827 12740 13594 -580 2313 59 O ATOM 2321 N ASN A 291 1.321 7.636 -67.776 1.00 79.74 N ANISOU 2321 N ASN A 291 10873 9767 9656 -298 1314 -210 N ATOM 2322 CA ASN A 291 1.072 9.065 -67.643 1.00 78.88 C ANISOU 2322 CA ASN A 291 10740 9933 9298 -212 879 -281 C ATOM 2323 C ASN A 291 0.392 9.609 -68.893 1.00 84.34 C ANISOU 2323 C ASN A 291 11669 10600 9777 -487 706 -562 C ATOM 2324 O ASN A 291 1.015 10.275 -69.721 1.00 85.75 O ANISOU 2324 O ASN A 291 12008 10700 9874 -566 633 -677 O ATOM 2325 CB ASN A 291 2.379 9.813 -67.369 1.00 78.01 C ANISOU 2325 CB ASN A 291 10585 9843 9214 -10 811 -171 C ATOM 2326 CG ASN A 291 2.159 11.280 -67.056 1.00 75.34 C ANISOU 2326 CG ASN A 291 10183 9806 8636 118 355 -213 C ATOM 2327 OD1 ASN A 291 1.607 11.628 -66.012 1.00 73.02 O ANISOU 2327 OD1 ASN A 291 9687 9781 8276 308 139 -111 O ATOM 2328 ND2 ASN A 291 2.599 12.150 -67.957 1.00 84.49 N ANISOU 2328 ND2 ASN A 291 11512 10924 9665 20 203 -361 N ATOM 2329 N VAL A 292 -0.898 9.314 -69.012 1.00 83.74 N ANISOU 2329 N VAL A 292 11609 10593 9615 -630 640 -668 N ATOM 2330 CA VAL A 292 -1.689 9.709 -70.167 1.00 84.57 C ANISOU 2330 CA VAL A 292 11934 10673 9526 -904 489 -937 C ATOM 2331 C VAL A 292 -3.054 10.190 -69.683 1.00 84.10 C ANISOU 2331 C VAL A 292 11775 10902 9278 -892 170 -989 C ATOM 2332 O VAL A 292 -3.556 9.714 -68.664 1.00 83.83 O ANISOU 2332 O VAL A 292 11540 10994 9318 -752 195 -837 O ATOM 2333 CB VAL A 292 -1.845 8.540 -71.172 1.00 83.75 C ANISOU 2333 CB VAL A 292 12024 10247 9549 -1177 840 -1053 C ATOM 2334 CG1 VAL A 292 -2.581 7.370 -70.530 1.00 81.96 C ANISOU 2334 CG1 VAL A 292 11667 9998 9476 -1171 1042 -946 C ATOM 2335 CG2 VAL A 292 -2.548 8.998 -72.445 1.00 92.07 C ANISOU 2335 CG2 VAL A 292 13322 11259 10401 -1461 687 -1339 C ATOM 2336 N GLN A 293 -3.636 11.142 -70.410 1.00 86.14 N ANISOU 2336 N GLN A 293 12171 11264 9293 -1036 -131 -1201 N ATOM 2337 CA GLN A 293 -4.894 11.773 -70.022 1.00 88.18 C ANISOU 2337 CA GLN A 293 12349 11810 9345 -1027 -475 -1269 C ATOM 2338 C GLN A 293 -4.825 12.330 -68.606 1.00 81.29 C ANISOU 2338 C GLN A 293 11202 11234 8450 -703 -690 -1065 C ATOM 2339 O GLN A 293 -4.112 13.297 -68.341 1.00 78.49 O ANISOU 2339 O GLN A 293 10797 11002 8022 -539 -892 -1021 O ATOM 2340 CB GLN A 293 -6.058 10.786 -70.132 1.00 90.97 C ANISOU 2340 CB GLN A 293 12720 12102 9743 -1195 -334 -1323 C ATOM 2341 CG GLN A 293 -6.488 10.471 -71.552 1.00 99.12 C ANISOU 2341 CG GLN A 293 14027 12910 10723 -1532 -234 -1571 C ATOM 2342 CD GLN A 293 -7.677 9.531 -71.597 1.00111.44 C ANISOU 2342 CD GLN A 293 15591 14423 12328 -1686 -117 -1617 C ATOM 2343 OE1 GLN A 293 -8.726 9.863 -72.150 1.00111.12 O ANISOU 2343 OE1 GLN A 293 15543 14426 12253 -1726 -294 -1680 O ATOM 2344 NE2 GLN A 293 -7.519 8.348 -71.013 1.00104.62 N ANISOU 2344 NE2 GLN A 293 14609 13437 11703 -1616 200 -1444 N ATOM 2345 N CYS A 294 -5.571 11.705 -67.703 1.00 80.04 N ANISOU 2345 N CYS A 294 10864 11188 8357 -611 -644 -941 N ATOM 2346 CA CYS A 294 -5.638 12.147 -66.318 1.00 79.43 C ANISOU 2346 CA CYS A 294 10519 11404 8258 -305 -841 -746 C ATOM 2347 C CYS A 294 -5.652 10.948 -65.369 1.00 79.16 C ANISOU 2347 C CYS A 294 10297 11325 8455 -174 -548 -523 C ATOM 2348 O CYS A 294 -6.200 11.014 -64.269 1.00 73.84 O ANISOU 2348 O CYS A 294 9404 10892 7758 18 -680 -386 O ATOM 2349 CB CYS A 294 -6.876 13.019 -66.106 1.00 71.45 C ANISOU 2349 CB CYS A 294 9468 10652 7029 -306 -1226 -836 C ATOM 2350 SG CYS A 294 -7.003 13.763 -64.475 1.00 75.06 S ANISOU 2350 SG CYS A 294 9668 11176 7676 13 -1370 -525 S ATOM 2351 N TRP A 295 -5.047 9.848 -65.809 1.00 82.31 N ANISOU 2351 N TRP A 295 10782 11414 9078 -279 -148 -487 N ATOM 2352 CA TRP A 295 -5.027 8.607 -65.035 1.00 82.88 C ANISOU 2352 CA TRP A 295 10696 11403 9390 -186 165 -286 C ATOM 2353 C TRP A 295 -6.451 8.173 -64.692 1.00 83.94 C ANISOU 2353 C TRP A 295 10749 11670 9475 -250 103 -303 C ATOM 2354 O TRP A 295 -6.688 7.530 -63.670 1.00 82.06 O ANISOU 2354 O TRP A 295 10301 11514 9363 -92 209 -109 O ATOM 2355 CB TRP A 295 -4.205 8.774 -63.750 1.00 69.98 C ANISOU 2355 CB TRP A 295 8819 9912 7859 155 158 -26 C ATOM 2356 CG TRP A 295 -2.819 9.313 -63.954 1.00 66.92 C ANISOU 2356 CG TRP A 295 8485 9431 7510 251 179 8 C ATOM 2357 CD1 TRP A 295 -2.149 9.430 -65.136 1.00 68.79 C ANISOU 2357 CD1 TRP A 295 8957 9432 7746 65 279 -142 C ATOM 2358 CD2 TRP A 295 -1.935 9.812 -62.941 1.00 64.43 C ANISOU 2358 CD2 TRP A 295 7982 9257 7241 561 94 208 C ATOM 2359 NE1 TRP A 295 -0.903 9.971 -64.922 1.00 71.39 N ANISOU 2359 NE1 TRP A 295 9256 9748 8122 238 263 -44 N ATOM 2360 CE2 TRP A 295 -0.748 10.213 -63.582 1.00 64.13 C ANISOU 2360 CE2 TRP A 295 8079 9054 7234 543 149 169 C ATOM 2361 CE3 TRP A 295 -2.034 9.957 -61.553 1.00 58.30 C ANISOU 2361 CE3 TRP A 295 6936 8731 6483 855 -23 416 C ATOM 2362 CZ2 TRP A 295 0.334 10.750 -62.885 1.00 60.04 C ANISOU 2362 CZ2 TRP A 295 7436 8607 6768 805 88 332 C ATOM 2363 CZ3 TRP A 295 -0.958 10.490 -60.862 1.00 54.77 C ANISOU 2363 CZ3 TRP A 295 6368 8356 6086 1117 -83 574 C ATOM 2364 CH2 TRP A 295 0.209 10.879 -61.529 1.00 56.30 C ANISOU 2364 CH2 TRP A 295 6701 8375 6313 1089 -28 531 C ATOM 2365 N THR A 296 -7.393 8.526 -65.561 1.00 90.25 N ANISOU 2365 N THR A 296 11714 12486 10091 -485 -68 -533 N ATOM 2366 CA THR A 296 -8.810 8.310 -65.298 1.00 98.99 C ANISOU 2366 CA THR A 296 12756 13743 11113 -553 -188 -572 C ATOM 2367 C THR A 296 -9.274 6.940 -65.781 1.00104.29 C ANISOU 2367 C THR A 296 13508 14158 11961 -765 153 -601 C ATOM 2368 O THR A 296 -8.534 6.228 -66.458 1.00113.21 O ANISOU 2368 O THR A 296 14773 14987 13256 -885 463 -624 O ATOM 2369 CB THR A 296 -9.672 9.401 -65.966 1.00 96.49 C ANISOU 2369 CB THR A 296 12573 13585 10504 -701 -562 -809 C ATOM 2370 OG1 THR A 296 -9.238 9.592 -67.319 1.00 97.12 O ANISOU 2370 OG1 THR A 296 12924 13437 10539 -938 -506 -1018 O ATOM 2371 CG2 THR A 296 -9.544 10.716 -65.216 1.00 88.80 C ANISOU 2371 CG2 THR A 296 11459 12934 9346 -462 -945 -757 C ATOM 2372 N ASN A 300 -13.463 1.401 -64.716 1.00 91.29 N ANISOU 2372 N ASN A 300 11525 12166 10995 -1167 1091 -318 N ATOM 2373 CA ASN A 300 -13.352 1.413 -63.262 1.00 83.67 C ANISOU 2373 CA ASN A 300 10263 11438 10089 -857 1050 -52 C ATOM 2374 C ASN A 300 -14.034 2.630 -62.644 1.00 78.38 C ANISOU 2374 C ASN A 300 9479 11145 9155 -711 625 -62 C ATOM 2375 O ASN A 300 -14.133 2.740 -61.420 1.00 68.61 O ANISOU 2375 O ASN A 300 7991 10147 7929 -454 540 142 O ATOM 2376 CB ASN A 300 -11.885 1.373 -62.839 1.00 85.30 C ANISOU 2376 CB ASN A 300 10401 11566 10441 -661 1222 108 C ATOM 2377 CG ASN A 300 -11.219 0.049 -63.158 1.00 96.60 C ANISOU 2377 CG ASN A 300 11882 12656 12166 -751 1662 176 C ATOM 2378 OD1 ASN A 300 -10.092 0.013 -63.654 1.00108.58 O ANISOU 2378 OD1 ASN A 300 13516 13974 13767 -770 1826 154 O ATOM 2379 ND2 ASN A 300 -11.915 -1.047 -62.875 1.00 87.26 N ANISOU 2379 ND2 ASN A 300 10609 11403 11143 -806 1855 261 N ATOM 2380 N MET A 301 -14.493 3.534 -63.505 1.00 72.20 N ANISOU 2380 N MET A 301 8883 10413 8136 -877 360 -303 N ATOM 2381 CA MET A 301 -15.232 4.727 -63.094 1.00 70.68 C ANISOU 2381 CA MET A 301 8618 10564 7673 -782 -62 -353 C ATOM 2382 C MET A 301 -14.463 5.604 -62.104 1.00 69.53 C ANISOU 2382 C MET A 301 8293 10660 7465 -464 -243 -196 C ATOM 2383 O MET A 301 -15.050 6.170 -61.183 1.00 63.51 O ANISOU 2383 O MET A 301 7345 10209 6577 -279 -501 -108 O ATOM 2384 CB MET A 301 -16.579 4.326 -62.489 1.00 76.35 C ANISOU 2384 CB MET A 301 9189 11450 8372 -777 -136 -292 C ATOM 2385 CG MET A 301 -17.441 3.456 -63.395 1.00 70.75 C ANISOU 2385 CG MET A 301 8638 10517 7724 -1082 24 -439 C ATOM 2386 SD MET A 301 -18.123 4.350 -64.805 1.00 77.27 S ANISOU 2386 SD MET A 301 9764 11316 8281 -1384 -245 -791 S ATOM 2387 CE MET A 301 -19.156 5.558 -63.981 1.00 61.21 C ANISOU 2387 CE MET A 301 7568 9727 5962 -1226 -718 -785 C ATOM 2388 N GLY A 302 -13.153 5.718 -62.303 1.00 69.67 N ANISOU 2388 N GLY A 302 8368 10532 7570 -401 -112 -163 N ATOM 2389 CA GLY A 302 -12.329 6.593 -61.490 1.00 61.81 C ANISOU 2389 CA GLY A 302 7231 9737 6518 -115 -285 -34 C ATOM 2390 C GLY A 302 -11.349 5.864 -60.590 1.00 64.72 C ANISOU 2390 C GLY A 302 7419 10036 7135 110 -6 229 C ATOM 2391 O GLY A 302 -10.150 6.138 -60.618 1.00 60.67 O ANISOU 2391 O GLY A 302 6931 9439 6682 211 60 278 O ATOM 2392 N PHE A 303 -11.866 4.946 -59.779 1.00 65.76 N ANISOU 2392 N PHE A 303 7366 10207 7412 193 152 403 N ATOM 2393 CA PHE A 303 -11.052 4.167 -58.848 1.00 62.65 C ANISOU 2393 CA PHE A 303 6782 9760 7264 408 424 666 C ATOM 2394 C PHE A 303 -10.034 3.293 -59.583 1.00 63.39 C ANISOU 2394 C PHE A 303 7023 9476 7586 274 809 657 C ATOM 2395 O PHE A 303 -10.380 2.612 -60.542 1.00 58.86 O ANISOU 2395 O PHE A 303 6628 8663 7074 4 988 515 O ATOM 2396 CB PHE A 303 -11.972 3.313 -57.971 1.00 56.30 C ANISOU 2396 CB PHE A 303 5770 9062 6562 479 515 829 C ATOM 2397 CG PHE A 303 -11.257 2.467 -56.963 1.00 54.45 C ANISOU 2397 CG PHE A 303 5324 8787 6579 698 791 1106 C ATOM 2398 CD1 PHE A 303 -10.667 3.038 -55.850 1.00 54.10 C ANISOU 2398 CD1 PHE A 303 5074 8968 6515 1019 663 1292 C ATOM 2399 CD2 PHE A 303 -11.210 1.093 -57.108 1.00 57.79 C ANISOU 2399 CD2 PHE A 303 5748 8952 7260 587 1172 1182 C ATOM 2400 CE1 PHE A 303 -10.023 2.255 -54.912 1.00 49.45 C ANISOU 2400 CE1 PHE A 303 4289 8344 6157 1221 916 1548 C ATOM 2401 CE2 PHE A 303 -10.569 0.307 -56.173 1.00 61.81 C ANISOU 2401 CE2 PHE A 303 6058 9424 8001 786 1425 1438 C ATOM 2402 CZ PHE A 303 -9.977 0.890 -55.073 1.00 53.61 C ANISOU 2402 CZ PHE A 303 4818 8613 6939 1104 1298 1621 C ATOM 2403 N TRP A 304 -8.780 3.309 -59.137 1.00 64.18 N ANISOU 2403 N TRP A 304 7051 9523 7812 462 935 805 N ATOM 2404 CA TRP A 304 -7.753 2.480 -59.765 1.00 62.84 C ANISOU 2404 CA TRP A 304 7009 9003 7866 355 1305 812 C ATOM 2405 C TRP A 304 -8.022 1.003 -59.484 1.00 66.91 C ANISOU 2405 C TRP A 304 7436 9349 8636 306 1660 944 C ATOM 2406 O TRP A 304 -8.364 0.629 -58.362 1.00 66.76 O ANISOU 2406 O TRP A 304 7177 9495 8696 496 1678 1147 O ATOM 2407 CB TRP A 304 -6.355 2.885 -59.286 1.00 59.79 C ANISOU 2407 CB TRP A 304 6552 8615 7551 584 1342 952 C ATOM 2408 CG TRP A 304 -5.883 4.209 -59.841 1.00 59.87 C ANISOU 2408 CG TRP A 304 6701 8699 7349 581 1058 799 C ATOM 2409 CD1 TRP A 304 -6.350 4.849 -60.955 1.00 58.60 C ANISOU 2409 CD1 TRP A 304 6765 8509 6991 349 873 539 C ATOM 2410 CD2 TRP A 304 -4.861 5.053 -59.294 1.00 57.16 C ANISOU 2410 CD2 TRP A 304 6273 8473 6974 825 923 902 C ATOM 2411 NE1 TRP A 304 -5.679 6.037 -61.136 1.00 57.22 N ANISOU 2411 NE1 TRP A 304 6648 8427 6665 432 633 476 N ATOM 2412 CE2 TRP A 304 -4.761 6.185 -60.128 1.00 55.48 C ANISOU 2412 CE2 TRP A 304 6241 8296 6543 724 657 696 C ATOM 2413 CE3 TRP A 304 -4.023 4.961 -58.179 1.00 57.44 C ANISOU 2413 CE3 TRP A 304 6097 8583 7145 1119 1000 1149 C ATOM 2414 CZ2 TRP A 304 -3.854 7.215 -59.882 1.00 52.89 C ANISOU 2414 CZ2 TRP A 304 5885 8074 6135 907 464 732 C ATOM 2415 CZ3 TRP A 304 -3.125 5.983 -57.937 1.00 46.57 C ANISOU 2415 CZ3 TRP A 304 4698 7310 5687 1301 809 1181 C ATOM 2416 CH2 TRP A 304 -3.048 7.094 -58.783 1.00 46.23 C ANISOU 2416 CH2 TRP A 304 4834 7299 5432 1195 543 975 C ATOM 2417 N TRP A 305 -7.849 0.169 -60.505 1.00 70.48 N ANISOU 2417 N TRP A 305 8083 9474 9223 56 1941 830 N ATOM 2418 CA TRP A 305 -8.215 -1.243 -60.430 1.00 76.65 C ANISOU 2418 CA TRP A 305 8814 10070 10238 -39 2268 915 C ATOM 2419 C TRP A 305 -7.435 -1.973 -59.341 1.00 74.64 C ANISOU 2419 C TRP A 305 8333 9797 10229 200 2516 1201 C ATOM 2420 O TRP A 305 -7.999 -2.632 -58.465 1.00 78.13 O ANISOU 2420 O TRP A 305 8571 10336 10778 303 2591 1370 O ATOM 2421 CB TRP A 305 -7.966 -1.907 -61.789 1.00 75.49 C ANISOU 2421 CB TRP A 305 8936 9559 10188 -340 2521 731 C ATOM 2422 CG TRP A 305 -8.415 -3.331 -61.892 1.00 83.85 C ANISOU 2422 CG TRP A 305 9977 10406 11475 -476 2840 779 C ATOM 2423 CD1 TRP A 305 -9.639 -3.777 -62.298 1.00 81.34 C ANISOU 2423 CD1 TRP A 305 9714 10066 11127 -674 2819 668 C ATOM 2424 CD2 TRP A 305 -7.636 -4.498 -61.610 1.00 84.59 C ANISOU 2424 CD2 TRP A 305 9999 10272 11869 -430 3227 948 C ATOM 2425 NE1 TRP A 305 -9.675 -5.150 -62.274 1.00 85.78 N ANISOU 2425 NE1 TRP A 305 10238 10402 11954 -750 3165 760 N ATOM 2426 CE2 TRP A 305 -8.457 -5.617 -61.856 1.00 86.89 C ANISOU 2426 CE2 TRP A 305 10300 10414 12300 -604 3421 931 C ATOM 2427 CE3 TRP A 305 -6.326 -4.707 -61.169 1.00 85.24 C ANISOU 2427 CE3 TRP A 305 10007 10261 12119 -258 3427 1113 C ATOM 2428 CZ2 TRP A 305 -8.011 -6.923 -61.675 1.00 90.57 C ANISOU 2428 CZ2 TRP A 305 10702 10644 13065 -611 3802 1072 C ATOM 2429 CZ3 TRP A 305 -5.886 -6.003 -60.989 1.00 88.11 C ANISOU 2429 CZ3 TRP A 305 10309 10392 12776 -266 3808 1252 C ATOM 2430 CH2 TRP A 305 -6.726 -7.094 -61.241 1.00 90.49 C ANISOU 2430 CH2 TRP A 305 10620 10551 13210 -442 3991 1230 C ATOM 2431 N ILE A 306 -6.130 -1.766 -59.373 1.00 46.05 N ANISOU 2431 N ILE A 306 4915 6124 6459 451 492 -146 N ATOM 2432 CA ILE A 306 -5.150 -2.489 -58.584 1.00 43.42 C ANISOU 2432 CA ILE A 306 4591 5730 6176 491 470 -187 C ATOM 2433 C ILE A 306 -5.369 -2.241 -57.098 1.00 48.70 C ANISOU 2433 C ILE A 306 5287 6299 6918 455 498 -220 C ATOM 2434 O ILE A 306 -4.972 -3.041 -56.244 1.00 44.10 O ANISOU 2434 O ILE A 306 4725 5653 6377 472 481 -278 O ATOM 2435 CB ILE A 306 -3.717 -2.068 -58.985 1.00 56.13 C ANISOU 2435 CB ILE A 306 6174 7380 7771 532 430 -176 C ATOM 2436 CG1 ILE A 306 -3.589 -1.950 -60.514 1.00 62.75 C ANISOU 2436 CG1 ILE A 306 6983 8338 8522 559 405 -144 C ATOM 2437 CG2 ILE A 306 -2.699 -3.057 -58.437 1.00 59.86 C ANISOU 2437 CG2 ILE A 306 6663 7801 8282 577 396 -215 C ATOM 2438 CD1 ILE A 306 -4.121 -0.646 -61.142 1.00 57.00 C ANISOU 2438 CD1 ILE A 306 6219 7634 7803 504 429 -125 C ATOM 2439 N LEU A 307 -6.032 -1.129 -56.802 1.00 45.45 N ANISOU 2439 N LEU A 307 4877 5877 6516 404 537 -191 N ATOM 2440 CA LEU A 307 -6.257 -0.703 -55.431 1.00 44.90 C ANISOU 2440 CA LEU A 307 4830 5721 6508 368 571 -218 C ATOM 2441 C LEU A 307 -7.403 -1.466 -54.770 1.00 42.12 C ANISOU 2441 C LEU A 307 4518 5322 6165 346 604 -238 C ATOM 2442 O LEU A 307 -7.707 -1.222 -53.603 1.00 38.19 O ANISOU 2442 O LEU A 307 4045 4758 5708 319 634 -264 O ATOM 2443 CB LEU A 307 -6.536 0.798 -55.379 1.00 37.64 C ANISOU 2443 CB LEU A 307 3903 4805 5595 326 598 -177 C ATOM 2444 CG LEU A 307 -5.361 1.723 -55.697 1.00 41.09 C ANISOU 2444 CG LEU A 307 4304 5269 6039 343 567 -164 C ATOM 2445 CD1 LEU A 307 -5.794 3.177 -55.633 1.00 46.86 C ANISOU 2445 CD1 LEU A 307 5032 5996 6778 300 593 -130 C ATOM 2446 CD2 LEU A 307 -4.215 1.464 -54.739 1.00 40.49 C ANISOU 2446 CD2 LEU A 307 4226 5134 6025 366 547 -214 C ATOM 2447 N ARG A 308 -8.059 -2.354 -55.519 1.00 44.00 N ANISOU 2447 N ARG A 308 4762 5596 6359 359 599 -224 N ATOM 2448 CA ARG A 308 -9.100 -3.198 -54.932 1.00 43.66 C ANISOU 2448 CA ARG A 308 4758 5510 6321 346 624 -239 C ATOM 2449 C ARG A 308 -8.589 -3.948 -53.710 1.00 41.91 C ANISOU 2449 C ARG A 308 4562 5214 6149 367 599 -322 C ATOM 2450 O ARG A 308 -9.228 -3.982 -52.656 1.00 42.10 O ANISOU 2450 O ARG A 308 4649 5187 6160 330 604 -328 O ATOM 2451 CB ARG A 308 -9.594 -4.237 -55.942 1.00 44.95 C ANISOU 2451 CB ARG A 308 4920 5719 6439 370 608 -225 C ATOM 2452 CG ARG A 308 -10.515 -3.742 -57.025 1.00 46.95 C ANISOU 2452 CG ARG A 308 5165 6039 6634 338 631 -151 C ATOM 2453 CD ARG A 308 -10.347 -4.639 -58.242 1.00 45.45 C ANISOU 2453 CD ARG A 308 4953 5914 6402 379 595 -154 C ATOM 2454 NE ARG A 308 -11.515 -4.648 -59.113 1.00 48.94 N ANISOU 2454 NE ARG A 308 5401 6403 6791 344 615 -102 N ATOM 2455 CZ ARG A 308 -11.882 -3.634 -59.886 1.00 50.47 C ANISOU 2455 CZ ARG A 308 5583 6653 6941 303 618 -62 C ATOM 2456 NH1 ARG A 308 -11.182 -2.508 -59.895 1.00 61.60 N ANISOU 2456 NH1 ARG A 308 6971 8080 8353 296 606 -62 N ATOM 2457 NH2 ARG A 308 -12.959 -3.742 -60.645 1.00 57.08 N ANISOU 2457 NH2 ARG A 308 6434 7523 7732 266 627 -27 N ATOM 2458 N PHE A 309 -7.437 -4.573 -53.885 1.00 41.37 N ANISOU 2458 N PHE A 309 4480 5149 6089 413 538 -372 N ATOM 2459 CA PHE A 309 -6.896 -5.519 -52.919 1.00 38.82 C ANISOU 2459 CA PHE A 309 4242 4778 5729 409 448 -425 C ATOM 2460 C PHE A 309 -6.594 -4.982 -51.512 1.00 38.04 C ANISOU 2460 C PHE A 309 4185 4621 5648 370 442 -452 C ATOM 2461 O PHE A 309 -6.930 -5.651 -50.532 1.00 38.70 O ANISOU 2461 O PHE A 309 4347 4666 5689 341 395 -472 O ATOM 2462 CB PHE A 309 -5.679 -6.184 -53.544 1.00 46.27 C ANISOU 2462 CB PHE A 309 5161 5747 6672 464 388 -457 C ATOM 2463 CG PHE A 309 -6.014 -6.916 -54.812 1.00 43.18 C ANISOU 2463 CG PHE A 309 4745 5411 6251 503 380 -442 C ATOM 2464 CD1 PHE A 309 -6.757 -8.085 -54.767 1.00 44.88 C ANISOU 2464 CD1 PHE A 309 5031 5615 6405 493 332 -448 C ATOM 2465 CD2 PHE A 309 -5.644 -6.409 -56.047 1.00 52.57 C ANISOU 2465 CD2 PHE A 309 5862 6669 7442 535 408 -401 C ATOM 2466 CE1 PHE A 309 -7.098 -8.754 -55.925 1.00 45.28 C ANISOU 2466 CE1 PHE A 309 5063 5714 6427 526 324 -437 C ATOM 2467 CE2 PHE A 309 -5.981 -7.076 -57.212 1.00 54.98 C ANISOU 2467 CE2 PHE A 309 6158 7032 7701 562 397 -380 C ATOM 2468 CZ PHE A 309 -6.709 -8.250 -57.150 1.00 55.67 C ANISOU 2468 CZ PHE A 309 6283 7097 7771 570 367 -418 C ATOM 2469 N PRO A 310 -5.921 -3.820 -51.386 1.00 34.24 N ANISOU 2469 N PRO A 310 3647 4135 5229 371 483 -453 N ATOM 2470 CA PRO A 310 -5.865 -3.326 -50.005 1.00 30.21 C ANISOU 2470 CA PRO A 310 3185 3567 4727 327 481 -478 C ATOM 2471 C PRO A 310 -7.249 -3.102 -49.397 1.00 31.64 C ANISOU 2471 C PRO A 310 3412 3727 4882 282 524 -453 C ATOM 2472 O PRO A 310 -7.467 -3.434 -48.228 1.00 31.24 O ANISOU 2472 O PRO A 310 3434 3637 4798 250 488 -477 O ATOM 2473 CB PRO A 310 -5.104 -1.998 -50.128 1.00 27.96 C ANISOU 2473 CB PRO A 310 2822 3281 4519 336 528 -473 C ATOM 2474 CG PRO A 310 -5.202 -1.620 -51.567 1.00 32.98 C ANISOU 2474 CG PRO A 310 3388 3985 5157 362 558 -414 C ATOM 2475 CD PRO A 310 -5.226 -2.919 -52.320 1.00 40.71 C ANISOU 2475 CD PRO A 310 4373 4997 6098 402 517 -424 C ATOM 2476 N VAL A 311 -8.195 -2.623 -50.203 1.00 31.02 N ANISOU 2476 N VAL A 311 3293 3680 4815 280 597 -399 N ATOM 2477 CA VAL A 311 -9.547 -2.407 -49.706 1.00 29.73 C ANISOU 2477 CA VAL A 311 3174 3499 4624 239 643 -360 C ATOM 2478 C VAL A 311 -10.146 -3.749 -49.331 1.00 33.84 C ANISOU 2478 C VAL A 311 3779 4010 5067 234 571 -361 C ATOM 2479 O VAL A 311 -10.787 -3.888 -48.279 1.00 30.48 O ANISOU 2479 O VAL A 311 3421 3552 4608 203 556 -359 O ATOM 2480 CB VAL A 311 -10.450 -1.715 -50.743 1.00 32.31 C ANISOU 2480 CB VAL A 311 3435 3866 4975 235 738 -290 C ATOM 2481 CG1 VAL A 311 -11.876 -1.636 -50.225 1.00 31.36 C ANISOU 2481 CG1 VAL A 311 3373 3727 4816 194 780 -240 C ATOM 2482 CG2 VAL A 311 -9.924 -0.333 -51.076 1.00 29.62 C ANISOU 2482 CG2 VAL A 311 3048 3543 4664 220 759 -265 C ATOM 2483 N PHE A 312 -9.872 -4.750 -50.167 1.00 30.88 N ANISOU 2483 N PHE A 312 3399 3666 4667 267 520 -367 N ATOM 2484 CA PHE A 312 -10.335 -6.101 -49.900 1.00 33.54 C ANISOU 2484 CA PHE A 312 3809 3996 4940 266 442 -370 C ATOM 2485 C PHE A 312 -9.808 -6.526 -48.548 1.00 30.59 C ANISOU 2485 C PHE A 312 3491 3580 4552 250 372 -421 C ATOM 2486 O PHE A 312 -10.560 -7.052 -47.719 1.00 31.82 O ANISOU 2486 O PHE A 312 3708 3715 4667 226 336 -408 O ATOM 2487 CB PHE A 312 -9.859 -7.084 -50.970 1.00 35.54 C ANISOU 2487 CB PHE A 312 4043 4284 5177 309 392 -384 C ATOM 2488 CG PHE A 312 -10.603 -6.984 -52.269 1.00 39.35 C ANISOU 2488 CG PHE A 312 4482 4815 5655 322 446 -331 C ATOM 2489 CD1 PHE A 312 -11.851 -6.387 -52.333 1.00 30.33 C ANISOU 2489 CD1 PHE A 312 3341 3677 4505 288 520 -263 C ATOM 2490 CD2 PHE A 312 -10.053 -7.499 -53.430 1.00 41.75 C ANISOU 2490 CD2 PHE A 312 4742 5162 5958 367 425 -344 C ATOM 2491 CE1 PHE A 312 -12.531 -6.302 -53.539 1.00 34.98 C ANISOU 2491 CE1 PHE A 312 3885 4315 5089 294 574 -207 C ATOM 2492 CE2 PHE A 312 -10.727 -7.417 -54.633 1.00 37.01 C ANISOU 2492 CE2 PHE A 312 4096 4614 5351 376 475 -295 C ATOM 2493 CZ PHE A 312 -11.965 -6.820 -54.688 1.00 30.58 C ANISOU 2493 CZ PHE A 312 3280 3805 4532 337 551 -225 C ATOM 2494 N LEU A 313 -8.533 -6.223 -48.306 1.00 29.63 N ANISOU 2494 N LEU A 313 3343 3448 4468 260 356 -470 N ATOM 2495 CA LEU A 313 -7.907 -6.627 -47.062 1.00 36.05 C ANISOU 2495 CA LEU A 313 4200 4227 5271 240 292 -517 C ATOM 2496 C LEU A 313 -8.665 -5.967 -45.928 1.00 30.37 C ANISOU 2496 C LEU A 313 3516 3480 4545 199 323 -506 C ATOM 2497 O LEU A 313 -9.072 -6.637 -44.970 1.00 29.75 O ANISOU 2497 O LEU A 313 3491 3387 4428 178 271 -512 O ATOM 2498 CB LEU A 313 -6.424 -6.243 -47.034 1.00 30.91 C ANISOU 2498 CB LEU A 313 3512 3569 4663 255 281 -559 C ATOM 2499 CG LEU A 313 -5.626 -6.687 -45.807 1.00 33.69 C ANISOU 2499 CG LEU A 313 3903 3890 5007 230 217 -605 C ATOM 2500 CD1 LEU A 313 -5.780 -8.185 -45.580 1.00 33.15 C ANISOU 2500 CD1 LEU A 313 3878 3826 4893 232 134 -615 C ATOM 2501 CD2 LEU A 313 -4.158 -6.315 -45.955 1.00 29.41 C ANISOU 2501 CD2 LEU A 313 3323 3345 4506 247 209 -630 C ATOM 2502 N ALA A 314 -8.929 -4.671 -46.088 1.00 24.11 N ANISOU 2502 N ALA A 314 2687 2683 3790 189 410 -485 N ATOM 2503 CA ALA A 314 -9.602 -3.913 -45.045 1.00 27.28 C ANISOU 2503 CA ALA A 314 3119 3057 4189 153 449 -478 C ATOM 2504 C ALA A 314 -10.993 -4.467 -44.824 1.00 26.85 C ANISOU 2504 C ALA A 314 3117 3008 4078 141 443 -426 C ATOM 2505 O ALA A 314 -11.486 -4.506 -43.696 1.00 27.18 O ANISOU 2505 O ALA A 314 3206 3030 4090 117 425 -427 O ATOM 2506 CB ALA A 314 -9.672 -2.443 -45.404 1.00 20.53 C ANISOU 2506 CB ALA A 314 2210 2198 3392 147 547 -460 C ATOM 2507 N ILE A 315 -11.620 -4.920 -45.901 1.00 23.59 N ANISOU 2507 N ILE A 315 2693 2623 3647 158 455 -378 N ATOM 2508 CA ILE A 315 -12.954 -5.473 -45.768 1.00 27.21 C ANISOU 2508 CA ILE A 315 3202 3086 4051 148 445 -316 C ATOM 2509 C ILE A 315 -12.869 -6.827 -45.078 1.00 31.01 C ANISOU 2509 C ILE A 315 3733 3561 4487 152 334 -338 C ATOM 2510 O ILE A 315 -13.666 -7.125 -44.181 1.00 35.36 O ANISOU 2510 O ILE A 315 4332 4103 4999 137 305 -310 O ATOM 2511 CB ILE A 315 -13.648 -5.585 -47.136 1.00 32.20 C ANISOU 2511 CB ILE A 315 3807 3752 4676 161 489 -254 C ATOM 2512 CG1 ILE A 315 -14.091 -4.193 -47.590 1.00 24.26 C ANISOU 2512 CG1 ILE A 315 2752 2753 3713 145 608 -210 C ATOM 2513 CG2 ILE A 315 -14.844 -6.522 -47.070 1.00 31.00 C ANISOU 2513 CG2 ILE A 315 3714 3604 4461 156 447 -191 C ATOM 2514 CD1 ILE A 315 -14.592 -4.136 -49.014 1.00 33.64 C ANISOU 2514 CD1 ILE A 315 3891 3984 4907 154 665 -151 C ATOM 2515 N LEU A 316 -11.858 -7.612 -45.449 1.00 31.80 N ANISOU 2515 N LEU A 316 3817 3669 4597 174 271 -387 N ATOM 2516 CA LEU A 316 -11.739 -8.970 -44.935 1.00 34.35 C ANISOU 2516 CA LEU A 316 4175 3989 4886 179 165 -406 C ATOM 2517 C LEU A 316 -11.592 -8.933 -43.424 1.00 32.97 C ANISOU 2517 C LEU A 316 4028 3796 4705 152 130 -433 C ATOM 2518 O LEU A 316 -12.335 -9.601 -42.697 1.00 30.67 O ANISOU 2518 O LEU A 316 3772 3504 4375 143 76 -404 O ATOM 2519 CB LEU A 316 -10.548 -9.686 -45.573 1.00 34.21 C ANISOU 2519 CB LEU A 316 4131 3980 4886 207 115 -457 C ATOM 2520 CG LEU A 316 -10.236 -11.109 -45.108 1.00 35.76 C ANISOU 2520 CG LEU A 316 4353 4174 5062 211 8 -482 C ATOM 2521 CD1 LEU A 316 -11.451 -12.017 -45.257 1.00 36.09 C ANISOU 2521 CD1 LEU A 316 4430 4222 5060 216 -39 -428 C ATOM 2522 CD2 LEU A 316 -9.055 -11.654 -45.892 1.00 36.51 C ANISOU 2522 CD2 LEU A 316 4419 4277 5177 242 -23 -527 C ATOM 2523 N ILE A 317 -10.669 -8.096 -42.959 1.00 27.42 N ANISOU 2523 N ILE A 317 3302 3078 4038 139 161 -482 N ATOM 2524 CA ILE A 317 -10.432 -7.950 -41.537 1.00 26.90 C ANISOU 2524 CA ILE A 317 3256 2998 3968 110 135 -513 C ATOM 2525 C ILE A 317 -11.704 -7.455 -40.875 1.00 28.80 C ANISOU 2525 C ILE A 317 3529 3235 4178 95 169 -465 C ATOM 2526 O ILE A 317 -12.089 -7.947 -39.802 1.00 29.68 O ANISOU 2526 O ILE A 317 3668 3352 4259 82 115 -460 O ATOM 2527 CB ILE A 317 -9.266 -6.982 -41.263 1.00 30.77 C ANISOU 2527 CB ILE A 317 3717 3469 4504 98 173 -568 C ATOM 2528 CG1 ILE A 317 -8.010 -7.467 -41.987 1.00 34.44 C ANISOU 2528 CG1 ILE A 317 4151 3940 4996 119 140 -602 C ATOM 2529 CG2 ILE A 317 -9.018 -6.846 -39.773 1.00 30.80 C ANISOU 2529 CG2 ILE A 317 3742 3462 4500 64 145 -603 C ATOM 2530 CD1 ILE A 317 -6.817 -6.560 -41.847 1.00 24.62 C ANISOU 2530 CD1 ILE A 317 2877 2680 3798 111 171 -642 C ATOM 2531 N ASN A 318 -12.410 -6.557 -41.563 1.00 31.64 N ANISOU 2531 N ASN A 318 3882 3593 4546 98 256 -421 N ATOM 2532 CA ASN A 318 -13.615 -5.979 -40.991 1.00 27.57 C ANISOU 2532 CA ASN A 318 3399 3073 4004 84 300 -367 C ATOM 2533 C ASN A 318 -14.620 -7.077 -40.722 1.00 33.55 C ANISOU 2533 C ASN A 318 4196 3847 4704 92 232 -308 C ATOM 2534 O ASN A 318 -15.302 -7.060 -39.687 1.00 34.06 O ANISOU 2534 O ASN A 318 4294 3913 4736 82 214 -282 O ATOM 2535 CB ASN A 318 -14.224 -4.933 -41.921 1.00 27.94 C ANISOU 2535 CB ASN A 318 3424 3118 4072 84 409 -318 C ATOM 2536 CG ASN A 318 -14.027 -3.518 -41.424 1.00 36.75 C ANISOU 2536 CG ASN A 318 4524 4211 5228 65 489 -343 C ATOM 2537 OD1 ASN A 318 -14.156 -3.237 -40.232 1.00 36.53 O ANISOU 2537 OD1 ASN A 318 4526 4169 5184 50 479 -363 O ATOM 2538 ND2 ASN A 318 -13.715 -2.611 -42.345 1.00 32.86 N ANISOU 2538 ND2 ASN A 318 3978 3717 4789 68 567 -342 N ATOM 2539 N PHE A 319 -14.646 -8.077 -41.604 1.00 32.55 N ANISOU 2539 N PHE A 319 4067 3735 4568 111 184 -290 N ATOM 2540 CA PHE A 319 -15.601 -9.160 -41.438 1.00 30.80 C ANISOU 2540 CA PHE A 319 3880 3526 4297 121 111 -228 C ATOM 2541 C PHE A 319 -15.373 -9.811 -40.089 1.00 29.83 C ANISOU 2541 C PHE A 319 3768 3408 4159 113 23 -256 C ATOM 2542 O PHE A 319 -16.305 -9.938 -39.286 1.00 30.79 O ANISOU 2542 O PHE A 319 3917 3537 4243 112 -1 -202 O ATOM 2543 CB PHE A 319 -15.483 -10.210 -42.546 1.00 25.75 C ANISOU 2543 CB PHE A 319 3232 2898 3655 143 61 -221 C ATOM 2544 CG PHE A 319 -16.243 -11.479 -42.252 1.00 32.38 C ANISOU 2544 CG PHE A 319 4103 3747 4454 153 -38 -171 C ATOM 2545 CD1 PHE A 319 -17.597 -11.569 -42.531 1.00 32.10 C ANISOU 2545 CD1 PHE A 319 4102 3718 4378 157 -28 -72 C ATOM 2546 CD2 PHE A 319 -15.612 -12.570 -41.675 1.00 27.99 C ANISOU 2546 CD2 PHE A 319 3538 3194 3903 159 -142 -214 C ATOM 2547 CE1 PHE A 319 -18.305 -12.718 -42.251 1.00 32.11 C ANISOU 2547 CE1 PHE A 319 4129 3726 4345 169 -126 -17 C ATOM 2548 CE2 PHE A 319 -16.319 -13.723 -41.390 1.00 34.77 C ANISOU 2548 CE2 PHE A 319 4415 4062 4733 170 -238 -164 C ATOM 2549 CZ PHE A 319 -17.669 -13.795 -41.680 1.00 23.70 C ANISOU 2549 CZ PHE A 319 3048 2665 3291 177 -233 -65 C ATOM 2550 N PHE A 320 -14.122 -10.166 -39.813 1.00 27.42 N ANISOU 2550 N PHE A 320 3435 3100 3884 109 -20 -335 N ATOM 2551 CA PHE A 320 -13.843 -10.901 -38.591 1.00 28.39 C ANISOU 2551 CA PHE A 320 3555 3235 3997 98 -106 -359 C ATOM 2552 C PHE A 320 -14.109 -10.018 -37.391 1.00 29.29 C ANISOU 2552 C PHE A 320 3680 3350 4100 78 -72 -363 C ATOM 2553 O PHE A 320 -14.471 -10.508 -36.321 1.00 28.60 O ANISOU 2553 O PHE A 320 3595 3284 3987 73 -134 -347 O ATOM 2554 CB PHE A 320 -12.410 -11.424 -38.574 1.00 24.72 C ANISOU 2554 CB PHE A 320 3056 2768 3567 91 -150 -436 C ATOM 2555 CG PHE A 320 -12.144 -12.483 -39.601 1.00 27.09 C ANISOU 2555 CG PHE A 320 3347 3071 3875 115 -200 -436 C ATOM 2556 CD1 PHE A 320 -12.588 -13.779 -39.407 1.00 31.82 C ANISOU 2556 CD1 PHE A 320 3950 3685 4457 125 -296 -406 C ATOM 2557 CD2 PHE A 320 -11.459 -12.185 -40.766 1.00 29.15 C ANISOU 2557 CD2 PHE A 320 3593 3322 4162 130 -154 -463 C ATOM 2558 CE1 PHE A 320 -12.350 -14.757 -40.354 1.00 28.85 C ANISOU 2558 CE1 PHE A 320 3567 3307 4088 148 -343 -410 C ATOM 2559 CE2 PHE A 320 -11.217 -13.161 -41.714 1.00 27.30 C ANISOU 2559 CE2 PHE A 320 3351 3092 3930 156 -200 -466 C ATOM 2560 CZ PHE A 320 -11.664 -14.447 -41.507 1.00 27.50 C ANISOU 2560 CZ PHE A 320 3386 3126 3938 164 -294 -443 C ATOM 2561 N ILE A 321 -13.958 -8.709 -37.570 1.00 26.36 N ANISOU 2561 N ILE A 321 3309 2958 3748 68 25 -383 N ATOM 2562 CA ILE A 321 -14.238 -7.809 -36.467 1.00 30.76 C ANISOU 2562 CA ILE A 321 3879 3512 4294 50 62 -390 C ATOM 2563 C ILE A 321 -15.742 -7.789 -36.252 1.00 31.72 C ANISOU 2563 C ILE A 321 4038 3646 4368 63 71 -299 C ATOM 2564 O ILE A 321 -16.224 -7.935 -35.119 1.00 28.51 O ANISOU 2564 O ILE A 321 3645 3260 3929 62 32 -281 O ATOM 2565 CB ILE A 321 -13.695 -6.400 -36.735 1.00 38.59 C ANISOU 2565 CB ILE A 321 4859 4475 5327 37 162 -434 C ATOM 2566 CG1 ILE A 321 -12.166 -6.432 -36.700 1.00 36.37 C ANISOU 2566 CG1 ILE A 321 4546 4184 5090 24 141 -517 C ATOM 2567 CG2 ILE A 321 -14.221 -5.414 -35.707 1.00 32.23 C ANISOU 2567 CG2 ILE A 321 4076 3663 4508 23 209 -433 C ATOM 2568 CD1 ILE A 321 -11.514 -5.119 -37.045 1.00 40.23 C ANISOU 2568 CD1 ILE A 321 5014 4644 5627 15 225 -556 C ATOM 2569 N PHE A 322 -16.472 -7.705 -37.363 1.00 28.00 N ANISOU 2569 N PHE A 322 3579 3168 3890 77 115 -235 N ATOM 2570 CA PHE A 322 -17.924 -7.610 -37.330 1.00 29.65 C ANISOU 2570 CA PHE A 322 3827 3386 4053 87 136 -132 C ATOM 2571 C PHE A 322 -18.483 -8.764 -36.517 1.00 28.06 C ANISOU 2571 C PHE A 322 3640 3213 3809 102 25 -87 C ATOM 2572 O PHE A 322 -19.186 -8.555 -35.519 1.00 22.64 O ANISOU 2572 O PHE A 322 2974 2542 3087 106 16 -47 O ATOM 2573 CB PHE A 322 -18.487 -7.631 -38.757 1.00 27.93 C ANISOU 2573 CB PHE A 322 3614 3163 3836 96 183 -69 C ATOM 2574 CG PHE A 322 -19.993 -7.614 -38.831 1.00 34.87 C ANISOU 2574 CG PHE A 322 4535 4049 4665 103 204 52 C ATOM 2575 CD1 PHE A 322 -20.729 -8.794 -38.745 1.00 33.49 C ANISOU 2575 CD1 PHE A 322 4384 3894 4447 121 110 124 C ATOM 2576 CD2 PHE A 322 -20.670 -6.422 -39.021 1.00 29.91 C ANISOU 2576 CD2 PHE A 322 3920 3409 4037 92 317 101 C ATOM 2577 CE1 PHE A 322 -22.106 -8.778 -38.821 1.00 21.18 C ANISOU 2577 CE1 PHE A 322 2867 2341 2841 129 127 247 C ATOM 2578 CE2 PHE A 322 -22.048 -6.398 -39.102 1.00 30.19 C ANISOU 2578 CE2 PHE A 322 3996 3451 4024 96 342 223 C ATOM 2579 CZ PHE A 322 -22.768 -7.577 -39.001 1.00 33.76 C ANISOU 2579 CZ PHE A 322 4478 3923 4429 116 245 299 C ATOM 2580 N VAL A 323 -18.090 -9.973 -36.905 1.00 27.60 N ANISOU 2580 N VAL A 323 3564 3165 3758 112 -62 -98 N ATOM 2581 CA VAL A 323 -18.565 -11.178 -36.248 1.00 28.97 C ANISOU 2581 CA VAL A 323 3737 3367 3902 127 -177 -52 C ATOM 2582 C VAL A 323 -18.295 -11.084 -34.758 1.00 29.17 C ANISOU 2582 C VAL A 323 3746 3417 3922 118 -215 -87 C ATOM 2583 O VAL A 323 -19.220 -11.233 -33.945 1.00 29.46 O ANISOU 2583 O VAL A 323 3796 3480 3918 132 -251 -18 O ATOM 2584 CB VAL A 323 -17.885 -12.441 -36.808 1.00 29.04 C ANISOU 2584 CB VAL A 323 3719 3379 3936 134 -264 -85 C ATOM 2585 CG1 VAL A 323 -18.373 -13.686 -36.076 1.00 30.73 C ANISOU 2585 CG1 VAL A 323 3922 3625 4131 150 -388 -36 C ATOM 2586 CG2 VAL A 323 -18.137 -12.558 -38.294 1.00 27.83 C ANISOU 2586 CG2 VAL A 323 3581 3208 3785 145 -230 -55 C ATOM 2587 N ARG A 324 -17.062 -10.729 -34.399 1.00 25.03 N ANISOU 2587 N ARG A 324 3191 2885 3434 94 -198 -189 N ATOM 2588 CA ARG A 324 -16.702 -10.728 -32.989 1.00 30.85 C ANISOU 2588 CA ARG A 324 3904 3650 4167 80 -238 -228 C ATOM 2589 C ARG A 324 -17.559 -9.721 -32.237 1.00 29.71 C ANISOU 2589 C ARG A 324 3790 3512 3986 84 -182 -192 C ATOM 2590 O ARG A 324 -18.047 -10.006 -31.136 1.00 31.28 O ANISOU 2590 O ARG A 324 3981 3751 4154 94 -236 -161 O ATOM 2591 CB ARG A 324 -15.219 -10.406 -32.796 1.00 32.39 C ANISOU 2591 CB ARG A 324 4068 3832 4407 49 -219 -337 C ATOM 2592 CG ARG A 324 -14.742 -10.537 -31.349 1.00 38.08 C ANISOU 2592 CG ARG A 324 4756 4589 5125 28 -267 -380 C ATOM 2593 CD ARG A 324 -15.214 -11.841 -30.712 1.00 34.17 C ANISOU 2593 CD ARG A 324 4228 4144 4612 41 -382 -328 C ATOM 2594 NE ARG A 324 -14.622 -12.055 -29.394 1.00 38.91 N ANISOU 2594 NE ARG A 324 4781 4787 5218 16 -429 -372 N ATOM 2595 CZ ARG A 324 -14.866 -13.113 -28.626 1.00 39.33 C ANISOU 2595 CZ ARG A 324 4784 4894 5264 22 -529 -336 C ATOM 2596 NH1 ARG A 324 -15.695 -14.060 -29.043 1.00 39.39 N ANISOU 2596 NH1 ARG A 324 4790 4915 5262 55 -598 -255 N ATOM 2597 NH2 ARG A 324 -14.279 -13.227 -27.442 1.00 44.43 N ANISOU 2597 NH2 ARG A 324 5379 5585 5918 -6 -562 -377 N ATOM 2598 N ILE A 325 -17.814 -8.578 -32.870 1.00 26.69 N ANISOU 2598 N ILE A 325 3439 3093 3608 81 -73 -187 N ATOM 2599 CA ILE A 325 -18.566 -7.530 -32.200 1.00 29.13 C ANISOU 2599 CA ILE A 325 3779 3402 3888 84 -8 -158 C ATOM 2600 C ILE A 325 -19.953 -8.046 -31.890 1.00 30.21 C ANISOU 2600 C ILE A 325 3942 3569 3967 115 -53 -40 C ATOM 2601 O ILE A 325 -20.455 -7.871 -30.772 1.00 35.05 O ANISOU 2601 O ILE A 325 4561 4212 4543 126 -72 -17 O ATOM 2602 CB ILE A 325 -18.666 -6.256 -33.053 1.00 27.49 C ANISOU 2602 CB ILE A 325 3592 3150 3703 75 119 -162 C ATOM 2603 CG1 ILE A 325 -17.307 -5.569 -33.136 1.00 27.37 C ANISOU 2603 CG1 ILE A 325 3547 3107 3745 47 161 -274 C ATOM 2604 CG2 ILE A 325 -19.695 -5.302 -32.472 1.00 32.95 C ANISOU 2604 CG2 ILE A 325 4321 3840 4360 83 185 -108 C ATOM 2605 CD1 ILE A 325 -17.285 -4.391 -34.077 1.00 27.63 C ANISOU 2605 CD1 ILE A 325 3584 3100 3816 40 277 -278 C ATOM 2606 N VAL A 326 -20.533 -8.766 -32.847 1.00 25.97 N ANISOU 2606 N VAL A 326 3418 3029 3421 130 -79 35 N ATOM 2607 CA VAL A 326 -21.884 -9.253 -32.654 1.00 29.20 C ANISOU 2607 CA VAL A 326 3857 3462 3776 160 -123 163 C ATOM 2608 C VAL A 326 -21.876 -10.183 -31.458 1.00 30.15 C ANISOU 2608 C VAL A 326 3944 3635 3878 176 -244 169 C ATOM 2609 O VAL A 326 -22.739 -10.085 -30.576 1.00 31.87 O ANISOU 2609 O VAL A 326 4174 3885 4050 200 -266 239 O ATOM 2610 CB VAL A 326 -22.425 -9.991 -33.888 1.00 34.70 C ANISOU 2610 CB VAL A 326 4570 4147 4467 171 -145 240 C ATOM 2611 CG1 VAL A 326 -23.830 -10.514 -33.613 1.00 27.79 C ANISOU 2611 CG1 VAL A 326 3727 3298 3534 203 -199 383 C ATOM 2612 CG2 VAL A 326 -22.421 -9.077 -35.102 1.00 33.26 C ANISOU 2612 CG2 VAL A 326 4407 3924 4306 154 -23 237 C ATOM 2613 N GLN A 327 -20.837 -11.012 -31.380 1.00 31.42 N ANISOU 2613 N GLN A 327 4055 3806 4078 163 -316 93 N ATOM 2614 CA GLN A 327 -20.758 -11.996 -30.316 1.00 27.65 C ANISOU 2614 CA GLN A 327 3528 3382 3595 174 -434 100 C ATOM 2615 C GLN A 327 -20.657 -11.311 -28.973 1.00 28.89 C ANISOU 2615 C GLN A 327 3671 3573 3734 169 -418 65 C ATOM 2616 O GLN A 327 -21.226 -11.777 -27.986 1.00 34.18 O ANISOU 2616 O GLN A 327 4316 4298 4373 192 -493 120 O ATOM 2617 CB GLN A 327 -19.565 -12.920 -30.519 1.00 25.63 C ANISOU 2617 CB GLN A 327 3218 3128 3391 153 -498 20 C ATOM 2618 CG GLN A 327 -19.746 -13.925 -31.629 1.00 27.62 C ANISOU 2618 CG GLN A 327 3474 3362 3657 167 -550 63 C ATOM 2619 CD GLN A 327 -18.626 -14.940 -31.664 1.00 30.45 C ANISOU 2619 CD GLN A 327 3775 3728 4066 150 -625 -8 C ATOM 2620 OE1 GLN A 327 -17.458 -14.598 -31.490 1.00 29.92 O ANISOU 2620 OE1 GLN A 327 3684 3651 4032 120 -590 -107 O ATOM 2621 NE2 GLN A 327 -18.979 -16.200 -31.879 1.00 32.22 N ANISOU 2621 NE2 GLN A 327 3977 3969 4298 170 -728 46 N ATOM 2622 N LEU A 328 -19.967 -10.177 -28.941 1.00 27.92 N ANISOU 2622 N LEU A 328 3561 3418 3629 140 -321 -24 N ATOM 2623 CA LEU A 328 -19.838 -9.467 -27.685 1.00 29.86 C ANISOU 2623 CA LEU A 328 3797 3692 3857 134 -302 -67 C ATOM 2624 C LEU A 328 -21.182 -8.840 -27.351 1.00 33.64 C ANISOU 2624 C LEU A 328 4324 4180 4277 168 -264 28 C ATOM 2625 O LEU A 328 -21.642 -8.922 -26.206 1.00 33.13 O ANISOU 2625 O LEU A 328 4243 4171 4175 189 -310 58 O ATOM 2626 CB LEU A 328 -18.727 -8.416 -27.752 1.00 28.01 C ANISOU 2626 CB LEU A 328 3566 3416 3661 94 -213 -186 C ATOM 2627 CG LEU A 328 -17.318 -8.990 -27.951 1.00 37.07 C ANISOU 2627 CG LEU A 328 4666 4557 4862 60 -250 -276 C ATOM 2628 CD1 LEU A 328 -16.290 -7.885 -28.136 1.00 33.88 C ANISOU 2628 CD1 LEU A 328 4271 4106 4495 26 -161 -376 C ATOM 2629 CD2 LEU A 328 -16.921 -9.897 -26.793 1.00 33.42 C ANISOU 2629 CD2 LEU A 328 4140 4159 4398 51 -352 -294 C ATOM 2630 N LEU A 329 -21.848 -8.286 -28.367 1.00 29.45 N ANISOU 2630 N LEU A 329 3848 3604 3739 175 -184 85 N ATOM 2631 CA LEU A 329 -23.082 -7.541 -28.125 1.00 38.06 C ANISOU 2631 CA LEU A 329 4989 4695 4776 202 -127 177 C ATOM 2632 C LEU A 329 -24.130 -8.432 -27.485 1.00 33.44 C ANISOU 2632 C LEU A 329 4399 4168 4137 246 -228 298 C ATOM 2633 O LEU A 329 -24.610 -8.147 -26.383 1.00 37.21 O ANISOU 2633 O LEU A 329 4876 4689 4573 270 -243 325 O ATOM 2634 CB LEU A 329 -23.638 -6.951 -29.421 1.00 34.48 C ANISOU 2634 CB LEU A 329 4585 4187 4327 197 -28 234 C ATOM 2635 CG LEU A 329 -22.934 -5.731 -30.006 1.00 38.97 C ANISOU 2635 CG LEU A 329 5162 4700 4944 163 95 144 C ATOM 2636 CD1 LEU A 329 -23.751 -5.160 -31.147 1.00 36.04 C ANISOU 2636 CD1 LEU A 329 4832 4292 4570 162 191 229 C ATOM 2637 CD2 LEU A 329 -22.704 -4.684 -28.935 1.00 38.55 C ANISOU 2637 CD2 LEU A 329 5113 4648 4886 156 145 77 C ATOM 2638 N VAL A 330 -24.418 -9.551 -28.143 1.00 30.93 N ANISOU 2638 N VAL A 330 4072 3857 3824 259 -306 367 N ATOM 2639 CA VAL A 330 -25.434 -10.470 -27.658 1.00 37.40 C ANISOU 2639 CA VAL A 330 4883 4729 4599 303 -413 495 C ATOM 2640 C VAL A 330 -25.024 -10.998 -26.295 1.00 37.68 C ANISOU 2640 C VAL A 330 4849 4835 4634 314 -509 457 C ATOM 2641 O VAL A 330 -25.880 -11.320 -25.475 1.00 39.38 O ANISOU 2641 O VAL A 330 5051 5107 4804 356 -576 553 O ATOM 2642 CB VAL A 330 -25.676 -11.648 -28.630 1.00 32.92 C ANISOU 2642 CB VAL A 330 4311 4151 4046 310 -489 563 C ATOM 2643 CG1 VAL A 330 -26.066 -11.132 -30.005 1.00 37.58 C ANISOU 2643 CG1 VAL A 330 4964 4679 4637 296 -391 601 C ATOM 2644 CG2 VAL A 330 -24.448 -12.532 -28.726 1.00 37.60 C ANISOU 2644 CG2 VAL A 330 4839 4748 4699 285 -560 458 C ATOM 2645 N ALA A 331 -23.717 -11.063 -26.042 1.00 40.29 N ANISOU 2645 N ALA A 331 5128 5165 5014 275 -514 322 N ATOM 2646 CA ALA A 331 -23.264 -11.516 -24.741 1.00 33.91 C ANISOU 2646 CA ALA A 331 4245 4429 4209 277 -596 282 C ATOM 2647 C ALA A 331 -23.662 -10.484 -23.702 1.00 39.07 C ANISOU 2647 C ALA A 331 4918 5112 4816 292 -544 277 C ATOM 2648 O ALA A 331 -24.352 -10.806 -22.733 1.00 39.18 O ANISOU 2648 O ALA A 331 4902 5197 4788 332 -613 351 O ATOM 2649 CB ALA A 331 -21.770 -11.739 -24.736 1.00 37.11 C ANISOU 2649 CB ALA A 331 4600 4825 4676 226 -601 146 C ATOM 2650 N LYS A 332 -23.285 -9.230 -23.952 1.00 39.32 N ANISOU 2650 N LYS A 332 6726 4634 3580 783 1169 -618 N ATOM 2651 CA LYS A 332 -23.511 -8.165 -22.981 1.00 46.96 C ANISOU 2651 CA LYS A 332 8035 5281 4525 924 1211 -564 C ATOM 2652 C LYS A 332 -24.998 -7.937 -22.754 1.00 50.31 C ANISOU 2652 C LYS A 332 8478 5563 5075 939 1475 -500 C ATOM 2653 O LYS A 332 -25.427 -7.641 -21.640 1.00 60.35 O ANISOU 2653 O LYS A 332 10013 6576 6340 1021 1549 -447 O ATOM 2654 CB LYS A 332 -22.843 -6.869 -23.450 1.00 53.26 C ANISOU 2654 CB LYS A 332 8902 6092 5243 980 1069 -564 C ATOM 2655 CG LYS A 332 -21.336 -6.975 -23.620 1.00 53.66 C ANISOU 2655 CG LYS A 332 8950 6267 5170 962 755 -609 C ATOM 2656 CD LYS A 332 -20.620 -6.933 -22.282 1.00 64.14 C ANISOU 2656 CD LYS A 332 10582 7346 6443 1066 622 -591 C ATOM 2657 CE LYS A 332 -20.466 -5.505 -21.785 1.00 73.35 C ANISOU 2657 CE LYS A 332 12018 8296 7556 1194 519 -559 C ATOM 2658 NZ LYS A 332 -19.597 -4.697 -22.688 1.00 69.82 N ANISOU 2658 NZ LYS A 332 11486 7993 7048 1183 242 -591 N ATOM 2659 N LEU A 333 -25.781 -8.090 -23.815 1.00 41.69 N ANISOU 2659 N LEU A 333 7075 4667 4097 841 1609 -489 N ATOM 2660 CA LEU A 333 -27.228 -7.973 -23.707 1.00 46.00 C ANISOU 2660 CA LEU A 333 7586 5099 4795 830 1843 -419 C ATOM 2661 C LEU A 333 -27.839 -9.120 -22.912 1.00 56.20 C ANISOU 2661 C LEU A 333 9043 6221 6089 834 1952 -388 C ATOM 2662 O LEU A 333 -28.821 -8.925 -22.196 1.00 65.43 O ANISOU 2662 O LEU A 333 10401 7146 7311 875 2137 -307 O ATOM 2663 CB LEU A 333 -27.859 -7.904 -25.097 1.00 45.83 C ANISOU 2663 CB LEU A 333 7146 5362 4905 708 1928 -389 C ATOM 2664 CG LEU A 333 -27.545 -6.632 -25.886 1.00 42.98 C ANISOU 2664 CG LEU A 333 6646 5113 4570 710 1950 -331 C ATOM 2665 CD1 LEU A 333 -28.047 -6.745 -27.314 1.00 53.09 C ANISOU 2665 CD1 LEU A 333 7393 6784 5995 532 1966 -257 C ATOM 2666 CD2 LEU A 333 -28.151 -5.420 -25.201 1.00 40.14 C ANISOU 2666 CD2 LEU A 333 6532 4428 4292 831 2113 -258 C ATOM 2667 N ARG A 334 -27.253 -10.311 -23.027 1.00 56.55 N ANISOU 2667 N ARG A 334 9078 6349 6059 801 1886 -423 N ATOM 2668 CA ARG A 334 -27.800 -11.483 -22.348 1.00 56.34 C ANISOU 2668 CA ARG A 334 9256 6128 6024 813 2037 -369 C ATOM 2669 C ARG A 334 -27.491 -11.425 -20.860 1.00 62.53 C ANISOU 2669 C ARG A 334 10474 6615 6670 938 2055 -302 C ATOM 2670 O ARG A 334 -28.318 -11.790 -20.025 1.00 77.23 O ANISOU 2670 O ARG A 334 12566 8248 8529 971 2243 -214 O ATOM 2671 CB ARG A 334 -27.246 -12.774 -22.962 1.00 59.04 C ANISOU 2671 CB ARG A 334 9439 6659 6335 741 1959 -426 C ATOM 2672 CG ARG A 334 -27.729 -14.066 -22.306 1.00 62.69 C ANISOU 2672 CG ARG A 334 10102 6930 6789 750 2107 -379 C ATOM 2673 CD ARG A 334 -26.762 -14.550 -21.231 1.00 66.92 C ANISOU 2673 CD ARG A 334 10958 7308 7161 849 2030 -354 C ATOM 2674 NE ARG A 334 -25.400 -14.674 -21.742 1.00 66.19 N ANISOU 2674 NE ARG A 334 10730 7430 6990 834 1795 -433 N ATOM 2675 CZ ARG A 334 -24.328 -14.847 -20.975 1.00 67.86 C ANISOU 2675 CZ ARG A 334 11173 7547 7065 921 1667 -419 C ATOM 2676 NH1 ARG A 334 -24.459 -14.907 -19.657 1.00 77.97 N ANISOU 2676 NH1 ARG A 334 12830 8544 8253 1034 1749 -326 N ATOM 2677 NH2 ARG A 334 -23.126 -14.953 -21.525 1.00 56.17 N ANISOU 2677 NH2 ARG A 334 9545 6263 5536 894 1457 -487 N ATOM 2678 N ALA A 335 -26.289 -10.959 -20.542 1.00 57.44 N ANISOU 2678 N ALA A 335 9934 5988 5901 1003 1851 -335 N ATOM 2679 CA ALA A 335 -25.840 -10.837 -19.164 1.00 60.67 C ANISOU 2679 CA ALA A 335 10741 6158 6153 1127 1825 -267 C ATOM 2680 C ALA A 335 -26.400 -9.566 -18.547 1.00 73.64 C ANISOU 2680 C ALA A 335 12536 7647 7797 1188 1894 -216 C ATOM 2681 O ALA A 335 -26.238 -9.320 -17.350 1.00 78.24 O ANISOU 2681 O ALA A 335 13452 8038 8239 1288 1901 -148 O ATOM 2682 CB ALA A 335 -24.325 -10.844 -19.097 1.00 59.68 C ANISOU 2682 CB ALA A 335 10661 6110 5906 1170 1564 -315 C ATOM 2683 N ARG A 336 -27.046 -8.761 -19.387 1.00 71.54 N ANISOU 2683 N ARG A 336 12015 7483 7685 1126 1942 -247 N ATOM 2684 CA ARG A 336 -27.557 -7.451 -19.003 1.00 75.03 C ANISOU 2684 CA ARG A 336 12537 7808 8163 1173 1996 -214 C ATOM 2685 C ARG A 336 -26.432 -6.579 -18.461 1.00 78.43 C ANISOU 2685 C ARG A 336 13134 8200 8467 1258 1773 -247 C ATOM 2686 O ARG A 336 -26.636 -5.753 -17.573 1.00 82.67 O ANISOU 2686 O ARG A 336 13895 8570 8945 1333 1804 -201 O ATOM 2687 CB ARG A 336 -28.681 -7.587 -17.976 1.00 84.11 C ANISOU 2687 CB ARG A 336 13948 8719 9290 1210 2246 -97 C ATOM 2688 CG ARG A 336 -29.858 -8.402 -18.476 1.00 85.70 C ANISOU 2688 CG ARG A 336 14001 8923 9636 1120 2464 -56 C ATOM 2689 CD ARG A 336 -30.881 -8.602 -17.384 1.00 98.02 C ANISOU 2689 CD ARG A 336 15849 10239 11156 1154 2705 65 C ATOM 2690 NE ARG A 336 -31.963 -9.488 -17.801 1.00109.89 N ANISOU 2690 NE ARG A 336 17239 11715 12801 1066 2900 105 N ATOM 2691 CZ ARG A 336 -33.153 -9.068 -18.217 1.00119.83 C ANISOU 2691 CZ ARG A 336 18357 12937 14236 1006 3068 148 C ATOM 2692 NH1 ARG A 336 -33.419 -7.771 -18.270 1.00126.85 N ANISOU 2692 NH1 ARG A 336 19196 13820 15182 1027 3075 162 N ATOM 2693 NH2 ARG A 336 -34.080 -9.946 -18.576 1.00117.93 N ANISOU 2693 NH2 ARG A 336 18027 12657 14124 927 3222 176 N ATOM 2694 N GLN A 337 -25.239 -6.779 -19.015 1.00 72.19 N ANISOU 2694 N GLN A 337 12224 7571 7634 1240 1543 -326 N ATOM 2695 CA GLN A 337 -24.086 -5.953 -18.698 1.00 75.42 C ANISOU 2695 CA GLN A 337 12744 7962 7949 1302 1297 -362 C ATOM 2696 C GLN A 337 -24.241 -4.607 -19.395 1.00 78.52 C ANISOU 2696 C GLN A 337 13088 8342 8405 1323 1285 -372 C ATOM 2697 O GLN A 337 -23.525 -3.649 -19.101 1.00 76.97 O ANISOU 2697 O GLN A 337 13049 8064 8133 1395 1109 -378 O ATOM 2698 CB GLN A 337 -22.790 -6.643 -19.132 1.00 75.37 C ANISOU 2698 CB GLN A 337 12661 8109 7869 1277 1076 -415 C ATOM 2699 CG GLN A 337 -21.562 -6.218 -18.346 1.00 84.68 C ANISOU 2699 CG GLN A 337 14085 9191 8898 1372 840 -398 C ATOM 2700 CD GLN A 337 -21.514 -6.843 -16.966 1.00 90.51 C ANISOU 2700 CD GLN A 337 15199 9724 9466 1482 906 -301 C ATOM 2701 OE1 GLN A 337 -21.774 -8.035 -16.803 1.00 95.17 O ANISOU 2701 OE1 GLN A 337 15832 10296 10031 1474 1028 -265 O ATOM 2702 NE2 GLN A 337 -21.187 -6.037 -15.962 1.00 94.66 N ANISOU 2702 NE2 GLN A 337 15997 10098 9870 1582 825 -261 N ATOM 2703 N MET A 338 -25.184 -4.559 -20.333 1.00 70.78 N ANISOU 2703 N MET A 338 11895 7433 7564 1266 1480 -360 N ATOM 2704 CA MET A 338 -25.521 -3.339 -21.052 1.00 72.65 C ANISOU 2704 CA MET A 338 12068 7638 7897 1297 1542 -340 C ATOM 2705 C MET A 338 -26.934 -3.441 -21.619 1.00 71.27 C ANISOU 2705 C MET A 338 11676 7491 7912 1231 1853 -276 C ATOM 2706 O MET A 338 -27.539 -4.511 -21.594 1.00 73.05 O ANISOU 2706 O MET A 338 11793 7785 8176 1152 1963 -268 O ATOM 2707 CB MET A 338 -24.522 -3.078 -22.178 1.00 71.13 C ANISOU 2707 CB MET A 338 11736 7633 7655 1292 1343 -406 C ATOM 2708 CG MET A 338 -24.872 -3.773 -23.479 1.00 60.30 C ANISOU 2708 CG MET A 338 9992 6570 6352 1177 1480 -415 C ATOM 2709 SD MET A 338 -23.910 -3.164 -24.877 1.00 63.00 S ANISOU 2709 SD MET A 338 10002 7266 6670 1097 1205 -388 S ATOM 2710 CE MET A 338 -24.843 -3.868 -26.229 1.00 49.91 C ANISOU 2710 CE MET A 338 7736 6020 5207 878 1440 -277 C ATOM 2711 N HIS A 339 -27.460 -2.327 -22.119 1.00 71.33 N ANISOU 2711 N HIS A 339 11599 7436 8065 1264 1980 -221 N ATOM 2712 CA HIS A 339 -28.747 -2.336 -22.809 1.00 71.82 C ANISOU 2712 CA HIS A 339 11380 7562 8348 1186 2273 -135 C ATOM 2713 C HIS A 339 -28.747 -1.318 -23.949 1.00 69.71 C ANISOU 2713 C HIS A 339 10816 7409 8260 1204 2360 -76 C ATOM 2714 O HIS A 339 -27.741 -0.656 -24.193 1.00 66.61 O ANISOU 2714 O HIS A 339 10387 7079 7843 1211 2054 -64 O ATOM 2715 CB HIS A 339 -29.894 -2.066 -21.833 1.00 82.55 C ANISOU 2715 CB HIS A 339 12910 8686 9770 1199 2451 -53 C ATOM 2716 CG HIS A 339 -29.812 -0.741 -21.146 1.00 78.70 C ANISOU 2716 CG HIS A 339 12633 7986 9284 1300 2409 -23 C ATOM 2717 ND1 HIS A 339 -28.864 -0.454 -20.187 1.00 82.70 N ANISOU 2717 ND1 HIS A 339 13422 8397 9603 1377 2164 -86 N ATOM 2718 CD2 HIS A 339 -30.576 0.370 -21.263 1.00 84.58 C ANISOU 2718 CD2 HIS A 339 13307 8611 10217 1322 2559 69 C ATOM 2719 CE1 HIS A 339 -29.041 0.780 -19.751 1.00 83.83 C ANISOU 2719 CE1 HIS A 339 13657 8380 9813 1435 2147 -50 C ATOM 2720 NE2 HIS A 339 -30.072 1.303 -20.390 1.00 91.53 N ANISOU 2720 NE2 HIS A 339 14427 9331 11019 1406 2380 46 N ATOM 2721 N HIS A 340 -29.868 -1.206 -24.656 1.00 66.31 N ANISOU 2721 N HIS A 340 10019 7107 8068 1101 2605 44 N ATOM 2722 CA HIS A 340 -29.901 -0.450 -25.908 1.00 66.40 C ANISOU 2722 CA HIS A 340 9458 7446 8324 939 2494 222 C ATOM 2723 C HIS A 340 -29.690 1.061 -25.755 1.00 67.00 C ANISOU 2723 C HIS A 340 9519 7381 8555 958 2270 347 C ATOM 2724 O HIS A 340 -29.319 1.733 -26.717 1.00 58.48 O ANISOU 2724 O HIS A 340 7991 6588 7642 802 2002 495 O ATOM 2725 CB HIS A 340 -31.216 -0.714 -26.650 1.00 66.83 C ANISOU 2725 CB HIS A 340 9114 7676 8602 804 2764 326 C ATOM 2726 CG HIS A 340 -32.431 -0.212 -25.938 1.00 74.58 C ANISOU 2726 CG HIS A 340 10299 8320 9719 871 2962 369 C ATOM 2727 ND1 HIS A 340 -33.076 -0.941 -24.962 1.00 84.13 N ANISOU 2727 ND1 HIS A 340 11879 9262 10825 912 3035 287 N ATOM 2728 CD2 HIS A 340 -33.128 0.941 -26.070 1.00 81.14 C ANISOU 2728 CD2 HIS A 340 10976 9064 10790 876 3083 520 C ATOM 2729 CE1 HIS A 340 -34.114 -0.255 -24.518 1.00 91.22 C ANISOU 2729 CE1 HIS A 340 12868 9922 11871 940 3210 380 C ATOM 2730 NE2 HIS A 340 -34.168 0.891 -25.174 1.00 92.65 N ANISOU 2730 NE2 HIS A 340 12755 10184 12262 936 3249 503 N ATOM 2731 N THR A 341 -29.930 1.602 -24.565 1.00 66.65 N ANISOU 2731 N THR A 341 9960 6900 8464 1147 2383 290 N ATOM 2732 CA THR A 341 -29.694 3.026 -24.344 1.00 61.75 C ANISOU 2732 CA THR A 341 9361 6124 7978 1175 2175 397 C ATOM 2733 C THR A 341 -28.203 3.330 -24.172 1.00 59.48 C ANISOU 2733 C THR A 341 9212 5856 7529 1195 1730 336 C ATOM 2734 O THR A 341 -27.789 4.486 -24.236 1.00 57.25 O ANISOU 2734 O THR A 341 8849 5539 7363 1178 1481 433 O ATOM 2735 CB THR A 341 -30.457 3.556 -23.109 1.00 72.18 C ANISOU 2735 CB THR A 341 11159 6959 9308 1370 2445 359 C ATOM 2736 OG1 THR A 341 -29.795 3.135 -21.911 1.00 71.11 O ANISOU 2736 OG1 THR A 341 11487 6686 8847 1453 2299 188 O ATOM 2737 CG2 THR A 341 -31.895 3.058 -23.106 1.00 69.41 C ANISOU 2737 CG2 THR A 341 10732 6592 9051 1343 2872 389 C ATOM 2738 N ASP A 342 -27.404 2.286 -23.958 1.00 62.25 N ANISOU 2738 N ASP A 342 9770 6266 7615 1232 1636 176 N ATOM 2739 CA ASP A 342 -25.960 2.429 -23.753 1.00 51.55 C ANISOU 2739 CA ASP A 342 8576 4932 6080 1259 1224 99 C ATOM 2740 C ASP A 342 -25.248 2.963 -24.987 1.00 45.73 C ANISOU 2740 C ASP A 342 7296 4590 5490 1058 854 243 C ATOM 2741 O ASP A 342 -25.676 2.719 -26.114 1.00 46.69 O ANISOU 2741 O ASP A 342 6910 5056 5773 882 905 359 O ATOM 2742 CB ASP A 342 -25.333 1.092 -23.354 1.00 58.60 C ANISOU 2742 CB ASP A 342 9766 5837 6662 1330 1232 -96 C ATOM 2743 CG ASP A 342 -25.577 0.742 -21.905 1.00 67.85 C ANISOU 2743 CG ASP A 342 11492 6650 7637 1504 1420 -231 C ATOM 2744 OD1 ASP A 342 -26.552 1.259 -21.324 1.00 73.18 O ANISOU 2744 OD1 ASP A 342 12200 7180 8427 1503 1610 -155 O ATOM 2745 OD2 ASP A 342 -24.790 -0.049 -21.348 1.00 76.31 O ANISOU 2745 OD2 ASP A 342 12714 7801 8480 1488 1255 -313 O ATOM 2746 N TYR A 343 -24.160 3.695 -24.769 1.00 40.92 N ANISOU 2746 N TYR A 343 6794 3928 4825 1085 482 233 N ATOM 2747 CA TYR A 343 -23.415 4.274 -25.878 1.00 46.23 C ANISOU 2747 CA TYR A 343 6980 4950 5636 907 112 366 C ATOM 2748 C TYR A 343 -22.810 3.228 -26.813 1.00 40.91 C ANISOU 2748 C TYR A 343 5996 4679 4868 761 -28 342 C ATOM 2749 O TYR A 343 -22.742 3.439 -28.025 1.00 36.54 O ANISOU 2749 O TYR A 343 4899 4490 4494 572 -174 487 O ATOM 2750 CB TYR A 343 -22.297 5.181 -25.359 1.00 44.98 C ANISOU 2750 CB TYR A 343 7049 4631 5408 980 -258 335 C ATOM 2751 CG TYR A 343 -21.464 5.756 -26.479 1.00 49.69 C ANISOU 2751 CG TYR A 343 7160 5580 6138 803 -648 464 C ATOM 2752 CD1 TYR A 343 -21.987 6.729 -27.316 1.00 44.41 C ANISOU 2752 CD1 TYR A 343 6031 5067 5777 676 -666 668 C ATOM 2753 CD2 TYR A 343 -20.167 5.310 -26.717 1.00 45.00 C ANISOU 2753 CD2 TYR A 343 6563 5168 5366 762 -993 383 C ATOM 2754 CE1 TYR A 343 -21.246 7.255 -28.350 1.00 47.37 C ANISOU 2754 CE1 TYR A 343 5957 5761 6279 517 -1014 788 C ATOM 2755 CE2 TYR A 343 -19.416 5.832 -27.755 1.00 40.99 C ANISOU 2755 CE2 TYR A 343 5607 4980 4987 600 -1346 503 C ATOM 2756 CZ TYR A 343 -19.962 6.805 -28.567 1.00 45.85 C ANISOU 2756 CZ TYR A 343 5772 5740 5910 480 -1353 704 C ATOM 2757 OH TYR A 343 -19.228 7.334 -29.604 1.00 46.95 O ANISOU 2757 OH TYR A 343 5463 6194 6182 323 -1698 826 O ATOM 2758 N ALA A 344 -22.377 2.102 -26.258 1.00 34.38 N ANISOU 2758 N ALA A 344 3941 4944 4177 120 78 456 N ATOM 2759 CA ALA A 344 -21.734 1.080 -27.074 1.00 34.03 C ANISOU 2759 CA ALA A 344 3899 4862 4167 39 54 397 C ATOM 2760 C ALA A 344 -22.728 0.488 -28.060 1.00 35.71 C ANISOU 2760 C ALA A 344 4061 5157 4351 4 20 419 C ATOM 2761 O ALA A 344 -22.402 0.243 -29.227 1.00 33.78 O ANISOU 2761 O ALA A 344 3830 4901 4104 -31 9 386 O ATOM 2762 CB ALA A 344 -21.141 -0.009 -26.196 1.00 30.90 C ANISOU 2762 CB ALA A 344 3495 4412 3834 -13 34 364 C ATOM 2763 N PHE A 345 -23.955 0.300 -27.591 1.00 32.12 N ANISOU 2763 N PHE A 345 3547 4783 3874 19 4 473 N ATOM 2764 CA PHE A 345 -25.010 -0.255 -28.425 1.00 34.56 C ANISOU 2764 CA PHE A 345 3799 5173 4159 -4 -27 491 C ATOM 2765 C PHE A 345 -25.363 0.708 -29.550 1.00 35.70 C ANISOU 2765 C PHE A 345 3970 5351 4244 45 -15 497 C ATOM 2766 O PHE A 345 -25.454 0.316 -30.717 1.00 31.39 O ANISOU 2766 O PHE A 345 3416 4819 3691 18 -35 475 O ATOM 2767 CB PHE A 345 -26.252 -0.561 -27.584 1.00 38.56 C ANISOU 2767 CB PHE A 345 4241 5752 4658 8 -40 542 C ATOM 2768 CG PHE A 345 -27.340 -1.261 -28.344 1.00 44.29 C ANISOU 2768 CG PHE A 345 4900 6559 5370 -18 -71 551 C ATOM 2769 CD1 PHE A 345 -27.380 -2.643 -28.403 1.00 41.71 C ANISOU 2769 CD1 PHE A 345 4524 6237 5086 -91 -100 532 C ATOM 2770 CD2 PHE A 345 -28.324 -0.538 -28.997 1.00 44.09 C ANISOU 2770 CD2 PHE A 345 4862 6604 5287 34 -72 574 C ATOM 2771 CE1 PHE A 345 -28.377 -3.289 -29.099 1.00 45.07 C ANISOU 2771 CE1 PHE A 345 4884 6736 5504 -109 -127 538 C ATOM 2772 CE2 PHE A 345 -29.323 -1.180 -29.694 1.00 46.57 C ANISOU 2772 CE2 PHE A 345 5114 6988 5593 18 -101 575 C ATOM 2773 CZ PHE A 345 -29.350 -2.556 -29.746 1.00 43.81 C ANISOU 2773 CZ PHE A 345 4711 6642 5293 -53 -128 558 C ATOM 2774 N ARG A 346 -25.550 1.975 -29.190 1.00 31.48 N ANISOU 2774 N ARG A 346 3469 4828 3664 120 16 525 N ATOM 2775 CA ARG A 346 -25.939 2.990 -30.157 1.00 39.24 C ANISOU 2775 CA ARG A 346 4486 5845 4579 175 31 529 C ATOM 2776 C ARG A 346 -24.844 3.209 -31.201 1.00 30.92 C ANISOU 2776 C ARG A 346 3500 4718 3532 163 51 474 C ATOM 2777 O ARG A 346 -25.135 3.461 -32.369 1.00 30.67 O ANISOU 2777 O ARG A 346 3487 4706 3460 179 48 461 O ATOM 2778 CB ARG A 346 -26.280 4.300 -29.440 1.00 35.37 C ANISOU 2778 CB ARG A 346 4020 5382 4039 255 61 570 C ATOM 2779 CG ARG A 346 -27.501 4.189 -28.532 1.00 37.64 C ANISOU 2779 CG ARG A 346 4243 5748 4312 272 41 626 C ATOM 2780 CD ARG A 346 -27.941 5.539 -27.971 1.00 29.56 C ANISOU 2780 CD ARG A 346 3242 4763 3228 352 64 671 C ATOM 2781 NE ARG A 346 -27.124 5.979 -26.844 1.00 34.32 N ANISOU 2781 NE ARG A 346 3872 5306 3864 375 92 686 N ATOM 2782 CZ ARG A 346 -26.219 6.950 -26.908 1.00 42.36 C ANISOU 2782 CZ ARG A 346 4954 6272 4868 417 132 670 C ATOM 2783 NH1 ARG A 346 -26.009 7.593 -28.049 1.00 35.77 N ANISOU 2783 NH1 ARG A 346 4170 5436 3984 438 151 641 N ATOM 2784 NH2 ARG A 346 -25.524 7.282 -25.829 1.00 44.01 N ANISOU 2784 NH2 ARG A 346 5180 6427 5115 441 155 681 N ATOM 2785 N LEU A 347 -23.589 3.095 -30.782 1.00 27.19 N ANISOU 2785 N LEU A 347 3065 4155 3110 135 70 437 N ATOM 2786 CA LEU A 347 -22.474 3.152 -31.720 1.00 29.29 C ANISOU 2786 CA LEU A 347 3394 4341 3395 111 88 377 C ATOM 2787 C LEU A 347 -22.493 1.937 -32.640 1.00 24.74 C ANISOU 2787 C LEU A 347 2784 3768 2849 37 44 353 C ATOM 2788 O LEU A 347 -22.211 2.036 -33.842 1.00 27.78 O ANISOU 2788 O LEU A 347 3206 4128 3222 31 46 324 O ATOM 2789 CB LEU A 347 -21.145 3.228 -30.965 1.00 25.56 C ANISOU 2789 CB LEU A 347 2964 3770 2979 96 115 335 C ATOM 2790 CG LEU A 347 -19.872 3.315 -31.805 1.00 27.55 C ANISOU 2790 CG LEU A 347 3284 3924 3258 68 138 263 C ATOM 2791 CD1 LEU A 347 -19.901 4.549 -32.695 1.00 23.89 C ANISOU 2791 CD1 LEU A 347 2884 3457 2734 132 183 258 C ATOM 2792 CD2 LEU A 347 -18.643 3.328 -30.905 1.00 30.96 C ANISOU 2792 CD2 LEU A 347 3750 4262 3750 57 161 215 C ATOM 2793 N ALA A 348 -22.851 0.792 -32.067 1.00 24.68 N ANISOU 2793 N ALA A 348 2708 3791 2879 -17 4 368 N ATOM 2794 CA ALA A 348 -22.938 -0.444 -32.830 1.00 31.39 C ANISOU 2794 CA ALA A 348 3514 4654 3758 -89 -42 352 C ATOM 2795 C ALA A 348 -24.039 -0.365 -33.880 1.00 33.00 C ANISOU 2795 C ALA A 348 3688 4934 3916 -60 -60 375 C ATOM 2796 O ALA A 348 -23.941 -0.994 -34.930 1.00 32.70 O ANISOU 2796 O ALA A 348 3641 4893 3893 -97 -87 355 O ATOM 2797 CB ALA A 348 -23.172 -1.630 -31.904 1.00 34.64 C ANISOU 2797 CB ALA A 348 3860 5089 4213 -145 -74 364 C ATOM 2798 N LYS A 349 -25.082 0.412 -33.605 1.00 32.56 N ANISOU 2798 N LYS A 349 3619 4947 3807 10 -48 416 N ATOM 2799 CA LYS A 349 -26.165 0.558 -34.571 1.00 33.75 C ANISOU 2799 CA LYS A 349 3746 5168 3910 48 -66 429 C ATOM 2800 C LYS A 349 -25.651 1.164 -35.870 1.00 33.70 C ANISOU 2800 C LYS A 349 3814 5116 3876 74 -49 394 C ATOM 2801 O LYS A 349 -26.025 0.726 -36.952 1.00 34.15 O ANISOU 2801 O LYS A 349 3854 5193 3929 69 -76 383 O ATOM 2802 CB LYS A 349 -27.292 1.425 -33.998 1.00 40.14 C ANISOU 2802 CB LYS A 349 4540 6052 4659 120 -54 470 C ATOM 2803 CG LYS A 349 -28.088 0.765 -32.885 1.00 30.72 C ANISOU 2803 CG LYS A 349 3268 4916 3490 99 -74 506 C ATOM 2804 CD LYS A 349 -28.934 1.777 -32.131 1.00 38.18 C ANISOU 2804 CD LYS A 349 4212 5914 4380 168 -57 547 C ATOM 2805 CE LYS A 349 -29.894 2.519 -33.051 1.00 41.87 C ANISOU 2805 CE LYS A 349 4690 6445 4775 233 -62 546 C ATOM 2806 NZ LYS A 349 -30.713 3.516 -32.301 1.00 38.02 N ANISOU 2806 NZ LYS A 349 4203 6014 4229 297 -50 585 N ATOM 2807 N SER A 350 -24.761 2.147 -35.759 1.00 31.31 N ANISOU 2807 N SER A 350 3592 4746 3558 104 -1 375 N ATOM 2808 CA SER A 350 -24.207 2.795 -36.940 1.00 27.23 C ANISOU 2808 CA SER A 350 3158 4174 3015 132 25 337 C ATOM 2809 C SER A 350 -23.102 1.962 -37.576 1.00 28.74 C ANISOU 2809 C SER A 350 3367 4283 3270 56 12 292 C ATOM 2810 O SER A 350 -23.122 1.696 -38.781 1.00 24.87 O ANISOU 2810 O SER A 350 2892 3780 2778 51 -4 273 O ATOM 2811 CB SER A 350 -23.658 4.178 -36.587 1.00 30.68 C ANISOU 2811 CB SER A 350 3677 4569 3413 193 87 329 C ATOM 2812 OG SER A 350 -24.645 4.995 -35.983 1.00 32.46 O ANISOU 2812 OG SER A 350 3888 4872 3575 261 96 373 O ATOM 2813 N THR A 351 -22.143 1.539 -36.757 1.00 29.96 N ANISOU 2813 N THR A 351 3522 4381 3482 0 16 274 N ATOM 2814 CA THR A 351 -20.965 0.856 -37.282 1.00 30.61 C ANISOU 2814 CA THR A 351 3630 4376 3623 -73 6 223 C ATOM 2815 C THR A 351 -21.302 -0.506 -37.892 1.00 24.83 C ANISOU 2815 C THR A 351 2829 3680 2925 -140 -57 229 C ATOM 2816 O THR A 351 -20.763 -0.876 -38.942 1.00 25.07 O ANISOU 2816 O THR A 351 2885 3663 2977 -175 -71 198 O ATOM 2817 CB THR A 351 -19.897 0.689 -36.180 1.00 30.88 C ANISOU 2817 CB THR A 351 3680 4344 3710 -114 21 193 C ATOM 2818 OG1 THR A 351 -19.385 1.980 -35.825 1.00 30.55 O ANISOU 2818 OG1 THR A 351 3710 4252 3644 -51 84 176 O ATOM 2819 CG2 THR A 351 -18.748 -0.184 -36.661 1.00 22.20 C ANISOU 2819 CG2 THR A 351 2598 3163 2673 -200 -1 136 C ATOM 2820 N LEU A 352 -22.238 -1.223 -37.274 1.00 24.03 N ANISOU 2820 N LEU A 352 2641 3663 2828 -154 -93 270 N ATOM 2821 CA LEU A 352 -22.597 -2.550 -37.761 1.00 28.71 C ANISOU 2821 CA LEU A 352 3158 4295 3454 -217 -151 277 C ATOM 2822 C LEU A 352 -23.528 -2.511 -38.964 1.00 30.83 C ANISOU 2822 C LEU A 352 3408 4617 3691 -175 -171 293 C ATOM 2823 O LEU A 352 -23.771 -3.543 -39.578 1.00 33.97 O ANISOU 2823 O LEU A 352 3747 5041 4117 -219 -218 296 O ATOM 2824 CB LEU A 352 -23.238 -3.387 -36.655 1.00 29.96 C ANISOU 2824 CB LEU A 352 3233 4519 3633 -249 -177 308 C ATOM 2825 CG LEU A 352 -22.316 -3.885 -35.542 1.00 34.43 C ANISOU 2825 CG LEU A 352 3806 5032 4244 -308 -175 286 C ATOM 2826 CD1 LEU A 352 -23.035 -4.929 -34.705 1.00 34.03 C ANISOU 2826 CD1 LEU A 352 3670 5047 4213 -345 -206 314 C ATOM 2827 CD2 LEU A 352 -21.023 -4.448 -36.115 1.00 33.40 C ANISOU 2827 CD2 LEU A 352 3713 4819 4159 -381 -192 234 C ATOM 2828 N THR A 353 -24.092 -1.350 -39.281 1.00 26.39 N ANISOU 2828 N THR A 353 2889 4073 3066 -86 -138 301 N ATOM 2829 CA THR A 353 -24.781 -1.221 -40.561 1.00 35.17 C ANISOU 2829 CA THR A 353 4005 5212 4146 -38 -153 300 C ATOM 2830 C THR A 353 -23.804 -0.758 -41.626 1.00 31.16 C ANISOU 2830 C THR A 353 3591 4610 3639 -32 -130 259 C ATOM 2831 O THR A 353 -23.823 -1.248 -42.754 1.00 32.77 O ANISOU 2831 O THR A 353 3792 4801 3857 -41 -159 248 O ATOM 2832 CB THR A 353 -25.970 -0.231 -40.513 1.00 35.24 C ANISOU 2832 CB THR A 353 4019 5290 4080 60 -134 321 C ATOM 2833 OG1 THR A 353 -25.506 1.068 -40.131 1.00 47.90 O ANISOU 2833 OG1 THR A 353 5709 6853 5638 110 -77 313 O ATOM 2834 CG2 THR A 353 -27.016 -0.699 -39.535 1.00 35.57 C ANISOU 2834 CG2 THR A 353 3967 5424 4124 55 -157 358 C ATOM 2835 N LEU A 354 -22.946 0.191 -41.262 1.00 23.14 N ANISOU 2835 N LEU A 354 2659 3525 2608 -15 -75 236 N ATOM 2836 CA LEU A 354 -22.029 0.767 -42.233 1.00 26.30 C ANISOU 2836 CA LEU A 354 3160 3829 3005 -3 -41 192 C ATOM 2837 C LEU A 354 -21.006 -0.237 -42.749 1.00 28.51 C ANISOU 2837 C LEU A 354 3438 4038 3358 -94 -71 161 C ATOM 2838 O LEU A 354 -20.687 -0.236 -43.938 1.00 29.47 O ANISOU 2838 O LEU A 354 3607 4107 3483 -90 -73 137 O ATOM 2839 CB LEU A 354 -21.305 1.970 -41.632 1.00 26.89 C ANISOU 2839 CB LEU A 354 3318 3844 3054 34 29 169 C ATOM 2840 CG LEU A 354 -22.123 3.251 -41.479 1.00 32.99 C ANISOU 2840 CG LEU A 354 4128 4666 3742 136 69 189 C ATOM 2841 CD1 LEU A 354 -21.235 4.392 -41.007 1.00 27.24 C ANISOU 2841 CD1 LEU A 354 3485 3868 2996 167 140 161 C ATOM 2842 CD2 LEU A 354 -22.815 3.605 -42.787 1.00 32.38 C ANISOU 2842 CD2 LEU A 354 4088 4604 3610 201 66 182 C ATOM 2843 N ILE A 355 -20.486 -1.092 -41.874 1.00 26.29 N ANISOU 2843 N ILE A 355 3106 3752 3131 -176 -96 160 N ATOM 2844 CA ILE A 355 -19.488 -2.057 -42.338 1.00 32.48 C ANISOU 2844 CA ILE A 355 3889 4472 3980 -268 -130 127 C ATOM 2845 C ILE A 355 -20.011 -3.026 -43.427 1.00 31.71 C ANISOU 2845 C ILE A 355 3736 4414 3900 -292 -191 148 C ATOM 2846 O ILE A 355 -19.409 -3.109 -44.506 1.00 31.28 O ANISOU 2846 O ILE A 355 3729 4291 3864 -309 -197 121 O ATOM 2847 CB ILE A 355 -18.898 -2.866 -41.147 1.00 29.00 C ANISOU 2847 CB ILE A 355 3403 4026 3589 -349 -152 118 C ATOM 2848 CG1 ILE A 355 -18.023 -1.965 -40.270 1.00 24.69 C ANISOU 2848 CG1 ILE A 355 2928 3409 3044 -331 -93 81 C ATOM 2849 CG2 ILE A 355 -18.099 -4.059 -41.646 1.00 23.35 C ANISOU 2849 CG2 ILE A 355 2668 3270 2933 -450 -204 91 C ATOM 2850 CD1 ILE A 355 -17.420 -2.665 -39.068 1.00 26.66 C ANISOU 2850 CD1 ILE A 355 3147 3644 3340 -397 -110 63 C ATOM 2851 N PRO A 356 -21.131 -3.750 -43.174 1.00 32.18 N ANISOU 2851 N PRO A 356 3694 4577 3955 -291 -235 193 N ATOM 2852 CA PRO A 356 -21.687 -4.555 -44.272 1.00 30.76 C ANISOU 2852 CA PRO A 356 3461 4435 3790 -298 -288 211 C ATOM 2853 C PRO A 356 -22.131 -3.759 -45.499 1.00 29.34 C ANISOU 2853 C PRO A 356 3340 4238 3569 -208 -270 205 C ATOM 2854 O PRO A 356 -22.010 -4.259 -46.614 1.00 26.40 O ANISOU 2854 O PRO A 356 2967 3841 3221 -220 -303 201 O ATOM 2855 CB PRO A 356 -22.885 -5.264 -43.625 1.00 25.43 C ANISOU 2855 CB PRO A 356 2673 3875 3113 -297 -323 254 C ATOM 2856 CG PRO A 356 -23.257 -4.423 -42.495 1.00 30.16 C ANISOU 2856 CG PRO A 356 3287 4501 3673 -251 -279 263 C ATOM 2857 CD PRO A 356 -21.965 -3.860 -41.964 1.00 28.80 C ANISOU 2857 CD PRO A 356 3197 4233 3511 -279 -237 227 C ATOM 2858 N LEU A 357 -22.646 -2.553 -45.299 1.00 23.70 N ANISOU 2858 N LEU A 357 2677 3536 2790 -118 -220 205 N ATOM 2859 CA LEU A 357 -23.194 -1.796 -46.420 1.00 23.92 C ANISOU 2859 CA LEU A 357 2764 3555 2768 -24 -204 195 C ATOM 2860 C LEU A 357 -22.080 -1.393 -47.365 1.00 27.91 C ANISOU 2860 C LEU A 357 3376 3941 3286 -30 -175 153 C ATOM 2861 O LEU A 357 -22.127 -1.684 -48.568 1.00 29.74 O ANISOU 2861 O LEU A 357 3625 4145 3530 -14 -199 146 O ATOM 2862 CB LEU A 357 -23.944 -0.557 -45.928 1.00 29.15 C ANISOU 2862 CB LEU A 357 3465 4260 3353 70 -157 200 C ATOM 2863 CG LEU A 357 -24.813 0.194 -46.941 1.00 37.59 C ANISOU 2863 CG LEU A 357 4582 5345 4356 179 -146 190 C ATOM 2864 CD1 LEU A 357 -25.824 -0.742 -47.583 1.00 33.21 C ANISOU 2864 CD1 LEU A 357 3937 4861 3820 192 -211 208 C ATOM 2865 CD2 LEU A 357 -25.521 1.358 -46.269 1.00 43.56 C ANISOU 2865 CD2 LEU A 357 5367 6152 5031 259 -105 197 C ATOM 2866 N LEU A 358 -21.062 -0.751 -46.804 1.00 28.40 N ANISOU 2866 N LEU A 358 3510 3930 3350 -52 -122 123 N ATOM 2867 CA LEU A 358 -19.922 -0.301 -47.588 1.00 26.64 C ANISOU 2867 CA LEU A 358 3396 3585 3142 -61 -84 74 C ATOM 2868 C LEU A 358 -19.117 -1.475 -48.136 1.00 27.16 C ANISOU 2868 C LEU A 358 3435 3600 3286 -160 -135 63 C ATOM 2869 O LEU A 358 -18.621 -1.424 -49.262 1.00 29.02 O ANISOU 2869 O LEU A 358 3735 3756 3536 -156 -131 37 O ATOM 2870 CB LEU A 358 -19.027 0.612 -46.749 1.00 30.87 C ANISOU 2870 CB LEU A 358 4004 4056 3669 -64 -15 40 C ATOM 2871 CG LEU A 358 -19.710 1.843 -46.141 1.00 27.10 C ANISOU 2871 CG LEU A 358 3557 3626 3114 30 39 53 C ATOM 2872 CD1 LEU A 358 -18.688 2.844 -45.624 1.00 28.79 C ANISOU 2872 CD1 LEU A 358 3861 3757 3322 39 115 10 C ATOM 2873 CD2 LEU A 358 -20.636 2.499 -47.146 1.00 34.99 C ANISOU 2873 CD2 LEU A 358 4601 4651 4043 131 49 58 C ATOM 2874 N GLY A 359 -19.019 -2.549 -47.358 1.00 25.91 N ANISOU 2874 N GLY A 359 3181 3488 3174 -246 -186 83 N ATOM 2875 CA GLY A 359 -18.246 -3.700 -47.790 1.00 27.29 C ANISOU 2875 CA GLY A 359 3326 3625 3418 -346 -240 73 C ATOM 2876 C GLY A 359 -18.902 -4.414 -48.955 1.00 29.10 C ANISOU 2876 C GLY A 359 3507 3889 3659 -333 -297 104 C ATOM 2877 O GLY A 359 -18.262 -4.674 -49.981 1.00 31.95 O ANISOU 2877 O GLY A 359 3910 4176 4054 -360 -314 85 O ATOM 2878 N VAL A 360 -20.194 -4.705 -48.808 1.00 30.52 N ANISOU 2878 N VAL A 360 3601 4180 3815 -287 -327 148 N ATOM 2879 CA VAL A 360 -20.941 -5.377 -49.860 1.00 32.22 C ANISOU 2879 CA VAL A 360 3761 4438 4043 -262 -382 176 C ATOM 2880 C VAL A 360 -20.977 -4.497 -51.096 1.00 32.14 C ANISOU 2880 C VAL A 360 3853 4358 4001 -171 -350 154 C ATOM 2881 O VAL A 360 -20.835 -4.988 -52.220 1.00 36.62 O ANISOU 2881 O VAL A 360 4424 4889 4601 -174 -386 156 O ATOM 2882 CB VAL A 360 -22.390 -5.709 -49.424 1.00 30.61 C ANISOU 2882 CB VAL A 360 3451 4363 3815 -216 -409 217 C ATOM 2883 CG1 VAL A 360 -23.227 -6.141 -50.622 1.00 21.81 C ANISOU 2883 CG1 VAL A 360 2296 3284 2708 -159 -454 235 C ATOM 2884 CG2 VAL A 360 -22.395 -6.785 -48.345 1.00 26.44 C ANISOU 2884 CG2 VAL A 360 2817 3903 3325 -308 -447 240 C ATOM 2885 N HIS A 361 -21.114 -3.190 -50.893 1.00 33.95 N ANISOU 2885 N HIS A 361 4170 4563 4167 -91 -280 131 N ATOM 2886 CA HIS A 361 -21.131 -2.293 -52.037 1.00 29.76 C ANISOU 2886 CA HIS A 361 3749 3960 3597 0 -242 102 C ATOM 2887 C HIS A 361 -19.801 -2.318 -52.785 1.00 34.11 C ANISOU 2887 C HIS A 361 4389 4380 4193 -52 -227 65 C ATOM 2888 O HIS A 361 -19.780 -2.335 -54.018 1.00 31.81 O ANISOU 2888 O HIS A 361 4146 4032 3910 -14 -237 56 O ATOM 2889 CB HIS A 361 -21.442 -0.859 -51.618 1.00 34.55 C ANISOU 2889 CB HIS A 361 4440 4565 4123 90 -167 82 C ATOM 2890 CG HIS A 361 -21.020 0.153 -52.634 1.00 43.11 C ANISOU 2890 CG HIS A 361 5666 5544 5170 162 -109 38 C ATOM 2891 ND1 HIS A 361 -21.771 0.443 -53.753 1.00 47.09 N ANISOU 2891 ND1 HIS A 361 6212 6045 5636 261 -116 32 N ATOM 2892 CD2 HIS A 361 -19.901 0.910 -52.725 1.00 38.30 C ANISOU 2892 CD2 HIS A 361 5172 4821 4559 150 -42 -8 C ATOM 2893 CE1 HIS A 361 -21.140 1.349 -54.480 1.00 50.74 C ANISOU 2893 CE1 HIS A 361 6813 6396 6069 307 -53 -14 C ATOM 2894 NE2 HIS A 361 -20.003 1.649 -53.878 1.00 40.58 N ANISOU 2894 NE2 HIS A 361 5571 5042 4805 240 -6 -39 N ATOM 2895 N PHE A 362 -18.690 -2.328 -52.050 1.00 31.07 N ANISOU 2895 N PHE A 362 4026 3940 3840 -137 -203 40 N ATOM 2896 CA PHE A 362 -17.398 -2.344 -52.724 1.00 30.18 C ANISOU 2896 CA PHE A 362 3997 3697 3773 -192 -187 -4 C ATOM 2897 C PHE A 362 -17.167 -3.662 -53.452 1.00 31.13 C ANISOU 2897 C PHE A 362 4052 3814 3961 -268 -269 18 C ATOM 2898 O PHE A 362 -16.590 -3.675 -54.538 1.00 32.57 O ANISOU 2898 O PHE A 362 4302 3902 4170 -271 -269 -3 O ATOM 2899 CB PHE A 362 -16.245 -2.087 -51.753 1.00 27.74 C ANISOU 2899 CB PHE A 362 3724 3328 3487 -265 -145 -47 C ATOM 2900 CG PHE A 362 -14.923 -1.904 -52.443 1.00 30.59 C ANISOU 2900 CG PHE A 362 4188 3545 3891 -310 -114 -106 C ATOM 2901 CD1 PHE A 362 -14.517 -0.645 -52.863 1.00 33.44 C ANISOU 2901 CD1 PHE A 362 4681 3809 4215 -241 -26 -155 C ATOM 2902 CD2 PHE A 362 -14.101 -2.993 -52.705 1.00 31.84 C ANISOU 2902 CD2 PHE A 362 4312 3664 4123 -421 -173 -115 C ATOM 2903 CE1 PHE A 362 -13.309 -0.471 -53.515 1.00 36.92 C ANISOU 2903 CE1 PHE A 362 5219 4111 4698 -282 8 -216 C ATOM 2904 CE2 PHE A 362 -12.893 -2.830 -53.359 1.00 36.38 C ANISOU 2904 CE2 PHE A 362 4982 4102 4739 -465 -146 -174 C ATOM 2905 CZ PHE A 362 -12.495 -1.566 -53.764 1.00 41.60 C ANISOU 2905 CZ PHE A 362 5775 4662 5368 -395 -53 -225 C ATOM 2906 N VAL A 363 -17.617 -4.769 -52.865 1.00 28.36 N ANISOU 2906 N VAL A 363 3571 3566 3639 -328 -338 61 N ATOM 2907 CA VAL A 363 -17.422 -6.060 -53.516 1.00 26.75 C ANISOU 2907 CA VAL A 363 3296 3371 3498 -402 -420 87 C ATOM 2908 C VAL A 363 -18.244 -6.132 -54.796 1.00 31.21 C ANISOU 2908 C VAL A 363 3857 3947 4055 -317 -448 114 C ATOM 2909 O VAL A 363 -17.762 -6.588 -55.842 1.00 29.23 O ANISOU 2909 O VAL A 363 3628 3631 3847 -341 -482 113 O ATOM 2910 CB VAL A 363 -17.802 -7.228 -52.588 1.00 30.93 C ANISOU 2910 CB VAL A 363 3687 4014 4053 -479 -483 126 C ATOM 2911 CG1 VAL A 363 -17.711 -8.553 -53.331 1.00 24.80 C ANISOU 2911 CG1 VAL A 363 2831 3258 3334 -547 -570 158 C ATOM 2912 CG2 VAL A 363 -16.904 -7.243 -51.367 1.00 30.48 C ANISOU 2912 CG2 VAL A 363 3640 3934 4009 -564 -462 93 C ATOM 2913 N VAL A 364 -19.478 -5.640 -54.715 1.00 35.74 N ANISOU 2913 N VAL A 364 4409 4598 4574 -212 -433 132 N ATOM 2914 CA VAL A 364 -20.355 -5.611 -55.877 1.00 34.87 C ANISOU 2914 CA VAL A 364 4300 4499 4450 -113 -456 148 C ATOM 2915 C VAL A 364 -19.746 -4.741 -56.968 1.00 34.03 C ANISOU 2915 C VAL A 364 4342 4259 4330 -55 -407 107 C ATOM 2916 O VAL A 364 -19.754 -5.106 -58.145 1.00 30.22 O ANISOU 2916 O VAL A 364 3873 3731 3877 -29 -441 114 O ATOM 2917 CB VAL A 364 -21.763 -5.078 -55.506 1.00 32.12 C ANISOU 2917 CB VAL A 364 3916 4251 4037 -6 -440 160 C ATOM 2918 CG1 VAL A 364 -22.505 -4.583 -56.738 1.00 26.57 C ANISOU 2918 CG1 VAL A 364 3270 3525 3302 123 -437 150 C ATOM 2919 CG2 VAL A 364 -22.566 -6.148 -54.779 1.00 29.05 C ANISOU 2919 CG2 VAL A 364 3370 3993 3673 -49 -501 205 C ATOM 2920 N PHE A 365 -19.177 -3.610 -56.565 1.00 32.37 N ANISOU 2920 N PHE A 365 5014 3262 4024 839 -1233 647 N ATOM 2921 CA PHE A 365 -18.549 -2.700 -57.513 1.00 39.37 C ANISOU 2921 CA PHE A 365 5850 4241 4869 435 -1325 807 C ATOM 2922 C PHE A 365 -17.369 -3.375 -58.195 1.00 41.48 C ANISOU 2922 C PHE A 365 5780 4809 5171 222 -1099 773 C ATOM 2923 O PHE A 365 -17.165 -3.237 -59.407 1.00 44.75 O ANISOU 2923 O PHE A 365 6087 5412 5504 -83 -990 857 O ATOM 2924 CB PHE A 365 -18.093 -1.425 -56.797 1.00 37.59 C ANISOU 2924 CB PHE A 365 5780 3790 4712 366 -1688 915 C ATOM 2925 CG PHE A 365 -17.005 -0.675 -57.513 1.00 48.98 C ANISOU 2925 CG PHE A 365 7092 5354 6164 -27 -1773 1047 C ATOM 2926 CD1 PHE A 365 -17.318 0.286 -58.458 1.00 56.89 C ANISOU 2926 CD1 PHE A 365 8201 6352 7062 -314 -1877 1209 C ATOM 2927 CD2 PHE A 365 -15.667 -0.918 -57.227 1.00 51.47 C ANISOU 2927 CD2 PHE A 365 7179 5783 6594 -108 -1754 1011 C ATOM 2928 CE1 PHE A 365 -16.318 0.984 -59.114 1.00 56.00 C ANISOU 2928 CE1 PHE A 365 7970 6350 6959 -676 -1957 1333 C ATOM 2929 CE2 PHE A 365 -14.665 -0.230 -57.883 1.00 55.29 C ANISOU 2929 CE2 PHE A 365 7542 6378 7088 -469 -1833 1134 C ATOM 2930 CZ PHE A 365 -14.990 0.722 -58.828 1.00 59.06 C ANISOU 2930 CZ PHE A 365 8128 6853 7461 -753 -1934 1295 C ATOM 2931 N ALA A 366 -16.618 -4.140 -57.409 1.00 42.82 N ANISOU 2931 N ALA A 366 5785 5024 5462 392 -1021 645 N ATOM 2932 CA ALA A 366 -15.427 -4.798 -57.912 1.00 41.04 C ANISOU 2932 CA ALA A 366 5236 5070 5287 215 -818 604 C ATOM 2933 C ALA A 366 -15.794 -5.846 -58.946 1.00 37.47 C ANISOU 2933 C ALA A 366 4623 4871 4744 176 -467 538 C ATOM 2934 O ALA A 366 -15.168 -5.924 -60.001 1.00 40.34 O ANISOU 2934 O ALA A 366 4794 5466 5069 -121 -327 590 O ATOM 2935 CB ALA A 366 -14.649 -5.424 -56.773 1.00 37.44 C ANISOU 2935 CB ALA A 366 4655 4590 4980 439 -812 474 C ATOM 2936 N PHE A 367 -16.829 -6.632 -58.657 1.00 37.45 N ANISOU 2936 N PHE A 367 4705 4822 4703 473 -328 425 N ATOM 2937 CA PHE A 367 -17.272 -7.649 -59.607 1.00 41.08 C ANISOU 2937 CA PHE A 367 5028 5509 5073 458 4 358 C ATOM 2938 C PHE A 367 -17.874 -7.043 -60.872 1.00 44.45 C ANISOU 2938 C PHE A 367 5540 5997 5351 184 16 494 C ATOM 2939 O PHE A 367 -17.582 -7.497 -61.979 1.00 46.66 O ANISOU 2939 O PHE A 367 5629 6529 5569 -33 243 503 O ATOM 2940 CB PHE A 367 -18.290 -8.586 -58.957 1.00 28.78 C ANISOU 2940 CB PHE A 367 3558 3869 3509 849 133 210 C ATOM 2941 CG PHE A 367 -17.672 -9.698 -58.163 1.00 30.44 C ANISOU 2941 CG PHE A 367 3576 4152 3837 1084 286 42 C ATOM 2942 CD1 PHE A 367 -17.280 -10.873 -58.784 1.00 42.53 C ANISOU 2942 CD1 PHE A 367 4839 5958 5363 1052 615 -59 C ATOM 2943 CD2 PHE A 367 -17.485 -9.573 -56.799 1.00 30.19 C ANISOU 2943 CD2 PHE A 367 3633 3916 3923 1336 101 -17 C ATOM 2944 CE1 PHE A 367 -16.712 -11.903 -58.060 1.00 30.64 C ANISOU 2944 CE1 PHE A 367 3179 4487 3975 1209 730 -212 C ATOM 2945 CE2 PHE A 367 -16.919 -10.600 -56.069 1.00 29.35 C ANISOU 2945 CE2 PHE A 367 3354 3869 3927 1511 237 -168 C ATOM 2946 CZ PHE A 367 -16.532 -11.767 -56.701 1.00 26.23 C ANISOU 2946 CZ PHE A 367 2741 3685 3541 1330 514 -253 C ATOM 2947 N VAL A 368 -18.711 -6.020 -60.705 1.00 42.44 N ANISOU 2947 N VAL A 368 5572 5513 5041 195 -230 600 N ATOM 2948 CA VAL A 368 -19.394 -5.411 -61.844 1.00 46.61 C ANISOU 2948 CA VAL A 368 6207 6075 5427 -42 -234 731 C ATOM 2949 C VAL A 368 -18.433 -4.691 -62.785 1.00 46.37 C ANISOU 2949 C VAL A 368 6047 6194 5378 -462 -283 870 C ATOM 2950 O VAL A 368 -18.596 -4.746 -64.006 1.00 54.03 O ANISOU 2950 O VAL A 368 6946 7342 6242 -698 -131 931 O ATOM 2951 CB VAL A 368 -20.489 -4.423 -61.380 1.00 44.30 C ANISOU 2951 CB VAL A 368 6259 5486 5087 72 -506 817 C ATOM 2952 CG1 VAL A 368 -21.095 -3.700 -62.567 1.00 46.24 C ANISOU 2952 CG1 VAL A 368 6610 5766 5192 -201 -530 966 C ATOM 2953 CG2 VAL A 368 -21.575 -5.163 -60.619 1.00 45.85 C ANISOU 2953 CG2 VAL A 368 6589 5552 5280 472 -432 687 C ATOM 2954 N THR A 369 -17.415 -4.044 -62.228 1.00 45.62 N ANISOU 2954 N THR A 369 5915 6031 5387 -555 -488 919 N ATOM 2955 CA THR A 369 -16.471 -3.306 -63.062 1.00 53.07 C ANISOU 2955 CA THR A 369 6740 7103 6320 -952 -553 1055 C ATOM 2956 C THR A 369 -15.638 -4.223 -63.955 1.00 53.00 C ANISOU 2956 C THR A 369 6405 7424 6307 -1132 -245 1002 C ATOM 2957 O THR A 369 -15.194 -3.812 -65.023 1.00 56.13 O ANISOU 2957 O THR A 369 6704 7978 6644 -1472 -211 1112 O ATOM 2958 CB THR A 369 -15.523 -2.441 -62.216 1.00 56.05 C ANISOU 2958 CB THR A 369 7143 7336 6819 -1003 -841 1115 C ATOM 2959 OG1 THR A 369 -15.100 -3.180 -61.064 1.00 61.65 O ANISOU 2959 OG1 THR A 369 7771 7998 7655 -714 -810 967 O ATOM 2960 CG2 THR A 369 -16.230 -1.182 -61.759 1.00 54.25 C ANISOU 2960 CG2 THR A 369 7235 6814 6564 -977 -1173 1231 C ATOM 2961 N ASP A 370 -15.428 -5.460 -63.519 1.00 55.35 N ANISOU 2961 N ASP A 370 6536 7825 6668 -904 -22 835 N ATOM 2962 CA ASP A 370 -14.639 -6.409 -64.298 1.00 60.77 C ANISOU 2962 CA ASP A 370 6909 8823 7358 -1049 281 771 C ATOM 2963 C ASP A 370 -15.449 -7.192 -65.335 1.00 62.09 C ANISOU 2963 C ASP A 370 7030 9166 7396 -1067 571 732 C ATOM 2964 O ASP A 370 -14.874 -7.929 -66.132 1.00 66.89 O ANISOU 2964 O ASP A 370 7388 10040 7986 -1215 829 692 O ATOM 2965 CB ASP A 370 -13.925 -7.388 -63.363 1.00 60.17 C ANISOU 2965 CB ASP A 370 6654 8790 7418 -811 391 611 C ATOM 2966 CG ASP A 370 -12.649 -6.810 -62.782 1.00 63.05 C ANISOU 2966 CG ASP A 370 6928 9117 7909 -924 199 656 C ATOM 2967 OD1 ASP A 370 -12.097 -5.868 -63.388 1.00 71.70 O ANISOU 2967 OD1 ASP A 370 8014 10246 8983 -1247 62 803 O ATOM 2968 OD2 ASP A 370 -12.190 -7.298 -61.729 1.00 62.28 O ANISOU 2968 OD2 ASP A 370 6768 8961 7934 -694 185 545 O ATOM 2969 N GLU A 371 -16.772 -7.043 -65.325 1.00 63.12 N ANISOU 2969 N GLU A 371 7397 9149 7435 -917 532 742 N ATOM 2970 CA GLU A 371 -17.620 -7.806 -66.242 1.00 64.04 C ANISOU 2970 CA GLU A 371 7486 9417 7430 -909 802 699 C ATOM 2971 C GLU A 371 -17.384 -7.458 -67.710 1.00 75.56 C ANISOU 2971 C GLU A 371 8846 11082 8781 -1302 896 821 C ATOM 2972 O GLU A 371 -17.431 -8.335 -68.575 1.00 84.98 O ANISOU 2972 O GLU A 371 9945 12357 9987 -1254 1106 706 O ATOM 2973 CB GLU A 371 -19.096 -7.584 -65.908 1.00 62.80 C ANISOU 2973 CB GLU A 371 7622 9040 7198 -679 709 702 C ATOM 2974 CG GLU A 371 -19.525 -8.123 -64.558 1.00 63.51 C ANISOU 2974 CG GLU A 371 7809 8948 7376 -263 670 565 C ATOM 2975 CD GLU A 371 -20.978 -7.817 -64.254 1.00 64.91 C ANISOU 2975 CD GLU A 371 8284 8902 7477 -52 563 581 C ATOM 2976 OE1 GLU A 371 -21.615 -7.112 -65.064 1.00 66.41 O ANISOU 2976 OE1 GLU A 371 8611 9068 7552 -238 499 707 O ATOM 2977 OE2 GLU A 371 -21.482 -8.280 -63.208 1.00 59.54 O ANISOU 2977 OE2 GLU A 371 7699 8070 6852 299 543 469 O ATOM 2978 N HIS A 372 -17.098 -6.185 -67.971 1.00 78.76 N ANISOU 2978 N HIS A 372 9352 11402 9170 -1560 647 986 N ATOM 2979 CA HIS A 372 -16.888 -5.671 -69.325 1.00 87.60 C ANISOU 2979 CA HIS A 372 10417 12670 10198 -1922 680 1107 C ATOM 2980 C HIS A 372 -17.927 -6.170 -70.330 1.00 88.86 C ANISOU 2980 C HIS A 372 10668 12789 10306 -1767 811 997 C ATOM 2981 O HIS A 372 -17.622 -6.984 -71.202 1.00 93.11 O ANISOU 2981 O HIS A 372 11087 13381 10907 -1690 971 865 O ATOM 2982 CB HIS A 372 -15.482 -6.028 -69.809 1.00 92.77 C ANISOU 2982 CB HIS A 372 10826 13465 10957 -2019 763 1028 C ATOM 2983 CG HIS A 372 -14.397 -5.272 -69.108 1.00 93.63 C ANISOU 2983 CG HIS A 372 10844 13592 11140 -2235 580 1155 C ATOM 2984 ND1 HIS A 372 -14.646 -4.420 -68.053 1.00 91.45 N ANISOU 2984 ND1 HIS A 372 10783 13046 10916 -2116 277 1211 N ATOM 2985 CD2 HIS A 372 -13.059 -5.232 -69.313 1.00 99.23 C ANISOU 2985 CD2 HIS A 372 11371 14395 11938 -2365 574 1137 C ATOM 2986 CE1 HIS A 372 -13.510 -3.892 -67.637 1.00 86.32 C ANISOU 2986 CE1 HIS A 372 10047 12378 10373 -2239 116 1258 C ATOM 2987 NE2 HIS A 372 -12.531 -4.368 -68.385 1.00 91.68 N ANISOU 2987 NE2 HIS A 372 10447 13326 11063 -2461 313 1249 N ATOM 2988 N ARG A 378 -23.729 -3.958 -67.893 1.00 69.86 N ANISOU 2988 N ARG A 378 8084 10035 8426 1709 -1094 -1876 N ATOM 2989 CA ARG A 378 -23.095 -3.682 -66.610 1.00 72.78 C ANISOU 2989 CA ARG A 378 8633 10424 8596 1627 -980 -1755 C ATOM 2990 C ARG A 378 -23.095 -2.190 -66.302 1.00 73.31 C ANISOU 2990 C ARG A 378 8541 10586 8729 1328 -961 -1627 C ATOM 2991 O ARG A 378 -22.961 -1.789 -65.145 1.00 69.69 O ANISOU 2991 O ARG A 378 8236 10011 8232 1174 -819 -1551 O ATOM 2992 CB ARG A 378 -21.660 -4.211 -66.590 1.00 74.75 C ANISOU 2992 CB ARG A 378 8924 11103 8377 1899 -1110 -1651 C ATOM 2993 CG ARG A 378 -20.733 -3.484 -67.546 1.00 75.74 C ANISOU 2993 CG ARG A 378 8763 11713 8303 1924 -1285 -1496 C ATOM 2994 CD ARG A 378 -19.306 -3.444 -67.031 1.00 67.99 C ANISOU 2994 CD ARG A 378 7868 10920 7044 1933 -1182 -1270 C ATOM 2995 NE ARG A 378 -18.633 -2.216 -67.446 1.00 76.17 N ANISOU 2995 NE ARG A 378 8746 12082 8112 1687 -1117 -1054 N ATOM 2996 CZ ARG A 378 -17.377 -1.910 -67.142 1.00 73.35 C ANISOU 2996 CZ ARG A 378 8409 11849 7612 1635 -1043 -868 C ATOM 2997 NH1 ARG A 378 -16.649 -2.747 -66.422 1.00 69.48 N ANISOU 2997 NH1 ARG A 378 8062 11390 6946 1793 -1010 -848 N ATOM 2998 NH2 ARG A 378 -16.847 -0.769 -67.560 1.00 75.14 N ANISOU 2998 NH2 ARG A 378 8526 12129 7896 1428 -1005 -713 N ATOM 2999 N SER A 379 -23.230 -1.370 -67.342 1.00 72.17 N ANISOU 2999 N SER A 379 8088 10658 8677 1251 -1105 -1603 N ATOM 3000 CA SER A 379 -23.214 0.080 -67.178 1.00 66.21 C ANISOU 3000 CA SER A 379 7153 10022 7981 974 -1106 -1480 C ATOM 3001 C SER A 379 -24.386 0.556 -66.326 1.00 58.97 C ANISOU 3001 C SER A 379 6362 8610 7432 673 -877 -1536 C ATOM 3002 O SER A 379 -24.272 1.541 -65.593 1.00 57.74 O ANISOU 3002 O SER A 379 6202 8462 7275 446 -803 -1426 O ATOM 3003 CB SER A 379 -23.237 0.773 -68.542 1.00 57.19 C ANISOU 3003 CB SER A 379 5780 9040 6908 912 -1186 -1387 C ATOM 3004 OG SER A 379 -24.317 0.305 -69.333 1.00 72.38 O ANISOU 3004 OG SER A 379 7642 10729 9129 943 -1201 -1564 O ATOM 3005 N ALA A 380 -25.504 -0.160 -66.409 1.00 62.43 N ANISOU 3005 N ALA A 380 6920 8618 8183 675 -766 -1707 N ATOM 3006 CA ALA A 380 -26.689 0.176 -65.628 1.00 60.81 C ANISOU 3006 CA ALA A 380 6848 7914 8345 407 -543 -1773 C ATOM 3007 C ALA A 380 -26.435 -0.026 -64.138 1.00 57.22 C ANISOU 3007 C ALA A 380 6695 7263 7783 352 -358 -1722 C ATOM 3008 O ALA A 380 -26.719 0.858 -63.319 1.00 53.95 O ANISOU 3008 O ALA A 380 6319 6698 7481 93 -230 -1655 O ATOM 3009 CB ALA A 380 -27.880 -0.664 -66.080 1.00 52.49 C ANISOU 3009 CB ALA A 380 5860 6457 7625 452 -474 -1969 C ATOM 3010 N LYS A 381 -25.878 -1.187 -63.798 1.00 57.56 N ANISOU 3010 N LYS A 381 6949 7319 7601 603 -349 -1753 N ATOM 3011 CA LYS A 381 -25.577 -1.514 -62.411 1.00 60.71 C ANISOU 3011 CA LYS A 381 7647 7546 7876 588 -180 -1711 C ATOM 3012 C LYS A 381 -24.542 -0.549 -61.846 1.00 49.57 C ANISOU 3012 C LYS A 381 6177 6479 6180 491 -223 -1519 C ATOM 3013 O LYS A 381 -24.613 -0.159 -60.676 1.00 48.20 O ANISOU 3013 O LYS A 381 6171 6115 6028 321 -60 -1462 O ATOM 3014 CB LYS A 381 -25.077 -2.958 -62.300 1.00 58.84 C ANISOU 3014 CB LYS A 381 7621 7315 7421 902 -189 -1776 C ATOM 3015 CG LYS A 381 -26.051 -3.985 -62.859 1.00 71.73 C ANISOU 3015 CG LYS A 381 9321 8615 9317 1016 -153 -1968 C ATOM 3016 CD LYS A 381 -25.592 -5.413 -62.593 1.00 71.63 C ANISOU 3016 CD LYS A 381 9551 8569 9098 1310 -136 -2031 C ATOM 3017 CE LYS A 381 -26.654 -6.415 -63.028 1.00 85.18 C ANISOU 3017 CE LYS A 381 11347 9920 11096 1355 -65 -2161 C ATOM 3018 NZ LYS A 381 -26.307 -7.812 -62.641 1.00 94.21 N ANISOU 3018 NZ LYS A 381 12712 11013 12068 1518 6 -2107 N ATOM 3019 N LEU A 382 -23.612 -0.131 -62.700 1.00 47.80 N ANISOU 3019 N LEU A 382 5706 6757 5701 593 -443 -1418 N ATOM 3020 CA LEU A 382 -22.589 0.825 -62.304 1.00 47.92 C ANISOU 3020 CA LEU A 382 5630 7139 5439 508 -509 -1231 C ATOM 3021 C LEU A 382 -23.199 2.187 -62.007 1.00 46.33 C ANISOU 3021 C LEU A 382 5313 6812 5479 162 -430 -1174 C ATOM 3022 O LEU A 382 -22.919 2.782 -60.964 1.00 43.83 O ANISOU 3022 O LEU A 382 5103 6463 5087 4 -327 -1072 O ATOM 3023 CB LEU A 382 -21.517 0.956 -63.390 1.00 49.98 C ANISOU 3023 CB LEU A 382 5634 7963 5393 699 -770 -1142 C ATOM 3024 CG LEU A 382 -20.491 -0.178 -63.461 1.00 53.92 C ANISOU 3024 CG LEU A 382 6250 8712 5526 1036 -863 -1131 C ATOM 3025 CD1 LEU A 382 -19.451 0.089 -64.539 1.00 55.31 C ANISOU 3025 CD1 LEU A 382 6169 9390 5458 1179 -1078 -1009 C ATOM 3026 CD2 LEU A 382 -19.824 -0.371 -62.107 1.00 51.09 C ANISOU 3026 CD2 LEU A 382 6153 8325 4935 1040 -739 -1046 C ATOM 3027 N PHE A 383 -24.049 2.671 -62.908 1.00 44.28 N ANISOU 3027 N PHE A 383 4840 6471 5512 46 -475 -1242 N ATOM 3028 CA PHE A 383 -24.664 3.974 -62.709 1.00 37.98 C ANISOU 3028 CA PHE A 383 3919 5558 4953 -280 -406 -1191 C ATOM 3029 C PHE A 383 -25.537 3.980 -61.463 1.00 44.76 C ANISOU 3029 C PHE A 383 5042 5908 6058 -482 -146 -1240 C ATOM 3030 O PHE A 383 -25.543 4.953 -60.707 1.00 41.14 O ANISOU 3030 O PHE A 383 4595 5407 5629 -719 -59 -1142 O ATOM 3031 CB PHE A 383 -25.497 4.376 -63.925 1.00 39.48 C ANISOU 3031 CB PHE A 383 3847 5723 5432 -353 -492 -1272 C ATOM 3032 CG PHE A 383 -24.680 4.722 -65.135 1.00 42.97 C ANISOU 3032 CG PHE A 383 3985 6684 5659 -221 -746 -1198 C ATOM 3033 CD1 PHE A 383 -23.363 5.130 -65.010 1.00 44.20 C ANISOU 3033 CD1 PHE A 383 4066 7295 5432 -151 -870 -1033 C ATOM 3034 CD2 PHE A 383 -25.231 4.639 -66.402 1.00 47.96 C ANISOU 3034 CD2 PHE A 383 4423 7332 6468 -162 -849 -1280 C ATOM 3035 CE1 PHE A 383 -22.613 5.448 -66.127 1.00 47.18 C ANISOU 3035 CE1 PHE A 383 4427 7836 5663 -20 -937 -825 C ATOM 3036 CE2 PHE A 383 -24.485 4.955 -67.520 1.00 51.12 C ANISOU 3036 CE2 PHE A 383 4828 7950 6646 -32 -921 -1035 C ATOM 3037 CZ PHE A 383 -23.177 5.359 -67.383 1.00 43.56 C ANISOU 3037 CZ PHE A 383 3928 7243 5381 24 -955 -829 C ATOM 3038 N PHE A 384 -26.235 2.874 -61.222 1.00 44.83 N ANISOU 3038 N PHE A 384 5269 5534 6230 -381 -23 -1388 N ATOM 3039 CA PHE A 384 -27.127 2.806 -60.074 1.00 41.76 C ANISOU 3039 CA PHE A 384 5135 4639 6092 -560 227 -1444 C ATOM 3040 C PHE A 384 -26.335 2.794 -58.771 1.00 39.25 C ANISOU 3040 C PHE A 384 5044 4356 5513 -564 325 -1335 C ATOM 3041 O PHE A 384 -26.577 3.611 -57.866 1.00 46.20 O ANISOU 3041 O PHE A 384 5995 5075 6486 -807 459 -1266 O ATOM 3042 CB PHE A 384 -28.022 1.567 -60.164 1.00 42.80 C ANISOU 3042 CB PHE A 384 5445 4368 6450 -433 328 -1629 C ATOM 3043 CG PHE A 384 -29.003 1.448 -59.034 1.00 38.75 C ANISOU 3043 CG PHE A 384 5179 3392 6154 -582 559 -1614 C ATOM 3044 CD1 PHE A 384 -30.179 2.178 -59.041 1.00 45.17 C ANISOU 3044 CD1 PHE A 384 5890 4168 7104 -716 572 -1421 C ATOM 3045 CD2 PHE A 384 -28.747 0.610 -57.962 1.00 42.52 C ANISOU 3045 CD2 PHE A 384 5946 3729 6481 -469 666 -1588 C ATOM 3046 CE1 PHE A 384 -31.081 2.075 -57.998 1.00 40.60 C ANISOU 3046 CE1 PHE A 384 5463 3456 6507 -729 652 -1260 C ATOM 3047 CE2 PHE A 384 -29.648 0.503 -56.917 1.00 41.90 C ANISOU 3047 CE2 PHE A 384 5989 3490 6440 -522 739 -1401 C ATOM 3048 CZ PHE A 384 -30.816 1.235 -56.937 1.00 39.46 C ANISOU 3048 CZ PHE A 384 5548 3185 6261 -647 721 -1258 C ATOM 3049 N ASP A 385 -25.368 1.884 -58.693 1.00 40.69 N ANISOU 3049 N ASP A 385 5336 4760 5363 -291 253 -1315 N ATOM 3050 CA ASP A 385 -24.582 1.734 -57.476 1.00 49.06 C ANISOU 3050 CA ASP A 385 6625 5857 6159 -262 342 -1221 C ATOM 3051 C ASP A 385 -23.755 2.973 -57.165 1.00 43.69 C ANISOU 3051 C ASP A 385 5811 5518 5273 -417 274 -1036 C ATOM 3052 O ASP A 385 -23.593 3.329 -56.004 1.00 41.60 O ANISOU 3052 O ASP A 385 5714 5136 4954 -548 409 -962 O ATOM 3053 CB ASP A 385 -23.659 0.516 -57.578 1.00 49.70 C ANISOU 3053 CB ASP A 385 6825 6150 5909 76 258 -1234 C ATOM 3054 CG ASP A 385 -24.374 -0.785 -57.282 1.00 59.40 C ANISOU 3054 CG ASP A 385 8310 6961 7298 209 399 -1397 C ATOM 3055 OD1 ASP A 385 -25.275 -0.785 -56.415 1.00 63.96 O ANISOU 3055 OD1 ASP A 385 9078 7084 8140 41 612 -1457 O ATOM 3056 OD2 ASP A 385 -24.031 -1.808 -57.910 1.00 68.19 O ANISOU 3056 OD2 ASP A 385 9437 8202 8272 483 298 -1464 O ATOM 3057 N LEU A 386 -23.245 3.636 -58.197 1.00 43.07 N ANISOU 3057 N LEU A 386 5428 5853 5083 -403 68 -962 N ATOM 3058 CA LEU A 386 -22.439 4.831 -57.977 1.00 45.61 C ANISOU 3058 CA LEU A 386 5604 6520 5207 -547 -10 -785 C ATOM 3059 C LEU A 386 -23.319 6.022 -57.623 1.00 39.28 C ANISOU 3059 C LEU A 386 4737 5471 4714 -893 106 -764 C ATOM 3060 O LEU A 386 -22.925 6.885 -56.823 1.00 37.97 O ANISOU 3060 O LEU A 386 4598 5377 4452 -1066 155 -637 O ATOM 3061 CB LEU A 386 -21.578 5.132 -59.203 1.00 47.89 C ANISOU 3061 CB LEU A 386 5587 7340 5267 -410 -271 -709 C ATOM 3062 CG LEU A 386 -20.481 4.083 -59.415 1.00 47.81 C ANISOU 3062 CG LEU A 386 5644 7639 4882 -74 -393 -691 C ATOM 3063 CD1 LEU A 386 -19.654 4.395 -60.641 1.00 51.26 C ANISOU 3063 CD1 LEU A 386 5777 8598 5102 61 -651 -614 C ATOM 3064 CD2 LEU A 386 -19.599 3.977 -58.182 1.00 50.82 C ANISOU 3064 CD2 LEU A 386 6246 8091 4970 -48 -316 -583 C ATOM 3065 N ALA A 387 -24.523 6.051 -58.192 1.00 35.60 N ANISOU 3065 N ALA A 387 4197 4706 4623 -993 155 -890 N ATOM 3066 CA ALA A 387 -25.487 7.082 -57.834 1.00 34.16 C ANISOU 3066 CA ALA A 387 3977 4236 4766 -1317 285 -887 C ATOM 3067 C ALA A 387 -25.816 6.993 -56.351 1.00 32.35 C ANISOU 3067 C ALA A 387 4058 3626 4607 -1446 521 -883 C ATOM 3068 O ALA A 387 -25.759 7.994 -55.638 1.00 31.42 O ANISOU 3068 O ALA A 387 3946 3495 4498 -1674 591 -778 O ATOM 3069 CB ALA A 387 -26.756 6.955 -58.666 1.00 38.53 C ANISOU 3069 CB ALA A 387 4428 4503 5710 -1377 309 -1037 C ATOM 3070 N LEU A 388 -26.158 5.798 -55.878 1.00 26.59 N ANISOU 3070 N LEU A 388 3087 3155 3863 361 -551 522 N ATOM 3071 CA LEU A 388 -26.427 5.642 -54.451 1.00 32.34 C ANISOU 3071 CA LEU A 388 3837 3887 4564 318 -555 508 C ATOM 3072 C LEU A 388 -25.180 5.836 -53.581 1.00 36.98 C ANISOU 3072 C LEU A 388 4419 4530 5103 315 -550 393 C ATOM 3073 O LEU A 388 -25.266 6.354 -52.466 1.00 32.10 O ANISOU 3073 O LEU A 388 3791 3916 4491 274 -487 351 O ATOM 3074 CB LEU A 388 -27.043 4.271 -54.175 1.00 39.39 C ANISOU 3074 CB LEU A 388 4812 4782 5372 316 -644 544 C ATOM 3075 CG LEU A 388 -28.442 4.063 -54.753 1.00 35.22 C ANISOU 3075 CG LEU A 388 4312 4221 4849 287 -590 599 C ATOM 3076 CD1 LEU A 388 -29.042 2.766 -54.245 1.00 37.82 C ANISOU 3076 CD1 LEU A 388 4712 4569 5088 274 -629 595 C ATOM 3077 CD2 LEU A 388 -29.336 5.239 -54.410 1.00 30.97 C ANISOU 3077 CD2 LEU A 388 3715 3629 4423 250 -507 673 C ATOM 3078 N SER A 389 -24.022 5.434 -54.094 1.00 29.02 N ANISOU 3078 N SER A 389 3420 3562 4045 362 -616 344 N ATOM 3079 CA SER A 389 -22.786 5.510 -53.321 1.00 35.32 C ANISOU 3079 CA SER A 389 4219 4413 4787 362 -621 237 C ATOM 3080 C SER A 389 -22.317 6.948 -53.134 1.00 35.29 C ANISOU 3080 C SER A 389 4141 4410 4857 337 -498 179 C ATOM 3081 O SER A 389 -21.560 7.245 -52.208 1.00 28.87 O ANISOU 3081 O SER A 389 3324 3627 4018 321 -474 93 O ATOM 3082 CB SER A 389 -21.679 4.687 -53.984 1.00 37.85 C ANISOU 3082 CB SER A 389 4573 4781 5029 422 -728 210 C ATOM 3083 OG SER A 389 -21.011 5.425 -54.992 1.00 36.06 O ANISOU 3083 OG SER A 389 4288 4561 4851 456 -690 202 O ATOM 3084 N SER A 390 -22.760 7.838 -54.019 1.00 32.66 N ANISOU 3084 N SER A 390 3750 4044 4616 336 -421 224 N ATOM 3085 CA SER A 390 -22.398 9.246 -53.899 1.00 29.04 C ANISOU 3085 CA SER A 390 3218 3584 4234 311 -304 175 C ATOM 3086 C SER A 390 -22.953 9.855 -52.608 1.00 26.88 C ANISOU 3086 C SER A 390 2940 3295 3979 253 -229 151 C ATOM 3087 O SER A 390 -22.419 10.844 -52.107 1.00 27.09 O ANISOU 3087 O SER A 390 2922 3330 4041 233 -155 86 O ATOM 3088 CB SER A 390 -22.892 10.036 -55.114 1.00 27.95 C ANISOU 3088 CB SER A 390 3017 3412 4190 321 -235 234 C ATOM 3089 OG SER A 390 -24.300 10.172 -55.111 1.00 25.45 O ANISOU 3089 OG SER A 390 2707 3048 3916 287 -189 311 O ATOM 3090 N PHE A 391 -24.020 9.260 -52.076 1.00 27.64 N ANISOU 3090 N PHE A 391 3083 3367 4052 232 -252 208 N ATOM 3091 CA PHE A 391 -24.672 9.757 -50.857 1.00 28.81 C ANISOU 3091 CA PHE A 391 3233 3501 4214 187 -188 201 C ATOM 3092 C PHE A 391 -24.090 9.174 -49.562 1.00 27.90 C ANISOU 3092 C PHE A 391 3161 3419 4023 189 -237 128 C ATOM 3093 O PHE A 391 -24.580 9.462 -48.456 1.00 31.81 O ANISOU 3093 O PHE A 391 3661 3904 4520 163 -196 120 O ATOM 3094 CB PHE A 391 -26.178 9.475 -50.913 1.00 29.49 C ANISOU 3094 CB PHE A 391 3342 3544 4317 166 -181 309 C ATOM 3095 CG PHE A 391 -26.923 10.347 -51.888 1.00 23.28 C ANISOU 3095 CG PHE A 391 2509 2721 3617 151 -97 373 C ATOM 3096 CD1 PHE A 391 -27.018 9.990 -53.222 1.00 22.71 C ANISOU 3096 CD1 PHE A 391 2432 2634 3564 183 -132 425 C ATOM 3097 CD2 PHE A 391 -27.528 11.526 -51.468 1.00 25.56 C ANISOU 3097 CD2 PHE A 391 2760 2990 3963 110 17 381 C ATOM 3098 CE1 PHE A 391 -27.699 10.788 -54.123 1.00 22.71 C ANISOU 3098 CE1 PHE A 391 2386 2599 3643 173 -48 479 C ATOM 3099 CE2 PHE A 391 -28.214 12.332 -52.364 1.00 18.69 C ANISOU 3099 CE2 PHE A 391 1847 2089 3167 95 100 436 C ATOM 3100 CZ PHE A 391 -28.299 11.961 -53.693 1.00 19.38 C ANISOU 3100 CZ PHE A 391 1926 2160 3276 126 71 483 C ATOM 3101 N GLN A 392 -23.053 8.353 -49.693 1.00 26.15 N ANISOU 3101 N GLN A 392 2970 3237 3731 222 -323 75 N ATOM 3102 CA GLN A 392 -22.495 7.653 -48.537 1.00 29.59 C ANISOU 3102 CA GLN A 392 3451 3707 4085 228 -376 4 C ATOM 3103 C GLN A 392 -21.918 8.594 -47.480 1.00 29.32 C ANISOU 3103 C GLN A 392 3386 3682 4072 210 -300 -87 C ATOM 3104 O GLN A 392 -21.991 8.298 -46.286 1.00 30.02 O ANISOU 3104 O GLN A 392 3504 3780 4124 206 -307 -124 O ATOM 3105 CB GLN A 392 -21.418 6.666 -48.992 1.00 30.08 C ANISOU 3105 CB GLN A 392 3552 3815 4063 268 -479 -37 C ATOM 3106 CG GLN A 392 -21.979 5.355 -49.528 1.00 37.12 C ANISOU 3106 CG GLN A 392 4501 4705 4898 290 -587 39 C ATOM 3107 CD GLN A 392 -20.901 4.445 -50.088 1.00 39.42 C ANISOU 3107 CD GLN A 392 4831 5044 5102 334 -690 3 C ATOM 3108 OE1 GLN A 392 -19.758 4.858 -50.257 1.00 38.31 O ANISOU 3108 OE1 GLN A 392 4669 4937 4951 350 -675 -66 O ATOM 3109 NE2 GLN A 392 -21.265 3.201 -50.382 1.00 39.15 N ANISOU 3109 NE2 GLN A 392 4857 5016 5003 357 -799 56 N ATOM 3110 N GLY A 393 -21.372 9.729 -47.905 1.00 29.17 N ANISOU 3110 N GLY A 393 3307 3658 4118 205 -228 -120 N ATOM 3111 CA GLY A 393 -20.803 10.667 -46.956 1.00 23.61 C ANISOU 3111 CA GLY A 393 2572 2958 3440 191 -161 -205 C ATOM 3112 C GLY A 393 -21.906 11.292 -46.132 1.00 27.54 C ANISOU 3112 C GLY A 393 3061 3421 3981 162 -91 -169 C ATOM 3113 O GLY A 393 -21.762 11.515 -44.923 1.00 27.88 O ANISOU 3113 O GLY A 393 3113 3468 4012 161 -70 -226 O ATOM 3114 N LEU A 394 -23.037 11.533 -46.787 1.00 28.17 N ANISOU 3114 N LEU A 394 3126 3467 4108 144 -57 -72 N ATOM 3115 CA LEU A 394 -24.216 12.024 -46.097 1.00 25.09 C ANISOU 3115 CA LEU A 394 2736 3047 3750 118 3 -19 C ATOM 3116 C LEU A 394 -24.686 10.986 -45.093 1.00 27.49 C ANISOU 3116 C LEU A 394 3100 3359 3987 129 -59 -3 C ATOM 3117 O LEU A 394 -25.006 11.320 -43.950 1.00 30.65 O ANISOU 3117 O LEU A 394 3505 3755 4388 127 -25 -19 O ATOM 3118 CB LEU A 394 -25.331 12.342 -47.095 1.00 26.36 C ANISOU 3118 CB LEU A 394 2878 3174 3965 98 44 88 C ATOM 3119 CG LEU A 394 -26.714 12.675 -46.527 1.00 24.16 C ANISOU 3119 CG LEU A 394 2609 2866 3707 72 96 168 C ATOM 3120 CD1 LEU A 394 -26.650 13.925 -45.678 1.00 28.10 C ANISOU 3120 CD1 LEU A 394 3073 3360 4242 57 183 122 C ATOM 3121 CD2 LEU A 394 -27.728 12.842 -47.645 1.00 24.47 C ANISOU 3121 CD2 LEU A 394 2634 2873 3790 53 128 271 C ATOM 3122 N LEU A 395 -24.679 9.717 -45.502 1.00 28.58 N ANISOU 3122 N LEU A 395 3282 3511 4067 147 -153 26 N ATOM 3123 CA LEU A 395 -25.147 8.659 -44.608 1.00 26.35 C ANISOU 3123 CA LEU A 395 3052 3237 3721 159 -218 46 C ATOM 3124 C LEU A 395 -24.264 8.524 -43.373 1.00 28.29 C ANISOU 3124 C LEU A 395 3313 3515 3920 178 -228 -63 C ATOM 3125 O LEU A 395 -24.764 8.355 -42.259 1.00 32.25 O ANISOU 3125 O LEU A 395 3832 4014 4406 185 -224 -59 O ATOM 3126 CB LEU A 395 -25.208 7.320 -45.337 1.00 30.94 C ANISOU 3126 CB LEU A 395 3679 3829 4247 175 -325 92 C ATOM 3127 CG LEU A 395 -25.638 6.152 -44.446 1.00 27.15 C ANISOU 3127 CG LEU A 395 3253 3363 3701 189 -400 112 C ATOM 3128 CD1 LEU A 395 -27.078 6.333 -43.990 1.00 31.80 C ANISOU 3128 CD1 LEU A 395 3841 3916 4327 171 -364 214 C ATOM 3129 CD2 LEU A 395 -25.455 4.825 -45.157 1.00 31.15 C ANISOU 3129 CD2 LEU A 395 3806 3886 4143 209 -517 138 C ATOM 3130 N VAL A 396 -22.953 8.616 -43.568 1.00 29.28 N ANISOU 3130 N VAL A 396 3430 3669 4025 190 -241 -159 N ATOM 3131 CA VAL A 396 -22.024 8.518 -42.451 1.00 30.63 C ANISOU 3131 CA VAL A 396 3615 3869 4153 209 -247 -270 C ATOM 3132 C VAL A 396 -22.189 9.709 -41.510 1.00 28.19 C ANISOU 3132 C VAL A 396 3271 3539 3902 203 -157 -303 C ATOM 3133 O VAL A 396 -22.219 9.547 -40.281 1.00 27.40 O ANISOU 3133 O VAL A 396 3189 3444 3777 223 -155 -345 O ATOM 3134 CB VAL A 396 -20.561 8.444 -42.941 1.00 28.84 C ANISOU 3134 CB VAL A 396 3387 3679 3894 222 -276 -359 C ATOM 3135 CG1 VAL A 396 -19.605 8.575 -41.777 1.00 30.34 C ANISOU 3135 CG1 VAL A 396 3584 3891 4053 239 -264 -478 C ATOM 3136 CG2 VAL A 396 -20.319 7.142 -43.689 1.00 27.32 C ANISOU 3136 CG2 VAL A 396 3241 3516 3625 239 -379 -335 C ATOM 3137 N ALA A 397 -22.328 10.899 -42.093 1.00 26.94 N ANISOU 3137 N ALA A 397 3060 3354 3820 181 -83 -282 N ATOM 3138 CA ALA A 397 -22.496 12.106 -41.292 1.00 28.05 C ANISOU 3138 CA ALA A 397 3168 3473 4017 176 0 -309 C ATOM 3139 C ALA A 397 -23.782 12.048 -40.476 1.00 33.62 C ANISOU 3139 C ALA A 397 3891 4158 4724 178 18 -235 C ATOM 3140 O ALA A 397 -23.824 12.520 -39.341 1.00 35.80 O ANISOU 3140 O ALA A 397 4165 4430 5007 197 51 -273 O ATOM 3141 CB ALA A 397 -22.490 13.336 -42.178 1.00 29.01 C ANISOU 3141 CB ALA A 397 3230 3573 4218 149 72 -289 C ATOM 3142 N VAL A 398 -24.820 11.439 -41.045 1.00 28.12 N ANISOU 3142 N VAL A 398 3214 3451 4020 165 -8 -127 N ATOM 3143 CA VAL A 398 -26.092 11.330 -40.345 1.00 29.46 C ANISOU 3143 CA VAL A 398 3401 3603 4188 168 4 -41 C ATOM 3144 C VAL A 398 -26.024 10.291 -39.229 1.00 34.55 C ANISOU 3144 C VAL A 398 4088 4271 4769 205 -58 -70 C ATOM 3145 O VAL A 398 -26.458 10.541 -38.103 1.00 34.63 O ANISOU 3145 O VAL A 398 4101 4277 4780 229 -33 -67 O ATOM 3146 CB VAL A 398 -27.241 10.968 -41.314 1.00 26.57 C ANISOU 3146 CB VAL A 398 3044 3216 3836 142 -7 89 C ATOM 3147 CG1 VAL A 398 -28.476 10.524 -40.543 1.00 26.95 C ANISOU 3147 CG1 VAL A 398 3120 3254 3867 152 -19 182 C ATOM 3148 CG2 VAL A 398 -27.565 12.145 -42.220 1.00 23.73 C ANISOU 3148 CG2 VAL A 398 2639 2830 3547 108 75 126 C ATOM 3149 N LEU A 399 -25.467 9.128 -39.546 1.00 30.94 N ANISOU 3149 N LEU A 399 3663 3839 4253 214 -141 -97 N ATOM 3150 CA LEU A 399 -25.393 8.035 -38.583 1.00 30.44 C ANISOU 3150 CA LEU A 399 3640 3802 4124 248 -205 -124 C ATOM 3151 C LEU A 399 -24.471 8.314 -37.392 1.00 35.60 C ANISOU 3151 C LEU A 399 4291 4476 4761 282 -184 -248 C ATOM 3152 O LEU A 399 -24.789 7.935 -36.265 1.00 36.34 O ANISOU 3152 O LEU A 399 4400 4576 4830 316 -194 -255 O ATOM 3153 CB LEU A 399 -24.945 6.753 -39.288 1.00 31.06 C ANISOU 3153 CB LEU A 399 3755 3907 4138 248 -301 -128 C ATOM 3154 CG LEU A 399 -26.034 5.734 -39.635 1.00 30.82 C ANISOU 3154 CG LEU A 399 3756 3869 4087 244 -368 -9 C ATOM 3155 CD1 LEU A 399 -27.203 6.393 -40.346 1.00 29.18 C ANISOU 3155 CD1 LEU A 399 3524 3617 3946 214 -320 112 C ATOM 3156 CD2 LEU A 399 -25.461 4.609 -40.481 1.00 30.81 C ANISOU 3156 CD2 LEU A 399 3791 3893 4024 246 -465 -20 C ATOM 3157 N TYR A 400 -23.346 8.986 -37.626 1.00 29.70 N ANISOU 3157 N TYR A 400 3522 3735 4029 276 -154 -344 N ATOM 3158 CA TYR A 400 -22.380 9.207 -36.546 1.00 31.49 C ANISOU 3158 CA TYR A 400 3749 3977 4238 309 -139 -468 C ATOM 3159 C TYR A 400 -22.536 10.534 -35.811 1.00 34.06 C ANISOU 3159 C TYR A 400 4039 4274 4629 321 -57 -489 C ATOM 3160 O TYR A 400 -21.994 10.706 -34.720 1.00 41.82 O ANISOU 3160 O TYR A 400 5024 5261 5603 359 -44 -577 O ATOM 3161 CB TYR A 400 -20.950 9.113 -37.086 1.00 32.39 C ANISOU 3161 CB TYR A 400 3864 4117 4324 303 -161 -568 C ATOM 3162 CG TYR A 400 -20.476 7.696 -37.272 1.00 28.02 C ANISOU 3162 CG TYR A 400 3360 3606 3681 313 -249 -592 C ATOM 3163 CD1 TYR A 400 -20.813 6.711 -36.358 1.00 27.78 C ANISOU 3163 CD1 TYR A 400 3367 3594 3595 342 -292 -597 C ATOM 3164 CD2 TYR A 400 -19.709 7.338 -38.369 1.00 28.44 C ANISOU 3164 CD2 TYR A 400 3422 3682 3703 297 -292 -607 C ATOM 3165 CE1 TYR A 400 -20.388 5.413 -36.523 1.00 27.31 C ANISOU 3165 CE1 TYR A 400 3353 3575 3448 350 -375 -621 C ATOM 3166 CE2 TYR A 400 -19.280 6.042 -38.543 1.00 24.30 C ANISOU 3166 CE2 TYR A 400 2948 3199 3087 309 -378 -627 C ATOM 3167 CZ TYR A 400 -19.621 5.085 -37.620 1.00 26.26 C ANISOU 3167 CZ TYR A 400 3233 3465 3278 332 -419 -636 C ATOM 3168 OH TYR A 400 -19.197 3.793 -37.804 1.00 25.13 O ANISOU 3168 OH TYR A 400 3141 3365 3040 342 -506 -657 O ATOM 3169 N CYS A 401 -23.262 11.475 -36.399 1.00 32.83 N ANISOU 3169 N CYS A 401 3851 4087 4536 291 -3 -411 N ATOM 3170 CA CYS A 401 -23.341 12.805 -35.807 1.00 34.42 C ANISOU 3170 CA CYS A 401 4019 4263 4796 300 71 -432 C ATOM 3171 C CYS A 401 -24.773 13.267 -35.552 1.00 35.50 C ANISOU 3171 C CYS A 401 4150 4375 4962 299 111 -317 C ATOM 3172 O CYS A 401 -25.172 13.478 -34.407 1.00 35.80 O ANISOU 3172 O CYS A 401 4196 4409 4999 341 127 -317 O ATOM 3173 CB CYS A 401 -22.625 13.821 -36.698 1.00 31.54 C ANISOU 3173 CB CYS A 401 3611 3887 4485 266 114 -469 C ATOM 3174 SG CYS A 401 -22.548 15.497 -36.015 1.00 39.86 S ANISOU 3174 SG CYS A 401 4624 4911 5611 276 196 -508 S ATOM 3175 N PHE A 402 -25.537 13.430 -36.626 1.00 28.01 N ANISOU 3175 N PHE A 402 3191 3413 4039 255 128 -218 N ATOM 3176 CA PHE A 402 -26.860 14.035 -36.536 1.00 34.56 C ANISOU 3176 CA PHE A 402 4014 4220 4898 245 177 -107 C ATOM 3177 C PHE A 402 -27.863 13.212 -35.724 1.00 32.87 C ANISOU 3177 C PHE A 402 3834 4011 4644 277 142 -28 C ATOM 3178 O PHE A 402 -28.692 13.773 -35.014 1.00 32.03 O ANISOU 3178 O PHE A 402 3726 3893 4551 298 180 29 O ATOM 3179 CB PHE A 402 -27.402 14.281 -37.945 1.00 31.34 C ANISOU 3179 CB PHE A 402 3588 3797 4522 191 201 -24 C ATOM 3180 CG PHE A 402 -26.506 15.144 -38.794 1.00 35.14 C ANISOU 3180 CG PHE A 402 4027 4274 5049 163 240 -89 C ATOM 3181 CD1 PHE A 402 -25.728 16.136 -38.218 1.00 32.19 C ANISOU 3181 CD1 PHE A 402 3626 3897 4706 177 280 -180 C ATOM 3182 CD2 PHE A 402 -26.435 14.959 -40.163 1.00 37.27 C ANISOU 3182 CD2 PHE A 402 4283 4542 5335 129 232 -57 C ATOM 3183 CE1 PHE A 402 -24.901 16.930 -38.991 1.00 26.15 C ANISOU 3183 CE1 PHE A 402 2819 3130 3988 152 312 -235 C ATOM 3184 CE2 PHE A 402 -25.609 15.752 -40.941 1.00 34.54 C ANISOU 3184 CE2 PHE A 402 3893 4195 5036 109 268 -112 C ATOM 3185 CZ PHE A 402 -24.842 16.737 -40.351 1.00 34.93 C ANISOU 3185 CZ PHE A 402 3913 4244 5117 119 308 -199 C ATOM 3186 N LEU A 403 -27.775 11.888 -35.810 1.00 35.71 N ANISOU 3186 N LEU A 403 4224 4389 4955 285 66 -22 N ATOM 3187 CA LEU A 403 -28.662 11.015 -35.041 1.00 31.97 C ANISOU 3187 CA LEU A 403 3780 3923 4445 319 25 53 C ATOM 3188 C LEU A 403 -28.113 10.699 -33.657 1.00 33.31 C ANISOU 3188 C LEU A 403 3960 4112 4584 382 6 -35 C ATOM 3189 O LEU A 403 -28.812 10.116 -32.828 1.00 37.55 O ANISOU 3189 O LEU A 403 4514 4658 5098 423 -20 19 O ATOM 3190 CB LEU A 403 -28.919 9.710 -35.795 1.00 31.84 C ANISOU 3190 CB LEU A 403 3790 3916 4391 299 -53 110 C ATOM 3191 CG LEU A 403 -29.790 9.785 -37.048 1.00 36.43 C ANISOU 3191 CG LEU A 403 4369 4474 5001 248 -45 227 C ATOM 3192 CD1 LEU A 403 -30.099 8.385 -37.556 1.00 27.36 C ANISOU 3192 CD1 LEU A 403 3253 3333 3811 243 -136 286 C ATOM 3193 CD2 LEU A 403 -31.072 10.560 -36.770 1.00 32.91 C ANISOU 3193 CD2 LEU A 403 3913 4004 4588 244 17 339 C ATOM 3194 N ASN A 404 -26.861 11.076 -33.413 1.00 35.58 N ANISOU 3194 N ASN A 404 4237 4409 4874 394 18 -169 N ATOM 3195 CA ASN A 404 -26.199 10.755 -32.156 1.00 33.88 C ANISOU 3195 CA ASN A 404 4033 4211 4629 456 2 -269 C ATOM 3196 C ASN A 404 -26.867 11.450 -30.975 1.00 41.01 C ANISOU 3196 C ASN A 404 4926 5099 5555 511 44 -240 C ATOM 3197 O ASN A 404 -27.181 12.640 -31.042 1.00 45.91 O ANISOU 3197 O ASN A 404 5526 5697 6223 502 103 -213 O ATOM 3198 CB ASN A 404 -24.719 11.135 -32.230 1.00 35.27 C ANISOU 3198 CB ASN A 404 4199 4394 4808 452 12 -414 C ATOM 3199 CG ASN A 404 -23.987 10.870 -30.940 1.00 40.09 C ANISOU 3199 CG ASN A 404 4822 5020 5391 517 2 -526 C ATOM 3200 OD1 ASN A 404 -23.568 11.800 -30.251 1.00 46.93 O ANISOU 3200 OD1 ASN A 404 5671 5870 6291 549 46 -592 O ATOM 3201 ND2 ASN A 404 -23.837 9.595 -30.594 1.00 38.22 N ANISOU 3201 ND2 ASN A 404 4614 4813 5092 539 -57 -548 N ATOM 3202 N LYS A 405 -27.081 10.709 -29.892 1.00 33.08 N ANISOU 3202 N LYS A 405 4750 3234 4583 335 883 -979 N ATOM 3203 CA LYS A 405 -27.812 11.237 -28.746 1.00 34.96 C ANISOU 3203 CA LYS A 405 5075 3724 4483 556 799 -897 C ATOM 3204 C LYS A 405 -27.062 12.347 -28.019 1.00 37.13 C ANISOU 3204 C LYS A 405 5439 4248 4420 546 742 -971 C ATOM 3205 O LYS A 405 -27.666 13.321 -27.586 1.00 31.98 O ANISOU 3205 O LYS A 405 4970 3803 3378 516 710 -823 O ATOM 3206 CB LYS A 405 -28.141 10.111 -27.762 1.00 40.39 C ANISOU 3206 CB LYS A 405 5616 4191 5541 829 1048 -605 C ATOM 3207 CG LYS A 405 -28.897 10.564 -26.521 1.00 45.48 C ANISOU 3207 CG LYS A 405 6460 5155 5666 1197 1132 -225 C ATOM 3208 CD LYS A 405 -29.162 9.402 -25.574 1.00 49.57 C ANISOU 3208 CD LYS A 405 6442 5742 6648 1376 1004 446 C ATOM 3209 CE LYS A 405 -29.824 9.871 -24.289 1.00 63.92 C ANISOU 3209 CE LYS A 405 8333 8110 7843 1593 827 927 C ATOM 3210 NZ LYS A 405 -30.072 8.739 -23.355 1.00 74.19 N ANISOU 3210 NZ LYS A 405 9095 9500 9595 1726 666 1592 N ATOM 3211 N GLU A 406 -25.748 12.198 -27.881 1.00 39.69 N ANISOU 3211 N GLU A 406 5695 4483 4904 575 701 -1100 N ATOM 3212 CA GLU A 406 -24.945 13.205 -27.193 1.00 40.23 C ANISOU 3212 CA GLU A 406 5808 4802 4677 538 656 -1176 C ATOM 3213 C GLU A 406 -24.887 14.515 -27.975 1.00 41.66 C ANISOU 3213 C GLU A 406 6172 5022 4634 359 613 -1171 C ATOM 3214 O GLU A 406 -24.916 15.605 -27.391 1.00 43.12 O ANISOU 3214 O GLU A 406 6457 5392 4534 333 571 -1087 O ATOM 3215 CB GLU A 406 -23.529 12.680 -26.942 1.00 38.88 C ANISOU 3215 CB GLU A 406 5635 4374 4764 599 724 -1270 C ATOM 3216 CG GLU A 406 -23.431 11.606 -25.864 1.00 40.41 C ANISOU 3216 CG GLU A 406 5590 4346 5417 789 1008 -998 C ATOM 3217 CD GLU A 406 -23.937 10.251 -26.325 1.00 50.44 C ANISOU 3217 CD GLU A 406 6447 5262 7455 780 1060 -791 C ATOM 3218 OE1 GLU A 406 -24.216 10.099 -27.534 1.00 49.78 O ANISOU 3218 OE1 GLU A 406 6478 5044 7394 568 1046 -1013 O ATOM 3219 OE2 GLU A 406 -24.053 9.338 -25.477 1.00 48.81 O ANISOU 3219 OE2 GLU A 406 5782 5142 7624 896 911 -229 O ATOM 3220 N VAL A 407 -24.833 14.399 -29.299 1.00 37.66 N ANISOU 3220 N VAL A 407 5698 4297 4312 212 674 -1199 N ATOM 3221 CA VAL A 407 -24.803 15.570 -30.163 1.00 38.37 C ANISOU 3221 CA VAL A 407 5904 4393 4282 49 702 -1178 C ATOM 3222 C VAL A 407 -26.110 16.338 -30.042 1.00 45.31 C ANISOU 3222 C VAL A 407 6919 5349 4949 82 662 -1018 C ATOM 3223 O VAL A 407 -26.116 17.546 -29.785 1.00 49.78 O ANISOU 3223 O VAL A 407 7596 5983 5335 84 608 -962 O ATOM 3224 CB VAL A 407 -24.576 15.182 -31.641 1.00 35.80 C ANISOU 3224 CB VAL A 407 5496 3903 4205 -174 866 -1231 C ATOM 3225 CG1 VAL A 407 -24.823 16.375 -32.556 1.00 28.51 C ANISOU 3225 CG1 VAL A 407 4689 2995 3150 -317 918 -1180 C ATOM 3226 CG2 VAL A 407 -23.175 14.621 -31.840 1.00 38.53 C ANISOU 3226 CG2 VAL A 407 5669 4165 4805 -269 945 -1374 C ATOM 3227 N GLN A 408 -27.217 15.619 -30.201 1.00 36.54 N ANISOU 3227 N GLN A 408 5801 4188 3895 115 692 -932 N ATOM 3228 CA GLN A 408 -28.536 16.224 -30.116 1.00 34.23 C ANISOU 3228 CA GLN A 408 5658 3903 3445 160 650 -753 C ATOM 3229 C GLN A 408 -28.791 16.792 -28.730 1.00 44.54 C ANISOU 3229 C GLN A 408 7030 5354 4539 333 538 -639 C ATOM 3230 O GLN A 408 -29.449 17.816 -28.590 1.00 44.14 O ANISOU 3230 O GLN A 408 7106 5289 4376 382 475 -540 O ATOM 3231 CB GLN A 408 -29.618 15.203 -30.467 1.00 27.82 C ANISOU 3231 CB GLN A 408 4817 3013 2741 180 702 -678 C ATOM 3232 CG GLN A 408 -29.625 14.770 -31.917 1.00 27.13 C ANISOU 3232 CG GLN A 408 4665 2790 2852 -9 833 -745 C ATOM 3233 CD GLN A 408 -30.781 13.841 -32.233 1.00 34.12 C ANISOU 3233 CD GLN A 408 5518 3612 3834 8 888 -661 C ATOM 3234 OE1 GLN A 408 -31.590 13.519 -31.361 1.00 40.57 O ANISOU 3234 OE1 GLN A 408 6379 4473 4564 175 823 -540 O ATOM 3235 NE2 GLN A 408 -30.866 13.404 -33.485 1.00 27.26 N ANISOU 3235 NE2 GLN A 408 4557 2657 3145 -165 1028 -708 N ATOM 3236 N SER A 409 -28.256 16.130 -27.709 1.00 40.35 N ANISOU 3236 N SER A 409 6398 4958 3977 430 528 -649 N ATOM 3237 CA SER A 409 -28.422 16.597 -26.342 1.00 45.54 C ANISOU 3237 CA SER A 409 7087 5791 4425 598 435 -500 C ATOM 3238 C SER A 409 -27.684 17.909 -26.132 1.00 47.91 C ANISOU 3238 C SER A 409 7443 6143 4619 549 383 -561 C ATOM 3239 O SER A 409 -28.207 18.832 -25.509 1.00 46.18 O ANISOU 3239 O SER A 409 7289 5980 4276 655 312 -468 O ATOM 3240 CB SER A 409 -27.923 15.550 -25.345 1.00 43.31 C ANISOU 3240 CB SER A 409 6676 5675 4106 698 461 -432 C ATOM 3241 OG SER A 409 -27.690 16.133 -24.073 1.00 47.35 O ANISOU 3241 OG SER A 409 7176 6401 4414 817 366 -288 O ATOM 3242 N GLU A 410 -26.468 17.990 -26.660 1.00 47.19 N ANISOU 3242 N GLU A 410 7298 6030 4602 404 430 -738 N ATOM 3243 CA GLU A 410 -25.702 19.222 -26.558 1.00 52.02 C ANISOU 3243 CA GLU A 410 7956 6685 5123 356 395 -795 C ATOM 3244 C GLU A 410 -26.353 20.361 -27.337 1.00 56.64 C ANISOU 3244 C GLU A 410 8675 7144 5702 315 389 -759 C ATOM 3245 O GLU A 410 -26.348 21.512 -26.892 1.00 60.12 O ANISOU 3245 O GLU A 410 9187 7628 6028 355 340 -727 O ATOM 3246 CB GLU A 410 -24.272 18.996 -27.043 1.00 55.81 C ANISOU 3246 CB GLU A 410 8334 7157 5715 247 441 -995 C ATOM 3247 CG GLU A 410 -23.369 18.423 -25.975 1.00 59.99 C ANISOU 3247 CG GLU A 410 8757 7845 6193 282 432 -1039 C ATOM 3248 CD GLU A 410 -23.272 19.339 -24.773 1.00 70.26 C ANISOU 3248 CD GLU A 410 10137 9304 7255 345 358 -899 C ATOM 3249 OE1 GLU A 410 -23.209 20.570 -24.975 1.00 59.77 O ANISOU 3249 OE1 GLU A 410 8885 7956 5868 322 329 -912 O ATOM 3250 OE2 GLU A 410 -23.274 18.833 -23.632 1.00 74.68 O ANISOU 3250 OE2 GLU A 410 10677 10003 7696 444 320 -754 O ATOM 3251 N LEU A 411 -26.941 20.034 -28.484 1.00 50.44 N ANISOU 3251 N LEU A 411 7923 6200 5041 231 448 -756 N ATOM 3252 CA LEU A 411 -27.604 21.050 -29.292 1.00 53.43 C ANISOU 3252 CA LEU A 411 8437 6451 5413 170 461 -699 C ATOM 3253 C LEU A 411 -28.868 21.557 -28.602 1.00 58.11 C ANISOU 3253 C LEU A 411 9119 7046 5913 328 383 -565 C ATOM 3254 O LEU A 411 -29.138 22.760 -28.589 1.00 62.62 O ANISOU 3254 O LEU A 411 9788 7588 6418 345 353 -540 O ATOM 3255 CB LEU A 411 -27.938 20.501 -30.680 1.00 43.31 C ANISOU 3255 CB LEU A 411 7160 5022 4276 20 564 -705 C ATOM 3256 CG LEU A 411 -26.731 20.206 -31.573 1.00 52.76 C ANISOU 3256 CG LEU A 411 8266 6187 5592 -149 667 -842 C ATOM 3257 CD1 LEU A 411 -27.153 19.488 -32.845 1.00 42.72 C ANISOU 3257 CD1 LEU A 411 6955 4805 4473 -297 797 -839 C ATOM 3258 CD2 LEU A 411 -25.991 21.492 -31.902 1.00 58.52 C ANISOU 3258 CD2 LEU A 411 9068 6908 6260 -233 680 -876 C ATOM 3259 N ARG A 412 -29.626 20.637 -28.014 1.00 53.97 N ANISOU 3259 N ARG A 412 8551 6561 5395 455 355 -487 N ATOM 3260 CA ARG A 412 -30.823 20.996 -27.264 1.00 57.28 C ANISOU 3260 CA ARG A 412 9017 7003 5744 641 287 -376 C ATOM 3261 C ARG A 412 -30.455 21.817 -26.042 1.00 62.48 C ANISOU 3261 C ARG A 412 9648 7833 6260 756 226 -376 C ATOM 3262 O ARG A 412 -31.206 22.691 -25.622 1.00 65.14 O ANISOU 3262 O ARG A 412 10036 8182 6533 863 185 -334 O ATOM 3263 CB ARG A 412 -31.593 19.752 -26.816 1.00 44.88 C ANISOU 3263 CB ARG A 412 7372 5471 4209 772 281 -290 C ATOM 3264 CG ARG A 412 -32.220 18.935 -27.924 1.00 54.79 C ANISOU 3264 CG ARG A 412 8658 6559 5599 681 339 -265 C ATOM 3265 CD ARG A 412 -32.990 17.766 -27.331 1.00 61.19 C ANISOU 3265 CD ARG A 412 9388 7425 6435 846 331 -169 C ATOM 3266 NE ARG A 412 -33.099 16.646 -28.260 1.00 63.74 N ANISOU 3266 NE ARG A 412 9691 7636 6890 727 412 -171 N ATOM 3267 CZ ARG A 412 -34.027 16.545 -29.206 1.00 66.53 C ANISOU 3267 CZ ARG A 412 10124 7832 7320 658 444 -121 C ATOM 3268 NH1 ARG A 412 -34.933 17.503 -29.355 1.00 72.55 N ANISOU 3268 NH1 ARG A 412 11006 8509 8049 710 393 -65 N ATOM 3269 NH2 ARG A 412 -34.049 15.488 -30.005 1.00 56.43 N ANISOU 3269 NH2 ARG A 412 8791 6492 6158 530 543 -136 N ATOM 3270 N ARG A 413 -29.291 21.526 -25.471 1.00 60.09 N ANISOU 3270 N ARG A 413 9257 7667 5907 729 227 -426 N ATOM 3271 CA ARG A 413 -28.860 22.206 -24.262 1.00 65.09 C ANISOU 3271 CA ARG A 413 9853 8482 6395 822 177 -408 C ATOM 3272 C ARG A 413 -28.440 23.639 -24.568 1.00 75.53 C ANISOU 3272 C ARG A 413 11267 9756 7674 745 170 -478 C ATOM 3273 O ARG A 413 -28.821 24.571 -23.855 1.00 75.76 O ANISOU 3273 O ARG A 413 11322 9859 7605 846 129 -444 O ATOM 3274 CB ARG A 413 -27.715 21.443 -23.597 1.00 63.81 C ANISOU 3274 CB ARG A 413 9582 8473 6192 802 180 -421 C ATOM 3275 CG ARG A 413 -27.344 21.963 -22.221 1.00 73.05 C ANISOU 3275 CG ARG A 413 10697 9855 7202 909 128 -356 C ATOM 3276 CD ARG A 413 -26.158 21.210 -21.648 1.00 74.87 C ANISOU 3276 CD ARG A 413 10835 10219 7394 873 127 -345 C ATOM 3277 NE ARG A 413 -25.004 21.262 -22.540 1.00 76.87 N ANISOU 3277 NE ARG A 413 11121 10366 7722 681 173 -514 N ATOM 3278 CZ ARG A 413 -24.171 22.294 -22.620 1.00 87.94 C ANISOU 3278 CZ ARG A 413 12566 11767 9079 597 170 -611 C ATOM 3279 NH1 ARG A 413 -24.367 23.364 -21.863 1.00 89.82 N ANISOU 3279 NH1 ARG A 413 12842 12088 9197 682 121 -556 N ATOM 3280 NH2 ARG A 413 -23.145 22.261 -23.458 1.00 88.95 N ANISOU 3280 NH2 ARG A 413 12677 11825 9294 436 225 -773 N ATOM 3281 N ARG A 414 -27.657 23.813 -25.630 1.00 72.31 N ANISOU 3281 N ARG A 414 10895 9239 7342 571 219 -576 N ATOM 3282 CA ARG A 414 -27.248 25.150 -26.044 1.00 63.80 C ANISOU 3282 CA ARG A 414 9901 8110 6231 496 224 -629 C ATOM 3283 C ARG A 414 -28.437 25.969 -26.549 1.00 69.24 C ANISOU 3283 C ARG A 414 10712 8662 6934 527 216 -568 C ATOM 3284 O ARG A 414 -28.478 27.187 -26.377 1.00 71.88 O ANISOU 3284 O ARG A 414 11115 8999 7198 547 194 -573 O ATOM 3285 CB ARG A 414 -26.158 25.059 -27.113 1.00 58.08 C ANISOU 3285 CB ARG A 414 9165 7311 5594 316 291 -738 C ATOM 3286 CG ARG A 414 -24.870 24.444 -26.589 1.00 62.31 C ANISOU 3286 CG ARG A 414 9578 7982 6115 290 295 -826 C ATOM 3287 CD ARG A 414 -24.031 23.837 -27.698 1.00 60.94 C ANISOU 3287 CD ARG A 414 9354 7721 6081 148 370 -939 C ATOM 3288 NE ARG A 414 -23.102 24.795 -28.287 1.00 58.32 N ANISOU 3288 NE ARG A 414 9064 7346 5750 50 399 -1017 N ATOM 3289 CZ ARG A 414 -21.869 25.009 -27.838 1.00 56.37 C ANISOU 3289 CZ ARG A 414 8756 7200 5463 46 383 -1110 C ATOM 3290 NH1 ARG A 414 -21.085 25.897 -28.436 1.00 61.05 N ANISOU 3290 NH1 ARG A 414 9402 7734 6060 -43 414 -1166 N ATOM 3291 NH2 ARG A 414 -21.417 24.333 -26.792 1.00 61.06 N ANISOU 3291 NH2 ARG A 414 9241 7952 6009 119 343 -1137 N ATOM 3292 N TRP A 415 -29.403 25.296 -27.167 1.00 69.68 N ANISOU 3292 N TRP A 415 10797 8599 7081 529 236 -510 N ATOM 3293 CA TRP A 415 -30.638 25.950 -27.589 1.00 73.93 C ANISOU 3293 CA TRP A 415 11447 9006 7635 568 226 -442 C ATOM 3294 C TRP A 415 -31.480 26.378 -26.389 1.00 82.80 C ANISOU 3294 C TRP A 415 12556 10240 8666 773 159 -393 C ATOM 3295 O TRP A 415 -32.121 27.430 -26.406 1.00 87.39 O ANISOU 3295 O TRP A 415 13223 10771 9212 817 139 -375 O ATOM 3296 CB TRP A 415 -31.448 25.017 -28.494 1.00 71.55 C ANISOU 3296 CB TRP A 415 11170 8562 7453 519 267 -386 C ATOM 3297 CG TRP A 415 -32.761 25.576 -28.965 1.00 74.66 C ANISOU 3297 CG TRP A 415 11682 8815 7872 555 258 -308 C ATOM 3298 CD1 TRP A 415 -33.002 26.220 -30.143 1.00 79.10 C ANISOU 3298 CD1 TRP A 415 12360 9215 8477 414 308 -285 C ATOM 3299 CD2 TRP A 415 -34.017 25.518 -28.276 1.00 78.58 C ANISOU 3299 CD2 TRP A 415 12181 9327 8351 745 204 -245 C ATOM 3300 NE1 TRP A 415 -34.326 26.576 -30.227 1.00 79.54 N ANISOU 3300 NE1 TRP A 415 12502 9173 8545 501 280 -209 N ATOM 3301 CE2 TRP A 415 -34.971 26.156 -29.093 1.00 80.31 C ANISOU 3301 CE2 TRP A 415 12529 9375 8610 709 216 -192 C ATOM 3302 CE3 TRP A 415 -34.425 24.993 -27.047 1.00 84.36 C ANISOU 3302 CE3 TRP A 415 12805 10215 9031 940 158 -226 C ATOM 3303 CZ2 TRP A 415 -36.308 26.285 -28.720 1.00 89.47 C ANISOU 3303 CZ2 TRP A 415 13718 10505 9772 869 175 -137 C ATOM 3304 CZ3 TRP A 415 -35.753 25.121 -26.677 1.00 92.38 C ANISOU 3304 CZ3 TRP A 415 13835 11220 10044 1098 129 -172 C ATOM 3305 CH2 TRP A 415 -36.678 25.762 -27.511 1.00 93.68 C ANISOU 3305 CH2 TRP A 415 14134 11200 10259 1064 134 -136 C ATOM 3306 N HIS A 416 -31.465 25.553 -25.346 1.00 82.47 N ANISOU 3306 N HIS A 416 12394 10362 8580 895 134 -368 N ATOM 3307 CA HIS A 416 -32.291 25.771 -24.162 1.00 83.40 C ANISOU 3307 CA HIS A 416 12457 10624 8606 1092 91 -312 C ATOM 3308 C HIS A 416 -31.697 26.834 -23.247 1.00 88.38 C ANISOU 3308 C HIS A 416 13073 11407 9103 1130 62 -339 C ATOM 3309 O HIS A 416 -32.421 27.520 -22.523 1.00 93.13 O ANISOU 3309 O HIS A 416 13669 12091 9625 1257 36 -309 O ATOM 3310 CB HIS A 416 -32.464 24.460 -23.392 1.00 86.65 C ANISOU 3310 CB HIS A 416 12727 11182 9012 1201 91 -251 C ATOM 3311 CG HIS A 416 -33.795 24.318 -22.725 1.00 91.79 C ANISOU 3311 CG HIS A 416 13324 11915 9637 1384 79 -175 C ATOM 3312 ND1 HIS A 416 -34.972 24.192 -23.431 1.00 92.22 N ANISOU 3312 ND1 HIS A 416 13448 11808 9785 1414 88 -152 N ATOM 3313 CD2 HIS A 416 -34.135 24.271 -21.415 1.00 92.47 C ANISOU 3313 CD2 HIS A 416 13281 12242 9612 1540 68 -109 C ATOM 3314 CE1 HIS A 416 -35.980 24.078 -22.585 1.00 98.61 C ANISOU 3314 CE1 HIS A 416 14170 12755 10544 1588 83 -93 C ATOM 3315 NE2 HIS A 416 -35.499 24.124 -21.355 1.00 98.05 N ANISOU 3315 NE2 HIS A 416 13971 12938 10345 1662 76 -61 N ATOM 3316 N ARG A 417 -30.373 26.957 -23.281 1.00 82.94 N ANISOU 3316 N ARG A 417 12370 10757 8386 1017 71 -400 N ATOM 3317 CA ARG A 417 -29.677 27.965 -22.494 1.00 86.36 C ANISOU 3317 CA ARG A 417 12796 11320 8696 1033 46 -429 C ATOM 3318 C ARG A 417 -30.087 29.364 -22.933 1.00 96.94 C ANISOU 3318 C ARG A 417 14256 12555 10021 1016 40 -455 C ATOM 3319 O ARG A 417 -30.146 30.290 -22.124 1.00103.10 O ANISOU 3319 O ARG A 417 15035 13443 10695 1096 11 -451 O ATOM 3320 CB ARG A 417 -28.163 27.804 -22.628 1.00 83.51 C ANISOU 3320 CB ARG A 417 12407 10995 8329 900 63 -499 C ATOM 3321 CG ARG A 417 -27.530 26.798 -21.681 1.00 91.97 C ANISOU 3321 CG ARG A 417 13352 12244 9349 944 51 -462 C ATOM 3322 CD ARG A 417 -26.036 26.697 -21.951 1.00 96.37 C ANISOU 3322 CD ARG A 417 13893 12810 9913 798 72 -550 C ATOM 3323 NE ARG A 417 -25.280 26.235 -20.791 1.00101.82 N ANISOU 3323 NE ARG A 417 14488 13692 10507 849 44 -504 N ATOM 3324 CZ ARG A 417 -23.953 26.166 -20.748 1.00102.92 C ANISOU 3324 CZ ARG A 417 14605 13871 10628 745 53 -571 C ATOM 3325 NH1 ARG A 417 -23.238 26.525 -21.806 1.00 99.25 N ANISOU 3325 NH1 ARG A 417 14184 13288 10239 588 97 -700 N ATOM 3326 NH2 ARG A 417 -23.341 25.735 -19.654 1.00 98.50 N ANISOU 3326 NH2 ARG A 417 13965 13481 9978 803 20 -501 N ATOM 3327 N ALA A 418 -30.382 29.504 -24.221 1.00 90.01 N ANISOU 3327 N ALA A 418 13481 11470 9250 910 70 -471 N ATOM 3328 CA ALA A 418 -30.763 30.792 -24.786 1.00 90.51 C ANISOU 3328 CA ALA A 418 13667 11414 9309 877 71 -481 C ATOM 3329 C ALA A 418 -32.227 31.104 -24.500 1.00 86.70 C ANISOU 3329 C ALA A 418 13220 10904 8817 1018 44 -422 C ATOM 3330 O ALA A 418 -33.048 31.160 -25.414 1.00 86.72 O ANISOU 3330 O ALA A 418 13315 10730 8905 984 60 -391 O ATOM 3331 CB ALA A 418 -30.498 30.812 -26.284 1.00 74.34 C ANISOU 3331 CB ALA A 418 11711 9165 7368 698 124 -500 C TER 3332 ALA A 418 HETATM 3333 N1 5MV A1201 -32.082 1.694 -39.704 1.00 30.54 N HETATM 3334 N3 5MV A1201 -27.299 5.977 -34.706 1.00 33.62 N HETATM 3335 C4 5MV A1201 -37.051 1.811 -41.030 1.00 45.65 C HETATM 3336 C5 5MV A1201 -36.922 1.255 -39.750 1.00 52.06 C HETATM 3337 C6 5MV A1201 -35.645 1.017 -39.211 1.00 49.37 C HETATM 3338 C7 5MV A1201 -33.172 1.056 -39.321 1.00 46.35 C HETATM 3339 C8 5MV A1201 -32.892 0.139 -38.272 1.00 42.58 C HETATM 3340 C10 5MV A1201 -30.455 -1.139 -34.686 1.00 31.57 C HETATM 3341 C13 5MV A1201 -29.554 -1.157 -37.361 1.00 33.53 C HETATM 3342 C15 5MV A1201 -29.275 -1.818 -35.010 1.00 38.07 C HETATM 3343 C17 5MV A1201 -27.355 -3.176 -34.307 1.00 37.47 C HETATM 3344 C20 5MV A1201 -29.732 1.748 -39.114 1.00 32.90 C HETATM 3345 C21 5MV A1201 -28.907 4.700 -35.990 1.00 35.31 C HETATM 3346 C22 5MV A1201 -27.866 3.962 -36.582 1.00 30.42 C HETATM 3347 C24 5MV A1201 -29.469 2.800 -38.022 1.00 33.49 C HETATM 3348 C26 5MV A1201 -30.237 4.487 -36.406 1.00 33.24 C HETATM 3349 C28 5MV A1201 -28.587 5.690 -34.922 1.00 36.57 C HETATM 3350 C1 5MV A1201 -34.477 1.325 -39.941 1.00 49.39 C HETATM 3351 C2 5MV A1201 -34.615 1.892 -41.230 1.00 45.63 C HETATM 3352 C3 5MV A1201 -35.896 2.128 -41.765 1.00 49.55 C HETATM 3353 CL1 5MV A1201 -36.069 2.808 -43.336 1.00 63.95 CL HETATM 3354 CL2 5MV A1201 -38.327 0.863 -38.834 1.00 54.78 CL HETATM 3355 C9 5MV A1201 -31.554 0.251 -38.039 1.00 39.00 C HETATM 3356 C11 5MV A1201 -31.168 -0.481 -35.693 1.00 28.66 C HETATM 3357 C12 5MV A1201 -30.747 -0.471 -37.040 1.00 40.14 C HETATM 3358 C14 5MV A1201 -28.822 -1.829 -36.351 1.00 32.78 C HETATM 3359 C16 5MV A1201 -28.551 -2.483 -33.999 1.00 39.37 C HETATM 3360 C18 5MV A1201 -26.911 -3.182 -35.644 1.00 40.95 C HETATM 3361 C19 5MV A1201 -27.634 -2.519 -36.655 1.00 39.19 C HETATM 3362 C25 5MV A1201 -30.515 3.541 -37.412 1.00 27.97 C HETATM 3363 N2 5MV A1201 -31.079 1.209 -38.933 1.00 37.39 N HETATM 3364 O1 5MV A1201 -26.595 -3.849 -33.375 1.00 33.35 O HETATM 3365 C27 5MV A1201 -26.664 -3.397 -32.029 1.00 34.16 C HETATM 3366 O2 5MV A1201 -29.506 6.193 -34.285 1.00 42.74 O HETATM 3367 C29 5MV A1201 -26.857 6.918 -33.687 1.00 30.64 C HETATM 3368 C30 5MV A1201 -27.071 6.381 -32.263 1.00 39.58 C HETATM 3369 C31 5MV A1201 -26.552 7.362 -31.221 1.00 41.57 C HETATM 3370 O3 5MV A1201 -27.349 7.765 -30.348 1.00 45.68 O HETATM 3371 O4 5MV A1201 -25.348 7.705 -31.301 1.00 36.34 O HETATM 3372 C32 5MV A1201 -29.592 2.354 -40.524 1.00 24.77 C HETATM 3373 C23 5MV A1201 -28.145 3.021 -37.585 1.00 27.55 C HETATM 3374 C1 OLA A1202 1.194 9.174 -36.710 1.00 61.99 C HETATM 3375 O1 OLA A1202 2.046 8.275 -36.482 1.00 61.67 O HETATM 3376 O2 OLA A1202 0.585 9.718 -35.751 1.00 61.12 O HETATM 3377 C2 OLA A1202 0.904 9.602 -38.133 1.00 56.07 C HETATM 3378 C3 OLA A1202 0.760 8.421 -39.068 1.00 50.01 C HETATM 3379 C4 OLA A1202 -0.071 8.746 -40.290 1.00 45.93 C HETATM 3380 C5 OLA A1202 0.736 9.406 -41.386 1.00 49.98 C HETATM 3381 C6 OLA A1202 -0.149 10.008 -42.455 1.00 48.98 C HETATM 3382 C7 OLA A1202 0.450 9.901 -43.841 1.00 51.93 C HETATM 3383 C8 OLA A1202 1.895 10.348 -43.887 1.00 57.11 C HETATM 3384 C1 OLA A1203 -30.078 -2.060 -62.948 1.00 68.24 C HETATM 3385 O1 OLA A1203 -29.474 -2.840 -63.733 1.00 67.47 O HETATM 3386 O2 OLA A1203 -30.751 -1.101 -63.409 1.00 76.54 O HETATM 3387 C2 OLA A1203 -29.998 -2.271 -61.452 1.00 52.50 C HETATM 3388 C3 OLA A1203 -31.247 -1.799 -60.741 1.00 46.50 C HETATM 3389 C4 OLA A1203 -31.323 -2.303 -59.316 1.00 49.39 C HETATM 3390 C5 OLA A1203 -32.654 -1.987 -58.667 1.00 51.39 C HETATM 3391 C6 OLA A1203 -32.690 -2.380 -57.206 1.00 49.08 C HETATM 3392 C7 OLA A1203 -33.696 -1.566 -56.423 1.00 50.11 C HETATM 3393 C8 OLA A1203 -33.699 -1.910 -54.950 1.00 55.71 C HETATM 3394 C9 OLA A1203 -35.096 -1.888 -54.367 1.00 49.36 C HETATM 3395 C10 OLA A1203 -35.291 -2.072 -53.046 1.00 51.34 C HETATM 3396 C11 OLA A1203 -34.119 -2.304 -52.119 1.00 60.53 C HETATM 3397 C12 OLA A1203 -34.502 -2.124 -50.666 1.00 54.80 C HETATM 3398 C13 OLA A1203 -33.696 -3.011 -49.743 1.00 62.96 C HETATM 3399 C1 OLA A1204 -25.327 0.639 -53.009 1.00 62.95 C HETATM 3400 O1 OLA A1204 -26.382 0.839 -53.668 1.00 60.59 O HETATM 3401 O2 OLA A1204 -24.317 0.141 -53.574 1.00 64.05 O HETATM 3402 C2 OLA A1204 -25.272 0.995 -51.538 1.00 54.60 C HETATM 3403 C3 OLA A1204 -25.061 2.476 -51.304 1.00 44.78 C HETATM 3404 C4 OLA A1204 -25.775 2.958 -50.060 1.00 44.04 C HETATM 3405 C5 OLA A1204 -26.086 4.436 -50.120 1.00 40.00 C HETATM 3406 C6 OLA A1204 -27.024 4.888 -49.022 1.00 47.37 C HETATM 3407 C7 OLA A1204 -27.744 6.167 -49.390 1.00 42.83 C HETATM 3408 C8 OLA A1204 -28.331 6.878 -48.189 1.00 42.02 C HETATM 3409 C9 OLA A1204 -28.036 8.363 -48.218 1.00 42.01 C HETATM 3410 C10 OLA A1204 -28.622 9.218 -47.354 1.00 42.86 C HETATM 3411 C11 OLA A1204 -29.604 8.725 -46.315 1.00 44.65 C HETATM 3412 C12 OLA A1204 -29.664 9.645 -45.116 1.00 41.00 C HETATM 3413 C13 OLA A1204 -31.081 9.980 -44.710 1.00 41.91 C HETATM 3414 C1 OLA A1205 -22.605 21.575 -57.369 1.00 45.13 C HETATM 3415 O1 OLA A1205 -22.592 21.665 -58.626 1.00 45.03 O HETATM 3416 O2 OLA A1205 -21.857 20.746 -56.789 1.00 57.80 O HETATM 3417 C2 OLA A1205 -23.523 22.455 -56.553 1.00 35.53 C HETATM 3418 C3 OLA A1205 -24.507 21.656 -55.730 1.00 42.68 C HETATM 3419 C4 OLA A1205 -25.579 21.027 -56.592 1.00 33.41 C HETATM 3420 C5 OLA A1205 -26.512 20.132 -55.808 1.00 36.38 C HETATM 3421 C6 OLA A1205 -27.262 20.873 -54.724 1.00 34.97 C HETATM 3422 C7 OLA A1205 -28.394 20.039 -54.167 1.00 39.31 C HETATM 3423 C8 OLA A1205 -28.940 20.590 -52.869 1.00 40.94 C HETATM 3424 C9 OLA A1205 -30.378 20.182 -52.632 1.00 44.37 C HETATM 3425 C1 OLA A1206 -24.053 18.740 -64.880 1.00 62.10 C HETATM 3426 O1 OLA A1206 -23.276 19.452 -65.570 1.00 61.85 O HETATM 3427 O2 OLA A1206 -24.901 17.999 -65.445 1.00 72.14 O HETATM 3428 C2 OLA A1206 -23.970 18.782 -63.370 1.00 49.58 C HETATM 3429 C3 OLA A1206 -25.293 19.136 -62.727 1.00 44.13 C HETATM 3430 C4 OLA A1206 -25.111 19.976 -61.483 1.00 43.19 C HETATM 3431 C5 OLA A1206 -26.398 20.623 -61.021 1.00 41.30 C HETATM 3432 C6 OLA A1206 -26.945 19.965 -59.774 1.00 39.91 C HETATM 3433 C7 OLA A1206 -28.137 20.702 -59.202 1.00 51.40 C HETATM 3434 C8 OLA A1206 -29.448 20.215 -59.779 1.00 54.84 C HETATM 3435 C9 OLA A1206 -30.536 20.122 -58.731 1.00 60.06 C HETATM 3436 C1 OLA A1207 -15.097 22.076 -55.260 1.00 45.20 C HETATM 3437 O1 OLA A1207 -15.498 23.265 -55.169 1.00 54.08 O HETATM 3438 O2 OLA A1207 -15.081 21.505 -56.384 1.00 42.82 O HETATM 3439 C2 OLA A1207 -14.638 21.334 -54.022 1.00 35.05 C HETATM 3440 C3 OLA A1207 -14.854 22.130 -52.754 1.00 33.29 C HETATM 3441 C4 OLA A1207 -14.188 21.494 -51.553 1.00 42.64 C HETATM 3442 C5 OLA A1207 -14.561 22.185 -50.257 1.00 37.70 C HETATM 3443 C6 OLA A1207 -14.114 21.419 -49.029 1.00 45.06 C HETATM 3444 C7 OLA A1207 -12.613 21.421 -48.821 1.00 44.68 C HETATM 3445 C8 OLA A1207 -12.252 21.455 -47.349 1.00 53.03 C HETATM 3446 C9 OLA A1207 -11.248 20.393 -46.952 1.00 54.86 C HETATM 3447 C10 OLA A1207 -10.966 20.168 -45.651 1.00 52.01 C HETATM 3448 C11 OLA A1207 -11.644 20.968 -44.557 1.00 46.97 C HETATM 3449 C12 OLA A1207 -11.155 20.587 -43.174 1.00 51.20 C HETATM 3450 C13 OLA A1207 -12.282 20.373 -42.185 1.00 48.66 C HETATM 3451 C14 OLA A1207 -12.592 21.612 -41.370 1.00 52.77 C HETATM 3452 C15 OLA A1207 -13.851 21.469 -40.538 1.00 49.98 C HETATM 3453 C16 OLA A1207 -14.503 22.800 -40.221 1.00 45.78 C HETATM 3454 C17 OLA A1207 -15.513 23.219 -41.270 1.00 47.23 C HETATM 3455 C18 OLA A1207 -14.933 24.148 -42.318 1.00 35.71 C HETATM 3456 C1 OLA A1208 -8.779 11.977 -28.523 1.00 60.18 C HETATM 3457 O1 OLA A1208 -9.701 12.833 -28.497 1.00 63.33 O HETATM 3458 O2 OLA A1208 -8.871 10.940 -27.815 1.00 65.34 O HETATM 3459 C2 OLA A1208 -7.563 12.191 -29.401 1.00 52.84 C HETATM 3460 C3 OLA A1208 -7.811 13.220 -30.482 1.00 59.29 C HETATM 3461 C4 OLA A1208 -6.632 13.381 -31.418 1.00 63.48 C HETATM 3462 C5 OLA A1208 -7.040 13.956 -32.758 1.00 57.66 C HETATM 3463 C6 OLA A1208 -5.969 13.808 -33.819 1.00 57.66 C HETATM 3464 C7 OLA A1208 -6.557 13.857 -35.213 1.00 46.32 C HETATM 3465 C8 OLA A1208 -5.542 14.149 -36.300 1.00 43.46 C HETATM 3466 C9 OLA A1208 -6.228 14.500 -37.603 1.00 44.91 C HETATM 3467 C10 OLA A1208 -5.559 14.552 -38.775 1.00 49.90 C HETATM 3468 C11 OLA A1208 -4.078 14.253 -38.859 1.00 43.51 C HETATM 3469 C12 OLA A1208 -3.520 14.611 -40.221 1.00 54.53 C HETATM 3470 C13 OLA A1208 -3.926 13.630 -41.302 1.00 44.93 C HETATM 3471 C14 OLA A1208 -4.347 14.322 -42.581 1.00 46.43 C HETATM 3472 C15 OLA A1208 -4.334 13.392 -43.776 1.00 47.98 C HETATM 3473 C16 OLA A1208 -5.355 13.778 -44.825 1.00 46.88 C HETATM 3474 C17 OLA A1208 -4.812 14.766 -45.835 1.00 51.67 C HETATM 3475 C18 OLA A1208 -3.855 14.125 -46.817 1.00 51.87 C HETATM 3476 C1 OLA A1209 -11.671 -10.899 -28.382 1.00 63.53 C HETATM 3477 O1 OLA A1209 -11.404 -11.131 -27.172 1.00 73.15 O HETATM 3478 O2 OLA A1209 -12.618 -10.126 -28.687 1.00 47.17 O HETATM 3479 C2 OLA A1209 -10.854 -11.556 -29.473 1.00 57.74 C HETATM 3480 C3 OLA A1209 -10.534 -10.597 -30.598 1.00 58.44 C HETATM 3481 C4 OLA A1209 -10.681 -11.231 -31.964 1.00 52.09 C HETATM 3482 C5 OLA A1209 -10.510 -10.220 -33.075 1.00 49.09 C HETATM 3483 C6 OLA A1209 -10.296 -10.871 -34.424 1.00 51.06 C HETATM 3484 C7 OLA A1209 -9.472 -9.992 -35.338 1.00 43.79 C HETATM 3485 C8 OLA A1209 -8.939 -10.734 -36.542 1.00 44.44 C HETATM 3486 C9 OLA A1209 -8.712 -9.798 -37.710 1.00 43.98 C HETATM 3487 C10 OLA A1209 -8.208 -10.252 -38.875 1.00 40.05 C HETATM 3488 C11 OLA A1209 -7.862 -11.714 -39.038 1.00 45.80 C HETATM 3489 C12 OLA A1209 -7.667 -12.105 -40.486 1.00 51.41 C HETATM 3490 C13 OLA A1209 -6.811 -11.109 -41.237 1.00 45.66 C HETATM 3491 C14 OLA A1209 -6.405 -11.616 -42.602 1.00 49.43 C HETATM 3492 C15 OLA A1209 -5.093 -11.015 -43.057 1.00 49.26 C HETATM 3493 C16 OLA A1209 -4.589 -11.626 -44.346 1.00 49.61 C HETATM 3494 C17 OLA A1209 -3.197 -11.147 -44.696 1.00 57.85 C HETATM 3495 C18 OLA A1209 -2.751 -11.631 -46.058 1.00 66.21 C HETATM 3496 C1 OLA A1210 2.875 18.748 -66.707 1.00 91.25 C HETATM 3497 O1 OLA A1210 2.723 17.762 -67.475 1.00 89.12 O HETATM 3498 O2 OLA A1210 3.510 19.762 -67.101 1.00 93.77 O HETATM 3499 C2 OLA A1210 2.297 18.717 -65.310 1.00 78.04 C HETATM 3500 C3 OLA A1210 2.273 17.328 -64.712 1.00 66.91 C HETATM 3501 C4 OLA A1210 2.230 17.383 -63.202 1.00 64.98 C HETATM 3502 C5 OLA A1210 1.666 16.124 -62.583 1.00 61.70 C HETATM 3503 C6 OLA A1210 1.576 16.240 -61.076 1.00 59.04 C HETATM 3504 C7 OLA A1210 0.505 15.346 -60.494 1.00 54.60 C HETATM 3505 C8 OLA A1210 1.078 14.235 -59.644 1.00 62.39 C HETATM 3506 C9 OLA A1210 1.747 14.760 -58.394 1.00 56.13 C HETATM 3507 C10 OLA A1210 1.891 13.957 -57.320 1.00 65.97 C HETATM 3508 C11 OLA A1210 1.388 12.530 -57.362 1.00 66.24 C HETATM 3509 C12 OLA A1210 1.381 11.888 -55.992 1.00 66.90 C HETATM 3510 C13 OLA A1210 2.770 11.525 -55.518 1.00 67.90 C HETATM 3511 C14 OLA A1210 2.847 11.437 -54.010 1.00 71.33 C HETATM 3512 C15 OLA A1210 4.245 11.122 -53.526 1.00 77.62 C HETATM 3513 C2 OLA A1211 -32.701 -2.192 -32.248 1.00 58.39 C HETATM 3514 C3 OLA A1211 -33.988 -2.904 -32.599 1.00 55.45 C HETATM 3515 C4 OLA A1211 -34.186 -3.044 -34.093 1.00 54.68 C HETATM 3516 C5 OLA A1211 -35.002 -1.910 -34.676 1.00 45.00 C HETATM 3517 C6 OLA A1211 -35.010 -1.921 -36.189 1.00 46.28 C HETATM 3518 C7 OLA A1211 -35.707 -3.136 -36.765 1.00 50.57 C HETATM 3519 C8 OLA A1211 -36.854 -2.758 -37.678 1.00 48.25 C HETATM 3520 C2 OLA A1212 -32.111 -6.144 -29.298 1.00 55.75 C HETATM 3521 C3 OLA A1212 -32.229 -5.524 -30.674 1.00 55.21 C HETATM 3522 C4 OLA A1212 -30.883 -5.357 -31.343 1.00 55.29 C HETATM 3523 C5 OLA A1212 -30.799 -6.069 -32.675 1.00 54.40 C HETATM 3524 C6 OLA A1212 -31.146 -5.158 -33.831 1.00 53.14 C HETATM 3525 C7 OLA A1212 -30.612 -5.673 -35.151 1.00 52.35 C HETATM 3526 C8 OLA A1212 -30.991 -4.777 -36.311 1.00 50.56 C HETATM 3527 C9 OLA A1212 -30.378 -5.241 -37.614 1.00 51.79 C HETATM 3528 C10 OLA A1212 -30.756 -4.688 -38.784 1.00 52.54 C HETATM 3529 C11 OLA A1212 -31.799 -3.591 -38.820 1.00 50.41 C HETATM 3530 C12 OLA A1212 -31.837 -2.888 -40.160 1.00 54.73 C HETATM 3531 C2 OLA A1213 -26.569 -7.732 -33.177 1.00 40.36 C HETATM 3532 C3 OLA A1213 -27.246 -7.889 -34.521 1.00 46.51 C HETATM 3533 C4 OLA A1213 -26.549 -7.108 -35.613 1.00 49.68 C HETATM 3534 C5 OLA A1213 -27.354 -7.068 -36.895 1.00 48.75 C HETATM 3535 C6 OLA A1213 -26.530 -6.607 -38.078 1.00 47.51 C HETATM 3536 C7 OLA A1213 -27.382 -6.290 -39.288 1.00 44.83 C HETATM 3537 C8 OLA A1213 -26.674 -5.376 -40.265 1.00 35.82 C HETATM 3538 C1 OLA A1214 -34.819 4.255 -37.197 1.00 53.28 C HETATM 3539 O1 OLA A1214 -35.879 4.921 -37.065 1.00 57.00 O HETATM 3540 O2 OLA A1214 -34.539 3.349 -36.367 1.00 52.43 O HETATM 3541 C2 OLA A1214 -33.880 4.545 -38.349 1.00 47.14 C HETATM 3542 C3 OLA A1214 -34.563 5.228 -39.514 1.00 46.58 C HETATM 3543 C4 OLA A1214 -33.624 5.482 -40.676 1.00 54.38 C HETATM 3544 C5 OLA A1214 -34.326 5.350 -42.013 1.00 55.96 C HETATM 3545 C6 OLA A1214 -33.449 5.698 -43.199 1.00 63.74 C HETATM 3546 C7 OLA A1214 -34.001 5.156 -44.502 1.00 56.79 C HETATM 3547 C8 OLA A1214 -34.248 6.223 -45.548 1.00 51.74 C HETATM 3548 C9 OLA A1214 -32.961 6.833 -46.061 1.00 52.63 C HETATM 3549 C10 OLA A1214 -32.512 6.573 -47.308 1.00 53.53 C HETATM 3550 C11 OLA A1214 -33.273 5.663 -48.249 1.00 52.52 C HETATM 3551 C12 OLA A1214 -32.510 5.416 -49.534 1.00 46.83 C HETATM 3552 C1 OLA A1215 -6.805 25.192 -66.088 1.00 67.86 C HETATM 3553 O1 OLA A1215 -6.136 25.762 -66.991 1.00 59.17 O HETATM 3554 O2 OLA A1215 -7.691 24.350 -66.395 1.00 68.67 O HETATM 3555 C2 OLA A1215 -6.548 25.519 -64.632 1.00 63.35 C HETATM 3556 C3 OLA A1215 -6.819 24.342 -63.721 1.00 67.16 C HETATM 3557 C4 OLA A1215 -7.521 24.755 -62.446 1.00 68.96 C HETATM 3558 C5 OLA A1215 -6.568 24.927 -61.284 1.00 61.40 C HETATM 3559 C6 OLA A1215 -7.273 25.454 -60.052 1.00 62.21 C HETATM 3560 C7 OLA A1215 -6.709 24.878 -58.772 1.00 68.10 C HETATM 3561 C8 OLA A1215 -6.515 25.937 -57.709 1.00 67.60 C HETATM 3562 C9 OLA A1215 -7.481 25.774 -56.556 1.00 61.86 C HETATM 3563 C48 PE5 A1216 -15.264 4.838 -51.110 1.00 42.90 C HETATM 3564 C50 PE5 A1216 -16.684 4.784 -50.610 1.00 43.18 C HETATM 3565 O1 PE5 A1216 -17.345 3.673 -51.214 1.00 47.49 O HETATM 3566 C1 PE5 A1216 -17.576 3.818 -52.628 1.00 48.98 C HETATM 3567 C2 PE5 A1216 -17.020 2.559 -53.342 1.00 54.34 C HETATM 3568 O2 PE5 A1216 -16.890 2.840 -54.740 1.00 54.13 O HETATM 3569 C3 PE5 A1216 -15.509 2.943 -55.147 1.00 54.52 C HETATM 3570 C4 PE5 A1216 -15.460 3.304 -56.606 1.00 54.54 C HETATM 3571 O3 PE5 A1216 -15.626 4.734 -56.723 1.00 53.31 O HETATM 3572 C5 PE5 A1216 -15.650 5.186 -58.062 1.00 46.72 C HETATM 3573 C6 PE5 A1216 -15.308 6.682 -58.055 1.00 52.98 C HETATM 3574 O4 PE5 A1216 -16.412 7.388 -57.456 1.00 43.90 O HETATM 3575 C7 PE5 A1216 -16.669 8.673 -58.066 1.00 49.78 C HETATM 3576 C8 PE5 A1216 -18.011 8.592 -58.798 1.00 50.10 C HETATM 3577 O5 PE5 A1216 -17.797 7.978 -60.082 1.00 59.11 O HETATM 3578 C9 PE5 A1216 -18.549 8.573 -61.127 1.00 46.35 C HETATM 3579 C10 PE5 A1216 -18.208 10.091 -61.158 1.00 44.95 C HETATM 3580 O6 PE5 A1216 -16.839 10.246 -61.592 1.00 64.83 O HETATM 3581 C11 PE5 A1216 -16.295 11.558 -61.340 1.00 52.61 C HETATM 3582 C12 PE5 A1216 -14.792 11.463 -61.437 1.00 61.25 C HETATM 3583 O7 PE5 A1216 -14.483 10.501 -62.441 1.00 71.68 O HETATM 3584 C13 PE5 A1216 -13.113 10.455 -62.800 1.00 64.62 C HETATM 3585 C14 PE5 A1216 -13.029 10.048 -64.240 1.00 70.18 C HETATM 3586 O8 PE5 A1216 -14.017 9.062 -64.481 1.00 77.10 O HETATM 3587 O1 TLA A1217 -21.976 -9.292 -44.670 1.00 61.79 O HETATM 3588 O11 TLA A1217 -20.925 -9.060 -42.764 1.00 53.39 O HETATM 3589 C1 TLA A1217 -21.058 -8.767 -43.983 1.00 58.88 C HETATM 3590 C2 TLA A1217 -20.118 -7.774 -44.628 1.00 52.20 C HETATM 3591 O2 TLA A1217 -19.997 -8.067 -46.000 1.00 50.13 O HETATM 3592 C3 TLA A1217 -18.760 -7.851 -43.978 1.00 43.59 C HETATM 3593 O3 TLA A1217 -18.233 -9.136 -44.184 1.00 55.28 O HETATM 3594 C4 TLA A1217 -17.847 -6.841 -44.637 1.00 54.27 C HETATM 3595 O4 TLA A1217 -18.017 -6.552 -45.851 1.00 43.80 O HETATM 3596 O41 TLA A1217 -16.920 -6.295 -43.978 1.00 44.44 O HETATM 3597 O HOH A1301 -33.589 2.924 -34.359 1.00 45.18 O HETATM 3598 O HOH A1302 -22.595 -15.050 -23.749 1.00 43.69 O HETATM 3599 O HOH A1303 -13.269 4.781 -25.526 1.00 46.56 O HETATM 3600 O HOH A1304 -18.493 5.666 -55.223 1.00 49.42 O HETATM 3601 O HOH A1305 -14.705 7.699 -27.330 1.00 41.41 O HETATM 3602 O HOH A1306 -20.190 9.480 -30.657 1.00 46.00 O HETATM 3603 O HOH A1307 -19.143 7.731 -51.458 1.00 32.31 O HETATM 3604 O HOH A1308 -20.302 7.682 -56.790 1.00 37.70 O HETATM 3605 O HOH A1309 -20.804 19.386 -63.892 1.00 41.53 O HETATM 3606 O HOH A1310 -21.178 11.583 -28.898 1.00 41.92 O HETATM 3607 O HOH A1311 -10.655 -4.356 -24.912 1.00 40.03 O HETATM 3608 O HOH A1312 -20.016 9.998 -50.471 1.00 24.94 O HETATM 3609 O HOH A1313 -23.495 7.067 -33.616 1.00 36.90 O HETATM 3610 O HOH A1314 -22.433 0.827 -19.538 1.00 69.77 O HETATM 3611 O HOH A1315 -22.314 8.630 -22.896 1.00 53.11 O HETATM 3612 O HOH A1316 -10.581 20.137 -25.792 1.00 62.91 O HETATM 3613 O HOH A1317 -24.213 5.324 -21.934 1.00 53.38 O HETATM 3614 O HOH A1318 -21.648 -2.254 -16.757 1.00 57.90 O HETATM 3615 O HOH A1319 -21.452 8.165 -32.583 1.00 34.97 O HETATM 3616 O HOH A1320 -19.377 12.760 -26.137 1.00 56.60 O HETATM 3617 O HOH A1321 -11.386 1.017 -27.041 1.00 41.22 O HETATM 3618 O HOH A1322 -31.940 3.449 -28.530 1.00 60.88 O HETATM 3619 O HOH A1323 -19.353 10.071 -27.002 1.00 54.10 O HETATM 3620 O HOH A1324 -19.092 8.555 -25.009 1.00 48.39 O CONECT 560 2350 CONECT 2350 560 CONECT 3333 3338 3363 CONECT 3334 3349 3367 CONECT 3335 3336 3352 CONECT 3336 3335 3337 3354 CONECT 3337 3336 3350 CONECT 3338 3333 3339 3350 CONECT 3339 3338 3355 CONECT 3340 3342 3356 CONECT 3341 3357 3358 CONECT 3342 3340 3358 3359 CONECT 3343 3359 3360 3364 CONECT 3344 3347 3363 3372 CONECT 3345 3346 3348 3349 CONECT 3346 3345 3373 CONECT 3347 3344 3362 3373 CONECT 3348 3345 3362 CONECT 3349 3334 3345 3366 CONECT 3350 3337 3338 3351 CONECT 3351 3350 3352 CONECT 3352 3335 3351 3353 CONECT 3353 3352 CONECT 3354 3336 CONECT 3355 3339 3357 3363 CONECT 3356 3340 3357 CONECT 3357 3341 3355 3356 CONECT 3358 3341 3342 3361 CONECT 3359 3342 3343 CONECT 3360 3343 3361 CONECT 3361 3358 3360 CONECT 3362 3347 3348 CONECT 3363 3333 3344 3355 CONECT 3364 3343 3365 CONECT 3365 3364 CONECT 3366 3349 CONECT 3367 3334 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 3371 CONECT 3370 3369 CONECT 3371 3369 CONECT 3372 3344 CONECT 3373 3346 3347 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 CONECT 3384 3385 3386 3387 CONECT 3385 3384 CONECT 3386 3384 CONECT 3387 3384 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 CONECT 3399 3400 3401 3402 CONECT 3400 3399 CONECT 3401 3399 CONECT 3402 3399 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 CONECT 3414 3415 3416 3417 CONECT 3415 3414 CONECT 3416 3414 CONECT 3417 3414 3418 CONECT 3418 3417 3419 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 CONECT 3425 3426 3427 3428 CONECT 3426 3425 CONECT 3427 3425 CONECT 3428 3425 3429 CONECT 3429 3428 3430 CONECT 3430 3429 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3434 CONECT 3436 3437 3438 3439 CONECT 3437 3436 CONECT 3438 3436 CONECT 3439 3436 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 3447 CONECT 3447 3446 3448 CONECT 3448 3447 3449 CONECT 3449 3448 3450 CONECT 3450 3449 3451 CONECT 3451 3450 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 CONECT 3454 3453 3455 CONECT 3455 3454 CONECT 3456 3457 3458 3459 CONECT 3457 3456 CONECT 3458 3456 CONECT 3459 3456 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3464 CONECT 3464 3463 3465 CONECT 3465 3464 3466 CONECT 3466 3465 3467 CONECT 3467 3466 3468 CONECT 3468 3467 3469 CONECT 3469 3468 3470 CONECT 3470 3469 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 CONECT 3476 3477 3478 3479 CONECT 3477 3476 CONECT 3478 3476 CONECT 3479 3476 3480 CONECT 3480 3479 3481 CONECT 3481 3480 3482 CONECT 3482 3481 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3485 CONECT 3485 3484 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3493 3495 CONECT 3495 3494 CONECT 3496 3497 3498 3499 CONECT 3497 3496 CONECT 3498 3496 CONECT 3499 3496 3500 CONECT 3500 3499 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 3504 CONECT 3504 3503 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 CONECT 3508 3507 3509 CONECT 3509 3508 3510 CONECT 3510 3509 3511 CONECT 3511 3510 3512 CONECT 3512 3511 CONECT 3513 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 CONECT 3520 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3523 3525 CONECT 3525 3524 3526 CONECT 3526 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 3529 CONECT 3529 3528 3530 CONECT 3530 3529 CONECT 3531 3532 CONECT 3532 3531 3533 CONECT 3533 3532 3534 CONECT 3534 3533 3535 CONECT 3535 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 CONECT 3538 3539 3540 3541 CONECT 3539 3538 CONECT 3540 3538 CONECT 3541 3538 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 3549 CONECT 3549 3548 3550 CONECT 3550 3549 3551 CONECT 3551 3550 CONECT 3552 3553 3554 3555 CONECT 3553 3552 CONECT 3554 3552 CONECT 3555 3552 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 3562 CONECT 3562 3561 CONECT 3563 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3566 CONECT 3566 3565 3567 CONECT 3567 3566 3568 CONECT 3568 3567 3569 CONECT 3569 3568 3570 CONECT 3570 3569 3571 CONECT 3571 3570 3572 CONECT 3572 3571 3573 CONECT 3573 3572 3574 CONECT 3574 3573 3575 CONECT 3575 3574 3576 CONECT 3576 3575 3577 CONECT 3577 3576 3578 CONECT 3578 3577 3579 CONECT 3579 3578 3580 CONECT 3580 3579 3581 CONECT 3581 3580 3582 CONECT 3582 3581 3583 CONECT 3583 3582 3584 CONECT 3584 3583 3585 CONECT 3585 3584 3586 CONECT 3586 3585 CONECT 3587 3589 CONECT 3588 3589 CONECT 3589 3587 3588 3590 CONECT 3590 3589 3591 3592 CONECT 3591 3590 CONECT 3592 3590 3593 3594 CONECT 3593 3592 CONECT 3594 3592 3595 3596 CONECT 3595 3594 CONECT 3596 3594 MASTER 757 0 17 23 3 0 26 6 3619 1 266 35 END