HEADER RECEPTOR 21-AUG-12 4GPO TITLE OLIGOMEIC TURKEY BETA1-ADRENERGIC G PROTEIN-COUPLED RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-1 ADRENERGIC RECEPTOR; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 33-243,272-276,279-367; COMPND 5 SYNONYM: BETA-1 ADRENORECEPTOR, BETA-1 ADRENOCEPTOR, BETA-T; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MELEAGRIS GALLOPAVO; SOURCE 3 ORGANISM_COMMON: COMMON TURKEY,WILD TURKEY; SOURCE 4 ORGANISM_TAXID: 9103; SOURCE 5 GENE: ADRB1; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HIGH FIVE; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL1393 KEYWDS SEVEN-TRANSMEMBRANE HELIX RECEPTOR, G-PROTEIN COUPLED RECEPTOR, KEYWDS 2 RECEPTOR EXPDTA X-RAY DIFFRACTION AUTHOR J.J.HUANG,S.CHEN,J.J.ZHANG,X.Y.HUANG REVDAT 3 19-JUN-13 4GPO 1 JRNL REVDAT 2 24-APR-13 4GPO 1 REMARK REVDAT 1 27-FEB-13 4GPO 0 JRNL AUTH J.HUANG,S.CHEN,J.J.ZHANG,X.Y.HUANG JRNL TITL CRYSTAL STRUCTURE OF OLIGOMERIC BETA-1-ADRENERGIC G JRNL TITL 2 PROTEIN-COUPLED RECEPTORS IN LIGAND-FREE BASAL STATE. JRNL REF NAT.STRUCT.MOL.BIOL. V. 20 419 2013 JRNL REFN ISSN 1545-9993 JRNL PMID 23435379 JRNL DOI 10.1038/NSMB.2504 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.78 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990 REMARK 3 COMPLETENESS FOR RANGE (%) : 83.6 REMARK 3 NUMBER OF REFLECTIONS : 13006 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.312 REMARK 3 R VALUE (WORKING SET) : 0.310 REMARK 3 FREE R VALUE : 0.355 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 642 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.7804 - 5.9721 0.98 2964 177 0.2928 0.2971 REMARK 3 2 5.9721 - 4.7464 0.99 2931 140 0.2949 0.3491 REMARK 3 3 4.7464 - 4.1483 0.98 2881 152 0.2667 0.3223 REMARK 3 4 4.1483 - 3.7698 0.74 2160 100 0.3692 0.4754 REMARK 3 5 3.7698 - 3.5000 0.48 1428 73 0.4767 0.5524 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 0.50 REMARK 3 SHRINKAGE RADIUS : 0.16 REMARK 3 K_SOL : 0.25 REMARK 3 B_SOL : 25.91 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.540 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.800 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.46830 REMARK 3 B22 (A**2) : 3.76430 REMARK 3 B33 (A**2) : -9.56310 REMARK 3 B12 (A**2) : -0.00000 REMARK 3 B13 (A**2) : 12.37010 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.006 4554 REMARK 3 ANGLE : 1.136 6205 REMARK 3 CHIRALITY : 0.084 746 REMARK 3 PLANARITY : 0.005 745 REMARK 3 DIHEDRAL : 17.260 1593 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 19 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: chain 'A' and (resseq 35:66) REMARK 3 ORIGIN FOR THE GROUP (A): -32.0337 -0.0373 10.0043 REMARK 3 T TENSOR REMARK 3 T11: 0.2712 T22: -0.2136 REMARK 3 T33: 0.3455 T12: -0.0687 REMARK 3 T13: 0.0922 T23: -0.0856 REMARK 3 L TENSOR REMARK 3 L11: 0.7954 L22: 0.7802 REMARK 3 L33: 1.0011 L12: -0.3959 REMARK 3 L13: 0.1726 L23: -0.5226 REMARK 3 S TENSOR REMARK 3 S11: -0.0231 S12: 0.1115 S13: -0.1781 REMARK 3 S21: -0.2534 S22: -0.1329 S23: 0.1042 REMARK 3 S31: -0.0391 S32: 0.1053 S33: -0.0755 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: chain 'A' and (resseq 67:140) REMARK 3 ORIGIN FOR THE GROUP (A): -31.6779 14.8504 15.6039 REMARK 3 T TENSOR REMARK 3 T11: -0.7398 T22: -0.3670 REMARK 3 T33: -0.8309 T12: -0.1937 REMARK 3 T13: 0.6566 T23: 0.3722 REMARK 3 L TENSOR REMARK 3 L11: 1.1122 L22: 0.4606 REMARK 3 L33: 0.8440 L12: 0.2447 REMARK 3 L13: -0.2688 L23: -0.0798 REMARK 3 S TENSOR REMARK 3 S11: 0.3702 S12: -0.5973 S13: -0.3338 REMARK 3 S21: -0.2171 S22: -0.0432 S23: 0.4835 REMARK 3 S31: 0.0616 S32: 0.7148 S33: 0.7066 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: chain 'A' and (resseq 141:157) REMARK 3 ORIGIN FOR THE GROUP (A): -13.8172 29.0914 29.0225 REMARK 3 T TENSOR REMARK 3 T11: 0.4548 T22: 0.9595 REMARK 3 T33: -0.0206 T12: -0.1557 REMARK 3 T13: -0.3652 T23: -0.2423 REMARK 3 L TENSOR REMARK 3 L11: 0.0327 L22: 0.0052 REMARK 3 L33: 0.1351 L12: -0.0144 REMARK 3 L13: -0.0677 L23: 0.0427 REMARK 3 S TENSOR REMARK 3 S11: 0.0179 S12: -0.0971 S13: -0.0546 REMARK 3 S21: 0.0005 S22: 0.0745 S23: -0.0461 REMARK 3 S31: -0.0430 S32: 0.1693 S33: 0.0683 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: chain 'A' and (resseq 158:217) REMARK 3 ORIGIN FOR THE GROUP (A): -40.8465 24.3572 6.5952 REMARK 3 T TENSOR REMARK 3 T11: 0.1652 T22: -0.4242 REMARK 3 T33: -0.1209 T12: -0.0030 REMARK 3 T13: 0.0980 T23: 0.2858 REMARK 3 L TENSOR REMARK 3 L11: 0.5839 L22: 0.7618 REMARK 3 L33: 0.9321 L12: 0.1082 REMARK 3 L13: -0.1097 L23: -0.3028 REMARK 3 S TENSOR REMARK 3 S11: -0.0763 S12: -0.3164 S13: -0.1530 REMARK 3 S21: 0.0864 S22: 0.1918 S23: 0.4947 REMARK 3 S31: -0.3915 S32: 0.3469 S33: 0.0198 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: chain 'A' and (resseq 218:282) REMARK 3 ORIGIN FOR THE GROUP (A): -9.6302 26.8288 13.3294 REMARK 3 T TENSOR REMARK 3 T11: 0.4419 T22: 0.1795 REMARK 3 T33: 0.2844 T12: -0.4605 REMARK 3 T13: -0.1232 T23: -0.2258 REMARK 3 L TENSOR REMARK 3 L11: 0.5580 L22: 0.3792 REMARK 3 L33: 1.3548 L12: -0.1284 REMARK 3 L13: 0.6264 L23: -0.5970 REMARK 3 S TENSOR REMARK 3 S11: -0.2215 S12: -0.0302 S13: 0.4020 REMARK 3 S21: 0.0832 S22: -0.0800 S23: -0.1500 REMARK 3 S31: -0.1820 S32: 0.2668 S33: -0.2197 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: chain 'A' and (resseq 283:315) REMARK 3 ORIGIN FOR THE GROUP (A): -19.8691 18.5761 7.0111 REMARK 3 T TENSOR REMARK 3 T11: 0.3927 T22: 0.5006 REMARK 3 T33: 0.8922 T12: 0.0648 REMARK 3 T13: -0.9164 T23: -0.0196 REMARK 3 L TENSOR REMARK 3 L11: 3.0940 L22: 1.5531 REMARK 3 L33: 2.1557 L12: 0.3177 REMARK 3 L13: 0.8890 L23: 0.2918 REMARK 3 S TENSOR REMARK 3 S11: -0.0385 S12: -0.0583 S13: 0.0589 REMARK 3 S21: -0.3286 S22: -0.0366 S23: 0.0436 REMARK 3 S31: -0.1503 S32: -0.0595 S33: 0.0994 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: chain 'A' and (resseq 316:332) REMARK 3 ORIGIN FOR THE GROUP (A): -33.0823 14.4248 -5.7092 REMARK 3 T TENSOR REMARK 3 T11: 0.7105 T22: 0.4627 REMARK 3 T33: 0.5676 T12: 0.2702 REMARK 3 T13: -0.8007 T23: 0.0683 REMARK 3 L TENSOR REMARK 3 L11: 2.2998 L22: 0.1917 REMARK 3 L33: 3.0273 L12: -0.6009 REMARK 3 L13: 1.0169 L23: -0.5571 REMARK 3 S TENSOR REMARK 3 S11: -0.0359 S12: 0.7049 S13: 0.2198 REMARK 3 S21: -0.3927 S22: -0.0547 S23: 0.3170 REMARK 3 S31: -0.0078 S32: -0.1148 S33: 0.0056 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: chain 'A' and (resseq 333:356) REMARK 3 ORIGIN FOR THE GROUP (A): -18.1693 6.0357 19.5227 REMARK 3 T TENSOR REMARK 3 T11: 0.2919 T22: 0.3679 REMARK 3 T33: 0.5314 T12: 0.1552 REMARK 3 T13: -0.1098 T23: -0.3360 REMARK 3 L TENSOR REMARK 3 L11: 1.7356 L22: 1.7364 REMARK 3 L33: 2.6998 L12: -0.5247 REMARK 3 L13: 0.5474 L23: -2.1476 REMARK 3 S TENSOR REMARK 3 S11: -0.2679 S12: -0.5086 S13: -0.1597 REMARK 3 S21: 0.1584 S22: -0.0303 S23: -0.2384 REMARK 3 S31: 0.0643 S32: 0.4482 S33: -0.2193 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: chain 'B' and (resseq 35:66) REMARK 3 ORIGIN FOR THE GROUP (A): -35.320 -8.454 13.858 REMARK 3 T TENSOR REMARK 3 T11: 0.5534 T22: 0.0883 REMARK 3 T33: 0.6228 T12: 0.0796 REMARK 3 T13: -0.1417 T23: 0.0395 REMARK 3 L TENSOR REMARK 3 L11: 0.9366 L22: 0.5619 REMARK 3 L33: 0.9693 L12: 0.6383 REMARK 3 L13: -0.4117 L23: 0.0329 REMARK 3 S TENSOR REMARK 3 S11: -0.0043 S12: -0.1785 S13: -0.0662 REMARK 3 S21: -0.2307 S22: -0.1029 S23: 0.0969 REMARK 3 S31: -0.3263 S32: 0.2061 S33: 0.0335 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: chain 'B' and (resseq 67:92) REMARK 3 ORIGIN FOR THE GROUP (A): -19.5419 -22.282 19.8999 REMARK 3 T TENSOR REMARK 3 T11: 0.0425 T22: 0.1100 REMARK 3 T33: -0.1007 T12: -0.3162 REMARK 3 T13: 0.1692 T23: 0.3032 REMARK 3 L TENSOR REMARK 3 L11: 0.7269 L22: 0.7476 REMARK 3 L33: 1.7315 L12: -0.0942 REMARK 3 L13: 0.0253 L23: -0.6875 REMARK 3 S TENSOR REMARK 3 S11: -0.3173 S12: -0.1939 S13: 0.0786 REMARK 3 S21: 0.2771 S22: -0.3312 S23: -0.4278 REMARK 3 S31: 0.1036 S32: 0.6493 S33: -0.4515 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: chain 'B' and (resseq 93:110) REMARK 3 ORIGIN FOR THE GROUP (A): -40.9625 -14.698 3.1920 REMARK 3 T TENSOR REMARK 3 T11: 0.3690 T22: -0.0682 REMARK 3 T33: 0.5556 T12: 0.0720 REMARK 3 T13: -0.3093 T23: 0.1681 REMARK 3 L TENSOR REMARK 3 L11: 1.8378 L22: 1.4786 REMARK 3 L33: 5.1686 L12: 1.5638 REMARK 3 L13: -0.7985 L23: 0.1543 REMARK 3 S TENSOR REMARK 3 S11: -0.0063 S12: 0.1149 S13: 0.3276 REMARK 3 S21: -0.1671 S22: 0.1516 S23: 0.3846 REMARK 3 S31: -0.5482 S32: -0.3470 S33: 0.0248 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: chain 'B' and (resseq 111:140) REMARK 3 ORIGIN FOR THE GROUP (A): -31.2626 -29.115 13.6133 REMARK 3 T TENSOR REMARK 3 T11: -0.6536 T22: -0.2127 REMARK 3 T33: -0.1099 T12: 0.4566 REMARK 3 T13: 0.4497 T23: -0.2280 REMARK 3 L TENSOR REMARK 3 L11: 0.9418 L22: 0.3565 REMARK 3 L33: 0.9509 L12: -0.3460 REMARK 3 L13: 0.1434 L23: -0.0797 REMARK 3 S TENSOR REMARK 3 S11: 0.0649 S12: -0.2348 S13: 0.0722 REMARK 3 S21: 0.1962 S22: -0.1474 S23: 0.1026 REMARK 3 S31: 0.0544 S32: 0.0496 S33: -0.2642 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: chain 'B' and (resseq 141:157) REMARK 3 ORIGIN FOR THE GROUP (A): -13.2429 -37.477 28.4213 REMARK 3 T TENSOR REMARK 3 T11: 0.6841 T22: 1.5539 REMARK 3 T33: 1.3272 T12: 0.2191 REMARK 3 T13: -0.3270 T23: -0.2721 REMARK 3 L TENSOR REMARK 3 L11: -0.0056 L22: -0.0022 REMARK 3 L33: 0.0010 L12: 0.0020 REMARK 3 L13: -0.0009 L23: 0.0012 REMARK 3 S TENSOR REMARK 3 S11: -0.1471 S12: 0.1479 S13: -0.2235 REMARK 3 S21: -0.2485 S22: 0.2291 S23: 0.0573 REMARK 3 S31: 0.0045 S32: 0.1279 S33: -0.0345 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: chain 'B' and (resseq 158:217) REMARK 3 ORIGIN FOR THE GROUP (A): -40.0747 -32.861 5.7378 REMARK 3 T TENSOR REMARK 3 T11: -0.2909 T22: -0.0017 REMARK 3 T33: 0.0583 T12: 0.1576 REMARK 3 T13: -0.5946 T23: 0.0767 REMARK 3 L TENSOR REMARK 3 L11: 2.2779 L22: 1.1187 REMARK 3 L33: 1.2305 L12: 0.1125 REMARK 3 L13: 0.7443 L23: 0.1993 REMARK 3 S TENSOR REMARK 3 S11: -0.3048 S12: 0.0628 S13: 0.2196 REMARK 3 S21: -0.3600 S22: 0.0528 S23: 0.2668 REMARK 3 S31: -0.3339 S32: 0.1133 S33: -0.0928 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: chain 'B' and (resseq 218:282) REMARK 3 ORIGIN FOR THE GROUP (A): -27.7842 -35.155 35.8230 REMARK 3 T TENSOR REMARK 3 T11: 0.4870 T22: 0.4245 REMARK 3 T33: 0.6947 T12: 0.1436 REMARK 3 T13: -0.3469 T23: 0.0340 REMARK 3 L TENSOR REMARK 3 L11: 3.0874 L22: 0.5860 REMARK 3 L33: 0.0151 L12: 1.3479 REMARK 3 L13: 0.2065 L23: 0.0963 REMARK 3 S TENSOR REMARK 3 S11: 0.4125 S12: -0.8612 S13: -0.3804 REMARK 3 S21: 0.4597 S22: -0.2680 S23: -0.3146 REMARK 3 S31: 0.2061 S32: 0.1057 S33: -0.0855 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: chain 'B' and (resseq 283:302) REMARK 3 ORIGIN FOR THE GROUP (A): -28.0644 -24.739 32.3494 REMARK 3 T TENSOR REMARK 3 T11: 0.7642 T22: 0.5732 REMARK 3 T33: 0.8475 T12: 0.1095 REMARK 3 T13: -0.4950 T23: -0.0402 REMARK 3 L TENSOR REMARK 3 L11: 2.0875 L22: 1.6583 REMARK 3 L33: 4.9132 L12: -1.8472 REMARK 3 L13: 1.4259 L23: -1.3661 REMARK 3 S TENSOR REMARK 3 S11: -0.1155 S12: -0.3626 S13: 0.1948 REMARK 3 S21: 0.6684 S22: -0.0315 S23: -0.8926 REMARK 3 S31: -0.2616 S32: 0.5166 S33: 0.1239 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: chain 'B' and (resseq 303:323) REMARK 3 ORIGIN FOR THE GROUP (A): -50.9389 -28.652 16.7077 REMARK 3 T TENSOR REMARK 3 T11: 0.0525 T22: 0.6377 REMARK 3 T33: 1.0108 T12: -0.0008 REMARK 3 T13: -0.8840 T23: 0.2897 REMARK 3 L TENSOR REMARK 3 L11: 2.2913 L22: 1.7004 REMARK 3 L33: 1.6306 L12: -0.1193 REMARK 3 L13: 1.2394 L23: -0.0352 REMARK 3 S TENSOR REMARK 3 S11: -0.0566 S12: 0.1159 S13: 0.0459 REMARK 3 S21: -0.2312 S22: -0.1515 S23: 0.1726 REMARK 3 S31: -0.1383 S32: -0.5088 S33: -0.0861 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: chain 'B' and (resseq 324:345) REMARK 3 ORIGIN FOR THE GROUP (A): -36.3107 -18.469 20.7451 REMARK 3 T TENSOR REMARK 3 T11: 0.4054 T22: 0.2215 REMARK 3 T33: 1.0227 T12: 0.2491 REMARK 3 T13: -0.7491 T23: -0.1103 REMARK 3 L TENSOR REMARK 3 L11: 0.6072 L22: 3.1116 REMARK 3 L33: 0.6221 L12: -0.6399 REMARK 3 L13: -0.3651 L23: -0.0917 REMARK 3 S TENSOR REMARK 3 S11: -0.0070 S12: -0.0692 S13: 0.0106 REMARK 3 S21: 0.0281 S22: 0.1036 S23: -0.1241 REMARK 3 S31: 0.1140 S32: 0.0718 S33: 0.0480 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: chain 'B' and (resseq 346:356) REMARK 3 ORIGIN FOR THE GROUP (A): -16.1263 -11.407 27.9748 REMARK 3 T TENSOR REMARK 3 T11: 1.0827 T22: 1.5914 REMARK 3 T33: 1.1822 T12: -0.3367 REMARK 3 T13: -0.0707 T23: -0.2059 REMARK 3 L TENSOR REMARK 3 L11: 4.0273 L22: 8.3758 REMARK 3 L33: 2.5740 L12: 3.5373 REMARK 3 L13: -0.3229 L23: 0.2914 REMARK 3 S TENSOR REMARK 3 S11: -0.1110 S12: -0.1624 S13: -0.2455 REMARK 3 S21: 0.1316 S22: 0.0652 S23: 0.4547 REMARK 3 S31: 0.1678 S32: -0.4567 S33: -0.0079 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 1 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: chain A and (resseq 36:237 or resseq 280: REMARK 3 356 ) REMARK 3 SELECTION : chain B and (resseq 36:237 or resseq 280: REMARK 3 356 ) REMARK 3 ATOM PAIRS NUMBER : 2217 REMARK 3 RMSD : 0.020 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4GPO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-12. REMARK 100 THE RCSB ID CODE IS RCSB074481. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-SEP-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 3.6-4.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X25 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000 REMARK 200 MONOCHROMATOR : SI 111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17463 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.350 REMARK 200 RESOLUTION RANGE LOW (A) : 67.570 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2 REMARK 200 DATA REDUNDANCY : 4.300 REMARK 200 R MERGE (I) : 0.14100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.20 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2Y04 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 71.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM SODIUM ACETATE, 100-300MM REMARK 280 AMMONIUM SULFATE, 26~30% PEG200, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 114.83000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.79500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 114.83000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.79500 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30210 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 31 REMARK 465 GLY A 32 REMARK 465 ALA A 33 REMARK 465 GLU A 34 REMARK 465 LEU A 35 REMARK 465 ILE A 268 REMARK 465 ARG A 269 REMARK 465 LYS A 270 REMARK 465 ILE A 271 REMARK 465 ASP A 272 REMARK 465 ARG A 273 REMARK 465 ALA A 274 REMARK 465 SER A 275 REMARK 465 LYS A 276 REMARK 465 ARG A 277 REMARK 465 LYS A 278 REMARK 465 ARG A 279 REMARK 465 LEU A 357 REMARK 465 ALA A 358 REMARK 465 PHE A 359 REMARK 465 PRO A 360 REMARK 465 ARG A 361 REMARK 465 LYS A 362 REMARK 465 ALA A 363 REMARK 465 ASP A 364 REMARK 465 ARG A 365 REMARK 465 ARG A 366 REMARK 465 LEU A 367 REMARK 465 HIS A 368 REMARK 465 HIS A 369 REMARK 465 HIS A 370 REMARK 465 HIS A 371 REMARK 465 HIS A 372 REMARK 465 HIS A 373 REMARK 465 MET B 31 REMARK 465 GLY B 32 REMARK 465 ALA B 33 REMARK 465 GLU B 34 REMARK 465 LEU B 35 REMARK 465 ARG B 269 REMARK 465 LYS B 270 REMARK 465 ILE B 271 REMARK 465 ASP B 272 REMARK 465 ARG B 273 REMARK 465 ALA B 274 REMARK 465 SER B 275 REMARK 465 LYS B 276 REMARK 465 ARG B 277 REMARK 465 LYS B 278 REMARK 465 ARG B 279 REMARK 465 LEU B 357 REMARK 465 ALA B 358 REMARK 465 PHE B 359 REMARK 465 PRO B 360 REMARK 465 ARG B 361 REMARK 465 LYS B 362 REMARK 465 ALA B 363 REMARK 465 ASP B 364 REMARK 465 ARG B 365 REMARK 465 ARG B 366 REMARK 465 LEU B 367 REMARK 465 HIS B 368 REMARK 465 HIS B 369 REMARK 465 HIS B 370 REMARK 465 HIS B 371 REMARK 465 HIS B 372 REMARK 465 HIS B 373 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 A 143 -73.07 -123.52 REMARK 500 ILE A 209 -62.29 -108.76 REMARK 500 PHE A 216 -60.72 -131.90 REMARK 500 ILE B 143 -73.06 -123.08 REMARK 500 ILE B 209 -61.89 -108.36 REMARK 500 PHE B 216 -60.16 -131.19 REMARK 500 REMARK 500 REMARK: NULL DBREF 4GPO A 31 368 UNP P07700 ADRB1_MELGA 31 368 DBREF 4GPO B 31 368 UNP P07700 ADRB1_MELGA 31 368 SEQADV 4GPO MET A 31 UNP P07700 VAL 31 CONFLICT SEQADV 4GPO GLY A 32 UNP P07700 SER 32 CONFLICT SEQADV 4GPO SER A 68 UNP P07700 ARG 68 CONFLICT SEQADV 4GPO VAL A 90 UNP P07700 MET 90 CONFLICT SEQADV 4GPO LEU A 116 UNP P07700 CYS 116 CONFLICT SEQADV 4GPO ALA A 227 UNP P07700 TYR 227 CONFLICT SEQADV 4GPO A UNP P07700 ARG 243 DELETION SEQADV 4GPO A UNP P07700 CYS 244 DELETION SEQADV 4GPO A UNP P07700 GLU 245 DELETION SEQADV 4GPO A UNP P07700 GLY 246 DELETION SEQADV 4GPO A UNP P07700 ARG 247 DELETION SEQADV 4GPO A UNP P07700 PHE 248 DELETION SEQADV 4GPO A UNP P07700 TYR 249 DELETION SEQADV 4GPO A UNP P07700 GLY 250 DELETION SEQADV 4GPO A UNP P07700 SER 251 DELETION SEQADV 4GPO A UNP P07700 GLN 252 DELETION SEQADV 4GPO A UNP P07700 GLU 253 DELETION SEQADV 4GPO A UNP P07700 GLN 254 DELETION SEQADV 4GPO A UNP P07700 PRO 255 DELETION SEQADV 4GPO A UNP P07700 GLN 256 DELETION SEQADV 4GPO A UNP P07700 PRO 257 DELETION SEQADV 4GPO A UNP P07700 PRO 258 DELETION SEQADV 4GPO A UNP P07700 PRO 259 DELETION SEQADV 4GPO A UNP P07700 LEU 260 DELETION SEQADV 4GPO A UNP P07700 PRO 261 DELETION SEQADV 4GPO A UNP P07700 GLN 262 DELETION SEQADV 4GPO A UNP P07700 HIS 263 DELETION SEQADV 4GPO A UNP P07700 GLN 264 DELETION SEQADV 4GPO A UNP P07700 PRO 265 DELETION SEQADV 4GPO A UNP P07700 ILE 266 DELETION SEQADV 4GPO A UNP P07700 LEU 267 DELETION SEQADV 4GPO A UNP P07700 GLY 268 DELETION SEQADV 4GPO A UNP P07700 ASN 269 DELETION SEQADV 4GPO A UNP P07700 GLY 270 DELETION SEQADV 4GPO A UNP P07700 THR 277 DELETION SEQADV 4GPO A UNP P07700 SER 278 DELETION SEQADV 4GPO LEU A 282 UNP P07700 ALA 282 CONFLICT SEQADV 4GPO ALA A 327 UNP P07700 PHE 327 CONFLICT SEQADV 4GPO MET A 338 UNP P07700 PHE 338 CONFLICT SEQADV 4GPO ALA A 358 UNP P07700 CYS 358 CONFLICT SEQADV 4GPO HIS A 369 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS A 370 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS A 371 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS A 372 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS A 373 UNP P07700 EXPRESSION TAG SEQADV 4GPO MET B 31 UNP P07700 VAL 31 CONFLICT SEQADV 4GPO GLY B 32 UNP P07700 SER 32 CONFLICT SEQADV 4GPO SER B 68 UNP P07700 ARG 68 CONFLICT SEQADV 4GPO VAL B 90 UNP P07700 MET 90 CONFLICT SEQADV 4GPO LEU B 116 UNP P07700 CYS 116 CONFLICT SEQADV 4GPO ALA B 227 UNP P07700 TYR 227 CONFLICT SEQADV 4GPO B UNP P07700 ARG 243 DELETION SEQADV 4GPO B UNP P07700 CYS 244 DELETION SEQADV 4GPO B UNP P07700 GLU 245 DELETION SEQADV 4GPO B UNP P07700 GLY 246 DELETION SEQADV 4GPO B UNP P07700 ARG 247 DELETION SEQADV 4GPO B UNP P07700 PHE 248 DELETION SEQADV 4GPO B UNP P07700 TYR 249 DELETION SEQADV 4GPO B UNP P07700 GLY 250 DELETION SEQADV 4GPO B UNP P07700 SER 251 DELETION SEQADV 4GPO B UNP P07700 GLN 252 DELETION SEQADV 4GPO B UNP P07700 GLU 253 DELETION SEQADV 4GPO B UNP P07700 GLN 254 DELETION SEQADV 4GPO B UNP P07700 PRO 255 DELETION SEQADV 4GPO B UNP P07700 GLN 256 DELETION SEQADV 4GPO B UNP P07700 PRO 257 DELETION SEQADV 4GPO B UNP P07700 PRO 258 DELETION SEQADV 4GPO B UNP P07700 PRO 259 DELETION SEQADV 4GPO B UNP P07700 LEU 260 DELETION SEQADV 4GPO B UNP P07700 PRO 261 DELETION SEQADV 4GPO B UNP P07700 GLN 262 DELETION SEQADV 4GPO B UNP P07700 HIS 263 DELETION SEQADV 4GPO B UNP P07700 GLN 264 DELETION SEQADV 4GPO B UNP P07700 PRO 265 DELETION SEQADV 4GPO B UNP P07700 ILE 266 DELETION SEQADV 4GPO B UNP P07700 LEU 267 DELETION SEQADV 4GPO B UNP P07700 GLY 268 DELETION SEQADV 4GPO B UNP P07700 ASN 269 DELETION SEQADV 4GPO B UNP P07700 GLY 270 DELETION SEQADV 4GPO B UNP P07700 THR 277 DELETION SEQADV 4GPO B UNP P07700 SER 278 DELETION SEQADV 4GPO LEU B 282 UNP P07700 ALA 282 CONFLICT SEQADV 4GPO ALA B 327 UNP P07700 PHE 327 CONFLICT SEQADV 4GPO MET B 338 UNP P07700 PHE 338 CONFLICT SEQADV 4GPO ALA B 358 UNP P07700 CYS 358 CONFLICT SEQADV 4GPO HIS B 369 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS B 370 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS B 371 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS B 372 UNP P07700 EXPRESSION TAG SEQADV 4GPO HIS B 373 UNP P07700 EXPRESSION TAG SEQRES 1 A 313 MET GLY ALA GLU LEU LEU SER GLN GLN TRP GLU ALA GLY SEQRES 2 A 313 MET SER LEU LEU MET ALA LEU VAL VAL LEU LEU ILE VAL SEQRES 3 A 313 ALA GLY ASN VAL LEU VAL ILE ALA ALA ILE GLY SER THR SEQRES 4 A 313 GLN ARG LEU GLN THR LEU THR ASN LEU PHE ILE THR SER SEQRES 5 A 313 LEU ALA CYS ALA ASP LEU VAL VAL GLY LEU LEU VAL VAL SEQRES 6 A 313 PRO PHE GLY ALA THR LEU VAL VAL ARG GLY THR TRP LEU SEQRES 7 A 313 TRP GLY SER PHE LEU CYS GLU LEU TRP THR SER LEU ASP SEQRES 8 A 313 VAL LEU CYS VAL THR ALA SER ILE GLU THR LEU CYS VAL SEQRES 9 A 313 ILE ALA ILE ASP ARG TYR LEU ALA ILE THR SER PRO PHE SEQRES 10 A 313 ARG TYR GLN SER LEU MET THR ARG ALA ARG ALA LYS VAL SEQRES 11 A 313 ILE ILE CYS THR VAL TRP ALA ILE SER ALA LEU VAL SER SEQRES 12 A 313 PHE LEU PRO ILE MET MET HIS TRP TRP ARG ASP GLU ASP SEQRES 13 A 313 PRO GLN ALA LEU LYS CYS TYR GLN ASP PRO GLY CYS CYS SEQRES 14 A 313 ASP PHE VAL THR ASN ARG ALA TYR ALA ILE ALA SER SER SEQRES 15 A 313 ILE ILE SER PHE TYR ILE PRO LEU LEU ILE MET ILE PHE SEQRES 16 A 313 VAL ALA LEU ARG VAL TYR ARG GLU ALA LYS GLU GLN ILE SEQRES 17 A 313 ARG LYS ILE ASP ARG ALA SER LYS ARG LYS ARG VAL MET SEQRES 18 A 313 LEU MET ARG GLU HIS LYS ALA LEU LYS THR LEU GLY ILE SEQRES 19 A 313 ILE MET GLY VAL PHE THR LEU CYS TRP LEU PRO PHE PHE SEQRES 20 A 313 LEU VAL ASN ILE VAL ASN VAL PHE ASN ARG ASP LEU VAL SEQRES 21 A 313 PRO ASP TRP LEU PHE VAL ALA PHE ASN TRP LEU GLY TYR SEQRES 22 A 313 ALA ASN SER ALA MET ASN PRO ILE ILE TYR CYS ARG SER SEQRES 23 A 313 PRO ASP PHE ARG LYS ALA PHE LYS ARG LEU LEU ALA PHE SEQRES 24 A 313 PRO ARG LYS ALA ASP ARG ARG LEU HIS HIS HIS HIS HIS SEQRES 25 A 313 HIS SEQRES 1 B 313 MET GLY ALA GLU LEU LEU SER GLN GLN TRP GLU ALA GLY SEQRES 2 B 313 MET SER LEU LEU MET ALA LEU VAL VAL LEU LEU ILE VAL SEQRES 3 B 313 ALA GLY ASN VAL LEU VAL ILE ALA ALA ILE GLY SER THR SEQRES 4 B 313 GLN ARG LEU GLN THR LEU THR ASN LEU PHE ILE THR SER SEQRES 5 B 313 LEU ALA CYS ALA ASP LEU VAL VAL GLY LEU LEU VAL VAL SEQRES 6 B 313 PRO PHE GLY ALA THR LEU VAL VAL ARG GLY THR TRP LEU SEQRES 7 B 313 TRP GLY SER PHE LEU CYS GLU LEU TRP THR SER LEU ASP SEQRES 8 B 313 VAL LEU CYS VAL THR ALA SER ILE GLU THR LEU CYS VAL SEQRES 9 B 313 ILE ALA ILE ASP ARG TYR LEU ALA ILE THR SER PRO PHE SEQRES 10 B 313 ARG TYR GLN SER LEU MET THR ARG ALA ARG ALA LYS VAL SEQRES 11 B 313 ILE ILE CYS THR VAL TRP ALA ILE SER ALA LEU VAL SER SEQRES 12 B 313 PHE LEU PRO ILE MET MET HIS TRP TRP ARG ASP GLU ASP SEQRES 13 B 313 PRO GLN ALA LEU LYS CYS TYR GLN ASP PRO GLY CYS CYS SEQRES 14 B 313 ASP PHE VAL THR ASN ARG ALA TYR ALA ILE ALA SER SER SEQRES 15 B 313 ILE ILE SER PHE TYR ILE PRO LEU LEU ILE MET ILE PHE SEQRES 16 B 313 VAL ALA LEU ARG VAL TYR ARG GLU ALA LYS GLU GLN ILE SEQRES 17 B 313 ARG LYS ILE ASP ARG ALA SER LYS ARG LYS ARG VAL MET SEQRES 18 B 313 LEU MET ARG GLU HIS LYS ALA LEU LYS THR LEU GLY ILE SEQRES 19 B 313 ILE MET GLY VAL PHE THR LEU CYS TRP LEU PRO PHE PHE SEQRES 20 B 313 LEU VAL ASN ILE VAL ASN VAL PHE ASN ARG ASP LEU VAL SEQRES 21 B 313 PRO ASP TRP LEU PHE VAL ALA PHE ASN TRP LEU GLY TYR SEQRES 22 B 313 ALA ASN SER ALA MET ASN PRO ILE ILE TYR CYS ARG SER SEQRES 23 B 313 PRO ASP PHE ARG LYS ALA PHE LYS ARG LEU LEU ALA PHE SEQRES 24 B 313 PRO ARG LYS ALA ASP ARG ARG LEU HIS HIS HIS HIS HIS SEQRES 25 B 313 HIS HELIX 1 1 LEU A 36 ALA A 42 1 7 HELIX 2 2 ALA A 42 SER A 68 1 27 HELIX 3 3 THR A 74 ASN A 77 5 4 HELIX 4 4 LEU A 78 GLY A 91 1 14 HELIX 5 5 LEU A 93 ARG A 104 1 12 HELIX 6 6 GLY A 110 ARG A 139 1 30 HELIX 7 7 ARG A 148 MET A 153 1 6 HELIX 8 8 ALA A 156 MET A 179 1 24 HELIX 9 9 ASP A 186 ASP A 195 1 10 HELIX 10 10 ALA A 206 PHE A 216 1 11 HELIX 11 11 PHE A 216 ALA A 234 1 19 HELIX 12 12 LEU A 282 ASN A 316 1 35 HELIX 13 13 PRO A 321 ASN A 339 1 19 HELIX 14 14 PRO A 340 ARG A 345 5 6 HELIX 15 15 SER A 346 ARG A 355 1 10 HELIX 16 16 SER B 37 ALA B 42 1 6 HELIX 17 17 ALA B 42 SER B 68 1 27 HELIX 18 18 THR B 74 ASN B 77 5 4 HELIX 19 19 LEU B 78 GLY B 91 1 14 HELIX 20 20 LEU B 93 ARG B 104 1 12 HELIX 21 21 GLY B 110 ARG B 139 1 30 HELIX 22 22 ARG B 148 MET B 153 1 6 HELIX 23 23 ALA B 156 MET B 179 1 24 HELIX 24 24 ASP B 186 ASP B 195 1 10 HELIX 25 25 ALA B 206 PHE B 216 1 11 HELIX 26 26 PHE B 216 ALA B 234 1 19 HELIX 27 27 LEU B 282 ASN B 316 1 35 HELIX 28 28 PRO B 321 ASN B 339 1 19 HELIX 29 29 PRO B 340 ARG B 345 5 6 HELIX 30 30 SER B 346 ARG B 355 1 10 SSBOND 1 CYS A 114 CYS A 199 1555 1555 2.03 SSBOND 2 CYS A 192 CYS A 198 1555 1555 2.03 SSBOND 3 CYS B 114 CYS B 199 1555 1555 2.03 SSBOND 4 CYS B 192 CYS B 198 1555 1555 2.03 CRYST1 229.660 79.590 69.040 90.00 101.83 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.004354 0.000000 0.000912 0.00000 SCALE2 0.000000 0.012564 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014799 0.00000 ATOM 1 N LEU A 36 -41.719 -8.351 -8.772 1.00102.61 N ANISOU 1 N LEU A 36 14271 10940 13775 -210 187 -1255 N ATOM 2 CA LEU A 36 -40.411 -7.891 -8.313 1.00 99.24 C ANISOU 2 CA LEU A 36 13715 10589 13401 -188 276 -1214 C ATOM 3 C LEU A 36 -40.531 -6.813 -7.236 1.00 80.15 C ANISOU 3 C LEU A 36 11379 8224 10849 -215 298 -1078 C ATOM 4 O LEU A 36 -39.667 -6.696 -6.366 1.00 27.52 O ANISOU 4 O LEU A 36 4934 1565 3956 -22 -221 -922 O ATOM 5 CB LEU A 36 -39.574 -7.370 -9.490 1.00 96.08 C ANISOU 5 CB LEU A 36 13194 10210 13103 -94 166 -1308 C ATOM 6 CG LEU A 36 -38.154 -6.872 -9.191 1.00 78.78 C ANISOU 6 CG LEU A 36 10910 8071 10953 6 35 -1275 C ATOM 7 CD1 LEU A 36 -37.275 -8.011 -8.704 1.00 97.89 C ANISOU 7 CD1 LEU A 36 13329 10473 13390 64 -47 -1268 C ATOM 8 CD2 LEU A 36 -37.527 -6.208 -10.407 1.00 48.82 C ANISOU 8 CD2 LEU A 36 7234 4264 7053 52 41 -1302 C ATOM 9 N SER A 37 -41.608 -6.035 -7.289 1.00105.98 N ANISOU 9 N SER A 37 14660 11493 14113 -227 224 -1079 N ATOM 10 CA SER A 37 -41.769 -4.887 -6.397 1.00124.88 C ANISOU 10 CA SER A 37 17092 13936 16420 -229 188 -978 C ATOM 11 C SER A 37 -42.034 -5.282 -4.945 1.00109.65 C ANISOU 11 C SER A 37 15209 12000 14454 -202 14 -899 C ATOM 12 O SER A 37 -41.602 -4.589 -4.026 1.00 91.48 O ANISOU 12 O SER A 37 12861 9746 12153 -169 -72 -835 O ATOM 13 CB SER A 37 -42.881 -3.959 -6.897 1.00147.53 C ANISOU 13 CB SER A 37 19879 16805 19370 -243 156 -1032 C ATOM 14 OG SER A 37 -42.929 -2.761 -6.138 1.00146.38 O ANISOU 14 OG SER A 37 19724 16711 19183 -245 155 -955 O ATOM 15 N GLN A 38 -42.750 -6.386 -4.746 1.00107.85 N ANISOU 15 N GLN A 38 14953 11718 14307 -228 -1 -946 N ATOM 16 CA GLN A 38 -43.063 -6.865 -3.401 1.00 99.06 C ANISOU 16 CA GLN A 38 13760 10601 13278 -236 -55 -918 C ATOM 17 C GLN A 38 -41.856 -7.525 -2.739 1.00101.67 C ANISOU 17 C GLN A 38 14074 10941 13615 -200 -74 -886 C ATOM 18 O GLN A 38 -41.816 -7.689 -1.515 1.00 71.52 O ANISOU 18 O GLN A 38 10162 7138 9876 -212 -68 -859 O ATOM 19 CB GLN A 38 -44.249 -7.834 -3.431 1.00 81.72 C ANISOU 19 CB GLN A 38 11538 8335 11177 -279 -73 -979 C ATOM 20 CG GLN A 38 -45.577 -7.201 -3.054 1.00 87.68 C ANISOU 20 CG GLN A 38 12209 9102 12005 -306 -107 -980 C ATOM 21 CD GLN A 38 -45.612 -6.728 -1.610 1.00 93.38 C ANISOU 21 CD GLN A 38 12817 9889 12774 -300 -109 -911 C ATOM 22 OE1 GLN A 38 -44.780 -7.122 -0.791 1.00 74.01 O ANISOU 22 OE1 GLN A 38 10329 7460 10332 -286 -87 -874 O ATOM 23 NE2 GLN A 38 -46.582 -5.878 -1.292 1.00102.24 N ANISOU 23 NE2 GLN A 38 13870 11043 13935 -308 -128 -897 N ATOM 24 N GLN A 39 -40.883 -7.914 -3.559 1.00116.18 N ANISOU 24 N GLN A 39 15989 12769 15387 -155 -90 -898 N ATOM 25 CA GLN A 39 -39.633 -8.479 -3.063 1.00100.39 C ANISOU 25 CA GLN A 39 13936 10778 13431 -111 -113 -887 C ATOM 26 C GLN A 39 -38.703 -7.370 -2.588 1.00 83.12 C ANISOU 26 C GLN A 39 11655 8658 11267 -89 -108 -846 C ATOM 27 O GLN A 39 -37.837 -7.584 -1.744 1.00 67.54 O ANISOU 27 O GLN A 39 9614 6702 9347 -92 -52 -824 O ATOM 28 CB GLN A 39 -38.957 -9.327 -4.142 1.00 84.19 C ANISOU 28 CB GLN A 39 11963 8686 11339 -55 -156 -933 C ATOM 29 CG GLN A 39 -39.696 -10.618 -4.452 1.00 85.88 C ANISOU 29 CG GLN A 39 12275 8820 11534 -96 -108 -974 C ATOM 30 CD GLN A 39 -39.158 -11.319 -5.680 1.00109.28 C ANISOU 30 CD GLN A 39 15368 11740 14412 -49 -115 -1017 C ATOM 31 OE1 GLN A 39 -38.341 -10.766 -6.418 1.00118.85 O ANISOU 31 OE1 GLN A 39 16504 12994 15660 64 -286 -1048 O ATOM 32 NE2 GLN A 39 -39.614 -12.545 -5.909 1.00117.92 N ANISOU 32 NE2 GLN A 39 16520 12758 15525 -101 -15 -1068 N ATOM 33 N TRP A 40 -38.874 -6.185 -3.156 1.00 81.05 N ANISOU 33 N TRP A 40 11400 8429 10965 -74 -148 -838 N ATOM 34 CA TRP A 40 -38.174 -5.010 -2.659 1.00 57.34 C ANISOU 34 CA TRP A 40 8313 5483 7991 -74 -119 -800 C ATOM 35 C TRP A 40 -38.887 -4.418 -1.446 1.00 48.36 C ANISOU 35 C TRP A 40 7136 4372 6865 -122 -81 -754 C ATOM 36 O TRP A 40 -38.238 -4.032 -0.478 1.00 29.47 O ANISOU 36 O TRP A 40 4673 2020 4506 -137 -22 -715 O ATOM 37 CB TRP A 40 -37.995 -3.971 -3.767 1.00 64.42 C ANISOU 37 CB TRP A 40 9187 6400 8889 -36 -172 -826 C ATOM 38 CG TRP A 40 -36.590 -3.919 -4.311 1.00 80.07 C ANISOU 38 CG TRP A 40 11134 8385 10903 -10 -108 -849 C ATOM 39 CD1 TRP A 40 -35.855 -2.795 -4.577 1.00 78.74 C ANISOU 39 CD1 TRP A 40 10949 8241 10729 -12 -54 -831 C ATOM 40 CD2 TRP A 40 -35.746 -5.032 -4.638 1.00 81.78 C ANISOU 40 CD2 TRP A 40 11376 8569 11128 15 -71 -882 C ATOM 41 NE1 TRP A 40 -34.614 -3.137 -5.057 1.00 69.19 N ANISOU 41 NE1 TRP A 40 9771 7018 9501 9 18 -840 N ATOM 42 CE2 TRP A 40 -34.521 -4.504 -5.103 1.00 86.72 C ANISOU 42 CE2 TRP A 40 12011 9200 11738 30 8 -878 C ATOM 43 CE3 TRP A 40 -35.906 -6.421 -4.586 1.00 71.71 C ANISOU 43 CE3 TRP A 40 10133 7253 9861 27 -94 -912 C ATOM 44 CZ2 TRP A 40 -33.465 -5.321 -5.512 1.00 94.05 C ANISOU 44 CZ2 TRP A 40 12972 10119 12645 59 75 -891 C ATOM 45 CZ3 TRP A 40 -34.856 -7.227 -4.994 1.00 72.57 C ANISOU 45 CZ3 TRP A 40 10260 7335 9980 60 -42 -945 C ATOM 46 CH2 TRP A 40 -33.655 -6.677 -5.449 1.00 82.08 C ANISOU 46 CH2 TRP A 40 11471 8554 11160 78 42 -937 C ATOM 47 N GLU A 41 -40.218 -4.363 -1.503 1.00 68.64 N ANISOU 47 N GLU A 41 9745 6924 9411 -149 -95 -760 N ATOM 48 CA GLU A 41 -41.042 -3.871 -0.392 1.00 89.22 C ANISOU 48 CA GLU A 41 12288 9550 12060 -187 -64 -734 C ATOM 49 C GLU A 41 -40.685 -4.542 0.933 1.00 98.57 C ANISOU 49 C GLU A 41 13359 10769 13325 -202 -4 -709 C ATOM 50 O GLU A 41 -40.543 -3.879 1.963 1.00 90.15 O ANISOU 50 O GLU A 41 12207 9763 12284 -210 37 -668 O ATOM 51 CB GLU A 41 -42.536 -4.081 -0.674 1.00 94.21 C ANISOU 51 CB GLU A 41 12947 10144 12704 -218 -67 -766 C ATOM 52 CG GLU A 41 -43.178 -3.026 -1.562 1.00103.85 C ANISOU 52 CG GLU A 41 14225 11373 13861 -221 -71 -773 C ATOM 53 CD GLU A 41 -44.649 -2.801 -1.233 1.00101.73 C ANISOU 53 CD GLU A 41 13907 11085 13659 -254 -70 -793 C ATOM 54 OE1 GLU A 41 -45.060 -3.095 -0.089 1.00 89.94 O ANISOU 54 OE1 GLU A 41 12310 9614 12251 -262 -73 -774 O ATOM 55 OE2 GLU A 41 -45.395 -2.327 -2.116 1.00106.56 O ANISOU 55 OE2 GLU A 41 14549 11680 14258 -265 -66 -827 O ATOM 56 N ALA A 42 -40.578 -5.866 0.912 1.00 97.73 N ANISOU 56 N ALA A 42 13251 10628 13254 -204 7 -733 N ATOM 57 CA ALA A 42 -40.132 -6.598 2.088 1.00 84.78 C ANISOU 57 CA ALA A 42 11503 9024 11684 -214 73 -707 C ATOM 58 C ALA A 42 -38.619 -6.831 2.057 1.00115.23 C ANISOU 58 C ALA A 42 15358 12901 15522 -194 118 -693 C ATOM 59 O ALA A 42 -38.034 -7.282 3.043 1.00129.51 O ANISOU 59 O ALA A 42 17084 14749 17373 -202 190 -664 O ATOM 60 CB ALA A 42 -40.886 -7.911 2.215 1.00 52.91 C ANISOU 60 CB ALA A 42 7452 4940 7712 -231 66 -738 C ATOM 61 N GLY A 43 -37.990 -6.515 0.924 1.00102.60 N ANISOU 61 N GLY A 43 13844 11276 13864 -165 81 -714 N ATOM 62 CA GLY A 43 -36.561 -6.729 0.750 1.00 69.58 C ANISOU 62 CA GLY A 43 9656 7111 9672 -144 131 -704 C ATOM 63 C GLY A 43 -35.657 -5.763 1.496 1.00 54.38 C ANISOU 63 C GLY A 43 7661 5264 7737 -157 207 -647 C ATOM 64 O GLY A 43 -34.739 -6.180 2.203 1.00 57.28 O ANISOU 64 O GLY A 43 7976 5667 8122 -164 291 -618 O ATOM 65 N MET A 44 -35.904 -4.467 1.333 1.00 50.13 N ANISOU 65 N MET A 44 7131 4747 7168 -160 178 -632 N ATOM 66 CA MET A 44 -35.100 -3.453 2.018 1.00 70.31 C ANISOU 66 CA MET A 44 9637 7369 9708 -175 242 -581 C ATOM 67 C MET A 44 -35.716 -2.866 3.292 1.00 78.58 C ANISOU 67 C MET A 44 10616 8462 10778 -199 260 -548 C ATOM 68 O MET A 44 -35.111 -2.007 3.934 1.00 94.40 O ANISOU 68 O MET A 44 12587 10515 12767 -210 304 -510 O ATOM 69 CB MET A 44 -34.681 -2.344 1.054 1.00103.88 C ANISOU 69 CB MET A 44 13939 11617 13915 -161 215 -580 C ATOM 70 CG MET A 44 -33.750 -2.840 -0.046 1.00126.88 C ANISOU 70 CG MET A 44 16900 14500 16807 -133 231 -604 C ATOM 71 SD MET A 44 -32.772 -4.273 0.473 1.00196.72 S ANISOU 71 SD MET A 44 25720 23351 25673 -132 319 -594 S ATOM 72 CE MET A 44 -31.718 -4.530 -0.960 1.00 21.69 C ANISOU 72 CE MET A 44 3626 1149 3466 -90 338 -620 C ATOM 73 N SER A 45 -36.914 -3.319 3.648 1.00 82.26 N ANISOU 73 N SER A 45 11065 8910 11280 -206 228 -566 N ATOM 74 CA SER A 45 -37.540 -2.917 4.902 1.00100.69 C ANISOU 74 CA SER A 45 13325 11285 13647 -222 253 -540 C ATOM 75 C SER A 45 -36.707 -3.423 6.081 1.00 71.53 C ANISOU 75 C SER A 45 9550 7641 9987 -229 341 -510 C ATOM 76 O SER A 45 -36.397 -2.681 7.027 1.00 63.25 O ANISOU 76 O SER A 45 8458 6642 8934 -236 380 -477 O ATOM 77 CB SER A 45 -38.958 -3.472 4.974 1.00 20.35 C ANISOU 77 CB SER A 45 3139 1077 3516 -227 212 -567 C ATOM 78 OG SER A 45 -38.959 -4.860 4.733 1.00 20.93 O ANISOU 78 OG SER A 45 3214 1113 3626 -227 216 -593 O ATOM 79 N LEU A 46 -36.338 -4.695 6.010 1.00 19.77 N ANISOU 79 N LEU A 46 2984 1066 3462 -227 370 -523 N ATOM 80 CA LEU A 46 -35.431 -5.281 6.981 1.00 70.32 C ANISOU 80 CA LEU A 46 9319 7507 9891 -231 455 -496 C ATOM 81 C LEU A 46 -34.188 -4.408 7.103 1.00 64.41 C ANISOU 81 C LEU A 46 8578 6801 9093 -231 501 -462 C ATOM 82 O LEU A 46 -33.818 -3.978 8.199 1.00 85.49 O ANISOU 82 O LEU A 46 11193 9521 11769 -238 549 -431 O ATOM 83 CB LEU A 46 -35.034 -6.691 6.540 1.00 98.68 C ANISOU 83 CB LEU A 46 12928 11058 13508 -223 471 -518 C ATOM 84 CG LEU A 46 -34.724 -7.744 7.609 1.00 79.94 C ANISOU 84 CG LEU A 46 10477 8703 11195 -227 541 -502 C ATOM 85 CD1 LEU A 46 -35.990 -8.510 8.026 1.00 53.99 C ANISOU 85 CD1 LEU A 46 7149 5387 7978 -234 511 -523 C ATOM 86 CD2 LEU A 46 -33.663 -8.701 7.095 1.00 59.58 C ANISOU 86 CD2 LEU A 46 7931 6097 8609 -216 578 -509 C ATOM 87 N LEU A 47 -33.555 -4.136 5.965 1.00 72.66 N ANISOU 87 N LEU A 47 9694 7823 10091 -223 484 -470 N ATOM 88 CA LEU A 47 -32.300 -3.382 5.933 1.00 92.67 C ANISOU 88 CA LEU A 47 12238 10390 12581 -225 531 -437 C ATOM 89 C LEU A 47 -32.394 -1.974 6.530 1.00101.21 C ANISOU 89 C LEU A 47 13307 11509 13639 -237 519 -411 C ATOM 90 O LEU A 47 -31.558 -1.566 7.356 1.00 96.41 O ANISOU 90 O LEU A 47 12666 10943 13023 -245 572 -378 O ATOM 91 CB LEU A 47 -31.758 -3.306 4.507 1.00 68.72 C ANISOU 91 CB LEU A 47 9285 7320 9507 -211 510 -453 C ATOM 92 CG LEU A 47 -30.512 -2.428 4.382 1.00 73.55 C ANISOU 92 CG LEU A 47 9911 7961 10075 -215 558 -416 C ATOM 93 CD1 LEU A 47 -29.619 -2.942 3.265 1.00100.34 C ANISOU 93 CD1 LEU A 47 13360 11323 13443 -196 584 -424 C ATOM 94 CD2 LEU A 47 -30.860 -0.940 4.190 1.00 18.40 C ANISOU 94 CD2 LEU A 47 2950 983 3057 -224 508 -405 C ATOM 95 N MET A 48 -33.393 -1.221 6.084 1.00 89.44 N ANISOU 95 N MET A 48 11851 9997 12136 -236 446 -427 N ATOM 96 CA MET A 48 -33.662 0.079 6.674 1.00 75.41 C ANISOU 96 CA MET A 48 10068 8245 10341 -245 426 -406 C ATOM 97 C MET A 48 -33.773 -0.061 8.194 1.00103.90 C ANISOU 97 C MET A 48 13602 11894 13981 -251 469 -387 C ATOM 98 O MET A 48 -33.203 0.739 8.939 1.00123.05 O ANISOU 98 O MET A 48 16015 14351 16389 -258 491 -361 O ATOM 99 CB MET A 48 -34.932 0.694 6.085 1.00 30.47 C ANISOU 99 CB MET A 48 4417 2519 4643 -238 341 -429 C ATOM 100 CG MET A 48 -34.808 1.124 4.632 1.00 24.67 C ANISOU 100 CG MET A 48 3756 1745 3872 -228 290 -446 C ATOM 101 SD MET A 48 -36.066 2.344 4.183 1.00118.39 S ANISOU 101 SD MET A 48 15669 13585 15727 -221 195 -459 S ATOM 102 CE MET A 48 -35.820 2.483 2.414 1.00128.91 C ANISOU 102 CE MET A 48 17074 14870 17036 -201 144 -488 C ATOM 103 N ALA A 49 -34.492 -1.084 8.653 1.00 90.51 N ANISOU 103 N ALA A 49 11859 10194 12337 -247 479 -403 N ATOM 104 CA ALA A 49 -34.578 -1.351 10.090 1.00 87.26 C ANISOU 104 CA ALA A 49 11371 9819 11963 -248 527 -387 C ATOM 105 C ALA A 49 -33.191 -1.561 10.718 1.00 92.85 C ANISOU 105 C ALA A 49 12052 10563 12663 -250 599 -360 C ATOM 106 O ALA A 49 -32.943 -1.166 11.869 1.00 98.50 O ANISOU 106 O ALA A 49 12729 11313 13382 -251 627 -340 O ATOM 107 CB ALA A 49 -35.476 -2.535 10.358 1.00 96.36 C ANISOU 107 CB ALA A 49 12476 10956 13180 -244 530 -406 C ATOM 108 N LEU A 50 -32.286 -2.180 9.962 1.00108.41 N ANISOU 108 N LEU A 50 14045 12522 14623 -249 627 -361 N ATOM 109 CA LEU A 50 -30.918 -2.396 10.444 1.00125.54 C ANISOU 109 CA LEU A 50 16192 14721 16785 -249 697 -335 C ATOM 110 C LEU A 50 -30.146 -1.091 10.634 1.00129.53 C ANISOU 110 C LEU A 50 16725 15249 17243 -257 693 -310 C ATOM 111 O LEU A 50 -29.466 -0.897 11.652 1.00144.29 O ANISOU 111 O LEU A 50 18560 17149 19114 -258 730 -288 O ATOM 112 CB LEU A 50 -30.138 -3.326 9.512 1.00117.11 C ANISOU 112 CB LEU A 50 15152 13630 15716 -243 729 -342 C ATOM 113 CG LEU A 50 -28.648 -3.455 9.853 1.00 94.25 C ANISOU 113 CG LEU A 50 12241 10761 12808 -240 801 -312 C ATOM 114 CD1 LEU A 50 -28.138 -4.870 9.589 1.00 88.89 C ANISOU 114 CD1 LEU A 50 11551 10064 12159 -229 854 -317 C ATOM 115 CD2 LEU A 50 -27.818 -2.412 9.108 1.00 65.37 C ANISOU 115 CD2 LEU A 50 8640 7102 9096 -246 792 -295 C ATOM 116 N VAL A 51 -30.235 -0.204 9.648 1.00105.19 N ANISOU 116 N VAL A 51 13706 12143 14120 -263 644 -314 N ATOM 117 CA VAL A 51 -29.605 1.107 9.783 1.00 76.55 C ANISOU 117 CA VAL A 51 10107 8526 10452 -275 628 -290 C ATOM 118 C VAL A 51 -30.214 1.878 10.967 1.00 71.53 C ANISOU 118 C VAL A 51 9450 7908 9821 -279 601 -284 C ATOM 119 O VAL A 51 -29.499 2.550 11.737 1.00 92.14 O ANISOU 119 O VAL A 51 12058 10536 12416 -288 609 -261 O ATOM 120 CB VAL A 51 -29.718 1.920 8.488 1.00 50.25 C ANISOU 120 CB VAL A 51 6847 5163 7084 -278 577 -295 C ATOM 121 CG1 VAL A 51 -28.754 3.082 8.527 1.00 46.41 C ANISOU 121 CG1 VAL A 51 6389 4682 6562 -294 573 -265 C ATOM 122 CG2 VAL A 51 -29.415 1.031 7.294 1.00 50.59 C ANISOU 122 CG2 VAL A 51 6917 5179 7124 -268 596 -310 C ATOM 123 N VAL A 52 -31.532 1.757 11.127 1.00 50.53 N ANISOU 123 N VAL A 52 6777 5238 7183 -272 567 -304 N ATOM 124 CA VAL A 52 -32.185 2.276 12.326 1.00 57.44 C ANISOU 124 CA VAL A 52 7626 6128 8069 -271 553 -299 C ATOM 125 C VAL A 52 -31.429 1.801 13.564 1.00 48.57 C ANISOU 125 C VAL A 52 6450 5040 6966 -268 613 -282 C ATOM 126 O VAL A 52 -31.045 2.614 14.401 1.00 16.30 O ANISOU 126 O VAL A 52 2370 964 2859 -274 604 -266 O ATOM 127 CB VAL A 52 -33.662 1.835 12.439 1.00 53.94 C ANISOU 127 CB VAL A 52 7158 5673 7665 -260 530 -321 C ATOM 128 CG1 VAL A 52 -34.167 2.033 13.866 1.00 15.99 C ANISOU 128 CG1 VAL A 52 2308 888 2881 -255 542 -313 C ATOM 129 CG2 VAL A 52 -34.538 2.586 11.437 1.00 43.00 C ANISOU 129 CG2 VAL A 52 5830 4252 6257 -260 457 -337 C ATOM 130 N LEU A 53 -31.191 0.492 13.665 1.00 63.08 N ANISOU 130 N LEU A 53 8238 6888 8841 -260 667 -287 N ATOM 131 CA LEU A 53 -30.420 -0.040 14.797 1.00 60.63 C ANISOU 131 CA LEU A 53 7876 6608 8552 -253 726 -271 C ATOM 132 C LEU A 53 -29.024 0.569 14.924 1.00 67.21 C ANISOU 132 C LEU A 53 8735 7452 9350 -262 738 -248 C ATOM 133 O LEU A 53 -28.518 0.782 16.031 1.00 33.88 O ANISOU 133 O LEU A 53 4494 3250 5130 -261 753 -233 O ATOM 134 CB LEU A 53 -30.292 -1.562 14.740 1.00 23.70 C ANISOU 134 CB LEU A 53 3148 1933 3923 -242 782 -278 C ATOM 135 CG LEU A 53 -29.611 -2.083 16.007 1.00 58.72 C ANISOU 135 CG LEU A 53 7527 6399 8385 -231 839 -261 C ATOM 136 CD1 LEU A 53 -30.297 -3.336 16.515 1.00 90.54 C ANISOU 136 CD1 LEU A 53 11491 10429 12480 -218 874 -270 C ATOM 137 CD2 LEU A 53 -28.105 -2.287 15.826 1.00 39.35 C ANISOU 137 CD2 LEU A 53 5081 3954 5915 -229 882 -243 C ATOM 138 N LEU A 54 -28.383 0.821 13.792 1.00 92.73 N ANISOU 138 N LEU A 54 12012 10668 12552 -270 730 -244 N ATOM 139 CA LEU A 54 -27.102 1.506 13.829 1.00 93.65 C ANISOU 139 CA LEU A 54 12156 10788 12640 -282 733 -219 C ATOM 140 C LEU A 54 -27.250 2.803 14.607 1.00 79.85 C ANISOU 140 C LEU A 54 10434 9037 10867 -298 677 -208 C ATOM 141 O LEU A 54 -26.413 3.125 15.457 1.00 36.24 O ANISOU 141 O LEU A 54 4905 3523 5340 -306 680 -188 O ATOM 142 CB LEU A 54 -26.608 1.814 12.421 1.00 92.92 C ANISOU 142 CB LEU A 54 12116 10673 12518 -291 722 -215 C ATOM 143 CG LEU A 54 -25.368 1.036 12.000 1.00 64.14 C ANISOU 143 CG LEU A 54 8460 7031 8880 -283 785 -201 C ATOM 144 CD1 LEU A 54 -25.698 -0.447 11.942 1.00 15.85 C ANISOU 144 CD1 LEU A 54 2302 918 2802 -263 837 -219 C ATOM 145 CD2 LEU A 54 -24.865 1.552 10.665 1.00 68.26 C ANISOU 145 CD2 LEU A 54 9040 7526 9368 -292 772 -192 C ATOM 146 N ILE A 55 -28.331 3.531 14.323 1.00 85.52 N ANISOU 146 N ILE A 55 11185 9738 11572 -301 622 -221 N ATOM 147 CA ILE A 55 -28.550 4.833 14.954 1.00 91.08 C ANISOU 147 CA ILE A 55 11925 10429 12251 -316 563 -212 C ATOM 148 C ILE A 55 -28.966 4.730 16.419 1.00100.51 C ANISOU 148 C ILE A 55 13086 11640 13463 -307 571 -213 C ATOM 149 O ILE A 55 -28.227 5.144 17.315 1.00113.51 O ANISOU 149 O ILE A 55 14738 13291 15100 -319 564 -196 O ATOM 150 CB ILE A 55 -29.634 5.645 14.237 1.00 82.85 C ANISOU 150 CB ILE A 55 10929 9359 11193 -317 502 -226 C ATOM 151 CG1 ILE A 55 -29.457 5.575 12.723 1.00 59.83 C ANISOU 151 CG1 ILE A 55 8044 6425 8265 -319 496 -230 C ATOM 152 CG2 ILE A 55 -29.612 7.088 14.721 1.00101.29 C ANISOU 152 CG2 ILE A 55 13312 11671 13502 -334 438 -213 C ATOM 153 CD1 ILE A 55 -30.507 6.360 11.967 1.00 24.99 C ANISOU 153 CD1 ILE A 55 3675 1981 3839 -317 433 -244 C ATOM 154 N VAL A 56 -30.159 4.194 16.653 1.00 87.91 N ANISOU 154 N VAL A 56 11456 10050 11894 -289 581 -232 N ATOM 155 CA VAL A 56 -30.698 4.055 18.003 1.00 91.08 C ANISOU 155 CA VAL A 56 11825 10466 12317 -278 594 -233 C ATOM 156 C VAL A 56 -29.735 3.352 18.954 1.00 94.87 C ANISOU 156 C VAL A 56 12260 10971 12814 -274 647 -219 C ATOM 157 O VAL A 56 -29.685 3.672 20.140 1.00 93.77 O ANISOU 157 O VAL A 56 12119 10837 12672 -274 642 -211 O ATOM 158 CB VAL A 56 -32.016 3.273 18.001 1.00 85.75 C ANISOU 158 CB VAL A 56 11103 9794 11683 -260 612 -252 C ATOM 159 CG1 VAL A 56 -32.498 3.061 19.422 1.00 93.22 C ANISOU 159 CG1 VAL A 56 12008 10756 12656 -248 635 -249 C ATOM 160 CG2 VAL A 56 -33.052 4.010 17.188 1.00 68.61 C ANISOU 160 CG2 VAL A 56 8977 7595 9498 -262 553 -265 C ATOM 161 N ALA A 57 -28.975 2.390 18.442 1.00 81.92 N ANISOU 161 N ALA A 57 10589 9345 11193 -269 696 -217 N ATOM 162 CA ALA A 57 -27.966 1.749 19.267 1.00 56.05 C ANISOU 162 CA ALA A 57 7275 6089 7934 -261 744 -202 C ATOM 163 C ALA A 57 -26.781 2.692 19.429 1.00 34.83 C ANISOU 163 C ALA A 57 4634 3390 5209 -284 709 -180 C ATOM 164 O ALA A 57 -26.556 3.228 20.513 1.00 37.63 O ANISOU 164 O ALA A 57 5000 3743 5553 -293 684 -168 O ATOM 165 CB ALA A 57 -27.524 0.433 18.657 1.00 54.41 C ANISOU 165 CB ALA A 57 7022 5891 7759 -246 807 -206 C ATOM 166 N GLY A 58 -26.055 2.927 18.337 1.00 71.80 N ANISOU 166 N GLY A 58 9347 8060 9872 -298 700 -172 N ATOM 167 CA GLY A 58 -24.798 3.658 18.390 1.00 82.48 C ANISOU 167 CA GLY A 58 10735 9401 11203 -324 670 -144 C ATOM 168 C GLY A 58 -24.856 4.975 19.142 1.00 78.22 C ANISOU 168 C GLY A 58 10245 8840 10636 -353 594 -132 C ATOM 169 O GLY A 58 -24.058 5.223 20.056 1.00 64.35 O ANISOU 169 O GLY A 58 8492 7081 8878 -370 575 -110 O ATOM 170 N ASN A 59 -25.806 5.822 18.764 1.00 74.63 N ANISOU 170 N ASN A 59 9832 8365 10160 -359 544 -145 N ATOM 171 CA ASN A 59 -25.935 7.132 19.383 1.00 75.38 C ANISOU 171 CA ASN A 59 9981 8429 10230 -384 467 -135 C ATOM 172 C ASN A 59 -26.191 7.044 20.874 1.00 83.50 C ANISOU 172 C ASN A 59 10996 9465 11266 -377 467 -137 C ATOM 173 O ASN A 59 -25.684 7.854 21.646 1.00106.54 O ANISOU 173 O ASN A 59 13951 12360 14170 -404 412 -119 O ATOM 174 CB ASN A 59 -27.043 7.944 18.715 1.00 75.08 C ANISOU 174 CB ASN A 59 9984 8367 10177 -381 421 -152 C ATOM 175 CG ASN A 59 -26.587 8.587 17.424 1.00 73.67 C ANISOU 175 CG ASN A 59 9843 8164 9984 -402 389 -140 C ATOM 176 OD1 ASN A 59 -25.824 9.555 17.437 1.00 72.62 O ANISOU 176 OD1 ASN A 59 9748 8001 9843 -436 334 -114 O ATOM 177 ND2 ASN A 59 -27.054 8.056 16.301 1.00 64.94 N ANISOU 177 ND2 ASN A 59 8728 7066 8882 -384 419 -156 N ATOM 178 N VAL A 60 -26.982 6.058 21.277 1.00 60.24 N ANISOU 178 N VAL A 60 7996 6547 8344 -343 526 -156 N ATOM 179 CA VAL A 60 -27.348 5.927 22.680 1.00 42.61 C ANISOU 179 CA VAL A 60 5749 4322 6120 -332 534 -158 C ATOM 180 C VAL A 60 -26.267 5.242 23.511 1.00 48.71 C ANISOU 180 C VAL A 60 6487 5113 6909 -333 568 -140 C ATOM 181 O VAL A 60 -26.244 5.392 24.727 1.00 42.43 O ANISOU 181 O VAL A 60 5698 4313 6111 -335 556 -134 O ATOM 182 CB VAL A 60 -28.687 5.201 22.863 1.00 37.79 C ANISOU 182 CB VAL A 60 5091 3730 5538 -298 579 -180 C ATOM 183 CG1 VAL A 60 -28.491 3.698 22.795 1.00 24.80 C ANISOU 183 CG1 VAL A 60 3366 2120 3938 -275 661 -182 C ATOM 184 CG2 VAL A 60 -29.311 5.592 24.187 1.00 47.03 C ANISOU 184 CG2 VAL A 60 6275 4892 6704 -292 562 -181 C ATOM 185 N LEU A 61 -25.383 4.483 22.868 1.00 69.43 N ANISOU 185 N LEU A 61 9077 7753 9550 -330 611 -131 N ATOM 186 CA LEU A 61 -24.234 3.918 23.577 1.00 68.94 C ANISOU 186 CA LEU A 61 8987 7702 9505 -332 635 -109 C ATOM 187 C LEU A 61 -23.189 5.014 23.749 1.00 77.36 C ANISOU 187 C LEU A 61 10112 8739 10544 -382 557 -77 C ATOM 188 O LEU A 61 -22.481 5.072 24.764 1.00 95.11 O ANISOU 188 O LEU A 61 12363 10983 12793 -400 536 -55 O ATOM 189 CB LEU A 61 -23.672 2.692 22.850 1.00 63.74 C ANISOU 189 CB LEU A 61 8271 7065 8881 -306 709 -109 C ATOM 190 CG LEU A 61 -24.508 1.417 23.056 1.00 73.90 C ANISOU 190 CG LEU A 61 9489 8379 10211 -263 784 -131 C ATOM 191 CD1 LEU A 61 -24.449 0.466 21.857 1.00 68.97 C ANISOU 191 CD1 LEU A 61 8831 7762 9611 -243 839 -142 C ATOM 192 CD2 LEU A 61 -24.113 0.702 24.344 1.00 64.09 C ANISOU 192 CD2 LEU A 61 8202 7150 8998 -243 821 -119 C ATOM 193 N VAL A 62 -23.121 5.901 22.761 1.00 68.56 N ANISOU 193 N VAL A 62 9044 7600 9406 -408 508 -72 N ATOM 194 CA VAL A 62 -22.370 7.142 22.907 1.00 62.96 C ANISOU 194 CA VAL A 62 8394 6853 8676 -464 417 -40 C ATOM 195 C VAL A 62 -22.876 7.938 24.101 1.00 77.22 C ANISOU 195 C VAL A 62 10240 8633 10468 -476 356 -44 C ATOM 196 O VAL A 62 -22.115 8.274 25.006 1.00 89.50 O ANISOU 196 O VAL A 62 11811 10171 12024 -511 309 -16 O ATOM 197 CB VAL A 62 -22.503 8.030 21.667 1.00 51.75 C ANISOU 197 CB VAL A 62 7015 5406 7240 -484 374 -37 C ATOM 198 CG1 VAL A 62 -22.412 9.501 22.055 1.00 16.68 C ANISOU 198 CG1 VAL A 62 2633 914 2789 -529 269 -18 C ATOM 199 CG2 VAL A 62 -21.447 7.666 20.642 1.00 73.06 C ANISOU 199 CG2 VAL A 62 9697 8113 9950 -498 400 -11 C ATOM 200 N ILE A 63 -24.170 8.238 24.087 1.00 87.74 N ANISOU 200 N ILE A 63 11589 9960 11790 -450 354 -76 N ATOM 201 CA ILE A 63 -24.819 8.986 25.159 1.00 88.21 C ANISOU 201 CA ILE A 63 11688 9991 11837 -451 304 -86 C ATOM 202 C ILE A 63 -24.600 8.326 26.521 1.00 91.18 C ANISOU 202 C ILE A 63 12039 10384 12222 -441 332 -81 C ATOM 203 O ILE A 63 -24.347 8.999 27.527 1.00109.95 O ANISOU 203 O ILE A 63 14455 12728 14592 -464 271 -70 O ATOM 204 CB ILE A 63 -26.329 9.124 24.879 1.00 81.60 C ANISOU 204 CB ILE A 63 10857 9154 10994 -414 318 -120 C ATOM 205 CG1 ILE A 63 -26.547 10.033 23.665 1.00 69.39 C ANISOU 205 CG1 ILE A 63 9348 7578 9438 -427 270 -122 C ATOM 206 CG2 ILE A 63 -27.058 9.656 26.104 1.00 82.73 C ANISOU 206 CG2 ILE A 63 11032 9273 11129 -403 286 -132 C ATOM 207 CD1 ILE A 63 -27.960 10.067 23.156 1.00 59.88 C ANISOU 207 CD1 ILE A 63 8145 6377 8231 -393 284 -151 C ATOM 208 N ALA A 64 -24.691 7.002 26.536 1.00 75.89 N ANISOU 208 N ALA A 64 10034 8494 10307 -405 424 -89 N ATOM 209 CA ALA A 64 -24.466 6.218 27.740 1.00 68.14 C ANISOU 209 CA ALA A 64 9016 7532 9342 -390 464 -82 C ATOM 210 C ALA A 64 -23.068 6.461 28.295 1.00 68.27 C ANISOU 210 C ALA A 64 9053 7532 9356 -435 416 -45 C ATOM 211 O ALA A 64 -22.914 6.882 29.443 1.00 47.40 O ANISOU 211 O ALA A 64 6442 4865 6701 -453 370 -34 O ATOM 212 CB ALA A 64 -24.670 4.740 27.448 1.00 41.29 C ANISOU 212 CB ALA A 64 5528 4177 5982 -345 568 -93 C ATOM 213 N ALA A 65 -22.048 6.205 27.482 1.00 65.68 N ANISOU 213 N ALA A 65 8704 7212 9038 -454 423 -21 N ATOM 214 CA ALA A 65 -20.678 6.385 27.949 1.00 51.83 C ANISOU 214 CA ALA A 65 6961 5446 7287 -505 375 25 C ATOM 215 C ALA A 65 -20.346 7.848 28.258 1.00 64.85 C ANISOU 215 C ALA A 65 8682 7041 8917 -569 253 51 C ATOM 216 O ALA A 65 -19.407 8.130 28.997 1.00 52.69 O ANISOU 216 O ALA A 65 7153 5482 7383 -619 194 93 O ATOM 217 CB ALA A 65 -19.694 5.813 26.952 1.00 21.33 C ANISOU 217 CB ALA A 65 3060 1603 3443 -511 411 50 C ATOM 218 N ILE A 66 -21.117 8.777 27.700 1.00 87.67 N ANISOU 218 N ILE A 66 11611 9901 11797 -567 212 28 N ATOM 219 CA ILE A 66 -20.909 10.191 28.001 1.00100.64 C ANISOU 219 CA ILE A 66 13299 11482 13458 -612 102 45 C ATOM 220 C ILE A 66 -21.455 10.540 29.378 1.00109.95 C ANISOU 220 C ILE A 66 14500 12634 14641 -598 74 24 C ATOM 221 O ILE A 66 -20.697 10.829 30.304 1.00106.50 O ANISOU 221 O ILE A 66 14057 12170 14239 -630 26 51 O ATOM 222 CB ILE A 66 -21.588 11.117 26.975 1.00107.85 C ANISOU 222 CB ILE A 66 14236 12367 14376 -604 76 23 C ATOM 223 CG1 ILE A 66 -20.915 11.010 25.605 1.00103.82 C ANISOU 223 CG1 ILE A 66 13708 11869 13868 -626 88 50 C ATOM 224 CG2 ILE A 66 -21.540 12.560 27.455 1.00118.54 C ANISOU 224 CG2 ILE A 66 15603 13652 15786 -626 6 18 C ATOM 225 CD1 ILE A 66 -21.567 11.876 24.541 1.00103.99 C ANISOU 225 CD1 ILE A 66 13752 11864 13896 -618 68 30 C ATOM 226 N GLY A 67 -22.777 10.506 29.507 1.00116.86 N ANISOU 226 N GLY A 67 14228 15848 14324 71 28 699 N ATOM 227 CA GLY A 67 -23.427 10.929 30.733 1.00135.98 C ANISOU 227 CA GLY A 67 16622 18332 16711 42 16 715 C ATOM 228 C GLY A 67 -22.940 10.186 31.962 1.00135.33 C ANISOU 228 C GLY A 67 16456 18408 16555 46 17 812 C ATOM 229 O GLY A 67 -22.984 10.715 33.073 1.00143.35 O ANISOU 229 O GLY A 67 17212 19557 17697 0 0 754 O ATOM 230 N SER A 68 -22.483 8.954 31.765 1.00114.49 N ANISOU 230 N SER A 68 13791 15785 13925 97 39 883 N ATOM 231 CA SER A 68 -22.090 8.104 32.884 1.00101.86 C ANISOU 231 CA SER A 68 12112 14328 12264 111 44 987 C ATOM 232 C SER A 68 -20.581 8.048 33.194 1.00 86.40 C ANISOU 232 C SER A 68 9826 12566 10436 102 39 939 C ATOM 233 O SER A 68 -20.167 7.316 34.093 1.00 59.70 O ANISOU 233 O SER A 68 6632 9280 6772 108 41 1117 O ATOM 234 CB SER A 68 -22.687 6.700 32.724 1.00 94.58 C ANISOU 234 CB SER A 68 11194 13335 11407 177 78 1057 C ATOM 235 OG SER A 68 -24.108 6.747 32.758 1.00 58.06 O ANISOU 235 OG SER A 68 6614 8596 6850 184 85 1033 O ATOM 236 N THR A 69 -19.763 8.804 32.463 1.00102.06 N ANISOU 236 N THR A 69 11833 14549 12397 69 25 878 N ATOM 237 CA THR A 69 -18.328 8.878 32.776 1.00105.16 C ANISOU 237 CA THR A 69 12410 15079 12466 39 13 985 C ATOM 238 C THR A 69 -17.838 10.310 32.982 1.00102.48 C ANISOU 238 C THR A 69 11790 14839 12310 -51 -15 828 C ATOM 239 O THR A 69 -18.285 11.235 32.305 1.00 95.27 O ANISOU 239 O THR A 69 11215 13792 11190 -76 -22 813 O ATOM 240 CB THR A 69 -17.447 8.210 31.703 1.00 83.25 C ANISOU 240 CB THR A 69 9373 12302 9955 93 32 914 C ATOM 241 OG1 THR A 69 -17.822 6.836 31.558 1.00106.36 O ANISOU 241 OG1 THR A 69 12301 15177 12933 172 65 983 O ATOM 242 CG2 THR A 69 -15.981 8.283 32.107 1.00 19.30 C ANISOU 242 CG2 THR A 69 1468 4360 1506 62 20 1029 C ATOM 243 N GLN A 70 -16.909 10.483 33.917 1.00 91.19 N ANISOU 243 N GLN A 70 10555 13579 10515 -91 -26 934 N ATOM 244 CA GLN A 70 -16.392 11.805 34.242 1.00 75.44 C ANISOU 244 CA GLN A 70 8545 11678 8440 -186 -46 855 C ATOM 245 C GLN A 70 -15.468 12.334 33.161 1.00 68.14 C ANISOU 245 C GLN A 70 7345 10745 7800 -221 -51 726 C ATOM 246 O GLN A 70 -15.605 13.480 32.740 1.00 70.10 O ANISOU 246 O GLN A 70 7938 10924 7774 -261 -55 697 O ATOM 247 CB GLN A 70 -15.663 11.795 35.588 1.00 90.03 C ANISOU 247 CB GLN A 70 9962 13768 10478 -255 -61 829 C ATOM 248 CG GLN A 70 -16.462 12.395 36.743 1.00 99.93 C ANISOU 248 CG GLN A 70 11197 15073 11699 -323 -74 812 C ATOM 249 CD GLN A 70 -17.419 11.407 37.386 1.00 98.48 C ANISOU 249 CD GLN A 70 11342 14847 11229 -237 -60 977 C ATOM 250 OE1 GLN A 70 -17.351 10.203 37.138 1.00108.49 O ANISOU 250 OE1 GLN A 70 12597 16085 12539 -155 -43 1063 O ATOM 251 NE2 GLN A 70 -18.314 11.914 38.222 1.00 79.63 N ANISOU 251 NE2 GLN A 70 8958 12469 8827 -282 -69 956 N ATOM 252 N ARG A 71 -14.533 11.495 32.715 1.00105.22 N ANISOU 252 N ARG A 71 12308 15470 12200 -152 -37 847 N ATOM 253 CA ARG A 71 -13.511 11.894 31.734 1.00136.71 C ANISOU 253 CA ARG A 71 16002 19475 16466 -180 -41 732 C ATOM 254 C ARG A 71 -14.102 12.342 30.391 1.00129.06 C ANISOU 254 C ARG A 71 15432 18290 15314 -151 -35 723 C ATOM 255 O ARG A 71 -13.459 13.059 29.616 1.00 83.01 O ANISOU 255 O ARG A 71 9348 12456 9735 -201 -43 604 O ATOM 256 CB ARG A 71 -12.498 10.760 31.503 1.00130.96 C ANISOU 256 CB ARG A 71 15528 18809 15422 -101 -25 882 C ATOM 257 CG ARG A 71 -11.691 10.358 32.737 1.00118.61 C ANISOU 257 CG ARG A 71 13861 17463 13741 -114 -28 960 C ATOM 258 CD ARG A 71 -12.448 9.357 33.599 1.00127.40 C ANISOU 258 CD ARG A 71 14595 18608 15205 -70 -19 966 C ATOM 259 NE ARG A 71 -12.444 9.729 35.011 1.00123.89 N ANISOU 259 NE ARG A 71 14439 18302 14331 -124 -31 1075 N ATOM 260 CZ ARG A 71 -12.975 8.994 35.982 1.00 93.92 C ANISOU 260 CZ ARG A 71 10605 14557 10525 -97 -26 1160 C ATOM 261 NH1 ARG A 71 -13.553 7.834 35.702 1.00 95.92 N ANISOU 261 NH1 ARG A 71 10499 14736 11211 -13 -4 1129 N ATOM 262 NH2 ARG A 71 -12.921 9.420 37.237 1.00 42.07 N ANISOU 262 NH2 ARG A 71 3569 8169 4245 -175 -45 1074 N ATOM 263 N LEU A 72 -15.322 11.894 30.119 1.00136.78 N ANISOU 263 N LEU A 72 16467 19114 16388 -102 -26 731 N ATOM 264 CA LEU A 72 -16.023 12.243 28.892 1.00122.33 C ANISOU 264 CA LEU A 72 14726 17092 14662 -85 -22 664 C ATOM 265 C LEU A 72 -17.004 13.404 29.093 1.00113.77 C ANISOU 265 C LEU A 72 13689 15936 13601 -139 -33 587 C ATOM 266 O LEU A 72 -17.705 13.810 28.165 1.00 97.24 O ANISOU 266 O LEU A 72 11474 13696 11777 -140 -33 485 O ATOM 267 CB LEU A 72 -16.728 11.005 28.343 1.00102.88 C ANISOU 267 CB LEU A 72 12298 14502 12288 0 0 712 C ATOM 268 CG LEU A 72 -15.746 9.881 28.002 1.00 88.43 C ANISOU 268 CG LEU A 72 10200 12750 10650 57 18 715 C ATOM 269 CD1 LEU A 72 -16.334 8.515 28.314 1.00 79.00 C ANISOU 269 CD1 LEU A 72 9228 11506 9283 118 40 863 C ATOM 270 CD2 LEU A 72 -15.296 9.979 26.547 1.00 95.50 C ANISOU 270 CD2 LEU A 72 11158 13548 11579 73 22 669 C ATOM 271 N GLN A 73 -17.040 13.938 30.311 1.00112.73 N ANISOU 271 N GLN A 73 13514 15927 13393 -199 -44 587 N ATOM 272 CA GLN A 73 -17.981 15.003 30.665 1.00 95.74 C ANISOU 272 CA GLN A 73 11178 13728 11469 -277 -56 474 C ATOM 273 C GLN A 73 -17.451 16.417 30.434 1.00 75.88 C ANISOU 273 C GLN A 73 8902 11235 8693 -344 -61 421 C ATOM 274 O GLN A 73 -18.063 17.399 30.865 1.00 57.73 O ANISOU 274 O GLN A 73 6410 8919 6605 -444 -56 328 O ATOM 275 CB GLN A 73 -18.523 14.830 32.087 1.00 74.51 C ANISOU 275 CB GLN A 73 8430 11137 8743 -299 -61 514 C ATOM 276 CG GLN A 73 -19.726 13.905 32.140 1.00 50.84 C ANISOU 276 CG GLN A 73 5469 8034 5815 -216 -52 564 C ATOM 277 CD GLN A 73 -20.433 13.947 33.470 1.00 62.65 C ANISOU 277 CD GLN A 73 6921 9605 7280 -245 -59 591 C ATOM 278 OE1 GLN A 73 -19.877 13.551 34.490 1.00 67.09 O ANISOU 278 OE1 GLN A 73 7385 10328 7779 -264 -63 647 O ATOM 279 NE2 GLN A 73 -21.669 14.432 33.469 1.00 78.48 N ANISOU 279 NE2 GLN A 73 8995 11497 9326 -250 -60 552 N ATOM 280 N THR A 74 -16.292 16.504 29.788 1.00 68.88 N ANISOU 280 N THR A 74 7771 10396 8006 -387 -54 375 N ATOM 281 CA THR A 74 -15.752 17.783 29.342 1.00 85.03 C ANISOU 281 CA THR A 74 9840 12443 10025 -474 -51 291 C ATOM 282 C THR A 74 -16.820 18.503 28.509 1.00 77.85 C ANISOU 282 C THR A 74 9048 11342 9188 -470 -45 228 C ATOM 283 O THR A 74 -17.571 17.860 27.773 1.00 79.30 O ANISOU 283 O THR A 74 9478 11390 9262 -351 -49 274 O ATOM 284 CB THR A 74 -14.444 17.583 28.524 1.00 56.48 C ANISOU 284 CB THR A 74 6426 8878 6154 -423 -54 324 C ATOM 285 OG1 THR A 74 -14.727 17.574 27.118 1.00 57.39 O ANISOU 285 OG1 THR A 74 6401 8824 6582 -411 -45 273 O ATOM 286 CG2 THR A 74 -13.763 16.267 28.912 1.00 26.67 C ANISOU 286 CG2 THR A 74 2581 5212 2340 -362 -57 424 C ATOM 287 N LEU A 75 -16.905 19.828 28.642 1.00 58.89 N ANISOU 287 N LEU A 75 6875 8947 6553 -517 -38 163 N ATOM 288 CA LEU A 75 -17.963 20.595 27.979 1.00 25.21 C ANISOU 288 CA LEU A 75 2694 4512 2371 -517 -27 100 C ATOM 289 C LEU A 75 -18.091 20.199 26.522 1.00 50.58 C ANISOU 289 C LEU A 75 5799 7568 5851 -481 -25 99 C ATOM 290 O LEU A 75 -19.185 19.921 26.046 1.00 20.71 O ANISOU 290 O LEU A 75 2226 3654 1990 -381 -28 113 O ATOM 291 CB LEU A 75 -17.692 22.103 28.028 1.00 13.14 C ANISOU 291 CB LEU A 75 1009 2985 999 -678 -1 4 C ATOM 292 CG LEU A 75 -17.496 22.870 29.330 1.00 16.09 C ANISOU 292 CG LEU A 75 1530 3512 1070 -726 12 -36 C ATOM 293 CD1 LEU A 75 -16.187 22.461 29.999 1.00 16.33 C ANISOU 293 CD1 LEU A 75 1244 3720 1241 -828 0 0 C ATOM 294 CD2 LEU A 75 -17.523 24.365 29.052 1.00 14.91 C ANISOU 294 CD2 LEU A 75 1236 3289 1140 -886 47 -126 C ATOM 295 N THR A 76 -16.961 20.166 25.821 1.00 87.24 N ANISOU 295 N THR A 76 10583 12261 10305 -445 -27 107 N ATOM 296 CA THR A 76 -16.952 19.966 24.377 1.00 66.38 C ANISOU 296 CA THR A 76 7988 9488 7745 -389 -25 101 C ATOM 297 C THR A 76 -17.662 18.662 24.020 1.00 55.61 C ANISOU 297 C THR A 76 6506 8027 6597 -315 -30 151 C ATOM 298 O THR A 76 -18.035 18.445 22.871 1.00 56.06 O ANISOU 298 O THR A 76 6632 7950 6718 -259 -27 142 O ATOM 299 CB THR A 76 -15.521 20.010 23.804 1.00 26.62 C ANISOU 299 CB THR A 76 2919 4535 2661 -410 -24 99 C ATOM 300 OG1 THR A 76 -14.901 21.258 24.162 1.00 22.00 O ANISOU 300 OG1 THR A 76 2153 4024 2181 -558 -8 31 O ATOM 301 CG2 THR A 76 -15.557 19.880 22.298 1.00 9.59 C ANISOU 301 CG2 THR A 76 814 2242 588 -359 -21 89 C ATOM 302 N ASN A 77 -17.857 17.803 25.016 1.00 71.57 N ANISOU 302 N ASN A 77 8471 10123 8598 -288 -35 207 N ATOM 303 CA ASN A 77 -18.651 16.591 24.839 1.00 77.93 C ANISOU 303 CA ASN A 77 9303 10846 9462 -195 -32 258 C ATOM 304 C ASN A 77 -20.113 16.737 25.287 1.00 63.99 C ANISOU 304 C ASN A 77 7586 8992 7735 -182 -31 248 C ATOM 305 O ASN A 77 -20.903 15.802 25.167 1.00 78.60 O ANISOU 305 O ASN A 77 9578 10763 9525 -103 -24 307 O ATOM 306 CB ASN A 77 -17.976 15.399 25.532 1.00 86.54 C ANISOU 306 CB ASN A 77 10304 12063 10514 -161 -33 337 C ATOM 307 CG ASN A 77 -16.764 14.878 24.762 1.00 89.34 C ANISOU 307 CG ASN A 77 10630 12459 10857 -137 -29 357 C ATOM 308 OD1 ASN A 77 -16.775 13.757 24.250 1.00 89.47 O ANISOU 308 OD1 ASN A 77 10812 12420 10761 -61 -15 435 O ATOM 309 ND2 ASN A 77 -15.719 15.695 24.672 1.00 84.43 N ANISOU 309 ND2 ASN A 77 9973 11926 10182 -202 -33 324 N ATOM 310 N LEU A 78 -20.467 17.907 25.810 1.00 45.99 N ANISOU 310 N LEU A 78 5441 6727 5306 -230 -37 216 N ATOM 311 CA LEU A 78 -21.857 18.211 26.133 1.00 46.07 C ANISOU 311 CA LEU A 78 5492 6648 5365 -221 -36 195 C ATOM 312 C LEU A 78 -22.620 18.656 24.882 1.00 37.72 C ANISOU 312 C LEU A 78 4512 5416 4403 -189 -29 143 C ATOM 313 O LEU A 78 -23.828 18.436 24.757 1.00 10.82 O ANISOU 313 O LEU A 78 1070 1902 1138 -158 -24 130 O ATOM 314 CB LEU A 78 -21.926 19.301 27.198 1.00 65.45 C ANISOU 314 CB LEU A 78 7931 9191 7745 -311 -35 150 C ATOM 315 CG LEU A 78 -23.278 19.440 27.894 1.00 69.09 C ANISOU 315 CG LEU A 78 8414 9605 8232 -305 -35 145 C ATOM 316 CD1 LEU A 78 -23.573 18.160 28.664 1.00 49.02 C ANISOU 316 CD1 LEU A 78 5825 7115 5686 -251 -44 234 C ATOM 317 CD2 LEU A 78 -23.287 20.660 28.807 1.00 9.06 C ANISOU 317 CD2 LEU A 78 808 2078 555 -408 -24 82 C ATOM 318 N PHE A 79 -21.905 19.304 23.966 1.00 32.52 N ANISOU 318 N PHE A 79 3875 4735 3748 -212 -24 102 N ATOM 319 CA PHE A 79 -22.458 19.617 22.662 1.00 38.39 C ANISOU 319 CA PHE A 79 4622 5320 4646 -189 -15 61 C ATOM 320 C PHE A 79 -22.586 18.305 21.905 1.00 53.52 C ANISOU 320 C PHE A 79 6612 7168 6557 -97 -18 104 C ATOM 321 O PHE A 79 -23.410 18.168 20.996 1.00 84.26 O ANISOU 321 O PHE A 79 10559 10925 10531 -54 -12 80 O ATOM 322 CB PHE A 79 -21.539 20.549 21.887 1.00 4.62 C ANISOU 322 CB PHE A 79 354 1050 352 -237 -7 23 C ATOM 323 CG PHE A 79 -21.282 21.871 22.561 1.00 5.67 C ANISOU 323 CG PHE A 79 546 1262 345 -310 10 -27 C ATOM 324 CD1 PHE A 79 -21.915 23.023 22.121 1.00 22.77 C ANISOU 324 CD1 PHE A 79 2700 3329 2624 -359 32 -72 C ATOM 325 CD2 PHE A 79 -20.372 21.974 23.598 1.00 27.26 C ANISOU 325 CD2 PHE A 79 3125 4143 3088 -414 8 -23 C ATOM 326 CE1 PHE A 79 -21.662 24.251 22.720 1.00 9.64 C ANISOU 326 CE1 PHE A 79 1028 1721 913 -461 61 -122 C ATOM 327 CE2 PHE A 79 -20.116 23.196 24.199 1.00 42.96 C ANISOU 327 CE2 PHE A 79 5213 6209 4902 -475 34 -84 C ATOM 328 CZ PHE A 79 -20.763 24.335 23.759 1.00 7.89 C ANISOU 328 CZ PHE A 79 734 1650 615 -545 60 -129 C ATOM 329 N ILE A 80 -21.754 17.340 22.279 1.00 21.31 N ANISOU 329 N ILE A 80 2479 3186 2431 -89 -20 159 N ATOM 330 CA ILE A 80 -21.835 16.005 21.703 1.00 13.05 C ANISOU 330 CA ILE A 80 1441 2090 1428 -32 -9 194 C ATOM 331 C ILE A 80 -22.931 15.181 22.372 1.00 7.36 C ANISOU 331 C ILE A 80 721 1344 731 0 0 225 C ATOM 332 O ILE A 80 -23.433 14.219 21.801 1.00 41.22 O ANISOU 332 O ILE A 80 4977 5569 5114 38 15 211 O ATOM 333 CB ILE A 80 -20.502 15.276 21.832 1.00 55.34 C ANISOU 333 CB ILE A 80 6739 7565 6724 -30 -8 247 C ATOM 334 CG1 ILE A 80 -19.382 16.091 21.164 1.00 67.26 C ANISOU 334 CG1 ILE A 80 8243 9109 8202 -67 -15 214 C ATOM 335 CG2 ILE A 80 -20.618 13.863 21.273 1.00 49.62 C ANISOU 335 CG2 ILE A 80 5945 6801 6109 26 9 259 C ATOM 336 CD1 ILE A 80 -19.604 16.402 19.683 1.00 8.82 C ANISOU 336 CD1 ILE A 80 842 1572 936 -55 -12 150 C ATOM 337 N THR A 81 -23.292 15.578 23.589 1.00 20.79 N ANISOU 337 N THR A 81 2392 3114 2392 -23 -7 242 N ATOM 338 CA THR A 81 -24.463 15.051 24.277 1.00 30.56 C ANISOU 338 CA THR A 81 3562 4332 3718 2 1 244 C ATOM 339 C THR A 81 -25.712 15.458 23.501 1.00 45.22 C ANISOU 339 C THR A 81 5512 6038 5632 17 6 184 C ATOM 340 O THR A 81 -26.509 14.617 23.065 1.00 27.22 O ANISOU 340 O THR A 81 3308 3683 3353 42 20 198 O ATOM 341 CB THR A 81 -24.574 15.673 25.672 1.00 28.24 C ANISOU 341 CB THR A 81 3213 4143 3374 -42 -13 259 C ATOM 342 OG1 THR A 81 -23.413 15.341 26.441 1.00 39.22 O ANISOU 342 OG1 THR A 81 4510 5692 4700 -67 -19 307 O ATOM 343 CG2 THR A 81 -25.826 15.197 26.380 1.00 17.91 C ANISOU 343 CG2 THR A 81 1991 2797 2016 -11 -4 309 C ATOM 344 N SER A 82 -25.868 16.765 23.319 1.00 50.35 N ANISOU 344 N SER A 82 6198 6650 6283 -14 -5 134 N ATOM 345 CA SER A 82 -26.963 17.301 22.527 1.00 39.55 C ANISOU 345 CA SER A 82 4938 5143 4946 -1 0 81 C ATOM 346 C SER A 82 -26.994 16.667 21.144 1.00 27.39 C ANISOU 346 C SER A 82 3437 3523 3446 9 4 44 C ATOM 347 O SER A 82 -28.036 16.234 20.680 1.00 6.38 O ANISOU 347 O SER A 82 803 816 806 3 2 9 O ATOM 348 CB SER A 82 -26.824 18.815 22.398 1.00 17.61 C ANISOU 348 CB SER A 82 2177 2349 2165 -27 -6 43 C ATOM 349 OG SER A 82 -27.788 19.345 21.504 1.00 0.00 O ANISOU 349 OG SER A 82 0 0 0 0 0 0 O ATOM 350 N LEU A 83 -25.845 16.604 20.487 1.00 10.18 N ANISOU 350 N LEU A 83 1249 1361 1258 7 3 51 N ATOM 351 CA LEU A 83 -25.814 16.099 19.124 1.00 21.46 C ANISOU 351 CA LEU A 83 2712 2728 2714 3 1 10 C ATOM 352 C LEU A 83 -26.168 14.624 19.033 1.00 28.47 C ANISOU 352 C LEU A 83 3584 3639 3595 16 9 39 C ATOM 353 O LEU A 83 -26.898 14.211 18.136 1.00 28.23 O ANISOU 353 O LEU A 83 3575 3575 3575 0 0 0 O ATOM 354 CB LEU A 83 -24.457 16.328 18.474 1.00 32.50 C ANISOU 354 CB LEU A 83 4096 4144 4108 4 2 18 C ATOM 355 CG LEU A 83 -24.662 16.591 16.988 1.00 51.73 C ANISOU 355 CG LEU A 83 6552 6552 6552 0 0 0 C ATOM 356 CD1 LEU A 83 -24.811 18.092 16.797 1.00 7.97 C ANISOU 356 CD1 LEU A 83 1010 1010 1010 0 0 0 C ATOM 357 CD2 LEU A 83 -23.528 16.019 16.158 1.00 0.00 C ANISOU 357 CD2 LEU A 83 0 0 0 0 0 0 C ATOM 358 N ALA A 84 -25.631 13.821 19.940 1.00 39.94 N ANISOU 358 N ALA A 84 4965 5174 5038 46 25 107 N ATOM 359 CA ALA A 84 -26.018 12.423 19.987 1.00 46.87 C ANISOU 359 CA ALA A 84 5820 6069 5919 70 42 143 C ATOM 360 C ALA A 84 -27.522 12.391 20.142 1.00 51.75 C ANISOU 360 C ALA A 84 6490 6639 6535 58 39 131 C ATOM 361 O ALA A 84 -28.190 11.502 19.615 1.00 50.16 O ANISOU 361 O ALA A 84 6295 6419 6344 62 46 130 O ATOM 362 CB ALA A 84 -25.359 11.725 21.148 1.00 57.04 C ANISOU 362 CB ALA A 84 7028 7460 7183 98 55 226 C ATOM 363 N CYS A 85 -28.054 13.374 20.867 1.00 51.89 N ANISOU 363 N CYS A 85 6513 6649 6553 48 32 114 N ATOM 364 CA CYS A 85 -29.498 13.475 21.026 1.00 37.21 C ANISOU 364 CA CYS A 85 4671 4759 4707 41 31 90 C ATOM 365 C CYS A 85 -30.189 13.697 19.681 1.00 23.41 C ANISOU 365 C CYS A 85 2954 2973 2968 12 10 19 C ATOM 366 O CYS A 85 -30.974 12.856 19.253 1.00 32.77 O ANISOU 366 O CYS A 85 4136 4159 4156 17 16 26 O ATOM 367 CB CYS A 85 -29.871 14.594 21.998 1.00 42.80 C ANISOU 367 CB CYS A 85 5366 5473 5422 38 27 74 C ATOM 368 SG CYS A 85 -29.449 14.280 23.718 1.00 98.05 S ANISOU 368 SG CYS A 85 12286 12566 12403 64 39 160 S ATOM 369 N ALA A 86 -29.874 14.799 19.000 1.00 28.31 N ANISOU 369 N ALA A 86 3585 3585 3585 0 0 0 N ATOM 370 CA ALA A 86 -30.540 15.113 17.738 1.00 49.25 C ANISOU 370 CA ALA A 86 6238 6238 6238 0 0 0 C ATOM 371 C ALA A 86 -30.443 13.907 16.817 1.00 49.43 C ANISOU 371 C ALA A 86 6260 6260 6260 0 0 0 C ATOM 372 O ALA A 86 -31.450 13.440 16.282 1.00 60.53 O ANISOU 372 O ALA A 86 7666 7666 7666 0 0 0 O ATOM 373 CB ALA A 86 -29.950 16.370 17.075 1.00 0.00 C ANISOU 373 CB ALA A 86 0 0 0 0 0 0 C ATOM 374 N ASP A 87 -29.230 13.389 16.662 1.00 47.29 N ANISOU 374 N ASP A 87 5989 5989 5989 0 0 0 N ATOM 375 CA ASP A 87 -28.987 12.230 15.808 1.00 63.01 C ANISOU 375 CA ASP A 87 7980 7980 7980 0 0 0 C ATOM 376 C ASP A 87 -29.881 11.059 16.220 1.00 52.80 C ANISOU 376 C ASP A 87 6686 6689 6688 3 4 6 C ATOM 377 O ASP A 87 -30.357 10.271 15.380 1.00 55.33 O ANISOU 377 O ASP A 87 7006 7008 7008 3 3 5 O ATOM 378 CB ASP A 87 -27.507 11.826 15.866 1.00 68.68 C ANISOU 378 CB ASP A 87 8699 8699 8699 0 0 0 C ATOM 379 CG ASP A 87 -26.592 12.863 15.239 1.00 57.24 C ANISOU 379 CG ASP A 87 7250 7250 7250 0 0 0 C ATOM 380 OD1 ASP A 87 -26.896 13.304 14.111 1.00 35.31 O ANISOU 380 OD1 ASP A 87 4472 4472 4472 0 0 0 O ATOM 381 OD2 ASP A 87 -25.578 13.237 15.875 1.00 48.86 O ANISOU 381 OD2 ASP A 87 6188 6188 6188 0 0 0 O ATOM 382 N LEU A 88 -30.119 10.961 17.523 1.00 30.99 N ANISOU 382 N LEU A 88 3902 3938 3934 28 27 41 N ATOM 383 CA LEU A 88 -30.937 9.889 18.053 1.00 37.01 C ANISOU 383 CA LEU A 88 4640 4713 4708 56 54 85 C ATOM 384 C LEU A 88 -32.411 10.060 17.680 1.00 44.78 C ANISOU 384 C LEU A 88 5650 5675 5688 40 38 66 C ATOM 385 O LEU A 88 -33.021 9.161 17.104 1.00 22.07 O ANISOU 385 O LEU A 88 2762 2807 2818 43 55 70 O ATOM 386 CB LEU A 88 -30.776 9.801 19.561 1.00 20.79 C ANISOU 386 CB LEU A 88 2550 2689 2661 85 77 138 C ATOM 387 CG LEU A 88 -31.351 8.503 20.109 1.00 33.87 C ANISOU 387 CG LEU A 88 4206 4351 4313 108 99 220 C ATOM 388 CD1 LEU A 88 -30.248 7.681 20.750 1.00 10.32 C ANISOU 388 CD1 LEU A 88 1185 1417 1320 139 118 296 C ATOM 389 CD2 LEU A 88 -32.486 8.795 21.082 1.00 52.25 C ANISOU 389 CD2 LEU A 88 6488 6696 6669 123 115 211 C ATOM 390 N VAL A 89 -32.987 11.214 17.993 1.00 61.64 N ANISOU 390 N VAL A 89 7791 7812 7817 20 26 33 N ATOM 391 CA VAL A 89 -34.364 11.478 17.598 1.00 55.99 C ANISOU 391 CA VAL A 89 7085 7092 7098 10 14 16 C ATOM 392 C VAL A 89 -34.511 11.216 16.101 1.00 32.51 C ANISOU 392 C VAL A 89 4117 4117 4117 0 0 0 C ATOM 393 O VAL A 89 -35.554 10.751 15.654 1.00 10.75 O ANISOU 393 O VAL A 89 1361 1361 1361 0 0 0 O ATOM 394 CB VAL A 89 -34.798 12.924 17.936 1.00 54.37 C ANISOU 394 CB VAL A 89 6886 6886 6886 0 0 0 C ATOM 395 CG1 VAL A 89 -36.274 13.115 17.649 1.00 32.66 C ANISOU 395 CG1 VAL A 89 4137 4137 4137 0 0 0 C ATOM 396 CG2 VAL A 89 -34.510 13.235 19.394 1.00 64.92 C ANISOU 396 CG2 VAL A 89 8219 8221 8227 8 9 13 C ATOM 397 N VAL A 90 -33.458 11.510 15.338 1.00 20.54 N ANISOU 397 N VAL A 90 2602 2602 2602 0 0 0 N ATOM 398 CA VAL A 90 -33.430 11.187 13.911 1.00 36.41 C ANISOU 398 CA VAL A 90 4611 4611 4611 0 0 0 C ATOM 399 C VAL A 90 -33.691 9.709 13.714 1.00 50.18 C ANISOU 399 C VAL A 90 6355 6355 6355 0 0 0 C ATOM 400 O VAL A 90 -34.630 9.320 13.011 1.00 36.10 O ANISOU 400 O VAL A 90 4572 4572 4572 0 0 0 O ATOM 401 CB VAL A 90 -32.047 11.464 13.263 1.00 58.55 C ANISOU 401 CB VAL A 90 7415 7415 7415 0 0 0 C ATOM 402 CG1 VAL A 90 -31.996 10.920 11.831 1.00 8.42 C ANISOU 402 CG1 VAL A 90 1067 1067 1067 0 0 0 C ATOM 403 CG2 VAL A 90 -31.725 12.936 13.275 1.00 91.98 C ANISOU 403 CG2 VAL A 90 11649 11649 11649 0 0 0 C ATOM 404 N GLY A 91 -32.846 8.887 14.337 1.00 44.77 N ANISOU 404 N GLY A 91 5668 5669 5675 9 9 13 N ATOM 405 CA GLY A 91 -32.937 7.444 14.167 1.00 12.19 C ANISOU 405 CA GLY A 91 1531 1540 1562 34 35 52 C ATOM 406 C GLY A 91 -34.026 6.803 15.002 1.00 18.18 C ANISOU 406 C GLY A 91 2264 2308 2335 53 73 84 C ATOM 407 O GLY A 91 -34.082 5.587 15.132 1.00 17.24 O ANISOU 407 O GLY A 91 2142 2175 2232 84 87 137 O ATOM 408 N LEU A 92 -34.896 7.630 15.565 1.00 27.08 N ANISOU 408 N LEU A 92 3408 3421 3462 50 55 80 N ATOM 409 CA LEU A 92 -35.973 7.152 16.415 1.00 42.40 C ANISOU 409 CA LEU A 92 5335 5357 5419 71 79 119 C ATOM 410 C LEU A 92 -37.328 7.523 15.816 1.00 69.53 C ANISOU 410 C LEU A 92 8780 8787 8851 57 69 94 C ATOM 411 O LEU A 92 -38.102 6.646 15.445 1.00 84.25 O ANISOU 411 O LEU A 92 10638 10646 10729 68 83 114 O ATOM 412 CB LEU A 92 -35.827 7.729 17.826 1.00 56.17 C ANISOU 412 CB LEU A 92 7050 7125 7168 76 104 130 C ATOM 413 CG LEU A 92 -36.784 7.256 18.927 1.00 70.52 C ANISOU 413 CG LEU A 92 8840 8948 9008 99 136 177 C ATOM 414 CD1 LEU A 92 -36.583 5.794 19.231 1.00 3.35 C ANISOU 414 CD1 LEU A 92 296 456 521 128 171 236 C ATOM 415 CD2 LEU A 92 -36.587 8.080 20.188 1.00 78.67 C ANISOU 415 CD2 LEU A 92 9891 9963 10036 112 114 205 C ATOM 416 N LEU A 93 -37.629 8.819 15.766 1.00 66.21 N ANISOU 416 N LEU A 93 8362 8380 8413 33 53 53 N ATOM 417 CA LEU A 93 -38.869 9.311 15.147 1.00 21.47 C ANISOU 417 CA LEU A 93 2710 2706 2743 25 34 40 C ATOM 418 C LEU A 93 -38.862 9.543 13.635 1.00 12.37 C ANISOU 418 C LEU A 93 1565 1565 1571 4 7 6 C ATOM 419 O LEU A 93 -39.860 9.269 12.977 1.00 19.69 O ANISOU 419 O LEU A 93 2491 2492 2500 5 9 8 O ATOM 420 CB LEU A 93 -39.398 10.542 15.876 1.00 23.44 C ANISOU 420 CB LEU A 93 2957 2962 2987 18 32 29 C ATOM 421 CG LEU A 93 -39.990 10.165 17.242 1.00 60.05 C ANISOU 421 CG LEU A 93 7576 7594 7648 41 70 67 C ATOM 422 CD1 LEU A 93 -40.611 11.362 17.938 1.00 75.66 C ANISOU 422 CD1 LEU A 93 9557 9569 9622 37 66 60 C ATOM 423 CD2 LEU A 93 -41.016 9.051 17.105 1.00 49.59 C ANISOU 423 CD2 LEU A 93 6235 6264 6344 57 98 97 C ATOM 424 N VAL A 94 -37.763 10.070 13.093 1.00 0.00 N ANISOU 424 N VAL A 94 0 0 0 0 0 0 N ATOM 425 CA VAL A 94 -37.693 10.400 11.664 1.00 24.03 C ANISOU 425 CA VAL A 94 3043 3043 3043 0 0 0 C ATOM 426 C VAL A 94 -37.376 9.285 10.691 1.00 2.28 C ANISOU 426 C VAL A 94 289 289 289 0 0 0 C ATOM 427 O VAL A 94 -37.955 9.233 9.615 1.00 0.00 O ANISOU 427 O VAL A 94 0 0 0 0 0 0 O ATOM 428 CB VAL A 94 -36.723 11.512 11.371 1.00 20.96 C ANISOU 428 CB VAL A 94 2655 2655 2655 0 0 0 C ATOM 429 CG1 VAL A 94 -36.145 11.312 10.001 1.00 0.00 C ANISOU 429 CG1 VAL A 94 0 0 0 0 0 0 C ATOM 430 CG2 VAL A 94 -37.448 12.829 11.440 1.00 7.79 C ANISOU 430 CG2 VAL A 94 986 986 986 0 0 0 C ATOM 431 N VAL A 95 -36.430 8.423 11.032 1.00 0.00 N ANISOU 431 N VAL A 95 0 0 0 0 0 0 N ATOM 432 CA VAL A 95 -36.086 7.330 10.128 1.00 47.57 C ANISOU 432 CA VAL A 95 6025 6025 6025 0 0 0 C ATOM 433 C VAL A 95 -37.145 6.245 9.961 1.00 44.41 C ANISOU 433 C VAL A 95 5624 5624 5625 1 1 1 C ATOM 434 O VAL A 95 -37.417 5.842 8.839 1.00 0.00 O ANISOU 434 O VAL A 95 0 0 0 0 0 0 O ATOM 435 CB VAL A 95 -34.760 6.651 10.478 1.00 54.17 C ANISOU 435 CB VAL A 95 6861 6861 6861 0 0 0 C ATOM 436 CG1 VAL A 95 -34.600 5.399 9.637 1.00 6.28 C ANISOU 436 CG1 VAL A 95 793 795 800 5 8 8 C ATOM 437 CG2 VAL A 95 -33.612 7.597 10.226 1.00 84.40 C ANISOU 437 CG2 VAL A 95 10690 10690 10690 0 0 0 C ATOM 438 N PRO A 96 -37.713 5.741 11.072 1.00 49.42 N ANISOU 438 N PRO A 96 6251 6246 6279 24 32 37 N ATOM 439 CA PRO A 96 -38.706 4.663 10.991 1.00 54.95 C ANISOU 439 CA PRO A 96 6943 6936 7000 42 57 68 C ATOM 440 C PRO A 96 -39.948 5.071 10.215 1.00 43.70 C ANISOU 440 C PRO A 96 5523 5514 5566 30 44 49 C ATOM 441 O PRO A 96 -40.425 4.345 9.343 1.00 17.85 O ANISOU 441 O PRO A 96 2248 2238 2296 32 48 52 O ATOM 442 CB PRO A 96 -39.085 4.440 12.457 1.00 19.18 C ANISOU 442 CB PRO A 96 2383 2414 2490 60 100 100 C ATOM 443 CG PRO A 96 -38.804 5.717 13.106 1.00 4.66 C ANISOU 443 CG PRO A 96 568 564 640 53 69 87 C ATOM 444 CD PRO A 96 -37.543 6.196 12.460 1.00 8.52 C ANISOU 444 CD PRO A 96 1066 1063 1107 34 44 53 C ATOM 445 N PHE A 97 -40.475 6.240 10.537 1.00 0.51 N ANISOU 445 N PHE A 97 57 50 86 20 30 32 N ATOM 446 CA PHE A 97 -41.616 6.738 9.814 1.00 0.31 C ANISOU 446 CA PHE A 97 32 33 51 11 21 17 C ATOM 447 C PHE A 97 -41.134 7.099 8.434 1.00 24.48 C ANISOU 447 C PHE A 97 3101 3101 3101 0 0 0 C ATOM 448 O PHE A 97 -41.885 7.022 7.469 1.00 0.00 O ANISOU 448 O PHE A 97 0 0 0 0 0 0 O ATOM 449 CB PHE A 97 -42.221 7.939 10.528 1.00 10.26 C ANISOU 449 CB PHE A 97 1297 1292 1310 9 14 14 C ATOM 450 CG PHE A 97 -43.023 7.568 11.734 1.00 49.61 C ANISOU 450 CG PHE A 97 6262 6267 6319 27 54 45 C ATOM 451 CD1 PHE A 97 -43.099 6.241 12.144 1.00 65.16 C ANISOU 451 CD1 PHE A 97 8228 8213 8317 50 77 87 C ATOM 452 CD2 PHE A 97 -43.718 8.528 12.446 1.00 23.94 C ANISOU 452 CD2 PHE A 97 3010 3014 3071 28 57 47 C ATOM 453 CE1 PHE A 97 -43.843 5.879 13.250 1.00 41.02 C ANISOU 453 CE1 PHE A 97 5134 5165 5287 65 122 117 C ATOM 454 CE2 PHE A 97 -44.467 8.176 13.552 1.00 30.93 C ANISOU 454 CE2 PHE A 97 3878 3891 3984 47 93 81 C ATOM 455 CZ PHE A 97 -44.528 6.847 13.955 1.00 46.75 C ANISOU 455 CZ PHE A 97 5860 5888 6015 64 124 116 C ATOM 456 N GLY A 98 -39.853 7.446 8.355 1.00 31.74 N ANISOU 456 N GLY A 98 4020 4020 4020 0 0 0 N ATOM 457 CA GLY A 98 -39.232 7.924 7.131 1.00 34.07 C ANISOU 457 CA GLY A 98 4315 4315 4315 0 0 0 C ATOM 458 C GLY A 98 -38.970 6.849 6.099 1.00 17.73 C ANISOU 458 C GLY A 98 2245 2245 2245 0 0 0 C ATOM 459 O GLY A 98 -38.706 7.134 4.940 1.00 0.00 O ANISOU 459 O GLY A 98 0 0 0 0 0 0 O ATOM 460 N ALA A 99 -39.030 5.601 6.529 1.00 18.76 N ANISOU 460 N ALA A 99 2376 2376 2376 0 0 0 N ATOM 461 CA ALA A 99 -38.988 4.490 5.609 1.00 41.32 C ANISOU 461 CA ALA A 99 5233 5233 5233 0 0 0 C ATOM 462 C ALA A 99 -40.367 4.370 4.966 1.00 58.86 C ANISOU 462 C ALA A 99 7455 7455 7455 0 0 0 C ATOM 463 O ALA A 99 -40.482 4.283 3.741 1.00 0.00 O ANISOU 463 O ALA A 99 0 0 0 0 0 0 O ATOM 464 CB ALA A 99 -38.628 3.210 6.348 1.00 27.57 C ANISOU 464 CB ALA A 99 3489 3485 3500 9 13 13 C ATOM 465 N THR A 100 -41.414 4.449 5.791 1.00 75.14 N ANISOU 465 N THR A 100 9516 9516 9516 0 0 0 N ATOM 466 CA THR A 100 -42.753 4.035 5.369 1.00 77.18 C ANISOU 466 CA THR A 100 9772 9772 9781 4 9 7 C ATOM 467 C THR A 100 -43.112 4.640 4.020 1.00 63.31 C ANISOU 467 C THR A 100 8018 8018 8018 0 0 0 C ATOM 468 O THR A 100 -43.909 4.078 3.277 1.00 86.36 O ANISOU 468 O THR A 100 10937 10937 10937 0 0 0 O ATOM 469 CB THR A 100 -43.861 4.367 6.414 1.00 3.02 C ANISOU 469 CB THR A 100 371 372 406 16 33 26 C ATOM 470 OG1 THR A 100 -44.314 5.714 6.241 1.00 0.21 O ANISOU 470 OG1 THR A 100 25 22 32 4 7 7 O ATOM 471 CG2 THR A 100 -43.361 4.152 7.832 1.00 0.87 C ANISOU 471 CG2 THR A 100 87 93 151 29 58 48 C ATOM 472 N LEU A 101 -42.512 5.780 3.702 1.00 39.45 N ANISOU 472 N LEU A 101 4997 4997 4997 0 0 0 N ATOM 473 CA LEU A 101 -42.750 6.431 2.420 1.00 53.60 C ANISOU 473 CA LEU A 101 6789 6789 6789 0 0 0 C ATOM 474 C LEU A 101 -41.942 5.773 1.301 1.00 46.06 C ANISOU 474 C LEU A 101 5834 5834 5834 0 0 0 C ATOM 475 O LEU A 101 -42.361 5.774 0.146 1.00 70.37 O ANISOU 475 O LEU A 101 8913 8913 8913 0 0 0 O ATOM 476 CB LEU A 101 -42.421 7.928 2.503 1.00 58.98 C ANISOU 476 CB LEU A 101 7470 7470 7470 0 0 0 C ATOM 477 CG LEU A 101 -43.065 8.900 1.514 1.00 19.15 C ANISOU 477 CG LEU A 101 2426 2426 2426 0 0 0 C ATOM 478 CD1 LEU A 101 -44.422 9.329 2.005 1.00 4.10 C ANISOU 478 CD1 LEU A 101 519 519 519 0 0 0 C ATOM 479 CD2 LEU A 101 -42.191 10.113 1.341 1.00 50.52 C ANISOU 479 CD2 LEU A 101 6399 6399 6399 0 0 0 C ATOM 480 N VAL A 102 -40.765 5.251 1.627 1.00 38.74 N ANISOU 480 N VAL A 102 4907 4907 4907 0 0 0 N ATOM 481 CA VAL A 102 -39.952 4.573 0.623 1.00 61.92 C ANISOU 481 CA VAL A 102 7842 7842 7842 0 0 0 C ATOM 482 C VAL A 102 -40.369 3.116 0.434 1.00120.06 C ANISOU 482 C VAL A 102 15206 15206 15206 0 0 0 C ATOM 483 O VAL A 102 -40.414 2.611 -0.689 1.00140.29 O ANISOU 483 O VAL A 102 17768 17768 17768 0 0 0 O ATOM 484 CB VAL A 102 -38.453 4.642 0.942 1.00 25.06 C ANISOU 484 CB VAL A 102 3174 3174 3174 0 0 0 C ATOM 485 CG1 VAL A 102 -37.657 4.595 -0.346 1.00 0.00 C ANISOU 485 CG1 VAL A 102 0 0 0 0 0 0 C ATOM 486 CG2 VAL A 102 -38.136 5.911 1.707 1.00 35.10 C ANISOU 486 CG2 VAL A 102 4445 4445 4445 0 0 0 C ATOM 487 N VAL A 103 -40.657 2.442 1.544 1.00133.70 N ANISOU 487 N VAL A 103 16933 16933 16933 0 0 0 N ATOM 488 CA VAL A 103 -41.031 1.033 1.524 1.00131.24 C ANISOU 488 CA VAL A 103 16622 16622 16622 0 0 0 C ATOM 489 C VAL A 103 -42.322 0.806 0.746 1.00129.35 C ANISOU 489 C VAL A 103 16383 16383 16383 0 0 0 C ATOM 490 O VAL A 103 -42.329 0.096 -0.260 1.00125.07 O ANISOU 490 O VAL A 103 15840 15840 15840 0 0 0 O ATOM 491 CB VAL A 103 -41.190 0.471 2.963 1.00117.73 C ANISOU 491 CB VAL A 103 14904 14892 14935 20 33 32 C ATOM 492 CG1 VAL A 103 -42.097 -0.752 2.973 1.00116.14 C ANISOU 492 CG1 VAL A 103 14681 14685 14761 37 76 61 C ATOM 493 CG2 VAL A 103 -39.830 0.143 3.572 1.00116.76 C ANISOU 493 CG2 VAL A 103 14773 14775 14817 26 50 39 C ATOM 494 N ARG A 104 -43.403 1.437 1.197 1.00138.42 N ANISOU 494 N ARG A 104 17531 17531 17531 0 0 0 N ATOM 495 CA ARG A 104 -44.721 1.257 0.590 1.00131.72 C ANISOU 495 CA ARG A 104 16681 16678 16687 3 6 5 C ATOM 496 C ARG A 104 -44.962 2.218 -0.573 1.00106.08 C ANISOU 496 C ARG A 104 13435 13435 13435 0 0 0 C ATOM 497 O ARG A 104 -45.880 2.025 -1.366 1.00 77.20 O ANISOU 497 O ARG A 104 9777 9777 9777 0 0 0 O ATOM 498 CB ARG A 104 -45.822 1.410 1.647 1.00118.48 C ANISOU 498 CB ARG A 104 14991 14992 15033 15 35 27 C ATOM 499 CG ARG A 104 -47.227 1.104 1.141 1.00119.02 C ANISOU 499 CG ARG A 104 15059 15045 15119 23 45 44 C ATOM 500 CD ARG A 104 -47.268 -0.237 0.419 1.00142.60 C ANISOU 500 CD ARG A 104 18039 18020 18123 31 60 60 C ATOM 501 NE ARG A 104 -48.581 -0.524 -0.157 1.00161.78 N ANISOU 501 NE ARG A 104 20459 20439 20570 36 71 73 N ATOM 502 CZ ARG A 104 -48.917 -0.285 -1.422 1.00159.28 C ANISOU 502 CZ ARG A 104 20152 20136 20233 26 52 52 C ATOM 503 NH1 ARG A 104 -48.035 0.250 -2.257 1.00159.40 N ANISOU 503 NH1 ARG A 104 20182 20175 20207 9 19 17 N ATOM 504 NH2 ARG A 104 -50.137 -0.583 -1.854 1.00143.67 N ANISOU 504 NH2 ARG A 104 18149 18161 18277 29 74 63 N ATOM 505 N GLY A 105 -44.119 3.240 -0.680 1.00109.11 N ANISOU 505 N GLY A 105 13819 13819 13819 0 0 0 N ATOM 506 CA GLY A 105 -44.253 4.235 -1.727 1.00 85.37 C ANISOU 506 CA GLY A 105 10812 10812 10812 0 0 0 C ATOM 507 C GLY A 105 -45.051 5.463 -1.314 1.00 70.03 C ANISOU 507 C GLY A 105 8869 8869 8869 0 0 0 C ATOM 508 O GLY A 105 -45.043 6.470 -2.025 1.00 23.50 O ANISOU 508 O GLY A 105 2976 2976 2976 0 0 0 O ATOM 509 N THR A 106 -45.738 5.384 -0.172 1.00 76.00 N ANISOU 509 N THR A 106 9625 9625 9625 0 0 0 N ATOM 510 CA THR A 106 -46.613 6.467 0.294 1.00 48.10 C ANISOU 510 CA THR A 106 6092 6092 6092 0 0 0 C ATOM 511 C THR A 106 -46.807 6.539 1.800 1.00 48.29 C ANISOU 511 C THR A 106 6116 6116 6116 0 0 0 C ATOM 512 O THR A 106 -46.497 5.610 2.538 1.00 35.02 O ANISOU 512 O THR A 106 4435 4435 4435 0 0 0 O ATOM 513 CB THR A 106 -48.019 6.336 -0.245 1.00 55.50 C ANISOU 513 CB THR A 106 7029 7029 7029 0 0 0 C ATOM 514 OG1 THR A 106 -48.678 5.276 0.454 1.00 54.21 O ANISOU 514 OG1 THR A 106 6866 6866 6866 0 0 0 O ATOM 515 CG2 THR A 106 -48.010 6.061 -1.739 1.00 96.97 C ANISOU 515 CG2 THR A 106 12281 12281 12281 0 0 0 C ATOM 516 N TRP A 107 -47.373 7.659 2.228 1.00 85.72 N ANISOU 516 N TRP A 107 10857 10857 10857 0 0 0 N ATOM 517 CA TRP A 107 -47.576 7.975 3.636 1.00 96.04 C ANISOU 517 CA TRP A 107 12163 12163 12163 0 0 0 C ATOM 518 C TRP A 107 -48.922 7.483 4.173 1.00 72.05 C ANISOU 518 C TRP A 107 9121 9120 9136 5 13 9 C ATOM 519 O TRP A 107 -49.974 7.905 3.706 1.00 75.12 O ANISOU 519 O TRP A 107 9509 9502 9530 8 16 14 O ATOM 520 CB TRP A 107 -47.503 9.488 3.795 1.00 92.74 C ANISOU 520 CB TRP A 107 11746 11746 11746 0 0 0 C ATOM 521 CG TRP A 107 -47.474 9.936 5.186 1.00 49.63 C ANISOU 521 CG TRP A 107 6286 6286 6286 0 0 0 C ATOM 522 CD1 TRP A 107 -48.530 10.348 5.935 1.00 25.61 C ANISOU 522 CD1 TRP A 107 3244 3244 3244 0 0 0 C ATOM 523 CD2 TRP A 107 -46.321 10.028 6.018 1.00 46.07 C ANISOU 523 CD2 TRP A 107 5835 5835 5835 0 0 0 C ATOM 524 NE1 TRP A 107 -48.105 10.695 7.191 1.00 52.42 N ANISOU 524 NE1 TRP A 107 6638 6635 6644 3 6 4 N ATOM 525 CE2 TRP A 107 -46.750 10.507 7.268 1.00 49.39 C ANISOU 525 CE2 TRP A 107 6255 6255 6255 0 0 0 C ATOM 526 CE3 TRP A 107 -44.966 9.752 5.826 1.00 42.04 C ANISOU 526 CE3 TRP A 107 5324 5324 5324 0 0 0 C ATOM 527 CZ2 TRP A 107 -45.871 10.718 8.325 1.00 48.14 C ANISOU 527 CZ2 TRP A 107 6097 6097 6097 0 0 0 C ATOM 528 CZ3 TRP A 107 -44.097 9.957 6.873 1.00 74.65 C ANISOU 528 CZ3 TRP A 107 9455 9455 9455 0 0 0 C ATOM 529 CH2 TRP A 107 -44.551 10.437 8.110 1.00 77.92 C ANISOU 529 CH2 TRP A 107 9869 9869 9869 0 0 0 C ATOM 530 N LEU A 108 -48.888 6.588 5.151 1.00 48.64 N ANISOU 530 N LEU A 108 6142 6144 6196 17 42 32 N ATOM 531 CA LEU A 108 -50.115 6.067 5.742 1.00 52.07 C ANISOU 531 CA LEU A 108 6569 6546 6671 37 71 71 C ATOM 532 C LEU A 108 -50.504 6.746 7.066 1.00 60.59 C ANISOU 532 C LEU A 108 7623 7634 7766 41 99 81 C ATOM 533 O LEU A 108 -51.545 6.448 7.648 1.00 79.96 O ANISOU 533 O LEU A 108 10077 10046 10258 59 115 121 O ATOM 534 CB LEU A 108 -50.001 4.549 5.945 1.00 73.60 C ANISOU 534 CB LEU A 108 9262 9278 9423 45 105 91 C ATOM 535 CG LEU A 108 -48.811 3.771 5.357 1.00 72.61 C ANISOU 535 CG LEU A 108 9164 9141 9282 43 81 85 C ATOM 536 CD1 LEU A 108 -48.832 2.322 5.834 1.00 61.32 C ANISOU 536 CD1 LEU A 108 7716 7692 7890 60 111 124 C ATOM 537 CD2 LEU A 108 -48.755 3.825 3.831 1.00 55.24 C ANISOU 537 CD2 LEU A 108 6964 6970 7054 27 64 52 C ATOM 538 N TRP A 109 -49.672 7.667 7.531 1.00 54.71 N ANISOU 538 N TRP A 109 6893 6898 6998 33 79 62 N ATOM 539 CA TRP A 109 -49.723 8.111 8.930 1.00 57.49 C ANISOU 539 CA TRP A 109 7253 7223 7368 45 86 84 C ATOM 540 C TRP A 109 -50.564 9.362 9.252 1.00 50.56 C ANISOU 540 C TRP A 109 6375 6342 6495 46 91 85 C ATOM 541 O TRP A 109 -50.478 9.907 10.352 1.00 31.49 O ANISOU 541 O TRP A 109 3957 3920 4087 51 100 93 O ATOM 542 CB TRP A 109 -48.303 8.230 9.490 1.00 50.08 C ANISOU 542 CB TRP A 109 6322 6297 6411 38 71 69 C ATOM 543 CG TRP A 109 -47.490 6.984 9.253 1.00 65.79 C ANISOU 543 CG TRP A 109 8295 8302 8399 37 82 67 C ATOM 544 CD1 TRP A 109 -46.787 6.663 8.125 1.00 95.42 C ANISOU 544 CD1 TRP A 109 12070 12053 12132 28 51 50 C ATOM 545 CD2 TRP A 109 -47.312 5.891 10.158 1.00 46.38 C ANISOU 545 CD2 TRP A 109 5838 5813 5972 57 100 108 C ATOM 546 NE1 TRP A 109 -46.177 5.440 8.278 1.00 77.26 N ANISOU 546 NE1 TRP A 109 9764 9745 9845 37 65 67 N ATOM 547 CE2 TRP A 109 -46.484 4.947 9.517 1.00 36.63 C ANISOU 547 CE2 TRP A 109 4585 4603 4728 51 108 95 C ATOM 548 CE3 TRP A 109 -47.767 5.621 11.448 1.00 65.20 C ANISOU 548 CE3 TRP A 109 8178 8209 8385 69 145 134 C ATOM 549 CZ2 TRP A 109 -46.104 3.763 10.120 1.00 15.70 C ANISOU 549 CZ2 TRP A 109 1915 1947 2104 67 136 127 C ATOM 550 CZ3 TRP A 109 -47.386 4.441 12.048 1.00 84.91 C ANISOU 550 CZ3 TRP A 109 10686 10667 10910 91 150 182 C ATOM 551 CH2 TRP A 109 -46.562 3.526 11.384 1.00 60.23 C ANISOU 551 CH2 TRP A 109 7562 7545 7778 90 146 179 C ATOM 552 N GLY A 110 -51.317 9.854 8.277 1.00 47.90 N ANISOU 552 N GLY A 110 6024 6026 6151 38 96 71 N ATOM 553 CA GLY A 110 -52.185 10.998 8.501 1.00 57.79 C ANISOU 553 CA GLY A 110 7291 7251 7416 45 95 83 C ATOM 554 C GLY A 110 -51.375 12.261 8.329 1.00 77.22 C ANISOU 554 C GLY A 110 9752 9746 9843 29 77 50 C ATOM 555 O GLY A 110 -50.187 12.273 8.651 1.00 97.19 O ANISOU 555 O GLY A 110 12291 12284 12353 22 57 37 O ATOM 556 N SER A 111 -51.999 13.333 7.852 1.00 77.49 N ANISOU 556 N SER A 111 9800 9764 9879 30 69 52 N ATOM 557 CA SER A 111 -51.223 14.521 7.493 1.00 87.59 C ANISOU 557 CA SER A 111 11087 11062 11132 19 44 30 C ATOM 558 C SER A 111 -50.873 15.403 8.692 1.00 55.59 C ANISOU 558 C SER A 111 7026 7013 7081 20 58 31 C ATOM 559 O SER A 111 -49.918 16.179 8.645 1.00 20.02 O ANISOU 559 O SER A 111 2533 2513 2559 12 31 19 O ATOM 560 CB SER A 111 -51.883 15.321 6.358 1.00 81.82 C ANISOU 560 CB SER A 111 10357 10333 10397 16 40 26 C ATOM 561 OG SER A 111 -51.223 15.084 5.111 1.00 34.19 O ANISOU 561 OG SER A 111 4329 4324 4338 4 9 6 O ATOM 562 N PHE A 112 -51.631 15.272 9.772 1.00 36.74 N ANISOU 562 N PHE A 112 4641 4592 4727 35 84 57 N ATOM 563 CA PHE A 112 -51.264 15.934 11.011 1.00 51.12 C ANISOU 563 CA PHE A 112 6448 6426 6550 35 104 56 C ATOM 564 C PHE A 112 -49.870 15.432 11.364 1.00 23.84 C ANISOU 564 C PHE A 112 3001 2983 3073 27 78 43 C ATOM 565 O PHE A 112 -48.889 16.189 11.474 1.00 38.84 O ANISOU 565 O PHE A 112 4909 4894 4956 19 56 28 O ATOM 566 CB PHE A 112 -52.261 15.539 12.097 1.00 78.94 C ANISOU 566 CB PHE A 112 9976 9903 10116 55 131 92 C ATOM 567 CG PHE A 112 -52.088 16.283 13.384 1.00 98.06 C ANISOU 567 CG PHE A 112 12374 12342 12541 55 162 90 C ATOM 568 CD1 PHE A 112 -52.752 17.480 13.599 1.00112.25 C ANISOU 568 CD1 PHE A 112 14170 14127 14354 60 185 96 C ATOM 569 CD2 PHE A 112 -51.270 15.782 14.384 1.00 80.92 C ANISOU 569 CD2 PHE A 112 10204 10176 10367 56 159 92 C ATOM 570 CE1 PHE A 112 -52.597 18.166 14.784 1.00111.53 C ANISOU 570 CE1 PHE A 112 14107 13988 14283 70 184 110 C ATOM 571 CE2 PHE A 112 -51.113 16.462 15.571 1.00 69.21 C ANISOU 571 CE2 PHE A 112 8745 8653 8900 66 157 106 C ATOM 572 CZ PHE A 112 -51.777 17.656 15.773 1.00 91.86 C ANISOU 572 CZ PHE A 112 11588 11539 11774 64 197 101 C ATOM 573 N LEU A 113 -49.792 14.119 11.499 1.00 29.11 N ANISOU 573 N LEU A 113 3675 3635 3750 34 74 54 N ATOM 574 CA LEU A 113 -48.530 13.446 11.726 1.00 54.71 C ANISOU 574 CA LEU A 113 6912 6902 6975 25 64 40 C ATOM 575 C LEU A 113 -47.533 13.728 10.597 1.00 78.06 C ANISOU 575 C LEU A 113 9882 9877 9902 9 23 13 C ATOM 576 O LEU A 113 -46.338 13.796 10.837 1.00 87.74 O ANISOU 576 O LEU A 113 11112 11112 11114 1 2 1 O ATOM 577 CB LEU A 113 -48.768 11.944 11.873 1.00 30.49 C ANISOU 577 CB LEU A 113 3833 3827 3925 34 84 57 C ATOM 578 CG LEU A 113 -47.542 11.066 12.075 1.00 12.11 C ANISOU 578 CG LEU A 113 1519 1491 1590 34 65 57 C ATOM 579 CD1 LEU A 113 -46.640 11.617 13.165 1.00 45.82 C ANISOU 579 CD1 LEU A 113 5791 5764 5854 33 61 53 C ATOM 580 CD2 LEU A 113 -48.004 9.700 12.429 1.00 12.48 C ANISOU 580 CD2 LEU A 113 1554 1522 1666 50 92 89 C ATOM 581 N CYS A 114 -48.023 13.882 9.371 1.00 78.59 N ANISOU 581 N CYS A 114 9953 9947 9962 5 10 7 N ATOM 582 CA CYS A 114 -47.158 14.218 8.248 1.00 0.00 C ANISOU 582 CA CYS A 114 0 0 0 0 0 0 C ATOM 583 C CYS A 114 -46.362 15.468 8.607 1.00 53.19 C ANISOU 583 C CYS A 114 6736 6736 6736 0 0 0 C ATOM 584 O CYS A 114 -45.123 15.455 8.592 1.00 78.10 O ANISOU 584 O CYS A 114 9891 9891 9891 0 0 0 O ATOM 585 CB CYS A 114 -48.003 14.451 7.000 1.00 0.00 C ANISOU 585 CB CYS A 114 0 0 0 0 0 0 C ATOM 586 SG CYS A 114 -47.128 14.956 5.506 1.00 73.48 S ANISOU 586 SG CYS A 114 9306 9306 9306 0 0 0 S ATOM 587 N GLU A 115 -47.078 16.535 8.963 1.00 31.33 N ANISOU 587 N GLU A 115 3968 3968 3968 0 0 0 N ATOM 588 CA GLU A 115 -46.455 17.776 9.427 1.00 42.17 C ANISOU 588 CA GLU A 115 5341 5341 5341 0 0 0 C ATOM 589 C GLU A 115 -45.463 17.488 10.549 1.00 56.07 C ANISOU 589 C GLU A 115 7101 7101 7101 0 0 0 C ATOM 590 O GLU A 115 -44.286 17.856 10.453 1.00 15.83 O ANISOU 590 O GLU A 115 2005 2005 2005 0 0 0 O ATOM 591 CB GLU A 115 -47.511 18.780 9.914 1.00 42.91 C ANISOU 591 CB GLU A 115 5435 5433 5437 1 3 2 C ATOM 592 CG GLU A 115 -48.216 19.574 8.815 1.00 72.60 C ANISOU 592 CG GLU A 115 9196 9189 9200 2 7 3 C ATOM 593 CD GLU A 115 -49.398 20.388 9.341 1.00 88.13 C ANISOU 593 CD GLU A 115 11159 11135 11191 14 52 18 C ATOM 594 OE1 GLU A 115 -49.865 20.112 10.467 1.00 88.01 O ANISOU 594 OE1 GLU A 115 11149 11092 11197 23 72 32 O ATOM 595 OE2 GLU A 115 -49.862 21.304 8.628 1.00 89.77 O ANISOU 595 OE2 GLU A 115 11368 11337 11405 16 63 21 O ATOM 596 N LEU A 116 -45.924 16.815 11.606 1.00 76.21 N ANISOU 596 N LEU A 116 9652 9652 9652 0 0 0 N ATOM 597 CA LEU A 116 -45.033 16.571 12.747 1.00 48.34 C ANISOU 597 CA LEU A 116 6122 6122 6122 0 0 0 C ATOM 598 C LEU A 116 -43.713 15.944 12.328 1.00 29.49 C ANISOU 598 C LEU A 116 3735 3735 3735 0 0 0 C ATOM 599 O LEU A 116 -42.637 16.498 12.566 1.00 23.67 O ANISOU 599 O LEU A 116 2998 2998 2998 0 0 0 O ATOM 600 CB LEU A 116 -45.701 15.692 13.802 1.00 26.40 C ANISOU 600 CB LEU A 116 3343 3328 3360 10 23 15 C ATOM 601 CG LEU A 116 -46.439 16.507 14.865 1.00 44.04 C ANISOU 601 CG LEU A 116 5577 5543 5614 22 50 31 C ATOM 602 CD1 LEU A 116 -47.735 17.070 14.292 1.00 56.86 C ANISOU 602 CD1 LEU A 116 7200 7154 7252 27 67 40 C ATOM 603 CD2 LEU A 116 -46.701 15.683 16.119 1.00 28.71 C ANISOU 603 CD2 LEU A 116 3630 3585 3694 35 76 53 C ATOM 604 N TRP A 117 -43.818 14.795 11.677 1.00 34.27 N ANISOU 604 N TRP A 117 4340 4340 4340 0 0 0 N ATOM 605 CA TRP A 117 -42.676 14.066 11.140 1.00 55.14 C ANISOU 605 CA TRP A 117 6984 6984 6984 0 0 0 C ATOM 606 C TRP A 117 -41.734 14.922 10.287 1.00 45.11 C ANISOU 606 C TRP A 117 5713 5713 5713 0 0 0 C ATOM 607 O TRP A 117 -40.519 14.856 10.457 1.00 20.98 O ANISOU 607 O TRP A 117 2657 2657 2657 0 0 0 O ATOM 608 CB TRP A 117 -43.164 12.874 10.318 1.00 46.02 C ANISOU 608 CB TRP A 117 5829 5829 5829 0 0 0 C ATOM 609 CG TRP A 117 -42.070 12.053 9.713 1.00 36.00 C ANISOU 609 CG TRP A 117 4560 4560 4560 0 0 0 C ATOM 610 CD1 TRP A 117 -41.472 10.964 10.266 1.00 21.39 C ANISOU 610 CD1 TRP A 117 2709 2709 2709 0 0 0 C ATOM 611 CD2 TRP A 117 -41.452 12.245 8.429 1.00 58.26 C ANISOU 611 CD2 TRP A 117 7379 7379 7379 0 0 0 C ATOM 612 NE1 TRP A 117 -40.514 10.465 9.413 1.00 44.51 N ANISOU 612 NE1 TRP A 117 5637 5637 5637 0 0 0 N ATOM 613 CE2 TRP A 117 -40.482 11.232 8.277 1.00 54.28 C ANISOU 613 CE2 TRP A 117 6875 6875 6875 0 0 0 C ATOM 614 CE3 TRP A 117 -41.622 13.175 7.396 1.00 58.27 C ANISOU 614 CE3 TRP A 117 7380 7380 7380 0 0 0 C ATOM 615 CZ2 TRP A 117 -39.685 11.119 7.129 1.00 34.17 C ANISOU 615 CZ2 TRP A 117 4328 4328 4328 0 0 0 C ATOM 616 CZ3 TRP A 117 -40.829 13.061 6.255 1.00 44.98 C ANISOU 616 CZ3 TRP A 117 5697 5697 5697 0 0 0 C ATOM 617 CH2 TRP A 117 -39.875 12.039 6.133 1.00 30.62 C ANISOU 617 CH2 TRP A 117 3878 3878 3878 0 0 0 C ATOM 618 N THR A 118 -42.275 15.706 9.358 1.00 0.00 N ANISOU 618 N THR A 118 0 0 0 0 0 0 N ATOM 619 CA THR A 118 -41.405 16.553 8.544 1.00 60.37 C ANISOU 619 CA THR A 118 7646 7646 7646 0 0 0 C ATOM 620 C THR A 118 -40.668 17.606 9.388 1.00 75.40 C ANISOU 620 C THR A 118 9549 9549 9549 0 0 0 C ATOM 621 O THR A 118 -39.468 17.839 9.195 1.00101.92 O ANISOU 621 O THR A 118 12908 12908 12908 0 0 0 O ATOM 622 CB THR A 118 -42.153 17.245 7.384 1.00 53.76 C ANISOU 622 CB THR A 118 6809 6809 6809 0 0 0 C ATOM 623 OG1 THR A 118 -43.441 17.685 7.828 1.00 67.43 O ANISOU 623 OG1 THR A 118 8540 8540 8540 0 0 0 O ATOM 624 CG2 THR A 118 -42.321 16.300 6.206 1.00 23.25 C ANISOU 624 CG2 THR A 118 2945 2945 2945 0 0 0 C ATOM 625 N SER A 119 -41.377 18.236 10.323 1.00 41.50 N ANISOU 625 N SER A 119 5256 5256 5256 0 0 0 N ATOM 626 CA SER A 119 -40.783 19.307 11.123 1.00 12.86 C ANISOU 626 CA SER A 119 1629 1629 1629 0 0 0 C ATOM 627 C SER A 119 -39.729 18.796 12.093 1.00 44.60 C ANISOU 627 C SER A 119 5649 5649 5649 0 0 0 C ATOM 628 O SER A 119 -38.854 19.546 12.537 1.00 0.00 O ANISOU 628 O SER A 119 0 0 0 0 0 0 O ATOM 629 CB SER A 119 -41.867 20.038 11.881 1.00 11.84 C ANISOU 629 CB SER A 119 1499 1499 1499 0 0 0 C ATOM 630 OG SER A 119 -42.885 20.429 10.987 1.00 12.49 O ANISOU 630 OG SER A 119 1582 1582 1582 0 0 0 O ATOM 631 N LEU A 120 -39.845 17.514 12.431 1.00 52.23 N ANISOU 631 N LEU A 120 6615 6615 6615 0 0 0 N ATOM 632 CA LEU A 120 -38.826 16.814 13.207 1.00 28.26 C ANISOU 632 CA LEU A 120 3579 3579 3579 0 0 0 C ATOM 633 C LEU A 120 -37.645 16.381 12.333 1.00 0.00 C ANISOU 633 C LEU A 120 0 0 0 0 0 0 C ATOM 634 O LEU A 120 -36.492 16.512 12.743 1.00 20.88 O ANISOU 634 O LEU A 120 2645 2645 2645 0 0 0 O ATOM 635 CB LEU A 120 -39.448 15.629 13.934 1.00 4.53 C ANISOU 635 CB LEU A 120 574 574 574 0 0 0 C ATOM 636 CG LEU A 120 -40.570 16.042 14.896 1.00 22.40 C ANISOU 636 CG LEU A 120 2837 2837 2837 0 0 0 C ATOM 637 CD1 LEU A 120 -41.636 14.960 15.008 1.00 53.22 C ANISOU 637 CD1 LEU A 120 6740 6740 6740 0 0 0 C ATOM 638 CD2 LEU A 120 -40.026 16.413 16.263 1.00 0.00 C ANISOU 638 CD2 LEU A 120 0 0 0 0 0 0 C ATOM 639 N ASP A 121 -37.937 15.893 11.127 1.00 0.00 N ANISOU 639 N ASP A 121 0 0 0 0 0 0 N ATOM 640 CA ASP A 121 -36.916 15.676 10.090 1.00 60.13 C ANISOU 640 CA ASP A 121 7616 7616 7616 0 0 0 C ATOM 641 C ASP A 121 -36.046 16.900 9.839 1.00 45.00 C ANISOU 641 C ASP A 121 5699 5699 5699 0 0 0 C ATOM 642 O ASP A 121 -34.873 16.766 9.511 1.00 24.41 O ANISOU 642 O ASP A 121 3091 3091 3091 0 0 0 O ATOM 643 CB ASP A 121 -37.538 15.249 8.751 1.00 63.74 C ANISOU 643 CB ASP A 121 8073 8073 8073 0 0 0 C ATOM 644 CG ASP A 121 -36.535 15.311 7.583 1.00 60.98 C ANISOU 644 CG ASP A 121 7723 7723 7723 0 0 0 C ATOM 645 OD1 ASP A 121 -35.360 14.950 7.784 1.00 0.00 O ANISOU 645 OD1 ASP A 121 0 0 0 0 0 0 O ATOM 646 OD2 ASP A 121 -36.916 15.716 6.461 1.00 26.58 O ANISOU 646 OD2 ASP A 121 3367 3367 3367 0 0 0 O ATOM 647 N VAL A 122 -36.626 18.090 9.911 1.00 0.00 N ANISOU 647 N VAL A 122 0 0 0 0 0 0 N ATOM 648 CA VAL A 122 -35.821 19.305 9.810 1.00 14.50 C ANISOU 648 CA VAL A 122 1836 1836 1836 0 0 0 C ATOM 649 C VAL A 122 -35.179 19.754 11.141 1.00 50.81 C ANISOU 649 C VAL A 122 6435 6435 6435 0 0 0 C ATOM 650 O VAL A 122 -34.006 20.182 11.184 1.00 0.00 O ANISOU 650 O VAL A 122 0 0 0 0 0 0 O ATOM 651 CB VAL A 122 -36.638 20.429 9.223 1.00 1.25 C ANISOU 651 CB VAL A 122 158 158 158 0 0 0 C ATOM 652 CG1 VAL A 122 -35.715 21.543 8.775 1.00 0.00 C ANISOU 652 CG1 VAL A 122 0 0 0 0 0 0 C ATOM 653 CG2 VAL A 122 -37.465 19.897 8.071 1.00 0.00 C ANISOU 653 CG2 VAL A 122 0 0 0 0 0 0 C ATOM 654 N LEU A 123 -35.958 19.667 12.219 1.00 37.96 N ANISOU 654 N LEU A 123 4808 4808 4808 0 0 0 N ATOM 655 CA LEU A 123 -35.476 20.067 13.538 1.00 27.61 C ANISOU 655 CA LEU A 123 3497 3497 3497 0 0 0 C ATOM 656 C LEU A 123 -34.171 19.371 13.892 1.00 22.36 C ANISOU 656 C LEU A 123 2832 2832 2832 0 0 0 C ATOM 657 O LEU A 123 -33.209 20.019 14.302 1.00 24.56 O ANISOU 657 O LEU A 123 3111 3111 3111 0 0 0 O ATOM 658 CB LEU A 123 -36.503 19.792 14.636 1.00 0.51 C ANISOU 658 CB LEU A 123 64 64 64 0 0 0 C ATOM 659 CG LEU A 123 -35.796 19.867 15.994 1.00 15.19 C ANISOU 659 CG LEU A 123 1924 1924 1924 0 0 0 C ATOM 660 CD1 LEU A 123 -35.169 21.219 16.123 1.00 0.00 C ANISOU 660 CD1 LEU A 123 0 0 0 0 0 0 C ATOM 661 CD2 LEU A 123 -36.715 19.609 17.165 1.00 6.17 C ANISOU 661 CD2 LEU A 123 782 782 782 0 0 0 C ATOM 662 N CYS A 124 -34.141 18.050 13.741 1.00 27.20 N ANISOU 662 N CYS A 124 3445 3445 3445 0 0 0 N ATOM 663 CA CYS A 124 -32.926 17.298 14.038 1.00 47.60 C ANISOU 663 CA CYS A 124 6028 6028 6028 0 0 0 C ATOM 664 C CYS A 124 -31.747 17.902 13.289 1.00 50.47 C ANISOU 664 C CYS A 124 6392 6392 6392 0 0 0 C ATOM 665 O CYS A 124 -30.608 17.888 13.779 1.00 75.94 O ANISOU 665 O CYS A 124 9618 9618 9618 0 0 0 O ATOM 666 CB CYS A 124 -33.091 15.828 13.661 1.00 60.71 C ANISOU 666 CB CYS A 124 7689 7689 7689 0 0 0 C ATOM 667 SG CYS A 124 -33.923 14.800 14.909 1.00 27.97 S ANISOU 667 SG CYS A 124 3542 3542 3542 0 0 0 S ATOM 668 N VAL A 125 -32.040 18.471 12.119 1.00 11.06 N ANISOU 668 N VAL A 125 1401 1401 1401 0 0 0 N ATOM 669 CA VAL A 125 -31.011 19.078 11.282 1.00 27.45 C ANISOU 669 CA VAL A 125 3477 3477 3477 0 0 0 C ATOM 670 C VAL A 125 -30.537 20.401 11.860 1.00 31.38 C ANISOU 670 C VAL A 125 3974 3974 3974 0 0 0 C ATOM 671 O VAL A 125 -29.347 20.548 12.165 1.00 22.94 O ANISOU 671 O VAL A 125 2906 2906 2906 0 0 0 O ATOM 672 CB VAL A 125 -31.449 19.253 9.813 1.00 16.72 C ANISOU 672 CB VAL A 125 2118 2118 2118 0 0 0 C ATOM 673 CG1 VAL A 125 -30.280 19.735 8.953 1.00 0.00 C ANISOU 673 CG1 VAL A 125 0 0 0 0 0 0 C ATOM 674 CG2 VAL A 125 -31.960 17.944 9.278 1.00 45.96 C ANISOU 674 CG2 VAL A 125 5821 5821 5821 0 0 0 C ATOM 675 N THR A 126 -31.441 21.370 11.999 1.00 0.00 N ANISOU 675 N THR A 126 0 0 0 0 0 0 N ATOM 676 CA THR A 126 -31.015 22.677 12.517 1.00 44.76 C ANISOU 676 CA THR A 126 5669 5669 5669 0 0 0 C ATOM 677 C THR A 126 -30.328 22.542 13.877 1.00 48.30 C ANISOU 677 C THR A 126 6117 6117 6117 0 0 0 C ATOM 678 O THR A 126 -29.431 23.320 14.207 1.00 18.93 O ANISOU 678 O THR A 126 2398 2398 2398 0 0 0 O ATOM 679 CB THR A 126 -32.160 23.704 12.605 1.00 16.01 C ANISOU 679 CB THR A 126 2028 2028 2028 0 0 0 C ATOM 680 OG1 THR A 126 -33.011 23.576 11.464 1.00 46.25 O ANISOU 680 OG1 THR A 126 5858 5858 5858 0 0 0 O ATOM 681 CG2 THR A 126 -31.604 25.102 12.629 1.00 0.00 C ANISOU 681 CG2 THR A 126 0 0 0 0 0 0 C ATOM 682 N ALA A 127 -30.748 21.541 14.651 1.00 65.52 N ANISOU 682 N ALA A 127 8298 8298 8298 0 0 0 N ATOM 683 CA ALA A 127 -30.105 21.216 15.924 1.00 44.03 C ANISOU 683 CA ALA A 127 5577 5577 5577 0 0 0 C ATOM 684 C ALA A 127 -28.688 20.708 15.686 1.00 30.37 C ANISOU 684 C ALA A 127 3846 3846 3846 0 0 0 C ATOM 685 O ALA A 127 -27.757 21.128 16.372 1.00 5.37 O ANISOU 685 O ALA A 127 680 680 680 0 0 0 O ATOM 686 CB ALA A 127 -30.912 20.189 16.691 1.00 31.27 C ANISOU 686 CB ALA A 127 3961 3961 3961 0 0 0 C ATOM 687 N SER A 128 -28.540 19.793 14.727 1.00 50.03 N ANISOU 687 N SER A 128 6337 6337 6337 0 0 0 N ATOM 688 CA SER A 128 -27.224 19.276 14.342 1.00 44.70 C ANISOU 688 CA SER A 128 5661 5661 5661 0 0 0 C ATOM 689 C SER A 128 -26.241 20.346 13.875 1.00 40.35 C ANISOU 689 C SER A 128 5111 5111 5111 0 0 0 C ATOM 690 O SER A 128 -25.209 20.574 14.517 1.00 32.68 O ANISOU 690 O SER A 128 4139 4139 4139 0 0 0 O ATOM 691 CB SER A 128 -27.346 18.174 13.291 1.00 9.50 C ANISOU 691 CB SER A 128 1203 1203 1203 0 0 0 C ATOM 692 OG SER A 128 -27.621 16.925 13.906 1.00 21.91 O ANISOU 692 OG SER A 128 2775 2775 2775 0 0 0 O ATOM 693 N ILE A 129 -26.539 20.997 12.758 1.00 0.00 N ANISOU 693 N ILE A 129 0 0 0 0 0 0 N ATOM 694 CA ILE A 129 -25.653 22.061 12.310 1.00 58.44 C ANISOU 694 CA ILE A 129 7401 7401 7401 0 0 0 C ATOM 695 C ILE A 129 -25.452 23.102 13.420 1.00 62.86 C ANISOU 695 C ILE A 129 7961 7961 7961 0 0 0 C ATOM 696 O ILE A 129 -24.323 23.342 13.838 1.00 0.00 O ANISOU 696 O ILE A 129 0 0 0 0 0 0 O ATOM 697 CB ILE A 129 -26.135 22.737 10.995 1.00 44.55 C ANISOU 697 CB ILE A 129 5642 5642 5642 0 0 0 C ATOM 698 CG1 ILE A 129 -25.130 23.807 10.519 1.00 44.30 C ANISOU 698 CG1 ILE A 129 5611 5611 5611 0 0 0 C ATOM 699 CG2 ILE A 129 -27.513 23.335 11.179 1.00 23.06 C ANISOU 699 CG2 ILE A 129 2920 2920 2920 0 0 0 C ATOM 700 CD1 ILE A 129 -23.935 23.271 9.715 1.00 0.00 C ANISOU 700 CD1 ILE A 129 0 0 0 0 0 0 C ATOM 701 N GLU A 130 -26.534 23.684 13.931 1.00 49.25 N ANISOU 701 N GLU A 130 6237 6237 6237 0 0 0 N ATOM 702 CA GLU A 130 -26.392 24.799 14.872 1.00 51.34 C ANISOU 702 CA GLU A 130 6502 6502 6502 0 0 0 C ATOM 703 C GLU A 130 -25.589 24.456 16.132 1.00 50.11 C ANISOU 703 C GLU A 130 6355 6349 6337 -32 18 -17 C ATOM 704 O GLU A 130 -24.696 25.211 16.520 1.00 21.50 O ANISOU 704 O GLU A 130 2752 2756 2662 -103 60 -62 O ATOM 705 CB GLU A 130 -27.747 25.433 15.208 1.00 27.51 C ANISOU 705 CB GLU A 130 3489 3480 3482 -9 9 -5 C ATOM 706 CG GLU A 130 -27.986 26.766 14.492 1.00 33.60 C ANISOU 706 CG GLU A 130 4285 4240 4240 -40 51 -30 C ATOM 707 CD GLU A 130 -29.459 27.095 14.332 1.00 63.04 C ANISOU 707 CD GLU A 130 8013 7965 7975 -31 51 -25 C ATOM 708 OE1 GLU A 130 -30.283 26.231 14.683 1.00 63.66 O ANISOU 708 OE1 GLU A 130 8069 8055 8062 -7 11 -5 O ATOM 709 OE2 GLU A 130 -29.797 28.208 13.861 1.00 1.23 O ANISOU 709 OE2 GLU A 130 208 106 154 -64 84 -41 O ATOM 710 N THR A 131 -25.899 23.325 16.759 1.00 46.96 N ANISOU 710 N THR A 131 5948 5948 5948 0 0 0 N ATOM 711 CA THR A 131 -25.067 22.801 17.837 1.00 29.79 C ANISOU 711 CA THR A 131 3772 3789 3758 -31 10 -13 C ATOM 712 C THR A 131 -23.608 22.711 17.393 1.00 44.81 C ANISOU 712 C THR A 131 5673 5730 5624 -65 18 -28 C ATOM 713 O THR A 131 -22.706 23.143 18.114 1.00 62.69 O ANISOU 713 O THR A 131 7899 8074 7845 -163 32 -53 O ATOM 714 CB THR A 131 -25.544 21.418 18.272 1.00 22.10 C ANISOU 714 CB THR A 131 2799 2799 2799 0 0 0 C ATOM 715 OG1 THR A 131 -26.564 21.572 19.259 1.00 41.90 O ANISOU 715 OG1 THR A 131 5307 5307 5307 0 0 0 O ATOM 716 CG2 THR A 131 -24.403 20.621 18.853 1.00 0.39 C ANISOU 716 CG2 THR A 131 39 87 24 -23 1 -2 C ATOM 717 N LEU A 132 -23.375 22.159 16.204 1.00 36.41 N ANISOU 717 N LEU A 132 4610 4616 4608 -7 2 -2 N ATOM 718 CA LEU A 132 -22.024 22.069 15.680 1.00 0.57 C ANISOU 718 CA LEU A 132 60 110 46 -44 8 -13 C ATOM 719 C LEU A 132 -21.355 23.431 15.682 1.00 34.55 C ANISOU 719 C LEU A 132 4370 4479 4279 -122 34 -53 C ATOM 720 O LEU A 132 -20.274 23.602 16.255 1.00 74.32 O ANISOU 720 O LEU A 132 9384 9609 9245 -195 44 -76 O ATOM 721 CB LEU A 132 -22.035 21.509 14.270 1.00 2.20 C ANISOU 721 CB LEU A 132 278 278 278 0 0 0 C ATOM 722 CG LEU A 132 -22.167 19.994 14.136 1.00 44.59 C ANISOU 722 CG LEU A 132 5648 5648 5648 0 0 0 C ATOM 723 CD1 LEU A 132 -22.357 19.599 12.682 1.00 78.92 C ANISOU 723 CD1 LEU A 132 9995 9995 9995 0 0 0 C ATOM 724 CD2 LEU A 132 -20.947 19.308 14.702 1.00 15.02 C ANISOU 724 CD2 LEU A 132 1902 1902 1902 0 0 0 C ATOM 725 N CYS A 133 -22.000 24.403 15.044 1.00 1.73 N ANISOU 725 N CYS A 133 217 279 162 -126 42 -54 N ATOM 726 CA CYS A 133 -21.440 25.746 14.932 1.00 30.11 C ANISOU 726 CA CYS A 133 3838 3918 3683 -193 85 -104 C ATOM 727 C CYS A 133 -21.137 26.306 16.301 1.00 49.98 C ANISOU 727 C CYS A 133 6334 6550 6106 -387 140 -184 C ATOM 728 O CYS A 133 -20.174 27.051 16.466 1.00 25.47 O ANISOU 728 O CYS A 133 3195 3448 3036 -401 126 -172 O ATOM 729 CB CYS A 133 -22.389 26.687 14.197 1.00 7.25 C ANISOU 729 CB CYS A 133 948 962 846 -195 92 -95 C ATOM 730 SG CYS A 133 -22.988 26.038 12.625 1.00140.18 S ANISOU 730 SG CYS A 133 17778 17759 17726 -86 49 -44 S ATOM 731 N VAL A 134 -21.962 25.956 17.284 1.00 66.43 N ANISOU 731 N VAL A 134 8431 8588 8222 -270 105 -139 N ATOM 732 CA VAL A 134 -21.629 26.301 18.658 1.00 46.01 C ANISOU 732 CA VAL A 134 5830 6089 5563 -355 122 -175 C ATOM 733 C VAL A 134 -20.288 25.643 19.042 1.00 26.97 C ANISOU 733 C VAL A 134 3310 3765 3171 -432 94 -156 C ATOM 734 O VAL A 134 -19.444 26.288 19.662 1.00 15.58 O ANISOU 734 O VAL A 134 1908 2445 1568 -482 122 -208 O ATOM 735 CB VAL A 134 -22.739 25.929 19.673 1.00 46.13 C ANISOU 735 CB VAL A 134 5846 6089 5593 -335 115 -164 C ATOM 736 CG1 VAL A 134 -22.687 26.861 20.859 1.00 5.90 C ANISOU 736 CG1 VAL A 134 692 1039 511 -476 138 -197 C ATOM 737 CG2 VAL A 134 -24.101 26.014 19.037 1.00 15.37 C ANISOU 737 CG2 VAL A 134 1979 2088 1773 -258 114 -140 C ATOM 738 N ILE A 135 -20.072 24.379 18.664 1.00 34.26 N ANISOU 738 N ILE A 135 4219 4682 4117 -359 61 -112 N ATOM 739 CA ILE A 135 -18.799 23.730 19.008 1.00 5.63 C ANISOU 739 CA ILE A 135 595 1189 356 -357 50 -107 C ATOM 740 C ILE A 135 -17.631 24.502 18.426 1.00 46.53 C ANISOU 740 C ILE A 135 5689 6405 5585 -455 62 -128 C ATOM 741 O ILE A 135 -16.697 24.850 19.144 1.00 47.27 O ANISOU 741 O ILE A 135 5724 6625 5612 -538 69 -148 O ATOM 742 CB ILE A 135 -18.656 22.287 18.497 1.00 4.82 C ANISOU 742 CB ILE A 135 477 1058 297 -277 21 -52 C ATOM 743 CG1 ILE A 135 -19.863 21.432 18.845 1.00 35.38 C ANISOU 743 CG1 ILE A 135 4311 4846 4285 -230 7 -19 C ATOM 744 CG2 ILE A 135 -17.439 21.664 19.109 1.00 6.00 C ANISOU 744 CG2 ILE A 135 561 1353 365 -307 9 -26 C ATOM 745 CD1 ILE A 135 -19.553 19.954 18.868 1.00 3.77 C ANISOU 745 CD1 ILE A 135 331 871 231 -161 -8 30 C ATOM 746 N ALA A 136 -17.688 24.758 17.119 1.00 42.31 N ANISOU 746 N ALA A 136 5269 5797 5010 -379 74 -142 N ATOM 747 CA ALA A 136 -16.584 25.408 16.407 1.00 36.05 C ANISOU 747 CA ALA A 136 4396 5028 4273 -469 83 -156 C ATOM 748 C ALA A 136 -16.384 26.852 16.850 1.00 55.99 C ANISOU 748 C ALA A 136 7008 7618 6646 -522 132 -230 C ATOM 749 O ALA A 136 -15.290 27.401 16.720 1.00 52.66 O ANISOU 749 O ALA A 136 6567 7277 6165 -588 148 -261 O ATOM 750 CB ALA A 136 -16.796 25.334 14.909 1.00 5.27 C ANISOU 750 CB ALA A 136 546 1025 431 -399 80 -141 C ATOM 751 N ILE A 137 -17.445 27.462 17.372 1.00 58.22 N ANISOU 751 N ILE A 137 7242 7825 7055 -583 140 -227 N ATOM 752 CA ILE A 137 -17.353 28.798 17.948 1.00 49.56 C ANISOU 752 CA ILE A 137 6149 6763 5919 -687 183 -283 C ATOM 753 C ILE A 137 -16.791 28.734 19.371 1.00 79.75 C ANISOU 753 C ILE A 137 10017 10756 9530 -699 199 -330 C ATOM 754 O ILE A 137 -16.287 29.728 19.885 1.00112.12 O ANISOU 754 O ILE A 137 14113 14927 13561 -793 235 -385 O ATOM 755 CB ILE A 137 -18.723 29.496 17.984 1.00 8.27 C ANISOU 755 CB ILE A 137 980 1434 730 -666 210 -293 C ATOM 756 CG1 ILE A 137 -18.580 30.987 17.686 1.00 9.20 C ANISOU 756 CG1 ILE A 137 1211 1580 704 -671 286 -375 C ATOM 757 CG2 ILE A 137 -19.387 29.295 19.332 1.00 10.07 C ANISOU 757 CG2 ILE A 137 1278 1728 822 -620 227 -324 C ATOM 758 CD1 ILE A 137 -19.913 31.737 17.630 1.00 26.57 C ANISOU 758 CD1 ILE A 137 3383 3643 3071 -723 293 -350 C ATOM 759 N ASP A 138 -16.877 27.562 20.001 1.00 62.87 N ANISOU 759 N ASP A 138 7840 8658 7389 -659 158 -285 N ATOM 760 CA ASP A 138 -16.325 27.354 21.340 1.00 50.32 C ANISOU 760 CA ASP A 138 6194 7214 5710 -721 150 -290 C ATOM 761 C ASP A 138 -14.811 27.190 21.290 1.00 57.05 C ANISOU 761 C ASP A 138 6842 8169 6664 -838 129 -266 C ATOM 762 O ASP A 138 -14.073 27.750 22.104 1.00 47.98 O ANISOU 762 O ASP A 138 5804 7180 5245 -855 157 -328 O ATOM 763 CB ASP A 138 -16.937 26.106 21.990 1.00 61.13 C ANISOU 763 CB ASP A 138 7537 8588 7102 -656 111 -231 C ATOM 764 CG ASP A 138 -16.111 25.591 23.172 1.00 88.45 C ANISOU 764 CG ASP A 138 10773 12195 10638 -765 84 -194 C ATOM 765 OD1 ASP A 138 -15.804 26.394 24.077 1.00110.51 O ANISOU 765 OD1 ASP A 138 13696 15112 13179 -793 115 -258 O ATOM 766 OD2 ASP A 138 -15.761 24.388 23.198 1.00 74.99 O ANISOU 766 OD2 ASP A 138 9171 10561 8759 -642 58 -147 O ATOM 767 N ARG A 139 -14.355 26.429 20.305 1.00 56.22 N ANISOU 767 N ARG A 139 6736 8038 6586 -767 106 -229 N ATOM 768 CA ARG A 139 -12.974 25.983 20.254 1.00 38.96 C ANISOU 768 CA ARG A 139 4473 5983 4348 -788 92 -214 C ATOM 769 C ARG A 139 -12.035 27.036 19.663 1.00 40.44 C ANISOU 769 C ARG A 139 4658 6204 4505 -868 119 -265 C ATOM 770 O ARG A 139 -10.852 26.780 19.466 1.00 60.00 O ANISOU 770 O ARG A 139 7250 8814 6735 -812 120 -282 O ATOM 771 CB ARG A 139 -12.870 24.649 19.510 1.00 52.07 C ANISOU 771 CB ARG A 139 6130 7608 6048 -679 60 -153 C ATOM 772 CG ARG A 139 -13.247 23.420 20.347 1.00 10.93 C ANISOU 772 CG ARG A 139 1028 2455 671 -566 36 -103 C ATOM 773 CD ARG A 139 -12.280 23.253 21.504 1.00 57.06 C ANISOU 773 CD ARG A 139 6617 8472 6591 -677 27 -84 C ATOM 774 NE ARG A 139 -11.962 21.855 21.783 1.00 99.87 N ANISOU 774 NE ARG A 139 12159 13975 11811 -552 3 -12 N ATOM 775 CZ ARG A 139 -10.912 21.450 22.499 1.00111.41 C ANISOU 775 CZ ARG A 139 13340 15596 13393 -627 -4 17 C ATOM 776 NH1 ARG A 139 -10.061 22.337 23.007 1.00 67.54 N ANISOU 776 NH1 ARG A 139 7950 10184 7529 -669 8 -29 N ATOM 777 NH2 ARG A 139 -10.706 20.154 22.704 1.00125.67 N ANISOU 777 NH2 ARG A 139 15099 17451 15197 -548 -20 89 N ATOM 778 N TYR A 140 -12.562 28.212 19.348 1.00 37.56 N ANISOU 778 N TYR A 140 4515 5786 3971 -832 169 -342 N ATOM 779 CA TYR A 140 -11.694 29.369 19.196 1.00 46.88 C ANISOU 779 CA TYR A 140 5526 6989 5296 -1016 190 -371 C ATOM 780 C TYR A 140 -11.386 29.875 20.604 1.00 82.54 C ANISOU 780 C TYR A 140 10174 11678 9509 -1021 225 -446 C ATOM 781 O TYR A 140 -10.356 30.511 20.834 1.00109.24 O ANISOU 781 O TYR A 140 13525 15174 12809 -1107 246 -490 O ATOM 782 CB TYR A 140 -12.353 30.461 18.354 1.00 62.09 C ANISOU 782 CB TYR A 140 7541 8781 7271 -1024 229 -406 C ATOM 783 CG TYR A 140 -11.535 31.735 18.231 1.00107.58 C ANISOU 783 CG TYR A 140 13296 14594 12987 -1137 272 -469 C ATOM 784 CD1 TYR A 140 -11.555 32.701 19.236 1.00137.62 C ANISOU 784 CD1 TYR A 140 17270 18508 16510 -1128 338 -571 C ATOM 785 CD2 TYR A 140 -10.755 31.983 17.105 1.00105.65 C ANISOU 785 CD2 TYR A 140 13056 14342 12745 -1141 278 -475 C ATOM 786 CE1 TYR A 140 -10.812 33.875 19.131 1.00138.53 C ANISOU 786 CE1 TYR A 140 17201 18614 16820 -1350 354 -585 C ATOM 787 CE2 TYR A 140 -10.009 33.159 16.990 1.00121.91 C ANISOU 787 CE2 TYR A 140 15290 16504 14528 -1132 349 -583 C ATOM 788 CZ TYR A 140 -10.042 34.101 18.008 1.00127.92 C ANISOU 788 CZ TYR A 140 15863 17262 15480 -1352 359 -589 C ATOM 789 OH TYR A 140 -9.311 35.269 17.911 1.00112.73 O ANISOU 789 OH TYR A 140 13935 15383 13514 -1461 404 -651 O ATOM 790 N LEU A 141 -12.280 29.568 21.544 1.00111.12 N ANISOU 790 N LEU A 141 14077 16320 11824 -773 -1703 -1195 N ATOM 791 CA LEU A 141 -12.118 29.968 22.945 1.00115.81 C ANISOU 791 CA LEU A 141 14660 16937 12405 -774 -1701 -1195 C ATOM 792 C LEU A 141 -11.287 28.966 23.738 1.00112.71 C ANISOU 792 C LEU A 141 14243 16572 12009 -762 -1715 -1197 C ATOM 793 O LEU A 141 -10.948 29.202 24.900 1.00116.89 O ANISOU 793 O LEU A 141 14759 17127 12528 -763 -1713 -1200 O ATOM 794 CB LEU A 141 -13.476 30.153 23.622 1.00118.58 C ANISOU 794 CB LEU A 141 15032 17264 12759 -765 -1707 -1173 C ATOM 795 CG LEU A 141 -14.254 31.418 23.262 1.00117.04 C ANISOU 795 CG LEU A 141 14858 17050 12560 -779 -1691 -1172 C ATOM 796 CD1 LEU A 141 -14.551 31.466 21.769 1.00 68.29 C ANISOU 796 CD1 LEU A 141 8700 10851 6397 -782 -1686 -1174 C ATOM 797 CD2 LEU A 141 -15.535 31.515 24.086 1.00130.73 C ANISOU 797 CD2 LEU A 141 16610 18764 14296 -768 -1698 -1151 C ATOM 798 N ALA A 142 -10.985 27.837 23.111 1.00 95.75 N ANISOU 798 N ALA A 142 12089 14419 9871 -751 -1727 -1196 N ATOM 799 CA ALA A 142 -10.053 26.878 23.681 1.00101.08 C ANISOU 799 CA ALA A 142 12739 15122 10543 -740 -1739 -1200 C ATOM 800 C ALA A 142 -8.667 27.137 23.114 1.00 93.80 C ANISOU 800 C ALA A 142 11796 14230 9615 -753 -1726 -1226 C ATOM 801 O ALA A 142 -7.735 26.379 23.375 1.00 96.09 O ANISOU 801 O ALA A 142 12063 14545 9901 -746 -1734 -1234 O ATOM 802 CB ALA A 142 -10.488 25.466 23.372 1.00111.64 C ANISOU 802 CB ALA A 142 14085 16440 11895 -720 -1760 -1184 C ATOM 803 N ILE A 143 -8.550 28.199 22.316 1.00 83.94 N ANISOU 803 N ILE A 143 10553 12977 8363 -773 -1707 -1239 N ATOM 804 CA ILE A 143 -7.294 28.542 21.645 1.00 81.86 C ANISOU 804 CA ILE A 143 10270 12738 8094 -788 -1694 -1264 C ATOM 805 C ILE A 143 -6.762 29.952 21.932 1.00 61.60 C ANISOU 805 C ILE A 143 7697 10196 5514 -811 -1671 -1282 C ATOM 806 O ILE A 143 -5.775 30.098 22.646 1.00 67.86 O ANISOU 806 O ILE A 143 8464 11025 6293 -816 -1665 -1297 O ATOM 807 CB ILE A 143 -7.385 28.334 20.122 1.00 75.63 C ANISOU 807 CB ILE A 143 9493 11926 7317 -790 -1692 -1266 C ATOM 808 CG1 ILE A 143 -7.445 26.842 19.796 1.00 53.87 C ANISOU 808 CG1 ILE A 143 6735 9158 4574 -770 -1713 -1255 C ATOM 809 CG2 ILE A 143 -6.190 28.965 19.430 1.00 69.31 C ANISOU 809 CG2 ILE A 143 8675 11149 6509 -810 -1674 -1293 C ATOM 810 CD1 ILE A 143 -6.209 26.078 20.206 1.00 46.86 C ANISOU 810 CD1 ILE A 143 5818 8306 3680 -763 -1719 -1267 C ATOM 811 N THR A 144 -7.391 30.984 21.374 1.00 54.00 N ANISOU 811 N THR A 144 6754 9212 4551 -825 -1656 -1282 N ATOM 812 CA THR A 144 -6.899 32.347 21.580 1.00105.40 C ANISOU 812 CA THR A 144 13258 15743 11047 -848 -1634 -1300 C ATOM 813 C THR A 144 -7.350 32.869 22.933 1.00134.05 C ANISOU 813 C THR A 144 16888 19380 14666 -848 -1633 -1292 C ATOM 814 O THR A 144 -6.853 33.887 23.421 1.00140.95 O ANISOU 814 O THR A 144 17751 20277 15525 -866 -1616 -1306 O ATOM 815 CB THR A 144 -7.367 33.316 20.478 1.00120.06 C ANISOU 815 CB THR A 144 15136 17574 12906 -864 -1617 -1303 C ATOM 816 OG1 THR A 144 -6.958 32.817 19.201 1.00148.40 O ANISOU 816 OG1 THR A 144 18724 21156 16505 -864 -1618 -1310 O ATOM 817 CG2 THR A 144 -6.765 34.707 20.686 1.00110.38 C ANISOU 817 CG2 THR A 144 13903 16372 11665 -889 -1593 -1323 C ATOM 818 N SER A 145 -8.295 32.158 23.537 1.00142.67 N ANISOU 818 N SER A 145 17991 20453 15765 -828 -1651 -1269 N ATOM 819 CA SER A 145 -8.809 32.543 24.842 1.00138.04 C ANISOU 819 CA SER A 145 17407 19872 15170 -826 -1652 -1259 C ATOM 820 C SER A 145 -8.895 31.348 25.784 1.00118.89 C ANISOU 820 C SER A 145 14972 17454 12748 -803 -1674 -1245 C ATOM 821 O SER A 145 -9.952 31.083 26.363 1.00 96.54 O ANISOU 821 O SER A 145 12157 14602 9921 -791 -1685 -1224 O ATOM 822 CB SER A 145 -10.202 33.138 24.661 1.00135.15 C ANISOU 822 CB SER A 145 17072 19469 14809 -826 -1650 -1242 C ATOM 823 OG SER A 145 -10.155 34.271 23.806 1.00141.59 O ANISOU 823 OG SER A 145 17898 20278 15621 -847 -1630 -1254 O ATOM 824 N PRO A 146 -7.773 30.645 25.976 1.00117.53 N ANISOU 824 N PRO A 146 14773 17311 12571 -799 -1679 -1257 N ATOM 825 CA PRO A 146 -7.815 29.455 26.822 1.00111.29 C ANISOU 825 CA PRO A 146 13974 16528 11784 -776 -1700 -1244 C ATOM 826 C PRO A 146 -7.918 29.823 28.290 1.00131.43 C ANISOU 826 C PRO A 146 16518 19098 14323 -775 -1700 -1240 C ATOM 827 O PRO A 146 -8.539 29.104 29.068 1.00147.32 O ANISOU 827 O PRO A 146 18535 21102 16339 -757 -1717 -1221 O ATOM 828 CB PRO A 146 -6.456 28.785 26.552 1.00112.83 C ANISOU 828 CB PRO A 146 14141 16753 11976 -775 -1702 -1262 C ATOM 829 CG PRO A 146 -5.625 29.808 25.780 1.00120.51 C ANISOU 829 CG PRO A 146 15105 17742 12941 -799 -1680 -1286 C ATOM 830 CD PRO A 146 -6.394 31.093 25.740 1.00122.47 C ANISOU 830 CD PRO A 146 15373 17973 13186 -815 -1664 -1284 C ATOM 831 N PHE A 147 -7.338 30.963 28.645 1.00134.35 N ANISOU 831 N PHE A 147 16875 19493 14678 -795 -1681 -1257 N ATOM 832 CA PHE A 147 -7.192 31.360 30.039 1.00129.08 C ANISOU 832 CA PHE A 147 16196 18852 13998 -796 -1679 -1258 C ATOM 833 C PHE A 147 -8.538 31.384 30.745 1.00129.19 C ANISOU 833 C PHE A 147 16233 18838 14016 -786 -1688 -1233 C ATOM 834 O PHE A 147 -8.648 31.040 31.921 1.00143.06 O ANISOU 834 O PHE A 147 17981 20607 15767 -774 -1698 -1225 O ATOM 835 CB PHE A 147 -6.520 32.728 30.105 1.00115.62 C ANISOU 835 CB PHE A 147 14480 17171 12278 -822 -1654 -1280 C ATOM 836 CG PHE A 147 -5.360 32.860 29.167 1.00117.81 C ANISOU 836 CG PHE A 147 14740 17468 12553 -835 -1642 -1304 C ATOM 837 CD1 PHE A 147 -4.156 32.234 29.448 1.00130.21 C ANISOU 837 CD1 PHE A 147 16280 19075 14118 -830 -1646 -1318 C ATOM 838 CD2 PHE A 147 -5.479 33.583 27.992 1.00101.54 C ANISOU 838 CD2 PHE A 147 12695 15389 10497 -852 -1628 -1311 C ATOM 839 CE1 PHE A 147 -3.086 32.336 28.584 1.00126.84 C ANISOU 839 CE1 PHE A 147 15838 18668 13689 -842 -1635 -1340 C ATOM 840 CE2 PHE A 147 -4.413 33.691 27.122 1.00112.13 C ANISOU 840 CE2 PHE A 147 14021 16749 11836 -864 -1617 -1333 C ATOM 841 CZ PHE A 147 -3.212 33.066 27.419 1.00120.78 C ANISOU 841 CZ PHE A 147 15085 17881 12926 -859 -1620 -1348 C ATOM 842 N ARG A 148 -9.564 31.774 30.003 1.00107.54 N ANISOU 842 N ARG A 148 13519 16059 11284 -789 -1685 -1222 N ATOM 843 CA ARG A 148 -10.903 31.944 30.550 1.00 96.21 C ANISOU 843 CA ARG A 148 12107 14596 9853 -781 -1691 -1200 C ATOM 844 C ARG A 148 -11.812 30.733 30.390 1.00 83.19 C ANISOU 844 C ARG A 148 10474 12916 8219 -758 -1714 -1177 C ATOM 845 O ARG A 148 -13.015 30.818 30.628 1.00 67.59 O ANISOU 845 O ARG A 148 8520 10913 6249 -751 -1719 -1159 O ATOM 846 CB ARG A 148 -11.568 33.153 29.928 1.00114.02 C ANISOU 846 CB ARG A 148 14384 16829 12108 -798 -1675 -1201 C ATOM 847 CG ARG A 148 -12.874 33.505 30.577 1.00147.88 C ANISOU 847 CG ARG A 148 18696 21094 16399 -792 -1678 -1181 C ATOM 848 CD ARG A 148 -12.850 34.911 31.100 1.00177.81 C ANISOU 848 CD ARG A 148 22486 24897 20175 -812 -1658 -1190 C ATOM 849 NE ARG A 148 -13.696 35.790 30.300 1.00209.31 N ANISOU 849 NE ARG A 148 26503 28858 24169 -822 -1647 -1187 N ATOM 850 CZ ARG A 148 -14.899 36.203 30.680 1.00215.52 C ANISOU 850 CZ ARG A 148 27311 29619 24956 -818 -1648 -1170 C ATOM 851 NH1 ARG A 148 -15.384 35.814 31.851 1.00217.04 N ANISOU 851 NH1 ARG A 148 27503 29814 25148 -804 -1660 -1155 N ATOM 852 NH2 ARG A 148 -15.614 37.013 29.908 1.00213.31 N ANISOU 852 NH2 ARG A 148 27054 29314 24679 -826 -1637 -1168 N ATOM 853 N TYR A 149 -11.251 29.619 29.946 1.00106.44 N ANISOU 853 N TYR A 149 13407 15865 11170 -747 -1726 -1179 N ATOM 854 CA TYR A 149 -12.059 28.455 29.642 1.00145.43 C ANISOU 854 CA TYR A 149 18360 20773 16123 -727 -1746 -1159 C ATOM 855 C TYR A 149 -13.112 28.242 30.739 1.00160.61 C ANISOU 855 C TYR A 149 20295 22682 18046 -713 -1758 -1137 C ATOM 856 O TYR A 149 -14.307 28.335 30.465 1.00192.82 O ANISOU 856 O TYR A 149 24400 26728 22135 -710 -1761 -1121 O ATOM 857 CB TYR A 149 -11.167 27.225 29.449 1.00169.13 C ANISOU 857 CB TYR A 149 21343 23791 19128 -714 -1759 -1164 C ATOM 858 CG TYR A 149 -11.732 26.177 28.514 1.00183.00 C ANISOU 858 CG TYR A 149 23114 25515 20901 -701 -1774 -1151 C ATOM 859 CD1 TYR A 149 -11.412 26.170 27.160 1.00177.41 C ANISOU 859 CD1 TYR A 149 22409 24797 20200 -708 -1768 -1161 C ATOM 860 CD2 TYR A 149 -12.575 25.184 28.991 1.00192.04 C ANISOU 860 CD2 TYR A 149 24271 26641 22055 -681 -1793 -1128 C ATOM 861 CE1 TYR A 149 -11.926 25.202 26.311 1.00180.46 C ANISOU 861 CE1 TYR A 149 22809 25157 20602 -696 -1781 -1149 C ATOM 862 CE2 TYR A 149 -13.092 24.216 28.153 1.00186.68 C ANISOU 862 CE2 TYR A 149 23605 25933 21390 -670 -1807 -1117 C ATOM 863 CZ TYR A 149 -12.767 24.227 26.815 1.00171.59 C ANISOU 863 CZ TYR A 149 21696 24014 19486 -677 -1800 -1127 C ATOM 864 OH TYR A 149 -13.288 23.258 25.984 1.00140.40 O ANISOU 864 OH TYR A 149 17760 20036 15551 -666 -1813 -1116 O ATOM 865 N GLN A 150 -12.682 27.980 31.973 1.00138.70 N ANISOU 865 N GLN A 150 17503 19935 15263 -707 -1764 -1137 N ATOM 866 CA GLN A 150 -13.626 27.680 33.063 1.00146.34 C ANISOU 866 CA GLN A 150 18481 20891 16231 -693 -1776 -1116 C ATOM 867 C GLN A 150 -14.355 28.904 33.662 1.00125.09 C ANISOU 867 C GLN A 150 15803 18194 13533 -704 -1764 -1112 C ATOM 868 O GLN A 150 -15.383 28.752 34.328 1.00122.10 O ANISOU 868 O GLN A 150 15439 17796 13157 -694 -1773 -1093 O ATOM 869 CB GLN A 150 -12.945 26.854 34.168 1.00152.20 C ANISOU 869 CB GLN A 150 19200 21662 16966 -680 -1789 -1115 C ATOM 870 CG GLN A 150 -13.885 25.939 34.969 1.00142.94 C ANISOU 870 CG GLN A 150 18040 20472 15799 -659 -1809 -1091 C ATOM 871 CD GLN A 150 -14.342 24.710 34.190 1.00131.42 C ANISOU 871 CD GLN A 150 16593 18985 14356 -643 -1825 -1077 C ATOM 872 OE1 GLN A 150 -13.668 24.261 33.261 1.00124.39 O ANISOU 872 OE1 GLN A 150 15695 18098 13470 -644 -1826 -1088 O ATOM 873 NE2 GLN A 150 -15.495 24.163 34.568 1.00115.77 N ANISOU 873 NE2 GLN A 150 14630 16975 12382 -630 -1839 -1055 N ATOM 874 N SER A 151 -13.832 30.107 33.428 1.00 93.09 N ANISOU 874 N SER A 151 11744 14156 9470 -725 -1743 -1130 N ATOM 875 CA SER A 151 -14.488 31.329 33.899 1.00 94.65 C ANISOU 875 CA SER A 151 11955 14348 9661 -737 -1729 -1128 C ATOM 876 C SER A 151 -15.774 31.623 33.113 1.00118.16 C ANISOU 876 C SER A 151 14964 17283 12650 -737 -1728 -1113 C ATOM 877 O SER A 151 -16.845 31.773 33.705 1.00122.57 O ANISOU 877 O SER A 151 15538 17823 13210 -730 -1733 -1096 O ATOM 878 CB SER A 151 -13.531 32.526 33.819 1.00 88.89 C ANISOU 878 CB SER A 151 11210 13646 8917 -761 -1707 -1152 C ATOM 879 OG SER A 151 -13.324 33.132 35.090 1.00 61.24 O ANISOU 879 OG SER A 151 7697 10170 5402 -767 -1701 -1155 O ATOM 880 N LEU A 152 -15.663 31.690 31.784 1.00130.81 N ANISOU 880 N LEU A 152 16572 18870 14259 -743 -1723 -1121 N ATOM 881 CA LEU A 152 -16.812 31.961 30.907 1.00137.60 C ANISOU 881 CA LEU A 152 17461 19692 15130 -743 -1721 -1109 C ATOM 882 C LEU A 152 -17.632 30.704 30.647 1.00149.34 C ANISOU 882 C LEU A 152 18960 21150 16631 -722 -1742 -1089 C ATOM 883 O LEU A 152 -18.793 30.609 31.047 1.00164.38 O ANISOU 883 O LEU A 152 20883 23032 18541 -712 -1749 -1071 O ATOM 884 CB LEU A 152 -16.361 32.547 29.565 1.00120.32 C ANISOU 884 CB LEU A 152 15275 17499 12942 -758 -1706 -1125 C ATOM 885 CG LEU A 152 -17.482 32.755 28.539 1.00100.86 C ANISOU 885 CG LEU A 152 12838 14995 10488 -757 -1704 -1115 C ATOM 886 CD1 LEU A 152 -18.418 33.877 28.975 1.00 68.71 C ANISOU 886 CD1 LEU A 152 8784 10911 6411 -764 -1693 -1107 C ATOM 887 CD2 LEU A 152 -16.922 33.027 27.146 1.00 98.67 C ANISOU 887 CD2 LEU A 152 12561 14715 10214 -769 -1693 -1130 C ATOM 888 N MET A 153 -17.017 29.738 29.976 1.00127.33 N ANISOU 888 N MET A 153 16163 18366 13851 -715 -1751 -1094 N ATOM 889 CA MET A 153 -17.681 28.481 29.698 1.00 96.26 C ANISOU 889 CA MET A 153 12239 14406 9931 -696 -1771 -1076 C ATOM 890 C MET A 153 -17.682 27.680 30.986 1.00 88.59 C ANISOU 890 C MET A 153 11257 13447 8956 -681 -1786 -1065 C ATOM 891 O MET A 153 -16.627 27.338 31.510 1.00101.56 O ANISOU 891 O MET A 153 12877 15121 10592 -680 -1789 -1075 O ATOM 892 CB MET A 153 -16.902 27.716 28.628 1.00 70.66 C ANISOU 892 CB MET A 153 8987 11166 6695 -694 -1775 -1086 C ATOM 893 CG MET A 153 -17.392 27.927 27.213 1.00 74.87 C ANISOU 893 CG MET A 153 9538 11671 7239 -699 -1769 -1087 C ATOM 894 SD MET A 153 -18.920 27.016 26.927 1.00180.87 S ANISOU 894 SD MET A 153 22989 25053 20680 -680 -1786 -1060 S ATOM 895 CE MET A 153 -19.198 27.316 25.182 1.00 67.58 C ANISOU 895 CE MET A 153 8656 10679 6341 -689 -1777 -1066 C ATOM 896 N THR A 154 -18.866 27.378 31.500 1.00 98.57 N ANISOU 896 N THR A 154 12539 14688 10226 -668 -1797 -1044 N ATOM 897 CA THR A 154 -18.974 26.553 32.692 1.00109.12 C ANISOU 897 CA THR A 154 13867 16032 11560 -653 -1813 -1032 C ATOM 898 C THR A 154 -19.864 25.382 32.336 1.00117.02 C ANISOU 898 C THR A 154 14884 17003 12576 -635 -1831 -1012 C ATOM 899 O THR A 154 -20.781 25.531 31.533 1.00101.39 O ANISOU 899 O THR A 154 12926 14993 10606 -636 -1830 -1005 O ATOM 900 CB THR A 154 -19.605 27.319 33.869 1.00 82.85 C ANISOU 900 CB THR A 154 10546 12708 8225 -655 -1809 -1024 C ATOM 901 OG1 THR A 154 -19.195 28.692 33.835 1.00 62.77 O ANISOU 901 OG1 THR A 154 7998 10180 5670 -674 -1788 -1039 O ATOM 902 CG2 THR A 154 -19.188 26.689 35.191 1.00 70.79 C ANISOU 902 CG2 THR A 154 9002 11204 6690 -644 -1820 -1019 C ATOM 903 N ARG A 155 -19.612 24.218 32.925 1.00113.56 N ANISOU 903 N ARG A 155 14436 16572 12139 -620 -1849 -1005 N ATOM 904 CA ARG A 155 -20.458 23.071 32.635 1.00103.27 C ANISOU 904 CA ARG A 155 13148 15241 10850 -604 -1866 -986 C ATOM 905 C ARG A 155 -21.890 23.472 32.966 1.00139.40 C ANISOU 905 C ARG A 155 17747 19788 15429 -601 -1867 -969 C ATOM 906 O ARG A 155 -22.845 22.805 32.567 1.00168.24 O ANISOU 906 O ARG A 155 21417 23412 19094 -591 -1877 -954 O ATOM 907 CB ARG A 155 -20.022 21.839 33.427 1.00102.75 C ANISOU 907 CB ARG A 155 13069 15189 10783 -588 -1884 -979 C ATOM 908 CG ARG A 155 -18.681 21.279 32.988 1.00104.90 C ANISOU 908 CG ARG A 155 13319 15485 11052 -589 -1886 -995 C ATOM 909 CD ARG A 155 -17.645 21.357 34.101 1.00112.22 C ANISOU 909 CD ARG A 155 14221 16452 11964 -588 -1885 -1005 C ATOM 910 NE ARG A 155 -17.589 20.121 34.879 1.00122.39 N ANISOU 910 NE ARG A 155 15503 17746 13254 -569 -1904 -992 N ATOM 911 CZ ARG A 155 -16.729 19.895 35.867 1.00 87.67 C ANISOU 911 CZ ARG A 155 11084 13382 8845 -564 -1907 -998 C ATOM 912 NH1 ARG A 155 -15.847 20.826 36.203 1.00107.65 N ANISOU 912 NH1 ARG A 155 13596 15944 11362 -577 -1892 -1016 N ATOM 913 NH2 ARG A 155 -16.749 18.738 36.518 1.00 49.68 N ANISOU 913 NH2 ARG A 155 6269 8573 4034 -547 -1925 -986 N ATOM 914 N ALA A 156 -22.018 24.567 33.714 1.00140.05 N ANISOU 914 N ALA A 156 17829 19882 15502 -610 -1855 -972 N ATOM 915 CA ALA A 156 -23.305 25.203 33.984 1.00111.63 C ANISOU 915 CA ALA A 156 14251 16259 11904 -610 -1851 -959 C ATOM 916 C ALA A 156 -23.777 26.116 32.844 1.00 98.90 C ANISOU 916 C ALA A 156 12655 14627 10296 -622 -1836 -964 C ATOM 917 O ALA A 156 -24.971 26.199 32.568 1.00 66.13 O ANISOU 917 O ALA A 156 8525 10448 6153 -617 -1838 -951 O ATOM 918 CB ALA A 156 -23.245 25.982 35.300 1.00 83.43 C ANISOU 918 CB ALA A 156 10673 12708 8320 -614 -1845 -959 C ATOM 919 N ARG A 157 -22.841 26.813 32.203 1.00109.85 N ANISOU 919 N ARG A 157 14031 16031 11677 -637 -1822 -984 N ATOM 920 CA ARG A 157 -23.184 27.820 31.193 1.00112.11 C ANISOU 920 CA ARG A 157 14330 16302 11965 -650 -1805 -991 C ATOM 921 C ARG A 157 -23.456 27.324 29.757 1.00 96.43 C ANISOU 921 C ARG A 157 12355 14292 9991 -648 -1808 -990 C ATOM 922 O ARG A 157 -24.094 28.023 28.971 1.00 66.37 O ANISOU 922 O ARG A 157 8565 10465 6188 -654 -1798 -990 O ATOM 923 CB ARG A 157 -22.162 28.974 31.208 1.00112.44 C ANISOU 923 CB ARG A 157 14358 16372 11993 -670 -1786 -1012 C ATOM 924 CG ARG A 157 -22.152 29.768 32.518 1.00114.94 C ANISOU 924 CG ARG A 157 14669 16707 12296 -675 -1779 -1012 C ATOM 925 CD ARG A 157 -21.540 31.156 32.355 1.00116.22 C ANISOU 925 CD ARG A 157 14825 16887 12446 -697 -1757 -1031 C ATOM 926 NE ARG A 157 -21.726 31.985 33.544 1.00130.33 N ANISOU 926 NE ARG A 157 16611 18688 14222 -702 -1750 -1029 N ATOM 927 CZ ARG A 157 -21.382 33.268 33.623 1.00136.26 C ANISOU 927 CZ ARG A 157 17360 19452 14961 -721 -1730 -1043 C ATOM 928 NH1 ARG A 157 -20.834 33.875 32.580 1.00131.73 N ANISOU 928 NH1 ARG A 157 16785 18881 14386 -736 -1716 -1059 N ATOM 929 NH2 ARG A 157 -21.588 33.947 34.743 1.00142.14 N ANISOU 929 NH2 ARG A 157 18103 20209 15696 -725 -1725 -1040 N ATOM 930 N ALA A 158 -22.970 26.136 29.410 1.00 75.64 N ANISOU 930 N ALA A 158 10338 10129 8271 -197 508 846 N ATOM 931 CA ALA A 158 -23.193 25.579 28.070 1.00 84.02 C ANISOU 931 CA ALA A 158 11327 11139 9456 -180 468 818 C ATOM 932 C ALA A 158 -24.550 24.884 27.899 1.00 87.46 C ANISOU 932 C ALA A 158 11736 11509 9986 -196 448 811 C ATOM 933 O ALA A 158 -25.043 24.728 26.771 1.00 78.80 O ANISOU 933 O ALA A 158 10659 10293 8989 -173 435 748 O ATOM 934 CB ALA A 158 -22.065 24.626 27.692 1.00 89.46 C ANISOU 934 CB ALA A 158 11976 11838 10176 -80 480 826 C ATOM 935 N LYS A 159 -25.141 24.469 29.020 1.00103.25 N ANISOU 935 N LYS A 159 13771 13504 11955 -201 474 837 N ATOM 936 CA LYS A 159 -26.452 23.815 29.029 1.00 98.56 C ANISOU 936 CA LYS A 159 13234 12735 11480 -71 532 797 C ATOM 937 C LYS A 159 -27.498 24.770 28.473 1.00 73.25 C ANISOU 937 C LYS A 159 10132 9358 8343 -14 573 713 C ATOM 938 O LYS A 159 -28.324 24.414 27.620 1.00 79.20 O ANISOU 938 O LYS A 159 10887 9991 9214 83 597 660 O ATOM 939 CB LYS A 159 -26.842 23.387 30.456 1.00 82.99 C ANISOU 939 CB LYS A 159 11285 10778 9471 -15 588 845 C ATOM 940 CG LYS A 159 -26.475 21.940 30.838 1.00 90.78 C ANISOU 940 CG LYS A 159 12191 11813 10490 66 598 896 C ATOM 941 CD LYS A 159 -26.858 21.607 32.293 1.00 91.89 C ANISOU 941 CD LYS A 159 12342 11979 10594 138 659 953 C ATOM 942 CE LYS A 159 -26.622 20.130 32.631 1.00 83.44 C ANISOU 942 CE LYS A 159 11146 10963 9593 278 681 1018 C ATOM 943 NZ LYS A 159 -26.970 19.787 34.046 1.00 62.82 N ANISOU 943 NZ LYS A 159 8533 8388 6947 350 738 1082 N ATOM 944 N VAL A 160 -27.446 25.999 28.965 1.00 21.81 N ANISOU 944 N VAL A 160 3719 2820 1747 -75 589 686 N ATOM 945 CA VAL A 160 -28.352 27.025 28.504 1.00 22.48 C ANISOU 945 CA VAL A 160 3952 2714 1877 -56 626 583 C ATOM 946 C VAL A 160 -28.157 27.218 27.018 1.00 48.63 C ANISOU 946 C VAL A 160 7264 5964 5251 -86 580 510 C ATOM 947 O VAL A 160 -29.119 27.408 26.296 1.00 65.16 O ANISOU 947 O VAL A 160 9418 7913 7426 -24 607 434 O ATOM 948 CB VAL A 160 -28.099 28.358 29.200 1.00 22.22 C ANISOU 948 CB VAL A 160 4055 2650 1738 -150 640 547 C ATOM 949 CG1 VAL A 160 -26.983 29.117 28.507 1.00 19.37 C ANISOU 949 CG1 VAL A 160 3722 2310 1326 -282 576 499 C ATOM 950 CG2 VAL A 160 -29.362 29.184 29.209 1.00 36.63 C ANISOU 950 CG2 VAL A 160 6038 4273 3607 -102 704 460 C ATOM 951 N ILE A 161 -26.909 27.158 26.560 1.00 59.05 N ANISOU 951 N ILE A 161 8511 7398 6527 -172 515 535 N ATOM 952 CA ILE A 161 -26.600 27.409 25.155 1.00 48.02 C ANISOU 952 CA ILE A 161 7126 5940 5178 -216 468 461 C ATOM 953 C ILE A 161 -27.175 26.353 24.236 1.00 42.48 C ANISOU 953 C ILE A 161 6336 5216 4587 -119 466 462 C ATOM 954 O ILE A 161 -27.748 26.681 23.199 1.00 39.79 O ANISOU 954 O ILE A 161 6056 4754 4308 -105 464 372 O ATOM 955 CB ILE A 161 -25.102 27.545 24.919 1.00 39.49 C ANISOU 955 CB ILE A 161 5994 4981 4031 -317 411 483 C ATOM 956 CG1 ILE A 161 -24.689 28.974 25.245 1.00 31.32 C ANISOU 956 CG1 ILE A 161 5109 3878 2912 -458 398 407 C ATOM 957 CG2 ILE A 161 -24.763 27.212 23.490 1.00 15.37 C ANISOU 957 CG2 ILE A 161 2891 1905 1044 -329 364 444 C ATOM 958 CD1 ILE A 161 -25.790 29.978 24.945 1.00 17.18 C ANISOU 958 CD1 ILE A 161 3486 1883 1157 -474 422 298 C ATOM 959 N ILE A 162 -27.034 25.087 24.615 1.00 14.83 N ANISOU 959 N ILE A 162 2703 1826 1107 -60 467 552 N ATOM 960 CA ILE A 162 -27.692 24.027 23.860 1.00 29.78 C ANISOU 960 CA ILE A 162 4534 3670 3112 44 481 537 C ATOM 961 C ILE A 162 -29.204 24.245 23.865 1.00 37.54 C ANISOU 961 C ILE A 162 5593 4503 4169 161 559 472 C ATOM 962 O ILE A 162 -29.881 24.106 22.831 1.00 28.41 O ANISOU 962 O ILE A 162 4436 3271 3089 221 574 407 O ATOM 963 CB ILE A 162 -27.397 22.647 24.433 1.00 21.12 C ANISOU 963 CB ILE A 162 3327 2665 2032 103 487 616 C ATOM 964 CG1 ILE A 162 -25.908 22.505 24.756 1.00 35.10 C ANISOU 964 CG1 ILE A 162 5044 4597 3696 -32 419 681 C ATOM 965 CG2 ILE A 162 -27.864 21.588 23.465 1.00 12.92 C ANISOU 965 CG2 ILE A 162 2211 1581 1116 221 507 591 C ATOM 966 CD1 ILE A 162 -25.484 21.091 25.109 1.00 23.70 C ANISOU 966 CD1 ILE A 162 3525 3200 2281 45 434 726 C ATOM 967 N CYS A 163 -29.728 24.595 25.038 1.00 20.28 N ANISOU 967 N CYS A 163 3466 2290 1949 193 613 492 N ATOM 968 CA CYS A 163 -31.146 24.896 25.176 1.00 33.31 C ANISOU 968 CA CYS A 163 5187 3812 3658 304 698 438 C ATOM 969 C CYS A 163 -31.630 25.987 24.215 1.00 32.96 C ANISOU 969 C CYS A 163 5256 3650 3618 269 697 327 C ATOM 970 O CYS A 163 -32.664 25.832 23.577 1.00 26.31 O ANISOU 970 O CYS A 163 4408 2741 2847 363 747 274 O ATOM 971 CB CYS A 163 -31.481 25.249 26.619 1.00 15.30 C ANISOU 971 CB CYS A 163 2967 1522 1323 324 752 478 C ATOM 972 SG CYS A 163 -31.729 23.795 27.632 1.00 92.82 S ANISOU 972 SG CYS A 163 12660 11419 11189 454 803 578 S ATOM 973 N THR A 164 -30.879 27.079 24.118 1.00 24.78 N ANISOU 973 N THR A 164 4317 2598 2502 132 645 290 N ATOM 974 CA THR A 164 -31.153 28.166 23.180 1.00 55.15 C ANISOU 974 CA THR A 164 8284 6328 6342 77 631 175 C ATOM 975 C THR A 164 -31.066 27.688 21.731 1.00 82.65 C ANISOU 975 C THR A 164 11700 9821 9881 83 589 133 C ATOM 976 O THR A 164 -31.862 28.098 20.880 1.00 98.55 O ANISOU 976 O THR A 164 13771 11754 11921 114 609 45 O ATOM 977 CB THR A 164 -30.157 29.334 23.375 1.00 65.26 C ANISOU 977 CB THR A 164 9671 7596 7528 -86 577 143 C ATOM 978 OG1 THR A 164 -30.595 30.170 24.452 1.00 33.57 O ANISOU 978 OG1 THR A 164 5778 3515 3462 -94 631 134 O ATOM 979 CG2 THR A 164 -30.056 30.168 22.111 1.00 94.05 C ANISOU 979 CG2 THR A 164 13406 11151 11177 -168 530 29 C ATOM 980 N VAL A 165 -30.091 26.827 21.451 1.00 74.05 N ANISOU 980 N VAL A 165 10491 8845 8801 53 532 198 N ATOM 981 CA VAL A 165 -30.002 26.193 20.143 1.00 50.50 C ANISOU 981 CA VAL A 165 7433 5880 5874 70 498 172 C ATOM 982 C VAL A 165 -31.306 25.459 19.800 1.00 81.19 C ANISOU 982 C VAL A 165 11267 9738 9843 215 569 155 C ATOM 983 O VAL A 165 -31.695 25.452 18.632 1.00 15.85 O ANISOU 983 O VAL A 165 2991 1436 1595 226 562 91 O ATOM 984 CB VAL A 165 -28.815 25.212 20.063 1.00 23.25 C ANISOU 984 CB VAL A 165 3847 2564 2423 37 444 262 C ATOM 985 CG1 VAL A 165 -28.723 24.603 18.690 1.00 17.89 C ANISOU 985 CG1 VAL A 165 3105 1892 1800 52 412 230 C ATOM 986 CG2 VAL A 165 -27.528 25.917 20.382 1.00 11.79 C ANISOU 986 CG2 VAL A 165 2423 1173 885 -99 388 284 C ATOM 987 N TRP A 166 -31.960 24.856 20.811 1.00 84.09 N ANISOU 987 N TRP A 166 11587 10121 10244 321 641 213 N ATOM 988 CA TRP A 166 -33.246 24.124 20.646 1.00 45.35 C ANISOU 988 CA TRP A 166 6597 5214 5419 453 717 211 C ATOM 989 C TRP A 166 -34.552 24.918 20.844 1.00 41.77 C ANISOU 989 C TRP A 166 6155 4743 4974 442 726 189 C ATOM 990 O TRP A 166 -35.651 24.431 20.527 1.00 10.41 O ANISOU 990 O TRP A 166 2066 824 1064 466 723 205 O ATOM 991 CB TRP A 166 -33.280 22.894 21.541 1.00 10.84 C ANISOU 991 CB TRP A 166 2114 905 1101 558 768 299 C ATOM 992 CG TRP A 166 -32.296 21.858 21.154 1.00 48.76 C ANISOU 992 CG TRP A 166 6809 5792 5926 546 716 348 C ATOM 993 CD1 TRP A 166 -30.941 21.959 21.213 1.00 57.87 C ANISOU 993 CD1 TRP A 166 7967 7003 7017 433 629 384 C ATOM 994 CD2 TRP A 166 -32.577 20.548 20.659 1.00 67.96 C ANISOU 994 CD2 TRP A 166 9087 8295 8441 595 712 373 C ATOM 995 NE1 TRP A 166 -30.354 20.795 20.779 1.00 69.28 N ANISOU 995 NE1 TRP A 166 9293 8524 8508 461 608 424 N ATOM 996 CE2 TRP A 166 -31.340 19.912 20.432 1.00 64.66 C ANISOU 996 CE2 TRP A 166 8619 7930 8019 593 682 413 C ATOM 997 CE3 TRP A 166 -33.756 19.850 20.385 1.00 87.87 C ANISOU 997 CE3 TRP A 166 11503 10860 11025 577 684 368 C ATOM 998 CZ2 TRP A 166 -31.250 18.611 19.943 1.00 57.00 C ANISOU 998 CZ2 TRP A 166 7510 7033 7113 607 655 436 C ATOM 999 CZ3 TRP A 166 -33.661 18.558 19.899 1.00 85.66 C ANISOU 999 CZ3 TRP A 166 11106 10646 10795 565 643 384 C ATOM 1000 CH2 TRP A 166 -32.421 17.954 19.685 1.00 66.65 C ANISOU 1000 CH2 TRP A 166 8662 8276 8386 574 626 413 C ATOM 1001 N ALA A 167 -34.431 26.139 21.347 1.00 54.21 N ANISOU 1001 N ALA A 167 7873 6243 6480 394 736 152 N ATOM 1002 CA ALA A 167 -35.519 27.101 21.265 1.00 57.68 C ANISOU 1002 CA ALA A 167 8328 6668 6921 371 733 123 C ATOM 1003 C ALA A 167 -35.524 27.727 19.870 1.00 50.84 C ANISOU 1003 C ALA A 167 7443 5822 6052 289 654 70 C ATOM 1004 O ALA A 167 -36.587 28.014 19.314 1.00 42.82 O ANISOU 1004 O ALA A 167 6371 4833 5064 295 647 62 O ATOM 1005 CB ALA A 167 -35.351 28.175 22.309 1.00 83.59 C ANISOU 1005 CB ALA A 167 11761 9867 10131 344 769 107 C ATOM 1006 N ILE A 168 -34.326 27.925 19.311 1.00 63.25 N ANISOU 1006 N ILE A 168 9062 7384 7588 213 596 39 N ATOM 1007 CA ILE A 168 -34.166 28.433 17.947 1.00 46.41 C ANISOU 1007 CA ILE A 168 6892 5284 5459 139 514 -2 C ATOM 1008 C ILE A 168 -34.507 27.374 16.917 1.00 33.64 C ANISOU 1008 C ILE A 168 5150 3731 3900 175 495 13 C ATOM 1009 O ILE A 168 -35.244 27.646 15.970 1.00 21.52 O ANISOU 1009 O ILE A 168 3561 2229 2385 164 467 -3 O ATOM 1010 CB ILE A 168 -32.737 28.896 17.677 1.00 35.01 C ANISOU 1010 CB ILE A 168 5514 3821 3966 36 452 -30 C ATOM 1011 CG1 ILE A 168 -32.420 30.142 18.505 1.00 39.90 C ANISOU 1011 CG1 ILE A 168 6254 4383 4525 -32 455 -49 C ATOM 1012 CG2 ILE A 168 -32.565 29.186 16.199 1.00 9.19 C ANISOU 1012 CG2 ILE A 168 2165 604 721 -15 373 -56 C ATOM 1013 CD1 ILE A 168 -30.939 30.386 18.713 1.00 52.00 C ANISOU 1013 CD1 ILE A 168 7868 5894 5997 -144 414 -60 C ATOM 1014 N SER A 169 -33.959 26.174 17.102 1.00 8.83 N ANISOU 1014 N SER A 169 1968 607 780 219 516 45 N ATOM 1015 CA SER A 169 -34.257 25.040 16.239 1.00 21.57 C ANISOU 1015 CA SER A 169 3460 2284 2453 252 503 65 C ATOM 1016 C SER A 169 -35.745 24.814 16.225 1.00 33.74 C ANISOU 1016 C SER A 169 4924 3856 4039 296 533 86 C ATOM 1017 O SER A 169 -36.329 24.658 15.152 1.00 9.69 O ANISOU 1017 O SER A 169 1822 845 1016 279 503 75 O ATOM 1018 CB SER A 169 -33.591 23.769 16.741 1.00 8.16 C ANISOU 1018 CB SER A 169 1711 608 781 312 537 115 C ATOM 1019 OG SER A 169 -32.189 23.861 16.684 1.00 16.11 O ANISOU 1019 OG SER A 169 2826 1562 1733 306 558 118 O ATOM 1020 N ALA A 170 -36.350 24.783 17.421 1.00 50.62 N ANISOU 1020 N ALA A 170 7068 5980 6187 349 593 119 N ATOM 1021 CA ALA A 170 -37.799 24.568 17.526 1.00 44.29 C ANISOU 1021 CA ALA A 170 6199 5202 5426 383 625 142 C ATOM 1022 C ALA A 170 -38.644 25.681 16.886 1.00 56.60 C ANISOU 1022 C ALA A 170 7798 6745 6964 351 616 110 C ATOM 1023 O ALA A 170 -39.624 25.410 16.178 1.00 8.85 O ANISOU 1023 O ALA A 170 1728 642 993 347 581 191 O ATOM 1024 CB ALA A 170 -38.199 24.363 18.984 1.00 9.69 C ANISOU 1024 CB ALA A 170 1820 806 1056 443 689 185 C ATOM 1025 N LEU A 171 -38.266 26.929 17.154 1.00 66.87 N ANISOU 1025 N LEU A 171 9202 7995 8209 316 609 75 N ATOM 1026 CA LEU A 171 -38.992 28.075 16.632 1.00 9.49 C ANISOU 1026 CA LEU A 171 2004 630 973 273 568 121 C ATOM 1027 C LEU A 171 -38.972 28.041 15.120 1.00 50.82 C ANISOU 1027 C LEU A 171 7211 5891 6207 236 522 101 C ATOM 1028 O LEU A 171 -40.013 27.994 14.470 1.00 57.69 O ANISOU 1028 O LEU A 171 8050 6770 7098 253 538 114 O ATOM 1029 CB LEU A 171 -38.321 29.356 17.091 1.00 9.94 C ANISOU 1029 CB LEU A 171 2168 636 974 222 555 87 C ATOM 1030 CG LEU A 171 -39.218 30.577 17.014 1.00 36.68 C ANISOU 1030 CG LEU A 171 5603 4137 4196 196 637 76 C ATOM 1031 CD1 LEU A 171 -40.149 30.569 18.217 1.00 52.98 C ANISOU 1031 CD1 LEU A 171 7674 6183 6273 253 716 107 C ATOM 1032 CD2 LEU A 171 -38.397 31.856 16.960 1.00 23.46 C ANISOU 1032 CD2 LEU A 171 4030 2429 2456 128 600 43 C ATOM 1033 N VAL A 172 -37.760 28.038 14.576 1.00 41.97 N ANISOU 1033 N VAL A 172 6100 4783 5065 185 466 71 N ATOM 1034 CA VAL A 172 -37.522 28.124 13.137 1.00 24.51 C ANISOU 1034 CA VAL A 172 3874 2593 2846 142 415 50 C ATOM 1035 C VAL A 172 -38.009 26.922 12.326 1.00 31.59 C ANISOU 1035 C VAL A 172 4679 3536 3786 172 413 67 C ATOM 1036 O VAL A 172 -38.623 27.099 11.277 1.00 48.42 O ANISOU 1036 O VAL A 172 6788 5785 5823 147 438 57 O ATOM 1037 CB VAL A 172 -36.041 28.342 12.851 1.00 26.73 C ANISOU 1037 CB VAL A 172 4171 2994 2990 73 393 22 C ATOM 1038 CG1 VAL A 172 -35.724 28.015 11.409 1.00 44.72 C ANISOU 1038 CG1 VAL A 172 6413 5298 5280 45 340 12 C ATOM 1039 CG2 VAL A 172 -35.666 29.764 13.183 1.00 8.45 C ANISOU 1039 CG2 VAL A 172 1960 514 735 25 351 7 C ATOM 1040 N SER A 173 -37.730 25.706 12.787 1.00 7.21 N ANISOU 1040 N SER A 173 1528 479 733 208 426 90 N ATOM 1041 CA SER A 173 -38.251 24.528 12.100 1.00 19.70 C ANISOU 1041 CA SER A 173 3008 2202 2277 214 472 105 C ATOM 1042 C SER A 173 -39.768 24.380 12.244 1.00 50.37 C ANISOU 1042 C SER A 173 6855 6087 6198 250 527 139 C ATOM 1043 O SER A 173 -40.471 24.238 11.232 1.00 6.99 O ANISOU 1043 O SER A 173 1352 504 801 266 470 152 O ATOM 1044 CB SER A 173 -37.559 23.255 12.590 1.00 40.14 C ANISOU 1044 CB SER A 173 5552 4722 4978 259 431 139 C ATOM 1045 OG SER A 173 -38.260 22.092 12.161 1.00 34.79 O ANISOU 1045 OG SER A 173 4788 4080 4350 292 447 161 O ATOM 1046 N PHE A 174 -40.257 24.425 13.493 1.00 65.88 N ANISOU 1046 N PHE A 174 8845 7928 8257 312 526 183 N ATOM 1047 CA PHE A 174 -41.657 24.093 13.811 1.00 42.73 C ANISOU 1047 CA PHE A 174 5871 4995 5371 353 577 232 C ATOM 1048 C PHE A 174 -42.725 25.175 13.559 1.00 37.46 C ANISOU 1048 C PHE A 174 5212 4416 4604 323 668 208 C ATOM 1049 O PHE A 174 -43.880 24.835 13.307 1.00 21.05 O ANISOU 1049 O PHE A 174 3078 2345 2574 342 701 241 O ATOM 1050 CB PHE A 174 -41.803 23.495 15.228 1.00 8.88 C ANISOU 1050 CB PHE A 174 1537 818 1018 352 684 279 C ATOM 1051 CG PHE A 174 -41.889 21.978 15.247 1.00 54.31 C ANISOU 1051 CG PHE A 174 7203 6603 6829 366 686 325 C ATOM 1052 CD1 PHE A 174 -40.788 21.205 15.588 1.00 70.68 C ANISOU 1052 CD1 PHE A 174 9267 8599 8988 437 608 300 C ATOM 1053 CD2 PHE A 174 -43.068 21.326 14.912 1.00 62.05 C ANISOU 1053 CD2 PHE A 174 8121 7591 7866 375 711 368 C ATOM 1054 CE1 PHE A 174 -40.861 19.810 15.597 1.00 35.60 C ANISOU 1054 CE1 PHE A 174 4743 4278 4505 378 666 372 C ATOM 1055 CE2 PHE A 174 -43.146 19.929 14.924 1.00 46.45 C ANISOU 1055 CE2 PHE A 174 6074 5635 5938 380 711 411 C ATOM 1056 CZ PHE A 174 -42.039 19.176 15.266 1.00 9.03 C ANISOU 1056 CZ PHE A 174 1328 828 1274 466 631 378 C ATOM 1057 N LEU A 175 -42.374 26.457 13.651 1.00 36.97 N ANISOU 1057 N LEU A 175 5243 4323 4481 300 656 173 N ATOM 1058 CA LEU A 175 -43.354 27.489 13.306 1.00 45.21 C ANISOU 1058 CA LEU A 175 6354 5212 5613 326 618 185 C ATOM 1059 C LEU A 175 -43.721 27.531 11.827 1.00 38.30 C ANISOU 1059 C LEU A 175 5440 4439 4674 314 651 118 C ATOM 1060 O LEU A 175 -44.894 27.405 11.487 1.00 37.34 O ANISOU 1060 O LEU A 175 5287 4309 4590 343 704 157 O ATOM 1061 CB LEU A 175 -42.893 28.879 13.773 1.00 52.85 C ANISOU 1061 CB LEU A 175 7404 6270 6405 275 677 139 C ATOM 1062 CG LEU A 175 -43.826 29.488 14.825 1.00 63.56 C ANISOU 1062 CG LEU A 175 8793 7596 7760 312 753 164 C ATOM 1063 CD1 LEU A 175 -45.179 29.750 14.248 1.00 73.88 C ANISOU 1063 CD1 LEU A 175 10079 8853 9138 375 791 135 C ATOM 1064 CD2 LEU A 175 -43.960 28.491 15.927 1.00 86.16 C ANISOU 1064 CD2 LEU A 175 11600 10472 10666 356 795 204 C ATOM 1065 N PRO A 176 -42.724 27.715 10.947 1.00 23.28 N ANISOU 1065 N PRO A 176 3565 2548 2734 263 575 75 N ATOM 1066 CA PRO A 176 -42.980 27.877 9.513 1.00 30.65 C ANISOU 1066 CA PRO A 176 4511 3481 3654 238 548 66 C ATOM 1067 C PRO A 176 -43.610 26.681 8.811 1.00 35.00 C ANISOU 1067 C PRO A 176 4984 4051 4263 264 574 107 C ATOM 1068 O PRO A 176 -44.160 26.860 7.727 1.00 50.79 O ANISOU 1068 O PRO A 176 7004 6036 6258 258 579 113 O ATOM 1069 CB PRO A 176 -41.588 28.141 8.947 1.00 36.38 C ANISOU 1069 CB PRO A 176 5256 4257 4308 153 459 62 C ATOM 1070 CG PRO A 176 -40.881 28.801 10.070 1.00 41.47 C ANISOU 1070 CG PRO A 176 5963 4875 4917 145 468 56 C ATOM 1071 CD PRO A 176 -41.331 28.054 11.278 1.00 8.05 C ANISOU 1071 CD PRO A 176 1702 528 827 215 485 95 C ATOM 1072 N ILE A 177 -43.531 25.488 9.389 1.00 36.05 N ANISOU 1072 N ILE A 177 5032 4214 4451 290 589 138 N ATOM 1073 CA ILE A 177 -44.235 24.342 8.809 1.00 36.81 C ANISOU 1073 CA ILE A 177 5036 4331 4619 310 612 186 C ATOM 1074 C ILE A 177 -45.716 24.319 9.177 1.00 37.70 C ANISOU 1074 C ILE A 177 5099 4429 4797 350 687 246 C ATOM 1075 O ILE A 177 -46.561 24.029 8.331 1.00 48.30 O ANISOU 1075 O ILE A 177 6393 5765 6194 357 712 285 O ATOM 1076 CB ILE A 177 -43.602 23.014 9.204 1.00 7.27 C ANISOU 1076 CB ILE A 177 1217 632 915 311 585 197 C ATOM 1077 CG1 ILE A 177 -42.373 22.765 8.352 1.00 6.55 C ANISOU 1077 CG1 ILE A 177 1147 556 787 274 519 156 C ATOM 1078 CG2 ILE A 177 -44.579 21.890 8.983 1.00 63.12 C ANISOU 1078 CG2 ILE A 177 8187 7724 8071 328 610 255 C ATOM 1079 CD1 ILE A 177 -41.941 21.338 8.338 1.00 72.44 C ANISOU 1079 CD1 ILE A 177 9410 8939 9176 275 498 175 C ATOM 1080 N MET A 178 -46.017 24.617 10.442 1.00 21.54 N ANISOU 1080 N MET A 178 3057 2374 2752 374 723 257 N ATOM 1081 CA MET A 178 -47.397 24.685 10.925 1.00 41.61 C ANISOU 1081 CA MET A 178 5556 4900 5353 410 793 313 C ATOM 1082 C MET A 178 -48.117 25.931 10.410 1.00 82.11 C ANISOU 1082 C MET A 178 10753 9982 10464 419 840 315 C ATOM 1083 O MET A 178 -49.344 26.042 10.500 1.00105.50 O ANISOU 1083 O MET A 178 13672 12924 13488 448 903 369 O ATOM 1084 CB MET A 178 -47.439 24.660 12.452 1.00 25.31 C ANISOU 1084 CB MET A 178 3492 2839 3286 435 819 320 C ATOM 1085 CG MET A 178 -47.292 23.279 13.044 1.00 30.99 C ANISOU 1085 CG MET A 178 4126 3599 4050 438 799 342 C ATOM 1086 SD MET A 178 -45.704 22.525 12.674 1.00 39.25 S ANISOU 1086 SD MET A 178 5237 4572 5104 404 659 365 S ATOM 1087 CE MET A 178 -46.059 20.801 13.032 1.00 72.10 C ANISOU 1087 CE MET A 178 9309 8754 9333 423 669 430 C ATOM 1088 N MET A 179 -47.337 26.866 9.880 1.00 71.47 N ANISOU 1088 N MET A 179 9511 8615 9031 390 803 257 N ATOM 1089 CA MET A 179 -47.868 28.085 9.296 1.00 47.14 C ANISOU 1089 CA MET A 179 6516 5485 5911 389 835 248 C ATOM 1090 C MET A 179 -48.250 27.789 7.867 1.00 37.59 C ANISOU 1090 C MET A 179 5282 4268 4732 383 836 267 C ATOM 1091 O MET A 179 -48.849 28.617 7.190 1.00 58.23 O ANISOU 1091 O MET A 179 7956 6840 7330 388 871 272 O ATOM 1092 CB MET A 179 -46.793 29.169 9.295 1.00 40.44 C ANISOU 1092 CB MET A 179 5789 4623 4953 342 770 173 C ATOM 1093 CG MET A 179 -47.264 30.499 9.813 1.00 18.62 C ANISOU 1093 CG MET A 179 3113 1814 2147 350 812 166 C ATOM 1094 SD MET A 179 -47.958 30.302 11.460 1.00104.15 S ANISOU 1094 SD MET A 179 13897 12643 13032 406 893 210 S ATOM 1095 CE MET A 179 -48.415 31.995 11.825 1.00183.71 C ANISOU 1095 CE MET A 179 24098 22658 23045 409 940 193 C ATOM 1096 N HIS A 180 -47.880 26.602 7.405 1.00 19.47 N ANISOU 1096 N HIS A 180 2904 2012 2480 373 798 279 N ATOM 1097 CA HIS A 180 -47.971 26.288 5.993 1.00 24.87 C ANISOU 1097 CA HIS A 180 3569 2693 3188 340 742 290 C ATOM 1098 C HIS A 180 -47.370 27.446 5.203 1.00 33.65 C ANISOU 1098 C HIS A 180 4819 3777 4189 283 659 228 C ATOM 1099 O HIS A 180 -47.824 27.763 4.115 1.00 64.23 O ANISOU 1099 O HIS A 180 8694 7626 8084 237 576 250 O ATOM 1100 CB HIS A 180 -49.418 26.007 5.570 1.00 30.55 C ANISOU 1100 CB HIS A 180 4181 3392 4034 341 742 375 C ATOM 1101 CG HIS A 180 -49.976 24.735 6.129 1.00 53.24 C ANISOU 1101 CG HIS A 180 6903 6303 7022 383 813 435 C ATOM 1102 ND1 HIS A 180 -49.956 23.543 5.437 1.00 76.32 N ANISOU 1102 ND1 HIS A 180 9730 9254 10015 357 754 461 N ATOM 1103 CD2 HIS A 180 -50.568 24.468 7.317 1.00 69.45 C ANISOU 1103 CD2 HIS A 180 8900 8367 9119 420 878 469 C ATOM 1104 CE1 HIS A 180 -50.508 22.597 6.174 1.00100.36 C ANISOU 1104 CE1 HIS A 180 12666 12327 13141 381 797 506 C ATOM 1105 NE2 HIS A 180 -50.890 23.133 7.321 1.00 99.34 N ANISOU 1105 NE2 HIS A 180 12570 12187 12989 408 844 508 N ATOM 1106 N TRP A 181 -46.341 28.079 5.756 1.00 31.41 N ANISOU 1106 N TRP A 181 4643 3496 3794 279 666 151 N ATOM 1107 CA TRP A 181 -45.593 29.072 5.003 1.00 8.41 C ANISOU 1107 CA TRP A 181 1840 575 781 212 570 87 C ATOM 1108 C TRP A 181 -44.934 28.334 3.841 1.00 28.69 C ANISOU 1108 C TRP A 181 4395 3170 3334 172 488 65 C ATOM 1109 O TRP A 181 -44.343 28.940 2.948 1.00 23.68 O ANISOU 1109 O TRP A 181 3808 2547 2644 108 386 26 O ATOM 1110 CB TRP A 181 -44.520 29.731 5.872 1.00 38.65 C ANISOU 1110 CB TRP A 181 5684 4429 4574 175 509 45 C ATOM 1111 CG TRP A 181 -44.958 30.990 6.550 1.00 70.91 C ANISOU 1111 CG TRP A 181 9836 8477 8628 183 547 42 C ATOM 1112 CD1 TRP A 181 -46.195 31.263 7.042 1.00 77.93 C ANISOU 1112 CD1 TRP A 181 10743 9324 9544 239 654 83 C ATOM 1113 CD2 TRP A 181 -44.161 32.160 6.791 1.00111.14 C ANISOU 1113 CD2 TRP A 181 14977 13577 13673 134 486 1 C ATOM 1114 NE1 TRP A 181 -46.222 32.526 7.587 1.00106.15 N ANISOU 1114 NE1 TRP A 181 14392 12870 13070 228 661 64 N ATOM 1115 CE2 TRP A 181 -44.985 33.099 7.443 1.00124.99 C ANISOU 1115 CE2 TRP A 181 16797 15284 15409 162 558 14 C ATOM 1116 CE3 TRP A 181 -42.831 32.503 6.519 1.00104.40 C ANISOU 1116 CE3 TRP A 181 14112 12665 12891 65 363 18 C ATOM 1117 CZ2 TRP A 181 -44.524 34.363 7.829 1.00121.31 C ANISOU 1117 CZ2 TRP A 181 16388 14808 14897 129 530 -16 C ATOM 1118 CZ3 TRP A 181 -42.373 33.758 6.905 1.00109.08 C ANISOU 1118 CZ3 TRP A 181 14783 13353 13311 31 393 8 C ATOM 1119 CH2 TRP A 181 -43.218 34.671 7.553 1.00106.60 C ANISOU 1119 CH2 TRP A 181 14532 12856 13116 58 415 16 C ATOM 1120 N TRP A 182 -45.023 27.007 3.876 1.00 33.24 N ANISOU 1120 N TRP A 182 4858 3773 3997 195 500 110 N ATOM 1121 CA TRP A 182 -44.402 26.165 2.861 1.00 22.40 C ANISOU 1121 CA TRP A 182 3447 2430 2633 153 411 103 C ATOM 1122 C TRP A 182 -45.371 25.740 1.777 1.00 9.62 C ANISOU 1122 C TRP A 182 1745 798 1113 124 341 176 C ATOM 1123 O TRP A 182 -44.981 25.030 0.858 1.00 36.60 O ANISOU 1123 O TRP A 182 5129 4234 4545 90 266 177 O ATOM 1124 CB TRP A 182 -43.720 24.938 3.484 1.00 19.07 C ANISOU 1124 CB TRP A 182 2955 2047 2245 184 447 104 C ATOM 1125 CG TRP A 182 -44.657 23.947 4.070 1.00 6.81 C ANISOU 1125 CG TRP A 182 1269 505 815 232 513 184 C ATOM 1126 CD1 TRP A 182 -45.347 24.069 5.237 1.00 45.53 C ANISOU 1126 CD1 TRP A 182 6137 5403 5758 292 618 215 C ATOM 1127 CD2 TRP A 182 -45.000 22.662 3.532 1.00 28.15 C ANISOU 1127 CD2 TRP A 182 3855 3229 3611 225 484 237 C ATOM 1128 NE1 TRP A 182 -46.107 22.946 5.460 1.00 70.73 N ANISOU 1128 NE1 TRP A 182 9192 8619 9065 316 649 285 N ATOM 1129 CE2 TRP A 182 -45.912 22.065 4.428 1.00 52.36 C ANISOU 1129 CE2 TRP A 182 6814 6307 6773 282 582 297 C ATOM 1130 CE3 TRP A 182 -44.627 21.959 2.381 1.00 7.01 C ANISOU 1130 CE3 TRP A 182 1158 562 944 178 390 238 C ATOM 1131 CZ2 TRP A 182 -46.454 20.795 4.212 1.00 23.20 C ANISOU 1131 CZ2 TRP A 182 2990 2639 3187 289 590 354 C ATOM 1132 CZ3 TRP A 182 -45.166 20.694 2.166 1.00 45.20 C ANISOU 1132 CZ3 TRP A 182 5879 5416 5880 186 394 291 C ATOM 1133 CH2 TRP A 182 -46.068 20.127 3.079 1.00 54.21 C ANISOU 1133 CH2 TRP A 182 6909 6572 7118 240 494 347 C ATOM 1134 N ARG A 183 -46.629 26.155 1.878 1.00 51.66 N ANISOU 1134 N ARG A 183 7037 6084 6507 137 362 235 N ATOM 1135 CA ARG A 183 -47.587 25.814 0.833 1.00 90.44 C ANISOU 1135 CA ARG A 183 11881 10967 11515 104 278 300 C ATOM 1136 C ARG A 183 -47.329 26.599 -0.448 1.00 91.67 C ANISOU 1136 C ARG A 183 12100 11106 11623 50 182 276 C ATOM 1137 O ARG A 183 -47.276 27.832 -0.439 1.00100.88 O ANISOU 1137 O ARG A 183 13364 12254 12710 46 197 239 O ATOM 1138 CB ARG A 183 -49.040 25.991 1.301 1.00125.42 C ANISOU 1138 CB ARG A 183 16257 15358 16038 137 332 365 C ATOM 1139 CG ARG A 183 -49.367 27.347 1.928 1.00136.11 C ANISOU 1139 CG ARG A 183 17688 16679 17347 161 398 354 C ATOM 1140 CD ARG A 183 -49.798 28.423 0.926 1.00 84.49 C ANISOU 1140 CD ARG A 183 11212 10091 10801 118 315 363 C ATOM 1141 NE ARG A 183 -49.482 29.760 1.431 1.00 40.80 N ANISOU 1141 NE ARG A 183 5796 4543 5164 132 375 315 N ATOM 1142 CZ ARG A 183 -50.037 30.306 2.512 1.00 41.70 C ANISOU 1142 CZ ARG A 183 5930 4635 5280 183 484 327 C ATOM 1143 NH1 ARG A 183 -50.952 29.640 3.211 1.00 11.25 N ANISOU 1143 NH1 ARG A 183 1970 777 1528 230 557 388 N ATOM 1144 NH2 ARG A 183 -49.674 31.525 2.898 1.00 27.68 N ANISOU 1144 NH2 ARG A 183 4282 2841 3394 188 529 273 N ATOM 1145 N ASP A 184 -47.150 25.872 -1.546 1.00 79.66 N ANISOU 1145 N ASP A 184 10531 9596 10141 15 98 290 N ATOM 1146 CA ASP A 184 -47.048 26.494 -2.858 1.00109.41 C ANISOU 1146 CA ASP A 184 14354 13358 13860 -20 34 262 C ATOM 1147 C ASP A 184 -48.412 26.351 -3.520 1.00116.52 C ANISOU 1147 C ASP A 184 15152 14201 14919 -20 8 358 C ATOM 1148 O ASP A 184 -48.980 25.259 -3.537 1.00123.25 O ANISOU 1148 O ASP A 184 15877 15069 15883 -15 -8 403 O ATOM 1149 CB ASP A 184 -45.963 25.817 -3.695 1.00 99.50 C ANISOU 1149 CB ASP A 184 13132 12154 12520 -50 -22 196 C ATOM 1150 CG ASP A 184 -45.575 26.628 -4.921 1.00 82.12 C ANISOU 1150 CG ASP A 184 11047 9967 10188 -104 -119 124 C ATOM 1151 OD1 ASP A 184 -45.516 27.878 -4.829 1.00 87.05 O ANISOU 1151 OD1 ASP A 184 11775 10580 10721 -117 -121 84 O ATOM 1152 OD2 ASP A 184 -45.328 26.008 -5.979 1.00 30.32 O ANISOU 1152 OD2 ASP A 184 4478 3431 3611 -137 -199 107 O ATOM 1153 N GLU A 185 -48.944 27.449 -4.048 1.00106.79 N ANISOU 1153 N GLU A 185 13980 12932 13665 -29 -6 356 N ATOM 1154 CA GLU A 185 -50.314 27.462 -4.555 1.00 98.28 C ANISOU 1154 CA GLU A 185 12830 11798 12714 -7 22 429 C ATOM 1155 C GLU A 185 -50.569 26.436 -5.656 1.00 98.89 C ANISOU 1155 C GLU A 185 12936 11869 12768 -18 -16 414 C ATOM 1156 O GLU A 185 -51.676 25.910 -5.779 1.00 81.10 O ANISOU 1156 O GLU A 185 10676 9581 10557 -15 -39 442 O ATOM 1157 CB GLU A 185 -50.714 28.868 -5.021 1.00 95.60 C ANISOU 1157 CB GLU A 185 12576 11409 12337 -26 -14 426 C ATOM 1158 CG GLU A 185 -51.045 29.838 -3.887 1.00112.06 C ANISOU 1158 CG GLU A 185 14678 13462 14438 -16 8 450 C ATOM 1159 CD GLU A 185 -52.303 29.454 -3.104 1.00114.12 C ANISOU 1159 CD GLU A 185 14908 13685 14766 -23 -53 496 C ATOM 1160 OE1 GLU A 185 -53.221 30.300 -3.010 1.00101.34 O ANISOU 1160 OE1 GLU A 185 13343 12001 13160 -14 -50 522 O ATOM 1161 OE2 GLU A 185 -52.373 28.320 -2.572 1.00112.07 O ANISOU 1161 OE2 GLU A 185 14675 13432 14475 -1 -17 485 O ATOM 1162 N ASP A 186 -49.537 26.137 -6.439 1.00116.88 N ANISOU 1162 N ASP A 186 15229 14212 14968 -70 -127 353 N ATOM 1163 CA ASP A 186 -49.687 25.267 -7.603 1.00116.79 C ANISOU 1163 CA ASP A 186 15187 14222 14966 -109 -236 343 C ATOM 1164 C ASP A 186 -50.376 23.940 -7.290 1.00 98.38 C ANISOU 1164 C ASP A 186 12762 11881 12736 -85 -204 390 C ATOM 1165 O ASP A 186 -50.140 23.333 -6.247 1.00103.13 O ANISOU 1165 O ASP A 186 13352 12489 13343 -48 -117 397 O ATOM 1166 CB ASP A 186 -48.339 25.026 -8.289 1.00113.43 C ANISOU 1166 CB ASP A 186 14820 13866 14414 -156 -329 264 C ATOM 1167 CG ASP A 186 -47.998 26.108 -9.297 1.00126.72 C ANISOU 1167 CG ASP A 186 16612 15562 15972 -209 -438 207 C ATOM 1168 OD1 ASP A 186 -47.395 25.781 -10.341 1.00128.62 O ANISOU 1168 OD1 ASP A 186 16893 15846 16132 -255 -544 159 O ATOM 1169 OD2 ASP A 186 -48.340 27.285 -9.050 1.00139.24 O ANISOU 1169 OD2 ASP A 186 18251 17115 17537 -204 -414 211 O ATOM 1170 N PRO A 187 -51.227 23.486 -8.217 1.00 74.83 N ANISOU 1170 N PRO A 187 9713 8890 9829 -116 -302 416 N ATOM 1171 CA PRO A 187 -52.097 22.322 -8.044 1.00 80.47 C ANISOU 1171 CA PRO A 187 10304 9602 10669 -109 -309 466 C ATOM 1172 C PRO A 187 -51.303 21.034 -7.906 1.00 75.67 C ANISOU 1172 C PRO A 187 9656 9041 10055 -109 -304 448 C ATOM 1173 O PRO A 187 -51.724 20.125 -7.196 1.00 88.55 O ANISOU 1173 O PRO A 187 11191 10680 11775 -88 -258 486 O ATOM 1174 CB PRO A 187 -52.905 22.306 -9.341 1.00 69.66 C ANISOU 1174 CB PRO A 187 8889 8218 9362 -154 -437 485 C ATOM 1175 CG PRO A 187 -51.998 22.922 -10.340 1.00 40.40 C ANISOU 1175 CG PRO A 187 5285 4534 5531 -193 -522 425 C ATOM 1176 CD PRO A 187 -51.265 23.996 -9.598 1.00 53.47 C ANISOU 1176 CD PRO A 187 7041 6189 7088 -169 -435 393 C ATOM 1177 N GLN A 188 -50.170 20.950 -8.588 1.00 53.12 N ANISOU 1177 N GLN A 188 6862 6221 7100 -136 -355 393 N ATOM 1178 CA GLN A 188 -49.324 19.780 -8.469 1.00 63.48 C ANISOU 1178 CA GLN A 188 8149 7572 8398 -133 -344 375 C ATOM 1179 C GLN A 188 -49.064 19.545 -6.982 1.00 70.54 C ANISOU 1179 C GLN A 188 9035 8468 9298 -82 -214 387 C ATOM 1180 O GLN A 188 -49.336 18.467 -6.451 1.00 48.90 O ANISOU 1180 O GLN A 188 6201 5741 6638 -66 -185 419 O ATOM 1181 CB GLN A 188 -48.024 19.976 -9.264 1.00 83.43 C ANISOU 1181 CB GLN A 188 10763 10140 10797 -167 -410 305 C ATOM 1182 CG GLN A 188 -48.213 19.899 -10.791 1.00 94.51 C ANISOU 1182 CG GLN A 188 12180 11551 12178 -222 -558 287 C ATOM 1183 CD GLN A 188 -47.641 21.098 -11.553 1.00 88.81 C ANISOU 1183 CD GLN A 188 11577 10848 11320 -260 -636 229 C ATOM 1184 OE1 GLN A 188 -48.309 22.123 -11.727 1.00 60.93 O ANISOU 1184 OE1 GLN A 188 8071 7286 7792 -268 -658 242 O ATOM 1185 NE2 GLN A 188 -46.408 20.960 -12.029 1.00 98.04 N ANISOU 1185 NE2 GLN A 188 12797 12066 12389 -250 -589 170 N ATOM 1186 N ALA A 189 -48.576 20.583 -6.309 1.00 93.92 N ANISOU 1186 N ALA A 189 12088 11420 12179 -59 -145 363 N ATOM 1187 CA ALA A 189 -48.291 20.525 -4.878 1.00 99.47 C ANISOU 1187 CA ALA A 189 12813 12123 12859 -19 -50 364 C ATOM 1188 C ALA A 189 -49.570 20.644 -4.053 1.00112.16 C ANISOU 1188 C ALA A 189 14334 13710 14571 1 -18 422 C ATOM 1189 O ALA A 189 -49.650 20.132 -2.939 1.00145.45 O ANISOU 1189 O ALA A 189 18465 17954 18844 33 53 446 O ATOM 1190 CB ALA A 189 -47.299 21.620 -4.485 1.00 63.22 C ANISOU 1190 CB ALA A 189 8320 7537 8164 0 20 319 C ATOM 1191 N LEU A 190 -50.564 21.332 -4.604 1.00 73.76 N ANISOU 1191 N LEU A 190 9469 8807 9750 -10 -50 448 N ATOM 1192 CA LEU A 190 -51.835 21.539 -3.920 1.00 49.70 C ANISOU 1192 CA LEU A 190 6330 5739 6815 14 -7 507 C ATOM 1193 C LEU A 190 -52.441 20.196 -3.562 1.00 58.47 C ANISOU 1193 C LEU A 190 7265 6883 8069 27 21 560 C ATOM 1194 O LEU A 190 -52.897 19.978 -2.434 1.00 77.92 O ANISOU 1194 O LEU A 190 9640 9362 10605 66 116 598 O ATOM 1195 CB LEU A 190 -52.789 22.292 -4.837 1.00 46.40 C ANISOU 1195 CB LEU A 190 5924 5273 6434 -7 -67 530 C ATOM 1196 CG LEU A 190 -53.928 23.089 -4.217 1.00 54.42 C ANISOU 1196 CG LEU A 190 6910 6248 7520 18 -19 578 C ATOM 1197 CD1 LEU A 190 -53.411 24.379 -3.582 1.00 44.60 C ANISOU 1197 CD1 LEU A 190 5817 4976 6154 33 24 543 C ATOM 1198 CD2 LEU A 190 -54.939 23.389 -5.298 1.00 51.55 C ANISOU 1198 CD2 LEU A 190 6509 5845 7231 -10 -98 610 C ATOM 1199 N LYS A 191 -52.432 19.300 -4.542 1.00 55.02 N ANISOU 1199 N LYS A 191 6779 6457 7670 -6 -57 561 N ATOM 1200 CA LYS A 191 -52.953 17.953 -4.390 1.00 68.03 C ANISOU 1200 CA LYS A 191 8273 8128 9448 -4 -47 608 C ATOM 1201 C LYS A 191 -52.162 17.154 -3.365 1.00 69.30 C ANISOU 1201 C LYS A 191 8400 8335 9594 29 41 601 C ATOM 1202 O LYS A 191 -52.723 16.302 -2.678 1.00 84.25 O ANISOU 1202 O LYS A 191 10162 10248 11600 50 104 652 O ATOM 1203 CB LYS A 191 -52.938 17.227 -5.732 1.00 94.55 C ANISOU 1203 CB LYS A 191 11614 11484 12826 -50 -163 599 C ATOM 1204 CG LYS A 191 -53.395 15.780 -5.661 1.00115.86 C ANISOU 1204 CG LYS A 191 14171 14199 15650 -53 -163 644 C ATOM 1205 CD LYS A 191 -53.406 15.142 -7.040 1.00115.76 C ANISOU 1205 CD LYS A 191 14156 14177 15650 -100 -289 632 C ATOM 1206 CE LYS A 191 -54.006 13.745 -7.003 1.00 88.74 C ANISOU 1206 CE LYS A 191 10597 10759 12362 -107 -296 681 C ATOM 1207 NZ LYS A 191 -54.200 13.184 -8.369 1.00 55.72 N ANISOU 1207 NZ LYS A 191 6413 6558 8199 -153 -428 675 N ATOM 1208 N CYS A 192 -50.864 17.429 -3.258 1.00 45.50 N ANISOU 1208 N CYS A 192 5502 5339 6447 32 48 541 N ATOM 1209 CA CYS A 192 -50.028 16.754 -2.266 1.00 61.21 C ANISOU 1209 CA CYS A 192 7464 7374 8419 65 131 532 C ATOM 1210 C CYS A 192 -50.217 17.331 -0.847 1.00 98.44 C ANISOU 1210 C CYS A 192 12160 12101 13141 115 247 548 C ATOM 1211 O CYS A 192 -49.919 16.663 0.148 1.00103.68 O ANISOU 1211 O CYS A 192 12756 12806 13833 153 337 563 O ATOM 1212 CB CYS A 192 -48.555 16.764 -2.699 1.00 19.99 C ANISOU 1212 CB CYS A 192 2362 2167 3065 49 91 465 C ATOM 1213 SG CYS A 192 -47.388 16.028 -1.510 1.00246.71 S ANISOU 1213 SG CYS A 192 31048 30938 31753 90 188 448 S ATOM 1214 N TYR A 193 -50.718 18.564 -0.762 1.00110.40 N ANISOU 1214 N TYR A 193 13738 13580 14628 117 247 547 N ATOM 1215 CA TYR A 193 -51.074 19.172 0.524 1.00 98.67 C ANISOU 1215 CA TYR A 193 12235 12099 13156 167 359 567 C ATOM 1216 C TYR A 193 -52.437 18.684 1.015 1.00 83.19 C ANISOU 1216 C TYR A 193 10122 10139 11349 191 426 646 C ATOM 1217 O TYR A 193 -52.648 18.498 2.217 1.00 67.14 O ANISOU 1217 O TYR A 193 8025 8132 9354 240 541 674 O ATOM 1218 CB TYR A 193 -51.089 20.703 0.430 1.00 79.56 C ANISOU 1218 CB TYR A 193 9948 9635 10648 159 337 538 C ATOM 1219 CG TYR A 193 -49.766 21.314 0.029 1.00 66.42 C ANISOU 1219 CG TYR A 193 8435 7967 8834 128 272 464 C ATOM 1220 CD1 TYR A 193 -48.607 20.553 0.012 1.00 62.25 C ANISOU 1220 CD1 TYR A 193 7915 7479 8257 123 262 428 C ATOM 1221 CD2 TYR A 193 -49.678 22.649 -0.327 1.00 81.18 C ANISOU 1221 CD2 TYR A 193 10431 9793 10621 102 220 436 C ATOM 1222 CE1 TYR A 193 -47.398 21.101 -0.353 1.00 65.74 C ANISOU 1222 CE1 TYR A 193 8478 7921 8578 91 201 366 C ATOM 1223 CE2 TYR A 193 -48.476 23.208 -0.698 1.00 95.22 C ANISOU 1223 CE2 TYR A 193 12321 11575 12285 65 153 379 C ATOM 1224 CZ TYR A 193 -47.337 22.431 -0.710 1.00100.09 C ANISOU 1224 CZ TYR A 193 12932 12236 12863 59 145 345 C ATOM 1225 OH TYR A 193 -46.131 22.982 -1.077 1.00127.89 O ANISOU 1225 OH TYR A 193 16514 15778 16302 31 104 295 O ATOM 1226 N GLN A 194 -53.367 18.509 0.076 1.00 73.36 N ANISOU 1226 N GLN A 194 8822 8862 10189 156 350 680 N ATOM 1227 CA GLN A 194 -54.710 18.032 0.407 1.00 61.24 C ANISOU 1227 CA GLN A 194 7134 7321 8812 169 397 759 C ATOM 1228 C GLN A 194 -54.821 16.512 0.550 1.00 79.63 C ANISOU 1228 C GLN A 194 9409 9673 11174 160 384 767 C ATOM 1229 O GLN A 194 -55.567 16.019 1.399 1.00 89.68 O ANISOU 1229 O GLN A 194 10657 10944 12472 179 431 791 O ATOM 1230 CB GLN A 194 -55.736 18.572 -0.587 1.00 47.51 C ANISOU 1230 CB GLN A 194 5388 5529 7134 134 310 784 C ATOM 1231 CG GLN A 194 -56.000 20.055 -0.389 1.00 83.14 C ANISOU 1231 CG GLN A 194 10000 10002 11588 150 331 774 C ATOM 1232 CD GLN A 194 -56.738 20.670 -1.550 1.00126.53 C ANISOU 1232 CD GLN A 194 15519 15443 17112 111 227 784 C ATOM 1233 OE1 GLN A 194 -56.861 20.060 -2.613 1.00148.50 O ANISOU 1233 OE1 GLN A 194 18268 18222 19934 69 125 785 O ATOM 1234 NE2 GLN A 194 -57.233 21.886 -1.359 1.00136.70 N ANISOU 1234 NE2 GLN A 194 16868 16688 18382 127 253 793 N ATOM 1235 N ASP A 195 -54.095 15.775 -0.285 1.00 93.44 N ANISOU 1235 N ASP A 195 11165 11436 12902 129 312 740 N ATOM 1236 CA ASP A 195 -54.029 14.320 -0.167 1.00120.40 C ANISOU 1236 CA ASP A 195 14566 14865 16314 122 298 734 C ATOM 1237 C ASP A 195 -53.152 13.917 1.022 1.00149.68 C ANISOU 1237 C ASP A 195 18332 18612 19927 156 370 699 C ATOM 1238 O ASP A 195 -51.959 14.230 1.053 1.00148.52 O ANISOU 1238 O ASP A 195 18247 18489 19695 162 377 655 O ATOM 1239 CB ASP A 195 -53.500 13.705 -1.466 1.00112.53 C ANISOU 1239 CB ASP A 195 13567 13868 15323 80 200 716 C ATOM 1240 CG ASP A 195 -53.093 12.252 -1.305 1.00118.86 C ANISOU 1240 CG ASP A 195 14372 14687 16103 80 203 704 C ATOM 1241 OD1 ASP A 195 -53.789 11.507 -0.582 1.00115.15 O ANISOU 1241 OD1 ASP A 195 13869 14213 15668 95 244 729 O ATOM 1242 OD2 ASP A 195 -52.071 11.851 -1.905 1.00127.99 O ANISOU 1242 OD2 ASP A 195 15561 15859 17212 65 165 671 O ATOM 1243 N PRO A 196 -53.748 13.224 2.010 1.00144.89 N ANISOU 1243 N PRO A 196 17705 18009 19337 175 416 719 N ATOM 1244 CA PRO A 196 -53.029 12.811 3.224 1.00126.54 C ANISOU 1244 CA PRO A 196 15430 15719 16931 202 468 689 C ATOM 1245 C PRO A 196 -51.850 11.884 2.923 1.00107.96 C ANISOU 1245 C PRO A 196 13107 13391 14521 190 437 651 C ATOM 1246 O PRO A 196 -50.926 11.778 3.731 1.00111.66 O ANISOU 1246 O PRO A 196 13627 13889 14908 207 463 615 O ATOM 1247 CB PRO A 196 -54.098 12.057 4.027 1.00 92.17 C ANISOU 1247 CB PRO A 196 11027 11357 12638 214 501 732 C ATOM 1248 CG PRO A 196 -55.404 12.578 3.517 1.00 81.21 C ANISOU 1248 CG PRO A 196 9577 9930 11349 205 491 781 C ATOM 1249 CD PRO A 196 -55.176 12.858 2.060 1.00106.00 C ANISOU 1249 CD PRO A 196 12707 13054 14514 170 416 774 C ATOM 1250 N GLY A 197 -51.889 11.233 1.764 1.00 87.68 N ANISOU 1250 N GLY A 197 10506 10810 11999 160 378 660 N ATOM 1251 CA GLY A 197 -50.896 10.238 1.398 1.00 80.79 C ANISOU 1251 CA GLY A 197 9654 9956 11088 150 353 633 C ATOM 1252 C GLY A 197 -49.602 10.783 0.824 1.00 83.59 C ANISOU 1252 C GLY A 197 10065 10329 11368 143 330 587 C ATOM 1253 O GLY A 197 -48.665 10.020 0.564 1.00 58.05 O ANISOU 1253 O GLY A 197 6852 7110 8095 138 316 563 O ATOM 1254 N CYS A 198 -49.537 12.094 0.614 1.00 87.51 N ANISOU 1254 N CYS A 198 10583 10819 11848 144 330 579 N ATOM 1255 CA CYS A 198 -48.289 12.694 0.166 1.00 64.52 C ANISOU 1255 CA CYS A 198 7728 7924 8864 141 316 537 C ATOM 1256 C CYS A 198 -47.680 13.568 1.251 1.00 85.59 C ANISOU 1256 C CYS A 198 10461 10611 11450 173 374 504 C ATOM 1257 O CYS A 198 -48.171 14.664 1.528 1.00 94.54 O ANISOU 1257 O CYS A 198 11602 11728 12589 187 403 515 O ATOM 1258 CB CYS A 198 -48.513 13.527 -1.093 1.00 15.81 C ANISOU 1258 CB CYS A 198 1536 1730 2741 111 254 551 C ATOM 1259 SG CYS A 198 -46.975 14.071 -1.863 1.00172.76 S ANISOU 1259 SG CYS A 198 21576 21607 22459 86 184 469 S ATOM 1260 N CYS A 199 -46.612 13.079 1.872 1.00 81.73 N ANISOU 1260 N CYS A 199 10019 10151 10885 184 385 464 N ATOM 1261 CA CYS A 199 -45.826 13.926 2.750 1.00 78.24 C ANISOU 1261 CA CYS A 199 9645 9724 10360 204 414 424 C ATOM 1262 C CYS A 199 -44.615 14.409 1.992 1.00 90.85 C ANISOU 1262 C CYS A 199 11295 11327 11898 196 393 384 C ATOM 1263 O CYS A 199 -43.753 15.093 2.537 1.00110.43 O ANISOU 1263 O CYS A 199 13841 13814 14302 208 405 343 O ATOM 1264 CB CYS A 199 -45.420 13.222 4.034 1.00 84.19 C ANISOU 1264 CB CYS A 199 10411 10502 11077 217 429 407 C ATOM 1265 SG CYS A 199 -45.180 14.413 5.367 1.00 70.27 S ANISOU 1265 SG CYS A 199 8703 8741 9254 242 463 382 S ATOM 1266 N ASP A 200 -44.560 14.038 0.720 1.00 85.70 N ANISOU 1266 N ASP A 200 10612 10666 11283 174 356 398 N ATOM 1267 CA ASP A 200 -43.499 14.501 -0.145 1.00 68.85 C ANISOU 1267 CA ASP A 200 8567 8524 9067 149 300 351 C ATOM 1268 C ASP A 200 -43.423 16.010 0.039 1.00 60.32 C ANISOU 1268 C ASP A 200 7594 7419 7904 140 282 314 C ATOM 1269 O ASP A 200 -44.426 16.724 -0.057 1.00 14.94 O ANISOU 1269 O ASP A 200 1855 1642 2179 131 269 335 O ATOM 1270 CB ASP A 200 -43.846 14.159 -1.587 1.00 75.67 C ANISOU 1270 CB ASP A 200 9454 9358 9941 97 197 354 C ATOM 1271 CG ASP A 200 -42.630 13.998 -2.456 1.00 98.44 C ANISOU 1271 CG ASP A 200 12428 12239 12734 66 132 303 C ATOM 1272 OD1 ASP A 200 -41.580 14.593 -2.133 1.00110.68 O ANISOU 1272 OD1 ASP A 200 14052 13800 14201 68 137 258 O ATOM 1273 OD2 ASP A 200 -42.730 13.271 -3.467 1.00 90.98 O ANISOU 1273 OD2 ASP A 200 11479 11282 11808 41 77 309 O ATOM 1274 N PHE A 201 -42.226 16.502 0.315 1.00 92.23 N ANISOU 1274 N PHE A 201 11716 11471 11856 142 283 260 N ATOM 1275 CA PHE A 201 -42.095 17.878 0.748 1.00108.39 C ANISOU 1275 CA PHE A 201 13850 13500 13832 140 287 225 C ATOM 1276 C PHE A 201 -41.929 18.758 -0.464 1.00101.07 C ANISOU 1276 C PHE A 201 13016 12545 12842 76 177 195 C ATOM 1277 O PHE A 201 -40.919 18.706 -1.166 1.00135.02 O ANISOU 1277 O PHE A 201 17358 16859 17086 49 130 152 O ATOM 1278 CB PHE A 201 -40.887 18.026 1.670 1.00117.64 C ANISOU 1278 CB PHE A 201 15056 14695 14945 174 342 177 C ATOM 1279 CG PHE A 201 -40.873 19.300 2.454 1.00 85.52 C ANISOU 1279 CG PHE A 201 11066 10609 10819 189 376 142 C ATOM 1280 CD1 PHE A 201 -41.775 19.498 3.485 1.00 83.15 C ANISOU 1280 CD1 PHE A 201 10720 10307 10567 221 430 181 C ATOM 1281 CD2 PHE A 201 -39.946 20.291 2.177 1.00 46.97 C ANISOU 1281 CD2 PHE A 201 6291 5717 5840 147 313 72 C ATOM 1282 CE1 PHE A 201 -41.762 20.664 4.221 1.00 82.06 C ANISOU 1282 CE1 PHE A 201 10651 10150 10377 220 435 153 C ATOM 1283 CE2 PHE A 201 -39.929 21.460 2.914 1.00 54.16 C ANISOU 1283 CE2 PHE A 201 7244 6618 6717 135 302 52 C ATOM 1284 CZ PHE A 201 -40.841 21.648 3.935 1.00 66.76 C ANISOU 1284 CZ PHE A 201 8813 8201 8351 179 374 89 C ATOM 1285 N VAL A 202 -42.941 19.574 -0.700 1.00 55.43 N ANISOU 1285 N VAL A 202 7252 6730 7078 60 151 219 N ATOM 1286 CA VAL A 202 -42.898 20.534 -1.780 1.00 48.98 C ANISOU 1286 CA VAL A 202 6495 5897 6217 17 78 197 C ATOM 1287 C VAL A 202 -43.252 21.872 -1.172 1.00 57.35 C ANISOU 1287 C VAL A 202 7622 6939 7228 29 117 176 C ATOM 1288 O VAL A 202 -44.211 21.982 -0.412 1.00 58.08 O ANISOU 1288 O VAL A 202 7677 7009 7380 57 163 222 O ATOM 1289 CB VAL A 202 -43.887 20.167 -2.899 1.00 66.50 C ANISOU 1289 CB VAL A 202 8649 8085 8533 -13 4 262 C ATOM 1290 CG1 VAL A 202 -45.242 19.822 -2.313 1.00 70.94 C ANISOU 1290 CG1 VAL A 202 9224 8607 9122 5 27 292 C ATOM 1291 CG2 VAL A 202 -43.995 21.296 -3.915 1.00 61.21 C ANISOU 1291 CG2 VAL A 202 8069 7407 7782 -31 -19 214 C ATOM 1292 N THR A 203 -42.464 22.888 -1.489 1.00 52.76 N ANISOU 1292 N THR A 203 7162 6368 6515 7 96 89 N ATOM 1293 CA THR A 203 -42.636 24.179 -0.856 1.00 35.24 C ANISOU 1293 CA THR A 203 5030 4130 4231 15 133 56 C ATOM 1294 C THR A 203 -42.653 25.330 -1.844 1.00 33.15 C ANISOU 1294 C THR A 203 4872 3855 3868 -33 62 4 C ATOM 1295 O THR A 203 -42.227 25.196 -2.994 1.00 14.71 O ANISOU 1295 O THR A 203 2500 1552 1536 -71 -19 -5 O ATOM 1296 CB THR A 203 -41.523 24.432 0.153 1.00 17.65 C ANISOU 1296 CB THR A 203 2830 1927 1951 28 169 0 C ATOM 1297 OG1 THR A 203 -40.258 24.144 -0.461 1.00 46.70 O ANISOU 1297 OG1 THR A 203 6432 5662 5648 -9 91 -19 O ATOM 1298 CG2 THR A 203 -41.718 23.545 1.365 1.00 5.10 C ANISOU 1298 CG2 THR A 203 1186 334 419 93 272 36 C ATOM 1299 N ASN A 204 -43.132 26.472 -1.364 1.00 29.55 N ANISOU 1299 N ASN A 204 4479 3370 3380 -25 96 -1 N ATOM 1300 CA ASN A 204 -43.212 27.692 -2.154 1.00 38.27 C ANISOU 1300 CA ASN A 204 5602 4477 4460 -63 34 -11 C ATOM 1301 C ASN A 204 -41.837 28.231 -2.516 1.00 42.66 C ANISOU 1301 C ASN A 204 6051 5110 5049 -83 -6 -33 C ATOM 1302 O ASN A 204 -40.822 27.803 -1.975 1.00 13.17 O ANISOU 1302 O ASN A 204 2297 1316 1392 -87 10 -1 O ATOM 1303 CB ASN A 204 -44.029 28.762 -1.428 1.00 42.09 C ANISOU 1303 CB ASN A 204 6178 4907 4908 -42 96 -6 C ATOM 1304 CG ASN A 204 -43.745 28.803 0.059 1.00 35.50 C ANISOU 1304 CG ASN A 204 5319 4077 4093 0 182 -7 C ATOM 1305 OD1 ASN A 204 -42.733 29.342 0.494 1.00 26.31 O ANISOU 1305 OD1 ASN A 204 4098 2958 2941 -18 154 -27 O ATOM 1306 ND2 ASN A 204 -44.645 28.239 0.847 1.00 29.72 N ANISOU 1306 ND2 ASN A 204 4547 3315 3431 56 272 49 N ATOM 1307 N ARG A 205 -41.806 29.140 -3.476 1.00 71.30 N ANISOU 1307 N ARG A 205 9718 8737 8635 -110 -43 5 N ATOM 1308 CA ARG A 205 -40.550 29.724 -3.906 1.00 91.26 C ANISOU 1308 CA ARG A 205 12276 11160 11240 -152 -57 8 C ATOM 1309 C ARG A 205 -39.656 30.096 -2.711 1.00 61.17 C ANISOU 1309 C ARG A 205 8483 7339 7419 -151 -23 3 C ATOM 1310 O ARG A 205 -38.602 29.494 -2.506 1.00 6.50 O ANISOU 1310 O ARG A 205 1533 431 506 -155 -22 3 O ATOM 1311 CB ARG A 205 -40.812 30.936 -4.818 1.00126.53 C ANISOU 1311 CB ARG A 205 16800 15595 15680 -180 -85 12 C ATOM 1312 CG ARG A 205 -41.417 32.181 -4.143 1.00117.13 C ANISOU 1312 CG ARG A 205 15671 14482 14352 -163 -67 9 C ATOM 1313 CD ARG A 205 -42.911 32.063 -3.818 1.00112.77 C ANISOU 1313 CD ARG A 205 15109 13931 13808 -134 -50 6 C ATOM 1314 NE ARG A 205 -43.397 33.280 -3.166 1.00101.18 N ANISOU 1314 NE ARG A 205 13703 12319 12423 -140 -14 1 N ATOM 1315 CZ ARG A 205 -44.053 34.259 -3.786 1.00 80.35 C ANISOU 1315 CZ ARG A 205 11146 9738 9646 -149 -41 -36 C ATOM 1316 NH1 ARG A 205 -44.441 35.335 -3.109 1.00 50.19 N ANISOU 1316 NH1 ARG A 205 7413 5873 5785 -143 0 -39 N ATOM 1317 NH2 ARG A 205 -44.326 34.161 -5.082 1.00 69.48 N ANISOU 1317 NH2 ARG A 205 9767 8361 8270 -172 -103 -26 N ATOM 1318 N ALA A 206 -40.110 31.054 -1.906 1.00 78.72 N ANISOU 1318 N ALA A 206 10752 9535 9622 -145 4 0 N ATOM 1319 CA ALA A 206 -39.287 31.681 -0.867 1.00 70.28 C ANISOU 1319 CA ALA A 206 9719 8446 8537 -154 29 -3 C ATOM 1320 C ALA A 206 -39.122 30.921 0.464 1.00 54.77 C ANISOU 1320 C ALA A 206 7723 6600 6488 -112 72 -7 C ATOM 1321 O ALA A 206 -38.253 31.263 1.263 1.00 60.81 O ANISOU 1321 O ALA A 206 8511 7248 7347 -136 78 -8 O ATOM 1322 CB ALA A 206 -39.767 33.105 -0.609 1.00 75.39 C ANISOU 1322 CB ALA A 206 10441 9051 9152 -165 42 -5 C ATOM 1323 N TYR A 207 -39.949 29.918 0.731 1.00 44.09 N ANISOU 1323 N TYR A 207 6317 5265 5170 -76 95 -7 N ATOM 1324 CA TYR A 207 -39.669 29.058 1.873 1.00 17.23 C ANISOU 1324 CA TYR A 207 2879 1782 1887 -53 122 -6 C ATOM 1325 C TYR A 207 -38.533 28.118 1.482 1.00 46.38 C ANISOU 1325 C TYR A 207 6528 5502 5594 -67 93 -6 C ATOM 1326 O TYR A 207 -37.757 27.666 2.326 1.00 6.79 O ANISOU 1326 O TYR A 207 1497 579 504 -54 116 -6 O ATOM 1327 CB TYR A 207 -40.903 28.268 2.307 1.00 20.26 C ANISOU 1327 CB TYR A 207 3219 2180 2298 -2 166 0 C ATOM 1328 CG TYR A 207 -40.658 27.400 3.520 1.00 64.05 C ANISOU 1328 CG TYR A 207 8725 7738 7872 35 210 8 C ATOM 1329 CD1 TYR A 207 -40.973 27.853 4.795 1.00 54.98 C ANISOU 1329 CD1 TYR A 207 7594 6634 6663 70 280 -23 C ATOM 1330 CD2 TYR A 207 -40.099 26.133 3.391 1.00 47.94 C ANISOU 1330 CD2 TYR A 207 6627 5731 5857 42 200 10 C ATOM 1331 CE1 TYR A 207 -40.748 27.069 5.902 1.00 46.52 C ANISOU 1331 CE1 TYR A 207 6486 5567 5622 104 322 -8 C ATOM 1332 CE2 TYR A 207 -39.869 25.341 4.492 1.00 47.98 C ANISOU 1332 CE2 TYR A 207 6593 5799 5838 83 260 -9 C ATOM 1333 CZ TYR A 207 -40.194 25.814 5.747 1.00 59.54 C ANISOU 1333 CZ TYR A 207 8075 7243 7303 111 311 0 C ATOM 1334 OH TYR A 207 -39.962 25.028 6.852 1.00 68.94 O ANISOU 1334 OH TYR A 207 9225 8441 8528 147 350 20 O ATOM 1335 N ALA A 208 -38.424 27.867 0.181 1.00 42.24 N ANISOU 1335 N ALA A 208 5988 5074 4986 -80 59 -5 N ATOM 1336 CA ALA A 208 -37.379 27.014 -0.359 1.00 38.93 C ANISOU 1336 CA ALA A 208 5531 4594 4665 -100 31 -3 C ATOM 1337 C ALA A 208 -36.109 27.842 -0.505 1.00 30.47 C ANISOU 1337 C ALA A 208 4502 3590 3487 -127 16 -2 C ATOM 1338 O ALA A 208 -35.107 27.381 -1.044 1.00 52.01 O ANISOU 1338 O ALA A 208 7208 6246 6306 -154 -3 0 O ATOM 1339 CB ALA A 208 -37.798 26.426 -1.689 1.00 68.62 C ANISOU 1339 CB ALA A 208 9265 8371 8436 -105 1 0 C ATOM 1340 N ILE A 209 -36.181 29.085 -0.040 1.00 26.08 N ANISOU 1340 N ILE A 209 4004 3009 2896 -142 26 -4 N ATOM 1341 CA ILE A 209 -35.013 29.955 0.103 1.00 39.97 C ANISOU 1341 CA ILE A 209 5807 4656 4725 -196 16 -3 C ATOM 1342 C ILE A 209 -34.652 30.159 1.582 1.00 33.44 C ANISOU 1342 C ILE A 209 4998 3817 3892 -192 43 -7 C ATOM 1343 O ILE A 209 -33.556 29.799 2.032 1.00 24.55 O ANISOU 1343 O ILE A 209 3861 2800 2667 -187 45 -8 O ATOM 1344 CB ILE A 209 -35.271 31.320 -0.541 1.00 53.67 C ANISOU 1344 CB ILE A 209 7611 6465 6317 -209 4 -1 C ATOM 1345 CG1 ILE A 209 -35.463 31.162 -2.053 1.00 63.73 C ANISOU 1345 CG1 ILE A 209 8874 7746 7596 -218 -29 5 C ATOM 1346 CG2 ILE A 209 -34.145 32.292 -0.207 1.00 33.69 C ANISOU 1346 CG2 ILE A 209 5131 3803 3868 -274 3 -1 C ATOM 1347 CD1 ILE A 209 -35.987 32.409 -2.730 1.00 90.17 C ANISOU 1347 CD1 ILE A 209 12284 11070 10906 -240 -43 8 C ATOM 1348 N ALA A 210 -35.578 30.757 2.326 1.00 31.63 N ANISOU 1348 N ALA A 210 4804 3670 3545 -159 76 -10 N ATOM 1349 CA ALA A 210 -35.414 30.971 3.758 1.00 33.38 C ANISOU 1349 CA ALA A 210 5047 3769 3867 -165 100 -13 C ATOM 1350 C ALA A 210 -34.961 29.700 4.452 1.00 49.82 C ANISOU 1350 C ALA A 210 7071 5881 5979 -137 110 -13 C ATOM 1351 O ALA A 210 -33.988 29.708 5.218 1.00 59.52 O ANISOU 1351 O ALA A 210 8309 7104 7200 -154 111 -14 O ATOM 1352 CB ALA A 210 -36.720 31.447 4.367 1.00 26.91 C ANISOU 1352 CB ALA A 210 4255 3039 2930 -121 149 -15 C ATOM 1353 N SER A 211 -35.655 28.605 4.157 1.00 52.01 N ANISOU 1353 N SER A 211 7289 6281 6193 -89 127 -11 N ATOM 1354 CA SER A 211 -35.378 27.339 4.813 1.00 54.41 C ANISOU 1354 CA SER A 211 7537 6517 6619 -64 132 -9 C ATOM 1355 C SER A 211 -33.876 27.103 4.775 1.00 50.63 C ANISOU 1355 C SER A 211 7051 6048 6137 -96 107 -10 C ATOM 1356 O SER A 211 -33.232 26.959 5.817 1.00 48.77 O ANISOU 1356 O SER A 211 6820 5894 5816 -86 130 -12 O ATOM 1357 CB SER A 211 -36.118 26.205 4.084 1.00 72.79 C ANISOU 1357 CB SER A 211 9802 8957 8899 -31 145 -5 C ATOM 1358 OG SER A 211 -35.867 24.926 4.644 1.00 87.12 O ANISOU 1358 OG SER A 211 11561 10790 10749 0 166 0 O ATOM 1359 N SER A 212 -33.321 27.134 3.567 1.00 52.34 N ANISOU 1359 N SER A 212 7261 6359 6265 -116 80 -10 N ATOM 1360 CA SER A 212 -31.935 26.739 3.310 1.00 66.55 C ANISOU 1360 CA SER A 212 9043 8090 8152 -153 52 -8 C ATOM 1361 C SER A 212 -30.892 27.737 3.815 1.00 57.28 C ANISOU 1361 C SER A 212 7921 6894 6950 -201 45 -9 C ATOM 1362 O SER A 212 -29.881 27.353 4.422 1.00 18.86 O ANISOU 1362 O SER A 212 3046 2124 1995 -195 47 -10 O ATOM 1363 CB SER A 212 -31.744 26.520 1.809 1.00 74.05 C ANISOU 1363 CB SER A 212 9976 9053 9106 -168 25 -4 C ATOM 1364 OG SER A 212 -32.766 25.682 1.289 1.00 85.47 O ANISOU 1364 OG SER A 212 11384 10592 10500 -121 32 -5 O ATOM 1365 N ILE A 213 -31.128 29.017 3.541 1.00 64.39 N ANISOU 1365 N ILE A 213 8881 7765 7821 -234 42 -8 N ATOM 1366 CA ILE A 213 -30.264 30.050 4.083 1.00 36.94 C ANISOU 1366 CA ILE A 213 5465 4369 4201 -262 43 -10 C ATOM 1367 C ILE A 213 -30.122 29.843 5.574 1.00 28.35 C ANISOU 1367 C ILE A 213 4376 3170 3224 -274 60 -13 C ATOM 1368 O ILE A 213 -29.031 29.547 6.057 1.00 22.00 O ANISOU 1368 O ILE A 213 3562 2377 2419 -300 53 -13 O ATOM 1369 CB ILE A 213 -30.818 31.445 3.845 1.00 7.93 C ANISOU 1369 CB ILE A 213 1861 668 484 -286 46 -11 C ATOM 1370 CG1 ILE A 213 -30.202 32.038 2.579 1.00 86.08 C ANISOU 1370 CG1 ILE A 213 11774 10448 10483 -358 17 -4 C ATOM 1371 CG2 ILE A 213 -30.493 32.340 5.014 1.00 8.54 C ANISOU 1371 CG2 ILE A 213 1992 600 651 -345 58 -14 C ATOM 1372 CD1 ILE A 213 -30.539 33.497 2.362 1.00105.25 C ANISOU 1372 CD1 ILE A 213 14288 12966 12737 -361 21 -5 C ATOM 1373 N ILE A 214 -31.232 29.975 6.299 1.00 43.18 N ANISOU 1373 N ILE A 214 6274 5138 4995 -216 97 -18 N ATOM 1374 CA ILE A 214 -31.181 29.919 7.760 1.00 57.29 C ANISOU 1374 CA ILE A 214 8074 6803 6889 -223 114 -19 C ATOM 1375 C ILE A 214 -30.688 28.582 8.317 1.00 65.57 C ANISOU 1375 C ILE A 214 9064 7882 7968 -191 117 -18 C ATOM 1376 O ILE A 214 -29.647 28.522 8.974 1.00 7.01 O ANISOU 1376 O ILE A 214 1654 467 543 -222 109 -20 O ATOM 1377 CB ILE A 214 -32.536 30.283 8.396 1.00 30.66 C ANISOU 1377 CB ILE A 214 4731 3519 3401 -165 166 -22 C ATOM 1378 CG1 ILE A 214 -32.732 31.806 8.366 1.00 29.68 C ANISOU 1378 CG1 ILE A 214 4690 3363 3224 -203 169 -25 C ATOM 1379 CG2 ILE A 214 -32.594 29.773 9.822 1.00 7.61 C ANISOU 1379 CG2 ILE A 214 1806 593 493 -132 201 -22 C ATOM 1380 CD1 ILE A 214 -34.130 32.284 7.994 1.00 8.54 C ANISOU 1380 CD1 ILE A 214 2029 543 671 -190 176 -22 C ATOM 1381 N SER A 215 -31.399 27.503 8.012 1.00 71.80 N ANISOU 1381 N SER A 215 9794 8695 8790 -135 128 -15 N ATOM 1382 CA SER A 215 -31.162 26.232 8.698 1.00 62.40 C ANISOU 1382 CA SER A 215 8551 7616 7544 -83 157 -14 C ATOM 1383 C SER A 215 -29.972 25.423 8.149 1.00 47.45 C ANISOU 1383 C SER A 215 6615 5745 5667 -100 125 -14 C ATOM 1384 O SER A 215 -29.626 24.370 8.692 1.00 5.08 O ANISOU 1384 O SER A 215 1209 392 330 -68 138 -11 O ATOM 1385 CB SER A 215 -32.446 25.389 8.722 1.00 68.00 C ANISOU 1385 CB SER A 215 9213 8334 8290 -20 195 -4 C ATOM 1386 OG SER A 215 -33.551 26.122 9.248 1.00 50.14 O ANISOU 1386 OG SER A 215 6987 6051 6013 -2 230 -1 O ATOM 1387 N PHE A 216 -29.359 25.907 7.068 1.00 21.99 N ANISOU 1387 N PHE A 216 3400 2444 2510 -160 81 -13 N ATOM 1388 CA PHE A 216 -28.160 25.261 6.508 1.00 55.19 C ANISOU 1388 CA PHE A 216 7570 6676 6725 -182 56 -11 C ATOM 1389 C PHE A 216 -26.999 26.185 6.196 1.00 60.30 C ANISOU 1389 C PHE A 216 8257 7401 7253 -235 33 -9 C ATOM 1390 O PHE A 216 -25.900 26.005 6.710 1.00 88.47 O ANISOU 1390 O PHE A 216 11812 10897 10904 -289 20 -6 O ATOM 1391 CB PHE A 216 -28.454 24.421 5.266 1.00 65.88 C ANISOU 1391 CB PHE A 216 8878 8125 8028 -143 52 -10 C ATOM 1392 CG PHE A 216 -27.278 23.578 4.813 1.00 64.80 C ANISOU 1392 CG PHE A 216 8704 8009 7908 -154 33 -7 C ATOM 1393 CD1 PHE A 216 -27.236 22.214 5.085 1.00 73.01 C ANISOU 1393 CD1 PHE A 216 9690 9003 9047 -121 43 -7 C ATOM 1394 CD2 PHE A 216 -26.216 24.148 4.127 1.00 57.77 C ANISOU 1394 CD2 PHE A 216 7828 7054 7069 -224 6 -2 C ATOM 1395 CE1 PHE A 216 -26.164 21.429 4.670 1.00 53.97 C ANISOU 1395 CE1 PHE A 216 7246 6613 6647 -129 29 -6 C ATOM 1396 CE2 PHE A 216 -25.139 23.369 3.711 1.00 80.98 C ANISOU 1396 CE2 PHE A 216 10731 10017 10019 -234 -7 2 C ATOM 1397 CZ PHE A 216 -25.114 22.008 3.984 1.00 65.64 C ANISOU 1397 CZ PHE A 216 8744 8153 8045 -171 3 -1 C ATOM 1398 N TYR A 217 -27.220 27.141 5.308 1.00 6.25 N ANISOU 1398 N TYR A 217 1441 457 475 -286 21 -6 N ATOM 1399 CA TYR A 217 -26.087 27.820 4.716 1.00 43.11 C ANISOU 1399 CA TYR A 217 6143 5221 5017 -322 1 0 C ATOM 1400 C TYR A 217 -25.336 28.729 5.675 1.00 23.67 C ANISOU 1400 C TYR A 217 3718 2652 2623 -414 0 0 C ATOM 1401 O TYR A 217 -24.180 28.460 5.997 1.00 35.98 O ANISOU 1401 O TYR A 217 5273 4334 4063 -415 -13 5 O ATOM 1402 CB TYR A 217 -26.483 28.552 3.438 1.00 54.60 C ANISOU 1402 CB TYR A 217 7616 6570 6561 -366 -8 2 C ATOM 1403 CG TYR A 217 -26.183 27.726 2.216 1.00 71.51 C ANISOU 1403 CG TYR A 217 9713 8736 8723 -351 -21 7 C ATOM 1404 CD1 TYR A 217 -24.923 27.754 1.626 1.00 85.43 C ANISOU 1404 CD1 TYR A 217 11472 10512 10475 -396 -36 13 C ATOM 1405 CD2 TYR A 217 -27.145 26.887 1.674 1.00 57.33 C ANISOU 1405 CD2 TYR A 217 7878 6949 6955 -296 -16 5 C ATOM 1406 CE1 TYR A 217 -24.641 26.983 0.518 1.00104.11 C ANISOU 1406 CE1 TYR A 217 13814 12983 12759 -350 -49 18 C ATOM 1407 CE2 TYR A 217 -26.874 26.113 0.566 1.00 67.88 C ANISOU 1407 CE2 TYR A 217 9180 8305 8308 -285 -27 8 C ATOM 1408 CZ TYR A 217 -25.623 26.163 -0.009 1.00106.18 C ANISOU 1408 CZ TYR A 217 14041 13245 13058 -298 -44 15 C ATOM 1409 OH TYR A 217 -25.359 25.389 -1.115 1.00122.86 O ANISOU 1409 OH TYR A 217 16114 15291 15275 -313 -48 16 O ATOM 1410 N ILE A 218 -25.961 29.796 6.143 1.00 43.81 N ANISOU 1410 N ILE A 218 6415 4985 5247 -1905 -287 -875 N ATOM 1411 CA ILE A 218 -25.204 30.711 6.982 1.00 62.02 C ANISOU 1411 CA ILE A 218 8697 7235 7634 -1888 -358 -930 C ATOM 1412 C ILE A 218 -24.520 30.005 8.168 1.00 64.76 C ANISOU 1412 C ILE A 218 9043 7615 7947 -1879 -332 -949 C ATOM 1413 O ILE A 218 -23.339 30.239 8.404 1.00 80.17 O ANISOU 1413 O ILE A 218 10991 9551 9920 -1889 -358 -951 O ATOM 1414 CB ILE A 218 -25.996 31.987 7.371 1.00 53.05 C ANISOU 1414 CB ILE A 218 7534 6026 6596 -1858 -442 -1000 C ATOM 1415 CG1 ILE A 218 -25.160 33.227 7.028 1.00 66.50 C ANISOU 1415 CG1 ILE A 218 9225 7654 8388 -1868 -523 -1016 C ATOM 1416 CG2 ILE A 218 -26.398 31.957 8.837 1.00 31.39 C ANISOU 1416 CG2 ILE A 218 4778 3282 3867 -1819 -460 -1070 C ATOM 1417 CD1 ILE A 218 -25.909 34.542 7.122 1.00 84.05 C ANISOU 1417 CD1 ILE A 218 11427 9798 10710 -1843 -607 -1083 C ATOM 1418 N PRO A 219 -25.232 29.109 8.887 1.00 61.74 N ANISOU 1418 N PRO A 219 8666 7285 7509 -1867 -279 -957 N ATOM 1419 CA PRO A 219 -24.508 28.426 9.969 1.00 93.43 C ANISOU 1419 CA PRO A 219 12678 11330 11490 -1861 -253 -970 C ATOM 1420 C PRO A 219 -23.345 27.566 9.467 1.00104.69 C ANISOU 1420 C PRO A 219 14126 12797 12853 -1891 -200 -912 C ATOM 1421 O PRO A 219 -22.334 27.475 10.155 1.00132.81 O ANISOU 1421 O PRO A 219 17681 16359 16420 -1891 -210 -925 O ATOM 1422 CB PRO A 219 -25.586 27.565 10.646 1.00 29.31 C ANISOU 1422 CB PRO A 219 4560 3263 3315 -1851 -201 -978 C ATOM 1423 CG PRO A 219 -26.673 27.452 9.665 1.00 29.07 C ANISOU 1423 CG PRO A 219 4540 3245 3261 -1863 -177 -944 C ATOM 1424 CD PRO A 219 -26.647 28.704 8.837 1.00 55.13 C ANISOU 1424 CD PRO A 219 7831 6478 6638 -1860 -245 -955 C ATOM 1425 N LEU A 220 -23.474 26.955 8.292 1.00 93.82 N ANISOU 1425 N LEU A 220 12777 11453 11417 -1916 -151 -852 N ATOM 1426 CA LEU A 220 -22.379 26.161 7.739 1.00 74.36 C ANISOU 1426 CA LEU A 220 10336 9024 8892 -1940 -107 -803 C ATOM 1427 C LEU A 220 -21.180 27.025 7.403 1.00 63.80 C ANISOU 1427 C LEU A 220 8984 7647 7610 -1953 -162 -803 C ATOM 1428 O LEU A 220 -20.072 26.753 7.843 1.00 51.39 O ANISOU 1428 O LEU A 220 7408 6088 6028 -1960 -159 -802 O ATOM 1429 CB LEU A 220 -22.801 25.417 6.477 1.00 61.96 C ANISOU 1429 CB LEU A 220 8804 7490 7248 -1961 -54 -744 C ATOM 1430 CG LEU A 220 -21.583 25.090 5.612 1.00 59.10 C ANISOU 1430 CG LEU A 220 8462 7143 6851 -1984 -38 -703 C ATOM 1431 CD1 LEU A 220 -20.711 24.059 6.308 1.00 50.96 C ANISOU 1431 CD1 LEU A 220 7441 6153 5768 -1985 6 -698 C ATOM 1432 CD2 LEU A 220 -21.992 24.616 4.228 1.00 80.19 C ANISOU 1432 CD2 LEU A 220 11172 9836 9461 -2003 -4 -652 C ATOM 1433 N LEU A 221 -21.406 28.057 6.599 1.00 62.79 N ANISOU 1433 N LEU A 221 8846 7472 7539 -1960 -215 -801 N ATOM 1434 CA LEU A 221 -20.330 28.929 6.160 1.00 74.85 C ANISOU 1434 CA LEU A 221 10359 8960 9120 -1981 -273 -793 C ATOM 1435 C LEU A 221 -19.696 29.577 7.375 1.00 76.69 C ANISOU 1435 C LEU A 221 10565 9154 9419 -1970 -333 -845 C ATOM 1436 O LEU A 221 -18.508 29.903 7.379 1.00 69.52 O ANISOU 1436 O LEU A 221 9646 8233 8534 -1994 -366 -835 O ATOM 1437 CB LEU A 221 -20.867 29.995 5.210 1.00 51.91 C ANISOU 1437 CB LEU A 221 7445 6004 6274 -1990 -325 -788 C ATOM 1438 CG LEU A 221 -21.744 29.439 4.089 1.00 59.66 C ANISOU 1438 CG LEU A 221 8454 7019 7195 -1996 -273 -745 C ATOM 1439 CD1 LEU A 221 -22.159 30.551 3.142 1.00 90.49 C ANISOU 1439 CD1 LEU A 221 12348 10871 11162 -2007 -330 -737 C ATOM 1440 CD2 LEU A 221 -21.032 28.317 3.339 1.00 29.89 C ANISOU 1440 CD2 LEU A 221 4716 3312 3330 -2019 -207 -689 C ATOM 1441 N ILE A 222 -20.501 29.747 8.415 1.00 67.92 N ANISOU 1441 N ILE A 222 9444 8025 8336 -1937 -349 -900 N ATOM 1442 CA ILE A 222 -20.024 30.343 9.651 1.00 62.94 C ANISOU 1442 CA ILE A 222 8794 7357 7765 -1921 -409 -958 C ATOM 1443 C ILE A 222 -19.163 29.367 10.450 1.00 49.81 C ANISOU 1443 C ILE A 222 7135 5745 6046 -1924 -364 -951 C ATOM 1444 O ILE A 222 -18.151 29.768 11.004 1.00 84.63 O ANISOU 1444 O ILE A 222 11532 10132 10491 -1934 -410 -968 O ATOM 1445 CB ILE A 222 -21.184 30.905 10.520 1.00 84.05 C ANISOU 1445 CB ILE A 222 11456 9993 10488 -1879 -450 -1030 C ATOM 1446 CG1 ILE A 222 -21.739 32.206 9.911 1.00 78.55 C ANISOU 1446 CG1 ILE A 222 10748 9223 9876 -1874 -524 -1055 C ATOM 1447 CG2 ILE A 222 -20.750 31.096 11.974 1.00 31.97 C ANISOU 1447 CG2 ILE A 222 4849 3379 3921 -1856 -491 -1092 C ATOM 1448 CD1 ILE A 222 -20.691 33.205 9.430 1.00 53.93 C ANISOU 1448 CD1 ILE A 222 7620 6049 6823 -1906 -592 -1047 C ATOM 1449 N MET A 223 -19.545 28.095 10.514 1.00 30.07 N ANISOU 1449 N MET A 223 4653 3312 3460 -1920 -278 -925 N ATOM 1450 CA MET A 223 -18.768 27.145 11.311 1.00 37.92 C ANISOU 1450 CA MET A 223 5651 4353 4404 -1922 -234 -920 C ATOM 1451 C MET A 223 -17.565 26.578 10.564 1.00 52.02 C ANISOU 1451 C MET A 223 7450 6173 6144 -1954 -202 -866 C ATOM 1452 O MET A 223 -16.642 26.066 11.183 1.00 71.85 O ANISOU 1452 O MET A 223 9957 8709 8633 -1960 -187 -865 O ATOM 1453 CB MET A 223 -19.635 26.022 11.869 1.00 29.15 C ANISOU 1453 CB MET A 223 4553 3296 3226 -1906 -162 -920 C ATOM 1454 CG MET A 223 -20.018 25.007 10.841 1.00 39.63 C ANISOU 1454 CG MET A 223 5911 4672 4473 -1923 -87 -861 C ATOM 1455 SD MET A 223 -20.019 23.340 11.506 1.00 27.81 S ANISOU 1455 SD MET A 223 4436 3246 2883 -1926 0 -840 S ATOM 1456 CE MET A 223 -20.376 22.400 10.018 1.00119.56 C ANISOU 1456 CE MET A 223 16103 14903 14422 -1950 64 -771 C ATOM 1457 N ILE A 224 -17.587 26.654 9.238 1.00 60.17 N ANISOU 1457 N ILE A 224 8495 7207 7161 -1974 -191 -822 N ATOM 1458 CA ILE A 224 -16.415 26.330 8.426 1.00 75.24 C ANISOU 1458 CA ILE A 224 10411 9141 9036 -2006 -176 -776 C ATOM 1459 C ILE A 224 -15.449 27.509 8.465 1.00 83.13 C ANISOU 1459 C ILE A 224 11380 10091 10113 -2028 -260 -784 C ATOM 1460 O ILE A 224 -14.234 27.341 8.637 1.00 75.14 O ANISOU 1460 O ILE A 224 10359 9098 9094 -2051 -267 -770 O ATOM 1461 CB ILE A 224 -16.793 26.020 6.969 1.00 80.90 C ANISOU 1461 CB ILE A 224 11155 9878 9707 -2020 -139 -728 C ATOM 1462 CG1 ILE A 224 -16.890 24.506 6.765 1.00 91.36 C ANISOU 1462 CG1 ILE A 224 12516 11265 10930 -2018 -51 -698 C ATOM 1463 CG2 ILE A 224 -15.772 26.636 6.010 1.00 29.21 C ANISOU 1463 CG2 ILE A 224 4597 3318 3183 -2055 -179 -695 C ATOM 1464 CD1 ILE A 224 -17.699 23.785 7.825 1.00 27.77 C ANISOU 1464 CD1 ILE A 224 4469 3232 2850 -1993 -12 -723 C ATOM 1465 N PHE A 225 -16.010 28.704 8.305 1.00 81.43 N ANISOU 1465 N PHE A 225 11151 9814 9975 -2025 -328 -807 N ATOM 1466 CA PHE A 225 -15.278 29.946 8.508 1.00 78.91 C ANISOU 1466 CA PHE A 225 10806 9435 9743 -2047 -420 -824 C ATOM 1467 C PHE A 225 -14.570 29.923 9.867 1.00 81.63 C ANISOU 1467 C PHE A 225 11136 9774 10105 -2041 -446 -862 C ATOM 1468 O PHE A 225 -13.382 30.230 9.952 1.00 32.25 O ANISOU 1468 O PHE A 225 4867 3515 3871 -2075 -484 -847 O ATOM 1469 CB PHE A 225 -16.250 31.127 8.391 1.00 90.43 C ANISOU 1469 CB PHE A 225 12256 10822 11281 -2033 -484 -861 C ATOM 1470 CG PHE A 225 -15.677 32.457 8.804 1.00111.73 C ANISOU 1470 CG PHE A 225 14932 13447 14075 -2051 -585 -893 C ATOM 1471 CD1 PHE A 225 -15.077 33.290 7.875 1.00113.18 C ANISOU 1471 CD1 PHE A 225 15106 13600 14299 -2097 -634 -856 C ATOM 1472 CD2 PHE A 225 -15.783 32.893 10.116 1.00113.53 C ANISOU 1472 CD2 PHE A 225 15151 13635 14351 -2025 -633 -963 C ATOM 1473 CE1 PHE A 225 -14.569 34.519 8.255 1.00115.26 C ANISOU 1473 CE1 PHE A 225 15352 13795 14646 -2122 -727 -884 C ATOM 1474 CE2 PHE A 225 -15.279 34.120 10.502 1.00101.28 C ANISOU 1474 CE2 PHE A 225 13586 12013 12883 -2045 -727 -999 C ATOM 1475 CZ PHE A 225 -14.671 34.934 9.571 1.00110.71 C ANISOU 1475 CZ PHE A 225 14773 13178 14115 -2096 -773 -958 C ATOM 1476 N VAL A 226 -15.296 29.524 10.914 1.00 92.56 N ANISOU 1476 N VAL A 226 12525 11164 11478 -2001 -425 -909 N ATOM 1477 CA VAL A 226 -14.777 29.504 12.289 1.00 92.57 C ANISOU 1477 CA VAL A 226 12516 11160 11495 -1990 -452 -952 C ATOM 1478 C VAL A 226 -13.873 28.297 12.568 1.00 71.32 C ANISOU 1478 C VAL A 226 9830 8538 8729 -2002 -386 -920 C ATOM 1479 O VAL A 226 -12.987 28.362 13.418 1.00 88.32 O ANISOU 1479 O VAL A 226 11970 10689 10897 -2011 -416 -937 O ATOM 1480 CB VAL A 226 -15.922 29.599 13.350 1.00 31.93 C ANISOU 1480 CB VAL A 226 4838 3461 3834 -1942 -461 -1019 C ATOM 1481 CG1 VAL A 226 -15.403 29.348 14.752 1.00 32.12 C ANISOU 1481 CG1 VAL A 226 4854 3493 3856 -1928 -475 -1059 C ATOM 1482 CG2 VAL A 226 -16.584 30.958 13.289 1.00 32.73 C ANISOU 1482 CG2 VAL A 226 4929 3482 4024 -1928 -547 -1067 C ATOM 1483 N ALA A 227 -14.086 27.202 11.851 1.00 34.25 N ANISOU 1483 N ALA A 227 5155 3903 3954 -2003 -300 -876 N ATOM 1484 CA ALA A 227 -13.182 26.066 11.950 1.00 63.79 C ANISOU 1484 CA ALA A 227 8904 7706 7626 -2016 -241 -845 C ATOM 1485 C ALA A 227 -11.820 26.502 11.439 1.00 89.37 C ANISOU 1485 C ALA A 227 12127 10942 10886 -2058 -282 -814 C ATOM 1486 O ALA A 227 -10.782 26.159 12.010 1.00 91.37 O ANISOU 1486 O ALA A 227 12369 11220 11126 -2072 -283 -810 O ATOM 1487 CB ALA A 227 -13.698 24.903 11.135 1.00 78.63 C ANISOU 1487 CB ALA A 227 10814 9639 9421 -2011 -151 -807 C ATOM 1488 N LEU A 228 -11.835 27.282 10.364 1.00101.66 N ANISOU 1488 N LEU A 228 13679 12471 12476 -2081 -318 -788 N ATOM 1489 CA LEU A 228 -10.595 27.694 9.724 1.00 98.81 C ANISOU 1489 CA LEU A 228 13299 12114 12131 -2129 -356 -747 C ATOM 1490 C LEU A 228 -9.597 28.415 10.630 1.00111.05 C ANISOU 1490 C LEU A 228 14819 13635 13739 -2155 -432 -764 C ATOM 1491 O LEU A 228 -8.471 27.947 10.784 1.00125.87 O ANISOU 1491 O LEU A 228 16683 15553 15587 -2181 -422 -739 O ATOM 1492 CB LEU A 228 -10.883 28.517 8.474 1.00 88.00 C ANISOU 1492 CB LEU A 228 11927 10715 10794 -2152 -389 -717 C ATOM 1493 CG LEU A 228 -11.235 27.608 7.307 1.00 85.64 C ANISOU 1493 CG LEU A 228 11656 10467 10417 -2148 -312 -678 C ATOM 1494 CD1 LEU A 228 -10.733 28.225 6.009 1.00 93.62 C ANISOU 1494 CD1 LEU A 228 12655 11473 11444 -2192 -345 -628 C ATOM 1495 CD2 LEU A 228 -10.620 26.228 7.545 1.00 29.97 C ANISOU 1495 CD2 LEU A 228 4620 3485 3283 -2142 -238 -666 C ATOM 1496 N ARG A 229 -9.989 29.538 11.230 1.00111.37 N ANISOU 1496 N ARG A 229 14851 13605 13861 -2149 -509 -808 N ATOM 1497 CA ARG A 229 -9.043 30.285 12.065 1.00129.23 C ANISOU 1497 CA ARG A 229 17089 15833 16179 -2179 -588 -825 C ATOM 1498 C ARG A 229 -8.528 29.413 13.214 1.00148.85 C ANISOU 1498 C ARG A 229 19574 18360 18624 -2164 -556 -845 C ATOM 1499 O ARG A 229 -7.363 29.519 13.628 1.00182.39 O ANISOU 1499 O ARG A 229 23802 22618 22881 -2201 -591 -830 O ATOM 1500 CB ARG A 229 -9.634 31.605 12.589 1.00114.12 C ANISOU 1500 CB ARG A 229 15173 13831 14356 -2170 -676 -882 C ATOM 1501 CG ARG A 229 -8.569 32.562 13.151 1.00118.90 C ANISOU 1501 CG ARG A 229 15760 14395 15022 -2219 -769 -887 C ATOM 1502 CD ARG A 229 -9.146 33.833 13.786 1.00128.06 C ANISOU 1502 CD ARG A 229 16926 15465 16266 -2208 -855 -958 C ATOM 1503 NE ARG A 229 -8.085 34.760 14.192 1.00130.04 N ANISOU 1503 NE ARG A 229 17167 15678 16565 -2268 -943 -953 N ATOM 1504 CZ ARG A 229 -8.278 35.888 14.873 1.00110.23 C ANISOU 1504 CZ ARG A 229 14670 13093 14121 -2272 -1027 -1015 C ATOM 1505 NH1 ARG A 229 -9.500 36.249 15.242 1.00108.32 N ANISOU 1505 NH1 ARG A 229 14443 12804 13909 -2215 -1034 -1093 N ATOM 1506 NH2 ARG A 229 -7.244 36.657 15.190 1.00 85.50 N ANISOU 1506 NH2 ARG A 229 11537 9934 11017 -2338 -1104 -996 N ATOM 1507 N VAL A 230 -9.394 28.538 13.714 1.00114.80 N ANISOU 1507 N VAL A 230 15282 14073 14264 -2114 -489 -874 N ATOM 1508 CA VAL A 230 -8.983 27.576 14.730 1.00104.25 C ANISOU 1508 CA VAL A 230 13948 12783 12881 -2099 -447 -888 C ATOM 1509 C VAL A 230 -7.878 26.640 14.210 1.00 87.40 C ANISOU 1509 C VAL A 230 11808 10718 10682 -2129 -396 -832 C ATOM 1510 O VAL A 230 -6.883 26.412 14.901 1.00116.36 O ANISOU 1510 O VAL A 230 15459 14407 14344 -2147 -410 -831 O ATOM 1511 CB VAL A 230 -10.188 26.790 15.321 1.00 56.04 C ANISOU 1511 CB VAL A 230 7863 6696 6733 -2046 -383 -922 C ATOM 1512 CG1 VAL A 230 -9.745 25.452 15.901 1.00 37.06 C ANISOU 1512 CG1 VAL A 230 5466 4360 4257 -2038 -310 -912 C ATOM 1513 CG2 VAL A 230 -10.898 27.629 16.385 1.00 47.48 C ANISOU 1513 CG2 VAL A 230 6775 5553 5711 -2016 -447 -992 C ATOM 1514 N TYR A 231 -8.027 26.124 12.991 1.00 47.23 N ANISOU 1514 N TYR A 231 6733 5664 5547 -2134 -341 -789 N ATOM 1515 CA TYR A 231 -6.992 25.251 12.423 1.00 74.78 C ANISOU 1515 CA TYR A 231 10218 9218 8976 -2160 -296 -743 C ATOM 1516 C TYR A 231 -5.771 26.006 11.879 1.00102.93 C ANISOU 1516 C TYR A 231 13748 12782 12577 -2219 -361 -701 C ATOM 1517 O TYR A 231 -4.791 25.386 11.461 1.00100.19 O ANISOU 1517 O TYR A 231 13388 12492 12186 -2245 -335 -663 O ATOM 1518 CB TYR A 231 -7.571 24.305 11.365 1.00 94.83 C ANISOU 1518 CB TYR A 231 12790 11797 11444 -2143 -212 -717 C ATOM 1519 CG TYR A 231 -8.498 23.255 11.942 1.00117.83 C ANISOU 1519 CG TYR A 231 15734 14730 14305 -2098 -139 -742 C ATOM 1520 CD1 TYR A 231 -9.881 23.418 11.898 1.00119.93 C ANISOU 1520 CD1 TYR A 231 16019 14969 14579 -2068 -126 -762 C ATOM 1521 CD2 TYR A 231 -7.993 22.106 12.545 1.00109.77 C ANISOU 1521 CD2 TYR A 231 14721 13757 13230 -2089 -87 -743 C ATOM 1522 CE1 TYR A 231 -10.734 22.467 12.432 1.00101.64 C ANISOU 1522 CE1 TYR A 231 13727 12676 12217 -2036 -63 -776 C ATOM 1523 CE2 TYR A 231 -8.840 21.149 13.083 1.00106.93 C ANISOU 1523 CE2 TYR A 231 14388 13414 12827 -2055 -25 -759 C ATOM 1524 CZ TYR A 231 -10.209 21.336 13.023 1.00100.18 C ANISOU 1524 CZ TYR A 231 13549 12534 11979 -2032 -14 -773 C ATOM 1525 OH TYR A 231 -11.051 20.386 13.558 1.00 87.12 O ANISOU 1525 OH TYR A 231 11918 10901 10282 -2007 44 -781 O ATOM 1526 N ARG A 232 -5.848 27.335 11.857 1.00118.12 N ANISOU 1526 N ARG A 232 15656 14644 14581 -2242 -446 -706 N ATOM 1527 CA ARG A 232 -4.678 28.178 11.607 1.00115.18 C ANISOU 1527 CA ARG A 232 15245 14264 14253 -2308 -522 -665 C ATOM 1528 C ARG A 232 -3.867 28.366 12.877 1.00119.62 C ANISOU 1528 C ARG A 232 15788 14821 14843 -2325 -570 -686 C ATOM 1529 O ARG A 232 -2.634 28.337 12.850 1.00133.54 O ANISOU 1529 O ARG A 232 17518 16623 16600 -2376 -594 -642 O ATOM 1530 CB ARG A 232 -5.080 29.547 11.053 1.00125.42 C ANISOU 1530 CB ARG A 232 16537 15492 15625 -2332 -597 -660 C ATOM 1531 CG ARG A 232 -4.025 30.630 11.265 1.00129.88 C ANISOU 1531 CG ARG A 232 17067 16029 16252 -2401 -695 -631 C ATOM 1532 CD ARG A 232 -4.210 31.772 10.285 1.00118.54 C ANISOU 1532 CD ARG A 232 15625 14547 14868 -2440 -754 -598 C ATOM 1533 NE ARG A 232 -4.360 33.068 10.938 1.00117.63 N ANISOU 1533 NE ARG A 232 15512 14347 14834 -2459 -850 -632 N ATOM 1534 CZ ARG A 232 -4.212 34.225 10.302 1.00136.38 C ANISOU 1534 CZ ARG A 232 17881 16678 17261 -2513 -924 -596 C ATOM 1535 NH1 ARG A 232 -3.904 34.229 9.011 1.00149.80 N ANISOU 1535 NH1 ARG A 232 19563 18414 18939 -2552 -912 -522 N ATOM 1536 NH2 ARG A 232 -4.361 35.375 10.944 1.00139.95 N ANISOU 1536 NH2 ARG A 232 18345 17049 17779 -2530 -1011 -633 N ATOM 1537 N GLU A 233 -4.564 28.576 13.990 1.00115.27 N ANISOU 1537 N GLU A 233 15253 14223 14320 -2285 -587 -750 N ATOM 1538 CA GLU A 233 -3.875 28.763 15.258 1.00126.87 C ANISOU 1538 CA GLU A 233 16708 15683 15814 -2298 -635 -777 C ATOM 1539 C GLU A 233 -3.297 27.442 15.746 1.00134.22 C ANISOU 1539 C GLU A 233 17636 16688 16672 -2285 -565 -769 C ATOM 1540 O GLU A 233 -2.371 27.417 16.559 1.00152.96 O ANISOU 1540 O GLU A 233 19990 19077 19052 -2310 -598 -768 O ATOM 1541 CB GLU A 233 -4.812 29.348 16.312 1.00125.33 C ANISOU 1541 CB GLU A 233 16533 15420 15668 -2255 -675 -855 C ATOM 1542 CG GLU A 233 -4.124 30.320 17.266 1.00146.89 C ANISOU 1542 CG GLU A 233 19249 18101 18461 -2290 -773 -881 C ATOM 1543 CD GLU A 233 -4.319 31.771 16.865 1.00160.29 C ANISOU 1543 CD GLU A 233 20947 19721 20236 -2322 -862 -887 C ATOM 1544 OE1 GLU A 233 -5.416 32.311 17.119 1.00168.80 O ANISOU 1544 OE1 GLU A 233 22046 20740 21352 -2279 -882 -949 O ATOM 1545 OE2 GLU A 233 -3.383 32.371 16.293 1.00153.33 O ANISOU 1545 OE2 GLU A 233 20044 18839 19374 -2393 -913 -828 O ATOM 1546 N ALA A 234 -3.846 26.346 15.235 1.00122.67 N ANISOU 1546 N ALA A 234 16197 15271 15140 -2247 -471 -763 N ATOM 1547 CA ALA A 234 -3.430 25.011 15.649 1.00117.53 C ANISOU 1547 CA ALA A 234 15551 14687 14417 -2230 -398 -760 C ATOM 1548 C ALA A 234 -2.106 24.598 15.016 1.00135.06 C ANISOU 1548 C ALA A 234 17742 16970 16605 -2277 -391 -702 C ATOM 1549 O ALA A 234 -1.409 23.725 15.532 1.00137.98 O ANISOU 1549 O ALA A 234 18103 17391 16932 -2277 -358 -699 O ATOM 1550 CB ALA A 234 -4.510 23.999 15.322 1.00105.02 C ANISOU 1550 CB ALA A 234 14005 13125 12772 -2179 -305 -772 C ATOM 1551 N LYS A 235 -1.767 25.222 13.892 1.00150.80 N ANISOU 1551 N LYS A 235 19717 18963 18619 -2318 -422 -655 N ATOM 1552 CA LYS A 235 -0.484 24.974 13.244 1.00167.34 C ANISOU 1552 CA LYS A 235 21771 21121 20689 -2371 -426 -595 C ATOM 1553 C LYS A 235 0.651 25.709 13.961 1.00186.91 C ANISOU 1553 C LYS A 235 24203 23600 23216 -2429 -511 -572 C ATOM 1554 O LYS A 235 1.782 25.218 14.019 1.00198.73 O ANISOU 1554 O LYS A 235 25661 25163 24684 -2462 -508 -534 O ATOM 1555 CB LYS A 235 -0.525 25.381 11.765 1.00157.03 C ANISOU 1555 CB LYS A 235 20456 19822 19385 -2399 -431 -546 C ATOM 1556 CG LYS A 235 -1.183 24.357 10.845 1.00152.48 C ANISOU 1556 CG LYS A 235 19919 19278 18739 -2358 -339 -548 C ATOM 1557 CD LYS A 235 -1.031 24.748 9.375 1.00148.37 C ANISOU 1557 CD LYS A 235 19383 18773 18217 -2394 -349 -495 C ATOM 1558 CE LYS A 235 -1.621 23.683 8.455 1.00127.79 C ANISOU 1558 CE LYS A 235 16821 16199 15536 -2356 -260 -499 C ATOM 1559 NZ LYS A 235 -1.458 24.015 7.010 1.00 90.76 N ANISOU 1559 NZ LYS A 235 12116 11528 10839 -2390 -268 -449 N ATOM 1560 N GLU A 236 0.340 26.879 14.513 1.00178.81 N ANISOU 1560 N GLU A 236 23179 22499 22263 -2441 -590 -595 N ATOM 1561 CA GLU A 236 1.354 27.751 15.104 1.00165.85 C ANISOU 1561 CA GLU A 236 21499 20845 20673 -2506 -682 -569 C ATOM 1562 C GLU A 236 2.133 27.081 16.235 1.00150.74 C ANISOU 1562 C GLU A 236 19569 18974 18733 -2507 -675 -581 C ATOM 1563 O GLU A 236 3.228 27.520 16.591 1.00161.61 O ANISOU 1563 O GLU A 236 20904 20369 20131 -2570 -739 -540 O ATOM 1564 CB GLU A 236 0.717 29.058 15.588 1.00160.14 C ANISOU 1564 CB GLU A 236 20795 20023 20028 -2509 -765 -610 C ATOM 1565 CG GLU A 236 0.864 29.316 17.077 1.00164.86 C ANISOU 1565 CG GLU A 236 21399 20585 20655 -2503 -812 -662 C ATOM 1566 CD GLU A 236 0.243 30.633 17.502 1.00174.74 C ANISOU 1566 CD GLU A 236 22673 21738 21983 -2505 -897 -709 C ATOM 1567 OE1 GLU A 236 -0.936 30.630 17.917 1.00165.86 O ANISOU 1567 OE1 GLU A 236 21584 20566 20870 -2439 -877 -782 O ATOM 1568 OE2 GLU A 236 0.931 31.672 17.419 1.00190.35 O ANISOU 1568 OE2 GLU A 236 24634 23687 24005 -2577 -986 -671 O ATOM 1569 N GLN A 237 1.568 26.016 16.790 1.00120.99 N ANISOU 1569 N GLN A 237 15832 15222 14915 -2442 -599 -631 N ATOM 1570 CA GLN A 237 2.197 25.318 17.901 1.00129.43 C ANISOU 1570 CA GLN A 237 16892 16329 15958 -2436 -587 -648 C ATOM 1571 C GLN A 237 3.602 24.830 17.551 1.00139.14 C ANISOU 1571 C GLN A 237 18068 17646 17153 -2489 -585 -581 C ATOM 1572 O GLN A 237 4.583 25.226 18.182 1.00136.44 O ANISOU 1572 O GLN A 237 17687 17319 16836 -2541 -647 -555 O ATOM 1573 CB GLN A 237 1.333 24.140 18.334 1.00127.85 C ANISOU 1573 CB GLN A 237 16734 16142 15700 -2361 -495 -700 C ATOM 1574 CG GLN A 237 1.132 23.109 17.248 1.00140.27 C ANISOU 1574 CG GLN A 237 18322 17768 17206 -2339 -406 -676 C ATOM 1575 CD GLN A 237 0.803 21.744 17.808 1.00175.38 C ANISOU 1575 CD GLN A 237 22799 22251 21588 -2286 -320 -708 C ATOM 1576 OE1 GLN A 237 0.404 21.615 18.966 1.00192.61 O ANISOU 1576 OE1 GLN A 237 24996 24411 23776 -2257 -321 -753 O ATOM 1577 NE2 GLN A 237 0.976 20.711 16.990 1.00182.91 N ANISOU 1577 NE2 GLN A 237 23761 23258 22479 -2276 -250 -685 N ATOM 1578 N VAL A 280 3.850 20.788 27.934 1.00115.48 N ANISOU 1578 N VAL A 280 15153 14695 14029 -2288 -520 -916 N ATOM 1579 CA VAL A 280 4.696 19.734 27.384 1.00116.95 C ANISOU 1579 CA VAL A 280 15314 14961 14161 -2302 -465 -867 C ATOM 1580 C VAL A 280 3.954 18.931 26.300 1.00 93.46 C ANISOU 1580 C VAL A 280 12365 12002 11143 -2263 -374 -858 C ATOM 1581 O VAL A 280 4.299 19.021 25.123 1.00 53.27 O ANISOU 1581 O VAL A 280 7259 6932 6049 -2287 -367 -815 O ATOM 1582 CB VAL A 280 5.307 18.844 28.512 1.00 52.15 C ANISOU 1582 CB VAL A 280 7097 6802 5917 -2297 -448 -878 C ATOM 1583 CG1 VAL A 280 5.887 17.544 27.959 1.00 32.23 C ANISOU 1583 CG1 VAL A 280 4559 4356 3331 -2292 -376 -844 C ATOM 1584 CG2 VAL A 280 6.366 19.635 29.287 1.00 34.06 C ANISOU 1584 CG2 VAL A 280 4769 4510 3664 -2355 -544 -866 C ATOM 1585 N MET A 281 2.918 18.184 26.675 1.00117.77 N ANISOU 1585 N MET A 281 15483 15073 14191 -2208 -307 -895 N ATOM 1586 CA MET A 281 2.176 17.399 25.683 1.00122.41 C ANISOU 1586 CA MET A 281 16099 15673 14740 -2175 -224 -884 C ATOM 1587 C MET A 281 0.781 17.948 25.381 1.00105.73 C ANISOU 1587 C MET A 281 14017 13504 12651 -2144 -215 -909 C ATOM 1588 O MET A 281 -0.149 17.806 26.177 1.00 77.68 O ANISOU 1588 O MET A 281 10486 9931 9098 -2109 -198 -947 O ATOM 1589 CB MET A 281 2.050 15.941 26.137 1.00132.80 C ANISOU 1589 CB MET A 281 17433 17029 15997 -2141 -148 -891 C ATOM 1590 CG MET A 281 3.356 15.168 26.161 1.00151.94 C ANISOU 1590 CG MET A 281 19828 19515 18386 -2164 -142 -864 C ATOM 1591 SD MET A 281 3.967 14.764 24.514 1.00203.93 S ANISOU 1591 SD MET A 281 26403 26140 24941 -2181 -112 -817 S ATOM 1592 CE MET A 281 5.319 13.660 24.927 1.00163.04 C ANISOU 1592 CE MET A 281 21191 21037 19718 -2192 -102 -801 C ATOM 1593 N LEU A 282 0.648 18.563 24.211 1.00107.67 N ANISOU 1593 N LEU A 282 14263 13731 12917 -2159 -228 -884 N ATOM 1594 CA LEU A 282 -0.645 18.994 23.695 1.00 85.12 C ANISOU 1594 CA LEU A 282 11435 10829 10078 -2131 -213 -900 C ATOM 1595 C LEU A 282 -1.206 18.042 22.644 1.00 92.45 C ANISOU 1595 C LEU A 282 12389 11782 10954 -2109 -128 -876 C ATOM 1596 O LEU A 282 -2.300 18.257 22.130 1.00105.57 O ANISOU 1596 O LEU A 282 14074 13414 12622 -2087 -108 -882 O ATOM 1597 CB LEU A 282 -0.550 20.406 23.120 1.00 95.71 C ANISOU 1597 CB LEU A 282 12761 12122 11481 -2162 -291 -892 C ATOM 1598 CG LEU A 282 -0.557 21.557 24.128 1.00131.37 C ANISOU 1598 CG LEU A 282 17269 16583 16063 -2172 -383 -931 C ATOM 1599 CD1 LEU A 282 0.581 21.435 25.141 1.00143.08 C ANISOU 1599 CD1 LEU A 282 18726 18091 17545 -2201 -422 -932 C ATOM 1600 CD2 LEU A 282 -0.496 22.893 23.402 1.00136.39 C ANISOU 1600 CD2 LEU A 282 17894 17166 16763 -2205 -459 -918 C ATOM 1601 N MET A 283 -0.450 17.000 22.312 1.00134.00 N ANISOU 1601 N MET A 283 15304 16667 18941 131 -4728 47 N ATOM 1602 CA MET A 283 -0.853 16.086 21.248 1.00120.75 C ANISOU 1602 CA MET A 283 13694 14843 17341 163 -4695 70 C ATOM 1603 C MET A 283 -2.263 15.551 21.489 1.00119.51 C ANISOU 1603 C MET A 283 13629 14624 17155 165 -4680 103 C ATOM 1604 O MET A 283 -3.073 15.500 20.568 1.00129.63 O ANISOU 1604 O MET A 283 15003 15772 18477 171 -4638 84 O ATOM 1605 CB MET A 283 0.152 14.938 21.097 1.00116.92 C ANISOU 1605 CB MET A 283 13126 14379 16918 203 -4732 112 C ATOM 1606 CG MET A 283 0.407 14.515 19.652 1.00115.12 C ANISOU 1606 CG MET A 283 12917 14042 16780 236 -4699 84 C ATOM 1607 SD MET A 283 1.046 15.849 18.615 1.00156.80 S ANISOU 1607 SD MET A 283 18167 19341 22067 203 -4654 15 S ATOM 1608 CE MET A 283 2.573 16.251 19.468 1.00108.21 C ANISOU 1608 CE MET A 283 11845 13377 15894 187 -4707 15 C ATOM 1609 N ARG A 284 -2.557 15.167 22.728 1.00119.78 N ANISOU 1609 N ARG A 284 13626 14774 17111 157 -4719 154 N ATOM 1610 CA ARG A 284 -3.903 14.728 23.087 1.00120.66 C ANISOU 1610 CA ARG A 284 13798 14872 17176 148 -4708 191 C ATOM 1611 C ARG A 284 -4.925 15.740 22.586 1.00109.19 C ANISOU 1611 C ARG A 284 12428 13352 15709 137 -4653 119 C ATOM 1612 O ARG A 284 -5.940 15.376 21.986 1.00139.11 O ANISOU 1612 O ARG A 284 16296 17031 19527 141 -4623 126 O ATOM 1613 CB ARG A 284 -4.034 14.559 24.603 1.00153.86 C ANISOU 1613 CB ARG A 284 17925 19278 21256 130 -4757 245 C ATOM 1614 CG ARG A 284 -3.361 13.312 25.165 1.00181.88 C ANISOU 1614 CG ARG A 284 21407 22879 24819 143 -4827 347 C ATOM 1615 CD ARG A 284 -4.386 12.276 25.622 1.00204.02 C ANISOU 1615 CD ARG A 284 24237 25688 27594 128 -4850 445 C ATOM 1616 NE ARG A 284 -5.239 11.815 24.528 1.00213.43 N ANISOU 1616 NE ARG A 284 25532 26679 28883 129 -4808 438 N ATOM 1617 CZ ARG A 284 -6.257 10.971 24.673 1.00208.83 C ANISOU 1617 CZ ARG A 284 24983 26064 28298 107 -4822 513 C ATOM 1618 NH1 ARG A 284 -6.560 10.489 25.871 1.00205.31 N ANISOU 1618 NH1 ARG A 284 24476 25780 27752 80 -4874 610 N ATOM 1619 NH2 ARG A 284 -6.975 10.610 23.619 1.00205.65 N ANISOU 1619 NH2 ARG A 284 24670 25480 27988 107 -4789 493 N ATOM 1620 N GLU A 285 -4.641 17.014 22.835 1.00 88.97 N ANISOU 1620 N GLU A 285 9844 10851 13109 125 -4651 49 N ATOM 1621 CA GLU A 285 -5.483 18.111 22.373 1.00 89.24 C ANISOU 1621 CA GLU A 285 9952 10810 13147 123 -4618 -25 C ATOM 1622 C GLU A 285 -5.753 18.000 20.874 1.00 94.21 C ANISOU 1622 C GLU A 285 10673 11245 13876 136 -4578 -34 C ATOM 1623 O GLU A 285 -6.873 18.227 20.411 1.00101.09 O ANISOU 1623 O GLU A 285 11622 12031 14755 144 -4551 -57 O ATOM 1624 CB GLU A 285 -4.812 19.449 22.696 1.00 84.33 C ANISOU 1624 CB GLU A 285 9288 10246 12508 106 -4642 -98 C ATOM 1625 CG GLU A 285 -5.489 20.671 22.107 1.00 86.28 C ANISOU 1625 CG GLU A 285 9610 10383 12789 108 -4627 -175 C ATOM 1626 CD GLU A 285 -6.121 21.554 23.167 1.00119.21 C ANISOU 1626 CD GLU A 285 13753 14667 16874 109 -4655 -245 C ATOM 1627 OE1 GLU A 285 -6.874 21.029 24.015 1.00141.50 O ANISOU 1627 OE1 GLU A 285 16543 17618 19601 116 -4652 -227 O ATOM 1628 OE2 GLU A 285 -5.859 22.775 23.157 1.00116.36 O ANISOU 1628 OE2 GLU A 285 13394 14278 16541 100 -4686 -321 O ATOM 1629 N HIS A 286 -4.723 17.629 20.123 1.00 99.34 N ANISOU 1629 N HIS A 286 11302 11849 14595 140 -4578 -19 N ATOM 1630 CA HIS A 286 -4.808 17.573 18.664 1.00106.09 C ANISOU 1630 CA HIS A 286 12223 12563 15525 151 -4545 -33 C ATOM 1631 C HIS A 286 -5.511 16.334 18.104 1.00114.10 C ANISOU 1631 C HIS A 286 13291 13486 16574 172 -4532 0 C ATOM 1632 O HIS A 286 -6.249 16.428 17.121 1.00117.86 O ANISOU 1632 O HIS A 286 13848 13853 17079 178 -4505 -22 O ATOM 1633 CB HIS A 286 -3.418 17.735 18.051 1.00115.49 C ANISOU 1633 CB HIS A 286 13344 13780 16757 146 -4551 -41 C ATOM 1634 CG HIS A 286 -2.906 19.139 18.102 1.00123.18 C ANISOU 1634 CG HIS A 286 14291 14790 17722 112 -4562 -80 C ATOM 1635 ND1 HIS A 286 -2.378 19.779 17.007 1.00128.87 N ANISOU 1635 ND1 HIS A 286 15010 15474 18482 90 -4551 -94 N ATOM 1636 CD2 HIS A 286 -2.872 20.034 19.121 1.00120.93 C ANISOU 1636 CD2 HIS A 286 13977 14579 17393 89 -4593 -109 C ATOM 1637 CE1 HIS A 286 -2.027 21.009 17.347 1.00119.46 C ANISOU 1637 CE1 HIS A 286 13793 14312 17284 51 -4579 -121 C ATOM 1638 NE2 HIS A 286 -2.313 21.187 18.618 1.00119.82 N ANISOU 1638 NE2 HIS A 286 13825 14419 17284 54 -4606 -140 N ATOM 1639 N LYS A 287 -5.275 15.178 18.718 1.00123.74 N ANISOU 1639 N LYS A 287 14467 14749 17798 182 -4561 55 N ATOM 1640 CA LYS A 287 -5.961 13.954 18.317 1.00114.66 C ANISOU 1640 CA LYS A 287 13366 13506 16694 195 -4567 90 C ATOM 1641 C LYS A 287 -7.440 14.057 18.687 1.00109.53 C ANISOU 1641 C LYS A 287 12776 12844 15996 175 -4553 101 C ATOM 1642 O LYS A 287 -8.292 13.469 18.023 1.00104.22 O ANISOU 1642 O LYS A 287 12168 12068 15362 178 -4545 105 O ATOM 1643 CB LYS A 287 -5.320 12.724 18.971 1.00113.92 C ANISOU 1643 CB LYS A 287 13204 13453 16626 207 -4623 156 C ATOM 1644 CG LYS A 287 -5.758 11.371 18.396 1.00116.71 C ANISOU 1644 CG LYS A 287 13600 13681 17062 223 -4649 185 C ATOM 1645 CD LYS A 287 -5.037 11.032 17.091 1.00126.08 C ANISOU 1645 CD LYS A 287 14786 14786 18333 267 -4644 127 C ATOM 1646 CE LYS A 287 -5.365 9.616 16.615 1.00125.64 C ANISOU 1646 CE LYS A 287 14761 14607 18370 291 -4691 142 C ATOM 1647 NZ LYS A 287 -4.709 9.277 15.316 1.00119.99 N ANISOU 1647 NZ LYS A 287 14032 13837 17722 346 -4689 65 N ATOM 1648 N ALA A 288 -7.742 14.810 19.744 1.00114.23 N ANISOU 1648 N ALA A 288 13338 13562 16504 158 -4554 98 N ATOM 1649 CA ALA A 288 -9.132 15.070 20.119 1.00110.20 C ANISOU 1649 CA ALA A 288 12858 13079 15934 147 -4538 93 C ATOM 1650 C ALA A 288 -9.756 16.179 19.267 1.00104.18 C ANISOU 1650 C ALA A 288 12167 12225 15190 160 -4503 14 C ATOM 1651 O ALA A 288 -10.979 16.275 19.160 1.00 97.14 O ANISOU 1651 O ALA A 288 11314 11313 14281 163 -4489 1 O ATOM 1652 CB ALA A 288 -9.230 15.417 21.597 1.00112.94 C ANISOU 1652 CB ALA A 288 13122 13626 16163 132 -4559 108 C ATOM 1653 N LEU A 289 -8.910 17.017 18.673 1.00 97.14 N ANISOU 1653 N LEU A 289 11284 11288 14335 167 -4498 -31 N ATOM 1654 CA LEU A 289 -9.365 18.093 17.794 1.00 71.83 C ANISOU 1654 CA LEU A 289 8149 7985 11159 175 -4483 -90 C ATOM 1655 C LEU A 289 -9.725 17.604 16.390 1.00 57.09 C ANISOU 1655 C LEU A 289 6357 5981 9355 185 -4465 -86 C ATOM 1656 O LEU A 289 -10.797 17.917 15.850 1.00 56.59 O ANISOU 1656 O LEU A 289 6358 5844 9298 194 -4457 -110 O ATOM 1657 CB LEU A 289 -8.264 19.147 17.676 1.00 71.43 C ANISOU 1657 CB LEU A 289 8069 7946 11125 165 -4497 -122 C ATOM 1658 CG LEU A 289 -8.646 20.525 17.139 1.00 63.84 C ANISOU 1658 CG LEU A 289 7164 6904 10189 166 -4506 -176 C ATOM 1659 CD1 LEU A 289 -9.280 21.330 18.247 1.00 58.43 C ANISOU 1659 CD1 LEU A 289 6458 6290 9454 178 -4529 -228 C ATOM 1660 CD2 LEU A 289 -7.432 21.248 16.595 1.00 58.19 C ANISOU 1660 CD2 LEU A 289 6423 6175 9512 140 -4522 -177 C ATOM 1661 N LYS A 290 -8.818 16.834 15.801 1.00 79.69 N ANISOU 1661 N LYS A 290 9199 8822 12257 187 -4465 -63 N ATOM 1662 CA LYS A 290 -8.980 16.394 14.423 1.00107.24 C ANISOU 1662 CA LYS A 290 12742 12212 15791 199 -4454 -73 C ATOM 1663 C LYS A 290 -10.268 15.596 14.295 1.00 99.82 C ANISOU 1663 C LYS A 290 11858 11210 14860 205 -4454 -62 C ATOM 1664 O LYS A 290 -10.997 15.709 13.306 1.00100.77 O ANISOU 1664 O LYS A 290 12044 11250 14995 212 -4448 -86 O ATOM 1665 CB LYS A 290 -7.780 15.551 13.988 1.00130.62 C ANISOU 1665 CB LYS A 290 15647 15196 18787 213 -4461 -62 C ATOM 1666 CG LYS A 290 -7.736 15.238 12.498 1.00145.12 C ANISOU 1666 CG LYS A 290 17516 16973 20650 232 -4452 -89 C ATOM 1667 CD LYS A 290 -6.477 14.457 12.135 1.00149.88 C ANISOU 1667 CD LYS A 290 18035 17629 21282 259 -4464 -96 C ATOM 1668 CE LYS A 290 -6.396 14.194 10.638 1.00147.65 C ANISOU 1668 CE LYS A 290 17765 17331 21003 283 -4456 -135 C ATOM 1669 NZ LYS A 290 -5.177 13.417 10.270 1.00143.81 N ANISOU 1669 NZ LYS A 290 17179 16921 20543 324 -4470 -158 N ATOM 1670 N THR A 291 -10.547 14.801 15.319 1.00 83.29 N ANISOU 1670 N THR A 291 9729 9166 12751 195 -4470 -19 N ATOM 1671 CA THR A 291 -11.753 13.992 15.341 1.00 82.83 C ANISOU 1671 CA THR A 291 9704 9067 12700 187 -4479 6 C ATOM 1672 C THR A 291 -13.017 14.856 15.445 1.00 72.88 C ANISOU 1672 C THR A 291 8476 7818 11396 187 -4462 -23 C ATOM 1673 O THR A 291 -14.100 14.413 15.073 1.00 91.92 O ANISOU 1673 O THR A 291 10924 10183 13820 184 -4466 -19 O ATOM 1674 CB THR A 291 -11.686 12.905 16.437 1.00 87.73 C ANISOU 1674 CB THR A 291 10267 9754 13313 166 -4511 81 C ATOM 1675 OG1 THR A 291 -10.622 11.992 16.133 1.00 66.64 O ANISOU 1675 OG1 THR A 291 7574 7039 10708 179 -4540 98 O ATOM 1676 CG2 THR A 291 -12.989 12.127 16.518 1.00 95.98 C ANISOU 1676 CG2 THR A 291 11335 10771 14363 144 -4527 120 C ATOM 1677 N LEU A 292 -12.887 16.090 15.926 1.00 56.35 N ANISOU 1677 N LEU A 292 6365 5786 9261 193 -4453 -59 N ATOM 1678 CA LEU A 292 -14.005 17.028 15.825 1.00 56.14 C ANISOU 1678 CA LEU A 292 6370 5749 9213 209 -4449 -107 C ATOM 1679 C LEU A 292 -14.086 17.561 14.405 1.00 70.77 C ANISOU 1679 C LEU A 292 8303 7471 11117 223 -4449 -142 C ATOM 1680 O LEU A 292 -15.177 17.699 13.852 1.00 76.59 O ANISOU 1680 O LEU A 292 9084 8153 11862 236 -4454 -163 O ATOM 1681 CB LEU A 292 -13.904 18.185 16.825 1.00 56.60 C ANISOU 1681 CB LEU A 292 6381 5908 9218 218 -4455 -148 C ATOM 1682 CG LEU A 292 -14.613 18.010 18.175 1.00 62.32 C ANISOU 1682 CG LEU A 292 7025 6802 9853 215 -4458 -139 C ATOM 1683 CD1 LEU A 292 -14.419 19.243 19.050 1.00 66.38 C ANISOU 1683 CD1 LEU A 292 7490 7416 10314 233 -4473 -205 C ATOM 1684 CD2 LEU A 292 -16.095 17.700 18.011 1.00 57.21 C ANISOU 1684 CD2 LEU A 292 6385 6162 9190 222 -4453 -141 C ATOM 1685 N GLY A 293 -12.933 17.856 13.810 1.00 70.35 N ANISOU 1685 N GLY A 293 8255 7386 11090 218 -4448 -143 N ATOM 1686 CA GLY A 293 -12.908 18.308 12.427 1.00 72.77 C ANISOU 1686 CA GLY A 293 8623 7601 11425 222 -4454 -159 C ATOM 1687 C GLY A 293 -13.681 17.363 11.527 1.00 77.79 C ANISOU 1687 C GLY A 293 9304 8175 12076 230 -4454 -154 C ATOM 1688 O GLY A 293 -14.531 17.775 10.719 1.00 81.99 O ANISOU 1688 O GLY A 293 9893 8647 12612 239 -4468 -174 O ATOM 1689 N ILE A 294 -13.393 16.076 11.689 1.00 79.78 N ANISOU 1689 N ILE A 294 9529 8441 12343 227 -4451 -130 N ATOM 1690 CA ILE A 294 -14.063 15.033 10.924 1.00 73.45 C ANISOU 1690 CA ILE A 294 8763 7577 11567 235 -4465 -131 C ATOM 1691 C ILE A 294 -15.573 15.211 10.944 1.00 76.01 C ANISOU 1691 C ILE A 294 9123 7875 11882 235 -4473 -139 C ATOM 1692 O ILE A 294 -16.196 15.251 9.897 1.00 86.01 O ANISOU 1692 O ILE A 294 10441 9083 13155 246 -4488 -162 O ATOM 1693 CB ILE A 294 -13.719 13.633 11.461 1.00 83.20 C ANISOU 1693 CB ILE A 294 9958 8818 12835 229 -4480 -97 C ATOM 1694 CG1 ILE A 294 -12.269 13.281 11.122 1.00106.74 C ANISOU 1694 CG1 ILE A 294 12900 11817 15838 244 -4482 -105 C ATOM 1695 CG2 ILE A 294 -14.676 12.589 10.903 1.00 55.29 C ANISOU 1695 CG2 ILE A 294 6462 5209 9337 229 -4508 -97 C ATOM 1696 CD1 ILE A 294 -11.856 11.900 11.577 1.00130.08 C ANISOU 1696 CD1 ILE A 294 15818 14759 18846 248 -4515 -77 C ATOM 1697 N ILE A 295 -16.152 15.354 12.131 1.00 73.51 N ANISOU 1697 N ILE A 295 8766 7625 11539 226 -4469 -123 N ATOM 1698 CA ILE A 295 -17.601 15.450 12.268 1.00 77.26 C ANISOU 1698 CA ILE A 295 9246 8112 11999 230 -4478 -132 C ATOM 1699 C ILE A 295 -18.223 16.436 11.290 1.00 89.26 C ANISOU 1699 C ILE A 295 10823 9567 13523 255 -4491 -181 C ATOM 1700 O ILE A 295 -19.185 16.114 10.599 1.00100.49 O ANISOU 1700 O ILE A 295 12275 10948 14957 261 -4510 -190 O ATOM 1701 CB ILE A 295 -17.993 15.877 13.681 1.00 55.53 C ANISOU 1701 CB ILE A 295 6421 5487 9189 226 -4468 -126 C ATOM 1702 CG1 ILE A 295 -17.500 14.844 14.685 1.00 55.93 C ANISOU 1702 CG1 ILE A 295 6408 5620 9222 193 -4467 -59 C ATOM 1703 CG2 ILE A 295 -19.496 16.058 13.786 1.00 55.80 C ANISOU 1703 CG2 ILE A 295 6438 5564 9200 237 -4478 -146 C ATOM 1704 CD1 ILE A 295 -17.883 13.446 14.327 1.00 56.08 C ANISOU 1704 CD1 ILE A 295 6439 5583 9286 166 -4491 -8 C ATOM 1705 N MET A 296 -17.673 17.640 11.236 1.00 75.05 N ANISOU 1705 N MET A 296 9038 7759 11719 267 -4491 -207 N ATOM 1706 CA MET A 296 -18.215 18.671 10.367 1.00 85.61 C ANISOU 1706 CA MET A 296 10431 9029 13069 288 -4521 -241 C ATOM 1707 C MET A 296 -17.851 18.407 8.917 1.00 90.92 C ANISOU 1707 C MET A 296 11160 9635 13751 280 -4533 -228 C ATOM 1708 O MET A 296 -18.570 18.818 8.005 1.00 85.77 O ANISOU 1708 O MET A 296 10556 8934 13100 291 -4567 -241 O ATOM 1709 CB MET A 296 -17.706 20.042 10.794 1.00 97.32 C ANISOU 1709 CB MET A 296 11911 10510 14557 297 -4535 -265 C ATOM 1710 CG MET A 296 -17.959 20.343 12.255 1.00 92.99 C ANISOU 1710 CG MET A 296 11294 10056 13982 313 -4526 -293 C ATOM 1711 SD MET A 296 -17.112 21.834 12.791 1.00 92.85 S ANISOU 1711 SD MET A 296 11268 10030 13980 323 -4554 -330 S ATOM 1712 CE MET A 296 -15.468 21.519 12.166 1.00147.95 C ANISOU 1712 CE MET A 296 18257 16986 20971 276 -4535 -271 C ATOM 1713 N GLY A 297 -16.730 17.730 8.696 1.00 93.44 N ANISOU 1713 N GLY A 297 11462 9972 14068 264 -4513 -205 N ATOM 1714 CA GLY A 297 -16.373 17.369 7.337 1.00 79.24 C ANISOU 1714 CA GLY A 297 9696 8152 12258 263 -4525 -202 C ATOM 1715 C GLY A 297 -17.417 16.431 6.762 1.00 78.23 C ANISOU 1715 C GLY A 297 9595 7991 12137 276 -4545 -216 C ATOM 1716 O GLY A 297 -18.045 16.721 5.740 1.00 98.03 O ANISOU 1716 O GLY A 297 12148 10473 14626 284 -4577 -227 O ATOM 1717 N VAL A 298 -17.620 15.312 7.449 1.00 54.64 N ANISOU 1717 N VAL A 298 6577 5007 9176 272 -4537 -209 N ATOM 1718 CA VAL A 298 -18.565 14.295 7.026 1.00 54.86 C ANISOU 1718 CA VAL A 298 6622 4999 9225 276 -4566 -216 C ATOM 1719 C VAL A 298 -19.964 14.874 6.978 1.00 55.05 C ANISOU 1719 C VAL A 298 6663 5015 9239 282 -4586 -227 C ATOM 1720 O VAL A 298 -20.729 14.594 6.065 1.00 55.33 O ANISOU 1720 O VAL A 298 6729 5020 9272 292 -4622 -244 O ATOM 1721 CB VAL A 298 -18.542 13.073 7.964 1.00 64.01 C ANISOU 1721 CB VAL A 298 7738 6160 10424 258 -4566 -186 C ATOM 1722 CG1 VAL A 298 -18.407 13.513 9.402 1.00 73.98 C ANISOU 1722 CG1 VAL A 298 8948 7491 11671 239 -4537 -153 C ATOM 1723 CG2 VAL A 298 -19.798 12.245 7.785 1.00 89.29 C ANISOU 1723 CG2 VAL A 298 10946 9327 13652 249 -4604 -182 C ATOM 1724 N PHE A 299 -20.298 15.688 7.966 1.00 55.04 N ANISOU 1724 N PHE A 299 6632 5054 9228 282 -4571 -224 N ATOM 1725 CA PHE A 299 -21.603 16.317 7.979 1.00 72.77 C ANISOU 1725 CA PHE A 299 8876 7308 11467 300 -4595 -247 C ATOM 1726 C PHE A 299 -21.785 17.098 6.689 1.00 70.71 C ANISOU 1726 C PHE A 299 8679 6990 11198 318 -4634 -269 C ATOM 1727 O PHE A 299 -22.701 16.830 5.921 1.00 74.30 O ANISOU 1727 O PHE A 299 9154 7425 11651 328 -4672 -281 O ATOM 1728 CB PHE A 299 -21.738 17.246 9.180 1.00 79.70 C ANISOU 1728 CB PHE A 299 9705 8249 12329 312 -4578 -261 C ATOM 1729 CG PHE A 299 -23.121 17.796 9.367 1.00 76.45 C ANISOU 1729 CG PHE A 299 9264 7872 11911 341 -4606 -297 C ATOM 1730 CD1 PHE A 299 -23.422 19.094 8.995 1.00 56.32 C ANISOU 1730 CD1 PHE A 299 6746 5279 9373 378 -4643 -341 C ATOM 1731 CD2 PHE A 299 -24.118 17.013 9.918 1.00 56.44 C ANISOU 1731 CD2 PHE A 299 6662 5420 9361 331 -4605 -284 C ATOM 1732 CE1 PHE A 299 -24.689 19.599 9.174 1.00 56.99 C ANISOU 1732 CE1 PHE A 299 6794 5401 9459 417 -4678 -386 C ATOM 1733 CE2 PHE A 299 -25.384 17.514 10.097 1.00 57.09 C ANISOU 1733 CE2 PHE A 299 6696 5563 9432 362 -4631 -322 C ATOM 1734 CZ PHE A 299 -25.670 18.809 9.725 1.00 57.37 C ANISOU 1734 CZ PHE A 299 6762 5553 9483 412 -4667 -380 C ATOM 1735 N THR A 300 -20.889 18.046 6.441 1.00 55.38 N ANISOU 1735 N THR A 300 6764 5029 9247 317 -4632 -265 N ATOM 1736 CA THR A 300 -20.952 18.856 5.232 1.00 55.69 C ANISOU 1736 CA THR A 300 6861 5028 9269 321 -4678 -264 C ATOM 1737 C THR A 300 -21.052 18.003 3.967 1.00 69.49 C ANISOU 1737 C THR A 300 8638 6779 10985 318 -4700 -259 C ATOM 1738 O THR A 300 -21.770 18.358 3.045 1.00 56.39 O ANISOU 1738 O THR A 300 7016 5104 9305 328 -4752 -262 O ATOM 1739 CB THR A 300 -19.740 19.793 5.116 1.00 75.70 C ANISOU 1739 CB THR A 300 9409 7557 11796 301 -4675 -239 C ATOM 1740 OG1 THR A 300 -19.675 20.641 6.271 1.00 55.58 O ANISOU 1740 OG1 THR A 300 6835 5001 9280 310 -4669 -256 O ATOM 1741 CG2 THR A 300 -19.856 20.643 3.862 1.00 81.93 C ANISOU 1741 CG2 THR A 300 10254 8316 12559 293 -4737 -215 C ATOM 1742 N LEU A 301 -20.341 16.880 3.915 1.00 82.36 N ANISOU 1742 N LEU A 301 10248 8433 12612 310 -4669 -256 N ATOM 1743 CA LEU A 301 -20.403 16.024 2.726 1.00 69.89 C ANISOU 1743 CA LEU A 301 8689 6866 10999 319 -4697 -270 C ATOM 1744 C LEU A 301 -21.714 15.261 2.610 1.00 70.68 C ANISOU 1744 C LEU A 301 8793 6939 11123 330 -4733 -292 C ATOM 1745 O LEU A 301 -22.125 14.880 1.512 1.00 87.69 O ANISOU 1745 O LEU A 301 10973 9102 13244 342 -4778 -311 O ATOM 1746 CB LEU A 301 -19.238 15.044 2.698 1.00 55.71 C ANISOU 1746 CB LEU A 301 6863 5100 9205 320 -4668 -279 C ATOM 1747 CG LEU A 301 -17.942 15.713 2.270 1.00 55.65 C ANISOU 1747 CG LEU A 301 6842 5157 9147 310 -4649 -260 C ATOM 1748 CD1 LEU A 301 -16.786 14.754 2.416 1.00 55.57 C ANISOU 1748 CD1 LEU A 301 6779 5187 9147 321 -4621 -278 C ATOM 1749 CD2 LEU A 301 -18.065 16.220 0.839 1.00 64.01 C ANISOU 1749 CD2 LEU A 301 7931 6270 10120 309 -4692 -252 C ATOM 1750 N CYS A 302 -22.339 15.004 3.754 1.00 64.32 N ANISOU 1750 N CYS A 302 7950 6122 10366 323 -4716 -287 N ATOM 1751 CA CYS A 302 -23.605 14.284 3.810 1.00 69.38 C ANISOU 1751 CA CYS A 302 8573 6756 11032 323 -4750 -295 C ATOM 1752 C CYS A 302 -24.835 15.152 3.523 1.00 65.42 C ANISOU 1752 C CYS A 302 8075 6264 10516 341 -4791 -310 C ATOM 1753 O CYS A 302 -25.714 14.760 2.757 1.00 61.36 O ANISOU 1753 O CYS A 302 7569 5748 9997 348 -4843 -325 O ATOM 1754 CB CYS A 302 -23.740 13.553 5.150 1.00 61.78 C ANISOU 1754 CB CYS A 302 7551 5812 10112 298 -4721 -268 C ATOM 1755 SG CYS A 302 -22.731 12.051 5.275 1.00 71.10 S ANISOU 1755 SG CYS A 302 8726 6953 11337 280 -4717 -253 S ATOM 1756 N TRP A 303 -24.911 16.313 4.162 1.00 57.09 N ANISOU 1756 N TRP A 303 7008 5221 9462 352 -4777 -311 N ATOM 1757 CA TRP A 303 -26.037 17.214 3.957 1.00 57.76 C ANISOU 1757 CA TRP A 303 7089 5310 9547 381 -4827 -335 C ATOM 1758 C TRP A 303 -25.811 18.391 3.015 1.00 63.67 C ANISOU 1758 C TRP A 303 7902 6017 10274 395 -4874 -334 C ATOM 1759 O TRP A 303 -26.734 19.160 2.777 1.00 66.74 O ANISOU 1759 O TRP A 303 8292 6395 10672 424 -4933 -353 O ATOM 1760 CB TRP A 303 -26.570 17.707 5.294 1.00 57.84 C ANISOU 1760 CB TRP A 303 7028 5372 9576 397 -4804 -352 C ATOM 1761 CG TRP A 303 -27.305 16.645 6.026 1.00 79.52 C ANISOU 1761 CG TRP A 303 9694 8192 12327 378 -4787 -341 C ATOM 1762 CD1 TRP A 303 -26.771 15.677 6.821 1.00 79.26 C ANISOU 1762 CD1 TRP A 303 9627 8192 12298 339 -4741 -303 C ATOM 1763 CD2 TRP A 303 -28.717 16.428 6.021 1.00 70.25 C ANISOU 1763 CD2 TRP A 303 8457 7079 11155 388 -4827 -357 C ATOM 1764 NE1 TRP A 303 -27.765 14.874 7.322 1.00 67.51 N ANISOU 1764 NE1 TRP A 303 8060 6780 10812 317 -4751 -284 N ATOM 1765 CE2 TRP A 303 -28.971 15.316 6.845 1.00 66.48 C ANISOU 1765 CE2 TRP A 303 7906 6676 10678 346 -4800 -319 C ATOM 1766 CE3 TRP A 303 -29.793 17.070 5.405 1.00 90.68 C ANISOU 1766 CE3 TRP A 303 11037 9673 13745 427 -4890 -394 C ATOM 1767 CZ2 TRP A 303 -30.256 14.832 7.066 1.00 90.00 C ANISOU 1767 CZ2 TRP A 303 10794 9747 13654 335 -4829 -315 C ATOM 1768 CZ3 TRP A 303 -31.071 16.588 5.625 1.00108.14 C ANISOU 1768 CZ3 TRP A 303 13157 11975 15956 426 -4918 -401 C ATOM 1769 CH2 TRP A 303 -31.291 15.480 6.447 1.00107.18 C ANISOU 1769 CH2 TRP A 303 12954 11939 15830 377 -4884 -361 C ATOM 1770 N LEU A 304 -24.594 18.566 2.514 1.00 84.95 N ANISOU 1770 N LEU A 304 10640 8697 12941 374 -4858 -306 N ATOM 1771 CA LEU A 304 -24.353 19.574 1.476 1.00 87.32 C ANISOU 1771 CA LEU A 304 10998 8976 13205 371 -4914 -281 C ATOM 1772 C LEU A 304 -24.904 19.204 0.096 1.00 78.97 C ANISOU 1772 C LEU A 304 9972 7944 12089 373 -4976 -274 C ATOM 1773 O LEU A 304 -25.527 20.036 -0.561 1.00 59.83 O ANISOU 1773 O LEU A 304 7579 5504 9650 384 -5052 -261 O ATOM 1774 CB LEU A 304 -22.880 19.954 1.367 1.00 87.03 C ANISOU 1774 CB LEU A 304 10977 8947 13142 339 -4881 -242 C ATOM 1775 CG LEU A 304 -22.643 21.161 0.461 1.00 87.18 C ANISOU 1775 CG LEU A 304 11047 8950 13128 321 -4948 -195 C ATOM 1776 CD1 LEU A 304 -23.371 22.375 1.010 1.00 58.90 C ANISOU 1776 CD1 LEU A 304 7478 5288 9615 344 -5004 -211 C ATOM 1777 CD2 LEU A 304 -21.160 21.436 0.322 1.00107.29 C ANISOU 1777 CD2 LEU A 304 13591 11535 15640 279 -4916 -147 C ATOM 1778 N PRO A 305 -24.652 17.960 -0.357 1.00 89.22 N ANISOU 1778 N PRO A 305 11261 9283 13354 367 -4955 -285 N ATOM 1779 CA PRO A 305 -25.126 17.542 -1.680 1.00 90.42 C ANISOU 1779 CA PRO A 305 11438 9480 13437 373 -5019 -289 C ATOM 1780 C PRO A 305 -26.645 17.627 -1.774 1.00 76.55 C ANISOU 1780 C PRO A 305 9671 7708 11707 396 -5084 -311 C ATOM 1781 O PRO A 305 -27.192 17.883 -2.846 1.00 65.16 O ANISOU 1781 O PRO A 305 8255 6297 10206 403 -5161 -303 O ATOM 1782 CB PRO A 305 -24.660 16.080 -1.776 1.00 84.35 C ANISOU 1782 CB PRO A 305 10647 8738 12663 372 -4985 -322 C ATOM 1783 CG PRO A 305 -24.439 15.646 -0.371 1.00 64.73 C ANISOU 1783 CG PRO A 305 8123 6207 10265 367 -4918 -328 C ATOM 1784 CD PRO A 305 -23.941 16.871 0.333 1.00 84.27 C ANISOU 1784 CD PRO A 305 10600 8662 12755 358 -4886 -299 C ATOM 1785 N PHE A 306 -27.315 17.409 -0.649 1.00 77.56 N ANISOU 1785 N PHE A 306 9748 7809 11911 407 -5056 -336 N ATOM 1786 CA PHE A 306 -28.767 17.512 -0.577 1.00 71.37 C ANISOU 1786 CA PHE A 306 8927 7034 11155 431 -5113 -360 C ATOM 1787 C PHE A 306 -29.221 18.970 -0.506 1.00 77.14 C ANISOU 1787 C PHE A 306 9667 7738 11903 460 -5163 -359 C ATOM 1788 O PHE A 306 -30.136 19.374 -1.218 1.00 77.46 O ANISOU 1788 O PHE A 306 9713 7788 11929 483 -5249 -363 O ATOM 1789 CB PHE A 306 -29.275 16.720 0.630 1.00 76.60 C ANISOU 1789 CB PHE A 306 9512 7715 11876 425 -5065 -378 C ATOM 1790 CG PHE A 306 -30.709 16.997 0.999 1.00 70.56 C ANISOU 1790 CG PHE A 306 8677 6993 11141 451 -5109 -404 C ATOM 1791 CD1 PHE A 306 -31.066 18.179 1.628 1.00 66.87 C ANISOU 1791 CD1 PHE A 306 8182 6529 10698 488 -5118 -424 C ATOM 1792 CD2 PHE A 306 -31.692 16.055 0.763 1.00 72.79 C ANISOU 1792 CD2 PHE A 306 8908 7319 11429 442 -5147 -414 C ATOM 1793 CE1 PHE A 306 -32.383 18.426 1.989 1.00 62.87 C ANISOU 1793 CE1 PHE A 306 7590 6084 10214 523 -5160 -458 C ATOM 1794 CE2 PHE A 306 -33.009 16.300 1.122 1.00 76.49 C ANISOU 1794 CE2 PHE A 306 9290 7854 11919 464 -5187 -437 C ATOM 1795 CZ PHE A 306 -33.353 17.484 1.742 1.00 63.60 C ANISOU 1795 CZ PHE A 306 7621 6240 10303 509 -5191 -461 C ATOM 1796 N PHE A 307 -28.573 19.756 0.352 1.00 87.62 N ANISOU 1796 N PHE A 307 10997 9030 13266 461 -5121 -355 N ATOM 1797 CA PHE A 307 -28.914 21.168 0.516 1.00 63.72 C ANISOU 1797 CA PHE A 307 7981 5954 10274 493 -5179 -365 C ATOM 1798 C PHE A 307 -28.209 22.040 -0.525 1.00 62.10 C ANISOU 1798 C PHE A 307 7860 5706 10030 471 -5238 -308 C ATOM 1799 O PHE A 307 -28.315 23.260 -0.486 1.00 62.74 O ANISOU 1799 O PHE A 307 7965 5723 10149 488 -5303 -303 O ATOM 1800 CB PHE A 307 -28.578 21.667 1.928 1.00 61.06 C ANISOU 1800 CB PHE A 307 7603 5603 9993 508 -5123 -396 C ATOM 1801 CG PHE A 307 -29.661 21.419 2.957 1.00 67.91 C ANISOU 1801 CG PHE A 307 8372 6536 10893 548 -5108 -453 C ATOM 1802 CD1 PHE A 307 -30.753 22.266 3.055 1.00 87.22 C ANISOU 1802 CD1 PHE A 307 10779 8985 13375 608 -5184 -503 C ATOM 1803 CD2 PHE A 307 -29.562 20.367 3.857 1.00 89.27 C ANISOU 1803 CD2 PHE A 307 11013 9317 13590 524 -5025 -452 C ATOM 1804 CE1 PHE A 307 -31.743 22.052 4.011 1.00109.88 C ANISOU 1804 CE1 PHE A 307 13534 11955 16261 646 -5168 -557 C ATOM 1805 CE2 PHE A 307 -30.547 20.151 4.816 1.00104.07 C ANISOU 1805 CE2 PHE A 307 12779 11290 15474 550 -5012 -490 C ATOM 1806 CZ PHE A 307 -31.638 20.993 4.891 1.00106.43 C ANISOU 1806 CZ PHE A 307 13026 11615 15797 611 -5079 -545 C ATOM 1807 N LEU A 308 -27.438 21.420 -1.412 1.00 75.27 N ANISOU 1807 N LEU A 308 9564 7417 11620 431 -5220 -265 N ATOM 1808 CA LEU A 308 -27.047 22.074 -2.658 1.00 77.97 C ANISOU 1808 CA LEU A 308 9967 7771 11886 405 -5293 -198 C ATOM 1809 C LEU A 308 -28.165 21.910 -3.685 1.00 86.94 C ANISOU 1809 C LEU A 308 11111 8948 12974 427 -5387 -198 C ATOM 1810 O LEU A 308 -28.507 22.844 -4.413 1.00 81.51 O ANISOU 1810 O LEU A 308 10463 8244 12262 429 -5489 -152 O ATOM 1811 CB LEU A 308 -25.737 21.500 -3.201 1.00 86.91 C ANISOU 1811 CB LEU A 308 11114 8977 12932 360 -5236 -158 C ATOM 1812 CG LEU A 308 -24.454 22.145 -2.682 1.00109.61 C ANISOU 1812 CG LEU A 308 13995 11827 15824 324 -5188 -120 C ATOM 1813 CD1 LEU A 308 -23.239 21.305 -3.061 1.00139.90 C ANISOU 1813 CD1 LEU A 308 17812 15763 19580 294 -5119 -103 C ATOM 1814 CD2 LEU A 308 -24.329 23.566 -3.216 1.00 90.05 C ANISOU 1814 CD2 LEU A 308 11568 9308 13338 298 -5280 -46 C ATOM 1815 N VAL A 309 -28.733 20.708 -3.726 1.00106.58 N ANISOU 1815 N VAL A 309 13560 11486 15450 440 -5362 -244 N ATOM 1816 CA VAL A 309 -29.775 20.366 -4.689 1.00100.62 C ANISOU 1816 CA VAL A 309 12801 10785 14645 458 -5450 -252 C ATOM 1817 C VAL A 309 -30.947 21.330 -4.624 1.00 85.22 C ANISOU 1817 C VAL A 309 10838 8793 12749 500 -5546 -259 C ATOM 1818 O VAL A 309 -31.313 21.955 -5.618 1.00 73.67 O ANISOU 1818 O VAL A 309 9412 7347 11232 506 -5653 -216 O ATOM 1819 CB VAL A 309 -30.306 18.939 -4.452 1.00 72.55 C ANISOU 1819 CB VAL A 309 9192 7267 11106 464 -5413 -310 C ATOM 1820 CG1 VAL A 309 -31.680 18.762 -5.089 1.00 66.42 C ANISOU 1820 CG1 VAL A 309 8388 6533 10317 489 -5512 -331 C ATOM 1821 CG2 VAL A 309 -29.320 17.917 -4.976 1.00 64.40 C ANISOU 1821 CG2 VAL A 309 8178 6288 10003 435 -5365 -311 C ATOM 1822 N ASN A 310 -31.507 21.471 -3.432 1.00 74.16 N ANISOU 1822 N ASN A 310 9377 7350 11450 534 -5514 -314 N ATOM 1823 CA ASN A 310 -32.745 22.209 -3.251 1.00 76.35 C ANISOU 1823 CA ASN A 310 9613 7611 11786 591 -5602 -347 C ATOM 1824 C ASN A 310 -32.656 23.620 -3.829 1.00103.65 C ANISOU 1824 C ASN A 310 13135 10999 15249 604 -5710 -299 C ATOM 1825 O ASN A 310 -33.677 24.264 -4.069 1.00130.15 O ANISOU 1825 O ASN A 310 16470 14341 18639 656 -5819 -314 O ATOM 1826 CB ASN A 310 -33.125 22.245 -1.767 1.00 66.70 C ANISOU 1826 CB ASN A 310 8306 6382 10654 625 -5537 -415 C ATOM 1827 CG ASN A 310 -34.612 22.444 -1.547 1.00 94.71 C ANISOU 1827 CG ASN A 310 11763 9975 14248 688 -5609 -470 C ATOM 1828 OD1 ASN A 310 -35.416 22.288 -2.468 1.00124.52 O ANISOU 1828 OD1 ASN A 310 15531 13789 17992 701 -5698 -461 O ATOM 1829 ND2 ASN A 310 -34.987 22.785 -0.318 1.00 92.80 N ANISOU 1829 ND2 ASN A 310 11439 9750 14072 731 -5574 -532 N ATOM 1830 N ILE A 311 -31.439 24.104 -4.052 1.00 67.86 N ANISOU 1830 N ILE A 311 8674 6425 10684 557 -5689 -237 N ATOM 1831 CA ILE A 311 -31.271 25.394 -4.706 1.00 69.08 C ANISOU 1831 CA ILE A 311 8897 6515 10837 551 -5804 -166 C ATOM 1832 C ILE A 311 -31.498 25.271 -6.202 1.00 89.53 C ANISOU 1832 C ILE A 311 11529 9185 13305 529 -5898 -90 C ATOM 1833 O ILE A 311 -32.152 26.118 -6.813 1.00 99.37 O ANISOU 1833 O ILE A 311 12800 10402 14555 555 -6034 -49 O ATOM 1834 CB ILE A 311 -29.893 26.002 -4.443 1.00 72.29 C ANISOU 1834 CB ILE A 311 9355 6863 11249 496 -5761 -112 C ATOM 1835 CG1 ILE A 311 -29.921 26.753 -3.122 1.00 67.79 C ANISOU 1835 CG1 ILE A 311 8758 6186 10813 534 -5745 -180 C ATOM 1836 CG2 ILE A 311 -29.527 26.981 -5.539 1.00 75.40 C ANISOU 1836 CG2 ILE A 311 9827 7237 11586 455 -5879 4 C ATOM 1837 CD1 ILE A 311 -31.048 27.741 -3.040 1.00 69.42 C ANISOU 1837 CD1 ILE A 311 8953 6315 11108 605 -5877 -221 C ATOM 1838 N VAL A 312 -30.957 24.212 -6.791 1.00 88.40 N ANISOU 1838 N VAL A 312 11389 9150 13048 488 -5833 -73 N ATOM 1839 CA VAL A 312 -31.201 23.945 -8.200 1.00 96.34 C ANISOU 1839 CA VAL A 312 12422 10270 13914 473 -5917 -16 C ATOM 1840 C VAL A 312 -32.682 23.631 -8.382 1.00103.95 C ANISOU 1840 C VAL A 312 13336 11256 14903 530 -5996 -71 C ATOM 1841 O VAL A 312 -33.239 23.816 -9.463 1.00 96.28 O ANISOU 1841 O VAL A 312 12384 10354 13845 537 -6113 -23 O ATOM 1842 CB VAL A 312 -30.347 22.781 -8.716 1.00 83.89 C ANISOU 1842 CB VAL A 312 10844 8818 12214 430 -5831 -18 C ATOM 1843 CG1 VAL A 312 -30.303 22.801 -10.234 1.00 79.66 C ANISOU 1843 CG1 VAL A 312 10344 8424 11498 405 -5925 57 C ATOM 1844 CG2 VAL A 312 -28.943 22.872 -8.145 1.00 68.94 C ANISOU 1844 CG2 VAL A 312 8963 6900 10330 387 -5723 3 C ATOM 1845 N ASN A 313 -33.312 23.155 -7.309 1.00110.40 N ANISOU 1845 N ASN A 313 14080 12035 15832 568 -5935 -165 N ATOM 1846 CA ASN A 313 -34.761 22.992 -7.273 1.00105.18 C ANISOU 1846 CA ASN A 313 13349 11398 15218 624 -6009 -220 C ATOM 1847 C ASN A 313 -35.434 24.302 -7.654 1.00 90.68 C ANISOU 1847 C ASN A 313 11531 9510 13415 671 -6157 -183 C ATOM 1848 O ASN A 313 -36.403 24.318 -8.411 1.00108.12 O ANISOU 1848 O ASN A 313 13716 11776 15587 703 -6273 -174 O ATOM 1849 CB ASN A 313 -35.215 22.534 -5.880 1.00115.40 C ANISOU 1849 CB ASN A 313 14552 12669 16627 654 -5917 -311 C ATOM 1850 CG ASN A 313 -36.713 22.712 -5.653 1.00119.89 C ANISOU 1850 CG ASN A 313 15026 13267 17260 720 -6001 -367 C ATOM 1851 OD1 ASN A 313 -37.144 23.647 -4.973 1.00103.30 O ANISOU 1851 OD1 ASN A 313 12890 11111 15248 777 -6036 -400 O ATOM 1852 ND2 ASN A 313 -37.509 21.804 -6.211 1.00134.91 N ANISOU 1852 ND2 ASN A 313 16877 15265 19117 717 -6038 -384 N ATOM 1853 N VAL A 314 -34.900 25.403 -7.138 1.00 74.52 N ANISOU 1853 N VAL A 314 9524 7350 11441 676 -6166 -160 N ATOM 1854 CA VAL A 314 -35.423 26.724 -7.462 1.00 85.32 C ANISOU 1854 CA VAL A 314 10919 8638 12859 721 -6321 -121 C ATOM 1855 C VAL A 314 -35.046 27.164 -8.881 1.00 91.66 C ANISOU 1855 C VAL A 314 11812 9480 13535 675 -6432 15 C ATOM 1856 O VAL A 314 -35.902 27.612 -9.642 1.00 84.25 O ANISOU 1856 O VAL A 314 10876 8561 12575 715 -6580 55 O ATOM 1857 CB VAL A 314 -34.972 27.782 -6.428 1.00 75.88 C ANISOU 1857 CB VAL A 314 9739 7298 11795 740 -6311 -149 C ATOM 1858 CG1 VAL A 314 -35.054 29.176 -7.016 1.00 77.85 C ANISOU 1858 CG1 VAL A 314 10057 7445 12079 755 -6482 -68 C ATOM 1859 CG2 VAL A 314 -35.813 27.680 -5.167 1.00 75.54 C ANISOU 1859 CG2 VAL A 314 9587 7243 11870 819 -6268 -283 C ATOM 1860 N PHE A 315 -33.773 27.023 -9.240 1.00 95.12 N ANISOU 1860 N PHE A 315 12315 9949 13878 595 -6364 90 N ATOM 1861 CA PHE A 315 -33.287 27.534 -10.524 1.00103.63 C ANISOU 1861 CA PHE A 315 13471 11088 14815 543 -6463 235 C ATOM 1862 C PHE A 315 -33.739 26.756 -11.769 1.00124.15 C ANISOU 1862 C PHE A 315 16065 13866 17241 537 -6516 267 C ATOM 1863 O PHE A 315 -34.298 27.336 -12.700 1.00122.04 O ANISOU 1863 O PHE A 315 15828 13636 16907 553 -6669 353 O ATOM 1864 CB PHE A 315 -31.766 27.701 -10.487 1.00104.94 C ANISOU 1864 CB PHE A 315 13689 11256 14926 459 -6377 308 C ATOM 1865 CG PHE A 315 -31.324 28.971 -9.821 1.00126.70 C ANISOU 1865 CG PHE A 315 16485 13840 17814 448 -6418 344 C ATOM 1866 CD1 PHE A 315 -30.441 29.832 -10.450 1.00146.75 C ANISOU 1866 CD1 PHE A 315 19098 16371 20289 375 -6484 492 C ATOM 1867 CD2 PHE A 315 -31.824 29.323 -8.578 1.00123.28 C ANISOU 1867 CD2 PHE A 315 16010 13265 17565 511 -6401 229 C ATOM 1868 CE1 PHE A 315 -30.045 31.009 -9.841 1.00146.98 C ANISOU 1868 CE1 PHE A 315 19164 16227 20454 359 -6539 524 C ATOM 1869 CE2 PHE A 315 -31.435 30.498 -7.965 1.00125.00 C ANISOU 1869 CE2 PHE A 315 16262 13323 17908 505 -6453 245 C ATOM 1870 CZ PHE A 315 -30.544 31.342 -8.596 1.00134.26 C ANISOU 1870 CZ PHE A 315 17514 14463 19035 427 -6526 392 C ATOM 1871 N ASN A 316 -33.495 25.450 -11.786 1.00139.11 N ANISOU 1871 N ASN A 316 18540 16579 17736 1291 -4709 1177 N ATOM 1872 CA ASN A 316 -33.958 24.603 -12.882 1.00152.55 C ANISOU 1872 CA ASN A 316 20160 18511 19291 1350 -4687 1193 C ATOM 1873 C ASN A 316 -34.631 23.346 -12.330 1.00145.09 C ANISOU 1873 C ASN A 316 19225 17534 18368 1364 -4639 992 C ATOM 1874 O ASN A 316 -33.980 22.513 -11.694 1.00159.65 O ANISOU 1874 O ASN A 316 21105 19327 20229 1324 -4571 882 O ATOM 1875 CB ASN A 316 -32.794 24.234 -13.815 1.00172.29 C ANISOU 1875 CB ASN A 316 22599 21234 21631 1338 -4645 1310 C ATOM 1876 CG ASN A 316 -32.400 25.373 -14.751 1.00174.79 C ANISOU 1876 CG ASN A 316 22870 21664 21877 1348 -4704 1545 C ATOM 1877 OD1 ASN A 316 -33.253 26.107 -15.249 1.00183.65 O ANISOU 1877 OD1 ASN A 316 23976 22796 23006 1396 -4775 1629 O ATOM 1878 ND2 ASN A 316 -31.102 25.516 -14.999 1.00166.99 N ANISOU 1878 ND2 ASN A 316 21859 20776 20813 1307 -4675 1659 N ATOM 1879 N ARG A 317 -35.930 23.206 -12.577 1.00114.46 N ANISOU 1879 N ARG A 317 15312 13690 14487 1421 -4677 955 N ATOM 1880 CA ARG A 317 -36.697 22.124 -11.961 1.00114.57 C ANISOU 1880 CA ARG A 317 15335 13656 14539 1427 -4648 778 C ATOM 1881 C ARG A 317 -36.373 20.731 -12.505 1.00122.33 C ANISOU 1881 C ARG A 317 16296 14769 15413 1420 -4604 712 C ATOM 1882 O ARG A 317 -36.017 19.834 -11.742 1.00113.21 O ANISOU 1882 O ARG A 317 15192 13521 14302 1387 -4550 580 O ATOM 1883 CB ARG A 317 -38.203 22.393 -12.056 1.00108.34 C ANISOU 1883 CB ARG A 317 14501 12892 13770 1490 -4707 771 C ATOM 1884 CG ARG A 317 -38.689 23.539 -11.184 1.00126.33 C ANISOU 1884 CG ARG A 317 16816 15010 16173 1516 -4748 774 C ATOM 1885 CD ARG A 317 -40.200 23.488 -10.984 1.00158.47 C ANISOU 1885 CD ARG A 317 20834 19115 20262 1587 -4784 726 C ATOM 1886 NE ARG A 317 -40.937 23.617 -12.239 1.00182.49 N ANISOU 1886 NE ARG A 317 23788 22358 23192 1646 -4835 839 N ATOM 1887 CZ ARG A 317 -41.372 24.770 -12.739 1.00181.01 C ANISOU 1887 CZ ARG A 317 23576 22208 22993 1715 -4901 971 C ATOM 1888 NH1 ARG A 317 -41.146 25.906 -12.093 1.00179.22 N ANISOU 1888 NH1 ARG A 317 23418 21813 22866 1733 -4935 1000 N ATOM 1889 NH2 ARG A 317 -42.035 24.788 -13.889 1.00171.86 N ANISOU 1889 NH2 ARG A 317 22326 21255 21719 1771 -4942 1073 N ATOM 1890 N ASP A 318 -36.481 20.557 -13.819 1.00138.80 N ANISOU 1890 N ASP A 318 18309 17075 17354 1457 -4633 804 N ATOM 1891 CA ASP A 318 -36.316 19.235 -14.427 1.00142.99 C ANISOU 1891 CA ASP A 318 18820 17738 17770 1464 -4615 729 C ATOM 1892 C ASP A 318 -34.861 18.857 -14.705 1.00149.97 C ANISOU 1892 C ASP A 318 19713 18705 18562 1449 -4560 758 C ATOM 1893 O ASP A 318 -34.579 17.752 -15.170 1.00149.37 O ANISOU 1893 O ASP A 318 19634 18733 18387 1465 -4547 687 O ATOM 1894 CB ASP A 318 -37.178 19.084 -15.690 1.00144.63 C ANISOU 1894 CB ASP A 318 18938 18166 17850 1514 -4680 790 C ATOM 1895 CG ASP A 318 -37.252 20.360 -16.512 1.00143.80 C ANISOU 1895 CG ASP A 318 18762 18193 17683 1552 -4722 988 C ATOM 1896 OD1 ASP A 318 -38.305 20.598 -17.142 1.00119.27 O ANISOU 1896 OD1 ASP A 318 15588 15199 14532 1597 -4781 1036 O ATOM 1897 OD2 ASP A 318 -36.261 21.121 -16.532 1.00157.55 O ANISOU 1897 OD2 ASP A 318 20513 19931 19418 1539 -4699 1103 O ATOM 1898 N LEU A 319 -33.941 19.774 -14.416 1.00155.83 N ANISOU 1898 N LEU A 319 20467 19408 19334 1422 -4534 864 N ATOM 1899 CA LEU A 319 -32.518 19.461 -14.487 1.00154.41 C ANISOU 1899 CA LEU A 319 20285 19309 19073 1406 -4473 897 C ATOM 1900 C LEU A 319 -32.126 18.636 -13.266 1.00137.24 C ANISOU 1900 C LEU A 319 18200 16946 17000 1371 -4412 725 C ATOM 1901 O LEU A 319 -31.011 18.121 -13.184 1.00124.45 O ANISOU 1901 O LEU A 319 16586 15384 15316 1367 -4354 715 O ATOM 1902 CB LEU A 319 -31.666 20.735 -14.574 1.00168.28 C ANISOU 1902 CB LEU A 319 22017 21096 20827 1380 -4476 1082 C ATOM 1903 CG LEU A 319 -31.256 21.228 -15.970 1.00184.14 C ANISOU 1903 CG LEU A 319 23916 23396 22652 1422 -4502 1288 C ATOM 1904 CD1 LEU A 319 -32.442 21.807 -16.732 1.00188.58 C ANISOU 1904 CD1 LEU A 319 24433 24022 23197 1468 -4578 1362 C ATOM 1905 CD2 LEU A 319 -30.127 22.251 -15.883 1.00183.18 C ANISOU 1905 CD2 LEU A 319 23783 23293 22525 1384 -4493 1456 C ATOM 1906 N VAL A 320 -33.071 18.494 -12.338 1.00142.48 N ANISOU 1906 N VAL A 320 18920 17408 17808 1355 -4423 598 N ATOM 1907 CA VAL A 320 -32.849 17.794 -11.073 1.00135.43 C ANISOU 1907 CA VAL A 320 18106 16329 17022 1324 -4369 441 C ATOM 1908 C VAL A 320 -33.763 16.579 -10.910 1.00125.26 C ANISOU 1908 C VAL A 320 16844 14995 15755 1342 -4382 291 C ATOM 1909 O VAL A 320 -34.880 16.711 -10.407 1.00109.43 O ANISOU 1909 O VAL A 320 14839 12894 13844 1336 -4414 242 O ATOM 1910 CB VAL A 320 -33.110 18.716 -9.867 1.00120.93 C ANISOU 1910 CB VAL A 320 16310 14289 15348 1282 -4371 422 C ATOM 1911 CG1 VAL A 320 -32.916 17.953 -8.566 1.00105.71 C ANISOU 1911 CG1 VAL A 320 14448 12200 13516 1255 -4312 266 C ATOM 1912 CG2 VAL A 320 -32.210 19.936 -9.920 1.00127.42 C ANISOU 1912 CG2 VAL A 320 17123 15118 16173 1251 -4377 565 C ATOM 1913 N PRO A 321 -33.292 15.392 -11.334 1.00125.22 N ANISOU 1913 N PRO A 321 16857 15064 15657 1368 -4365 221 N ATOM 1914 CA PRO A 321 -34.037 14.134 -11.182 1.00108.84 C ANISOU 1914 CA PRO A 321 14822 12928 13604 1379 -4391 79 C ATOM 1915 C PRO A 321 -34.568 13.963 -9.756 1.00 99.78 C ANISOU 1915 C PRO A 321 13723 11567 12621 1338 -4367 -21 C ATOM 1916 O PRO A 321 -33.912 14.402 -8.814 1.00109.90 O ANISOU 1916 O PRO A 321 15035 12745 13977 1310 -4309 -26 O ATOM 1917 CB PRO A 321 -32.982 13.073 -11.500 1.00 99.19 C ANISOU 1917 CB PRO A 321 13643 11765 12281 1415 -4359 17 C ATOM 1918 CG PRO A 321 -32.084 13.750 -12.493 1.00115.09 C ANISOU 1918 CG PRO A 321 15587 13992 14149 1441 -4347 162 C ATOM 1919 CD PRO A 321 -32.028 15.199 -12.071 1.00125.28 C ANISOU 1919 CD PRO A 321 16842 15240 15519 1395 -4331 288 C ATOM 1920 N ASP A 322 -35.744 13.355 -9.609 1.00 95.41 N ANISOU 1920 N ASP A 322 13164 10973 12115 1332 -4417 -87 N ATOM 1921 CA ASP A 322 -36.446 13.317 -8.321 1.00104.60 C ANISOU 1921 CA ASP A 322 14338 11985 13420 1297 -4403 -149 C ATOM 1922 C ASP A 322 -36.122 12.099 -7.449 1.00116.27 C ANISOU 1922 C ASP A 322 15887 13337 14954 1277 -4369 -267 C ATOM 1923 O ASP A 322 -36.538 12.037 -6.292 1.00129.96 O ANISOU 1923 O ASP A 322 17623 14961 16796 1246 -4346 -310 O ATOM 1924 CB ASP A 322 -37.965 13.428 -8.533 1.00114.39 C ANISOU 1924 CB ASP A 322 15506 13277 14679 1298 -4475 -128 C ATOM 1925 CG ASP A 322 -38.724 13.734 -7.245 1.00115.31 C ANISOU 1925 CG ASP A 322 15599 13292 14920 1276 -4458 -154 C ATOM 1926 OD1 ASP A 322 -38.849 14.927 -6.896 1.00120.78 O ANISOU 1926 OD1 ASP A 322 16265 13973 15652 1291 -4449 -101 O ATOM 1927 OD2 ASP A 322 -39.208 12.786 -6.588 1.00112.75 O ANISOU 1927 OD2 ASP A 322 15280 12910 14650 1249 -4463 -222 O ATOM 1928 N TRP A 323 -35.396 11.126 -7.992 1.00122.01 N ANISOU 1928 N TRP A 323 16668 14088 15601 1304 -4369 -317 N ATOM 1929 CA TRP A 323 -34.968 9.988 -7.180 1.00127.88 C ANISOU 1929 CA TRP A 323 17490 14704 16394 1297 -4340 -423 C ATOM 1930 C TRP A 323 -33.749 10.374 -6.347 1.00127.99 C ANISOU 1930 C TRP A 323 17538 14661 16433 1293 -4244 -429 C ATOM 1931 O TRP A 323 -33.613 9.965 -5.194 1.00131.49 O ANISOU 1931 O TRP A 323 18015 14982 16963 1267 -4202 -492 O ATOM 1932 CB TRP A 323 -34.710 8.742 -8.041 1.00136.26 C ANISOU 1932 CB TRP A 323 18610 15801 17362 1344 -4393 -489 C ATOM 1933 CG TRP A 323 -33.343 8.648 -8.661 1.00153.61 C ANISOU 1933 CG TRP A 323 20841 18090 19435 1408 -4351 -489 C ATOM 1934 CD1 TRP A 323 -32.706 9.600 -9.405 1.00159.10 C ANISOU 1934 CD1 TRP A 323 21478 18945 20029 1430 -4323 -387 C ATOM 1935 CD2 TRP A 323 -32.463 7.516 -8.621 1.00164.13 C ANISOU 1935 CD2 TRP A 323 22262 19382 20717 1465 -4339 -584 C ATOM 1936 NE1 TRP A 323 -31.477 9.138 -9.814 1.00162.98 N ANISOU 1936 NE1 TRP A 323 22001 19520 20403 1494 -4287 -406 N ATOM 1937 CE2 TRP A 323 -31.305 7.861 -9.346 1.00171.72 C ANISOU 1937 CE2 TRP A 323 23204 20505 21538 1525 -4295 -536 C ATOM 1938 CE3 TRP A 323 -32.539 6.247 -8.035 1.00156.06 C ANISOU 1938 CE3 TRP A 323 21333 18209 19754 1474 -4367 -696 C ATOM 1939 CZ2 TRP A 323 -30.231 6.984 -9.501 1.00173.56 C ANISOU 1939 CZ2 TRP A 323 23503 20765 21677 1607 -4272 -608 C ATOM 1940 CZ3 TRP A 323 -31.472 5.378 -8.190 1.00145.93 C ANISOU 1940 CZ3 TRP A 323 20132 16925 18389 1558 -4351 -773 C ATOM 1941 CH2 TRP A 323 -30.334 5.750 -8.916 1.00157.15 C ANISOU 1941 CH2 TRP A 323 21529 18521 19661 1630 -4301 -736 C ATOM 1942 N LEU A 324 -32.879 11.184 -6.941 1.00123.30 N ANISOU 1942 N LEU A 324 16919 14174 15755 1313 -4214 -350 N ATOM 1943 CA LEU A 324 -31.738 11.758 -6.240 1.00105.77 C ANISOU 1943 CA LEU A 324 14708 11929 13549 1298 -4132 -326 C ATOM 1944 C LEU A 324 -32.216 12.593 -5.058 1.00 97.75 C ANISOU 1944 C LEU A 324 13676 10798 12667 1244 -4113 -326 C ATOM 1945 O LEU A 324 -31.588 12.608 -3.997 1.00116.14 O ANISOU 1945 O LEU A 324 16030 13046 15051 1222 -4051 -368 O ATOM 1946 CB LEU A 324 -30.929 12.641 -7.191 1.00 93.11 C ANISOU 1946 CB LEU A 324 13055 10488 11834 1316 -4124 -200 C ATOM 1947 CG LEU A 324 -29.474 12.240 -7.427 1.00 93.16 C ANISOU 1947 CG LEU A 324 13073 10593 11729 1355 -4066 -187 C ATOM 1948 CD1 LEU A 324 -29.389 10.771 -7.818 1.00113.73 C ANISOU 1948 CD1 LEU A 324 15738 13212 14264 1421 -4082 -298 C ATOM 1949 CD2 LEU A 324 -28.839 13.129 -8.490 1.00 56.50 C ANISOU 1949 CD2 LEU A 324 8352 6154 6962 1366 -4071 -27 C ATOM 1950 N PHE A 325 -33.331 13.289 -5.255 1.00 85.40 N ANISOU 1950 N PHE A 325 12062 9242 11143 1234 -4168 -281 N ATOM 1951 CA PHE A 325 -33.909 14.140 -4.225 1.00106.64 C ANISOU 1951 CA PHE A 325 14729 11845 13943 1205 -4164 -284 C ATOM 1952 C PHE A 325 -34.132 13.325 -2.959 1.00103.44 C ANISOU 1952 C PHE A 325 14347 11332 13622 1185 -4127 -387 C ATOM 1953 O PHE A 325 -33.998 13.841 -1.853 1.00133.61 O ANISOU 1953 O PHE A 325 18166 15084 17515 1165 -4090 -413 O ATOM 1954 CB PHE A 325 -35.227 14.749 -4.720 1.00147.50 C ANISOU 1954 CB PHE A 325 19844 17071 19130 1220 -4237 -230 C ATOM 1955 CG PHE A 325 -35.605 16.054 -4.049 1.00133.78 C ANISOU 1955 CG PHE A 325 18080 15284 17467 1219 -4248 -198 C ATOM 1956 CD1 PHE A 325 -34.746 17.145 -4.075 1.00 85.53 C ANISOU 1956 CD1 PHE A 325 11986 9157 11355 1207 -4242 -134 C ATOM 1957 CD2 PHE A 325 -36.843 16.197 -3.431 1.00136.91 C ANISOU 1957 CD2 PHE A 325 18429 15663 17926 1236 -4276 -224 C ATOM 1958 CE1 PHE A 325 -35.104 18.339 -3.473 1.00 80.67 C ANISOU 1958 CE1 PHE A 325 11362 8478 10810 1213 -4273 -116 C ATOM 1959 CE2 PHE A 325 -37.207 17.389 -2.830 1.00117.46 C ANISOU 1959 CE2 PHE A 325 15947 13164 15519 1258 -4296 -206 C ATOM 1960 CZ PHE A 325 -36.337 18.461 -2.850 1.00102.08 C ANISOU 1960 CZ PHE A 325 14037 11171 13579 1248 -4300 -160 C ATOM 1961 N VAL A 326 -34.490 12.055 -3.123 1.00 77.06 N ANISOU 1961 N VAL A 326 11027 7982 10270 1190 -4146 -441 N ATOM 1962 CA VAL A 326 -34.609 11.147 -1.984 1.00 92.89 C ANISOU 1962 CA VAL A 326 13054 9893 12346 1168 -4116 -520 C ATOM 1963 C VAL A 326 -33.262 10.547 -1.543 1.00111.71 C ANISOU 1963 C VAL A 326 15506 12231 14706 1173 -4047 -576 C ATOM 1964 O VAL A 326 -32.953 10.466 -0.342 1.00115.93 O ANISOU 1964 O VAL A 326 16046 12702 15300 1151 -3991 -620 O ATOM 1965 CB VAL A 326 -35.616 10.026 -2.271 1.00 86.68 C ANISOU 1965 CB VAL A 326 12261 9102 11570 1161 -4183 -541 C ATOM 1966 CG1 VAL A 326 -35.750 9.124 -1.060 1.00104.61 C ANISOU 1966 CG1 VAL A 326 14545 11282 13920 1129 -4159 -596 C ATOM 1967 CG2 VAL A 326 -36.963 10.620 -2.644 1.00 91.20 C ANISOU 1967 CG2 VAL A 326 12747 9750 12155 1159 -4246 -478 C ATOM 1968 N ALA A 327 -32.459 10.140 -2.523 1.00112.70 N ANISOU 1968 N ALA A 327 15673 12415 14732 1212 -4050 -572 N ATOM 1969 CA ALA A 327 -31.166 9.516 -2.252 1.00 92.31 C ANISOU 1969 CA ALA A 327 13149 9823 12101 1239 -3987 -619 C ATOM 1970 C ALA A 327 -30.278 10.380 -1.358 1.00 83.84 C ANISOU 1970 C ALA A 327 12058 8746 11052 1214 -3908 -600 C ATOM 1971 O ALA A 327 -29.501 9.855 -0.564 1.00 83.40 O ANISOU 1971 O ALA A 327 12035 8656 10999 1219 -3849 -654 O ATOM 1972 CB ALA A 327 -30.447 9.191 -3.555 1.00 82.09 C ANISOU 1972 CB ALA A 327 11879 8642 10671 1304 -4004 -598 C ATOM 1973 N PHE A 328 -30.379 11.699 -1.503 1.00 83.39 N ANISOU 1973 N PHE A 328 11952 8724 11008 1190 -3917 -522 N ATOM 1974 CA PHE A 328 -29.572 12.614 -0.697 1.00 62.03 C ANISOU 1974 CA PHE A 328 9232 6005 8331 1160 -3864 -498 C ATOM 1975 C PHE A 328 -30.120 12.868 0.709 1.00 63.26 C ANISOU 1975 C PHE A 328 9375 6064 8598 1126 -3847 -558 C ATOM 1976 O PHE A 328 -29.338 13.030 1.646 1.00 88.94 O ANISOU 1976 O PHE A 328 12633 9293 11869 1111 -3791 -585 O ATOM 1977 CB PHE A 328 -29.317 13.930 -1.433 1.00 46.92 C ANISOU 1977 CB PHE A 328 7282 4160 6387 1147 -3894 -380 C ATOM 1978 CG PHE A 328 -28.354 13.803 -2.583 1.00 83.87 C ANISOU 1978 CG PHE A 328 11952 8979 10935 1179 -3884 -299 C ATOM 1979 CD1 PHE A 328 -27.590 12.656 -2.740 1.00 92.57 C ANISOU 1979 CD1 PHE A 328 13084 10133 11954 1227 -3839 -347 C ATOM 1980 CD2 PHE A 328 -28.209 14.827 -3.504 1.00 81.76 C ANISOU 1980 CD2 PHE A 328 11640 8807 10619 1170 -3923 -167 C ATOM 1981 CE1 PHE A 328 -26.703 12.534 -3.798 1.00 90.88 C ANISOU 1981 CE1 PHE A 328 12846 10084 11599 1273 -3828 -270 C ATOM 1982 CE2 PHE A 328 -27.323 14.711 -4.563 1.00 73.61 C ANISOU 1982 CE2 PHE A 328 10577 7945 9448 1203 -3912 -73 C ATOM 1983 CZ PHE A 328 -26.571 13.564 -4.709 1.00 79.89 C ANISOU 1983 CZ PHE A 328 11392 8813 10150 1259 -3862 -127 C ATOM 1984 N ASN A 329 -31.447 12.903 0.863 1.00 45.54 N ANISOU 1984 N ASN A 329 7101 3786 6415 1122 -3896 -572 N ATOM 1985 CA ASN A 329 -32.043 13.025 2.198 1.00 59.83 C ANISOU 1985 CA ASN A 329 8881 5540 8311 1106 -3879 -624 C ATOM 1986 C ASN A 329 -31.768 11.763 2.994 1.00 65.06 C ANISOU 1986 C ASN A 329 9565 6170 8984 1101 -3829 -694 C ATOM 1987 O ASN A 329 -31.666 11.811 4.216 1.00 85.63 O ANISOU 1987 O ASN A 329 12150 8753 11634 1089 -3785 -734 O ATOM 1988 CB ASN A 329 -33.553 13.331 2.167 1.00 45.81 C ANISOU 1988 CB ASN A 329 7049 3775 6583 1117 -3940 -605 C ATOM 1989 CG ASN A 329 -33.974 14.373 3.228 1.00 65.33 C ANISOU 1989 CG ASN A 329 9477 6229 9116 1127 -3938 -619 C ATOM 1990 OD1 ASN A 329 -33.337 14.515 4.272 1.00 67.63 O ANISOU 1990 OD1 ASN A 329 9776 6489 9430 1118 -3888 -666 O ATOM 1991 ND2 ASN A 329 -35.050 15.103 2.950 1.00 66.30 N ANISOU 1991 ND2 ASN A 329 9552 6383 9255 1157 -3998 -581 N ATOM 1992 N TRP A 330 -31.639 10.631 2.313 1.00 44.12 N ANISOU 1992 N TRP A 330 6956 3520 6288 1115 -3843 -708 N ATOM 1993 CA TRP A 330 -31.194 9.436 3.025 1.00 76.27 C ANISOU 1993 CA TRP A 330 11064 7552 10364 1114 -3804 -771 C ATOM 1994 C TRP A 330 -29.678 9.448 3.285 1.00 79.55 C ANISOU 1994 C TRP A 330 11516 7992 10719 1132 -3729 -792 C ATOM 1995 O TRP A 330 -29.225 9.177 4.401 1.00 41.56 O ANISOU 1995 O TRP A 330 6700 3164 5927 1123 -3672 -834 O ATOM 1996 CB TRP A 330 -31.678 8.150 2.339 1.00 73.37 C ANISOU 1996 CB TRP A 330 10741 7153 9983 1127 -3865 -789 C ATOM 1997 CG TRP A 330 -33.142 7.883 2.590 1.00 66.93 C ANISOU 1997 CG TRP A 330 9871 6316 9244 1094 -3926 -765 C ATOM 1998 CD1 TRP A 330 -34.184 8.205 1.771 1.00 70.07 C ANISOU 1998 CD1 TRP A 330 10229 6750 9644 1093 -3997 -715 C ATOM 1999 CD2 TRP A 330 -33.724 7.267 3.753 1.00 79.45 C ANISOU 1999 CD2 TRP A 330 11417 7869 10903 1058 -3919 -772 C ATOM 2000 NE1 TRP A 330 -35.375 7.821 2.342 1.00 80.70 N ANISOU 2000 NE1 TRP A 330 11510 8095 11058 1060 -4035 -688 N ATOM 2001 CE2 TRP A 330 -35.120 7.243 3.558 1.00 88.29 C ANISOU 2001 CE2 TRP A 330 12467 9015 12064 1037 -3988 -716 C ATOM 2002 CE3 TRP A 330 -33.199 6.730 4.935 1.00 65.73 C ANISOU 2002 CE3 TRP A 330 9682 6103 9188 1044 -3861 -808 C ATOM 2003 CZ2 TRP A 330 -35.999 6.701 4.501 1.00 82.93 C ANISOU 2003 CZ2 TRP A 330 11716 8345 11450 999 -4001 -683 C ATOM 2004 CZ3 TRP A 330 -34.076 6.198 5.872 1.00 54.63 C ANISOU 2004 CZ3 TRP A 330 8209 4697 7851 1007 -3874 -778 C ATOM 2005 CH2 TRP A 330 -35.458 6.185 5.647 1.00 61.76 C ANISOU 2005 CH2 TRP A 330 9037 5634 8794 984 -3944 -710 C ATOM 2006 N LEU A 331 -28.903 9.800 2.264 1.00 93.51 N ANISOU 2006 N LEU A 331 13303 9823 12403 1162 -3727 -749 N ATOM 2007 CA LEU A 331 -27.456 9.911 2.409 1.00 84.04 C ANISOU 2007 CA LEU A 331 12116 8683 11133 1185 -3657 -740 C ATOM 2008 C LEU A 331 -27.162 10.723 3.661 1.00 87.14 C ANISOU 2008 C LEU A 331 12470 9055 11584 1144 -3608 -744 C ATOM 2009 O LEU A 331 -26.246 10.408 4.417 1.00 78.69 O ANISOU 2009 O LEU A 331 11405 8004 10489 1154 -3541 -773 O ATOM 2010 CB LEU A 331 -26.841 10.582 1.173 1.00 71.74 C ANISOU 2010 CB LEU A 331 10545 7228 9485 1208 -3670 -648 C ATOM 2011 CG LEU A 331 -25.319 10.579 0.993 1.00 55.59 C ANISOU 2011 CG LEU A 331 8494 5294 7334 1246 -3604 -606 C ATOM 2012 CD1 LEU A 331 -24.931 11.151 -0.366 1.00 60.03 C ANISOU 2012 CD1 LEU A 331 9022 5989 7798 1267 -3631 -492 C ATOM 2013 CD2 LEU A 331 -24.618 11.340 2.111 1.00 42.37 C ANISOU 2013 CD2 LEU A 331 6786 3611 5700 1203 -3546 -588 C ATOM 2014 N GLY A 332 -27.958 11.766 3.873 1.00101.45 N ANISOU 2014 N GLY A 332 14244 10835 13467 1109 -3648 -719 N ATOM 2015 CA GLY A 332 -27.841 12.600 5.054 1.00109.51 C ANISOU 2015 CA GLY A 332 15233 11828 14546 1082 -3623 -736 C ATOM 2016 C GLY A 332 -28.319 11.916 6.324 1.00 85.77 C ANISOU 2016 C GLY A 332 12208 8791 11591 1080 -3590 -811 C ATOM 2017 O GLY A 332 -27.703 12.056 7.381 1.00 67.76 O ANISOU 2017 O GLY A 332 9911 6518 9316 1076 -3536 -842 O ATOM 2018 N TYR A 333 -29.424 11.183 6.236 1.00 41.94 N ANISOU 2018 N TYR A 333 4416 4828 6693 303 -646 -1950 N ATOM 2019 CA TYR A 333 -29.899 10.441 7.392 1.00 60.63 C ANISOU 2019 CA TYR A 333 6819 7176 9040 316 -654 -1943 C ATOM 2020 C TYR A 333 -28.712 9.662 7.925 1.00 81.35 C ANISOU 2020 C TYR A 333 9465 9805 11641 350 -662 -1968 C ATOM 2021 O TYR A 333 -28.505 9.580 9.132 1.00 90.74 O ANISOU 2021 O TYR A 333 10633 11027 12816 391 -679 -1984 O ATOM 2022 CB TYR A 333 -31.043 9.488 7.023 1.00 79.78 C ANISOU 2022 CB TYR A 333 9351 9508 11455 257 -643 -1904 C ATOM 2023 CG TYR A 333 -32.401 10.143 6.822 1.00 84.92 C ANISOU 2023 CG TYR A 333 9985 10152 12130 223 -640 -1872 C ATOM 2024 CD1 TYR A 333 -32.925 11.018 7.758 1.00 47.69 C ANISOU 2024 CD1 TYR A 333 5196 5494 7429 265 -645 -1880 C ATOM 2025 CD2 TYR A 333 -33.161 9.875 5.690 1.00107.64 C ANISOU 2025 CD2 TYR A 333 12939 12957 15004 146 -640 -1837 C ATOM 2026 CE1 TYR A 333 -34.158 11.607 7.568 1.00 24.81 C ANISOU 2026 CE1 TYR A 333 2289 2584 4553 239 -638 -1853 C ATOM 2027 CE2 TYR A 333 -34.392 10.462 5.496 1.00 84.24 C ANISOU 2027 CE2 TYR A 333 9962 9984 12063 109 -642 -1803 C ATOM 2028 CZ TYR A 333 -34.881 11.324 6.441 1.00 37.17 C ANISOU 2028 CZ TYR A 333 3914 4081 6127 161 -635 -1811 C ATOM 2029 OH TYR A 333 -36.105 11.901 6.248 1.00 48.03 O ANISOU 2029 OH TYR A 333 5281 5442 7527 127 -634 -1778 O ATOM 2030 N ALA A 334 -27.909 9.132 7.006 1.00 93.81 N ANISOU 2030 N ALA A 334 11092 11348 13204 335 -647 -1976 N ATOM 2031 CA ALA A 334 -26.749 8.319 7.363 1.00101.66 C ANISOU 2031 CA ALA A 334 12124 12331 14171 369 -646 -2000 C ATOM 2032 C ALA A 334 -25.857 9.007 8.395 1.00 99.00 C ANISOU 2032 C ALA A 334 11685 12085 13846 423 -678 -2029 C ATOM 2033 O ALA A 334 -25.199 8.344 9.198 1.00 77.86 O ANISOU 2033 O ALA A 334 9031 9407 11144 458 -683 -2043 O ATOM 2034 CB ALA A 334 -25.941 7.966 6.117 1.00 90.98 C ANISOU 2034 CB ALA A 334 10835 10938 12794 357 -622 -2013 C ATOM 2035 N ASN A 335 -25.851 10.335 8.390 1.00 31.45 N ANISOU 2035 N ASN A 335 3033 3593 5322 431 -702 -2038 N ATOM 2036 CA ASN A 335 -25.009 11.065 9.316 1.00 25.89 C ANISOU 2036 CA ASN A 335 2260 2954 4623 477 -745 -2071 C ATOM 2037 C ASN A 335 -25.237 10.477 10.696 1.00 27.70 C ANISOU 2037 C ASN A 335 2523 3189 4812 509 -760 -2079 C ATOM 2038 O ASN A 335 -24.297 10.029 11.346 1.00 41.99 O ANISOU 2038 O ASN A 335 4340 5015 6600 542 -777 -2100 O ATOM 2039 CB ASN A 335 -25.345 12.559 9.281 1.00 42.33 C ANISOU 2039 CB ASN A 335 4277 5071 6736 483 -769 -2080 C ATOM 2040 CG ASN A 335 -24.282 13.426 9.946 1.00 55.08 C ANISOU 2040 CG ASN A 335 5848 6724 8357 526 -821 -2119 C ATOM 2041 OD1 ASN A 335 -24.600 14.386 10.645 1.00 26.30 O ANISOU 2041 OD1 ASN A 335 2200 3090 4704 550 -858 -2139 O ATOM 2042 ND2 ASN A 335 -23.017 13.094 9.725 1.00 26.16 N ANISOU 2042 ND2 ASN A 335 2168 3071 4701 535 -829 -2133 N ATOM 2043 N SER A 336 -26.500 10.411 11.104 1.00 67.46 N ANISOU 2043 N SER A 336 7587 8207 9836 500 -750 -2060 N ATOM 2044 CA SER A 336 -26.858 9.972 12.448 1.00 69.96 C ANISOU 2044 CA SER A 336 7939 8534 10109 535 -761 -2068 C ATOM 2045 C SER A 336 -26.137 8.691 12.860 1.00 80.74 C ANISOU 2045 C SER A 336 9358 9871 11450 554 -748 -2069 C ATOM 2046 O SER A 336 -25.552 8.626 13.938 1.00 96.88 O ANISOU 2046 O SER A 336 11400 11954 13456 603 -773 -2096 O ATOM 2047 CB SER A 336 -28.369 9.771 12.553 1.00 67.10 C ANISOU 2047 CB SER A 336 7615 8135 9744 513 -736 -2037 C ATOM 2048 OG SER A 336 -28.886 10.441 13.683 1.00 26.03 O ANISOU 2048 OG SER A 336 2413 2979 4500 558 -757 -2060 O ATOM 2049 N ALA A 337 -26.178 7.675 12.004 1.00 67.62 N ANISOU 2049 N ALA A 337 7761 8131 9800 520 -708 -2042 N ATOM 2050 CA ALA A 337 -25.532 6.404 12.317 1.00 66.02 C ANISOU 2050 CA ALA A 337 7637 7875 9573 547 -684 -2042 C ATOM 2051 C ALA A 337 -24.020 6.511 12.162 1.00 86.24 C ANISOU 2051 C ALA A 337 10168 10472 12127 578 -694 -2071 C ATOM 2052 O ALA A 337 -23.278 5.672 12.670 1.00115.30 O ANISOU 2052 O ALA A 337 13897 14129 15781 623 -674 -2077 O ATOM 2053 CB ALA A 337 -26.085 5.280 11.446 1.00 36.99 C ANISOU 2053 CB ALA A 337 4078 4075 5900 508 -640 -2010 C ATOM 2054 N MET A 338 -23.572 7.547 11.458 1.00 55.99 N ANISOU 2054 N MET A 338 6260 6691 8323 560 -717 -2086 N ATOM 2055 CA MET A 338 -22.148 7.769 11.244 1.00 63.90 C ANISOU 2055 CA MET A 338 7224 7727 9327 585 -731 -2114 C ATOM 2056 C MET A 338 -21.491 8.366 12.489 1.00 88.99 C ANISOU 2056 C MET A 338 10338 10980 12493 628 -788 -2147 C ATOM 2057 O MET A 338 -20.331 8.083 12.788 1.00102.04 O ANISOU 2057 O MET A 338 11989 12649 14132 664 -797 -2167 O ATOM 2058 CB MET A 338 -21.914 8.680 10.030 1.00 63.08 C ANISOU 2058 CB MET A 338 7063 7641 9262 551 -735 -2116 C ATOM 2059 CG MET A 338 -22.347 8.087 8.693 1.00 63.85 C ANISOU 2059 CG MET A 338 7243 7664 9352 515 -681 -2094 C ATOM 2060 SD MET A 338 -22.340 9.269 7.318 1.00 87.36 S ANISOU 2060 SD MET A 338 10151 10670 12370 476 -684 -2094 S ATOM 2061 CE MET A 338 -20.621 9.207 6.813 1.00 57.19 C ANISOU 2061 CE MET A 338 6322 6867 8542 508 -677 -2125 C ATOM 2062 N ASN A 339 -22.240 9.185 13.221 1.00 99.55 N ANISOU 2062 N ASN A 339 11642 12357 13826 633 -826 -2154 N ATOM 2063 CA ASN A 339 -21.678 9.934 14.352 1.00103.23 C ANISOU 2063 CA ASN A 339 12075 12882 14267 679 -888 -2195 C ATOM 2064 C ASN A 339 -21.049 9.118 15.489 1.00105.27 C ANISOU 2064 C ASN A 339 12370 13157 14471 730 -897 -2214 C ATOM 2065 O ASN A 339 -19.863 9.284 15.779 1.00101.71 O ANISOU 2065 O ASN A 339 11892 12737 14016 756 -933 -2243 O ATOM 2066 CB ASN A 339 -22.696 10.937 14.910 1.00 99.07 C ANISOU 2066 CB ASN A 339 11548 12372 13721 688 -915 -2205 C ATOM 2067 CG ASN A 339 -22.625 12.286 14.218 1.00 79.73 C ANISOU 2067 CG ASN A 339 9053 9922 11318 670 -940 -2215 C ATOM 2068 OD1 ASN A 339 -21.967 12.438 13.180 1.00 29.31 O ANISOU 2068 OD1 ASN A 339 2625 3527 4985 645 -928 -2205 O ATOM 2069 ND2 ASN A 339 -23.301 13.278 14.793 1.00 74.66 N ANISOU 2069 ND2 ASN A 339 8434 9284 10648 690 -971 -2236 N ATOM 2070 N PRO A 340 -21.833 8.234 16.134 1.00100.54 N ANISOU 2070 N PRO A 340 11835 12535 13832 747 -862 -2195 N ATOM 2071 CA PRO A 340 -21.290 7.520 17.295 1.00 69.56 C ANISOU 2071 CA PRO A 340 7933 8635 9861 816 -873 -2225 C ATOM 2072 C PRO A 340 -20.013 6.779 16.948 1.00 65.72 C ANISOU 2072 C PRO A 340 7412 8140 9417 854 -876 -2265 C ATOM 2073 O PRO A 340 -19.201 6.534 17.843 1.00 68.44 O ANISOU 2073 O PRO A 340 7700 8541 9762 939 -938 -2350 O ATOM 2074 CB PRO A 340 -22.393 6.512 17.641 1.00 68.17 C ANISOU 2074 CB PRO A 340 7830 8406 9665 827 -811 -2187 C ATOM 2075 CG PRO A 340 -23.198 6.374 16.399 1.00 90.45 C ANISOU 2075 CG PRO A 340 10679 11155 12532 752 -764 -2134 C ATOM 2076 CD PRO A 340 -23.162 7.726 15.753 1.00102.47 C ANISOU 2076 CD PRO A 340 12125 12723 14086 714 -812 -2154 C ATOM 2077 N ILE A 341 -19.845 6.446 15.665 1.00 73.89 N ANISOU 2077 N ILE A 341 8489 9109 10477 806 -808 -2210 N ATOM 2078 CA ILE A 341 -18.710 5.648 15.191 1.00 57.37 C ANISOU 2078 CA ILE A 341 6399 6987 8413 861 -776 -2235 C ATOM 2079 C ILE A 341 -17.498 6.501 14.823 1.00 39.15 C ANISOU 2079 C ILE A 341 3971 4748 6158 873 -854 -2313 C ATOM 2080 O ILE A 341 -16.433 5.972 14.503 1.00 38.36 O ANISOU 2080 O ILE A 341 3851 4640 6084 945 -831 -2347 O ATOM 2081 CB ILE A 341 -19.085 4.754 13.987 1.00 44.08 C ANISOU 2081 CB ILE A 341 4853 5184 6712 834 -655 -2149 C ATOM 2082 CG1 ILE A 341 -20.580 4.424 14.003 1.00 65.67 C ANISOU 2082 CG1 ILE A 341 7655 7861 9436 782 -633 -2105 C ATOM 2083 CG2 ILE A 341 -18.249 3.479 13.992 1.00 30.01 C ANISOU 2083 CG2 ILE A 341 3132 3337 4933 949 -575 -2148 C ATOM 2084 CD1 ILE A 341 -21.030 3.545 12.852 1.00 29.66 C ANISOU 2084 CD1 ILE A 341 3210 3178 4882 763 -563 -2074 C ATOM 2085 N ILE A 342 -17.663 7.819 14.866 1.00 54.56 N ANISOU 2085 N ILE A 342 5847 6755 8130 825 -932 -2332 N ATOM 2086 CA ILE A 342 -16.519 8.718 14.795 1.00 90.79 C ANISOU 2086 CA ILE A 342 10296 11407 12793 853 -1037 -2429 C ATOM 2087 C ILE A 342 -15.985 8.919 16.214 1.00 78.93 C ANISOU 2087 C ILE A 342 8716 9979 11294 938 -1156 -2539 C ATOM 2088 O ILE A 342 -14.901 9.461 16.424 1.00 56.53 O ANISOU 2088 O ILE A 342 5759 7193 8528 995 -1265 -2648 O ATOM 2089 CB ILE A 342 -16.889 10.069 14.155 1.00 93.97 C ANISOU 2089 CB ILE A 342 10686 11802 13216 789 -1040 -2380 C ATOM 2090 CG1 ILE A 342 -17.643 9.842 12.846 1.00 90.48 C ANISOU 2090 CG1 ILE A 342 10334 11300 12745 710 -928 -2271 C ATOM 2091 CG2 ILE A 342 -15.645 10.898 13.898 1.00100.55 C ANISOU 2091 CG2 ILE A 342 11389 12666 14150 829 -1130 -2475 C ATOM 2092 CD1 ILE A 342 -17.800 11.089 12.007 1.00105.53 C ANISOU 2092 CD1 ILE A 342 12212 13201 14682 663 -928 -2237 C ATOM 2093 N TYR A 343 -16.757 8.452 17.186 1.00 82.38 N ANISOU 2093 N TYR A 343 9225 10419 11655 959 -1137 -2516 N ATOM 2094 CA TYR A 343 -16.364 8.542 18.581 1.00 81.88 C ANISOU 2094 CA TYR A 343 9115 10432 11562 1052 -1243 -2620 C ATOM 2095 C TYR A 343 -15.633 7.288 19.023 1.00 78.09 C ANISOU 2095 C TYR A 343 8614 9980 11076 1145 -1238 -2677 C ATOM 2096 O TYR A 343 -15.245 7.159 20.181 1.00102.45 O ANISOU 2096 O TYR A 343 11657 13147 14123 1244 -1322 -2768 O ATOM 2097 CB TYR A 343 -17.586 8.785 19.456 1.00 95.98 C ANISOU 2097 CB TYR A 343 10997 12217 13254 1046 -1220 -2574 C ATOM 2098 CG TYR A 343 -18.231 10.114 19.190 1.00 98.20 C ANISOU 2098 CG TYR A 343 11336 12461 13514 979 -1207 -2515 C ATOM 2099 CD1 TYR A 343 -17.590 11.292 19.538 1.00105.90 C ANISOU 2099 CD1 TYR A 343 12315 13439 14483 985 -1293 -2568 C ATOM 2100 CD2 TYR A 343 -19.474 10.195 18.579 1.00 91.01 C ANISOU 2100 CD2 TYR A 343 10507 11496 12578 901 -1106 -2404 C ATOM 2101 CE1 TYR A 343 -18.169 12.518 19.290 1.00126.25 C ANISOU 2101 CE1 TYR A 343 14986 15960 17023 913 -1273 -2508 C ATOM 2102 CE2 TYR A 343 -20.064 11.419 18.327 1.00107.85 C ANISOU 2102 CE2 TYR A 343 12698 13596 14684 848 -1092 -2355 C ATOM 2103 CZ TYR A 343 -19.406 12.579 18.683 1.00113.92 C ANISOU 2103 CZ TYR A 343 13479 14362 15442 856 -1171 -2406 C ATOM 2104 OH TYR A 343 -19.983 13.806 18.437 1.00 69.33 O ANISOU 2104 OH TYR A 343 7878 8675 9789 824 -1184 -2399 O ATOM 2105 N CYS A 344 -15.443 6.362 18.092 1.00 70.23 N ANISOU 2105 N CYS A 344 7674 8908 10103 1142 -1106 -2594 N ATOM 2106 CA CYS A 344 -14.617 5.195 18.359 1.00110.41 C ANISOU 2106 CA CYS A 344 12757 14001 15194 1281 -1017 -2556 C ATOM 2107 C CYS A 344 -13.158 5.621 18.427 1.00153.63 C ANISOU 2107 C CYS A 344 18064 19580 20729 1375 -1097 -2618 C ATOM 2108 O CYS A 344 -12.281 4.814 18.745 1.00180.74 O ANISOU 2108 O CYS A 344 21416 23083 24174 1522 -1016 -2497 O ATOM 2109 CB CYS A 344 -14.810 4.125 17.281 1.00102.50 C ANISOU 2109 CB CYS A 344 11877 12872 14195 1287 -828 -2411 C ATOM 2110 SG CYS A 344 -16.265 3.078 17.510 1.00102.00 S ANISOU 2110 SG CYS A 344 11980 12692 14084 1256 -720 -2309 S ATOM 2111 N ARG A 345 -12.904 6.889 18.120 1.00154.31 N ANISOU 2111 N ARG A 345 18069 19694 20868 1295 -1251 -2754 N ATOM 2112 CA ARG A 345 -11.542 7.421 18.070 1.00151.37 C ANISOU 2112 CA ARG A 345 17498 19439 20575 1354 -1341 -2744 C ATOM 2113 C ARG A 345 -10.948 7.844 19.424 1.00160.04 C ANISOU 2113 C ARG A 345 18468 20712 21627 1354 -1529 -2716 C ATOM 2114 O ARG A 345 -9.728 7.949 19.556 1.00175.11 O ANISOU 2114 O ARG A 345 20212 22782 23539 1328 -1589 -2514 O ATOM 2115 CB ARG A 345 -11.448 8.566 17.054 1.00121.65 C ANISOU 2115 CB ARG A 345 13712 15620 16889 1232 -1423 -2834 C ATOM 2116 CG ARG A 345 -11.370 8.089 15.612 1.00 96.71 C ANISOU 2116 CG ARG A 345 10599 12391 13755 1232 -1248 -2730 C ATOM 2117 CD ARG A 345 -11.201 9.240 14.638 1.00 87.29 C ANISOU 2117 CD ARG A 345 9356 11165 12645 1127 -1329 -2807 C ATOM 2118 NE ARG A 345 -10.415 8.835 13.476 1.00111.51 N ANISOU 2118 NE ARG A 345 12357 14274 15739 1194 -1181 -2628 N ATOM 2119 CZ ARG A 345 -10.888 8.124 12.456 1.00121.60 C ANISOU 2119 CZ ARG A 345 13786 15455 16963 1208 -1006 -2573 C ATOM 2120 NH1 ARG A 345 -10.089 7.802 11.445 1.00109.78 N ANISOU 2120 NH1 ARG A 345 12236 13999 15475 1312 -867 -2425 N ATOM 2121 NH2 ARG A 345 -12.157 7.733 12.445 1.00120.83 N ANISOU 2121 NH2 ARG A 345 13872 15254 16782 1112 -967 -2578 N ATOM 2122 N SER A 346 -11.797 8.079 20.425 1.00156.73 N ANISOU 2122 N SER A 346 18151 20274 21126 1348 -1618 -2866 N ATOM 2123 CA SER A 346 -11.312 8.456 21.755 1.00138.54 C ANISOU 2123 CA SER A 346 15826 18116 18696 1298 -1775 -2800 C ATOM 2124 C SER A 346 -11.262 7.265 22.708 1.00159.43 C ANISOU 2124 C SER A 346 18384 20891 21302 1473 -1721 -2712 C ATOM 2125 O SER A 346 -12.269 6.590 22.916 1.00167.55 O ANISOU 2125 O SER A 346 19523 21826 22312 1580 -1588 -2785 O ATOM 2126 CB SER A 346 -12.166 9.574 22.363 1.00100.41 C ANISOU 2126 CB SER A 346 11220 13175 13755 1207 -1824 -2903 C ATOM 2127 OG SER A 346 -11.551 10.842 22.197 1.00 81.74 O ANISOU 2127 OG SER A 346 8903 10785 11371 1028 -1918 -2803 O ATOM 2128 N PRO A 347 -10.079 7.003 23.289 1.00166.91 N ANISOU 2128 N PRO A 347 19169 22031 22217 1480 -1781 -2494 N ATOM 2129 CA PRO A 347 -9.928 5.947 24.296 1.00165.17 C ANISOU 2129 CA PRO A 347 18877 21940 21939 1634 -1718 -2364 C ATOM 2130 C PRO A 347 -10.643 6.322 25.594 1.00161.24 C ANISOU 2130 C PRO A 347 18508 21483 21273 1611 -1845 -2493 C ATOM 2131 O PRO A 347 -11.093 5.429 26.319 1.00149.44 O ANISOU 2131 O PRO A 347 17035 20021 19724 1749 -1737 -2446 O ATOM 2132 CB PRO A 347 -8.415 5.883 24.515 1.00169.65 C ANISOU 2132 CB PRO A 347 19231 22718 22510 1600 -1791 -2090 C ATOM 2133 CG PRO A 347 -7.920 7.233 24.132 1.00173.03 C ANISOU 2133 CG PRO A 347 19670 23140 22934 1368 -1979 -2110 C ATOM 2134 CD PRO A 347 -8.805 7.688 23.010 1.00169.56 C ANISOU 2134 CD PRO A 347 19379 22475 22572 1333 -1898 -2318 C ATOM 2135 N ASP A 348 -10.748 7.623 25.872 1.00165.94 N ANISOU 2135 N ASP A 348 19215 22059 21776 1444 -2051 -2634 N ATOM 2136 CA ASP A 348 -11.570 8.107 26.975 1.00157.23 C ANISOU 2136 CA ASP A 348 18299 20949 20492 1444 -2134 -2781 C ATOM 2137 C ASP A 348 -12.929 7.462 26.818 1.00142.86 C ANISOU 2137 C ASP A 348 16568 19017 18694 1593 -1958 -2907 C ATOM 2138 O ASP A 348 -13.534 6.983 27.781 1.00130.79 O ANISOU 2138 O ASP A 348 15096 17550 17050 1708 -1908 -2903 O ATOM 2139 CB ASP A 348 -11.761 9.625 26.896 1.00157.63 C ANISOU 2139 CB ASP A 348 18567 20842 20484 1264 -2202 -2851 C ATOM 2140 CG ASP A 348 -10.456 10.388 26.909 1.00150.83 C ANISOU 2140 CG ASP A 348 17649 20043 19617 1066 -2365 -2689 C ATOM 2141 OD1 ASP A 348 -9.444 9.837 27.385 1.00140.29 O ANISOU 2141 OD1 ASP A 348 16129 18910 18263 1065 -2457 -2523 O ATOM 2142 OD2 ASP A 348 -10.451 11.549 26.446 1.00149.95 O ANISOU 2142 OD2 ASP A 348 17663 19788 19523 910 -2398 -2690 O ATOM 2143 N PHE A 349 -13.401 7.475 25.577 1.00140.21 N ANISOU 2143 N PHE A 349 16266 18504 18504 1572 -1839 -2978 N ATOM 2144 CA PHE A 349 -14.706 6.950 25.235 1.00131.28 C ANISOU 2144 CA PHE A 349 15245 17222 17412 1662 -1657 -3059 C ATOM 2145 C PHE A 349 -14.723 5.417 25.203 1.00137.27 C ANISOU 2145 C PHE A 349 15948 17981 18229 1778 -1449 -2863 C ATOM 2146 O PHE A 349 -15.592 4.801 25.807 1.00149.11 O ANISOU 2146 O PHE A 349 17529 19473 19653 1820 -1357 -2799 O ATOM 2147 CB PHE A 349 -15.161 7.542 23.901 1.00113.10 C ANISOU 2147 CB PHE A 349 12988 14765 15221 1511 -1594 -3015 C ATOM 2148 CG PHE A 349 -16.567 7.188 23.529 1.00120.06 C ANISOU 2148 CG PHE A 349 13982 15551 16086 1433 -1436 -2867 C ATOM 2149 CD1 PHE A 349 -17.379 6.502 24.410 1.00121.19 C ANISOU 2149 CD1 PHE A 349 14189 15722 16134 1506 -1372 -2832 C ATOM 2150 CD2 PHE A 349 -17.072 7.529 22.292 1.00126.27 C ANISOU 2150 CD2 PHE A 349 14804 16227 16946 1298 -1351 -2761 C ATOM 2151 CE1 PHE A 349 -18.667 6.167 24.065 1.00116.48 C ANISOU 2151 CE1 PHE A 349 13684 15036 15536 1438 -1244 -2711 C ATOM 2152 CE2 PHE A 349 -18.359 7.194 21.938 1.00123.36 C ANISOU 2152 CE2 PHE A 349 14532 15780 16558 1229 -1227 -2642 C ATOM 2153 CZ PHE A 349 -19.159 6.514 22.825 1.00116.92 C ANISOU 2153 CZ PHE A 349 13774 14983 15667 1296 -1180 -2624 C ATOM 2154 N ARG A 350 -13.757 4.803 24.524 1.00118.47 N ANISOU 2154 N ARG A 350 13463 15603 15949 1786 -1369 -2707 N ATOM 2155 CA ARG A 350 -13.757 3.350 24.374 1.00 88.20 C ANISOU 2155 CA ARG A 350 9653 11715 12145 1852 -1159 -2492 C ATOM 2156 C ARG A 350 -13.662 2.625 25.717 1.00108.78 C ANISOU 2156 C ARG A 350 12181 14474 14677 1992 -1152 -2381 C ATOM 2157 O ARG A 350 -14.214 1.539 25.878 1.00116.57 O ANISOU 2157 O ARG A 350 13235 15388 15670 2043 -1000 -2256 O ATOM 2158 CB ARG A 350 -12.650 2.889 23.420 1.00 89.54 C ANISOU 2158 CB ARG A 350 9737 11871 12414 1873 -1066 -2342 C ATOM 2159 CG ARG A 350 -12.832 1.460 22.921 1.00118.69 C ANISOU 2159 CG ARG A 350 13523 15426 16146 1935 -840 -2163 C ATOM 2160 CD ARG A 350 -12.122 1.211 21.594 1.00135.23 C ANISOU 2160 CD ARG A 350 15627 17439 18317 1938 -728 -2076 C ATOM 2161 NE ARG A 350 -12.459 -0.103 21.047 1.00158.28 N ANISOU 2161 NE ARG A 350 18689 20189 21262 1997 -528 -1946 N ATOM 2162 CZ ARG A 350 -12.118 -0.526 19.833 1.00162.10 C ANISOU 2162 CZ ARG A 350 19251 20557 21781 2018 -397 -1875 C ATOM 2163 NH1 ARG A 350 -11.424 0.262 19.023 1.00158.24 N ANISOU 2163 NH1 ARG A 350 18692 20119 21313 1988 -432 -1903 N ATOM 2164 NH2 ARG A 350 -12.473 -1.738 19.426 1.00162.40 N ANISOU 2164 NH2 ARG A 350 19443 20428 21835 2081 -235 -1777 N ATOM 2165 N LYS A 351 -12.967 3.231 26.678 1.00119.05 N ANISOU 2165 N LYS A 351 13335 15997 15903 2037 -1339 -2405 N ATOM 2166 CA LYS A 351 -12.845 2.649 28.016 1.00127.63 C ANISOU 2166 CA LYS A 351 14346 17265 16881 2149 -1358 -2282 C ATOM 2167 C LYS A 351 -14.193 2.580 28.718 1.00118.27 C ANISOU 2167 C LYS A 351 13293 16047 15599 2205 -1322 -2379 C ATOM 2168 O LYS A 351 -14.471 1.644 29.462 1.00112.35 O ANISOU 2168 O LYS A 351 12523 15356 14809 2308 -1224 -2235 O ATOM 2169 CB LYS A 351 -11.854 3.441 28.870 1.00136.81 C ANISOU 2169 CB LYS A 351 15424 18649 17908 2062 -1583 -2240 C ATOM 2170 CG LYS A 351 -10.399 3.171 28.537 1.00143.61 C ANISOU 2170 CG LYS A 351 16083 19628 18853 2049 -1602 -2027 C ATOM 2171 CD LYS A 351 -10.051 1.701 28.726 1.00138.76 C ANISOU 2171 CD LYS A 351 15348 19065 18309 2234 -1409 -1789 C ATOM 2172 CE LYS A 351 -8.621 1.416 28.291 1.00121.05 C ANISOU 2172 CE LYS A 351 12915 16930 16149 2238 -1385 -1545 C ATOM 2173 NZ LYS A 351 -8.295 -0.037 28.333 1.00 91.68 N ANISOU 2173 NZ LYS A 351 9146 13194 12495 2400 -1152 -1295 N ATOM 2174 N ALA A 352 -15.023 3.587 28.483 1.00111.84 N ANISOU 2174 N ALA A 352 12620 15137 14736 2121 -1389 -2590 N ATOM 2175 CA ALA A 352 -16.374 3.596 29.015 1.00 85.16 C ANISOU 2175 CA ALA A 352 9365 11726 11267 2177 -1334 -2660 C ATOM 2176 C ALA A 352 -17.308 2.788 28.113 1.00 79.76 C ANISOU 2176 C ALA A 352 8793 10825 10686 2074 -1138 -2538 C ATOM 2177 O ALA A 352 -18.425 2.464 28.501 1.00 63.66 O ANISOU 2177 O ALA A 352 6823 8764 8601 2095 -1060 -2485 O ATOM 2178 CB ALA A 352 -16.870 5.022 29.162 1.00 76.97 C ANISOU 2178 CB ALA A 352 8464 10674 10106 2107 -1478 -2886 C ATOM 2179 N PHE A 353 -16.846 2.481 26.903 1.00 93.03 N ANISOU 2179 N PHE A 353 10480 12364 12505 1975 -1071 -2483 N ATOM 2180 CA PHE A 353 -17.618 1.694 25.944 1.00103.92 C ANISOU 2180 CA PHE A 353 11962 13542 13981 1885 -919 -2373 C ATOM 2181 C PHE A 353 -17.512 0.213 26.251 1.00137.98 C ANISOU 2181 C PHE A 353 16241 17833 18354 1998 -780 -2179 C ATOM 2182 O PHE A 353 -18.455 -0.549 26.039 1.00156.28 O ANISOU 2182 O PHE A 353 18633 20024 20723 1982 -681 -2096 O ATOM 2183 CB PHE A 353 -17.153 1.951 24.505 1.00104.84 C ANISOU 2183 CB PHE A 353 12115 13529 14192 1758 -903 -2390 C ATOM 2184 CG PHE A 353 -17.832 1.071 23.480 1.00143.37 C ANISOU 2184 CG PHE A 353 17105 18215 19155 1685 -762 -2279 C ATOM 2185 CD1 PHE A 353 -19.129 1.339 23.066 1.00165.29 C ANISOU 2185 CD1 PHE A 353 19976 20900 21927 1567 -753 -2289 C ATOM 2186 CD2 PHE A 353 -17.176 -0.023 22.932 1.00145.64 C ANISOU 2186 CD2 PHE A 353 17401 18417 19519 1751 -641 -2156 C ATOM 2187 CE1 PHE A 353 -19.758 0.532 22.127 1.00170.72 C ANISOU 2187 CE1 PHE A 353 20760 21420 22687 1507 -650 -2202 C ATOM 2188 CE2 PHE A 353 -17.801 -0.833 21.991 1.00141.42 C ANISOU 2188 CE2 PHE A 353 16994 17694 19045 1699 -532 -2083 C ATOM 2189 CZ PHE A 353 -19.092 -0.554 21.590 1.00155.20 C ANISOU 2189 CZ PHE A 353 18828 19354 20786 1571 -549 -2114 C ATOM 2190 N LYS A 354 -16.353 -0.194 26.752 1.00141.63 N ANISOU 2190 N LYS A 354 16574 18421 18818 2115 -784 -2092 N ATOM 2191 CA LYS A 354 -16.115 -1.599 27.026 1.00127.18 C ANISOU 2191 CA LYS A 354 14701 16568 17054 2231 -652 -1884 C ATOM 2192 C LYS A 354 -16.895 -2.031 28.259 1.00122.78 C ANISOU 2192 C LYS A 354 14109 16112 16430 2323 -644 -1813 C ATOM 2193 O LYS A 354 -17.795 -2.868 28.174 1.00114.89 O ANISOU 2193 O LYS A 354 13170 14986 15498 2333 -546 -1726 O ATOM 2194 CB LYS A 354 -14.615 -1.891 27.177 1.00102.73 C ANISOU 2194 CB LYS A 354 11455 13599 13980 2328 -650 -1765 C ATOM 2195 CG LYS A 354 -13.863 -0.965 28.119 1.00 85.53 C ANISOU 2195 CG LYS A 354 9123 11687 11688 2361 -827 -1820 C ATOM 2196 CD LYS A 354 -12.883 -1.751 28.988 1.00 96.13 C ANISOU 2196 CD LYS A 354 10294 13216 13016 2495 -806 -1595 C ATOM 2197 CE LYS A 354 -12.020 -2.694 28.154 1.00 91.02 C ANISOU 2197 CE LYS A 354 9615 12465 12505 2550 -649 -1410 C ATOM 2198 NZ LYS A 354 -11.140 -3.559 28.998 1.00 69.87 N ANISOU 2198 NZ LYS A 354 6771 9952 9826 2685 -605 -1158 N ATOM 2199 N ARG A 355 -16.555 -1.446 29.401 1.00107.17 N ANISOU 2199 N ARG A 355 12030 14375 14315 2398 -757 -1847 N ATOM 2200 CA ARG A 355 -17.200 -1.794 30.657 1.00103.07 C ANISOU 2200 CA ARG A 355 11467 14001 13695 2508 -750 -1763 C ATOM 2201 C ARG A 355 -18.694 -1.515 30.602 1.00120.70 C ANISOU 2201 C ARG A 355 13813 16146 15901 2462 -722 -1834 C ATOM 2202 O ARG A 355 -19.474 -2.088 31.363 1.00133.79 O ANISOU 2202 O ARG A 355 15442 17866 17528 2548 -663 -1712 O ATOM 2203 CB ARG A 355 -16.574 -1.008 31.800 1.00 74.80 C ANISOU 2203 CB ARG A 355 7786 10706 9930 2591 -908 -1825 C ATOM 2204 CG ARG A 355 -15.355 -0.219 31.393 1.00104.50 C ANISOU 2204 CG ARG A 355 11480 14528 13696 2538 -1044 -1922 C ATOM 2205 CD ARG A 355 -14.915 0.672 32.527 1.00129.09 C ANISOU 2205 CD ARG A 355 14543 17902 16602 2568 -1245 -1994 C ATOM 2206 NE ARG A 355 -16.008 1.515 32.996 1.00141.16 N ANISOU 2206 NE ARG A 355 16224 19437 17975 2567 -1298 -2170 N ATOM 2207 CZ ARG A 355 -16.035 2.104 34.185 1.00159.18 C ANISOU 2207 CZ ARG A 355 18554 21911 20015 2604 -1423 -2210 C ATOM 2208 NH1 ARG A 355 -15.030 1.948 35.031 1.00170.65 N ANISOU 2208 NH1 ARG A 355 19907 23572 21362 2616 -1526 -2085 N ATOM 2209 NH2 ARG A 355 -17.068 2.851 34.534 1.00164.60 N ANISOU 2209 NH2 ARG A 355 19395 22587 20557 2637 -1443 -2367 N ATOM 2210 N LEU A 356 -19.086 -0.635 29.691 1.00118.59 N ANISOU 2210 N LEU A 356 13658 15749 15652 2327 -762 -2003 N ATOM 2211 CA LEU A 356 -20.488 -0.297 29.513 1.00125.51 C ANISOU 2211 CA LEU A 356 14631 16545 16512 2269 -734 -2047 C ATOM 2212 C LEU A 356 -21.327 -1.537 29.216 1.00124.94 C ANISOU 2212 C LEU A 356 14563 16329 16581 2276 -603 -1874 C ATOM 2213 O LEU A 356 -22.149 -1.953 30.031 1.00126.21 O ANISOU 2213 O LEU A 356 14673 16575 16707 2374 -560 -1763 O ATOM 2214 CB LEU A 356 -20.637 0.711 28.380 1.00134.61 C ANISOU 2214 CB LEU A 356 15891 17562 17693 2097 -790 -2208 C ATOM 2215 CG LEU A 356 -22.051 1.242 28.168 1.00146.97 C ANISOU 2215 CG LEU A 356 17542 19067 19233 2029 -773 -2240 C ATOM 2216 CD1 LEU A 356 -22.564 1.876 29.449 1.00136.09 C ANISOU 2216 CD1 LEU A 356 16156 17885 17667 2164 -815 -2284 C ATOM 2217 CD2 LEU A 356 -22.071 2.236 27.019 1.00162.03 C ANISOU 2217 CD2 LEU A 356 19531 20859 21174 1847 -833 -2354 C TER 2218 LEU A 356 ATOM 2219 N LEU B 36 -55.561 -0.256 7.619 1.00104.41 N ANISOU 2219 N LEU B 36 14327 10413 14931 1342 -1629 -67 N ATOM 2220 CA LEU B 36 -54.873 -0.704 8.826 1.00 97.52 C ANISOU 2220 CA LEU B 36 13417 9582 14055 1296 -1548 -95 C ATOM 2221 C LEU B 36 -53.829 -1.777 8.519 1.00 86.60 C ANISOU 2221 C LEU B 36 12033 8255 12616 1229 -1526 -80 C ATOM 2222 O LEU B 36 -52.830 -1.899 9.227 1.00 39.99 O ANISOU 2222 O LEU B 36 6134 2371 6691 1181 -1459 -82 O ATOM 2223 CB LEU B 36 -55.880 -1.225 9.861 1.00 95.45 C ANISOU 2223 CB LEU B 36 13056 9359 13851 1326 -1537 -142 C ATOM 2224 CG LEU B 36 -55.334 -1.726 11.206 1.00 82.90 C ANISOU 2224 CG LEU B 36 11420 7814 12264 1283 -1460 -170 C ATOM 2225 CD1 LEU B 36 -54.703 -0.592 11.988 1.00 99.35 C ANISOU 2225 CD1 LEU B 36 13556 9843 14348 1272 -1397 -174 C ATOM 2226 CD2 LEU B 36 -56.418 -2.394 12.041 1.00 57.58 C ANISOU 2226 CD2 LEU B 36 8115 4651 9111 1311 -1461 -215 C ATOM 2227 N SER B 37 -54.057 -2.545 7.457 1.00105.55 N ANISOU 2227 N SER B 37 14429 10679 14996 1226 -1579 -66 N ATOM 2228 CA SER B 37 -53.203 -3.690 7.140 1.00127.85 C ANISOU 2228 CA SER B 37 17244 13553 17779 1170 -1553 -56 C ATOM 2229 C SER B 37 -51.818 -3.287 6.632 1.00112.83 C ANISOU 2229 C SER B 37 15425 11626 15818 1120 -1523 -22 C ATOM 2230 O SER B 37 -50.831 -3.972 6.903 1.00 96.00 O ANISOU 2230 O SER B 37 13283 9530 13661 1072 -1468 -17 O ATOM 2231 CB SER B 37 -53.891 -4.620 6.130 1.00150.29 C ANISOU 2231 CB SER B 37 20064 16420 20621 1181 -1611 -55 C ATOM 2232 OG SER B 37 -53.156 -5.820 5.947 1.00151.98 O ANISOU 2232 OG SER B 37 20260 16678 20807 1132 -1573 -52 O ATOM 2233 N GLN B 38 -51.752 -2.183 5.890 1.00102.98 N ANISOU 2233 N GLN B 38 14260 10315 14552 1133 -1559 3 N ATOM 2234 CA GLN B 38 -50.486 -1.697 5.348 1.00 91.73 C ANISOU 2234 CA GLN B 38 12921 8860 13071 1084 -1536 34 C ATOM 2235 C GLN B 38 -49.629 -1.033 6.423 1.00 98.21 C ANISOU 2235 C GLN B 38 13758 9667 13890 1057 -1461 28 C ATOM 2236 O GLN B 38 -48.418 -0.868 6.253 1.00 72.51 O ANISOU 2236 O GLN B 38 10555 6404 10592 1005 -1422 46 O ATOM 2237 CB GLN B 38 -50.729 -0.730 4.187 1.00 78.96 C ANISOU 2237 CB GLN B 38 11391 7176 11433 1105 -1602 67 C ATOM 2238 CG GLN B 38 -50.586 -1.361 2.810 1.00 89.68 C ANISOU 2238 CG GLN B 38 12787 8538 12749 1082 -1663 88 C ATOM 2239 CD GLN B 38 -49.166 -1.826 2.517 1.00 96.71 C ANISOU 2239 CD GLN B 38 13715 9444 13585 1011 -1616 99 C ATOM 2240 OE1 GLN B 38 -48.214 -1.426 3.190 1.00 84.89 O ANISOU 2240 OE1 GLN B 38 12234 7945 12075 977 -1545 100 O ATOM 2241 NE2 GLN B 38 -49.019 -2.674 1.504 1.00101.54 N ANISOU 2241 NE2 GLN B 38 14345 10068 14169 986 -1657 105 N ATOM 2242 N GLN B 39 -50.266 -0.646 7.524 1.00115.82 N ANISOU 2242 N GLN B 39 15945 11891 16169 1090 -1439 0 N ATOM 2243 CA GLN B 39 -49.558 -0.085 8.672 1.00 98.27 C ANISOU 2243 CA GLN B 39 13731 9656 13952 1063 -1364 -13 C ATOM 2244 C GLN B 39 -48.920 -1.190 9.507 1.00 83.56 C ANISOU 2244 C GLN B 39 11802 7865 12083 1022 -1308 -23 C ATOM 2245 O GLN B 39 -47.937 -0.965 10.208 1.00 61.97 O ANISOU 2245 O GLN B 39 9084 5130 9332 979 -1245 -20 O ATOM 2246 CB GLN B 39 -50.499 0.763 9.530 1.00 83.05 C ANISOU 2246 CB GLN B 39 11788 7687 12082 1113 -1356 -42 C ATOM 2247 CG GLN B 39 -50.947 2.056 8.859 1.00 84.61 C ANISOU 2247 CG GLN B 39 12061 7795 12291 1154 -1394 -25 C ATOM 2248 CD GLN B 39 -52.068 2.750 9.606 1.00106.32 C ANISOU 2248 CD GLN B 39 14783 10503 15111 1218 -1389 -55 C ATOM 2249 OE1 GLN B 39 -52.649 2.192 10.535 1.00120.07 O ANISOU 2249 OE1 GLN B 39 16444 12288 16891 1233 -1369 -91 O ATOM 2250 NE2 GLN B 39 -52.378 3.975 9.201 1.00111.88 N ANISOU 2250 NE2 GLN B 39 15557 11118 15836 1257 -1403 -38 N ATOM 2251 N TRP B 40 -49.503 -2.384 9.441 1.00 84.31 N ANISOU 2251 N TRP B 40 11823 8018 12194 1036 -1330 -33 N ATOM 2252 CA TRP B 40 -48.888 -3.565 10.034 1.00 52.81 C ANISOU 2252 CA TRP B 40 7774 4094 8199 1001 -1282 -33 C ATOM 2253 C TRP B 40 -47.824 -4.157 9.118 1.00 45.97 C ANISOU 2253 C TRP B 40 6941 3241 7285 958 -1271 -1 C ATOM 2254 O TRP B 40 -46.762 -4.550 9.585 1.00 36.21 O ANISOU 2254 O TRP B 40 5696 2029 6032 918 -1213 14 O ATOM 2255 CB TRP B 40 -49.939 -4.608 10.406 1.00 56.57 C ANISOU 2255 CB TRP B 40 8159 4619 8716 1030 -1301 -58 C ATOM 2256 CG TRP B 40 -50.232 -4.661 11.889 1.00 79.82 C ANISOU 2256 CG TRP B 40 11044 7587 11698 1035 -1260 -86 C ATOM 2257 CD1 TRP B 40 -50.367 -5.787 12.658 1.00 75.75 C ANISOU 2257 CD1 TRP B 40 10449 7130 11203 1026 -1233 -96 C ATOM 2258 CD2 TRP B 40 -50.415 -3.549 12.779 1.00 80.43 C ANISOU 2258 CD2 TRP B 40 11139 7623 11796 1047 -1236 -106 C ATOM 2259 NE1 TRP B 40 -50.632 -5.447 13.960 1.00 59.01 N ANISOU 2259 NE1 TRP B 40 8297 5011 9113 1031 -1201 -121 N ATOM 2260 CE2 TRP B 40 -50.666 -4.080 14.063 1.00 80.61 C ANISOU 2260 CE2 TRP B 40 11092 7687 11851 1043 -1199 -131 C ATOM 2261 CE3 TRP B 40 -50.397 -2.160 12.618 1.00 73.27 C ANISOU 2261 CE3 TRP B 40 10306 6646 10889 1060 -1238 -107 C ATOM 2262 CZ2 TRP B 40 -50.894 -3.266 15.176 1.00 92.35 C ANISOU 2262 CZ2 TRP B 40 12580 9141 13369 1049 -1173 -163 C ATOM 2263 CZ3 TRP B 40 -50.623 -1.357 13.724 1.00 72.02 C ANISOU 2263 CZ3 TRP B 40 10148 6454 10761 1068 -1197 -136 C ATOM 2264 CH2 TRP B 40 -50.867 -1.911 14.983 1.00 79.64 C ANISOU 2264 CH2 TRP B 40 11044 7458 11759 1062 -1171 -168 C ATOM 2265 N GLU B 41 -48.112 -4.207 7.817 1.00 68.24 N ANISOU 2265 N GLU B 41 9800 6042 10087 968 -1326 11 N ATOM 2266 CA GLU B 41 -47.154 -4.678 6.808 1.00 89.28 C ANISOU 2266 CA GLU B 41 12507 8709 12707 927 -1317 38 C ATOM 2267 C GLU B 41 -45.792 -3.995 6.924 1.00 98.54 C ANISOU 2267 C GLU B 41 13741 9858 13843 880 -1267 59 C ATOM 2268 O GLU B 41 -44.748 -4.650 6.880 1.00 92.35 O ANISOU 2268 O GLU B 41 12952 9096 13039 841 -1222 75 O ATOM 2269 CB GLU B 41 -47.691 -4.464 5.387 1.00 92.11 C ANISOU 2269 CB GLU B 41 12919 9033 13046 943 -1390 49 C ATOM 2270 CG GLU B 41 -48.672 -5.523 4.907 1.00105.01 C ANISOU 2270 CG GLU B 41 14500 10697 14703 968 -1430 34 C ATOM 2271 CD GLU B 41 -48.604 -5.739 3.402 1.00102.07 C ANISOU 2271 CD GLU B 41 14188 10297 14296 953 -1485 51 C ATOM 2272 OE1 GLU B 41 -47.549 -5.434 2.802 1.00 90.82 O ANISOU 2272 OE1 GLU B 41 12834 8845 12828 913 -1475 72 O ATOM 2273 OE2 GLU B 41 -49.604 -6.216 2.821 1.00105.72 O ANISOU 2273 OE2 GLU B 41 14631 10760 14776 981 -1550 39 O ATOM 2274 N ALA B 42 -45.805 -2.672 7.035 1.00 99.34 N ANISOU 2274 N ALA B 42 13902 9905 13937 885 -1278 60 N ATOM 2275 CA ALA B 42 -44.575 -1.931 7.273 1.00 87.70 C ANISOU 2275 CA ALA B 42 12490 8399 12433 838 -1240 73 C ATOM 2276 C ALA B 42 -44.337 -1.702 8.773 1.00118.80 C ANISOU 2276 C ALA B 42 16393 12348 16399 830 -1189 55 C ATOM 2277 O ALA B 42 -43.263 -1.249 9.174 1.00133.67 O ANISOU 2277 O ALA B 42 18316 14210 18261 785 -1157 61 O ATOM 2278 CB ALA B 42 -44.591 -0.614 6.509 1.00 51.84 C ANISOU 2278 CB ALA B 42 8049 3782 7866 838 -1280 84 C ATOM 2279 N GLY B 43 -45.338 -2.025 9.594 1.00104.09 N ANISOU 2279 N GLY B 43 14456 10512 14580 870 -1186 31 N ATOM 2280 CA GLY B 43 -45.264 -1.812 11.032 1.00 62.99 C ANISOU 2280 CA GLY B 43 9218 5312 9404 863 -1147 9 C ATOM 2281 C GLY B 43 -44.369 -2.778 11.786 1.00 48.46 C ANISOU 2281 C GLY B 43 7328 3523 7563 827 -1109 18 C ATOM 2282 O GLY B 43 -43.529 -2.362 12.580 1.00 55.49 O ANISOU 2282 O GLY B 43 8239 4395 8450 790 -1084 18 O ATOM 2283 N MET B 44 -44.557 -4.072 11.556 1.00 43.80 N ANISOU 2283 N MET B 44 6671 2991 6979 838 -1108 29 N ATOM 2284 CA MET B 44 -43.745 -5.079 12.233 1.00 68.10 C ANISOU 2284 CA MET B 44 9696 6114 10063 812 -1072 46 C ATOM 2285 C MET B 44 -42.594 -5.647 11.408 1.00 73.94 C ANISOU 2285 C MET B 44 10460 6860 10772 779 -1055 81 C ATOM 2286 O MET B 44 -41.849 -6.500 11.891 1.00 95.58 O ANISOU 2286 O MET B 44 13159 9634 13523 762 -1025 103 O ATOM 2287 CB MET B 44 -44.618 -6.195 12.812 1.00102.47 C ANISOU 2287 CB MET B 44 13957 10523 14455 842 -1068 34 C ATOM 2288 CG MET B 44 -45.534 -5.706 13.934 1.00127.52 C ANISOU 2288 CG MET B 44 17097 13689 17665 865 -1078 -2 C ATOM 2289 SD MET B 44 -44.855 -4.267 14.805 1.00194.62 S ANISOU 2289 SD MET B 44 25659 22125 26161 833 -1069 -16 S ATOM 2290 CE MET B 44 -46.065 -4.021 16.108 1.00 35.25 C ANISOU 2290 CE MET B 44 5422 1939 6034 863 -1075 -66 C ATOM 2291 N SER B 45 -42.454 -5.187 10.168 1.00 74.11 N ANISOU 2291 N SER B 45 10550 6848 10760 772 -1077 87 N ATOM 2292 CA SER B 45 -41.325 -5.590 9.334 1.00 80.34 C ANISOU 2292 CA SER B 45 11373 7632 11520 737 -1061 115 C ATOM 2293 C SER B 45 -40.017 -5.084 9.954 1.00 76.39 C ANISOU 2293 C SER B 45 10907 7111 11005 690 -1038 130 C ATOM 2294 O SER B 45 -39.032 -5.824 10.110 1.00 61.85 O ANISOU 2294 O SER B 45 9043 5290 9168 667 -1009 156 O ATOM 2295 CB SER B 45 -41.501 -5.044 7.919 1.00 35.30 C ANISOU 2295 CB SER B 45 5745 1887 5781 734 -1102 115 C ATOM 2296 OG SER B 45 -41.756 -3.658 7.955 1.00 35.92 O ANISOU 2296 OG SER B 45 5889 1915 5845 735 -1130 105 O ATOM 2297 N LEU B 46 -40.024 -3.812 10.323 1.00 35.18 N ANISOU 2297 N LEU B 46 5745 1847 5774 676 -1053 115 N ATOM 2298 CA LEU B 46 -38.911 -3.226 11.043 1.00 73.24 C ANISOU 2298 CA LEU B 46 10604 6641 10583 625 -1039 123 C ATOM 2299 C LEU B 46 -38.579 -4.103 12.244 1.00 69.27 C ANISOU 2299 C LEU B 46 10019 6182 10117 623 -1018 135 C ATOM 2300 O LEU B 46 -37.437 -4.538 12.411 1.00 90.05 O ANISOU 2300 O LEU B 46 12646 8821 12746 588 -1005 166 O ATOM 2301 CB LEU B 46 -39.283 -1.819 11.516 1.00 99.56 C ANISOU 2301 CB LEU B 46 13997 9918 13913 618 -1050 94 C ATOM 2302 CG LEU B 46 -38.186 -0.761 11.639 1.00 79.18 C ANISOU 2302 CG LEU B 46 11510 7279 11296 553 -1045 95 C ATOM 2303 CD1 LEU B 46 -37.996 0.002 10.318 1.00 58.38 C ANISOU 2303 CD1 LEU B 46 8970 4598 8614 538 -1063 101 C ATOM 2304 CD2 LEU B 46 -38.528 0.186 12.776 1.00 55.66 C ANISOU 2304 CD2 LEU B 46 8551 4259 8338 544 -1036 61 C ATOM 2305 N LEU B 47 -39.589 -4.376 13.069 1.00 75.27 N ANISOU 2305 N LEU B 47 10714 6969 10916 660 -1021 115 N ATOM 2306 CA LEU B 47 -39.396 -5.130 14.312 1.00 94.91 C ANISOU 2306 CA LEU B 47 13124 9494 13443 658 -1012 127 C ATOM 2307 C LEU B 47 -38.816 -6.540 14.117 1.00103.46 C ANISOU 2307 C LEU B 47 14144 10627 14540 664 -991 169 C ATOM 2308 O LEU B 47 -37.860 -6.946 14.807 1.00 93.87 O ANISOU 2308 O LEU B 47 12900 9422 13345 638 -986 204 O ATOM 2309 CB LEU B 47 -40.702 -5.205 15.100 1.00 64.91 C ANISOU 2309 CB LEU B 47 9269 5713 9681 698 -1021 92 C ATOM 2310 CG LEU B 47 -40.611 -6.092 16.342 1.00 76.20 C ANISOU 2310 CG LEU B 47 10612 7184 11156 697 -1019 106 C ATOM 2311 CD1 LEU B 47 -41.559 -5.583 17.411 1.00 97.71 C ANISOU 2311 CD1 LEU B 47 13314 9895 13916 709 -1034 62 C ATOM 2312 CD2 LEU B 47 -40.864 -7.575 16.026 1.00 33.24 C ANISOU 2312 CD2 LEU B 47 5094 1805 5732 729 -1001 132 C ATOM 2313 N MET B 48 -39.417 -7.295 13.201 1.00 89.02 N ANISOU 2313 N MET B 48 12292 8824 12707 698 -979 167 N ATOM 2314 CA MET B 48 -38.879 -8.595 12.839 1.00 76.31 C ANISOU 2314 CA MET B 48 10635 7248 11110 705 -947 202 C ATOM 2315 C MET B 48 -37.406 -8.445 12.466 1.00101.08 C ANISOU 2315 C MET B 48 13818 10359 14230 664 -936 236 C ATOM 2316 O MET B 48 -36.569 -9.240 12.895 1.00121.22 O ANISOU 2316 O MET B 48 16322 12929 16807 659 -916 277 O ATOM 2317 CB MET B 48 -39.674 -9.219 11.691 1.00 33.09 C ANISOU 2317 CB MET B 48 5159 1785 5628 735 -939 187 C ATOM 2318 CG MET B 48 -41.079 -9.668 12.062 1.00 32.96 C ANISOU 2318 CG MET B 48 5086 1802 5636 774 -949 159 C ATOM 2319 SD MET B 48 -41.734 -10.902 10.914 1.00109.04 S ANISOU 2319 SD MET B 48 14699 11456 15276 799 -933 155 S ATOM 2320 CE MET B 48 -43.437 -11.030 11.453 1.00128.25 C ANISOU 2320 CE MET B 48 17079 13915 17735 836 -963 116 C ATOM 2321 N ALA B 49 -37.086 -7.416 11.683 1.00 91.67 N ANISOU 2321 N ALA B 49 12715 9119 12995 635 -952 223 N ATOM 2322 CA ALA B 49 -35.687 -7.136 11.346 1.00 94.52 C ANISOU 2322 CA ALA B 49 13130 9449 13336 586 -947 250 C ATOM 2323 C ALA B 49 -34.821 -6.922 12.601 1.00101.98 C ANISOU 2323 C ALA B 49 14057 10389 14301 551 -958 278 C ATOM 2324 O ALA B 49 -33.638 -7.309 12.640 1.00102.09 O ANISOU 2324 O ALA B 49 14064 10399 14325 523 -950 321 O ATOM 2325 CB ALA B 49 -35.590 -5.940 10.418 1.00100.69 C ANISOU 2325 CB ALA B 49 14017 10176 14063 554 -968 228 C ATOM 2326 N LEU B 50 -35.412 -6.307 13.625 1.00114.71 N ANISOU 2326 N LEU B 50 15661 11998 15924 551 -981 255 N ATOM 2327 CA LEU B 50 -34.706 -6.088 14.889 1.00126.03 C ANISOU 2327 CA LEU B 50 17078 13423 17384 509 -1003 280 C ATOM 2328 C LEU B 50 -34.378 -7.393 15.611 1.00130.39 C ANISOU 2328 C LEU B 50 17520 14027 17996 531 -997 334 C ATOM 2329 O LEU B 50 -33.253 -7.586 16.095 1.00147.98 O ANISOU 2329 O LEU B 50 19727 16251 20248 492 -1012 391 O ATOM 2330 CB LEU B 50 -35.499 -5.166 15.815 1.00112.69 C ANISOU 2330 CB LEU B 50 15407 11710 15700 502 -1025 235 C ATOM 2331 CG LEU B 50 -34.902 -5.042 17.218 1.00 92.81 C ANISOU 2331 CG LEU B 50 12865 9181 13219 453 -1055 259 C ATOM 2332 CD1 LEU B 50 -35.068 -3.629 17.769 1.00 86.54 C ANISOU 2332 CD1 LEU B 50 12158 8323 12401 402 -1070 208 C ATOM 2333 CD2 LEU B 50 -35.495 -6.090 18.158 1.00 65.61 C ANISOU 2333 CD2 LEU B 50 9300 5790 9839 493 -1061 278 C ATOM 2334 N VAL B 51 -35.360 -8.284 15.699 1.00101.62 N ANISOU 2334 N VAL B 51 13802 10430 14378 588 -978 324 N ATOM 2335 CA VAL B 51 -35.105 -9.596 16.285 1.00 72.27 C ANISOU 2335 CA VAL B 51 9980 6763 10717 612 -965 378 C ATOM 2336 C VAL B 51 -34.047 -10.363 15.475 1.00 69.85 C ANISOU 2336 C VAL B 51 9665 6461 10413 615 -932 427 C ATOM 2337 O VAL B 51 -33.165 -11.035 16.046 1.00 90.69 O ANISOU 2337 O VAL B 51 12235 9121 13103 610 -933 496 O ATOM 2338 CB VAL B 51 -36.387 -10.410 16.398 1.00 47.32 C ANISOU 2338 CB VAL B 51 6759 3648 7574 666 -945 351 C ATOM 2339 CG1 VAL B 51 -36.171 -11.565 17.340 1.00 43.57 C ANISOU 2339 CG1 VAL B 51 6177 3219 7160 682 -940 406 C ATOM 2340 CG2 VAL B 51 -37.507 -9.524 16.904 1.00 50.76 C ANISOU 2340 CG2 VAL B 51 7216 4068 8001 667 -973 291 C ATOM 2341 N VAL B 52 -34.119 -10.243 14.148 1.00 43.21 N ANISOU 2341 N VAL B 52 6357 3064 6995 620 -906 396 N ATOM 2342 CA VAL B 52 -33.046 -10.748 13.295 1.00 53.89 C ANISOU 2342 CA VAL B 52 7723 4402 8349 612 -876 431 C ATOM 2343 C VAL B 52 -31.696 -10.264 13.817 1.00 57.10 C ANISOU 2343 C VAL B 52 8139 4784 8771 559 -905 484 C ATOM 2344 O VAL B 52 -30.790 -11.071 14.034 1.00 35.28 O ANISOU 2344 O VAL B 52 5309 2036 6058 564 -892 550 O ATOM 2345 CB VAL B 52 -33.197 -10.306 11.825 1.00 51.69 C ANISOU 2345 CB VAL B 52 7536 4086 8018 602 -861 387 C ATOM 2346 CG1 VAL B 52 -31.878 -10.492 11.071 1.00 33.58 C ANISOU 2346 CG1 VAL B 52 5276 1759 5724 572 -841 420 C ATOM 2347 CG2 VAL B 52 -34.319 -11.070 11.151 1.00 39.98 C ANISOU 2347 CG2 VAL B 52 6032 2626 6534 648 -833 355 C ATOM 2348 N LEU B 53 -31.567 -8.955 14.040 1.00 66.50 N ANISOU 2348 N LEU B 53 9410 5934 9922 505 -946 459 N ATOM 2349 CA LEU B 53 -30.320 -8.414 14.595 1.00 61.17 C ANISOU 2349 CA LEU B 53 8756 5230 9257 435 -982 511 C ATOM 2350 C LEU B 53 -29.936 -9.032 15.939 1.00 72.03 C ANISOU 2350 C LEU B 53 10015 6644 10710 432 -1009 590 C ATOM 2351 O LEU B 53 -28.756 -9.253 16.216 1.00 34.40 O ANISOU 2351 O LEU B 53 5208 1878 5983 394 -1025 674 O ATOM 2352 CB LEU B 53 -30.370 -6.895 14.739 1.00 34.40 C ANISOU 2352 CB LEU B 53 5481 1786 5805 368 -1017 463 C ATOM 2353 CG LEU B 53 -29.002 -6.379 15.195 1.00 68.37 C ANISOU 2353 CG LEU B 53 9821 6054 10103 273 -1054 520 C ATOM 2354 CD1 LEU B 53 -28.625 -5.123 14.434 1.00 98.51 C ANISOU 2354 CD1 LEU B 53 13790 9810 13830 202 -1056 471 C ATOM 2355 CD2 LEU B 53 -28.914 -6.177 16.710 1.00 39.22 C ANISOU 2355 CD2 LEU B 53 6080 2368 6454 226 -1103 561 C ATOM 2356 N LEU B 54 -30.930 -9.283 16.785 1.00 96.28 N ANISOU 2356 N LEU B 54 13025 9749 13807 467 -1017 573 N ATOM 2357 CA LEU B 54 -30.672 -9.980 18.040 1.00 95.95 C ANISOU 2357 CA LEU B 54 12858 9753 13845 468 -1041 657 C ATOM 2358 C LEU B 54 -29.930 -11.277 17.767 1.00 87.79 C ANISOU 2358 C LEU B 54 11724 8766 12868 509 -1002 739 C ATOM 2359 O LEU B 54 -28.949 -11.605 18.448 1.00 34.25 O ANISOU 2359 O LEU B 54 4851 2013 6151 483 -1022 851 O ATOM 2360 CB LEU B 54 -31.976 -10.289 18.768 1.00 91.56 C ANISOU 2360 CB LEU B 54 12251 9230 13309 511 -1041 616 C ATOM 2361 CG LEU B 54 -32.169 -9.520 20.066 1.00 71.21 C ANISOU 2361 CG LEU B 54 9669 6633 10756 456 -1100 622 C ATOM 2362 CD1 LEU B 54 -32.270 -8.031 19.764 1.00 34.04 C ANISOU 2362 CD1 LEU B 54 5105 1851 5979 401 -1119 542 C ATOM 2363 CD2 LEU B 54 -33.402 -10.041 20.792 1.00 73.33 C ANISOU 2363 CD2 LEU B 54 9868 6938 11057 503 -1097 591 C ATOM 2364 N ILE B 55 -30.397 -12.004 16.753 1.00 85.23 N ANISOU 2364 N ILE B 55 11413 8450 12522 569 -943 691 N ATOM 2365 CA ILE B 55 -29.806 -13.300 16.422 1.00 94.10 C ANISOU 2365 CA ILE B 55 12450 9607 13696 613 -893 752 C ATOM 2366 C ILE B 55 -28.437 -13.180 15.757 1.00104.42 C ANISOU 2366 C ILE B 55 13775 10881 15017 583 -885 802 C ATOM 2367 O ILE B 55 -27.421 -13.581 16.328 1.00115.56 O ANISOU 2367 O ILE B 55 15085 12323 16501 572 -891 912 O ATOM 2368 CB ILE B 55 -30.700 -14.114 15.473 1.00 85.98 C ANISOU 2368 CB ILE B 55 11447 8584 12637 672 -832 683 C ATOM 2369 CG1 ILE B 55 -32.158 -14.056 15.914 1.00 66.33 C ANISOU 2369 CG1 ILE B 55 8961 6117 10123 692 -841 622 C ATOM 2370 CG2 ILE B 55 -30.217 -15.554 15.402 1.00105.07 C ANISOU 2370 CG2 ILE B 55 13770 11035 15115 718 -779 742 C ATOM 2371 CD1 ILE B 55 -33.070 -14.846 15.019 1.00 32.79 C ANISOU 2371 CD1 ILE B 55 4734 1876 5850 737 -790 568 C ATOM 2372 N VAL B 56 -28.422 -12.644 14.539 1.00 90.20 N ANISOU 2372 N VAL B 56 12094 9024 13152 567 -868 733 N ATOM 2373 CA VAL B 56 -27.191 -12.499 13.770 1.00 94.77 C ANISOU 2373 CA VAL B 56 12708 9562 13740 531 -858 766 C ATOM 2374 C VAL B 56 -26.090 -11.796 14.565 1.00 94.85 C ANISOU 2374 C VAL B 56 12694 9564 13780 455 -915 854 C ATOM 2375 O VAL B 56 -24.910 -12.108 14.415 1.00 91.37 O ANISOU 2375 O VAL B 56 12199 9122 13397 436 -904 939 O ATOM 2376 CB VAL B 56 -27.432 -11.725 12.464 1.00 89.70 C ANISOU 2376 CB VAL B 56 12215 8857 13009 503 -848 675 C ATOM 2377 CG1 VAL B 56 -26.116 -11.495 11.736 1.00 98.15 C ANISOU 2377 CG1 VAL B 56 13331 9878 14085 450 -843 707 C ATOM 2378 CG2 VAL B 56 -28.411 -12.470 11.584 1.00 59.88 C ANISOU 2378 CG2 VAL B 56 8450 5089 9211 563 -793 612 C ATOM 2379 N ALA B 57 -26.470 -10.844 15.408 1.00 74.97 N ANISOU 2379 N ALA B 57 10215 7040 11229 405 -974 841 N ATOM 2380 CA ALA B 57 -25.487 -10.187 16.251 1.00 51.02 C ANISOU 2380 CA ALA B 57 7146 4082 8158 304 -993 906 C ATOM 2381 C ALA B 57 -25.103 -11.119 17.382 1.00 35.56 C ANISOU 2381 C ALA B 57 4991 2271 6249 321 -967 1014 C ATOM 2382 O ALA B 57 -23.987 -11.634 17.414 1.00 36.01 O ANISOU 2382 O ALA B 57 4939 2436 6307 303 -920 1093 O ATOM 2383 CB ALA B 57 -26.028 -8.881 16.797 1.00 52.39 C ANISOU 2383 CB ALA B 57 7422 4240 8245 230 -1034 836 C ATOM 2384 N GLY B 58 -26.048 -11.366 18.286 1.00 62.03 N ANISOU 2384 N GLY B 58 8295 5626 9646 358 -999 1018 N ATOM 2385 CA GLY B 58 -25.771 -12.101 19.511 1.00 84.81 C ANISOU 2385 CA GLY B 58 11003 8660 12561 358 -985 1122 C ATOM 2386 C GLY B 58 -25.040 -13.421 19.331 1.00 78.95 C ANISOU 2386 C GLY B 58 10121 7966 11909 427 -937 1230 C ATOM 2387 O GLY B 58 -24.002 -13.668 19.960 1.00 58.77 O ANISOU 2387 O GLY B 58 7434 5570 9327 382 -908 1329 O ATOM 2388 N ASN B 59 -25.577 -14.275 18.468 1.00 77.14 N ANISOU 2388 N ASN B 59 9919 7602 11790 535 -925 1212 N ATOM 2389 CA ASN B 59 -24.975 -15.578 18.226 1.00 74.24 C ANISOU 2389 CA ASN B 59 9429 7274 11504 606 -860 1291 C ATOM 2390 C ASN B 59 -23.547 -15.475 17.714 1.00 84.69 C ANISOU 2390 C ASN B 59 10717 8652 12808 565 -818 1345 C ATOM 2391 O ASN B 59 -22.695 -16.281 18.075 1.00102.24 O ANISOU 2391 O ASN B 59 12789 10976 15082 590 -773 1456 O ATOM 2392 CB ASN B 59 -25.818 -16.394 17.247 1.00 71.28 C ANISOU 2392 CB ASN B 59 9119 6863 11100 675 -794 1167 C ATOM 2393 CG ASN B 59 -27.007 -17.045 17.909 1.00 69.52 C ANISOU 2393 CG ASN B 59 8863 6682 10869 715 -788 1130 C ATOM 2394 OD1 ASN B 59 -26.866 -18.026 18.641 1.00 68.82 O ANISOU 2394 OD1 ASN B 59 8646 6662 10839 749 -764 1213 O ATOM 2395 ND2 ASN B 59 -28.191 -16.509 17.650 1.00 60.94 N ANISOU 2395 ND2 ASN B 59 7890 5556 9708 709 -807 1011 N ATOM 2396 N VAL B 60 -23.293 -14.490 16.859 1.00 69.48 N ANISOU 2396 N VAL B 60 8930 6677 10793 499 -823 1257 N ATOM 2397 CA VAL B 60 -21.980 -14.350 16.246 1.00 49.31 C ANISOU 2397 CA VAL B 60 6357 4184 8194 449 -771 1278 C ATOM 2398 C VAL B 60 -20.975 -13.668 17.170 1.00 55.78 C ANISOU 2398 C VAL B 60 7094 5197 8902 335 -770 1336 C ATOM 2399 O VAL B 60 -19.770 -13.819 16.991 1.00 47.93 O ANISOU 2399 O VAL B 60 6018 4303 7889 302 -721 1391 O ATOM 2400 CB VAL B 60 -22.049 -13.617 14.897 1.00 36.71 C ANISOU 2400 CB VAL B 60 4944 2460 6543 416 -772 1164 C ATOM 2401 CG1 VAL B 60 -22.096 -12.120 15.111 1.00 36.65 C ANISOU 2401 CG1 VAL B 60 5059 2474 6392 300 -817 1097 C ATOM 2402 CG2 VAL B 60 -20.858 -13.996 14.037 1.00 42.84 C ANISOU 2402 CG2 VAL B 60 5685 3264 7330 406 -699 1187 C ATOM 2403 N LEU B 61 -21.462 -12.903 18.144 1.00 72.74 N ANISOU 2403 N LEU B 61 9263 7402 10974 269 -820 1319 N ATOM 2404 CA LEU B 61 -20.570 -12.331 19.152 1.00 72.20 C ANISOU 2404 CA LEU B 61 9103 7532 10797 152 -818 1378 C ATOM 2405 C LEU B 61 -20.211 -13.431 20.143 1.00 77.08 C ANISOU 2405 C LEU B 61 9510 8288 11488 200 -805 1522 C ATOM 2406 O LEU B 61 -19.085 -13.491 20.652 1.00 89.88 O ANISOU 2406 O LEU B 61 11000 10087 13063 141 -782 1614 O ATOM 2407 CB LEU B 61 -21.198 -11.111 19.835 1.00 63.92 C ANISOU 2407 CB LEU B 61 8155 6493 9639 54 -865 1301 C ATOM 2408 CG LEU B 61 -21.145 -9.835 18.978 1.00 73.97 C ANISOU 2408 CG LEU B 61 9620 7675 10810 -27 -870 1182 C ATOM 2409 CD1 LEU B 61 -22.328 -8.898 19.243 1.00 68.38 C ANISOU 2409 CD1 LEU B 61 9053 6863 10064 -50 -918 1080 C ATOM 2410 CD2 LEU B 61 -19.808 -9.108 19.144 1.00 63.68 C ANISOU 2410 CD2 LEU B 61 8290 6530 9377 -167 -837 1203 C ATOM 2411 N VAL B 62 -21.171 -14.319 20.384 1.00 70.90 N ANISOU 2411 N VAL B 62 8694 7423 10820 308 -820 1544 N ATOM 2412 CA VAL B 62 -20.889 -15.561 21.096 1.00 71.46 C ANISOU 2412 CA VAL B 62 8577 7585 10990 381 -801 1686 C ATOM 2413 C VAL B 62 -19.792 -16.341 20.381 1.00 85.91 C ANISOU 2413 C VAL B 62 10317 9433 12891 436 -735 1758 C ATOM 2414 O VAL B 62 -18.760 -16.659 20.969 1.00 97.83 O ANISOU 2414 O VAL B 62 11668 11111 14392 413 -714 1878 O ATOM 2415 CB VAL B 62 -22.133 -16.461 21.189 1.00 63.49 C ANISOU 2415 CB VAL B 62 7572 6445 10106 497 -816 1683 C ATOM 2416 CG1 VAL B 62 -21.731 -17.935 21.203 1.00 38.33 C ANISOU 2416 CG1 VAL B 62 4234 3267 7061 609 -767 1809 C ATOM 2417 CG2 VAL B 62 -22.955 -16.105 22.415 1.00 71.98 C ANISOU 2417 CG2 VAL B 62 8634 7581 11133 449 -870 1681 C ATOM 2418 N ILE B 63 -20.028 -16.641 19.108 1.00 89.09 N ANISOU 2418 N ILE B 63 10819 9667 13366 507 -702 1683 N ATOM 2419 CA ILE B 63 -19.085 -17.389 18.285 1.00 84.15 C ANISOU 2419 CA ILE B 63 10126 9030 12817 563 -629 1727 C ATOM 2420 C ILE B 63 -17.715 -16.726 18.265 1.00 88.64 C ANISOU 2420 C ILE B 63 10645 9754 13281 460 -605 1755 C ATOM 2421 O ILE B 63 -16.679 -17.395 18.330 1.00104.33 O ANISOU 2421 O ILE B 63 12479 11840 15321 490 -553 1859 O ATOM 2422 CB ILE B 63 -19.617 -17.520 16.855 1.00 75.55 C ANISOU 2422 CB ILE B 63 9188 7736 11781 618 -602 1610 C ATOM 2423 CG1 ILE B 63 -20.847 -18.427 16.858 1.00 73.62 C ANISOU 2423 CG1 ILE B 63 8959 7352 11661 729 -611 1600 C ATOM 2424 CG2 ILE B 63 -18.540 -18.054 15.929 1.00 75.37 C ANISOU 2424 CG2 ILE B 63 9116 7709 11813 645 -518 1631 C ATOM 2425 CD1 ILE B 63 -21.583 -18.475 15.554 1.00 64.01 C ANISOU 2425 CD1 ILE B 63 7904 5970 10445 759 -592 1457 C ATOM 2426 N ALA B 64 -17.729 -15.401 18.186 1.00 75.71 N ANISOU 2426 N ALA B 64 9135 8136 11496 339 -641 1662 N ATOM 2427 CA ALA B 64 -16.518 -14.598 18.201 1.00 77.95 C ANISOU 2427 CA ALA B 64 9393 8568 11656 217 -622 1670 C ATOM 2428 C ALA B 64 -15.719 -14.839 19.479 1.00 72.15 C ANISOU 2428 C ALA B 64 8456 8064 10893 176 -628 1812 C ATOM 2429 O ALA B 64 -14.555 -15.251 19.425 1.00 54.69 O ANISOU 2429 O ALA B 64 6107 5973 8700 177 -582 1898 O ATOM 2430 CB ALA B 64 -16.869 -13.125 18.059 1.00 39.94 C ANISOU 2430 CB ALA B 64 4762 3722 6692 93 -664 1546 C ATOM 2431 N ALA B 65 -16.345 -14.597 20.629 1.00 63.94 N ANISOU 2431 N ALA B 65 7392 7091 9811 139 -684 1838 N ATOM 2432 CA ALA B 65 -15.648 -14.778 21.902 1.00 63.94 C ANISOU 2432 CA ALA B 65 7203 7322 9768 86 -698 1976 C ATOM 2433 C ALA B 65 -15.265 -16.236 22.168 1.00 72.14 C ANISOU 2433 C ALA B 65 8048 8405 10957 215 -668 2132 C ATOM 2434 O ALA B 65 -14.363 -16.513 22.961 1.00 53.17 O ANISOU 2434 O ALA B 65 5465 6203 8533 184 -667 2267 O ATOM 2435 CB ALA B 65 -16.467 -14.224 23.048 1.00 41.52 C ANISOU 2435 CB ALA B 65 4390 4537 6850 12 -759 1961 C ATOM 2436 N ILE B 66 -15.943 -17.168 21.505 1.00 95.23 N ANISOU 2436 N ILE B 66 11007 11143 14033 357 -643 2117 N ATOM 2437 CA ILE B 66 -15.602 -18.581 21.650 1.00106.72 C ANISOU 2437 CA ILE B 66 12293 12610 15647 489 -602 2258 C ATOM 2438 C ILE B 66 -14.337 -18.909 20.871 1.00115.89 C ANISOU 2438 C ILE B 66 13372 13811 16851 515 -529 2297 C ATOM 2439 O ILE B 66 -13.288 -19.183 21.458 1.00106.71 O ANISOU 2439 O ILE B 66 12029 12833 15684 501 -517 2430 O ATOM 2440 CB ILE B 66 -16.726 -19.515 21.152 1.00109.08 C ANISOU 2440 CB ILE B 66 12657 12690 16098 628 -586 2222 C ATOM 2441 CG1 ILE B 66 -17.951 -19.424 22.055 1.00105.78 C ANISOU 2441 CG1 ILE B 66 12280 12250 15662 619 -652 2210 C ATOM 2442 CG2 ILE B 66 -16.245 -20.956 21.120 1.00115.00 C ANISOU 2442 CG2 ILE B 66 13246 13430 17019 763 -524 2358 C ATOM 2443 CD1 ILE B 66 -19.097 -20.294 21.587 1.00108.51 C ANISOU 2443 CD1 ILE B 66 12693 12389 16146 743 -638 2167 C ATOM 2444 N GLY B 67 -14.443 -18.871 19.546 1.00121.49 N ANISOU 2444 N GLY B 67 14800 16506 14854 -1187 -662 1232 N ATOM 2445 CA GLY B 67 -13.350 -19.287 18.686 1.00140.60 C ANISOU 2445 CA GLY B 67 17063 19023 17335 -1141 -666 1400 C ATOM 2446 C GLY B 67 -12.056 -18.543 18.948 1.00137.67 C ANISOU 2446 C GLY B 67 16616 18706 16985 -1167 -727 1512 C ATOM 2447 O GLY B 67 -10.969 -19.064 18.698 1.00145.18 O ANISOU 2447 O GLY B 67 17421 19755 17987 -1128 -724 1673 O ATOM 2448 N SER B 68 -12.174 -17.316 19.442 1.00114.95 N ANISOU 2448 N SER B 68 13840 15767 14070 -1226 -776 1431 N ATOM 2449 CA SER B 68 -11.007 -16.459 19.640 1.00104.74 C ANISOU 2449 CA SER B 68 12493 14519 12786 -1268 -845 1529 C ATOM 2450 C SER B 68 -10.430 -16.400 21.072 1.00 88.84 C ANISOU 2450 C SER B 68 10463 12540 10753 -1324 -890 1575 C ATOM 2451 O SER B 68 -9.471 -15.666 21.320 1.00 53.72 O ANISOU 2451 O SER B 68 5977 8130 6305 -1372 -955 1657 O ATOM 2452 CB SER B 68 -11.278 -15.057 19.079 1.00 98.82 C ANISOU 2452 CB SER B 68 11837 13696 12013 -1293 -877 1454 C ATOM 2453 OG SER B 68 -11.515 -15.110 17.677 1.00 67.97 O ANISOU 2453 OG SER B 68 7913 9782 8130 -1247 -845 1449 O ATOM 2454 N THR B 69 -11.004 -17.156 22.008 1.00106.52 N ANISOU 2454 N THR B 69 12731 14769 12973 -1326 -860 1529 N ATOM 2455 CA THR B 69 -10.445 -17.230 23.366 1.00110.66 C ANISOU 2455 CA THR B 69 13227 15336 13481 -1378 -899 1583 C ATOM 2456 C THR B 69 -10.147 -18.664 23.798 1.00103.92 C ANISOU 2456 C THR B 69 12257 14575 12654 -1341 -860 1686 C ATOM 2457 O THR B 69 -10.891 -19.590 23.474 1.00 98.48 O ANISOU 2457 O THR B 69 11569 13877 11971 -1288 -797 1653 O ATOM 2458 CB THR B 69 -11.359 -16.567 24.429 1.00 98.24 C ANISOU 2458 CB THR B 69 11810 13664 11852 -1426 -910 1436 C ATOM 2459 OG1 THR B 69 -11.579 -15.193 24.093 1.00109.84 O ANISOU 2459 OG1 THR B 69 13376 15058 13301 -1444 -942 1363 O ATOM 2460 CG2 THR B 69 -10.714 -16.641 25.814 1.00 24.58 C ANISOU 2460 CG2 THR B 69 2447 4385 2507 -1488 -956 1502 C ATOM 2461 N GLN B 70 -9.057 -18.838 24.539 1.00 92.15 N ANISOU 2461 N GLN B 70 10661 13177 11176 -1367 -896 1819 N ATOM 2462 CA GLN B 70 -8.654 -20.161 25.002 1.00 80.91 C ANISOU 2462 CA GLN B 70 9107 11856 9781 -1316 -853 1943 C ATOM 2463 C GLN B 70 -9.564 -20.694 26.107 1.00 78.74 C ANISOU 2463 C GLN B 70 8906 11549 9463 -1342 -834 1860 C ATOM 2464 O GLN B 70 -10.008 -21.841 26.042 1.00 81.70 O ANISOU 2464 O GLN B 70 9233 11955 9853 -1275 -769 1888 O ATOM 2465 CB GLN B 70 -7.199 -20.153 25.485 1.00 93.35 C ANISOU 2465 CB GLN B 70 10543 13546 11378 -1334 -894 2113 C ATOM 2466 CG GLN B 70 -6.199 -20.739 24.493 1.00101.34 C ANISOU 2466 CG GLN B 70 11392 14657 12456 -1238 -853 2277 C ATOM 2467 CD GLN B 70 -5.744 -19.737 23.445 1.00103.49 C ANISOU 2467 CD GLN B 70 11675 14908 12740 -1259 -894 2279 C ATOM 2468 OE1 GLN B 70 -5.989 -18.538 23.566 1.00114.37 O ANISOU 2468 OE1 GLN B 70 13169 16211 14077 -1347 -962 2181 O ATOM 2469 NE2 GLN B 70 -5.071 -20.228 22.412 1.00 89.97 N ANISOU 2469 NE2 GLN B 70 9841 13263 11082 -1168 -847 2398 N ATOM 2470 N ARG B 71 -9.840 -19.858 27.109 1.00106.18 N ANISOU 2470 N ARG B 71 12494 14962 12887 -1434 -886 1767 N ATOM 2471 CA ARG B 71 -10.618 -20.266 28.286 1.00134.36 C ANISOU 2471 CA ARG B 71 16137 18502 16410 -1472 -873 1694 C ATOM 2472 C ARG B 71 -12.038 -20.725 27.943 1.00129.06 C ANISOU 2472 C ARG B 71 15574 17748 15716 -1440 -811 1553 C ATOM 2473 O ARG B 71 -12.683 -21.446 28.718 1.00 87.01 O ANISOU 2473 O ARG B 71 10279 12423 10359 -1453 -783 1519 O ATOM 2474 CB ARG B 71 -10.674 -19.134 29.322 1.00130.18 C ANISOU 2474 CB ARG B 71 15721 17905 15835 -1565 -934 1613 C ATOM 2475 CG ARG B 71 -9.320 -18.724 29.896 1.00121.09 C ANISOU 2475 CG ARG B 71 14473 16840 14694 -1623 -1006 1750 C ATOM 2476 CD ARG B 71 -8.607 -17.712 29.002 1.00132.18 C ANISOU 2476 CD ARG B 71 15863 18238 16121 -1628 -1052 1781 C ATOM 2477 NE ARG B 71 -7.211 -18.074 28.753 1.00130.35 N ANISOU 2477 NE ARG B 71 15456 18139 15932 -1618 -1076 1970 N ATOM 2478 CZ ARG B 71 -6.352 -17.333 28.053 1.00 99.34 C ANISOU 2478 CZ ARG B 71 11484 14237 12024 -1630 -1122 2039 C ATOM 2479 NH1 ARG B 71 -6.736 -16.174 27.530 1.00 99.23 N ANISOU 2479 NH1 ARG B 71 11585 14128 11989 -1653 -1153 1941 N ATOM 2480 NH2 ARG B 71 -5.103 -17.744 27.875 1.00 45.42 N ANISOU 2480 NH2 ARG B 71 4490 7534 5232 -1615 -1134 2214 N ATOM 2481 N LEU B 72 -12.521 -20.281 26.787 1.00137.08 N ANISOU 2481 N LEU B 72 16648 18694 16742 -1405 -790 1471 N ATOM 2482 CA LEU B 72 -13.852 -20.632 26.309 1.00124.58 C ANISOU 2482 CA LEU B 72 15172 17029 15135 -1379 -732 1333 C ATOM 2483 C LEU B 72 -13.818 -21.794 25.308 1.00114.64 C ANISOU 2483 C LEU B 72 13838 15789 13931 -1276 -632 1398 C ATOM 2484 O LEU B 72 -14.855 -22.211 24.784 1.00102.99 O ANISOU 2484 O LEU B 72 12491 14177 12463 -1211 -504 1264 O ATOM 2485 CB LEU B 72 -14.527 -19.394 25.712 1.00107.44 C ANISOU 2485 CB LEU B 72 13138 14735 12949 -1378 -731 1184 C ATOM 2486 CG LEU B 72 -14.703 -18.270 26.738 1.00 95.83 C ANISOU 2486 CG LEU B 72 11773 13192 11446 -1424 -765 1102 C ATOM 2487 CD1 LEU B 72 -14.504 -16.894 26.109 1.00 83.65 C ANISOU 2487 CD1 LEU B 72 10273 11599 9912 -1416 -798 1073 C ATOM 2488 CD2 LEU B 72 -16.056 -18.382 27.449 1.00 96.00 C ANISOU 2488 CD2 LEU B 72 11933 13115 11429 -1421 -711 946 C ATOM 2489 N GLN B 73 -12.622 -22.321 25.059 1.00107.07 N ANISOU 2489 N GLN B 73 12724 14924 13032 -1213 -612 1573 N ATOM 2490 CA GLN B 73 -12.433 -23.378 24.065 1.00 92.27 C ANISOU 2490 CA GLN B 73 10833 12993 11233 -1062 -439 1614 C ATOM 2491 C GLN B 73 -12.566 -24.791 24.620 1.00 73.59 C ANISOU 2491 C GLN B 73 8523 10546 8890 -951 -252 1619 C ATOM 2492 O GLN B 73 -12.256 -25.768 23.933 1.00 55.56 O ANISOU 2492 O GLN B 73 6227 8225 6660 -825 -109 1672 O ATOM 2493 CB GLN B 73 -11.130 -23.197 23.287 1.00 73.34 C ANISOU 2493 CB GLN B 73 8246 10734 8887 -1033 -505 1798 C ATOM 2494 CG GLN B 73 -11.300 -22.279 22.088 1.00 56.61 C ANISOU 2494 CG GLN B 73 6129 8614 6765 -1066 -583 1762 C ATOM 2495 CD GLN B 73 -10.114 -22.304 21.159 1.00 68.53 C ANISOU 2495 CD GLN B 73 7465 10238 8335 -1007 -608 1940 C ATOM 2496 OE1 GLN B 73 -9.011 -21.898 21.530 1.00 73.10 O ANISOU 2496 OE1 GLN B 73 7955 10897 8923 -1038 -669 2049 O ATOM 2497 NE2 GLN B 73 -10.331 -22.787 19.940 1.00 76.60 N ANISOU 2497 NE2 GLN B 73 8521 11179 9404 -904 -480 1911 N ATOM 2498 N THR B 74 -13.000 -24.881 25.874 1.00 70.10 N ANISOU 2498 N THR B 74 8150 10083 8401 -1000 -259 1567 N ATOM 2499 CA THR B 74 -13.336 -26.161 26.487 1.00 85.15 C ANISOU 2499 CA THR B 74 10149 11894 10311 -905 -84 1548 C ATOM 2500 C THR B 74 -14.336 -26.889 25.577 1.00 77.55 C ANISOU 2500 C THR B 74 9342 10753 9370 -815 90 1418 C ATOM 2501 O THR B 74 -15.195 -26.247 24.970 1.00 83.93 O ANISOU 2501 O THR B 74 10227 11495 10167 -858 62 1290 O ATOM 2502 CB THR B 74 -13.913 -25.965 27.926 1.00 53.17 C ANISOU 2502 CB THR B 74 6178 7829 6197 -986 -126 1480 C ATOM 2503 OG1 THR B 74 -15.346 -25.978 27.901 1.00 48.54 O ANISOU 2503 OG1 THR B 74 5770 7090 5583 -990 -56 1294 O ATOM 2504 CG2 THR B 74 -13.432 -24.647 28.535 1.00 23.16 C ANISOU 2504 CG2 THR B 74 2279 4167 2353 -1144 -351 1520 C ATOM 2505 N LEU B 75 -14.214 -28.214 25.463 1.00 58.58 N ANISOU 2505 N LEU B 75 6987 8277 6992 -697 261 1452 N ATOM 2506 CA LEU B 75 -15.058 -28.988 24.542 1.00 36.21 C ANISOU 2506 CA LEU B 75 4306 5277 4176 -628 424 1339 C ATOM 2507 C LEU B 75 -16.527 -28.603 24.672 1.00 58.77 C ANISOU 2507 C LEU B 75 7320 8007 7004 -681 440 1153 C ATOM 2508 O LEU B 75 -17.206 -28.324 23.682 1.00 19.40 O ANISOU 2508 O LEU B 75 2392 2946 2035 -681 463 1056 O ATOM 2509 CB LEU B 75 -14.944 -30.497 24.800 1.00 22.68 C ANISOU 2509 CB LEU B 75 2664 3492 2460 -531 587 1372 C ATOM 2510 CG LEU B 75 -13.617 -31.246 24.731 1.00 24.32 C ANISOU 2510 CG LEU B 75 2728 3808 2706 -426 616 1561 C ATOM 2511 CD1 LEU B 75 -12.695 -30.817 25.867 1.00 25.34 C ANISOU 2511 CD1 LEU B 75 2703 4100 2824 -455 500 1701 C ATOM 2512 CD2 LEU B 75 -13.883 -32.748 24.771 1.00 24.80 C ANISOU 2512 CD2 LEU B 75 2901 3764 2758 -332 778 1546 C ATOM 2513 N THR B 76 -17.005 -28.579 25.912 1.00 85.68 N ANISOU 2513 N THR B 76 10778 11404 10371 -717 423 1116 N ATOM 2514 CA THR B 76 -18.419 -28.378 26.183 1.00 69.42 C ANISOU 2514 CA THR B 76 8843 9239 8293 -739 444 963 C ATOM 2515 C THR B 76 -18.899 -27.083 25.524 1.00 52.68 C ANISOU 2515 C THR B 76 6695 7157 6163 -824 300 876 C ATOM 2516 O THR B 76 -20.096 -26.879 25.336 1.00 60.70 O ANISOU 2516 O THR B 76 7795 8100 7168 -839 301 741 O ATOM 2517 CB THR B 76 -18.723 -28.416 27.703 1.00 47.66 C ANISOU 2517 CB THR B 76 6118 6500 5489 -776 415 956 C ATOM 2518 OG1 THR B 76 -18.234 -29.646 28.260 1.00 20.21 O ANISOU 2518 OG1 THR B 76 2678 2990 2009 -698 549 1039 O ATOM 2519 CG2 THR B 76 -20.211 -28.335 27.946 1.00 17.95 C ANISOU 2519 CG2 THR B 76 2458 2648 1713 -787 428 810 C ATOM 2520 N ASN B 77 -17.956 -26.218 25.163 1.00 66.34 N ANISOU 2520 N ASN B 77 8302 9015 7891 -883 164 956 N ATOM 2521 CA ASN B 77 -18.279 -25.007 24.416 1.00 81.43 C ANISOU 2521 CA ASN B 77 10197 10961 9780 -960 32 884 C ATOM 2522 C ASN B 77 -18.093 -25.152 22.899 1.00 65.37 C ANISOU 2522 C ASN B 77 8143 8896 7799 -896 93 899 C ATOM 2523 O ASN B 77 -18.346 -24.216 22.142 1.00 77.79 O ANISOU 2523 O ASN B 77 9708 10494 9354 -946 -2 846 O ATOM 2524 CB ASN B 77 -17.493 -23.807 24.963 1.00 88.32 C ANISOU 2524 CB ASN B 77 10963 11988 10605 -1079 -175 955 C ATOM 2525 CG ASN B 77 -18.050 -23.294 26.283 1.00 83.45 C ANISOU 2525 CG ASN B 77 10409 11383 9917 -1176 -262 880 C ATOM 2526 OD1 ASN B 77 -18.569 -22.181 26.363 1.00 86.22 O ANISOU 2526 OD1 ASN B 77 10805 11754 10202 -1275 -392 786 O ATOM 2527 ND2 ASN B 77 -17.958 -24.114 27.321 1.00 78.85 N ANISOU 2527 ND2 ASN B 77 9840 10781 9337 -1144 -185 919 N ATOM 2528 N LEU B 78 -17.643 -26.322 22.462 1.00 36.51 N ANISOU 2528 N LEU B 78 4491 5185 4197 -791 251 968 N ATOM 2529 CA LEU B 78 -17.563 -26.614 21.039 1.00 42.23 C ANISOU 2529 CA LEU B 78 5223 5856 4966 -730 334 966 C ATOM 2530 C LEU B 78 -18.931 -27.056 20.502 1.00 45.49 C ANISOU 2530 C LEU B 78 5783 6108 5393 -689 455 819 C ATOM 2531 O LEU B 78 -19.273 -26.822 19.327 1.00 27.87 O ANISOU 2531 O LEU B 78 3566 3838 3184 -675 469 771 O ATOM 2532 CB LEU B 78 -16.512 -27.693 20.776 1.00 66.43 C ANISOU 2532 CB LEU B 78 8239 8936 8065 -645 439 1095 C ATOM 2533 CG LEU B 78 -16.046 -27.825 19.321 1.00 57.86 C ANISOU 2533 CG LEU B 78 7112 7852 7021 -596 478 1136 C ATOM 2534 CD1 LEU B 78 -15.377 -26.533 18.888 1.00 48.55 C ANISOU 2534 CD1 LEU B 78 5779 6817 5851 -650 302 1214 C ATOM 2535 CD2 LEU B 78 -15.111 -29.017 19.157 1.00 20.91 C ANISOU 2535 CD2 LEU B 78 2382 3193 2369 -498 579 1260 C ATOM 2536 N PHE B 79 -19.707 -27.708 21.367 1.00 42.37 N ANISOU 2536 N PHE B 79 5472 5634 4992 -660 531 767 N ATOM 2537 CA PHE B 79 -21.093 -28.028 21.051 1.00 34.25 C ANISOU 2537 CA PHE B 79 4512 4523 3980 -627 567 661 C ATOM 2538 C PHE B 79 -21.873 -26.723 21.051 1.00 51.76 C ANISOU 2538 C PHE B 79 6752 6786 6127 -749 394 518 C ATOM 2539 O PHE B 79 -22.913 -26.592 20.399 1.00 69.81 O ANISOU 2539 O PHE B 79 9108 9023 8395 -770 375 385 O ATOM 2540 CB PHE B 79 -21.695 -28.972 22.086 1.00 15.67 C ANISOU 2540 CB PHE B 79 2198 2135 1619 -591 623 660 C ATOM 2541 CG PHE B 79 -20.984 -30.286 22.209 1.00 20.31 C ANISOU 2541 CG PHE B 79 2748 2704 2263 -456 752 796 C ATOM 2542 CD1 PHE B 79 -21.521 -31.433 21.653 1.00 16.88 C ANISOU 2542 CD1 PHE B 79 2294 2339 1779 -504 716 797 C ATOM 2543 CD2 PHE B 79 -19.788 -30.381 22.907 1.00 37.20 C ANISOU 2543 CD2 PHE B 79 4989 4803 4343 -513 820 798 C ATOM 2544 CE1 PHE B 79 -20.869 -32.654 21.781 1.00 20.87 C ANISOU 2544 CE1 PHE B 79 2840 2879 2210 -563 752 830 C ATOM 2545 CE2 PHE B 79 -19.129 -31.600 23.039 1.00 41.93 C ANISOU 2545 CE2 PHE B 79 5664 5428 4840 -610 843 797 C ATOM 2546 CZ PHE B 79 -19.670 -32.736 22.476 1.00 19.13 C ANISOU 2546 CZ PHE B 79 2695 2660 1913 -651 771 833 C ATOM 2547 N ILE B 80 -21.364 -25.755 21.802 1.00 27.02 N ANISOU 2547 N ILE B 80 3571 3752 2942 -837 261 540 N ATOM 2548 CA ILE B 80 -21.952 -24.431 21.832 1.00 13.79 C ANISOU 2548 CA ILE B 80 1922 2127 1189 -947 101 426 C ATOM 2549 C ILE B 80 -21.479 -23.614 20.639 1.00 13.71 C ANISOU 2549 C ILE B 80 1854 2174 1183 -964 32 456 C ATOM 2550 O ILE B 80 -22.126 -22.654 20.240 1.00 48.08 O ANISOU 2550 O ILE B 80 6251 6542 5474 -1024 -62 353 O ATOM 2551 CB ILE B 80 -21.584 -23.707 23.119 1.00 48.23 C ANISOU 2551 CB ILE B 80 6258 6580 5489 -1038 -24 452 C ATOM 2552 CG1 ILE B 80 -22.020 -24.528 24.346 1.00 65.42 C ANISOU 2552 CG1 ILE B 80 8491 8702 7662 -1020 49 431 C ATOM 2553 CG2 ILE B 80 -22.163 -22.315 23.111 1.00 37.49 C ANISOU 2553 CG2 ILE B 80 4942 5265 4036 -1143 -178 341 C ATOM 2554 CD1 ILE B 80 -23.491 -24.847 24.422 1.00 13.34 C ANISOU 2554 CD1 ILE B 80 2023 2002 1043 -1019 96 263 C ATOM 2555 N THR B 81 -20.344 -24.011 20.074 1.00 19.99 N ANISOU 2555 N THR B 81 2554 2999 2042 -907 84 600 N ATOM 2556 CA THR B 81 -19.864 -23.473 18.804 1.00 38.54 C ANISOU 2556 CA THR B 81 4843 5389 4411 -903 47 642 C ATOM 2557 C THR B 81 -20.843 -23.874 17.711 1.00 41.61 C ANISOU 2557 C THR B 81 5318 5666 4825 -851 146 535 C ATOM 2558 O THR B 81 -21.419 -23.029 17.003 1.00 20.85 O ANISOU 2558 O THR B 81 2718 3049 2155 -894 69 448 O ATOM 2559 CB THR B 81 -18.489 -24.084 18.439 1.00 39.11 C ANISOU 2559 CB THR B 81 4806 5505 4548 -840 108 811 C ATOM 2560 OG1 THR B 81 -17.525 -23.747 19.445 1.00 55.05 O ANISOU 2560 OG1 THR B 81 6721 7649 6546 -889 -2 926 O ATOM 2561 CG2 THR B 81 -18.008 -23.606 17.064 1.00 20.72 C ANISOU 2561 CG2 THR B 81 2412 3216 2245 -829 78 858 C ATOM 2562 N SER B 82 -21.041 -25.183 17.592 1.00 49.51 N ANISOU 2562 N SER B 82 6361 6564 5887 -757 315 547 N ATOM 2563 CA SER B 82 -22.005 -25.719 16.642 1.00 46.84 C ANISOU 2563 CA SER B 82 6093 6132 5571 -712 391 457 C ATOM 2564 C SER B 82 -23.378 -25.092 16.842 1.00 40.03 C ANISOU 2564 C SER B 82 5334 5251 4624 -796 294 261 C ATOM 2565 O SER B 82 -24.018 -24.672 15.886 1.00 11.56 O ANISOU 2565 O SER B 82 1775 1624 993 -816 266 161 O ATOM 2566 CB SER B 82 -22.109 -27.232 16.794 1.00 19.24 C ANISOU 2566 CB SER B 82 2617 2565 2130 -615 537 511 C ATOM 2567 OG SER B 82 -23.156 -27.748 15.991 1.00 13.30 O ANISOU 2567 OG SER B 82 1951 1741 1360 -622 554 379 O ATOM 2568 N LEU B 83 -23.825 -25.028 18.091 1.00 26.44 N ANISOU 2568 N LEU B 83 3660 3532 2854 -841 254 201 N ATOM 2569 CA LEU B 83 -25.165 -24.537 18.373 1.00 22.23 C ANISOU 2569 CA LEU B 83 3246 2962 2238 -909 192 7 C ATOM 2570 C LEU B 83 -25.331 -23.062 18.046 1.00 27.91 C ANISOU 2570 C LEU B 83 3967 3758 2880 -982 59 -49 C ATOM 2571 O LEU B 83 -26.352 -22.650 17.504 1.00 23.42 O ANISOU 2571 O LEU B 83 3398 3124 2378 -870 83 -103 O ATOM 2572 CB LEU B 83 -25.547 -24.781 19.824 1.00 18.79 C ANISOU 2572 CB LEU B 83 2858 2512 1771 -940 185 -32 C ATOM 2573 CG LEU B 83 -27.042 -25.044 19.889 1.00 31.84 C ANISOU 2573 CG LEU B 83 4599 4065 3432 -901 219 -178 C ATOM 2574 CD1 LEU B 83 -27.255 -26.541 19.758 1.00 10.65 C ANISOU 2574 CD1 LEU B 83 2007 1275 763 -893 341 -225 C ATOM 2575 CD2 LEU B 83 -27.650 -24.487 21.165 1.00 9.93 C ANISOU 2575 CD2 LEU B 83 1793 1301 680 -857 175 -173 C ATOM 2576 N ALA B 84 -24.337 -22.259 18.400 1.00 40.17 N ANISOU 2576 N ALA B 84 5429 5416 4417 -1018 -34 65 N ATOM 2577 CA ALA B 84 -24.363 -20.858 18.024 1.00 44.74 C ANISOU 2577 CA ALA B 84 5967 6022 5012 -980 -102 79 C ATOM 2578 C ALA B 84 -24.473 -20.818 16.516 1.00 51.95 C ANISOU 2578 C ALA B 84 6879 6923 5936 -962 -81 62 C ATOM 2579 O ALA B 84 -25.117 -19.930 15.958 1.00 54.21 O ANISOU 2579 O ALA B 84 7162 7167 6268 -876 -76 27 O ATOM 2580 CB ALA B 84 -23.105 -20.160 18.476 1.00 49.95 C ANISOU 2580 CB ALA B 84 6538 6792 5649 -1040 -206 208 C ATOM 2581 N CYS B 85 -23.850 -21.797 15.860 1.00 46.75 N ANISOU 2581 N CYS B 85 6193 6267 5304 -968 -21 124 N ATOM 2582 CA CYS B 85 -23.948 -21.901 14.409 1.00 34.56 C ANISOU 2582 CA CYS B 85 4645 4690 3797 -928 28 116 C ATOM 2583 C CYS B 85 -25.388 -22.125 13.947 1.00 19.52 C ANISOU 2583 C CYS B 85 2865 2694 1858 -921 68 -64 C ATOM 2584 O CYS B 85 -25.941 -21.294 13.235 1.00 25.26 O ANISOU 2584 O CYS B 85 3564 3403 2629 -842 53 -76 O ATOM 2585 CB CYS B 85 -23.050 -23.023 13.881 1.00 44.08 C ANISOU 2585 CB CYS B 85 5777 5857 5116 -839 159 253 C ATOM 2586 SG CYS B 85 -21.276 -22.711 13.998 1.00 96.04 S ANISOU 2586 SG CYS B 85 12206 12543 11743 -831 125 463 S ATOM 2587 N ALA B 86 -26.002 -23.225 14.377 1.00 27.27 N ANISOU 2587 N ALA B 86 3915 3582 2863 -892 157 -133 N ATOM 2588 CA ALA B 86 -27.361 -23.546 13.949 1.00 40.66 C ANISOU 2588 CA ALA B 86 5619 5184 4647 -761 207 -194 C ATOM 2589 C ALA B 86 -28.257 -22.348 14.207 1.00 44.62 C ANISOU 2589 C ALA B 86 6062 5741 5151 -643 182 -142 C ATOM 2590 O ALA B 86 -28.969 -21.888 13.315 1.00 53.78 O ANISOU 2590 O ALA B 86 7220 6892 6321 -634 195 -151 O ATOM 2591 CB ALA B 86 -27.896 -24.798 14.663 1.00 9.09 C ANISOU 2591 CB ALA B 86 1672 1108 675 -734 279 -232 C ATOM 2592 N ASP B 87 -28.195 -21.831 15.431 1.00 51.02 N ANISOU 2592 N ASP B 87 6867 6577 5942 -664 151 -121 N ATOM 2593 CA ASP B 87 -28.997 -20.678 15.829 1.00 57.73 C ANISOU 2593 CA ASP B 87 7665 7362 6907 -737 127 -103 C ATOM 2594 C ASP B 87 -28.763 -19.515 14.874 1.00 47.10 C ANISOU 2594 C ASP B 87 6292 6050 5555 -744 94 -80 C ATOM 2595 O ASP B 87 -29.681 -18.743 14.549 1.00 53.81 O ANISOU 2595 O ASP B 87 7199 6964 6284 -676 113 -95 O ATOM 2596 CB ASP B 87 -28.673 -20.271 17.271 1.00 55.80 C ANISOU 2596 CB ASP B 87 7417 7141 6642 -766 97 -81 C ATOM 2597 CG ASP B 87 -29.109 -21.316 18.280 1.00 53.16 C ANISOU 2597 CG ASP B 87 7164 6849 6184 -696 145 -116 C ATOM 2598 OD1 ASP B 87 -30.265 -21.785 18.186 1.00 38.73 O ANISOU 2598 OD1 ASP B 87 5360 4981 4375 -677 196 -149 O ATOM 2599 OD2 ASP B 87 -28.295 -21.677 19.158 1.00 43.56 O ANISOU 2599 OD2 ASP B 87 5945 5653 4952 -713 121 -98 O ATOM 2600 N LEU B 88 -27.525 -19.409 14.409 1.00 31.66 N ANISOU 2600 N LEU B 88 4303 4137 3590 -756 52 -46 N ATOM 2601 CA LEU B 88 -27.153 -18.334 13.510 1.00 38.21 C ANISOU 2601 CA LEU B 88 5103 5003 4412 -767 15 -14 C ATOM 2602 C LEU B 88 -27.772 -18.502 12.122 1.00 40.74 C ANISOU 2602 C LEU B 88 5435 5296 4750 -739 49 -44 C ATOM 2603 O LEU B 88 -28.445 -17.605 11.626 1.00 18.54 O ANISOU 2603 O LEU B 88 2625 2479 1939 -737 51 -46 O ATOM 2604 CB LEU B 88 -25.639 -18.220 13.413 1.00 26.29 C ANISOU 2604 CB LEU B 88 3590 3614 2785 -774 -91 15 C ATOM 2605 CG LEU B 88 -25.223 -16.911 12.760 1.00 39.02 C ANISOU 2605 CG LEU B 88 5164 5264 4397 -770 -144 64 C ATOM 2606 CD1 LEU B 88 -24.405 -16.084 13.728 1.00 9.68 C ANISOU 2606 CD1 LEU B 88 1450 1605 623 -788 -165 182 C ATOM 2607 CD2 LEU B 88 -24.470 -17.195 11.467 1.00 56.82 C ANISOU 2607 CD2 LEU B 88 7389 7573 6626 -833 -163 118 C ATOM 2608 N VAL B 89 -27.557 -19.651 11.496 1.00 53.50 N ANISOU 2608 N VAL B 89 7114 6956 6259 -659 84 -74 N ATOM 2609 CA VAL B 89 -28.191 -19.916 10.211 1.00 51.15 C ANISOU 2609 CA VAL B 89 6828 6626 5981 -638 124 -106 C ATOM 2610 C VAL B 89 -29.695 -19.674 10.328 1.00 41.90 C ANISOU 2610 C VAL B 89 5630 5352 4938 -687 149 -122 C ATOM 2611 O VAL B 89 -30.339 -19.231 9.375 1.00 7.80 O ANISOU 2611 O VAL B 89 1309 1028 625 -680 157 -128 O ATOM 2612 CB VAL B 89 -27.928 -21.355 9.732 1.00 45.36 C ANISOU 2612 CB VAL B 89 6115 5820 5298 -655 137 -177 C ATOM 2613 CG1 VAL B 89 -28.470 -21.551 8.335 1.00 21.02 C ANISOU 2613 CG1 VAL B 89 3043 2740 2202 -604 207 -162 C ATOM 2614 CG2 VAL B 89 -26.442 -21.659 9.763 1.00 63.52 C ANISOU 2614 CG2 VAL B 89 8441 8181 7513 -801 139 -140 C ATOM 2615 N VAL B 90 -30.245 -19.963 11.509 1.00 28.99 N ANISOU 2615 N VAL B 90 4057 3771 3186 -629 180 -144 N ATOM 2616 CA VAL B 90 -31.644 -19.648 11.795 1.00 40.08 C ANISOU 2616 CA VAL B 90 5430 5084 4714 -687 187 -146 C ATOM 2617 C VAL B 90 -31.881 -18.172 11.574 1.00 42.62 C ANISOU 2617 C VAL B 90 5780 5506 4907 -635 172 -139 C ATOM 2618 O VAL B 90 -32.727 -17.787 10.762 1.00 31.88 O ANISOU 2618 O VAL B 90 4374 4067 3673 -687 170 -136 O ATOM 2619 CB VAL B 90 -32.039 -19.934 13.263 1.00 65.91 C ANISOU 2619 CB VAL B 90 8717 8343 7981 -695 197 -151 C ATOM 2620 CG1 VAL B 90 -33.443 -19.400 13.560 1.00 8.23 C ANISOU 2620 CG1 VAL B 90 1420 1029 679 -697 212 -160 C ATOM 2621 CG2 VAL B 90 -31.968 -21.408 13.558 1.00 86.88 C ANISOU 2621 CG2 VAL B 90 11439 11044 10529 -625 254 -186 C ATOM 2622 N GLY B 91 -31.126 -17.349 12.302 1.00 34.86 N ANISOU 2622 N GLY B 91 4789 4553 3903 -654 130 -108 N ATOM 2623 CA GLY B 91 -31.319 -15.909 12.259 1.00 8.16 C ANISOU 2623 CA GLY B 91 1401 1190 508 -668 101 -87 C ATOM 2624 C GLY B 91 -30.691 -15.260 11.046 1.00 22.89 C ANISOU 2624 C GLY B 91 3195 3011 2493 -733 66 -58 C ATOM 2625 O GLY B 91 -30.562 -14.044 10.987 1.00 26.10 O ANISOU 2625 O GLY B 91 3650 3505 2761 -689 40 -36 O ATOM 2626 N LEU B 92 -30.303 -16.081 10.077 1.00 37.53 N ANISOU 2626 N LEU B 92 5041 4862 4357 -718 76 -67 N ATOM 2627 CA LEU B 92 -29.658 -15.600 8.863 1.00 47.63 C ANISOU 2627 CA LEU B 92 6298 6167 5632 -722 50 -46 C ATOM 2628 C LEU B 92 -30.480 -15.977 7.630 1.00 69.30 C ANISOU 2628 C LEU B 92 9103 8951 8276 -640 93 -83 C ATOM 2629 O LEU B 92 -30.982 -15.101 6.931 1.00 88.84 O ANISOU 2629 O LEU B 92 11522 11365 10868 -699 80 -72 O ATOM 2630 CB LEU B 92 -28.237 -16.164 8.757 1.00 60.98 C ANISOU 2630 CB LEU B 92 8022 7955 7194 -672 22 -20 C ATOM 2631 CG LEU B 92 -27.328 -15.682 7.621 1.00 73.82 C ANISOU 2631 CG LEU B 92 9616 9620 8812 -682 -22 22 C ATOM 2632 CD1 LEU B 92 -27.028 -14.206 7.763 1.00 8.55 C ANISOU 2632 CD1 LEU B 92 1267 1324 656 -776 -67 69 C ATOM 2633 CD2 LEU B 92 -26.036 -16.496 7.593 1.00 81.30 C ANISOU 2633 CD2 LEU B 92 10515 10592 9782 -721 -91 20 C ATOM 2634 N LEU B 93 -30.575 -17.275 7.339 1.00 61.91 N ANISOU 2634 N LEU B 93 7912 6533 9077 -302 -1944 400 N ATOM 2635 CA LEU B 93 -31.397 -17.762 6.225 1.00 35.68 C ANISOU 2635 CA LEU B 93 4582 3202 5773 -285 -1949 378 C ATOM 2636 C LEU B 93 -32.888 -17.998 6.498 1.00 23.37 C ANISOU 2636 C LEU B 93 3004 1631 4245 -275 -1956 369 C ATOM 2637 O LEU B 93 -33.729 -17.722 5.638 1.00 27.58 O ANISOU 2637 O LEU B 93 3546 2150 4782 -276 -1977 370 O ATOM 2638 CB LEU B 93 -30.761 -18.985 5.566 1.00 40.64 C ANISOU 2638 CB LEU B 93 5189 3817 6435 -269 -1951 364 C ATOM 2639 CG LEU B 93 -29.531 -18.605 4.735 1.00 63.96 C ANISOU 2639 CG LEU B 93 8162 6775 9363 -279 -1954 374 C ATOM 2640 CD1 LEU B 93 -28.947 -19.812 4.016 1.00 72.27 C ANISOU 2640 CD1 LEU B 93 9205 7804 10451 -223 -1936 364 C ATOM 2641 CD2 LEU B 93 -29.874 -17.489 3.745 1.00 53.09 C ANISOU 2641 CD2 LEU B 93 6840 5414 7918 -304 -1962 389 C ATOM 2642 N VAL B 94 -33.212 -18.533 7.672 1.00 21.89 N ANISOU 2642 N VAL B 94 2791 1442 4084 -270 -1947 369 N ATOM 2643 CA VAL B 94 -34.603 -18.874 7.968 1.00 36.60 C ANISOU 2643 CA VAL B 94 4633 3294 5978 -264 -1952 367 C ATOM 2644 C VAL B 94 -35.523 -17.763 8.442 1.00 22.26 C ANISOU 2644 C VAL B 94 2824 1459 4175 -253 -1953 377 C ATOM 2645 O VAL B 94 -36.674 -17.710 8.033 1.00 22.55 O ANISOU 2645 O VAL B 94 2850 1476 4241 -239 -1953 382 O ATOM 2646 CB VAL B 94 -34.721 -19.988 8.970 1.00 28.16 C ANISOU 2646 CB VAL B 94 3549 2221 4929 -263 -1951 370 C ATOM 2647 CG1 VAL B 94 -35.984 -19.790 9.790 1.00 22.14 C ANISOU 2647 CG1 VAL B 94 2770 1453 4188 -264 -1951 379 C ATOM 2648 CG2 VAL B 94 -34.748 -21.310 8.238 1.00 22.26 C ANISOU 2648 CG2 VAL B 94 2808 1457 4192 -253 -1966 365 C ATOM 2649 N VAL B 95 -35.044 -16.906 9.333 1.00 22.31 N ANISOU 2649 N VAL B 95 2862 1462 4151 -243 -1930 390 N ATOM 2650 CA VAL B 95 -35.883 -15.816 9.832 1.00 55.63 C ANISOU 2650 CA VAL B 95 7126 5637 8373 -199 -1885 406 C ATOM 2651 C VAL B 95 -36.228 -14.726 8.821 1.00 60.64 C ANISOU 2651 C VAL B 95 7827 6214 8998 -164 -1868 421 C ATOM 2652 O VAL B 95 -37.383 -14.324 8.748 1.00 24.23 O ANISOU 2652 O VAL B 95 3228 1550 4427 -111 -1834 433 O ATOM 2653 CB VAL B 95 -35.310 -15.141 11.072 1.00 62.89 C ANISOU 2653 CB VAL B 95 8101 6544 9252 -196 -1847 423 C ATOM 2654 CG1 VAL B 95 -36.109 -13.892 11.376 1.00 23.82 C ANISOU 2654 CG1 VAL B 95 3245 1503 4304 -136 -1763 436 C ATOM 2655 CG2 VAL B 95 -35.359 -16.095 12.238 1.00 87.66 C ANISOU 2655 CG2 VAL B 95 11186 9718 12403 -219 -1858 425 C ATOM 2656 N PRO B 96 -35.226 -14.218 8.072 1.00 59.50 N ANISOU 2656 N PRO B 96 7738 6067 8801 -188 -1887 428 N ATOM 2657 CA PRO B 96 -35.480 -13.140 7.113 1.00 63.11 C ANISOU 2657 CA PRO B 96 8294 6450 9236 -161 -1870 452 C ATOM 2658 C PRO B 96 -36.450 -13.564 6.033 1.00 53.54 C ANISOU 2658 C PRO B 96 7034 5235 8073 -149 -1909 456 C ATOM 2659 O PRO B 96 -37.409 -12.855 5.736 1.00 37.04 O ANISOU 2659 O PRO B 96 4994 3070 6011 -90 -1879 486 O ATOM 2660 CB PRO B 96 -34.109 -12.920 6.479 1.00 24.22 C ANISOU 2660 CB PRO B 96 3418 1547 4238 -217 -1899 459 C ATOM 2661 CG PRO B 96 -33.435 -14.202 6.630 1.00 23.17 C ANISOU 2661 CG PRO B 96 3171 1507 4125 -254 -1947 433 C ATOM 2662 CD PRO B 96 -33.832 -14.674 7.986 1.00 22.91 C ANISOU 2662 CD PRO B 96 3085 1491 4129 -240 -1924 422 C ATOM 2663 N PHE B 97 -36.207 -14.724 5.448 1.00 23.94 N ANISOU 2663 N PHE B 97 3203 1555 4338 -201 -1966 433 N ATOM 2664 CA PHE B 97 -37.125 -15.217 4.452 1.00 24.17 C ANISOU 2664 CA PHE B 97 3199 1578 4407 -209 -2000 441 C ATOM 2665 C PHE B 97 -38.409 -15.575 5.166 1.00 37.58 C ANISOU 2665 C PHE B 97 4845 3265 6169 -176 -1973 447 C ATOM 2666 O PHE B 97 -39.497 -15.486 4.595 1.00 25.05 O ANISOU 2666 O PHE B 97 3250 1645 4623 -152 -1980 478 O ATOM 2667 CB PHE B 97 -36.526 -16.416 3.727 1.00 29.35 C ANISOU 2667 CB PHE B 97 3809 2288 5054 -268 -2046 416 C ATOM 2668 CG PHE B 97 -35.490 -16.040 2.715 1.00 64.63 C ANISOU 2668 CG PHE B 97 8330 6762 9466 -294 -2074 422 C ATOM 2669 CD1 PHE B 97 -35.106 -14.711 2.574 1.00 65.72 C ANISOU 2669 CD1 PHE B 97 8561 6857 9552 -280 -2064 452 C ATOM 2670 CD2 PHE B 97 -34.916 -16.996 1.896 1.00 22.99 C ANISOU 2670 CD2 PHE B 97 3041 1523 4170 -316 -2075 409 C ATOM 2671 CE1 PHE B 97 -34.162 -14.338 1.642 1.00 37.81 C ANISOU 2671 CE1 PHE B 97 5092 3324 5950 -315 -2090 468 C ATOM 2672 CE2 PHE B 97 -33.972 -16.634 0.961 1.00 43.61 C ANISOU 2672 CE2 PHE B 97 5706 4141 6724 -336 -2088 422 C ATOM 2673 CZ PHE B 97 -33.594 -15.299 0.833 1.00 53.89 C ANISOU 2673 CZ PHE B 97 7086 5408 7981 -350 -2123 451 C ATOM 2674 N GLY B 98 -38.259 -15.925 6.441 1.00 33.71 N ANISOU 2674 N GLY B 98 4325 2800 5685 -173 -1943 427 N ATOM 2675 CA GLY B 98 -39.342 -16.419 7.270 1.00 38.07 C ANISOU 2675 CA GLY B 98 4827 3350 6286 -154 -1918 431 C ATOM 2676 C GLY B 98 -40.322 -15.357 7.704 1.00 25.00 C ANISOU 2676 C GLY B 98 3206 1628 4666 -64 -1856 462 C ATOM 2677 O GLY B 98 -41.415 -15.660 8.170 1.00 25.28 O ANISOU 2677 O GLY B 98 3199 1655 4752 -33 -1833 477 O ATOM 2678 N ALA B 99 -39.923 -14.103 7.553 1.00 25.73 N ANISOU 2678 N ALA B 99 3389 1658 4728 -12 -1820 479 N ATOM 2679 CA ALA B 99 -40.823 -12.988 7.755 1.00 45.96 C ANISOU 2679 CA ALA B 99 6019 4120 7322 106 -1743 518 C ATOM 2680 C ALA B 99 -41.708 -12.871 6.523 1.00 54.07 C ANISOU 2680 C ALA B 99 7037 5120 8387 151 -1775 567 C ATOM 2681 O ALA B 99 -42.930 -12.796 6.630 1.00 29.05 O ANISOU 2681 O ALA B 99 3836 1924 5278 243 -1745 607 O ATOM 2682 CB ALA B 99 -40.034 -11.705 7.963 1.00 27.91 C ANISOU 2682 CB ALA B 99 3879 1743 4981 142 -1677 526 C ATOM 2683 N THR B 100 -41.083 -12.941 5.348 1.00 76.46 N ANISOU 2683 N THR B 100 9894 7972 11185 87 -1842 570 N ATOM 2684 CA THR B 100 -41.732 -12.532 4.107 1.00 80.52 C ANISOU 2684 CA THR B 100 10438 8440 11715 133 -1873 633 C ATOM 2685 C THR B 100 -43.123 -13.144 3.985 1.00 68.08 C ANISOU 2685 C THR B 100 8768 6889 10211 175 -1884 674 C ATOM 2686 O THR B 100 -43.998 -12.587 3.326 1.00 84.87 O ANISOU 2686 O THR B 100 10913 8970 12362 281 -1884 755 O ATOM 2687 CB THR B 100 -40.881 -12.874 2.844 1.00 28.48 C ANISOU 2687 CB THR B 100 3862 1886 5073 23 -1958 623 C ATOM 2688 OG1 THR B 100 -41.092 -14.235 2.454 1.00 27.44 O ANISOU 2688 OG1 THR B 100 3628 1834 4964 -70 -2016 598 O ATOM 2689 CG2 THR B 100 -39.405 -12.650 3.097 1.00 27.64 C ANISOU 2689 CG2 THR B 100 3812 1799 4892 -38 -1956 577 C ATOM 2690 N LEU B 101 -43.325 -14.290 4.626 1.00 46.73 N ANISOU 2690 N LEU B 101 5970 4255 7530 102 -1893 632 N ATOM 2691 CA LEU B 101 -44.621 -14.956 4.604 1.00 57.35 C ANISOU 2691 CA LEU B 101 7232 5626 8931 126 -1900 674 C ATOM 2692 C LEU B 101 -45.583 -14.307 5.595 1.00 52.59 C ANISOU 2692 C LEU B 101 6616 4992 8372 283 -1819 709 C ATOM 2693 O LEU B 101 -46.790 -14.311 5.371 1.00 72.91 O ANISOU 2693 O LEU B 101 9134 7585 10985 384 -1817 781 O ATOM 2694 CB LEU B 101 -44.473 -16.454 4.912 1.00 70.07 C ANISOU 2694 CB LEU B 101 8780 7304 10541 -11 -1937 624 C ATOM 2695 CG LEU B 101 -45.567 -17.426 4.454 1.00 37.18 C ANISOU 2695 CG LEU B 101 4554 3167 6407 -50 -1971 672 C ATOM 2696 CD1 LEU B 101 -45.318 -17.851 3.025 1.00 27.31 C ANISOU 2696 CD1 LEU B 101 3323 1921 5131 -136 -2042 691 C ATOM 2697 CD2 LEU B 101 -45.600 -18.648 5.349 1.00 59.22 C ANISOU 2697 CD2 LEU B 101 7313 5993 9195 -133 -1972 632 C ATOM 2698 N VAL B 102 -45.058 -13.790 6.707 1.00 45.47 N ANISOU 2698 N VAL B 102 5762 4057 7458 314 -1753 664 N ATOM 2699 CA VAL B 102 -45.904 -13.112 7.693 1.00 74.67 C ANISOU 2699 CA VAL B 102 9466 7708 11196 476 -1659 689 C ATOM 2700 C VAL B 102 -46.168 -11.653 7.321 1.00122.33 C ANISOU 2700 C VAL B 102 15610 13635 17236 667 -1593 753 C ATOM 2701 O VAL B 102 -47.284 -11.154 7.471 1.00144.01 O ANISOU 2701 O VAL B 102 18335 16357 20024 864 -1540 816 O ATOM 2702 CB VAL B 102 -45.327 -13.181 9.122 1.00 29.93 C ANISOU 2702 CB VAL B 102 3822 2033 5516 431 -1602 623 C ATOM 2703 CG1 VAL B 102 -46.456 -13.146 10.141 1.00 30.69 C ANISOU 2703 CG1 VAL B 102 3872 2120 5667 550 -1529 637 C ATOM 2704 CG2 VAL B 102 -44.505 -14.434 9.297 1.00 33.85 C ANISOU 2704 CG2 VAL B 102 4265 2619 5976 244 -1677 567 C ATOM 2705 N VAL B 103 -45.129 -10.971 6.846 1.00134.22 N ANISOU 2705 N VAL B 103 17235 15074 18690 627 -1594 743 N ATOM 2706 CA VAL B 103 -45.226 -9.562 6.476 1.00132.11 C ANISOU 2706 CA VAL B 103 17117 14664 18414 794 -1521 809 C ATOM 2707 C VAL B 103 -46.218 -9.342 5.339 1.00132.26 C ANISOU 2707 C VAL B 103 17105 14688 18458 934 -1567 919 C ATOM 2708 O VAL B 103 -47.214 -8.635 5.506 1.00131.11 O ANISOU 2708 O VAL B 103 16977 14487 18350 1172 -1496 998 O ATOM 2709 CB VAL B 103 -43.840 -8.989 6.069 1.00115.44 C ANISOU 2709 CB VAL B 103 15148 12486 16228 687 -1527 782 C ATOM 2710 CG1 VAL B 103 -43.994 -7.770 5.175 1.00113.62 C ANISOU 2710 CG1 VAL B 103 15074 12111 15986 822 -1491 874 C ATOM 2711 CG2 VAL B 103 -43.009 -8.653 7.301 1.00114.14 C ANISOU 2711 CG2 VAL B 103 15068 12270 16031 636 -1436 714 C ATOM 2712 N ARG B 104 -45.957 -9.972 4.195 1.00138.42 N ANISOU 2712 N ARG B 104 17835 15544 19215 801 -1684 930 N ATOM 2713 CA ARG B 104 -46.790 -9.792 3.006 1.00131.18 C ANISOU 2713 CA ARG B 104 16892 14645 18305 909 -1744 1046 C ATOM 2714 C ARG B 104 -47.973 -10.763 2.968 1.00109.94 C ANISOU 2714 C ARG B 104 14021 12097 15653 935 -1793 1083 C ATOM 2715 O ARG B 104 -48.914 -10.576 2.196 1.00 87.97 O ANISOU 2715 O ARG B 104 11185 9369 12871 1080 -1835 1199 O ATOM 2716 CB ARG B 104 -45.942 -9.936 1.734 1.00115.47 C ANISOU 2716 CB ARG B 104 14955 12656 16262 748 -1841 1046 C ATOM 2717 CG ARG B 104 -46.690 -9.638 0.444 1.00116.01 C ANISOU 2717 CG ARG B 104 15021 12734 16323 851 -1911 1181 C ATOM 2718 CD ARG B 104 -47.421 -8.305 0.532 1.00141.43 C ANISOU 2718 CD ARG B 104 18334 15849 19554 1150 -1834 1305 C ATOM 2719 NE ARG B 104 -48.221 -8.018 -0.660 1.00162.29 N ANISOU 2719 NE ARG B 104 20955 18529 22177 1288 -1912 1461 N ATOM 2720 CZ ARG B 104 -49.524 -8.262 -0.770 1.00159.12 C ANISOU 2720 CZ ARG B 104 20403 18264 21791 1469 -1944 1561 C ATOM 2721 NH1 ARG B 104 -50.190 -8.807 0.241 1.00159.28 N ANISOU 2721 NH1 ARG B 104 20285 18383 21851 1524 -1899 1512 N ATOM 2722 NH2 ARG B 104 -50.165 -7.961 -1.893 1.00144.30 N ANISOU 2722 NH2 ARG B 104 18505 16447 19874 1600 -2030 1715 N ATOM 2723 N GLY B 105 -47.925 -11.786 3.817 1.00108.71 N ANISOU 2723 N GLY B 105 13776 12011 15519 803 -1788 995 N ATOM 2724 CA GLY B 105 -48.973 -12.790 3.875 1.00 84.69 C ANISOU 2724 CA GLY B 105 10580 9098 12502 796 -1826 1025 C ATOM 2725 C GLY B 105 -48.697 -14.012 3.018 1.00 76.22 C ANISOU 2725 C GLY B 105 9466 8086 11410 571 -1921 1009 C ATOM 2726 O GLY B 105 -49.386 -15.024 3.151 1.00 34.00 O ANISOU 2726 O GLY B 105 4018 2829 6071 514 -1947 1022 O ATOM 2727 N THR B 106 -47.689 -13.920 2.148 1.00 82.33 N ANISOU 2727 N THR B 106 10325 8807 12149 449 -1967 982 N ATOM 2728 CA THR B 106 -47.373 -14.987 1.191 1.00 60.63 C ANISOU 2728 CA THR B 106 7560 6098 9380 255 -2048 969 C ATOM 2729 C THR B 106 -45.909 -15.065 0.747 1.00 58.02 C ANISOU 2729 C THR B 106 7314 5723 9007 105 -2078 883 C ATOM 2730 O THR B 106 -45.116 -14.145 0.945 1.00 38.14 O ANISOU 2730 O THR B 106 4877 3151 6465 146 -2049 853 O ATOM 2731 CB THR B 106 -48.172 -14.856 -0.106 1.00 57.13 C ANISOU 2731 CB THR B 106 7087 5702 8916 309 -2119 1099 C ATOM 2732 OG1 THR B 106 -47.617 -13.792 -0.888 1.00 55.51 O ANISOU 2732 OG1 THR B 106 6984 5425 8682 361 -2139 1134 O ATOM 2733 CG2 THR B 106 -49.644 -14.596 0.175 1.00 91.48 C ANISOU 2733 CG2 THR B 106 11323 10157 13278 519 -2108 1209 C ATOM 2734 N TRP B 107 -45.589 -16.184 0.110 1.00 86.78 N ANISOU 2734 N TRP B 107 10940 9400 12632 -57 -2135 852 N ATOM 2735 CA TRP B 107 -44.245 -16.500 -0.348 1.00 92.17 C ANISOU 2735 CA TRP B 107 11676 10081 13265 -180 -2169 772 C ATOM 2736 C TRP B 107 -43.971 -16.000 -1.768 1.00 74.82 C ANISOU 2736 C TRP B 107 9541 7860 11028 -208 -2232 825 C ATOM 2737 O TRP B 107 -44.617 -16.429 -2.722 1.00 71.52 O ANISOU 2737 O TRP B 107 9109 7457 10609 -254 -2284 897 O ATOM 2738 CB TRP B 107 -44.074 -18.014 -0.313 1.00 88.19 C ANISOU 2738 CB TRP B 107 11136 9622 12752 -307 -2194 719 C ATOM 2739 CG TRP B 107 -42.692 -18.454 -0.531 1.00 54.45 C ANISOU 2739 CG TRP B 107 6896 5373 8420 -377 -2216 638 C ATOM 2740 CD1 TRP B 107 -42.133 -18.855 -1.705 1.00 25.92 C ANISOU 2740 CD1 TRP B 107 3320 1771 4757 -452 -2272 636 C ATOM 2741 CD2 TRP B 107 -41.672 -18.540 0.455 1.00 46.71 C ANISOU 2741 CD2 TRP B 107 5913 4419 7415 -360 -2179 562 C ATOM 2742 NE1 TRP B 107 -40.817 -19.189 -1.509 1.00 53.19 N ANISOU 2742 NE1 TRP B 107 6803 5273 8134 -432 -2216 570 N ATOM 2743 CE2 TRP B 107 -40.509 -19.003 -0.188 1.00 42.95 C ANISOU 2743 CE2 TRP B 107 5475 3980 6864 -390 -2180 528 C ATOM 2744 CE3 TRP B 107 -41.629 -18.272 1.824 1.00 50.15 C ANISOU 2744 CE3 TRP B 107 6325 4858 7870 -306 -2122 535 C ATOM 2745 CZ2 TRP B 107 -39.314 -19.205 0.488 1.00 40.88 C ANISOU 2745 CZ2 TRP B 107 5223 3755 6555 -359 -2122 477 C ATOM 2746 CZ3 TRP B 107 -40.445 -18.469 2.495 1.00 82.68 C ANISOU 2746 CZ3 TRP B 107 10452 9010 11952 -310 -2103 479 C ATOM 2747 CH2 TRP B 107 -39.300 -18.933 1.827 1.00 81.21 C ANISOU 2747 CH2 TRP B 107 10298 8859 11699 -332 -2103 454 C ATOM 2748 N LEU B 108 -43.009 -15.094 -1.907 1.00 64.34 N ANISOU 2748 N LEU B 108 8293 6497 9657 -189 -2229 801 N ATOM 2749 CA LEU B 108 -42.643 -14.569 -3.218 1.00 61.23 C ANISOU 2749 CA LEU B 108 7979 6073 9211 -225 -2292 851 C ATOM 2750 C LEU B 108 -41.402 -15.242 -3.829 1.00 62.42 C ANISOU 2750 C LEU B 108 8155 6266 9297 -361 -2336 777 C ATOM 2751 O LEU B 108 -41.019 -14.947 -4.957 1.00 81.68 O ANISOU 2751 O LEU B 108 10664 8691 11681 -417 -2394 813 O ATOM 2752 CB LEU B 108 -42.425 -13.050 -3.136 1.00 76.54 C ANISOU 2752 CB LEU B 108 10025 7932 11125 -108 -2263 897 C ATOM 2753 CG LEU B 108 -42.797 -12.283 -1.856 1.00 71.35 C ANISOU 2753 CG LEU B 108 9377 7229 10504 44 -2171 898 C ATOM 2754 CD1 LEU B 108 -42.337 -10.831 -1.950 1.00 59.53 C ANISOU 2754 CD1 LEU B 108 8038 5621 8959 135 -2137 942 C ATOM 2755 CD2 LEU B 108 -44.289 -12.349 -1.533 1.00 48.79 C ANISOU 2755 CD2 LEU B 108 6438 4384 7716 177 -2145 978 C ATOM 2756 N TRP B 109 -40.791 -16.160 -3.091 1.00 55.04 N ANISOU 2756 N TRP B 109 7166 5386 8360 -398 -2309 687 N ATOM 2757 CA TRP B 109 -39.423 -16.598 -3.382 1.00 55.44 C ANISOU 2757 CA TRP B 109 7241 5483 8341 -455 -2324 625 C ATOM 2758 C TRP B 109 -39.255 -17.846 -4.260 1.00 48.55 C ANISOU 2758 C TRP B 109 6369 4666 7411 -505 -2312 620 C ATOM 2759 O TRP B 109 -38.160 -18.389 -4.372 1.00 30.93 O ANISOU 2759 O TRP B 109 4161 2483 5109 -487 -2249 580 O ATOM 2760 CB TRP B 109 -38.631 -16.717 -2.080 1.00 48.01 C ANISOU 2760 CB TRP B 109 6268 4575 7400 -412 -2263 557 C ATOM 2761 CG TRP B 109 -38.728 -15.477 -1.254 1.00 61.14 C ANISOU 2761 CG TRP B 109 7964 6191 9074 -336 -2217 572 C ATOM 2762 CD1 TRP B 109 -39.717 -15.161 -0.373 1.00 89.65 C ANISOU 2762 CD1 TRP B 109 11546 9770 12746 -265 -2172 591 C ATOM 2763 CD2 TRP B 109 -37.816 -14.372 -1.247 1.00 55.21 C ANISOU 2763 CD2 TRP B 109 7306 5411 8262 -317 -2204 579 C ATOM 2764 NE1 TRP B 109 -39.475 -13.932 0.193 1.00 81.59 N ANISOU 2764 NE1 TRP B 109 10599 8695 11707 -191 -2125 607 N ATOM 2765 CE2 TRP B 109 -38.314 -13.426 -0.327 1.00 53.52 C ANISOU 2765 CE2 TRP B 109 7126 5135 8073 -229 -2144 600 C ATOM 2766 CE3 TRP B 109 -36.623 -14.094 -1.919 1.00 69.72 C ANISOU 2766 CE3 TRP B 109 9214 7261 10015 -364 -2229 576 C ATOM 2767 CZ2 TRP B 109 -37.661 -12.224 -0.062 1.00 34.46 C ANISOU 2767 CZ2 TRP B 109 4832 2658 5602 -196 -2106 617 C ATOM 2768 CZ3 TRP B 109 -35.972 -12.899 -1.652 1.00 83.59 C ANISOU 2768 CZ3 TRP B 109 11082 8966 11713 -343 -2198 596 C ATOM 2769 CH2 TRP B 109 -36.493 -11.980 -0.731 1.00 63.12 C ANISOU 2769 CH2 TRP B 109 8539 6298 9145 -264 -2135 614 C ATOM 2770 N GLY B 110 -40.345 -18.339 -4.827 1.00 41.14 N ANISOU 2770 N GLY B 110 5417 3720 6496 -545 -2342 672 N ATOM 2771 CA GLY B 110 -40.263 -19.479 -5.719 1.00 57.56 C ANISOU 2771 CA GLY B 110 7529 5850 8492 -578 -2306 682 C ATOM 2772 C GLY B 110 -40.285 -20.743 -4.891 1.00 78.68 C ANISOU 2772 C GLY B 110 10171 8562 11160 -537 -2235 635 C ATOM 2773 O GLY B 110 -39.761 -20.761 -3.779 1.00 91.15 O ANISOU 2773 O GLY B 110 11718 10147 12766 -482 -2191 580 O ATOM 2774 N SER B 111 -40.863 -21.811 -5.428 1.00 77.09 N ANISOU 2774 N SER B 111 9577 9655 10058 241 356 -40 N ATOM 2775 CA SER B 111 -41.070 -23.000 -4.614 1.00 83.32 C ANISOU 2775 CA SER B 111 10366 10436 10856 217 347 -55 C ATOM 2776 C SER B 111 -39.815 -23.862 -4.482 1.00 59.67 C ANISOU 2776 C SER B 111 7397 7440 7835 210 339 -20 C ATOM 2777 O SER B 111 -39.682 -24.622 -3.528 1.00 38.29 O ANISOU 2777 O SER B 111 4694 4714 5141 185 339 -21 O ATOM 2778 CB SER B 111 -42.291 -23.804 -5.078 1.00 76.76 C ANISOU 2778 CB SER B 111 9511 9632 10021 234 333 -95 C ATOM 2779 OG SER B 111 -43.408 -23.560 -4.225 1.00 28.50 O ANISOU 2779 OG SER B 111 3379 3498 3951 213 345 -126 O ATOM 2780 N PHE B 112 -38.891 -23.736 -5.426 1.00 35.57 N ANISOU 2780 N PHE B 112 4362 4406 4746 235 336 13 N ATOM 2781 CA PHE B 112 -37.607 -24.400 -5.286 1.00 48.77 C ANISOU 2781 CA PHE B 112 6062 6078 6389 232 332 53 C ATOM 2782 C PHE B 112 -37.014 -23.900 -3.977 1.00 34.62 C ANISOU 2782 C PHE B 112 4281 4248 4626 199 347 69 C ATOM 2783 O PHE B 112 -36.722 -24.664 -3.034 1.00 45.48 O ANISOU 2783 O PHE B 112 5662 5611 6006 180 344 70 O ATOM 2784 CB PHE B 112 -36.716 -23.998 -6.455 1.00 74.18 C ANISOU 2784 CB PHE B 112 9301 9319 9566 264 334 96 C ATOM 2785 CG PHE B 112 -35.416 -24.733 -6.508 1.00 98.40 C ANISOU 2785 CG PHE B 112 12400 12398 12590 274 329 142 C ATOM 2786 CD1 PHE B 112 -35.310 -25.926 -7.204 1.00114.24 C ANISOU 2786 CD1 PHE B 112 14411 14438 14556 297 311 142 C ATOM 2787 CD2 PHE B 112 -34.294 -24.231 -5.870 1.00 86.17 C ANISOU 2787 CD2 PHE B 112 10874 10828 11039 262 342 183 C ATOM 2788 CE1 PHE B 112 -34.110 -26.608 -7.262 1.00112.10 C ANISOU 2788 CE1 PHE B 112 14171 14185 14237 313 306 188 C ATOM 2789 CE2 PHE B 112 -33.090 -24.908 -5.923 1.00 77.45 C ANISOU 2789 CE2 PHE B 112 9798 9741 9888 277 336 227 C ATOM 2790 CZ PHE B 112 -32.998 -26.098 -6.622 1.00 93.45 C ANISOU 2790 CZ PHE B 112 11834 11806 11868 304 318 232 C ATOM 2791 N LEU B 113 -36.877 -22.585 -3.921 1.00 36.43 N ANISOU 2791 N LEU B 113 4509 4458 4875 195 364 78 N ATOM 2792 CA LEU B 113 -36.434 -21.910 -2.718 1.00 56.73 C ANISOU 2792 CA LEU B 113 7082 6994 7479 165 378 81 C ATOM 2793 C LEU B 113 -37.367 -22.196 -1.534 1.00 77.00 C ANISOU 2793 C LEU B 113 9629 9543 10084 137 377 39 C ATOM 2794 O LEU B 113 -36.920 -22.257 -0.397 1.00 81.67 O ANISOU 2794 O LEU B 113 10225 10115 10691 115 381 39 O ATOM 2795 CB LEU B 113 -36.328 -20.409 -2.985 1.00 32.19 C ANISOU 2795 CB LEU B 113 3970 3869 4393 167 398 89 C ATOM 2796 CG LEU B 113 -35.913 -19.523 -1.818 1.00 23.07 C ANISOU 2796 CG LEU B 113 2809 2678 3278 138 413 82 C ATOM 2797 CD1 LEU B 113 -34.699 -20.082 -1.105 1.00 54.85 C ANISOU 2797 CD1 LEU B 113 6854 6699 7288 127 407 105 C ATOM 2798 CD2 LEU B 113 -35.619 -18.158 -2.339 1.00 11.73 C ANISOU 2798 CD2 LEU B 113 1371 1225 1859 145 436 98 C ATOM 2799 N CYS B 114 -38.658 -22.365 -1.804 1.00 70.65 N ANISOU 2799 N CYS B 114 8803 8749 9292 142 374 4 N ATOM 2800 CA CYS B 114 -39.614 -22.709 -0.762 1.00 5.98 C ANISOU 2800 CA CYS B 114 595 543 1136 119 376 -33 C ATOM 2801 C CYS B 114 -39.121 -23.955 -0.034 1.00 45.29 C ANISOU 2801 C CYS B 114 5586 5517 6105 105 369 -22 C ATOM 2802 O CYS B 114 -38.926 -23.942 1.188 1.00 78.62 O ANISOU 2802 O CYS B 114 9808 9718 10347 83 376 -27 O ATOM 2803 CB CYS B 114 -40.990 -22.939 -1.384 1.00 6.29 C ANISOU 2803 CB CYS B 114 610 600 1179 133 371 -67 C ATOM 2804 SG CYS B 114 -42.300 -23.422 -0.256 1.00 74.61 S ANISOU 2804 SG CYS B 114 9238 9236 9873 109 377 -112 S ATOM 2805 N GLU B 115 -38.887 -25.019 -0.799 1.00 20.95 N ANISOU 2805 N GLU B 115 2514 2457 2990 122 355 -8 N ATOM 2806 CA GLU B 115 -38.315 -26.258 -0.270 1.00 43.50 C ANISOU 2806 CA GLU B 115 5384 5311 5832 116 350 8 C ATOM 2807 C GLU B 115 -37.035 -25.964 0.508 1.00 65.11 C ANISOU 2807 C GLU B 115 8142 8036 8559 108 355 40 C ATOM 2808 O GLU B 115 -36.915 -26.341 1.682 1.00 30.49 O ANISOU 2808 O GLU B 115 3760 3635 4190 91 360 37 O ATOM 2809 CB GLU B 115 -38.009 -27.258 -1.398 1.00 50.31 C ANISOU 2809 CB GLU B 115 6256 6206 6653 143 335 21 C ATOM 2810 CG GLU B 115 -39.204 -28.064 -1.900 1.00 79.88 C ANISOU 2810 CG GLU B 115 9978 9964 10408 149 328 -16 C ATOM 2811 CD GLU B 115 -38.891 -28.860 -3.167 1.00 92.50 C ANISOU 2811 CD GLU B 115 11579 11602 11963 183 310 -12 C ATOM 2812 OE1 GLU B 115 -37.874 -28.563 -3.833 1.00 86.72 O ANISOU 2812 OE1 GLU B 115 10865 10890 11194 205 304 18 O ATOM 2813 OE2 GLU B 115 -39.667 -29.782 -3.500 1.00 96.24 O ANISOU 2813 OE2 GLU B 115 12036 12089 12443 189 302 -42 O ATOM 2814 N LEU B 116 -36.081 -25.283 -0.131 1.00 83.52 N ANISOU 2814 N LEU B 116 10490 10378 10867 124 354 69 N ATOM 2815 CA LEU B 116 -34.801 -25.036 0.543 1.00 52.22 C ANISOU 2815 CA LEU B 116 6545 6406 6891 120 357 99 C ATOM 2816 C LEU B 116 -34.988 -24.420 1.922 1.00 32.05 C ANISOU 2816 C LEU B 116 3976 3824 4376 94 367 74 C ATOM 2817 O LEU B 116 -34.564 -24.984 2.941 1.00 14.88 O ANISOU 2817 O LEU B 116 1808 1646 2199 87 366 77 O ATOM 2818 CB LEU B 116 -33.902 -24.133 -0.298 1.00 29.87 C ANISOU 2818 CB LEU B 116 3727 3583 4040 138 361 130 C ATOM 2819 CG LEU B 116 -32.981 -24.937 -1.215 1.00 52.05 C ANISOU 2819 CG LEU B 116 6562 6423 6792 168 350 173 C ATOM 2820 CD1 LEU B 116 -33.767 -25.508 -2.391 1.00 54.49 C ANISOU 2820 CD1 LEU B 116 6863 6757 7082 189 341 161 C ATOM 2821 CD2 LEU B 116 -31.800 -24.101 -1.696 1.00 39.40 C ANISOU 2821 CD2 LEU B 116 4979 4825 5167 184 358 214 C ATOM 2822 N TRP B 117 -35.654 -23.273 1.935 1.00 29.86 N ANISOU 2822 N TRP B 117 3680 3533 4132 84 377 48 N ATOM 2823 CA TRP B 117 -35.981 -22.544 3.151 1.00 51.75 C ANISOU 2823 CA TRP B 117 6434 6285 6943 63 387 16 C ATOM 2824 C TRP B 117 -36.633 -23.416 4.228 1.00 40.63 C ANISOU 2824 C TRP B 117 5016 4873 5547 52 386 -7 C ATOM 2825 O TRP B 117 -36.235 -23.371 5.376 1.00 5.40 O ANISOU 2825 O TRP B 117 553 406 1092 44 388 -15 O ATOM 2826 CB TRP B 117 -36.884 -21.357 2.810 1.00 41.14 C ANISOU 2826 CB TRP B 117 5067 4932 5631 60 398 -12 C ATOM 2827 CG TRP B 117 -37.296 -20.537 3.998 1.00 38.91 C ANISOU 2827 CG TRP B 117 4763 4635 5387 43 408 -50 C ATOM 2828 CD1 TRP B 117 -36.655 -19.443 4.495 1.00 28.20 C ANISOU 2828 CD1 TRP B 117 3400 3265 4050 36 417 -57 C ATOM 2829 CD2 TRP B 117 -38.450 -20.739 4.831 1.00 53.24 C ANISOU 2829 CD2 TRP B 117 6556 6448 7225 36 412 -90 C ATOM 2830 NE1 TRP B 117 -37.331 -18.953 5.589 1.00 44.23 N ANISOU 2830 NE1 TRP B 117 5404 5290 6110 26 424 -101 N ATOM 2831 CE2 TRP B 117 -38.438 -19.729 5.813 1.00 47.16 C ANISOU 2831 CE2 TRP B 117 5767 5670 6481 28 422 -120 C ATOM 2832 CE3 TRP B 117 -39.489 -21.675 4.842 1.00 54.49 C ANISOU 2832 CE3 TRP B 117 6707 6613 7384 37 409 -104 C ATOM 2833 CZ2 TRP B 117 -39.422 -19.628 6.792 1.00 32.63 C ANISOU 2833 CZ2 TRP B 117 3903 3833 4662 26 428 -161 C ATOM 2834 CZ3 TRP B 117 -40.466 -21.571 5.817 1.00 44.28 C ANISOU 2834 CZ3 TRP B 117 5391 5319 6115 31 418 -143 C ATOM 2835 CH2 TRP B 117 -40.425 -20.554 6.777 1.00 30.82 C ANISOU 2835 CH2 TRP B 117 3670 3611 4431 29 427 -171 C ATOM 2836 N THR B 118 -37.643 -24.198 3.863 1.00 5.45 N ANISOU 2836 N THR B 118 554 422 1095 53 384 -19 N ATOM 2837 CA THR B 118 -38.296 -25.049 4.855 1.00 49.39 C ANISOU 2837 CA THR B 118 6111 5980 6675 42 388 -38 C ATOM 2838 C THR B 118 -37.337 -26.095 5.431 1.00 73.57 C ANISOU 2838 C THR B 118 9196 9046 9713 47 384 -8 C ATOM 2839 O THR B 118 -37.313 -26.334 6.645 1.00107.24 O ANISOU 2839 O THR B 118 13456 13304 13985 42 391 -16 O ATOM 2840 CB THR B 118 -39.558 -25.739 4.325 1.00 46.67 C ANISOU 2840 CB THR B 118 5752 5637 6343 41 389 -58 C ATOM 2841 OG1 THR B 118 -39.337 -26.191 2.987 1.00 64.24 O ANISOU 2841 OG1 THR B 118 7988 7879 8541 57 378 -38 O ATOM 2842 CG2 THR B 118 -40.749 -24.789 4.356 1.00 23.68 C ANISOU 2842 CG2 THR B 118 2813 2722 3463 37 397 -99 C ATOM 2843 N SER B 119 -36.543 -26.720 4.568 1.00 48.27 N ANISOU 2843 N SER B 119 6012 5855 6472 62 374 28 N ATOM 2844 CA SER B 119 -35.637 -27.784 5.009 1.00 25.01 C ANISOU 2844 CA SER B 119 3088 2917 3498 72 371 59 C ATOM 2845 C SER B 119 -34.505 -27.267 5.889 1.00 30.04 C ANISOU 2845 C SER B 119 3734 3556 4122 76 370 72 C ATOM 2846 O SER B 119 -33.918 -28.012 6.681 1.00 4.65 O ANISOU 2846 O SER B 119 530 346 889 84 370 89 O ATOM 2847 CB SER B 119 -35.064 -28.498 3.797 1.00 25.23 C ANISOU 2847 CB SER B 119 3134 2965 3486 92 360 91 C ATOM 2848 OG SER B 119 -36.114 -28.903 2.941 1.00 26.46 O ANISOU 2848 OG SER B 119 3276 3124 3654 92 359 70 O ATOM 2849 N LEU B 120 -34.201 -25.983 5.715 1.00 47.48 N ANISOU 2849 N LEU B 120 5936 5764 6341 72 370 63 N ATOM 2850 CA LEU B 120 -33.257 -25.275 6.576 1.00 36.75 C ANISOU 2850 CA LEU B 120 4577 4407 4980 73 370 61 C ATOM 2851 C LEU B 120 -33.901 -24.848 7.898 1.00 5.06 C ANISOU 2851 C LEU B 120 540 385 998 61 378 20 C ATOM 2852 O LEU B 120 -33.281 -24.962 8.960 1.00 26.31 O ANISOU 2852 O LEU B 120 3232 3087 3679 69 376 16 O ATOM 2853 CB LEU B 120 -32.666 -24.079 5.834 1.00 8.04 C ANISOU 2853 CB LEU B 120 941 768 1346 74 370 67 C ATOM 2854 CG LEU B 120 -31.908 -24.483 4.564 1.00 16.24 C ANISOU 2854 CG LEU B 120 2003 1822 2344 94 363 112 C ATOM 2855 CD1 LEU B 120 -31.974 -23.395 3.509 1.00 56.51 C ANISOU 2855 CD1 LEU B 120 7101 6916 7456 94 370 115 C ATOM 2856 CD2 LEU B 120 -30.478 -24.847 4.872 1.00 4.37 C ANISOU 2856 CD2 LEU B 120 520 336 803 112 356 145 C ATOM 2857 N ASP B 121 -35.146 -24.379 7.827 1.00 5.32 N ANISOU 2857 N ASP B 121 552 405 1064 48 386 -13 N ATOM 2858 CA ASP B 121 -35.986 -24.167 9.018 1.00 61.77 C ANISOU 2858 CA ASP B 121 7678 7552 8239 42 396 -53 C ATOM 2859 C ASP B 121 -36.083 -25.386 9.927 1.00 45.87 C ANISOU 2859 C ASP B 121 5671 5545 6213 50 399 -46 C ATOM 2860 O ASP B 121 -36.205 -25.244 11.143 1.00 8.53 O ANISOU 2860 O ASP B 121 928 824 1488 57 405 -69 O ATOM 2861 CB ASP B 121 -37.412 -23.742 8.641 1.00 69.30 C ANISOU 2861 CB ASP B 121 8611 8496 9225 32 405 -84 C ATOM 2862 CG ASP B 121 -38.378 -23.823 9.825 1.00 49.22 C ANISOU 2862 CG ASP B 121 6046 5956 6701 32 416 -121 C ATOM 2863 OD1 ASP B 121 -37.958 -23.468 10.949 1.00 6.54 O ANISOU 2863 OD1 ASP B 121 632 561 1292 40 418 -137 O ATOM 2864 OD2 ASP B 121 -39.545 -24.249 9.633 1.00 40.60 O ANISOU 2864 OD2 ASP B 121 4943 4859 5625 29 424 -136 O ATOM 2865 N VAL B 122 -36.107 -26.577 9.338 1.00 5.46 N ANISOU 2865 N VAL B 122 571 424 1080 53 397 -16 N ATOM 2866 CA VAL B 122 -36.061 -27.795 10.137 1.00 9.68 C ANISOU 2866 CA VAL B 122 1115 960 1602 63 404 -1 C ATOM 2867 C VAL B 122 -34.641 -28.228 10.530 1.00 58.94 C ANISOU 2867 C VAL B 122 7376 7216 7802 83 395 33 C ATOM 2868 O VAL B 122 -34.395 -28.659 11.674 1.00 5.38 O ANISOU 2868 O VAL B 122 593 443 1009 97 400 34 O ATOM 2869 CB VAL B 122 -36.767 -28.924 9.432 1.00 5.42 C ANISOU 2869 CB VAL B 122 583 408 1070 57 410 13 C ATOM 2870 CG1 VAL B 122 -37.040 -30.050 10.413 1.00 5.58 C ANISOU 2870 CG1 VAL B 122 607 421 1092 64 425 20 C ATOM 2871 CG2 VAL B 122 -38.045 -28.401 8.836 1.00 5.63 C ANISOU 2871 CG2 VAL B 122 587 424 1130 41 414 -21 C ATOM 2872 N LEU B 123 -33.712 -28.123 9.578 1.00 31.53 N ANISOU 2872 N LEU B 123 3922 3752 4306 88 382 62 N ATOM 2873 CA LEU B 123 -32.329 -28.526 9.822 1.00 20.14 C ANISOU 2873 CA LEU B 123 2501 2330 2823 110 373 96 C ATOM 2874 C LEU B 123 -31.738 -27.831 11.032 1.00 13.69 C ANISOU 2874 C LEU B 123 1670 1528 2002 119 370 73 C ATOM 2875 O LEU B 123 -31.155 -28.480 11.897 1.00 23.98 O ANISOU 2875 O LEU B 123 2981 2848 3281 139 369 87 O ATOM 2876 CB LEU B 123 -31.436 -28.254 8.619 1.00 12.49 C ANISOU 2876 CB LEU B 123 1548 1370 1827 118 361 125 C ATOM 2877 CG LEU B 123 -29.975 -28.326 9.075 1.00 30.44 C ANISOU 2877 CG LEU B 123 3836 3669 4061 141 351 150 C ATOM 2878 CD1 LEU B 123 -29.712 -29.681 9.698 1.00 4.42 C ANISOU 2878 CD1 LEU B 123 558 383 737 161 354 179 C ATOM 2879 CD2 LEU B 123 -28.992 -28.051 7.948 1.00 16.69 C ANISOU 2879 CD2 LEU B 123 2113 1941 2289 154 342 183 C ATOM 2880 N CYS B 124 -31.872 -26.509 11.083 1.00 13.69 N ANISOU 2880 N CYS B 124 1649 1525 2027 107 369 39 N ATOM 2881 CA CYS B 124 -31.403 -25.759 12.244 1.00 45.47 C ANISOU 2881 CA CYS B 124 5654 5569 6052 116 366 6 C ATOM 2882 C CYS B 124 -31.935 -26.376 13.539 1.00 52.74 C ANISOU 2882 C CYS B 124 6566 6503 6971 129 375 -11 C ATOM 2883 O CYS B 124 -31.253 -26.366 14.576 1.00 76.01 O ANISOU 2883 O CYS B 124 9505 9478 9896 151 370 -22 O ATOM 2884 CB CYS B 124 -31.831 -24.298 12.154 1.00 60.51 C ANISOU 2884 CB CYS B 124 7535 7462 7993 97 370 -34 C ATOM 2885 SG CYS B 124 -30.756 -23.262 11.149 1.00 30.05 S ANISOU 2885 SG CYS B 124 3683 3598 4137 90 363 -21 S ATOM 2886 N VAL B 125 -33.139 -26.943 13.463 1.00 24.72 N ANISOU 2886 N VAL B 125 3015 2934 3442 119 388 -13 N ATOM 2887 CA VAL B 125 -33.783 -27.550 14.624 1.00 26.04 C ANISOU 2887 CA VAL B 125 3173 3111 3611 133 402 -26 C ATOM 2888 C VAL B 125 -33.140 -28.874 15.000 1.00 28.78 C ANISOU 2888 C VAL B 125 3543 3466 3926 154 404 15 C ATOM 2889 O VAL B 125 -32.649 -29.013 16.126 1.00 32.31 O ANISOU 2889 O VAL B 125 3984 3942 4351 180 404 8 O ATOM 2890 CB VAL B 125 -35.282 -27.744 14.434 1.00 6.21 C ANISOU 2890 CB VAL B 125 651 576 1134 116 419 -43 C ATOM 2891 CG1 VAL B 125 -35.910 -28.241 15.728 1.00 6.64 C ANISOU 2891 CG1 VAL B 125 692 643 1187 136 437 -59 C ATOM 2892 CG2 VAL B 125 -35.912 -26.438 14.024 1.00 54.53 C ANISOU 2892 CG2 VAL B 125 6748 6688 7283 98 418 -81 C ATOM 2893 N THR B 126 -33.164 -29.854 14.092 1.00 24.04 N ANISOU 2893 N THR B 126 2968 2844 3322 147 407 56 N ATOM 2894 CA THR B 126 -32.543 -31.154 14.407 1.00 40.53 C ANISOU 2894 CA THR B 126 5082 4938 5380 169 412 102 C ATOM 2895 C THR B 126 -31.074 -31.007 14.836 1.00 39.82 C ANISOU 2895 C THR B 126 5001 4881 5247 195 395 118 C ATOM 2896 O THR B 126 -30.574 -31.772 15.662 1.00 5.58 O ANISOU 2896 O THR B 126 676 559 884 222 400 141 O ATOM 2897 CB THR B 126 -32.678 -32.183 13.263 1.00 30.48 C ANISOU 2897 CB THR B 126 3833 3642 4105 161 416 143 C ATOM 2898 OG1 THR B 126 -33.970 -32.068 12.657 1.00 46.78 O ANISOU 2898 OG1 THR B 126 5883 5680 6211 133 426 118 O ATOM 2899 CG2 THR B 126 -32.546 -33.576 13.802 1.00 5.41 C ANISOU 2899 CG2 THR B 126 679 462 914 180 433 182 C ATOM 2900 N ALA B 127 -30.402 -29.998 14.285 1.00 57.26 N ANISOU 2900 N ALA B 127 7204 7100 7451 189 377 105 N ATOM 2901 CA ALA B 127 -29.043 -29.651 14.699 1.00 43.13 C ANISOU 2901 CA ALA B 127 5415 5343 5628 211 361 109 C ATOM 2902 C ALA B 127 -29.025 -29.157 16.134 1.00 29.96 C ANISOU 2902 C ALA B 127 3719 3704 3962 226 361 63 C ATOM 2903 O ALA B 127 -28.185 -29.578 16.925 1.00 5.73 O ANISOU 2903 O ALA B 127 654 664 861 254 356 74 O ATOM 2904 CB ALA B 127 -28.445 -28.595 13.778 1.00 36.06 C ANISOU 2904 CB ALA B 127 4517 4449 4736 198 347 101 C ATOM 2905 N SER B 128 -29.942 -28.242 16.452 1.00 54.58 N ANISOU 2905 N SER B 128 6807 6819 7112 212 366 12 N ATOM 2906 CA SER B 128 -30.099 -27.729 17.822 1.00 53.02 C ANISOU 2906 CA SER B 128 6577 6657 6912 232 368 -38 C ATOM 2907 C SER B 128 -30.385 -28.805 18.877 1.00 44.10 C ANISOU 2907 C SER B 128 5450 5540 5767 257 382 -27 C ATOM 2908 O SER B 128 -29.570 -29.027 19.784 1.00 28.20 O ANISOU 2908 O SER B 128 3429 3562 3724 285 377 -32 O ATOM 2909 CB SER B 128 -31.163 -26.629 17.888 1.00 12.30 C ANISOU 2909 CB SER B 128 1393 1492 1789 216 376 -84 C ATOM 2910 OG SER B 128 -30.613 -25.372 17.540 1.00 20.75 O ANISOU 2910 OG SER B 128 2451 2565 2868 206 364 -107 O ATOM 2911 N ILE B 129 -31.535 -29.466 18.777 1.00 6.67 N ANISOU 2911 N ILE B 129 717 770 1046 247 404 -13 N ATOM 2912 CA ILE B 129 -31.821 -30.540 19.714 1.00 48.06 C ANISOU 2912 CA ILE B 129 5965 6018 6276 271 423 6 C ATOM 2913 C ILE B 129 -30.692 -31.578 19.720 1.00 68.72 C ANISOU 2913 C ILE B 129 8616 8638 8857 292 420 65 C ATOM 2914 O ILE B 129 -30.095 -31.815 20.763 1.00 7.02 O ANISOU 2914 O ILE B 129 797 857 1015 324 420 66 O ATOM 2915 CB ILE B 129 -33.187 -31.215 19.454 1.00 28.24 C ANISOU 2915 CB ILE B 129 3462 3469 3798 256 450 18 C ATOM 2916 CG1 ILE B 129 -33.476 -32.284 20.514 1.00 34.57 C ANISOU 2916 CG1 ILE B 129 4270 4276 4590 284 476 39 C ATOM 2917 CG2 ILE B 129 -33.231 -31.825 18.080 1.00 12.83 C ANISOU 2917 CG2 ILE B 129 1541 1474 1860 229 450 63 C ATOM 2918 CD1 ILE B 129 -34.070 -31.736 21.823 1.00 19.49 C ANISOU 2918 CD1 ILE B 129 2322 2407 2677 308 487 -16 C ATOM 2919 N GLU B 130 -30.361 -32.156 18.563 1.00 62.11 N ANISOU 2919 N GLU B 130 7811 7772 8015 279 416 116 N ATOM 2920 CA GLU B 130 -29.382 -33.257 18.522 1.00 58.95 C ANISOU 2920 CA GLU B 130 7448 7377 7572 305 415 181 C ATOM 2921 C GLU B 130 -27.994 -32.914 19.084 1.00 50.75 C ANISOU 2921 C GLU B 130 6408 6384 6490 335 393 183 C ATOM 2922 O GLU B 130 -27.422 -33.686 19.854 1.00 9.44 O ANISOU 2922 O GLU B 130 1192 1173 1220 371 397 218 O ATOM 2923 CB GLU B 130 -29.289 -33.881 17.124 1.00 22.86 C ANISOU 2923 CB GLU B 130 2909 2778 3000 290 413 227 C ATOM 2924 CG GLU B 130 -30.031 -35.214 17.018 1.00 43.08 C ANISOU 2924 CG GLU B 130 5491 5306 5572 290 441 267 C ATOM 2925 CD GLU B 130 -30.455 -35.550 15.603 1.00 62.02 C ANISOU 2925 CD GLU B 130 7901 7675 7990 263 442 281 C ATOM 2926 OE1 GLU B 130 -30.242 -34.704 14.713 1.00 65.60 O ANISOU 2926 OE1 GLU B 130 8347 8133 8446 245 422 262 O ATOM 2927 OE2 GLU B 130 -31.002 -36.654 15.380 1.00 9.16 O ANISOU 2927 OE2 GLU B 130 1211 965 1305 257 452 289 O ATOM 2928 N THR B 131 -27.459 -31.762 18.695 1.00 51.12 N ANISOU 2928 N THR B 131 6436 6446 6542 321 372 145 N ATOM 2929 CA THR B 131 -26.255 -31.231 19.322 1.00 28.74 C ANISOU 2929 CA THR B 131 3588 3654 3677 343 353 128 C ATOM 2930 C THR B 131 -26.430 -31.151 20.834 1.00 37.66 C ANISOU 2930 C THR B 131 4689 4815 4804 366 361 90 C ATOM 2931 O THR B 131 -25.555 -31.586 21.584 1.00 58.73 O ANISOU 2931 O THR B 131 7366 7517 7430 402 356 114 O ATOM 2932 CB THR B 131 -25.919 -29.844 18.775 1.00 9.36 C ANISOU 2932 CB THR B 131 1106 1204 1247 318 336 77 C ATOM 2933 OG1 THR B 131 -25.128 -29.993 17.594 1.00 37.64 O ANISOU 2933 OG1 THR B 131 4718 4778 4807 316 324 124 O ATOM 2934 CG2 THR B 131 -25.150 -29.042 19.790 1.00 6.40 C ANISOU 2934 CG2 THR B 131 695 870 866 333 326 23 C ATOM 2935 N LEU B 132 -27.560 -30.602 21.279 1.00 33.26 N ANISOU 2935 N LEU B 132 4099 4253 4286 350 374 33 N ATOM 2936 CA LEU B 132 -27.848 -30.518 22.704 1.00 7.52 C ANISOU 2936 CA LEU B 132 809 1026 1024 373 387 -8 C ATOM 2937 C LEU B 132 -27.743 -31.874 23.369 1.00 35.60 C ANISOU 2937 C LEU B 132 4396 4585 4544 410 403 56 C ATOM 2938 O LEU B 132 -26.994 -32.038 24.333 1.00 70.47 O ANISOU 2938 O LEU B 132 8809 9042 8925 445 400 61 O ATOM 2939 CB LEU B 132 -29.243 -29.966 22.933 1.00 16.18 C ANISOU 2939 CB LEU B 132 1872 2118 2156 358 400 -64 C ATOM 2940 CG LEU B 132 -29.419 -28.457 22.816 1.00 39.02 C ANISOU 2940 CG LEU B 132 4723 5035 5069 343 383 -141 C ATOM 2941 CD1 LEU B 132 -30.884 -28.087 22.904 1.00 66.56 C ANISOU 2941 CD1 LEU B 132 8195 8522 8573 343 396 -166 C ATOM 2942 CD2 LEU B 132 -28.646 -27.770 23.905 1.00 21.11 C ANISOU 2942 CD2 LEU B 132 2411 2814 2796 358 377 -206 C ATOM 2943 N CYS B 133 -28.493 -32.849 22.856 1.00 7.58 N ANISOU 2943 N CYS B 133 879 996 1005 404 423 107 N ATOM 2944 CA CYS B 133 -28.475 -34.212 23.398 1.00 40.69 C ANISOU 2944 CA CYS B 133 5105 5185 5170 439 444 173 C ATOM 2945 C CYS B 133 -27.053 -34.764 23.436 1.00 55.50 C ANISOU 2945 C CYS B 133 7011 7089 6986 475 425 231 C ATOM 2946 O CYS B 133 -26.694 -35.518 24.342 1.00 30.31 O ANISOU 2946 O CYS B 133 3835 3923 3757 519 434 269 O ATOM 2947 CB CYS B 133 -29.365 -35.157 22.587 1.00 7.59 C ANISOU 2947 CB CYS B 133 943 937 1005 419 467 218 C ATOM 2948 SG CYS B 133 -31.004 -34.516 22.260 1.00130.40 S ANISOU 2948 SG CYS B 133 16465 16459 16623 377 484 158 S ATOM 2949 N VAL B 134 -26.239 -34.398 22.450 1.00 71.20 N ANISOU 2949 N VAL B 134 9012 9078 8964 460 399 240 N ATOM 2950 CA VAL B 134 -24.829 -34.739 22.536 1.00 48.07 C ANISOU 2950 CA VAL B 134 6104 6188 5972 498 377 285 C ATOM 2951 C VAL B 134 -24.235 -34.094 23.795 1.00 15.88 C ANISOU 2951 C VAL B 134 1994 2168 1872 526 364 241 C ATOM 2952 O VAL B 134 -23.495 -34.743 24.519 1.00 13.78 O ANISOU 2952 O VAL B 134 1744 1941 1551 574 358 282 O ATOM 2953 CB VAL B 134 -24.029 -34.348 21.272 1.00 34.89 C ANISOU 2953 CB VAL B 134 4448 4517 4292 480 352 297 C ATOM 2954 CG1 VAL B 134 -22.833 -35.274 21.109 1.00 6.71 C ANISOU 2954 CG1 VAL B 134 914 978 658 518 335 359 C ATOM 2955 CG2 VAL B 134 -24.899 -34.429 20.040 1.00 6.38 C ANISOU 2955 CG2 VAL B 134 848 853 724 438 364 301 C ATOM 2956 N ILE B 135 -24.568 -32.832 24.072 1.00 29.65 N ANISOU 2956 N ILE B 135 3691 3917 3657 497 361 157 N ATOM 2957 CA ILE B 135 -24.019 -32.181 25.267 1.00 17.37 C ANISOU 2957 CA ILE B 135 2100 2416 2085 521 352 109 C ATOM 2958 C ILE B 135 -24.385 -32.954 26.519 1.00 43.96 C ANISOU 2958 C ILE B 135 5469 5809 5426 563 372 129 C ATOM 2959 O ILE B 135 -23.515 -33.297 27.315 1.00 59.66 O ANISOU 2959 O ILE B 135 7462 7849 7357 610 359 154 O ATOM 2960 CB ILE B 135 -24.505 -30.728 25.499 1.00 17.74 C ANISOU 2960 CB ILE B 135 2090 2459 2190 483 357 9 C ATOM 2961 CG1 ILE B 135 -24.372 -29.858 24.259 1.00 55.21 C ANISOU 2961 CG1 ILE B 135 6829 7173 6974 438 345 -18 C ATOM 2962 CG2 ILE B 135 -23.685 -30.097 26.591 1.00 21.10 C ANISOU 2962 CG2 ILE B 135 2485 2939 2593 507 348 -32 C ATOM 2963 CD1 ILE B 135 -24.302 -28.380 24.593 1.00 8.14 C ANISOU 2963 CD1 ILE B 135 816 1216 1061 411 349 -108 C ATOM 2964 N ALA B 136 -25.680 -33.213 26.693 1.00 33.63 N ANISOU 2964 N ALA B 136 4155 4468 4154 550 403 118 N ATOM 2965 CA ALA B 136 -26.176 -33.868 27.905 1.00 28.77 C ANISOU 2965 CA ALA B 136 3536 3874 3520 590 428 132 C ATOM 2966 C ALA B 136 -25.684 -35.309 28.019 1.00 55.24 C ANISOU 2966 C ALA B 136 6939 7229 6819 637 433 231 C ATOM 2967 O ALA B 136 -25.609 -35.862 29.115 1.00 58.85 O ANISOU 2967 O ALA B 136 7398 7722 7240 685 446 255 O ATOM 2968 CB ALA B 136 -27.691 -33.814 27.964 1.00 9.67 C ANISOU 2968 CB ALA B 136 1100 1421 1154 565 461 99 C ATOM 2969 N ILE B 137 -25.352 -35.915 26.884 1.00 51.97 N ANISOU 2969 N ILE B 137 6566 6779 6401 625 426 288 N ATOM 2970 CA ILE B 137 -24.763 -37.249 26.875 1.00 49.27 C ANISOU 2970 CA ILE B 137 6273 6439 6008 669 431 382 C ATOM 2971 C ILE B 137 -23.259 -37.183 27.186 1.00 85.45 C ANISOU 2971 C ILE B 137 10862 11087 10520 712 395 403 C ATOM 2972 O ILE B 137 -22.658 -38.178 27.593 1.00110.71 O ANISOU 2972 O ILE B 137 14085 14307 13671 755 395 461 O ATOM 2973 CB ILE B 137 -24.976 -37.943 25.515 1.00 8.51 C ANISOU 2973 CB ILE B 137 1151 1218 866 640 440 432 C ATOM 2974 CG1 ILE B 137 -25.227 -39.432 25.705 1.00 8.73 C ANISOU 2974 CG1 ILE B 137 1203 1219 894 652 465 479 C ATOM 2975 CG2 ILE B 137 -23.778 -37.738 24.610 1.00 20.54 C ANISOU 2975 CG2 ILE B 137 2680 2760 2364 626 400 431 C ATOM 2976 CD1 ILE B 137 -25.514 -40.177 24.405 1.00 37.34 C ANISOU 2976 CD1 ILE B 137 4833 4793 4563 593 460 465 C ATOM 2977 N ASP B 138 -22.659 -36.006 26.998 1.00 78.49 N ANISOU 2977 N ASP B 138 9948 10234 9642 690 363 343 N ATOM 2978 CA ASP B 138 -21.241 -35.789 27.300 1.00 53.16 C ANISOU 2978 CA ASP B 138 6737 7092 6370 727 327 350 C ATOM 2979 C ASP B 138 -21.024 -35.620 28.793 1.00 55.95 C ANISOU 2979 C ASP B 138 7059 7509 6689 771 323 324 C ATOM 2980 O ASP B 138 -20.088 -36.171 29.366 1.00 54.38 O ANISOU 2980 O ASP B 138 6874 7368 6420 828 306 368 O ATOM 2981 CB ASP B 138 -20.721 -34.534 26.593 1.00 57.34 C ANISOU 2981 CB ASP B 138 7239 7624 6923 685 300 288 C ATOM 2982 CG ASP B 138 -19.441 -34.005 27.218 1.00 86.79 C ANISOU 2982 CG ASP B 138 10946 11430 10602 717 265 265 C ATOM 2983 OD1 ASP B 138 -18.494 -34.802 27.375 1.00115.17 O ANISOU 2983 OD1 ASP B 138 14567 15068 14123 769 247 328 O ATOM 2984 OD2 ASP B 138 -19.380 -32.803 27.567 1.00 72.12 O ANISOU 2984 OD2 ASP B 138 9041 9587 8774 693 257 184 O ATOM 2985 N ARG B 139 -21.920 -34.867 29.417 1.00 53.53 N ANISOU 2985 N ARG B 139 6711 7197 6430 748 341 252 N ATOM 2986 CA ARG B 139 -21.739 -34.429 30.791 1.00 43.22 C ANISOU 2986 CA ARG B 139 5367 5958 5097 782 337 208 C ATOM 2987 C ARG B 139 -22.157 -35.482 31.814 1.00 38.39 C ANISOU 2987 C ARG B 139 4771 5367 4450 838 363 260 C ATOM 2988 O ARG B 139 -22.160 -35.223 33.012 1.00 55.78 O ANISOU 2988 O ARG B 139 6941 7627 6627 872 365 229 O ATOM 2989 CB ARG B 139 -22.456 -33.100 31.031 1.00 47.87 C ANISOU 2989 CB ARG B 139 5903 6537 5748 736 348 106 C ATOM 2990 CG ARG B 139 -21.691 -31.882 30.503 1.00 23.01 C ANISOU 2990 CG ARG B 139 2728 3396 2618 700 319 46 C ATOM 2991 CD ARG B 139 -20.379 -31.698 31.250 1.00 55.93 C ANISOU 2991 CD ARG B 139 6882 7649 6721 744 283 40 C ATOM 2992 NE ARG B 139 -20.064 -30.293 31.509 1.00100.63 N ANISOU 2992 NE ARG B 139 12494 13332 12410 716 271 -49 N ATOM 2993 CZ ARG B 139 -19.183 -29.880 32.418 1.00110.47 C ANISOU 2993 CZ ARG B 139 13709 14656 13607 749 244 -82 C ATOM 2994 NH1 ARG B 139 -18.529 -30.765 33.164 1.00 60.65 N ANISOU 2994 NH1 ARG B 139 7411 8416 7218 813 225 -33 N ATOM 2995 NH2 ARG B 139 -18.958 -28.582 32.585 1.00126.39 N ANISOU 2995 NH2 ARG B 139 15683 16685 15656 720 236 -164 N ATOM 2996 N TYR B 140 -22.546 -36.659 31.347 1.00 25.47 N ANISOU 2996 N TYR B 140 3181 3682 2813 848 387 340 N ATOM 2997 CA TYR B 140 -22.537 -37.813 32.230 1.00 44.25 C ANISOU 2997 CA TYR B 140 5584 6085 5144 913 407 411 C ATOM 2998 C TYR B 140 -21.097 -38.310 32.285 1.00 74.06 C ANISOU 2998 C TYR B 140 9383 9916 8840 966 372 469 C ATOM 2999 O TYR B 140 -20.683 -38.941 33.257 1.00103.05 O ANISOU 2999 O TYR B 140 13055 13635 12465 1021 374 500 O ATOM 3000 CB TYR B 140 -23.481 -38.907 31.734 1.00 66.86 C ANISOU 3000 CB TYR B 140 8489 8871 8043 904 451 475 C ATOM 3001 CG TYR B 140 -23.453 -40.185 32.556 1.00107.13 C ANISOU 3001 CG TYR B 140 13620 13985 13100 972 479 559 C ATOM 3002 CD1 TYR B 140 -22.464 -41.144 32.356 1.00138.45 C ANISOU 3002 CD1 TYR B 140 17600 17946 17060 963 464 574 C ATOM 3003 CD2 TYR B 140 -24.426 -40.443 33.516 1.00 98.13 C ANISOU 3003 CD2 TYR B 140 12464 12844 11977 993 520 555 C ATOM 3004 CE1 TYR B 140 -22.435 -42.318 33.096 1.00136.07 C ANISOU 3004 CE1 TYR B 140 17307 17643 16750 994 490 610 C ATOM 3005 CE2 TYR B 140 -24.406 -41.617 34.259 1.00115.98 C ANISOU 3005 CE2 TYR B 140 14754 15114 14201 1058 551 637 C ATOM 3006 CZ TYR B 140 -23.407 -42.551 34.044 1.00124.62 C ANISOU 3006 CZ TYR B 140 15859 16199 15291 1045 534 648 C ATOM 3007 OH TYR B 140 -23.374 -43.720 34.773 1.00115.99 O ANISOU 3007 OH TYR B 140 14776 15105 14191 1078 562 687 O ATOM 3008 N LEU B 141 -20.336 -38.005 31.235 1.00116.01 N ANISOU 3008 N LEU B 141 9581 18060 16439 2382 -3544 -2240 N ATOM 3009 CA LEU B 141 -18.929 -38.394 31.149 1.00116.56 C ANISOU 3009 CA LEU B 141 9632 18171 16484 2386 -3479 -2330 C ATOM 3010 C LEU B 141 -18.011 -37.384 31.827 1.00113.72 C ANISOU 3010 C LEU B 141 9262 17867 16078 2408 -3444 -2327 C ATOM 3011 O LEU B 141 -16.806 -37.606 31.949 1.00117.53 O ANISOU 3011 O LEU B 141 9725 18387 16543 2422 -3388 -2393 O ATOM 3012 CB LEU B 141 -18.503 -38.568 29.694 1.00117.08 C ANISOU 3012 CB LEU B 141 9750 18256 16480 2295 -3473 -2414 C ATOM 3013 CG LEU B 141 -18.990 -39.834 28.996 1.00120.90 C ANISOU 3013 CG LEU B 141 10234 18692 17010 2277 -3487 -2448 C ATOM 3014 CD1 LEU B 141 -20.507 -39.885 28.962 1.00 93.67 C ANISOU 3014 CD1 LEU B 141 6798 15187 13605 2274 -3552 -2368 C ATOM 3015 CD2 LEU B 141 -18.404 -39.920 27.593 1.00134.24 C ANISOU 3015 CD2 LEU B 141 11974 20408 18623 2187 -3474 -2536 C ATOM 3016 N ALA B 142 -18.583 -36.261 32.240 1.00 99.09 N ANISOU 3016 N ALA B 142 7426 16021 14202 2410 -3478 -2251 N ATOM 3017 CA ALA B 142 -17.863 -35.299 33.057 1.00103.87 C ANISOU 3017 CA ALA B 142 8016 16674 14776 2443 -3449 -2233 C ATOM 3018 C ALA B 142 -18.180 -35.557 34.519 1.00 94.47 C ANISOU 3018 C ALA B 142 6762 15456 13675 2544 -3445 -2166 C ATOM 3019 O ALA B 142 -17.767 -34.793 35.390 1.00100.70 O ANISOU 3019 O ALA B 142 7532 16276 14453 2584 -3427 -2134 O ATOM 3020 CB ALA B 142 -18.241 -33.885 32.678 1.00115.10 C ANISOU 3020 CB ALA B 142 9492 18122 16118 2386 -3485 -2191 C ATOM 3021 N ILE B 143 -18.940 -36.624 34.773 1.00 90.97 N ANISOU 3021 N ILE B 143 6288 14956 13320 2584 -3464 -2142 N ATOM 3022 CA ILE B 143 -19.375 -36.974 36.128 1.00 90.52 C ANISOU 3022 CA ILE B 143 6171 14866 13356 2680 -3465 -2075 C ATOM 3023 C ILE B 143 -18.982 -38.384 36.603 1.00 90.67 C ANISOU 3023 C ILE B 143 6153 14846 13451 2732 -3414 -2104 C ATOM 3024 O ILE B 143 -18.102 -38.527 37.451 1.00 90.45 O ANISOU 3024 O ILE B 143 6115 14818 13432 2771 -3343 -2105 O ATOM 3025 CB ILE B 143 -20.895 -36.780 36.305 1.00 90.31 C ANISOU 3025 CB ILE B 143 6180 14773 13362 2672 -3514 -1968 C ATOM 3026 CG1 ILE B 143 -21.237 -35.292 36.305 1.00 89.98 C ANISOU 3026 CG1 ILE B 143 6180 14756 13253 2637 -3544 -1910 C ATOM 3027 CG2 ILE B 143 -21.366 -37.408 37.602 1.00 89.94 C ANISOU 3027 CG2 ILE B 143 6142 14638 13394 2728 -3464 -1871 C ATOM 3028 CD1 ILE B 143 -20.622 -34.526 37.450 1.00 89.44 C ANISOU 3028 CD1 ILE B 143 6129 14690 13164 2667 -3480 -1854 C ATOM 3029 N THR B 144 -19.633 -39.420 36.079 1.00 91.03 N ANISOU 3029 N THR B 144 6182 14855 13551 2730 -3447 -2125 N ATOM 3030 CA THR B 144 -19.338 -40.782 36.528 1.00120.35 C ANISOU 3030 CA THR B 144 9865 18526 17337 2777 -3399 -2147 C ATOM 3031 C THR B 144 -18.081 -41.299 35.848 1.00136.79 C ANISOU 3031 C THR B 144 11925 20661 19389 2759 -3363 -2268 C ATOM 3032 O THR B 144 -17.508 -42.316 36.248 1.00140.29 O ANISOU 3032 O THR B 144 12321 21095 19886 2809 -3322 -2310 O ATOM 3033 CB THR B 144 -20.503 -41.755 36.260 1.00125.33 C ANISOU 3033 CB THR B 144 10493 19089 18037 2779 -3440 -2119 C ATOM 3034 OG1 THR B 144 -21.693 -41.262 36.886 1.00150.86 O ANISOU 3034 OG1 THR B 144 13769 22261 21289 2782 -3459 -1994 O ATOM 3035 CG2 THR B 144 -20.183 -43.147 36.815 1.00114.47 C ANISOU 3035 CG2 THR B 144 9089 17668 16737 2829 -3385 -2135 C ATOM 3036 N SER B 145 -17.656 -40.582 34.815 1.00144.62 N ANISOU 3036 N SER B 145 12973 21693 20284 2676 -3363 -2313 N ATOM 3037 CA SER B 145 -16.464 -40.960 34.075 1.00140.38 C ANISOU 3037 CA SER B 145 12446 21193 19698 2637 -3314 -2416 C ATOM 3038 C SER B 145 -15.548 -39.761 33.831 1.00122.04 C ANISOU 3038 C SER B 145 10156 18936 17277 2595 -3290 -2444 C ATOM 3039 O SER B 145 -15.158 -39.490 32.692 1.00104.37 O ANISOU 3039 O SER B 145 7968 16727 14962 2514 -3288 -2503 O ATOM 3040 CB SER B 145 -16.896 -41.550 32.735 1.00137.74 C ANISOU 3040 CB SER B 145 12155 20835 19345 2562 -3339 -2460 C ATOM 3041 OG SER B 145 -17.724 -42.688 32.928 1.00140.32 O ANISOU 3041 OG SER B 145 12453 21100 19762 2599 -3360 -2437 O ATOM 3042 N PRO B 146 -15.164 -39.062 34.906 1.00116.37 N ANISOU 3042 N PRO B 146 9408 18244 16562 2650 -3271 -2405 N ATOM 3043 CA PRO B 146 -14.349 -37.861 34.726 1.00113.49 C ANISOU 3043 CA PRO B 146 9074 17943 16104 2612 -3251 -2425 C ATOM 3044 C PRO B 146 -12.927 -38.218 34.342 1.00134.27 C ANISOU 3044 C PRO B 146 11701 20620 18697 2596 -3189 -2526 C ATOM 3045 O PRO B 146 -12.275 -37.489 33.596 1.00147.18 O ANISOU 3045 O PRO B 146 13379 22302 20242 2531 -3176 -2572 O ATOM 3046 CB PRO B 146 -14.370 -37.204 36.111 1.00112.18 C ANISOU 3046 CB PRO B 146 8868 17785 15969 2688 -3245 -2353 C ATOM 3047 CG PRO B 146 -14.994 -38.220 37.055 1.00116.85 C ANISOU 3047 CG PRO B 146 9401 18322 16674 2772 -3252 -2309 C ATOM 3048 CD PRO B 146 -15.154 -39.508 36.308 1.00118.45 C ANISOU 3048 CD PRO B 146 9604 18489 16913 2752 -3251 -2363 C ATOM 3049 N PHE B 147 -12.463 -39.349 34.863 1.00137.42 N ANISOU 3049 N PHE B 147 12046 21002 19164 2656 -3151 -2561 N ATOM 3050 CA PHE B 147 -11.066 -39.741 34.763 1.00131.23 C ANISOU 3050 CA PHE B 147 11246 20259 18357 2659 -3087 -2650 C ATOM 3051 C PHE B 147 -10.614 -39.760 33.316 1.00129.11 C ANISOU 3051 C PHE B 147 11031 20015 18010 2565 -3081 -2732 C ATOM 3052 O PHE B 147 -9.476 -39.418 33.001 1.00145.10 O ANISOU 3052 O PHE B 147 13068 22092 19970 2538 -3039 -2797 O ATOM 3053 CB PHE B 147 -10.882 -41.109 35.412 1.00117.44 C ANISOU 3053 CB PHE B 147 9437 18480 16706 2733 -3057 -2671 C ATOM 3054 CG PHE B 147 -11.607 -41.244 36.720 1.00118.50 C ANISOU 3054 CG PHE B 147 9521 18577 16928 2821 -3074 -2584 C ATOM 3055 CD1 PHE B 147 -11.123 -40.619 37.858 1.00130.34 C ANISOU 3055 CD1 PHE B 147 10999 20095 18429 2875 -3041 -2543 C ATOM 3056 CD2 PHE B 147 -12.781 -41.975 36.811 1.00100.36 C ANISOU 3056 CD2 PHE B 147 7211 16216 14705 2842 -3115 -2536 C ATOM 3057 CE1 PHE B 147 -11.786 -40.727 39.063 1.00124.43 C ANISOU 3057 CE1 PHE B 147 10281 19263 17734 2913 -3014 -2426 C ATOM 3058 CE2 PHE B 147 -13.449 -42.088 38.016 1.00106.90 C ANISOU 3058 CE2 PHE B 147 8044 16977 15595 2895 -3102 -2430 C ATOM 3059 CZ PHE B 147 -12.950 -41.463 39.144 1.00114.26 C ANISOU 3059 CZ PHE B 147 9000 17902 16513 2923 -3043 -2369 C ATOM 3060 N ARG B 148 -11.530 -40.148 32.441 1.00102.47 N ANISOU 3060 N ARG B 148 7691 16602 14641 2516 -3125 -2726 N ATOM 3061 CA ARG B 148 -11.229 -40.325 31.033 1.00 96.83 C ANISOU 3061 CA ARG B 148 7027 15902 13863 2427 -3124 -2802 C ATOM 3062 C ARG B 148 -11.535 -39.114 30.164 1.00 93.65 C ANISOU 3062 C ARG B 148 6692 15525 13366 2343 -3160 -2788 C ATOM 3063 O ARG B 148 -11.485 -39.193 28.937 1.00 94.12 O ANISOU 3063 O ARG B 148 6799 15591 13371 2264 -3169 -2841 O ATOM 3064 CB ARG B 148 -11.958 -41.545 30.496 1.00116.85 C ANISOU 3064 CB ARG B 148 9560 18382 16457 2419 -3147 -2815 C ATOM 3065 CG ARG B 148 -11.530 -41.888 29.092 1.00149.86 C ANISOU 3065 CG ARG B 148 13786 22577 20578 2335 -3139 -2902 C ATOM 3066 CD ARG B 148 -10.970 -43.292 28.996 1.00175.69 C ANISOU 3066 CD ARG B 148 17022 25832 23902 2360 -3100 -2972 C ATOM 3067 NE ARG B 148 -11.898 -44.170 28.294 1.00208.14 N ANISOU 3067 NE ARG B 148 21145 29888 28050 2333 -3137 -2972 N ATOM 3068 CZ ARG B 148 -11.744 -44.577 27.042 1.00214.35 C ANISOU 3068 CZ ARG B 148 21972 30677 28796 2260 -3138 -3039 C ATOM 3069 NH1 ARG B 148 -10.674 -44.205 26.353 1.00214.43 N ANISOU 3069 NH1 ARG B 148 22010 30739 28725 2207 -3103 -3115 N ATOM 3070 NH2 ARG B 148 -12.656 -45.368 26.494 1.00213.23 N ANISOU 3070 NH2 ARG B 148 21840 30484 28695 2241 -3174 -3032 N ATOM 3071 N TYR B 149 -11.880 -38.004 30.796 1.00105.53 N ANISOU 3071 N TYR B 149 8201 17042 14852 2359 -3181 -2716 N ATOM 3072 CA TYR B 149 -12.324 -36.837 30.051 1.00146.21 C ANISOU 3072 CA TYR B 149 13417 22214 19922 2284 -3221 -2691 C ATOM 3073 C TYR B 149 -11.436 -36.611 28.818 1.00160.71 C ANISOU 3073 C TYR B 149 15302 24096 21666 2199 -3198 -2781 C ATOM 3074 O TYR B 149 -11.918 -36.704 27.688 1.00191.65 O ANISOU 3074 O TYR B 149 19267 28000 25550 2126 -3229 -2802 O ATOM 3075 CB TYR B 149 -12.367 -35.601 30.958 1.00169.63 C ANISOU 3075 CB TYR B 149 16378 25207 22868 2316 -3228 -2621 C ATOM 3076 CG TYR B 149 -13.397 -34.557 30.565 1.00183.95 C ANISOU 3076 CG TYR B 149 18241 27012 24638 2266 -3289 -2554 C ATOM 3077 CD1 TYR B 149 -14.675 -34.560 31.117 1.00178.81 C ANISOU 3077 CD1 TYR B 149 17579 26312 24050 2301 -3339 -2463 C ATOM 3078 CD2 TYR B 149 -13.084 -33.561 29.655 1.00190.79 C ANISOU 3078 CD2 TYR B 149 19167 27922 25403 2184 -3295 -2580 C ATOM 3079 CE1 TYR B 149 -15.609 -33.601 30.760 1.00178.34 C ANISOU 3079 CE1 TYR B 149 17565 26246 23951 2256 -3394 -2401 C ATOM 3080 CE2 TYR B 149 -14.009 -32.602 29.294 1.00184.86 C ANISOU 3080 CE2 TYR B 149 18463 27165 24612 2139 -3350 -2519 C ATOM 3081 CZ TYR B 149 -15.270 -32.624 29.848 1.00167.74 C ANISOU 3081 CZ TYR B 149 16281 24946 22505 2174 -3399 -2430 C ATOM 3082 OH TYR B 149 -16.189 -31.665 29.484 1.00135.38 O ANISOU 3082 OH TYR B 149 12230 20842 18368 2128 -3453 -2370 O ATOM 3083 N GLN B 150 -10.147 -36.348 29.025 1.00140.35 N ANISOU 3083 N GLN B 150 12711 21570 19046 2208 -3143 -2836 N ATOM 3084 CA GLN B 150 -9.242 -36.039 27.907 1.00148.10 C ANISOU 3084 CA GLN B 150 13738 22599 19935 2128 -3118 -2921 C ATOM 3085 C GLN B 150 -8.782 -37.260 27.080 1.00130.45 C ANISOU 3085 C GLN B 150 11502 20352 17711 2101 -3093 -3010 C ATOM 3086 O GLN B 150 -8.320 -37.103 25.945 1.00123.01 O ANISOU 3086 O GLN B 150 10606 19437 16695 2024 -3086 -3075 O ATOM 3087 CB GLN B 150 -8.036 -35.210 28.388 1.00154.18 C ANISOU 3087 CB GLN B 150 14499 23432 20650 2142 -3070 -2947 C ATOM 3088 CG GLN B 150 -7.414 -34.282 27.327 1.00144.92 C ANISOU 3088 CG GLN B 150 13388 22312 19363 2052 -3065 -2998 C ATOM 3089 CD GLN B 150 -8.271 -33.059 27.009 1.00132.40 C ANISOU 3089 CD GLN B 150 11853 20730 17724 2003 -3119 -2932 C ATOM 3090 OE1 GLN B 150 -9.074 -32.614 27.832 1.00128.55 O ANISOU 3090 OE1 GLN B 150 11350 20221 17274 2047 -3151 -2845 O ATOM 3091 NE2 GLN B 150 -8.100 -32.512 25.808 1.00115.19 N ANISOU 3091 NE2 GLN B 150 9734 18578 15456 1912 -3130 -2974 N ATOM 3092 N SER B 151 -8.909 -38.464 27.638 1.00 94.61 N ANISOU 3092 N SER B 151 6910 15773 13263 2165 -3079 -3012 N ATOM 3093 CA SER B 151 -8.553 -39.684 26.908 1.00 98.14 C ANISOU 3093 CA SER B 151 7354 16205 13729 2144 -3057 -3092 C ATOM 3094 C SER B 151 -9.547 -39.983 25.774 1.00117.71 C ANISOU 3094 C SER B 151 9880 18646 16200 2076 -3108 -3090 C ATOM 3095 O SER B 151 -9.153 -40.123 24.611 1.00122.32 O ANISOU 3095 O SER B 151 10504 19246 16726 2003 -3101 -3160 O ATOM 3096 CB SER B 151 -8.459 -40.883 27.865 1.00 95.06 C ANISOU 3096 CB SER B 151 6895 15781 13443 2234 -3030 -3090 C ATOM 3097 OG SER B 151 -7.166 -41.480 27.853 1.00 95.27 O ANISOU 3097 OG SER B 151 6897 15840 13463 2248 -2967 -3176 O ATOM 3098 N LEU B 152 -10.833 -40.063 26.119 1.00128.85 N ANISOU 3098 N LEU B 152 11285 20005 17666 2099 -3159 -3008 N ATOM 3099 CA LEU B 152 -11.894 -40.338 25.144 1.00137.30 C ANISOU 3099 CA LEU B 152 12396 21035 18736 2040 -3212 -2996 C ATOM 3100 C LEU B 152 -12.296 -39.079 24.386 1.00150.65 C ANISOU 3100 C LEU B 152 14153 22749 20338 1962 -3251 -2971 C ATOM 3101 O LEU B 152 -12.103 -38.979 23.172 1.00165.40 O ANISOU 3101 O LEU B 152 16071 24633 22139 1880 -3256 -3026 O ATOM 3102 CB LEU B 152 -13.133 -40.925 25.825 1.00121.42 C ANISOU 3102 CB LEU B 152 10354 18960 16821 2097 -3252 -2917 C ATOM 3103 CG LEU B 152 -14.337 -41.138 24.899 1.00111.69 C ANISOU 3103 CG LEU B 152 9163 17683 15591 2040 -3311 -2893 C ATOM 3104 CD1 LEU B 152 -14.067 -42.261 23.899 1.00 96.42 C ANISOU 3104 CD1 LEU B 152 7240 15735 13662 2000 -3296 -2976 C ATOM 3105 CD2 LEU B 152 -15.612 -41.411 25.689 1.00105.03 C ANISOU 3105 CD2 LEU B 152 8291 16781 14833 2097 -3355 -2800 C ATOM 3106 N MET B 153 -12.851 -38.116 25.114 1.00128.57 N ANISOU 3106 N MET B 153 11356 19954 17542 1988 -3279 -2888 N ATOM 3107 CA MET B 153 -13.247 -36.857 24.513 1.00105.96 C ANISOU 3107 CA MET B 153 8551 17113 14597 1920 -3317 -2857 C ATOM 3108 C MET B 153 -11.984 -36.046 24.287 1.00 95.12 C ANISOU 3108 C MET B 153 7197 15808 13136 1888 -3273 -2914 C ATOM 3109 O MET B 153 -11.283 -35.698 25.233 1.00 98.89 O ANISOU 3109 O MET B 153 7639 16316 13619 1943 -3237 -2906 O ATOM 3110 CB MET B 153 -14.177 -36.098 25.461 1.00 94.56 C ANISOU 3110 CB MET B 153 7096 15650 13184 1965 -3356 -2750 C ATOM 3111 CG MET B 153 -15.654 -36.321 25.217 1.00 94.60 C ANISOU 3111 CG MET B 153 7117 15597 13231 1953 -3420 -2685 C ATOM 3112 SD MET B 153 -16.207 -35.408 23.768 1.00181.93 S ANISOU 3112 SD MET B 153 18264 26669 24193 1837 -3469 -2688 S ATOM 3113 CE MET B 153 -17.968 -35.729 23.803 1.00 94.84 C ANISOU 3113 CE MET B 153 7239 15566 13231 1845 -3541 -2600 C ATOM 3114 N THR B 154 -11.693 -35.743 23.030 1.00104.31 N ANISOU 3114 N THR B 154 8418 16998 14218 1799 -3277 -2971 N ATOM 3115 CA THR B 154 -10.547 -34.911 22.707 1.00117.04 C ANISOU 3115 CA THR B 154 10055 18676 15740 1760 -3240 -3024 C ATOM 3116 C THR B 154 -11.071 -33.742 21.894 1.00124.51 C ANISOU 3116 C THR B 154 11067 19638 16603 1680 -3284 -2998 C ATOM 3117 O THR B 154 -12.028 -33.895 21.136 1.00 95.81 O ANISOU 3117 O THR B 154 7467 15968 12969 1633 -3331 -2979 O ATOM 3118 CB THR B 154 -9.486 -35.675 21.880 1.00 96.08 C ANISOU 3118 CB THR B 154 7405 16044 13057 1724 -3193 -3134 C ATOM 3119 OG1 THR B 154 -9.437 -37.047 22.294 1.00 96.22 O ANISOU 3119 OG1 THR B 154 7371 16025 13163 1782 -3171 -3156 O ATOM 3120 CG2 THR B 154 -8.114 -35.032 22.052 1.00 95.97 C ANISOU 3120 CG2 THR B 154 7389 16096 12979 1722 -3139 -3185 C ATOM 3121 N ARG B 155 -10.458 -32.574 22.045 1.00124.69 N ANISOU 3121 N ARG B 155 11108 19713 16555 1664 -3269 -2995 N ATOM 3122 CA ARG B 155 -10.885 -31.427 21.256 1.00109.03 C ANISOU 3122 CA ARG B 155 9188 17749 14488 1587 -3309 -2973 C ATOM 3123 C ARG B 155 -10.812 -31.830 19.790 1.00139.48 C ANISOU 3123 C ARG B 155 13094 21605 18296 1499 -3316 -3045 C ATOM 3124 O ARG B 155 -11.383 -31.173 18.925 1.00165.92 O ANISOU 3124 O ARG B 155 16499 24955 21587 1427 -3357 -3031 O ATOM 3125 CB ARG B 155 -10.026 -30.194 21.547 1.00103.46 C ANISOU 3125 CB ARG B 155 8495 17106 13708 1579 -3282 -2977 C ATOM 3126 CG ARG B 155 -10.224 -29.633 22.947 1.00107.69 C ANISOU 3126 CG ARG B 155 8990 17642 14285 1658 -3283 -2897 C ATOM 3127 CD ARG B 155 -8.945 -29.707 23.773 1.00113.97 C ANISOU 3127 CD ARG B 155 9739 18477 15086 1715 -3219 -2936 C ATOM 3128 NE ARG B 155 -8.173 -28.469 23.692 1.00128.30 N ANISOU 3128 NE ARG B 155 11583 20354 16812 1683 -3200 -2949 N ATOM 3129 CZ ARG B 155 -7.049 -28.242 24.364 1.00 93.77 C ANISOU 3129 CZ ARG B 155 7179 16025 12426 1723 -3147 -2978 C ATOM 3130 NH1 ARG B 155 -6.563 -29.174 25.170 1.00109.61 N ANISOU 3130 NH1 ARG B 155 9125 18019 14503 1797 -3107 -2997 N ATOM 3131 NH2 ARG B 155 -6.413 -27.085 24.232 1.00 93.62 N ANISOU 3131 NH2 ARG B 155 7189 16060 12322 1689 -3134 -2988 N ATOM 3132 N ALA B 156 -10.086 -32.916 19.531 1.00139.96 N ANISOU 3132 N ALA B 156 13133 21665 18381 1507 -3274 -3122 N ATOM 3133 CA ALA B 156 -10.037 -33.553 18.217 1.00114.91 C ANISOU 3133 CA ALA B 156 9997 18485 15180 1435 -3278 -3193 C ATOM 3134 C ALA B 156 -11.234 -34.478 17.948 1.00107.02 C ANISOU 3134 C ALA B 156 8995 17418 14249 1437 -3322 -3162 C ATOM 3135 O ALA B 156 -11.708 -34.572 16.815 1.00 97.54 O ANISOU 3135 O ALA B 156 7843 16204 13015 1364 -3353 -3183 O ATOM 3136 CB ALA B 156 -8.729 -34.317 18.049 1.00 97.23 C ANISOU 3136 CB ALA B 156 7735 16274 12935 1442 -3215 -3290 C ATOM 3137 N ARG B 157 -11.703 -35.175 18.983 1.00116.55 N ANISOU 3137 N ARG B 157 10147 18584 15553 1520 -3324 -3114 N ATOM 3138 CA ARG B 157 -12.748 -36.193 18.814 1.00116.11 C ANISOU 3138 CA ARG B 157 10081 18465 15572 1531 -3359 -3090 C ATOM 3139 C ARG B 157 -14.214 -35.702 18.803 1.00113.80 C ANISOU 3139 C ARG B 157 9812 18131 15294 1518 -3429 -2998 C ATOM 3140 O ARG B 157 -15.097 -36.403 18.307 1.00 97.17 O ANISOU 3140 O ARG B 157 7716 15977 13226 1501 -3464 -2987 O ATOM 3141 CB ARG B 157 -12.558 -37.344 19.816 1.00109.99 C ANISOU 3141 CB ARG B 157 9235 17661 14897 1623 -3328 -3091 C ATOM 3142 CG ARG B 157 -11.257 -38.131 19.602 1.00115.19 C ANISOU 3142 CG ARG B 157 9871 18346 15549 1627 -3265 -3190 C ATOM 3143 CD ARG B 157 -11.303 -39.521 20.230 1.00120.19 C ANISOU 3143 CD ARG B 157 10445 18938 16284 1700 -3245 -3198 C ATOM 3144 NE ARG B 157 -10.158 -40.346 19.839 1.00137.12 N ANISOU 3144 NE ARG B 157 12575 21105 18421 1693 -3190 -3297 N ATOM 3145 CZ ARG B 157 -10.009 -41.629 20.162 1.00140.00 C ANISOU 3145 CZ ARG B 157 12893 21439 18862 1743 -3165 -3326 C ATOM 3146 NH1 ARG B 157 -10.935 -42.243 20.884 1.00131.33 N ANISOU 3146 NH1 ARG B 157 11758 20287 17855 1804 -3191 -3263 N ATOM 3147 NH2 ARG B 157 -8.935 -42.300 19.761 1.00144.26 N ANISOU 3147 NH2 ARG B 157 13423 22002 19387 1733 -3115 -3417 N ATOM 3148 N ALA B 158 -14.480 -34.512 19.338 1.00 74.03 N ANISOU 3148 N ALA B 158 8590 10137 9400 309 -892 111 N ATOM 3149 CA ALA B 158 -15.848 -33.975 19.354 1.00 80.05 C ANISOU 3149 CA ALA B 158 9390 10834 10192 269 -896 159 C ATOM 3150 C ALA B 158 -16.248 -33.280 18.051 1.00 83.23 C ANISOU 3150 C ALA B 158 9834 11141 10649 228 -931 166 C ATOM 3151 O ALA B 158 -17.442 -33.134 17.757 1.00 73.84 O ANISOU 3151 O ALA B 158 8710 9843 9504 206 -927 169 O ATOM 3152 CB ALA B 158 -16.038 -33.035 20.530 1.00 93.64 C ANISOU 3152 CB ALA B 158 11098 12555 11926 260 -943 170 C ATOM 3153 N LYS B 159 -15.247 -32.847 17.285 1.00100.63 N ANISOU 3153 N LYS B 159 12013 13361 12862 208 -963 173 N ATOM 3154 CA LYS B 159 -15.476 -32.188 15.999 1.00 98.53 C ANISOU 3154 CA LYS B 159 11787 13004 12645 145 -986 214 C ATOM 3155 C LYS B 159 -16.204 -33.151 15.080 1.00 79.31 C ANISOU 3155 C LYS B 159 9383 10549 10202 152 -937 212 C ATOM 3156 O LYS B 159 -17.203 -32.803 14.434 1.00 86.47 O ANISOU 3156 O LYS B 159 10349 11353 11152 114 -943 233 O ATOM 3157 CB LYS B 159 -14.150 -31.750 15.352 1.00 84.75 C ANISOU 3157 CB LYS B 159 9992 11307 10901 111 -1023 245 C ATOM 3158 CG LYS B 159 -13.724 -30.298 15.645 1.00 92.87 C ANISOU 3158 CG LYS B 159 11017 12294 11975 55 -1097 285 C ATOM 3159 CD LYS B 159 -12.363 -29.954 15.012 1.00 95.42 C ANISOU 3159 CD LYS B 159 11280 12680 12294 7 -1130 333 C ATOM 3160 CE LYS B 159 -11.989 -28.476 15.199 1.00 83.03 C ANISOU 3160 CE LYS B 159 9711 11059 10778 -63 -1213 386 C ATOM 3161 NZ LYS B 159 -10.653 -28.127 14.616 1.00 68.17 N ANISOU 3161 NZ LYS B 159 7763 9251 8888 -125 -1245 449 N ATOM 3162 N VAL B 160 -15.696 -34.376 15.035 1.00 32.05 N ANISOU 3162 N VAL B 160 3360 4650 4169 205 -901 175 N ATOM 3163 CA VAL B 160 -16.300 -35.407 14.215 1.00 33.58 C ANISOU 3163 CA VAL B 160 3573 4835 4350 221 -861 163 C ATOM 3164 C VAL B 160 -17.733 -35.613 14.663 1.00 49.39 C ANISOU 3164 C VAL B 160 5629 6767 6371 213 -832 173 C ATOM 3165 O VAL B 160 -18.615 -35.808 13.842 1.00 56.57 O ANISOU 3165 O VAL B 160 6582 7607 7304 192 -821 180 O ATOM 3166 CB VAL B 160 -15.554 -36.734 14.333 1.00 33.82 C ANISOU 3166 CB VAL B 160 3584 4905 4362 276 -836 109 C ATOM 3167 CG1 VAL B 160 -16.040 -37.502 15.553 1.00 15.04 C ANISOU 3167 CG1 VAL B 160 1215 2541 1957 310 -792 95 C ATOM 3168 CG2 VAL B 160 -15.750 -37.557 13.074 1.00 35.50 C ANISOU 3168 CG2 VAL B 160 3809 5100 4579 281 -822 94 C ATOM 3169 N ILE B 161 -17.962 -35.557 15.971 1.00 59.18 N ANISOU 3169 N ILE B 161 6865 8016 7606 230 -830 167 N ATOM 3170 CA ILE B 161 -19.288 -35.808 16.518 1.00 58.65 C ANISOU 3170 CA ILE B 161 6846 7871 7567 227 -815 162 C ATOM 3171 C ILE B 161 -20.306 -34.751 16.105 1.00 50.73 C ANISOU 3171 C ILE B 161 5915 6724 6635 190 -853 151 C ATOM 3172 O ILE B 161 -21.435 -35.078 15.724 1.00 40.79 O ANISOU 3172 O ILE B 161 4707 5382 5409 183 -843 134 O ATOM 3173 CB ILE B 161 -19.243 -35.951 18.040 1.00 44.93 C ANISOU 3173 CB ILE B 161 5077 6193 5802 255 -811 164 C ATOM 3174 CG1 ILE B 161 -18.823 -37.377 18.376 1.00 28.10 C ANISOU 3174 CG1 ILE B 161 2910 4140 3625 280 -760 182 C ATOM 3175 CG2 ILE B 161 -20.599 -35.619 18.648 1.00 13.95 C ANISOU 3175 CG2 ILE B 161 1207 2175 1919 252 -821 139 C ATOM 3176 CD1 ILE B 161 -19.314 -38.389 17.348 1.00 17.63 C ANISOU 3176 CD1 ILE B 161 1608 2781 2311 279 -735 178 C ATOM 3177 N ILE B 162 -19.907 -33.486 16.177 1.00 14.31 N ANISOU 3177 N ILE B 162 1307 2078 2053 166 -905 158 N ATOM 3178 CA ILE B 162 -20.770 -32.435 15.679 1.00 22.43 C ANISOU 3178 CA ILE B 162 2404 2960 3160 130 -956 153 C ATOM 3179 C ILE B 162 -21.025 -32.658 14.190 1.00 46.63 C ANISOU 3179 C ILE B 162 5493 5984 6240 94 -949 184 C ATOM 3180 O ILE B 162 -22.162 -32.530 13.702 1.00 51.09 O ANISOU 3180 O ILE B 162 6118 6439 6856 79 -964 169 O ATOM 3181 CB ILE B 162 -20.154 -31.053 15.871 1.00 25.03 C ANISOU 3181 CB ILE B 162 2732 3252 3527 102 -1026 170 C ATOM 3182 CG1 ILE B 162 -19.572 -30.901 17.280 1.00 34.84 C ANISOU 3182 CG1 ILE B 162 3927 4574 4735 141 -1033 144 C ATOM 3183 CG2 ILE B 162 -21.198 -29.997 15.592 1.00 22.60 C ANISOU 3183 CG2 ILE B 162 2502 2775 3311 75 -1092 155 C ATOM 3184 CD1 ILE B 162 -19.165 -29.474 17.628 1.00 16.40 C ANISOU 3184 CD1 ILE B 162 1600 2179 2453 120 -1118 145 C ATOM 3185 N CYS B 163 -19.961 -33.001 13.469 1.00 14.29 N ANISOU 3185 N CYS B 163 1344 1987 2097 85 -931 220 N ATOM 3186 CA CYS B 163 -20.077 -33.282 12.044 1.00 37.85 C ANISOU 3186 CA CYS B 163 4336 4969 5077 58 -923 248 C ATOM 3187 C CYS B 163 -21.109 -34.375 11.734 1.00 37.72 C ANISOU 3187 C CYS B 163 4347 4926 5057 84 -882 215 C ATOM 3188 O CYS B 163 -21.922 -34.213 10.828 1.00 28.83 O ANISOU 3188 O CYS B 163 3265 3721 3967 57 -899 223 O ATOM 3189 CB CYS B 163 -18.712 -33.628 11.450 1.00 14.64 C ANISOU 3189 CB CYS B 163 1324 2163 2074 64 -909 270 C ATOM 3190 SG CYS B 163 -17.753 -32.176 10.987 1.00100.11 S ANISOU 3190 SG CYS B 163 12130 12982 12924 -11 -976 346 S ATOM 3191 N THR B 164 -21.069 -35.472 12.489 1.00 32.45 N ANISOU 3191 N THR B 164 3656 4322 4351 131 -837 183 N ATOM 3192 CA THR B 164 -22.034 -36.568 12.385 1.00 59.65 C ANISOU 3192 CA THR B 164 7128 7735 7802 150 -805 155 C ATOM 3193 C THR B 164 -23.450 -36.104 12.719 1.00 85.61 C ANISOU 3193 C THR B 164 10486 10885 11156 136 -829 126 C ATOM 3194 O THR B 164 -24.422 -36.515 12.076 1.00 97.90 O ANISOU 3194 O THR B 164 12083 12373 12742 130 -829 107 O ATOM 3195 CB THR B 164 -21.658 -37.736 13.326 1.00 67.31 C ANISOU 3195 CB THR B 164 8056 8791 8728 193 -766 145 C ATOM 3196 OG1 THR B 164 -20.669 -38.557 12.696 1.00 40.08 O ANISOU 3196 OG1 THR B 164 4550 5453 5225 216 -744 156 O ATOM 3197 CG2 THR B 164 -22.880 -38.587 13.647 1.00 95.16 C ANISOU 3197 CG2 THR B 164 11623 12250 12283 201 -751 119 C ATOM 3198 N VAL B 165 -23.561 -35.250 13.731 1.00 78.94 N ANISOU 3198 N VAL B 165 9654 10008 10333 138 -855 112 N ATOM 3199 CA VAL B 165 -24.830 -34.605 14.038 1.00 59.88 C ANISOU 3199 CA VAL B 165 7301 7470 7979 134 -891 72 C ATOM 3200 C VAL B 165 -25.395 -33.868 12.813 1.00 76.28 C ANISOU 3200 C VAL B 165 9430 9436 10117 93 -937 84 C ATOM 3201 O VAL B 165 -26.605 -33.858 12.619 1.00 12.27 O ANISOU 3201 O VAL B 165 1374 1233 2056 93 -954 48 O ATOM 3202 CB VAL B 165 -24.694 -33.632 15.225 1.00 30.57 C ANISOU 3202 CB VAL B 165 3587 3750 4278 151 -925 50 C ATOM 3203 CG1 VAL B 165 -26.031 -33.002 15.556 1.00 18.09 C ANISOU 3203 CG1 VAL B 165 2066 2053 2756 161 -965 -6 C ATOM 3204 CG2 VAL B 165 -24.141 -34.357 16.433 1.00 12.85 C ANISOU 3204 CG2 VAL B 165 1285 1631 1968 190 -884 50 C ATOM 3205 N TRP B 166 -24.515 -33.272 11.998 1.00 78.39 N ANISOU 3205 N TRP B 166 9678 9725 10382 57 -959 139 N ATOM 3206 CA TRP B 166 -24.904 -32.545 10.768 1.00 46.90 C ANISOU 3206 CA TRP B 166 5729 5649 6443 8 -1010 175 C ATOM 3207 C TRP B 166 -24.892 -33.340 9.448 1.00 37.08 C ANISOU 3207 C TRP B 166 4469 4457 5164 -3 -983 202 C ATOM 3208 O TRP B 166 -25.257 -32.818 8.392 1.00 13.34 O ANISOU 3208 O TRP B 166 1489 1393 2186 -44 -1025 238 O ATOM 3209 CB TRP B 166 -24.034 -31.310 10.590 1.00 13.91 C ANISOU 3209 CB TRP B 166 1541 1461 2285 -39 -1066 235 C ATOM 3210 CG TRP B 166 -24.260 -30.278 11.627 1.00 51.56 C ANISOU 3210 CG TRP B 166 6341 6139 7111 -32 -1121 204 C ATOM 3211 CD1 TRP B 166 -23.974 -30.380 12.954 1.00 62.15 C ANISOU 3211 CD1 TRP B 166 7658 7529 8428 15 -1102 158 C ATOM 3212 CD2 TRP B 166 -24.812 -28.974 11.432 1.00 67.30 C ANISOU 3212 CD2 TRP B 166 8395 7980 9195 -69 -1214 213 C ATOM 3213 NE1 TRP B 166 -24.315 -29.222 13.601 1.00 77.21 N ANISOU 3213 NE1 TRP B 166 9604 9332 10401 18 -1175 128 N ATOM 3214 CE2 TRP B 166 -24.834 -28.341 12.690 1.00 70.70 C ANISOU 3214 CE2 TRP B 166 8834 8373 9654 -32 -1248 158 C ATOM 3215 CE3 TRP B 166 -25.288 -28.278 10.321 1.00 83.20 C ANISOU 3215 CE3 TRP B 166 10455 9887 11269 -128 -1280 262 C ATOM 3216 CZ2 TRP B 166 -25.318 -27.045 12.864 1.00 60.68 C ANISOU 3216 CZ2 TRP B 166 7623 6953 8478 -45 -1348 140 C ATOM 3217 CZ3 TRP B 166 -25.764 -26.995 10.496 1.00 79.38 C ANISOU 3217 CZ3 TRP B 166 10031 9249 10881 -151 -1382 256 C ATOM 3218 CH2 TRP B 166 -25.776 -26.391 11.755 1.00 62.19 C ANISOU 3218 CH2 TRP B 166 7865 7027 8738 -105 -1416 191 C ATOM 3219 N ALA B 167 -24.427 -34.579 9.497 1.00 52.71 N ANISOU 3219 N ALA B 167 6401 6549 7076 36 -921 187 N ATOM 3220 CA ALA B 167 -24.686 -35.531 8.428 1.00 59.04 C ANISOU 3220 CA ALA B 167 7194 7389 7850 47 -897 183 C ATOM 3221 C ALA B 167 -26.059 -36.153 8.657 1.00 41.98 C ANISOU 3221 C ALA B 167 5087 5131 5733 65 -893 127 C ATOM 3222 O ALA B 167 -26.782 -36.447 7.706 1.00 26.35 O ANISOU 3222 O ALA B 167 3132 3109 3770 59 -907 119 O ATOM 3223 CB ALA B 167 -23.620 -36.599 8.407 1.00 87.78 C ANISOU 3223 CB ALA B 167 10763 11181 11409 88 -846 181 C ATOM 3224 N ILE B 168 -26.405 -36.349 9.932 1.00 60.13 N ANISOU 3224 N ILE B 168 7398 7404 8046 87 -878 89 N ATOM 3225 CA ILE B 168 -27.722 -36.862 10.332 1.00 57.79 C ANISOU 3225 CA ILE B 168 7144 7025 7787 100 -878 37 C ATOM 3226 C ILE B 168 -28.825 -35.818 10.197 1.00 41.59 C ANISOU 3226 C ILE B 168 5154 4841 5807 79 -935 14 C ATOM 3227 O ILE B 168 -29.895 -36.092 9.645 1.00 26.66 O ANISOU 3227 O ILE B 168 3301 2875 3952 76 -953 -13 O ATOM 3228 CB ILE B 168 -27.730 -37.337 11.785 1.00 43.85 C ANISOU 3228 CB ILE B 168 5359 5301 6001 130 -848 14 C ATOM 3229 CG1 ILE B 168 -26.850 -38.581 11.943 1.00 42.48 C ANISOU 3229 CG1 ILE B 168 5131 5240 5770 152 -801 32 C ATOM 3230 CG2 ILE B 168 -29.157 -37.627 12.223 1.00 10.98 C ANISOU 3230 CG2 ILE B 168 1235 1062 1876 138 -857 -33 C ATOM 3231 CD1 ILE B 168 -26.384 -38.834 13.365 1.00 51.75 C ANISOU 3231 CD1 ILE B 168 6267 6489 6908 177 -778 38 C ATOM 3232 N SER B 169 -28.566 -34.627 10.726 1.00 12.49 N ANISOU 3232 N SER B 169 1478 1122 2145 68 -971 22 N ATOM 3233 CA SER B 169 -29.471 -33.491 10.561 1.00 25.67 C ANISOU 3233 CA SER B 169 3205 2657 3890 50 -1042 2 C ATOM 3234 C SER B 169 -29.777 -33.276 9.088 1.00 43.98 C ANISOU 3234 C SER B 169 5551 4922 6239 11 -1080 39 C ATOM 3235 O SER B 169 -30.938 -33.132 8.716 1.00 12.48 O ANISOU 3235 O SER B 169 1608 832 2301 8 -1119 6 O ATOM 3236 CB SER B 169 -28.839 -32.215 11.112 1.00 15.62 C ANISOU 3236 CB SER B 169 1933 1359 2641 38 -1088 19 C ATOM 3237 OG SER B 169 -28.648 -32.296 12.515 1.00 31.47 O ANISOU 3237 OG SER B 169 3887 3482 4590 62 -1044 27 O ATOM 3238 N ALA B 170 -28.721 -33.260 8.266 1.00 56.69 N ANISOU 3238 N ALA B 170 7121 6611 7806 -16 -1070 108 N ATOM 3239 CA ALA B 170 -28.823 -33.015 6.821 1.00 44.14 C ANISOU 3239 CA ALA B 170 5541 5007 6223 -56 -1107 159 C ATOM 3240 C ALA B 170 -29.548 -34.137 6.082 1.00 47.92 C ANISOU 3240 C ALA B 170 6025 5499 6684 -32 -1082 128 C ATOM 3241 O ALA B 170 -30.400 -33.884 5.221 1.00 14.22 O ANISOU 3241 O ALA B 170 1794 1155 2453 -52 -1130 131 O ATOM 3242 CB ALA B 170 -27.448 -32.789 6.214 1.00 13.49 C ANISOU 3242 CB ALA B 170 1602 1244 2281 -86 -1098 240 C ATOM 3243 N LEU B 171 -29.199 -35.376 6.409 1.00 58.96 N ANISOU 3243 N LEU B 171 7384 6990 8029 9 -1014 99 N ATOM 3244 CA LEU B 171 -29.851 -36.525 5.797 1.00 13.97 C ANISOU 3244 CA LEU B 171 1691 1297 2321 36 -996 63 C ATOM 3245 C LEU B 171 -31.345 -36.504 6.078 1.00 56.29 C ANISOU 3245 C LEU B 171 7112 6524 7751 38 -1029 6 C ATOM 3246 O LEU B 171 -32.169 -36.484 5.159 1.00 59.00 O ANISOU 3246 O LEU B 171 7487 6807 8125 30 -1068 0 O ATOM 3247 CB LEU B 171 -29.269 -37.806 6.369 1.00 11.61 C ANISOU 3247 CB LEU B 171 1349 1093 1971 76 -933 38 C ATOM 3248 CG LEU B 171 -29.495 -39.025 5.491 1.00 39.46 C ANISOU 3248 CG LEU B 171 4864 4654 5475 103 -920 13 C ATOM 3249 CD1 LEU B 171 -28.481 -39.011 4.353 1.00 49.77 C ANISOU 3249 CD1 LEU B 171 6114 6087 6710 107 -916 58 C ATOM 3250 CD2 LEU B 171 -29.382 -40.301 6.308 1.00 32.20 C ANISOU 3250 CD2 LEU B 171 3927 3763 4543 136 -878 -25 C ATOM 3251 N VAL B 172 -31.671 -36.486 7.369 1.00 53.14 N ANISOU 3251 N VAL B 172 6723 6095 7372 53 -1014 -33 N ATOM 3252 CA VAL B 172 -33.046 -36.579 7.864 1.00 35.81 C ANISOU 3252 CA VAL B 172 4567 3817 5224 65 -1031 -90 C ATOM 3253 C VAL B 172 -33.949 -35.387 7.530 1.00 36.56 C ANISOU 3253 C VAL B 172 4683 3879 5330 56 -1060 -84 C ATOM 3254 O VAL B 172 -35.092 -35.573 7.121 1.00 43.92 O ANISOU 3254 O VAL B 172 5623 4804 6259 65 -1057 -103 O ATOM 3255 CB VAL B 172 -33.058 -36.796 9.377 1.00 33.85 C ANISOU 3255 CB VAL B 172 4303 3594 4964 88 -1002 -121 C ATOM 3256 CG1 VAL B 172 -34.433 -36.509 9.948 1.00 40.66 C ANISOU 3256 CG1 VAL B 172 5173 4451 5825 106 -995 -154 C ATOM 3257 CG2 VAL B 172 -32.619 -38.202 9.690 1.00 10.84 C ANISOU 3257 CG2 VAL B 172 1347 770 2000 106 -943 -116 C ATOM 3258 N SER B 173 -33.451 -34.169 7.719 1.00 15.79 N ANISOU 3258 N SER B 173 2060 1222 2717 38 -1096 -59 N ATOM 3259 CA SER B 173 -34.215 -32.993 7.330 1.00 12.86 C ANISOU 3259 CA SER B 173 1711 810 2367 28 -1140 -53 C ATOM 3260 C SER B 173 -34.319 -32.855 5.815 1.00 50.86 C ANISOU 3260 C SER B 173 6540 5593 7193 -6 -1185 -7 C ATOM 3261 O SER B 173 -35.427 -32.735 5.293 1.00 21.96 O ANISOU 3261 O SER B 173 2894 1912 3539 1 -1202 -23 O ATOM 3262 CB SER B 173 -33.598 -31.728 7.908 1.00 41.41 C ANISOU 3262 CB SER B 173 5332 4397 6005 15 -1179 -36 C ATOM 3263 OG SER B 173 -34.147 -30.575 7.283 1.00 33.18 O ANISOU 3263 OG SER B 173 4313 3303 4991 -4 -1239 -16 O ATOM 3264 N PHE B 174 -33.174 -32.886 5.120 1.00 61.77 N ANISOU 3264 N PHE B 174 7917 6970 8582 -46 -1216 53 N ATOM 3265 CA PHE B 174 -33.120 -32.547 3.687 1.00 53.81 C ANISOU 3265 CA PHE B 174 6926 5928 7591 -93 -1284 116 C ATOM 3266 C PHE B 174 -33.544 -33.626 2.685 1.00 36.01 C ANISOU 3266 C PHE B 174 4676 3678 5327 -81 -1288 104 C ATOM 3267 O PHE B 174 -34.019 -33.283 1.603 1.00 24.89 O ANISOU 3267 O PHE B 174 3290 2233 3934 -109 -1352 138 O ATOM 3268 CB PHE B 174 -31.760 -31.940 3.280 1.00 14.57 C ANISOU 3268 CB PHE B 174 1933 996 2607 -150 -1313 211 C ATOM 3269 CG PHE B 174 -31.761 -30.423 3.198 1.00 76.57 C ANISOU 3269 CG PHE B 174 9819 8760 10515 -207 -1398 264 C ATOM 3270 CD1 PHE B 174 -31.241 -29.652 4.230 1.00 71.67 C ANISOU 3270 CD1 PHE B 174 9191 8134 9906 -204 -1394 259 C ATOM 3271 CD2 PHE B 174 -32.291 -29.769 2.093 1.00 63.90 C ANISOU 3271 CD2 PHE B 174 8240 7113 8926 -252 -1473 314 C ATOM 3272 CE1 PHE B 174 -31.248 -28.258 4.162 1.00 42.19 C ANISOU 3272 CE1 PHE B 174 5476 4353 6202 -241 -1460 299 C ATOM 3273 CE2 PHE B 174 -32.300 -28.370 2.019 1.00 54.73 C ANISOU 3273 CE2 PHE B 174 7098 5905 7793 -295 -1541 360 C ATOM 3274 CZ PHE B 174 -31.779 -27.620 3.057 1.00 17.24 C ANISOU 3274 CZ PHE B 174 2342 1150 3059 -286 -1533 349 C ATOM 3275 N LEU B 175 -33.376 -34.907 3.011 1.00 33.45 N ANISOU 3275 N LEU B 175 4321 3429 4961 -35 -1215 60 N ATOM 3276 CA LEU B 175 -33.882 -35.949 2.106 1.00 51.07 C ANISOU 3276 CA LEU B 175 6547 5690 7169 -8 -1209 35 C ATOM 3277 C LEU B 175 -35.407 -36.017 1.988 1.00 47.95 C ANISOU 3277 C LEU B 175 6189 5217 6812 8 -1232 -14 C ATOM 3278 O LEU B 175 -35.950 -35.911 0.890 1.00 49.21 O ANISOU 3278 O LEU B 175 6371 5341 6987 -3 -1293 0 O ATOM 3279 CB LEU B 175 -33.349 -37.338 2.477 1.00 50.25 C ANISOU 3279 CB LEU B 175 6399 5682 7010 38 -1131 -2 C ATOM 3280 CG LEU B 175 -32.486 -37.942 1.359 1.00 62.83 C ANISOU 3280 CG LEU B 175 7936 7418 8519 55 -1112 31 C ATOM 3281 CD1 LEU B 175 -33.272 -38.222 0.110 1.00 65.48 C ANISOU 3281 CD1 LEU B 175 8288 7738 8855 64 -1160 23 C ATOM 3282 CD2 LEU B 175 -31.435 -36.925 1.053 1.00 89.92 C ANISOU 3282 CD2 LEU B 175 11331 10929 11905 16 -1122 113 C ATOM 3283 N PRO B 176 -36.101 -36.202 3.121 1.00 29.92 N ANISOU 3283 N PRO B 176 3893 2962 4514 37 -1168 -60 N ATOM 3284 CA PRO B 176 -37.554 -36.380 3.116 1.00 30.10 C ANISOU 3284 CA PRO B 176 3922 2977 4539 57 -1159 -95 C ATOM 3285 C PRO B 176 -38.353 -35.172 2.626 1.00 38.45 C ANISOU 3285 C PRO B 176 5003 3983 5623 41 -1221 -79 C ATOM 3286 O PRO B 176 -39.523 -35.339 2.287 1.00 53.44 O ANISOU 3286 O PRO B 176 6908 5863 7532 55 -1236 -102 O ATOM 3287 CB PRO B 176 -37.865 -36.654 4.586 1.00 40.76 C ANISOU 3287 CB PRO B 176 5251 4363 5872 77 -1095 -128 C ATOM 3288 CG PRO B 176 -36.638 -37.278 5.099 1.00 45.08 C ANISOU 3288 CG PRO B 176 5781 4944 6403 78 -1061 -123 C ATOM 3289 CD PRO B 176 -35.529 -36.529 4.436 1.00 12.42 C ANISOU 3289 CD PRO B 176 1654 786 2279 50 -1108 -79 C ATOM 3290 N ILE B 177 -37.765 -33.981 2.606 1.00 26.67 N ANISOU 3290 N ILE B 177 3523 2464 4148 11 -1263 -39 N ATOM 3291 CA ILE B 177 -38.463 -32.840 2.021 1.00 32.64 C ANISOU 3291 CA ILE B 177 4305 3160 4936 -8 -1340 -18 C ATOM 3292 C ILE B 177 -38.358 -32.809 0.496 1.00 48.09 C ANISOU 3292 C ILE B 177 6287 5075 6910 -44 -1425 33 C ATOM 3293 O ILE B 177 -39.338 -32.524 -0.196 1.00 66.24 O ANISOU 3293 O ILE B 177 8608 7328 9231 -45 -1484 31 O ATOM 3294 CB ILE B 177 -37.988 -31.518 2.589 1.00 15.55 C ANISOU 3294 CB ILE B 177 2147 972 2790 -30 -1367 6 C ATOM 3295 CG1 ILE B 177 -38.652 -31.283 3.935 1.00 15.27 C ANISOU 3295 CG1 ILE B 177 2099 953 2751 12 -1322 -55 C ATOM 3296 CG2 ILE B 177 -38.356 -30.389 1.648 1.00 69.21 C ANISOU 3296 CG2 ILE B 177 8975 7698 9625 -68 -1470 51 C ATOM 3297 CD1 ILE B 177 -38.574 -29.855 4.382 1.00 72.60 C ANISOU 3297 CD1 ILE B 177 9372 8170 10043 3 -1373 -48 C ATOM 3298 N MET B 178 -37.169 -33.105 -0.020 1.00 23.83 N ANISOU 3298 N MET B 178 3213 2013 3829 -77 -1442 83 N ATOM 3299 CA MET B 178 -36.951 -33.161 -1.464 1.00 41.76 C ANISOU 3299 CA MET B 178 5509 4246 6112 -122 -1537 145 C ATOM 3300 C MET B 178 -37.578 -34.401 -2.081 1.00 81.15 C ANISOU 3300 C MET B 178 10502 9238 11094 -77 -1535 93 C ATOM 3301 O MET B 178 -37.707 -34.506 -3.302 1.00114.41 O ANISOU 3301 O MET B 178 14709 13496 15265 -85 -1582 131 O ATOM 3302 CB MET B 178 -35.459 -33.123 -1.785 1.00 36.64 C ANISOU 3302 CB MET B 178 4815 3711 5396 -156 -1513 223 C ATOM 3303 CG MET B 178 -34.861 -31.730 -1.727 1.00 46.59 C ANISOU 3303 CG MET B 178 6088 4934 6680 -232 -1570 308 C ATOM 3304 SD MET B 178 -35.026 -30.957 -0.101 1.00 77.02 S ANISOU 3304 SD MET B 178 9955 8719 10589 -208 -1536 250 S ATOM 3305 CE MET B 178 -34.672 -29.243 -0.511 1.00 76.22 C ANISOU 3305 CE MET B 178 9876 8565 10519 -294 -1637 350 C ATOM 3306 N MET B 179 -37.957 -35.341 -1.224 1.00 65.44 N ANISOU 3306 N MET B 179 8484 7296 9083 -18 -1439 16 N ATOM 3307 CA MET B 179 -38.621 -36.565 -1.649 1.00 51.47 C ANISOU 3307 CA MET B 179 6713 5535 7308 27 -1428 -39 C ATOM 3308 C MET B 179 -40.103 -36.285 -1.782 1.00 40.76 C ANISOU 3308 C MET B 179 5369 4148 5971 40 -1448 -63 C ATOM 3309 O MET B 179 -40.872 -37.125 -2.250 1.00 49.11 O ANISOU 3309 O MET B 179 6427 5200 7032 70 -1457 -101 O ATOM 3310 CB MET B 179 -38.418 -37.659 -0.600 1.00 48.78 C ANISOU 3310 CB MET B 179 6336 5258 6939 66 -1322 -92 C ATOM 3311 CG MET B 179 -38.002 -38.991 -1.163 1.00 17.26 C ANISOU 3311 CG MET B 179 2337 1282 2939 100 -1324 -128 C ATOM 3312 SD MET B 179 -36.489 -38.788 -2.104 1.00105.62 S ANISOU 3312 SD MET B 179 13475 12622 14034 92 -1319 -54 S ATOM 3313 CE MET B 179 -36.209 -40.472 -2.645 1.00183.62 C ANISOU 3313 CE MET B 179 23310 22598 23858 160 -1281 -113 C ATOM 3314 N HIS B 180 -40.500 -35.097 -1.347 1.00 16.25 N ANISOU 3314 N HIS B 180 2272 1021 2882 20 -1463 -45 N ATOM 3315 CA HIS B 180 -41.906 -34.793 -1.187 1.00 35.95 C ANISOU 3315 CA HIS B 180 4771 3490 5399 39 -1476 -77 C ATOM 3316 C HIS B 180 -42.567 -35.963 -0.457 1.00 48.81 C ANISOU 3316 C HIS B 180 6369 5167 7009 79 -1393 -134 C ATOM 3317 O HIS B 180 -43.703 -36.318 -0.742 1.00 73.37 O ANISOU 3317 O HIS B 180 9482 8258 10139 97 -1414 -161 O ATOM 3318 CB HIS B 180 -42.576 -34.509 -2.535 1.00 33.21 C ANISOU 3318 CB HIS B 180 4461 3072 5084 25 -1592 -55 C ATOM 3319 CG HIS B 180 -42.124 -33.233 -3.177 1.00 60.09 C ANISOU 3319 CG HIS B 180 7901 6420 8512 -31 -1691 16 C ATOM 3320 ND1 HIS B 180 -42.791 -32.039 -3.009 1.00 82.34 N ANISOU 3320 ND1 HIS B 180 10733 9188 11363 -44 -1744 25 N ATOM 3321 CD2 HIS B 180 -41.069 -32.965 -3.984 1.00 75.45 C ANISOU 3321 CD2 HIS B 180 9869 8345 10454 -87 -1759 91 C ATOM 3322 CE1 HIS B 180 -42.168 -31.090 -3.687 1.00103.60 C ANISOU 3322 CE1 HIS B 180 13458 11834 14072 -107 -1837 103 C ATOM 3323 NE2 HIS B 180 -41.120 -31.625 -4.285 1.00103.83 N ANISOU 3323 NE2 HIS B 180 13491 11883 14076 -141 -1847 153 N ATOM 3324 N TRP B 181 -41.843 -36.572 0.479 1.00 41.61 N ANISOU 3324 N TRP B 181 5430 4314 6066 87 -1308 -145 N ATOM 3325 CA TRP B 181 -42.443 -37.566 1.358 1.00 17.47 C ANISOU 3325 CA TRP B 181 2345 1297 2995 110 -1238 -183 C ATOM 3326 C TRP B 181 -43.464 -36.851 2.218 1.00 21.27 C ANISOU 3326 C TRP B 181 2822 1766 3493 116 -1238 -201 C ATOM 3327 O TRP B 181 -44.212 -37.472 2.969 1.00 35.30 O ANISOU 3327 O TRP B 181 4579 3563 5271 130 -1204 -227 O ATOM 3328 CB TRP B 181 -41.395 -38.233 2.252 1.00 39.84 C ANISOU 3328 CB TRP B 181 5156 4185 5797 111 -1166 -184 C ATOM 3329 CG TRP B 181 -40.799 -39.499 1.689 1.00 83.92 C ANISOU 3329 CG TRP B 181 10732 9786 11368 122 -1154 -193 C ATOM 3330 CD1 TRP B 181 -40.533 -39.775 0.375 1.00 82.33 C ANISOU 3330 CD1 TRP B 181 10547 9558 11176 129 -1212 -192 C ATOM 3331 CD2 TRP B 181 -40.411 -40.668 2.428 1.00114.91 C ANISOU 3331 CD2 TRP B 181 14632 13753 15276 132 -1096 -209 C ATOM 3332 NE1 TRP B 181 -39.995 -41.036 0.253 1.00100.49 N ANISOU 3332 NE1 TRP B 181 12832 11884 13465 150 -1189 -217 N ATOM 3333 CE2 TRP B 181 -39.912 -41.606 1.497 1.00122.91 C ANISOU 3333 CE2 TRP B 181 15646 14764 16289 149 -1117 -224 C ATOM 3334 CE3 TRP B 181 -40.437 -41.012 3.786 1.00105.70 C ANISOU 3334 CE3 TRP B 181 13444 12618 14099 129 -1042 -212 C ATOM 3335 CZ2 TRP B 181 -39.441 -42.864 1.882 1.00119.11 C ANISOU 3335 CZ2 TRP B 181 15145 14312 15801 162 -1082 -244 C ATOM 3336 CZ3 TRP B 181 -39.967 -42.264 4.166 1.00108.18 C ANISOU 3336 CZ3 TRP B 181 13739 12957 14407 135 -1012 -221 C ATOM 3337 CH2 TRP B 181 -39.475 -43.172 3.217 1.00105.32 C ANISOU 3337 CH2 TRP B 181 13378 12592 14048 151 -1030 -237 C ATOM 3338 N TRP B 182 -43.461 -35.526 2.121 1.00 21.84 N ANISOU 3338 N TRP B 182 2913 1802 3585 105 -1287 -186 N ATOM 3339 CA TRP B 182 -44.374 -34.692 2.887 1.00 20.95 C ANISOU 3339 CA TRP B 182 2797 1668 3495 117 -1304 -211 C ATOM 3340 C TRP B 182 -45.600 -34.261 2.114 1.00 16.51 C ANISOU 3340 C TRP B 182 2252 1046 2976 124 -1384 -223 C ATOM 3341 O TRP B 182 -46.431 -33.547 2.640 1.00 23.59 O ANISOU 3341 O TRP B 182 3147 1917 3901 139 -1416 -250 O ATOM 3342 CB TRP B 182 -43.662 -33.458 3.431 1.00 30.13 C ANISOU 3342 CB TRP B 182 3968 2820 4659 107 -1317 -197 C ATOM 3343 CG TRP B 182 -43.248 -32.461 2.400 1.00 16.43 C ANISOU 3343 CG TRP B 182 2264 1031 2949 78 -1396 -155 C ATOM 3344 CD1 TRP B 182 -42.218 -32.578 1.515 1.00 48.82 C ANISOU 3344 CD1 TRP B 182 6379 5130 7042 46 -1415 -106 C ATOM 3345 CD2 TRP B 182 -43.829 -31.173 2.171 1.00 26.19 C ANISOU 3345 CD2 TRP B 182 3521 2200 4229 72 -1482 -153 C ATOM 3346 NE1 TRP B 182 -42.132 -31.450 0.734 1.00 69.95 N ANISOU 3346 NE1 TRP B 182 9084 7741 9751 13 -1511 -63 N ATOM 3347 CE2 TRP B 182 -43.107 -30.569 1.120 1.00 55.49 C ANISOU 3347 CE2 TRP B 182 7261 5869 7955 29 -1552 -92 C ATOM 3348 CE3 TRP B 182 -44.890 -30.473 2.749 1.00 18.02 C ANISOU 3348 CE3 TRP B 182 2485 1132 3228 98 -1517 -195 C ATOM 3349 CZ2 TRP B 182 -43.411 -29.297 0.635 1.00 29.81 C ANISOU 3349 CZ2 TRP B 182 4037 2540 4748 6 -1656 -67 C ATOM 3350 CZ3 TRP B 182 -45.193 -29.208 2.266 1.00 57.90 C ANISOU 3350 CZ3 TRP B 182 7564 6108 8328 85 -1619 -181 C ATOM 3351 CH2 TRP B 182 -44.455 -28.635 1.218 1.00 56.18 C ANISOU 3351 CH2 TRP B 182 7376 5846 8123 37 -1687 -115 C ATOM 3352 N ARG B 183 -45.718 -34.684 0.866 1.00 65.54 N ANISOU 3352 N ARG B 183 8479 7230 9195 116 -1430 -207 N ATOM 3353 CA ARG B 183 -46.915 -34.350 0.103 1.00 97.69 C ANISOU 3353 CA ARG B 183 12568 11239 13312 124 -1517 -219 C ATOM 3354 C ARG B 183 -48.128 -35.149 0.587 1.00 93.45 C ANISOU 3354 C ARG B 183 12005 10713 12790 152 -1495 -263 C ATOM 3355 O ARG B 183 -48.098 -36.381 0.656 1.00 97.98 O ANISOU 3355 O ARG B 183 12560 11324 13344 159 -1443 -271 O ATOM 3356 CB ARG B 183 -46.701 -34.520 -1.414 1.00128.38 C ANISOU 3356 CB ARG B 183 16486 15082 17209 108 -1594 -187 C ATOM 3357 CG ARG B 183 -46.130 -35.867 -1.856 1.00133.97 C ANISOU 3357 CG ARG B 183 17186 15831 17887 115 -1552 -189 C ATOM 3358 CD ARG B 183 -47.184 -36.947 -2.097 1.00 83.52 C ANISOU 3358 CD ARG B 183 10783 9439 11513 143 -1553 -228 C ATOM 3359 NE ARG B 183 -46.623 -38.273 -1.859 1.00 45.55 N ANISOU 3359 NE ARG B 183 5950 4686 6672 155 -1477 -242 N ATOM 3360 CZ ARG B 183 -45.657 -38.819 -2.592 1.00 43.53 C ANISOU 3360 CZ ARG B 183 5705 4439 6397 156 -1487 -232 C ATOM 3361 NH1 ARG B 183 -45.146 -38.153 -3.621 1.00 19.53 N ANISOU 3361 NH1 ARG B 183 2702 1354 3365 140 -1574 -201 N ATOM 3362 NH2 ARG B 183 -45.204 -40.033 -2.294 1.00 34.69 N ANISOU 3362 NH2 ARG B 183 4561 3366 5254 171 -1423 -253 N ATOM 3363 N ASP B 184 -49.188 -34.432 0.945 1.00 81.15 N ANISOU 3363 N ASP B 184 10446 9116 11273 169 -1544 -291 N ATOM 3364 CA ASP B 184 -50.460 -35.059 1.276 1.00111.64 C ANISOU 3364 CA ASP B 184 14283 12972 15164 193 -1552 -331 C ATOM 3365 C ASP B 184 -51.342 -34.916 0.047 1.00112.74 C ANISOU 3365 C ASP B 184 14444 13041 15351 198 -1654 -334 C ATOM 3366 O ASP B 184 -51.459 -33.827 -0.508 1.00117.75 O ANISOU 3366 O ASP B 184 15107 13616 16015 193 -1738 -324 O ATOM 3367 CB ASP B 184 -51.105 -34.389 2.498 1.00106.65 C ANISOU 3367 CB ASP B 184 13631 12337 14556 216 -1557 -370 C ATOM 3368 CG ASP B 184 -52.244 -35.215 3.100 1.00 85.23 C ANISOU 3368 CG ASP B 184 10883 9630 11872 239 -1554 -408 C ATOM 3369 OD1 ASP B 184 -52.147 -36.467 3.142 1.00 86.08 O ANISOU 3369 OD1 ASP B 184 10973 9773 11961 231 -1503 -397 O ATOM 3370 OD2 ASP B 184 -53.237 -34.600 3.543 1.00 26.71 O ANISOU 3370 OD2 ASP B 184 3459 2182 4509 267 -1613 -450 O ATOM 3371 N GLU B 185 -51.946 -36.017 -0.388 1.00104.23 N ANISOU 3371 N GLU B 185 13355 11963 14286 208 -1657 -347 N ATOM 3372 CA GLU B 185 -52.690 -36.029 -1.648 1.00103.63 C ANISOU 3372 CA GLU B 185 13301 11819 14253 215 -1759 -350 C ATOM 3373 C GLU B 185 -53.836 -35.011 -1.703 1.00103.89 C ANISOU 3373 C GLU B 185 13341 11780 14351 232 -1861 -376 C ATOM 3374 O GLU B 185 -54.158 -34.488 -2.775 1.00 80.92 O ANISOU 3374 O GLU B 185 10467 8802 11478 229 -1969 -364 O ATOM 3375 CB GLU B 185 -53.208 -37.440 -1.965 1.00103.11 C ANISOU 3375 CB GLU B 185 13216 11764 14196 228 -1746 -368 C ATOM 3376 CG GLU B 185 -52.145 -38.405 -2.497 1.00112.53 C ANISOU 3376 CG GLU B 185 14416 12997 15342 219 -1697 -347 C ATOM 3377 CD GLU B 185 -51.610 -38.016 -3.873 1.00108.61 C ANISOU 3377 CD GLU B 185 13966 12455 14844 212 -1782 -323 C ATOM 3378 OE1 GLU B 185 -51.671 -38.861 -4.791 1.00 89.14 O ANISOU 3378 OE1 GLU B 185 11512 9973 12386 227 -1822 -334 O ATOM 3379 OE2 GLU B 185 -51.116 -36.878 -4.037 1.00109.71 O ANISOU 3379 OE2 GLU B 185 14133 12571 14980 193 -1819 -293 O ATOM 3380 N ASP B 186 -54.430 -34.718 -0.547 1.00121.25 N ANISOU 3380 N ASP B 186 15509 13991 16569 250 -1839 -411 N ATOM 3381 CA ASP B 186 -55.610 -33.854 -0.485 1.00119.02 C ANISOU 3381 CA ASP B 186 15224 13641 16358 276 -1940 -451 C ATOM 3382 C ASP B 186 -55.428 -32.525 -1.213 1.00100.95 C ANISOU 3382 C ASP B 186 12979 11283 14095 265 -2039 -430 C ATOM 3383 O ASP B 186 -54.359 -31.918 -1.171 1.00107.85 O ANISOU 3383 O ASP B 186 13874 12171 14932 240 -2013 -394 O ATOM 3384 CB ASP B 186 -56.046 -33.615 0.963 1.00113.99 C ANISOU 3384 CB ASP B 186 14547 13031 15734 302 -1906 -496 C ATOM 3385 CG ASP B 186 -56.969 -34.702 1.477 1.00125.99 C ANISOU 3385 CG ASP B 186 16022 14567 17283 322 -1889 -530 C ATOM 3386 OD1 ASP B 186 -57.889 -34.379 2.257 1.00128.35 O ANISOU 3386 OD1 ASP B 186 16288 14845 17633 355 -1930 -583 O ATOM 3387 OD2 ASP B 186 -56.779 -35.878 1.096 1.00136.47 O ANISOU 3387 OD2 ASP B 186 17343 15921 18587 305 -1844 -506 O ATOM 3388 N PRO B 187 -56.498 -32.065 -1.869 1.00 74.79 N ANISOU 3388 N PRO B 187 9678 7886 10854 283 -2164 -453 N ATOM 3389 CA PRO B 187 -56.484 -30.908 -2.766 1.00 83.31 C ANISOU 3389 CA PRO B 187 10805 8877 11972 268 -2291 -427 C ATOM 3390 C PRO B 187 -56.220 -29.617 -2.010 1.00 78.45 C ANISOU 3390 C PRO B 187 10193 8245 11371 270 -2308 -437 C ATOM 3391 O PRO B 187 -55.592 -28.699 -2.541 1.00 89.26 O ANISOU 3391 O PRO B 187 11602 9568 12745 238 -2370 -392 O ATOM 3392 CB PRO B 187 -57.902 -30.902 -3.331 1.00 74.22 C ANISOU 3392 CB PRO B 187 9652 7646 10903 297 -2415 -466 C ATOM 3393 CG PRO B 187 -58.724 -31.512 -2.240 1.00 37.38 C ANISOU 3393 CG PRO B 187 4926 3022 6254 336 -2355 -529 C ATOM 3394 CD PRO B 187 -57.863 -32.563 -1.629 1.00 45.80 C ANISOU 3394 CD PRO B 187 5970 4191 7241 319 -2203 -508 C ATOM 3395 N GLN B 188 -56.702 -29.544 -0.778 1.00 52.11 N ANISOU 3395 N GLN B 188 6814 4940 8047 306 -2264 -496 N ATOM 3396 CA GLN B 188 -56.442 -28.375 0.033 1.00 65.29 C ANISOU 3396 CA GLN B 188 8483 6596 9730 317 -2280 -517 C ATOM 3397 C GLN B 188 -54.935 -28.117 0.021 1.00 67.78 C ANISOU 3397 C GLN B 188 8823 6950 9979 273 -2212 -455 C ATOM 3398 O GLN B 188 -54.486 -27.029 -0.353 1.00 34.81 O ANISOU 3398 O GLN B 188 4681 2718 5826 250 -2286 -424 O ATOM 3399 CB GLN B 188 -56.983 -28.592 1.450 1.00 86.09 C ANISOU 3399 CB GLN B 188 11064 9277 12368 364 -2225 -590 C ATOM 3400 CG GLN B 188 -58.508 -28.523 1.528 1.00 92.28 C ANISOU 3400 CG GLN B 188 11819 10005 13238 413 -2323 -663 C ATOM 3401 CD GLN B 188 -59.149 -29.729 2.205 1.00 82.98 C ANISOU 3401 CD GLN B 188 10590 8884 12056 437 -2258 -701 C ATOM 3402 OE1 GLN B 188 -59.428 -30.747 1.565 1.00 37.25 O ANISOU 3402 OE1 GLN B 188 4794 3099 6261 422 -2244 -677 O ATOM 3403 NE2 GLN B 188 -59.410 -29.605 3.501 1.00 96.10 N ANISOU 3403 NE2 GLN B 188 12210 10580 13725 477 -2233 -764 N ATOM 3404 N ALA B 189 -54.171 -29.148 0.387 1.00 94.52 N ANISOU 3404 N ALA B 189 12192 10429 13294 260 -2081 -434 N ATOM 3405 CA ALA B 189 -52.709 -29.092 0.416 1.00104.79 C ANISOU 3405 CA ALA B 189 13507 11775 14532 222 -2009 -379 C ATOM 3406 C ALA B 189 -52.105 -29.210 -0.986 1.00117.71 C ANISOU 3406 C ALA B 189 15184 13381 16158 178 -2054 -311 C ATOM 3407 O ALA B 189 -51.018 -28.694 -1.249 1.00152.40 O ANISOU 3407 O ALA B 189 19601 17773 20530 141 -2056 -260 O ATOM 3408 CB ALA B 189 -52.152 -30.178 1.336 1.00 68.37 C ANISOU 3408 CB ALA B 189 8860 7263 9853 227 -1868 -386 C ATOM 3409 N LEU B 190 -52.811 -29.903 -1.873 1.00 69.97 N ANISOU 3409 N LEU B 190 9146 7309 10131 183 -2101 -312 N ATOM 3410 CA LEU B 190 -52.357 -30.105 -3.242 1.00 39.53 C ANISOU 3410 CA LEU B 190 5332 3420 6269 147 -2163 -255 C ATOM 3411 C LEU B 190 -52.121 -28.760 -3.911 1.00 55.59 C ANISOU 3411 C LEU B 190 7412 5365 8343 110 -2293 -206 C ATOM 3412 O LEU B 190 -51.100 -28.539 -4.575 1.00 74.59 O ANISOU 3412 O LEU B 190 9851 7763 10725 60 -2318 -138 O ATOM 3413 CB LEU B 190 -53.424 -30.870 -4.013 1.00 46.64 C ANISOU 3413 CB LEU B 190 6235 4285 7202 169 -2224 -278 C ATOM 3414 CG LEU B 190 -53.020 -31.661 -5.248 1.00 58.23 C ANISOU 3414 CG LEU B 190 7733 5745 8648 148 -2257 -239 C ATOM 3415 CD1 LEU B 190 -52.298 -32.944 -4.844 1.00 47.45 C ANISOU 3415 CD1 LEU B 190 6334 4476 7218 156 -2118 -247 C ATOM 3416 CD2 LEU B 190 -54.271 -31.966 -6.056 1.00 54.26 C ANISOU 3416 CD2 LEU B 190 7243 5173 8202 172 -2368 -265 C ATOM 3417 N LYS B 191 -53.085 -27.865 -3.719 1.00 59.07 N ANISOU 3417 N LYS B 191 7857 5736 8851 131 -2386 -241 N ATOM 3418 CA LYS B 191 -53.032 -26.514 -4.259 1.00 72.92 C ANISOU 3418 CA LYS B 191 9655 7392 10658 97 -2528 -200 C ATOM 3419 C LYS B 191 -51.884 -25.704 -3.666 1.00 75.22 C ANISOU 3419 C LYS B 191 9950 7705 10927 67 -2488 -167 C ATOM 3420 O LYS B 191 -51.311 -24.852 -4.342 1.00 83.02 O ANISOU 3420 O LYS B 191 10980 8630 11933 11 -2585 -96 O ATOM 3421 CB LYS B 191 -54.359 -25.798 -4.002 1.00 98.43 C ANISOU 3421 CB LYS B 191 12880 10546 13973 140 -2631 -261 C ATOM 3422 CG LYS B 191 -54.387 -24.351 -4.462 1.00118.47 C ANISOU 3422 CG LYS B 191 15463 12972 16579 108 -2791 -226 C ATOM 3423 CD LYS B 191 -55.756 -23.727 -4.220 1.00118.88 C ANISOU 3423 CD LYS B 191 15504 12944 16722 160 -2903 -298 C ATOM 3424 CE LYS B 191 -55.849 -22.326 -4.807 1.00 93.20 C ANISOU 3424 CE LYS B 191 12300 9563 13548 125 -3087 -259 C ATOM 3425 NZ LYS B 191 -57.235 -21.784 -4.733 1.00 53.06 N ANISOU 3425 NZ LYS B 191 7207 4388 8564 179 -3218 -332 N ATOM 3426 N CYS B 192 -51.554 -25.966 -2.403 1.00 55.79 N ANISOU 3426 N CYS B 192 7444 5326 8426 99 -2355 -213 N ATOM 3427 CA CYS B 192 -50.433 -25.294 -1.745 1.00 67.21 C ANISOU 3427 CA CYS B 192 8890 6798 9849 77 -2310 -188 C ATOM 3428 C CYS B 192 -49.074 -25.864 -2.183 1.00 97.34 C ANISOU 3428 C CYS B 192 12713 10670 13600 28 -2241 -117 C ATOM 3429 O CYS B 192 -48.050 -25.189 -2.067 1.00105.24 O ANISOU 3429 O CYS B 192 13726 11669 14592 -10 -2245 -70 O ATOM 3430 CB CYS B 192 -50.593 -25.330 -0.219 1.00 25.96 C ANISOU 3430 CB CYS B 192 3620 1633 4610 130 -2213 -264 C ATOM 3431 SG CYS B 192 -49.238 -24.582 0.722 1.00246.93 S ANISOU 3431 SG CYS B 192 31602 29652 32568 113 -2156 -245 S ATOM 3432 N TYR B 193 -49.068 -27.099 -2.687 1.00111.83 N ANISOU 3432 N TYR B 193 14542 12553 15396 30 -2187 -112 N ATOM 3433 CA TYR B 193 -47.859 -27.699 -3.264 1.00 99.92 C ANISOU 3433 CA TYR B 193 13043 11087 13835 -13 -2146 -49 C ATOM 3434 C TYR B 193 -47.624 -27.204 -4.690 1.00 82.70 C ANISOU 3434 C TYR B 193 10918 8827 11678 -78 -2290 36 C ATOM 3435 O TYR B 193 -46.484 -26.999 -5.106 1.00 68.47 O ANISOU 3435 O TYR B 193 9132 7031 9851 -137 -2304 112 O ATOM 3436 CB TYR B 193 -47.929 -29.233 -3.262 1.00 76.49 C ANISOU 3436 CB TYR B 193 10048 8192 10821 18 -2047 -81 C ATOM 3437 CG TYR B 193 -48.091 -29.848 -1.893 1.00 67.63 C ANISOU 3437 CG TYR B 193 8876 7151 9669 65 -1913 -146 C ATOM 3438 CD1 TYR B 193 -47.916 -29.088 -0.744 1.00 61.33 C ANISOU 3438 CD1 TYR B 193 8062 6367 8875 78 -1878 -170 C ATOM 3439 CD2 TYR B 193 -48.419 -31.185 -1.748 1.00 86.26 C ANISOU 3439 CD2 TYR B 193 11209 9566 12001 94 -1836 -180 C ATOM 3440 CE1 TYR B 193 -48.066 -29.640 0.507 1.00 60.00 C ANISOU 3440 CE1 TYR B 193 7854 6266 8678 114 -1775 -221 C ATOM 3441 CE2 TYR B 193 -48.575 -31.748 -0.498 1.00 99.59 C ANISOU 3441 CE2 TYR B 193 12856 11321 13663 124 -1731 -226 C ATOM 3442 CZ TYR B 193 -48.396 -30.972 0.626 1.00 97.13 C ANISOU 3442 CZ TYR B 193 12532 11022 13352 133 -1703 -244 C ATOM 3443 OH TYR B 193 -48.547 -31.526 1.874 1.00125.97 O ANISOU 3443 OH TYR B 193 16148 14734 16979 160 -1616 -284 O ATOM 3444 N GLN B 194 -48.709 -27.045 -5.442 1.00 72.72 N ANISOU 3444 N GLN B 194 9682 7487 10463 -73 -2405 30 N ATOM 3445 CA GLN B 194 -48.614 -26.568 -6.822 1.00 63.52 C ANISOU 3445 CA GLN B 194 8578 6235 9320 -143 -2566 119 C ATOM 3446 C GLN B 194 -48.504 -25.045 -6.953 1.00 81.85 C ANISOU 3446 C GLN B 194 10933 8472 11693 -198 -2690 176 C ATOM 3447 O GLN B 194 -47.800 -24.543 -7.830 1.00 87.79 O ANISOU 3447 O GLN B 194 11730 9184 12443 -287 -2791 282 O ATOM 3448 CB GLN B 194 -49.767 -27.115 -7.657 1.00 56.26 C ANISOU 3448 CB GLN B 194 7682 5265 8431 -119 -2653 95 C ATOM 3449 CG GLN B 194 -49.618 -28.598 -7.950 1.00 83.71 C ANISOU 3449 CG GLN B 194 11143 8806 11858 -91 -2573 71 C ATOM 3450 CD GLN B 194 -50.892 -29.219 -8.467 1.00128.49 C ANISOU 3450 CD GLN B 194 16821 14437 17563 -46 -2634 20 C ATOM 3451 OE1 GLN B 194 -51.963 -28.615 -8.399 1.00150.25 O ANISOU 3451 OE1 GLN B 194 19581 17128 20378 -24 -2712 -11 O ATOM 3452 NE2 GLN B 194 -50.786 -30.437 -8.989 1.00138.37 N ANISOU 3452 NE2 GLN B 194 18073 15720 18781 -28 -2607 7 N ATOM 3453 N ASP B 195 -49.206 -24.316 -6.090 1.00 92.04 N ANISOU 3453 N ASP B 195 12204 9735 13033 -149 -2694 109 N ATOM 3454 CA ASP B 195 -49.088 -22.862 -6.043 1.00118.50 C ANISOU 3454 CA ASP B 195 15580 13003 16440 -189 -2807 148 C ATOM 3455 C ASP B 195 -47.762 -22.455 -5.389 1.00149.48 C ANISOU 3455 C ASP B 195 19488 16980 20329 -221 -2729 183 C ATOM 3456 O ASP B 195 -47.513 -22.775 -4.223 1.00145.66 O ANISOU 3456 O ASP B 195 18957 16573 19815 -165 -2590 115 O ATOM 3457 CB ASP B 195 -50.282 -22.256 -5.299 1.00107.83 C ANISOU 3457 CB ASP B 195 14211 11603 15157 -119 -2845 54 C ATOM 3458 CG ASP B 195 -50.070 -20.799 -4.936 1.00117.94 C ANISOU 3458 CG ASP B 195 15506 12809 16496 -141 -2938 70 C ATOM 3459 OD1 ASP B 195 -49.493 -20.049 -5.754 1.00115.21 O ANISOU 3459 OD1 ASP B 195 15207 12397 16171 -227 -3057 171 O ATOM 3460 OD2 ASP B 195 -50.484 -20.398 -3.827 1.00129.67 O ANISOU 3460 OD2 ASP B 195 16959 14300 18010 -77 -2900 -17 O ATOM 3461 N PRO B 196 -46.899 -21.754 -6.149 1.00147.46 N ANISOU 3461 N PRO B 196 19271 16681 20076 -319 -2826 298 N ATOM 3462 CA PRO B 196 -45.580 -21.335 -5.653 1.00126.09 C ANISOU 3462 CA PRO B 196 16549 14018 17341 -361 -2768 345 C ATOM 3463 C PRO B 196 -45.678 -20.411 -4.442 1.00109.56 C ANISOU 3463 C PRO B 196 14432 11905 15289 -311 -2749 277 C ATOM 3464 O PRO B 196 -44.723 -20.303 -3.671 1.00119.15 O ANISOU 3464 O PRO B 196 15622 13174 16476 -310 -2661 276 O ATOM 3465 CB PRO B 196 -44.982 -20.571 -6.841 1.00 92.98 C ANISOU 3465 CB PRO B 196 12408 9759 13160 -488 -2923 491 C ATOM 3466 CG PRO B 196 -45.713 -21.083 -8.041 1.00 83.25 C ANISOU 3466 CG PRO B 196 11217 8485 11929 -517 -3022 528 C ATOM 3467 CD PRO B 196 -47.105 -21.380 -7.562 1.00109.10 C ANISOU 3467 CD PRO B 196 14474 11734 15244 -406 -3003 400 C ATOM 3468 N GLY B 197 -46.827 -19.760 -4.283 1.00 83.38 N ANISOU 3468 N GLY B 197 11127 8509 12046 -268 -2840 218 N ATOM 3469 CA GLY B 197 -47.019 -18.773 -3.236 1.00 79.73 C ANISOU 3469 CA GLY B 197 10649 8008 11635 -223 -2858 154 C ATOM 3470 C GLY B 197 -47.350 -19.327 -1.861 1.00 85.22 C ANISOU 3470 C GLY B 197 11293 8785 12303 -125 -2711 34 C ATOM 3471 O GLY B 197 -47.445 -18.571 -0.891 1.00 66.89 O ANISOU 3471 O GLY B 197 8957 6442 10018 -84 -2720 -25 O ATOM 3472 N CYS B 198 -47.535 -20.639 -1.761 1.00 86.74 N ANISOU 3472 N CYS B 198 11457 9067 12432 -90 -2587 0 N ATOM 3473 CA CYS B 198 -47.757 -21.238 -0.455 1.00 66.35 C ANISOU 3473 CA CYS B 198 8827 6569 9815 -14 -2451 -95 C ATOM 3474 C CYS B 198 -46.576 -22.105 -0.053 1.00 83.77 C ANISOU 3474 C CYS B 198 11009 8881 11939 -26 -2304 -71 C ATOM 3475 O CYS B 198 -46.373 -23.193 -0.596 1.00 86.13 O ANISOU 3475 O CYS B 198 11303 9235 12188 -40 -2241 -45 O ATOM 3476 CB CYS B 198 -49.039 -22.068 -0.448 1.00 28.32 C ANISOU 3476 CB CYS B 198 3991 1769 5001 42 -2429 -163 C ATOM 3477 SG CYS B 198 -49.532 -22.630 1.199 1.00178.29 S ANISOU 3477 SG CYS B 198 22928 20848 23965 126 -2300 -275 S ATOM 3478 N CYS B 199 -45.783 -21.612 0.890 1.00 84.94 N ANISOU 3478 N CYS B 199 11143 9052 12077 -20 -2260 -82 N ATOM 3479 CA CYS B 199 -44.776 -22.450 1.512 1.00 85.24 C ANISOU 3479 CA CYS B 199 11153 9192 12044 -17 -2121 -78 C ATOM 3480 C CYS B 199 -45.322 -22.938 2.838 1.00 96.71 C ANISOU 3480 C CYS B 199 12568 10704 13475 57 -2029 -173 C ATOM 3481 O CYS B 199 -44.635 -23.625 3.591 1.00114.87 O ANISOU 3481 O CYS B 199 14842 13085 15719 69 -1919 -185 O ATOM 3482 CB CYS B 199 -43.445 -21.728 1.692 1.00 89.55 C ANISOU 3482 CB CYS B 199 11706 9730 12588 -63 -2132 -20 C ATOM 3483 SG CYS B 199 -42.030 -22.871 1.680 1.00 69.45 S ANISOU 3483 SG CYS B 199 9138 7289 9960 -93 -2004 31 S ATOM 3484 N ASP B 200 -46.569 -22.576 3.116 1.00 89.67 N ANISOU 3484 N ASP B 200 11673 9769 12629 103 -2087 -240 N ATOM 3485 CA ASP B 200 -47.233 -23.041 4.317 1.00 71.23 C ANISOU 3485 CA ASP B 200 9302 7486 10278 168 -2019 -328 C ATOM 3486 C ASP B 200 -47.006 -24.545 4.352 1.00 74.41 C ANISOU 3486 C ASP B 200 9681 7984 10607 166 -1893 -317 C ATOM 3487 O ASP B 200 -47.220 -25.251 3.363 1.00 22.61 O ANISOU 3487 O ASP B 200 3129 1426 4035 143 -1892 -281 O ATOM 3488 CB ASP B 200 -48.724 -22.722 4.232 1.00 73.62 C ANISOU 3488 CB ASP B 200 9603 7730 10641 210 -2106 -390 C ATOM 3489 CG ASP B 200 -49.371 -22.569 5.588 1.00 95.04 C ANISOU 3489 CG ASP B 200 12283 10464 13365 280 -2092 -487 C ATOM 3490 OD1 ASP B 200 -48.869 -23.164 6.567 1.00105.75 O ANISOU 3490 OD1 ASP B 200 13614 11902 14666 298 -1989 -507 O ATOM 3491 OD2 ASP B 200 -50.391 -21.850 5.668 1.00 87.05 O ANISOU 3491 OD2 ASP B 200 11270 9384 12421 318 -2193 -546 O ATOM 3492 N PHE B 201 -46.539 -25.041 5.486 1.00 97.26 N ANISOU 3492 N PHE B 201 12547 10951 13455 190 -1798 -346 N ATOM 3493 CA PHE B 201 -46.089 -26.419 5.538 1.00109.96 C ANISOU 3493 CA PHE B 201 14136 12644 14998 180 -1687 -326 C ATOM 3494 C PHE B 201 -47.253 -27.306 5.908 1.00100.93 C ANISOU 3494 C PHE B 201 12968 11531 13851 218 -1658 -378 C ATOM 3495 O PHE B 201 -47.770 -27.256 7.024 1.00137.99 O ANISOU 3495 O PHE B 201 17639 16243 18549 262 -1649 -441 O ATOM 3496 CB PHE B 201 -44.974 -26.567 6.573 1.00121.02 C ANISOU 3496 CB PHE B 201 15521 14104 16357 184 -1611 -327 C ATOM 3497 CG PHE B 201 -44.188 -27.837 6.449 1.00 87.19 C ANISOU 3497 CG PHE B 201 11223 9892 12013 162 -1514 -291 C ATOM 3498 CD1 PHE B 201 -43.339 -28.033 5.373 1.00 85.38 C ANISOU 3498 CD1 PHE B 201 11009 9659 11771 115 -1514 -223 C ATOM 3499 CD2 PHE B 201 -44.276 -28.822 7.422 1.00 48.23 C ANISOU 3499 CD2 PHE B 201 6260 5024 7041 189 -1436 -324 C ATOM 3500 CE1 PHE B 201 -42.605 -29.192 5.258 1.00 87.04 C ANISOU 3500 CE1 PHE B 201 11206 9932 11935 101 -1436 -198 C ATOM 3501 CE2 PHE B 201 -43.542 -29.985 7.314 1.00 50.79 C ANISOU 3501 CE2 PHE B 201 6572 5406 7318 170 -1359 -293 C ATOM 3502 CZ PHE B 201 -42.706 -30.172 6.229 1.00 72.98 C ANISOU 3502 CZ PHE B 201 9397 8213 10118 129 -1357 -234 C ATOM 3503 N VAL B 202 -47.660 -28.128 4.958 1.00 40.29 N ANISOU 3503 N VAL B 202 5291 3852 6164 201 -1653 -354 N ATOM 3504 CA VAL B 202 -48.716 -29.082 5.203 1.00 41.46 C ANISOU 3504 CA VAL B 202 5414 4026 6312 229 -1628 -393 C ATOM 3505 C VAL B 202 -48.175 -30.417 4.759 1.00 57.09 C ANISOU 3505 C VAL B 202 7387 6062 8242 204 -1548 -353 C ATOM 3506 O VAL B 202 -47.592 -30.526 3.682 1.00 72.55 O ANISOU 3506 O VAL B 202 9367 8008 10191 171 -1559 -304 O ATOM 3507 CB VAL B 202 -49.989 -28.725 4.423 1.00 60.16 C ANISOU 3507 CB VAL B 202 7794 6323 8742 242 -1727 -414 C ATOM 3508 CG1 VAL B 202 -49.651 -28.384 2.985 1.00 69.90 C ANISOU 3508 CG1 VAL B 202 9065 7504 9991 201 -1790 -354 C ATOM 3509 CG2 VAL B 202 -50.992 -29.860 4.496 1.00 57.00 C ANISOU 3509 CG2 VAL B 202 7366 5947 8343 263 -1703 -443 C ATOM 3510 N THR B 203 -48.341 -31.432 5.596 1.00 48.51 N ANISOU 3510 N THR B 203 6271 5033 7128 221 -1478 -376 N ATOM 3511 CA THR B 203 -47.732 -32.718 5.312 1.00 43.84 C ANISOU 3511 CA THR B 203 5672 4494 6493 199 -1404 -343 C ATOM 3512 C THR B 203 -48.703 -33.882 5.443 1.00 32.74 C ANISOU 3512 C THR B 203 4241 3103 5095 213 -1388 -365 C ATOM 3513 O THR B 203 -49.770 -33.753 6.036 1.00 17.55 O ANISOU 3513 O THR B 203 2300 1162 3206 242 -1423 -409 O ATOM 3514 CB THR B 203 -46.536 -32.957 6.226 1.00 16.28 C ANISOU 3514 CB THR B 203 2170 1060 2957 193 -1331 -331 C ATOM 3515 OG1 THR B 203 -46.920 -32.654 7.569 1.00 40.89 O ANISOU 3515 OG1 THR B 203 5267 4188 6081 226 -1330 -378 O ATOM 3516 CG2 THR B 203 -45.391 -32.061 5.826 1.00 16.34 C ANISOU 3516 CG2 THR B 203 2199 1052 2957 169 -1344 -295 C ATOM 3517 N ASN B 204 -48.305 -35.020 4.885 1.00 21.61 N ANISOU 3517 N ASN B 204 2829 1722 3659 194 -1344 -337 N ATOM 3518 CA ASN B 204 -49.091 -36.241 4.934 1.00 36.71 C ANISOU 3518 CA ASN B 204 4720 3646 5584 201 -1331 -349 C ATOM 3519 C ASN B 204 -49.201 -36.775 6.348 1.00 41.42 C ANISOU 3519 C ASN B 204 5283 4278 6175 214 -1292 -368 C ATOM 3520 O ASN B 204 -48.499 -36.328 7.248 1.00 15.63 O ANISOU 3520 O ASN B 204 2015 1039 2886 218 -1265 -372 O ATOM 3521 CB ASN B 204 -48.527 -37.311 3.992 1.00 41.57 C ANISOU 3521 CB ASN B 204 5340 4278 6175 181 -1301 -319 C ATOM 3522 CG ASN B 204 -47.018 -37.355 3.998 1.00 39.05 C ANISOU 3522 CG ASN B 204 5030 3999 5810 164 -1248 -288 C ATOM 3523 OD1 ASN B 204 -46.402 -37.886 4.921 1.00 26.18 O ANISOU 3523 OD1 ASN B 204 3382 2412 4153 161 -1191 -285 O ATOM 3524 ND2 ASN B 204 -46.411 -36.799 2.959 1.00 37.98 N ANISOU 3524 ND2 ASN B 204 4921 3840 5670 151 -1280 -265 N ATOM 3525 N ARG B 205 -50.131 -37.696 6.547 1.00 74.79 N ANISOU 3525 N ARG B 205 9486 8499 10433 221 -1303 -382 N ATOM 3526 CA ARG B 205 -50.333 -38.291 7.855 1.00 90.33 C ANISOU 3526 CA ARG B 205 11419 10489 12412 232 -1287 -397 C ATOM 3527 C ARG B 205 -49.006 -38.660 8.531 1.00 65.04 C ANISOU 3527 C ARG B 205 8216 7337 9161 217 -1221 -371 C ATOM 3528 O ARG B 205 -48.650 -38.073 9.557 1.00 16.12 O ANISOU 3528 O ARG B 205 2013 1156 2955 234 -1219 -390 O ATOM 3529 CB ARG B 205 -51.268 -39.512 7.752 1.00124.87 C ANISOU 3529 CB ARG B 205 15766 14846 16832 228 -1306 -396 C ATOM 3530 CG ARG B 205 -50.700 -40.757 7.050 1.00112.58 C ANISOU 3530 CG ARG B 205 14213 13306 15255 198 -1263 -355 C ATOM 3531 CD ARG B 205 -50.644 -40.634 5.528 1.00113.94 C ANISOU 3531 CD ARG B 205 14416 13460 15415 193 -1278 -348 C ATOM 3532 NE ARG B 205 -50.076 -41.841 4.926 1.00104.92 N ANISOU 3532 NE ARG B 205 13274 12333 14256 176 -1245 -325 N ATOM 3533 CZ ARG B 205 -50.794 -42.819 4.380 1.00 82.33 C ANISOU 3533 CZ ARG B 205 10401 9446 11433 175 -1273 -328 C ATOM 3534 NH1 ARG B 205 -50.188 -43.885 3.867 1.00 52.89 N ANISOU 3534 NH1 ARG B 205 6674 5731 7691 166 -1248 -315 N ATOM 3535 NH2 ARG B 205 -52.117 -42.729 4.344 1.00 70.84 N ANISOU 3535 NH2 ARG B 205 8931 7947 10037 188 -1332 -350 N ATOM 3536 N ALA B 206 -48.275 -39.605 7.934 1.00 75.63 N ANISOU 3536 N ALA B 206 9562 8698 10475 190 -1178 -334 N ATOM 3537 CA ALA B 206 -47.103 -40.232 8.559 1.00 64.25 C ANISOU 3537 CA ALA B 206 8113 7298 9002 176 -1125 -309 C ATOM 3538 C ALA B 206 -45.773 -39.461 8.495 1.00 52.10 C ANISOU 3538 C ALA B 206 6596 5784 7416 171 -1094 -296 C ATOM 3539 O ALA B 206 -44.837 -39.801 9.213 1.00 57.38 O ANISOU 3539 O ALA B 206 7256 6482 8064 166 -1061 -284 O ATOM 3540 CB ALA B 206 -46.920 -41.655 8.032 1.00 68.20 C ANISOU 3540 CB ALA B 206 8605 7804 9505 157 -1104 -284 C ATOM 3541 N TYR B 207 -45.662 -38.453 7.636 1.00 40.08 N ANISOU 3541 N TYR B 207 5100 4243 5887 170 -1113 -296 N ATOM 3542 CA TYR B 207 -44.493 -37.585 7.712 1.00 13.44 C ANISOU 3542 CA TYR B 207 1741 880 2484 164 -1098 -283 C ATOM 3543 C TYR B 207 -44.682 -36.652 8.906 1.00 48.88 C ANISOU 3543 C TYR B 207 6224 5367 6983 187 -1116 -313 C ATOM 3544 O TYR B 207 -43.723 -36.213 9.539 1.00 13.38 O ANISOU 3544 O TYR B 207 1729 889 2467 189 -1100 -310 O ATOM 3545 CB TYR B 207 -44.299 -36.786 6.430 1.00 13.80 C ANISOU 3545 CB TYR B 207 1814 895 2534 153 -1131 -267 C ATOM 3546 CG TYR B 207 -43.068 -35.912 6.460 1.00 54.58 C ANISOU 3546 CG TYR B 207 6992 6064 7682 141 -1127 -246 C ATOM 3547 CD1 TYR B 207 -41.867 -36.354 5.923 1.00 67.83 C ANISOU 3547 CD1 TYR B 207 8673 7762 9337 124 -1103 -215 C ATOM 3548 CD2 TYR B 207 -43.098 -34.651 7.041 1.00 49.37 C ANISOU 3548 CD2 TYR B 207 6340 5384 7036 151 -1157 -259 C ATOM 3549 CE1 TYR B 207 -40.731 -35.558 5.956 1.00 56.93 C ANISOU 3549 CE1 TYR B 207 7302 6380 7950 110 -1109 -192 C ATOM 3550 CE2 TYR B 207 -41.966 -33.850 7.079 1.00 44.00 C ANISOU 3550 CE2 TYR B 207 5670 4699 6348 137 -1162 -237 C ATOM 3551 CZ TYR B 207 -40.789 -34.311 6.534 1.00 49.81 C ANISOU 3551 CZ TYR B 207 6407 5455 7063 114 -1138 -200 C ATOM 3552 OH TYR B 207 -39.667 -33.525 6.563 1.00 53.26 O ANISOU 3552 OH TYR B 207 6852 5884 7500 98 -1152 -173 O ATOM 3553 N ALA B 208 -45.941 -36.404 9.244 1.00 55.64 N ANISOU 3553 N ALA B 208 7071 6198 7873 211 -1159 -349 N ATOM 3554 CA ALA B 208 -46.286 -35.558 10.378 1.00 43.91 C ANISOU 3554 CA ALA B 208 5575 4706 6402 246 -1191 -396 C ATOM 3555 C ALA B 208 -46.198 -36.392 11.647 1.00 22.87 C ANISOU 3555 C ALA B 208 2881 2074 3734 262 -1174 -412 C ATOM 3556 O ALA B 208 -46.556 -35.943 12.731 1.00 46.96 O ANISOU 3556 O ALA B 208 5917 5128 6799 303 -1207 -464 O ATOM 3557 CB ALA B 208 -47.682 -34.977 10.208 1.00 76.96 C ANISOU 3557 CB ALA B 208 9758 8849 10634 272 -1256 -438 C ATOM 3558 N ILE B 209 -45.752 -37.631 11.487 1.00 15.86 N ANISOU 3558 N ILE B 209 1984 1207 2835 234 -1134 -373 N ATOM 3559 CA ILE B 209 -45.420 -38.502 12.608 1.00 38.63 C ANISOU 3559 CA ILE B 209 4841 4114 5723 240 -1124 -373 C ATOM 3560 C ILE B 209 -43.902 -38.700 12.729 1.00 34.18 C ANISOU 3560 C ILE B 209 4285 3580 5120 221 -1079 -341 C ATOM 3561 O ILE B 209 -43.290 -38.360 13.753 1.00 22.53 O ANISOU 3561 O ILE B 209 2804 2120 3635 242 -1085 -362 O ATOM 3562 CB ILE B 209 -46.085 -39.867 12.448 1.00 50.34 C ANISOU 3562 CB ILE B 209 6300 5584 7243 220 -1128 -348 C ATOM 3563 CG1 ILE B 209 -47.607 -39.716 12.510 1.00 60.87 C ANISOU 3563 CG1 ILE B 209 7617 6883 8629 243 -1185 -385 C ATOM 3564 CG2 ILE B 209 -45.556 -40.838 13.501 1.00 37.05 C ANISOU 3564 CG2 ILE B 209 4588 3912 5577 213 -1126 -328 C ATOM 3565 CD1 ILE B 209 -48.354 -40.973 12.139 1.00 87.38 C ANISOU 3565 CD1 ILE B 209 10950 10217 12034 219 -1196 -355 C ATOM 3566 N ALA B 210 -43.317 -39.284 11.684 1.00 37.17 N ANISOU 3566 N ALA B 210 4676 3965 5481 188 -1043 -299 N ATOM 3567 CA ALA B 210 -41.873 -39.487 11.581 1.00 44.29 C ANISOU 3567 CA ALA B 210 5584 4892 6352 171 -1007 -271 C ATOM 3568 C ALA B 210 -41.105 -38.214 11.904 1.00 57.09 C ANISOU 3568 C ALA B 210 7220 6517 7953 184 -1012 -284 C ATOM 3569 O ALA B 210 -40.167 -38.218 12.715 1.00 53.35 O ANISOU 3569 O ALA B 210 6739 6061 7470 190 -1005 -285 O ATOM 3570 CB ALA B 210 -41.519 -39.961 10.179 1.00 26.69 C ANISOU 3570 CB ALA B 210 3369 2663 4108 149 -985 -244 C ATOM 3571 N SER B 211 -41.521 -37.122 11.272 1.00 57.27 N ANISOU 3571 N SER B 211 7263 6517 7980 187 -1033 -293 N ATOM 3572 CA SER B 211 -40.834 -35.860 11.426 1.00 47.99 C ANISOU 3572 CA SER B 211 6102 5332 6799 193 -1048 -299 C ATOM 3573 C SER B 211 -40.622 -35.640 12.909 1.00 48.85 C ANISOU 3573 C SER B 211 6197 5457 6907 226 -1060 -337 C ATOM 3574 O SER B 211 -39.485 -35.519 13.360 1.00 47.50 O ANISOU 3574 O SER B 211 6026 5301 6722 226 -1050 -330 O ATOM 3575 CB SER B 211 -41.695 -34.734 10.842 1.00 69.84 C ANISOU 3575 CB SER B 211 8887 8059 9589 199 -1092 -314 C ATOM 3576 OG SER B 211 -41.098 -33.456 10.999 1.00 86.36 O ANISOU 3576 OG SER B 211 10994 10131 11688 203 -1120 -317 O ATOM 3577 N SER B 212 -41.720 -35.672 13.667 1.00 57.24 N ANISOU 3577 N SER B 212 7245 6515 7987 260 -1089 -383 N ATOM 3578 CA SER B 212 -41.739 -35.278 15.081 1.00 66.54 C ANISOU 3578 CA SER B 212 8410 7709 9165 312 -1119 -445 C ATOM 3579 C SER B 212 -41.055 -36.264 16.017 1.00 57.97 C ANISOU 3579 C SER B 212 7287 6695 8043 319 -1084 -423 C ATOM 3580 O SER B 212 -40.279 -35.866 16.888 1.00 24.99 O ANISOU 3580 O SER B 212 3086 2595 3815 345 -1063 -419 O ATOM 3581 CB SER B 212 -43.177 -35.058 15.541 1.00 66.95 C ANISOU 3581 CB SER B 212 8446 7750 9241 356 -1165 -506 C ATOM 3582 OG SER B 212 -43.862 -34.219 14.628 1.00 86.20 O ANISOU 3582 OG SER B 212 10903 10151 11699 346 -1186 -503 O ATOM 3583 N ILE B 213 -41.358 -37.548 15.848 1.00 62.51 N ANISOU 3583 N ILE B 213 7833 7309 8610 293 -1050 -368 N ATOM 3584 CA ILE B 213 -40.647 -38.574 16.598 1.00 36.06 C ANISOU 3584 CA ILE B 213 4423 4087 5193 287 -984 -292 C ATOM 3585 C ILE B 213 -39.150 -38.365 16.468 1.00 29.21 C ANISOU 3585 C ILE B 213 3569 3228 4301 272 -960 -272 C ATOM 3586 O ILE B 213 -38.465 -38.086 17.449 1.00 12.18 O ANISOU 3586 O ILE B 213 1376 1167 2086 298 -935 -256 O ATOM 3587 CB ILE B 213 -40.972 -39.978 16.103 1.00 12.84 C ANISOU 3587 CB ILE B 213 1465 1141 2273 250 -966 -238 C ATOM 3588 CG1 ILE B 213 -42.120 -40.567 16.924 1.00109.84 C ANISOU 3588 CG1 ILE B 213 13684 13509 14540 271 -960 -205 C ATOM 3589 CG2 ILE B 213 -39.749 -40.868 16.216 1.00 11.87 C ANISOU 3589 CG2 ILE B 213 1318 1079 2114 228 -918 -175 C ATOM 3590 CD1 ILE B 213 -42.398 -42.029 16.631 1.00108.35 C ANISOU 3590 CD1 ILE B 213 13468 13321 14378 235 -946 -141 C ATOM 3591 N ILE B 214 -38.645 -38.489 15.246 1.00 48.00 N ANISOU 3591 N ILE B 214 5996 5518 6724 232 -970 -271 N ATOM 3592 CA ILE B 214 -37.203 -38.426 15.040 1.00 67.13 C ANISOU 3592 CA ILE B 214 8420 7964 9121 217 -944 -241 C ATOM 3593 C ILE B 214 -36.581 -37.089 15.438 1.00 66.97 C ANISOU 3593 C ILE B 214 8413 7940 9094 238 -965 -268 C ATOM 3594 O ILE B 214 -35.767 -37.035 16.355 1.00 11.66 O ANISOU 3594 O ILE B 214 1368 1030 2033 257 -935 -245 O ATOM 3595 CB ILE B 214 -36.816 -38.779 13.581 1.00 47.50 C ANISOU 3595 CB ILE B 214 5973 5400 6676 178 -954 -232 C ATOM 3596 CG1 ILE B 214 -36.876 -40.302 13.384 1.00 39.47 C ANISOU 3596 CG1 ILE B 214 4929 4415 5652 162 -924 -197 C ATOM 3597 CG2 ILE B 214 -35.426 -38.234 13.255 1.00 10.97 C ANISOU 3597 CG2 ILE B 214 1350 789 2030 168 -944 -210 C ATOM 3598 CD1 ILE B 214 -37.482 -40.768 12.076 1.00 10.87 C ANISOU 3598 CD1 ILE B 214 1338 719 2072 141 -943 -209 C ATOM 3599 N SER B 215 -37.005 -36.009 14.792 1.00 67.48 N ANISOU 3599 N SER B 215 8530 7890 9218 235 -1025 -316 N ATOM 3600 CA SER B 215 -36.291 -34.741 14.904 1.00 61.12 C ANISOU 3600 CA SER B 215 7745 7050 8427 243 -1059 -333 C ATOM 3601 C SER B 215 -36.658 -33.934 16.160 1.00 36.75 C ANISOU 3601 C SER B 215 4643 3998 5322 298 -1081 -388 C ATOM 3602 O SER B 215 -36.088 -32.872 16.400 1.00 12.98 O ANISOU 3602 O SER B 215 1647 957 2328 312 -1118 -411 O ATOM 3603 CB SER B 215 -36.473 -33.901 13.628 1.00 67.26 C ANISOU 3603 CB SER B 215 8546 7795 9216 210 -1066 -298 C ATOM 3604 OG SER B 215 -36.108 -34.619 12.455 1.00 33.73 O ANISOU 3604 OG SER B 215 4301 3553 4963 171 -1038 -247 O ATOM 3605 N PHE B 216 -37.612 -34.424 16.949 1.00 12.80 N ANISOU 3605 N PHE B 216 1575 1033 2255 333 -1064 -408 N ATOM 3606 CA PHE B 216 -37.937 -33.780 18.231 1.00 64.17 C ANISOU 3606 CA PHE B 216 8049 7608 8723 397 -1077 -460 C ATOM 3607 C PHE B 216 -38.023 -34.701 19.445 1.00 57.50 C ANISOU 3607 C PHE B 216 7124 6938 7787 425 -1016 -415 C ATOM 3608 O PHE B 216 -37.316 -34.511 20.437 1.00 83.17 O ANISOU 3608 O PHE B 216 10333 10289 10978 454 -995 -404 O ATOM 3609 CB PHE B 216 -39.205 -32.932 18.157 1.00 67.58 C ANISOU 3609 CB PHE B 216 8513 7954 9210 434 -1147 -549 C ATOM 3610 CG PHE B 216 -39.457 -32.095 19.401 1.00 62.44 C ANISOU 3610 CG PHE B 216 7833 7365 8525 511 -1173 -623 C ATOM 3611 CD1 PHE B 216 -39.208 -30.727 19.396 1.00 65.59 C ANISOU 3611 CD1 PHE B 216 8277 7664 8980 539 -1247 -700 C ATOM 3612 CD2 PHE B 216 -39.946 -32.673 20.565 1.00 57.58 C ANISOU 3612 CD2 PHE B 216 7144 6910 7825 556 -1129 -614 C ATOM 3613 CE1 PHE B 216 -39.446 -29.950 20.520 1.00 51.82 C ANISOU 3613 CE1 PHE B 216 6509 5973 7209 618 -1278 -787 C ATOM 3614 CE2 PHE B 216 -40.183 -31.902 21.695 1.00 82.28 C ANISOU 3614 CE2 PHE B 216 10241 10107 10914 633 -1153 -691 C ATOM 3615 CZ PHE B 216 -39.932 -30.538 21.671 1.00 70.51 C ANISOU 3615 CZ PHE B 216 8800 8511 9480 669 -1227 -789 C ATOM 3616 N TYR B 217 -38.932 -35.666 19.388 1.00 27.78 N ANISOU 3616 N TYR B 217 3332 3209 4014 416 -993 -381 N ATOM 3617 CA TYR B 217 -39.330 -36.359 20.604 1.00 49.30 C ANISOU 3617 CA TYR B 217 5973 6098 6662 447 -953 -332 C ATOM 3618 C TYR B 217 -38.248 -37.263 21.169 1.00 32.51 C ANISOU 3618 C TYR B 217 3791 4090 4472 428 -894 -234 C ATOM 3619 O TYR B 217 -37.709 -36.984 22.235 1.00 42.29 O ANISOU 3619 O TYR B 217 4984 5433 5650 460 -880 -221 O ATOM 3620 CB TYR B 217 -40.658 -37.100 20.420 1.00 52.49 C ANISOU 3620 CB TYR B 217 6353 6509 7083 442 -954 -311 C ATOM 3621 CG TYR B 217 -41.813 -36.275 20.921 1.00 68.84 C ANISOU 3621 CG TYR B 217 8412 8588 9156 500 -997 -390 C ATOM 3622 CD1 TYR B 217 -42.166 -36.292 22.266 1.00 86.83 C ANISOU 3622 CD1 TYR B 217 10608 11025 11357 552 -978 -372 C ATOM 3623 CD2 TYR B 217 -42.521 -35.443 20.064 1.00 51.56 C ANISOU 3623 CD2 TYR B 217 6291 6251 7047 506 -1062 -483 C ATOM 3624 CE1 TYR B 217 -43.207 -35.524 22.740 1.00103.33 C ANISOU 3624 CE1 TYR B 217 12684 13133 13445 615 -1018 -458 C ATOM 3625 CE2 TYR B 217 -43.562 -34.671 20.526 1.00 66.07 C ANISOU 3625 CE2 TYR B 217 8117 8096 8892 567 -1108 -568 C ATOM 3626 CZ TYR B 217 -43.903 -34.715 21.863 1.00105.64 C ANISOU 3626 CZ TYR B 217 13045 13273 13820 625 -1084 -562 C ATOM 3627 OH TYR B 217 -44.944 -33.944 22.321 1.00122.81 O ANISOU 3627 OH TYR B 217 15202 15464 15998 694 -1132 -659 O ATOM 3628 N ILE B 218 -37.897 -38.330 20.474 1.00 39.44 N ANISOU 3628 N ILE B 218 4687 3686 6613 1078 -1374 -240 N ATOM 3629 CA ILE B 218 -36.922 -39.226 21.071 1.00 55.94 C ANISOU 3629 CA ILE B 218 6770 5732 8753 1108 -1449 -237 C ATOM 3630 C ILE B 218 -35.634 -38.505 21.528 1.00 59.31 C ANISOU 3630 C ILE B 218 7176 6173 9187 1120 -1497 -261 C ATOM 3631 O ILE B 218 -35.177 -38.740 22.639 1.00 78.40 O ANISOU 3631 O ILE B 218 9619 8568 11602 1143 -1555 -217 O ATOM 3632 CB ILE B 218 -36.671 -40.498 20.227 1.00 49.40 C ANISOU 3632 CB ILE B 218 5891 4864 8013 1115 -1463 -277 C ATOM 3633 CG1 ILE B 218 -36.862 -41.737 21.106 1.00 61.28 C ANISOU 3633 CG1 ILE B 218 7424 6303 9557 1137 -1516 -215 C ATOM 3634 CG2 ILE B 218 -35.297 -40.469 19.590 1.00 30.59 C ANISOU 3634 CG2 ILE B 218 3435 2484 5702 1122 -1496 -355 C ATOM 3635 CD1 ILE B 218 -36.882 -43.046 20.343 1.00 82.92 C ANISOU 3635 CD1 ILE B 218 10112 8992 12402 1142 -1524 -252 C ATOM 3636 N PRO B 219 -35.070 -37.597 20.706 1.00 56.66 N ANISOU 3636 N PRO B 219 6794 5878 8857 1104 -1473 -320 N ATOM 3637 CA PRO B 219 -33.874 -36.925 21.229 1.00 66.19 C ANISOU 3637 CA PRO B 219 7986 7095 10068 1116 -1519 -341 C ATOM 3638 C PRO B 219 -34.172 -36.068 22.456 1.00106.57 C ANISOU 3638 C PRO B 219 13149 12224 15120 1122 -1523 -296 C ATOM 3639 O PRO B 219 -33.320 -35.977 23.335 1.00137.78 O ANISOU 3639 O PRO B 219 17107 16172 19073 1144 -1579 -285 O ATOM 3640 CB PRO B 219 -33.393 -36.057 20.054 1.00 29.14 C ANISOU 3640 CB PRO B 219 3235 2447 5391 1092 -1485 -404 C ATOM 3641 CG PRO B 219 -34.542 -35.942 19.161 1.00 32.65 C ANISOU 3641 CG PRO B 219 3674 2913 5819 1064 -1418 -395 C ATOM 3642 CD PRO B 219 -35.365 -37.189 19.324 1.00 55.06 C ANISOU 3642 CD PRO B 219 6545 5713 8663 1075 -1416 -364 C ATOM 3643 N LEU B 220 -35.352 -35.461 22.529 1.00 91.66 N ANISOU 3643 N LEU B 220 11288 10353 13186 1102 -1465 -274 N ATOM 3644 CA LEU B 220 -35.701 -34.667 23.703 1.00 74.04 C ANISOU 3644 CA LEU B 220 9091 8131 10908 1110 -1465 -249 C ATOM 3645 C LEU B 220 -35.809 -35.536 24.946 1.00 62.76 C ANISOU 3645 C LEU B 220 7709 6662 9474 1139 -1551 -198 C ATOM 3646 O LEU B 220 -35.171 -35.262 25.954 1.00 43.30 O ANISOU 3646 O LEU B 220 5248 4186 7017 1160 -1641 -201 O ATOM 3647 CB LEU B 220 -37.020 -33.925 23.507 1.00 65.08 C ANISOU 3647 CB LEU B 220 7967 7008 9753 1082 -1391 -243 C ATOM 3648 CG LEU B 220 -37.667 -33.604 24.858 1.00 69.26 C ANISOU 3648 CG LEU B 220 8535 7506 10276 1097 -1442 -239 C ATOM 3649 CD1 LEU B 220 -36.837 -32.568 25.596 1.00 60.91 C ANISOU 3649 CD1 LEU B 220 7448 6447 9247 1111 -1506 -296 C ATOM 3650 CD2 LEU B 220 -39.114 -33.148 24.706 1.00 84.09 C ANISOU 3650 CD2 LEU B 220 10425 9377 12147 1072 -1369 -232 C ATOM 3651 N LEU B 221 -36.634 -36.575 24.870 1.00 64.38 N ANISOU 3651 N LEU B 221 7945 6845 9670 1138 -1533 -148 N ATOM 3652 CA LEU B 221 -36.881 -37.446 26.009 1.00 73.45 C ANISOU 3652 CA LEU B 221 9137 7953 10819 1157 -1623 -79 C ATOM 3653 C LEU B 221 -35.572 -38.093 26.419 1.00 78.18 C ANISOU 3653 C LEU B 221 9711 8529 11465 1180 -1718 -56 C ATOM 3654 O LEU B 221 -35.366 -38.435 27.585 1.00 69.72 O ANISOU 3654 O LEU B 221 8659 7434 10396 1193 -1831 8 O ATOM 3655 CB LEU B 221 -37.911 -38.516 25.650 1.00 45.43 C ANISOU 3655 CB LEU B 221 5615 4383 7263 1149 -1577 -30 C ATOM 3656 CG LEU B 221 -39.171 -37.974 24.973 1.00 55.49 C ANISOU 3656 CG LEU B 221 6904 5682 8496 1123 -1467 -51 C ATOM 3657 CD1 LEU B 221 -40.173 -39.093 24.738 1.00 92.32 C ANISOU 3657 CD1 LEU B 221 11600 10326 13152 1118 -1431 0 C ATOM 3658 CD2 LEU B 221 -39.792 -36.850 25.793 1.00 32.51 C ANISOU 3658 CD2 LEU B 221 4018 2774 5561 1118 -1483 -68 C ATOM 3659 N ILE B 222 -34.684 -38.243 25.443 1.00 67.96 N ANISOU 3659 N ILE B 222 8366 7242 10212 1180 -1681 -103 N ATOM 3660 CA ILE B 222 -33.384 -38.841 25.687 1.00 58.25 C ANISOU 3660 CA ILE B 222 7101 5984 9047 1200 -1762 -93 C ATOM 3661 C ILE B 222 -32.459 -37.864 26.393 1.00 47.31 C ANISOU 3661 C ILE B 222 5706 4620 7649 1210 -1827 -114 C ATOM 3662 O ILE B 222 -31.737 -38.260 27.292 1.00 83.76 O ANISOU 3662 O ILE B 222 10317 9213 12295 1226 -1933 -61 O ATOM 3663 CB ILE B 222 -32.729 -39.390 24.388 1.00 83.32 C ANISOU 3663 CB ILE B 222 10216 9139 12304 1197 -1734 -163 C ATOM 3664 CG1 ILE B 222 -33.406 -40.700 23.949 1.00 78.78 C ANISOU 3664 CG1 ILE B 222 9634 8509 11788 1195 -1731 -144 C ATOM 3665 CG2 ILE B 222 -31.225 -39.580 24.560 1.00 33.57 C ANISOU 3665 CG2 ILE B 222 3867 2814 6075 1215 -1808 -181 C ATOM 3666 CD1 ILE B 222 -33.676 -41.701 25.071 1.00 54.23 C ANISOU 3666 CD1 ILE B 222 6554 5354 8696 1208 -1798 -31 C ATOM 3667 N MET B 223 -32.471 -36.595 26.006 1.00 32.00 N ANISOU 3667 N MET B 223 3758 2726 5675 1198 -1769 -184 N ATOM 3668 CA MET B 223 -31.556 -35.643 26.630 1.00 37.97 C ANISOU 3668 CA MET B 223 4498 3501 6428 1209 -1828 -217 C ATOM 3669 C MET B 223 -32.082 -35.086 27.954 1.00 65.32 C ANISOU 3669 C MET B 223 7996 6965 9857 1220 -1910 -197 C ATOM 3670 O MET B 223 -31.309 -34.580 28.759 1.00 76.07 O ANISOU 3670 O MET B 223 9344 8337 11221 1236 -1999 -209 O ATOM 3671 CB MET B 223 -31.173 -34.514 25.673 1.00 31.34 C ANISOU 3671 CB MET B 223 3621 2703 5585 1190 -1747 -300 C ATOM 3672 CG MET B 223 -32.267 -33.510 25.463 1.00 30.44 C ANISOU 3672 CG MET B 223 3515 2611 5440 1166 -1676 -326 C ATOM 3673 SD MET B 223 -31.613 -31.841 25.364 1.00 40.94 S ANISOU 3673 SD MET B 223 4798 3974 6784 1155 -1660 -403 S ATOM 3674 CE MET B 223 -33.139 -30.897 25.290 1.00121.28 C ANISOU 3674 CE MET B 223 14974 14148 16957 1126 -1587 -416 C ATOM 3675 N ILE B 224 -33.392 -35.165 28.169 1.00 64.98 N ANISOU 3675 N ILE B 224 7992 6912 9785 1211 -1888 -174 N ATOM 3676 CA ILE B 224 -33.987 -34.838 29.463 1.00 68.74 C ANISOU 3676 CA ILE B 224 8499 7385 10233 1223 -1990 -155 C ATOM 3677 C ILE B 224 -33.779 -36.012 30.405 1.00 76.02 C ANISOU 3677 C ILE B 224 9445 8293 11146 1228 -2120 -33 C ATOM 3678 O ILE B 224 -33.397 -35.841 31.569 1.00 67.29 O ANISOU 3678 O ILE B 224 8339 7214 10013 1233 -2263 8 O ATOM 3679 CB ILE B 224 -35.485 -34.536 29.343 1.00 63.42 C ANISOU 3679 CB ILE B 224 7856 6700 9539 1209 -1923 -174 C ATOM 3680 CG1 ILE B 224 -35.708 -33.024 29.304 1.00 77.71 C ANISOU 3680 CG1 ILE B 224 9632 8522 11374 1208 -1882 -286 C ATOM 3681 CG2 ILE B 224 -36.248 -35.157 30.510 1.00 33.58 C ANISOU 3681 CG2 ILE B 224 4128 2906 5726 1216 -2041 -95 C ATOM 3682 CD1 ILE B 224 -34.785 -32.285 28.352 1.00 31.34 C ANISOU 3682 CD1 ILE B 224 3703 2676 5527 1194 -1803 -344 C ATOM 3683 N PHE B 225 -34.035 -37.207 29.879 1.00 79.50 N ANISOU 3683 N PHE B 225 9895 8702 11608 1218 -2076 32 N ATOM 3684 CA PHE B 225 -33.692 -38.451 30.554 1.00 81.60 C ANISOU 3684 CA PHE B 225 10163 8944 11896 1214 -2183 160 C ATOM 3685 C PHE B 225 -32.227 -38.416 31.017 1.00 88.14 C ANISOU 3685 C PHE B 225 10947 9784 12758 1224 -2279 183 C ATOM 3686 O PHE B 225 -31.931 -38.723 32.171 1.00 38.56 O ANISOU 3686 O PHE B 225 4668 3528 6456 1209 -2425 294 O ATOM 3687 CB PHE B 225 -33.969 -39.632 29.610 1.00 90.85 C ANISOU 3687 CB PHE B 225 11325 10069 13124 1211 -2099 180 C ATOM 3688 CG PHE B 225 -33.457 -40.963 30.099 1.00113.68 C ANISOU 3688 CG PHE B 225 14193 12917 16083 1208 -2197 298 C ATOM 3689 CD1 PHE B 225 -34.265 -41.804 30.853 1.00115.49 C ANISOU 3689 CD1 PHE B 225 14454 13130 16298 1186 -2267 424 C ATOM 3690 CD2 PHE B 225 -32.181 -41.394 29.762 1.00113.36 C ANISOU 3690 CD2 PHE B 225 14092 12845 16133 1221 -2219 287 C ATOM 3691 CE1 PHE B 225 -33.798 -43.035 31.284 1.00115.85 C ANISOU 3691 CE1 PHE B 225 14465 13129 16425 1174 -2359 544 C ATOM 3692 CE2 PHE B 225 -31.709 -42.622 30.190 1.00104.86 C ANISOU 3692 CE2 PHE B 225 12981 11713 15149 1216 -2312 395 C ATOM 3693 CZ PHE B 225 -32.517 -43.443 30.951 1.00114.35 C ANISOU 3693 CZ PHE B 225 14208 12898 16343 1191 -2383 528 C ATOM 3694 N VAL B 226 -31.324 -38.007 30.123 1.00 98.38 N ANISOU 3694 N VAL B 226 12204 11079 14098 1238 -2204 88 N ATOM 3695 CA VAL B 226 -29.878 -37.979 30.399 1.00 97.37 C ANISOU 3695 CA VAL B 226 12031 10955 14012 1250 -2277 96 C ATOM 3696 C VAL B 226 -29.442 -36.779 31.250 1.00 72.67 C ANISOU 3696 C VAL B 226 8900 7885 10828 1255 -2354 64 C ATOM 3697 O VAL B 226 -28.452 -36.845 31.980 1.00 72.75 O ANISOU 3697 O VAL B 226 8882 7916 10845 1256 -2464 119 O ATOM 3698 CB VAL B 226 -29.036 -38.068 29.085 1.00 36.60 C ANISOU 3698 CB VAL B 226 4288 3236 6383 1259 -2179 5 C ATOM 3699 CG1 VAL B 226 -27.562 -37.813 29.352 1.00 37.34 C ANISOU 3699 CG1 VAL B 226 4338 3334 6515 1272 -2245 -5 C ATOM 3700 CG2 VAL B 226 -29.212 -39.430 28.440 1.00 36.92 C ANISOU 3700 CG2 VAL B 226 4310 3217 6501 1257 -2150 39 C ATOM 3701 N ALA B 227 -30.186 -35.684 31.164 1.00 48.13 N ANISOU 3701 N ALA B 227 5811 4804 7674 1257 -2302 -27 N ATOM 3702 CA ALA B 227 -29.948 -34.550 32.042 1.00 68.85 C ANISOU 3702 CA ALA B 227 8421 7482 10256 1266 -2388 -78 C ATOM 3703 C ALA B 227 -30.212 -34.991 33.471 1.00 91.87 C ANISOU 3703 C ALA B 227 11350 10453 13102 1243 -2565 44 C ATOM 3704 O ALA B 227 -29.471 -34.644 34.394 1.00 91.90 O ANISOU 3704 O ALA B 227 11322 10536 13060 1230 -2694 71 O ATOM 3705 CB ALA B 227 -30.859 -33.396 31.677 1.00 80.43 C ANISOU 3705 CB ALA B 227 9892 8951 11718 1272 -2301 -203 C ATOM 3706 N LEU B 228 -31.271 -35.777 33.644 1.00104.84 N ANISOU 3706 N LEU B 228 13035 12079 14719 1222 -2575 131 N ATOM 3707 CA LEU B 228 -31.684 -36.194 34.981 1.00100.04 C ANISOU 3707 CA LEU B 228 12441 11558 14012 1169 -2749 268 C ATOM 3708 C LEU B 228 -30.619 -36.914 35.810 1.00110.72 C ANISOU 3708 C LEU B 228 13758 12971 15338 1122 -2887 426 C ATOM 3709 O LEU B 228 -30.277 -36.447 36.893 1.00122.48 O ANISOU 3709 O LEU B 228 15220 14603 16715 1064 -3033 465 O ATOM 3710 CB LEU B 228 -32.966 -37.019 34.920 1.00 87.66 C ANISOU 3710 CB LEU B 228 10928 9953 12427 1147 -2723 346 C ATOM 3711 CG LEU B 228 -34.188 -36.123 34.766 1.00 83.49 C ANISOU 3711 CG LEU B 228 10429 9423 11871 1166 -2671 222 C ATOM 3712 CD1 LEU B 228 -35.372 -36.749 35.481 1.00 93.21 C ANISOU 3712 CD1 LEU B 228 11710 10695 13012 1112 -2756 336 C ATOM 3713 CD2 LEU B 228 -33.872 -34.740 35.329 1.00 39.33 C ANISOU 3713 CD2 LEU B 228 4788 3918 6239 1175 -2748 89 C ATOM 3714 N ARG B 229 -30.092 -38.036 35.321 1.00112.59 N ANISOU 3714 N ARG B 229 13983 13121 15676 1133 -2847 509 N ATOM 3715 CA ARG B 229 -29.099 -38.778 36.103 1.00128.83 C ANISOU 3715 CA ARG B 229 15994 15218 17738 1088 -2979 670 C ATOM 3716 C ARG B 229 -27.880 -37.896 36.405 1.00152.96 C ANISOU 3716 C ARG B 229 19004 18341 20773 1095 -3029 613 C ATOM 3717 O ARG B 229 -27.268 -37.997 37.480 1.00184.12 O ANISOU 3717 O ARG B 229 22914 22404 24640 1027 -3178 739 O ATOM 3718 CB ARG B 229 -28.683 -40.095 35.425 1.00109.19 C ANISOU 3718 CB ARG B 229 13482 12603 15403 1111 -2928 731 C ATOM 3719 CG ARG B 229 -27.938 -41.050 36.368 1.00114.99 C ANISOU 3719 CG ARG B 229 14166 13362 16162 1052 -3082 933 C ATOM 3720 CD ARG B 229 -27.399 -42.310 35.679 1.00128.68 C ANISOU 3720 CD ARG B 229 15854 14951 18087 1081 -3048 965 C ATOM 3721 NE ARG B 229 -26.810 -43.241 36.648 1.00133.89 N ANISOU 3721 NE ARG B 229 16459 15622 18790 1016 -3206 1175 N ATOM 3722 CZ ARG B 229 -26.167 -44.366 36.336 1.00112.88 C ANISOU 3722 CZ ARG B 229 13735 12837 16316 1025 -3227 1231 C ATOM 3723 NH1 ARG B 229 -26.010 -44.724 35.067 1.00108.21 N ANISOU 3723 NH1 ARG B 229 13126 12117 15870 1092 -3103 1082 N ATOM 3724 NH2 ARG B 229 -25.675 -45.136 37.298 1.00 88.04 N ANISOU 3724 NH2 ARG B 229 10534 9703 13214 952 -3383 1436 N ATOM 3725 N VAL B 230 -27.541 -37.018 35.464 1.00123.75 N ANISOU 3725 N VAL B 230 15302 14587 17131 1162 -2905 429 N ATOM 3726 CA VAL B 230 -26.468 -36.055 35.688 1.00105.19 C ANISOU 3726 CA VAL B 230 12910 12296 14762 1174 -2939 352 C ATOM 3727 C VAL B 230 -26.796 -35.129 36.870 1.00 85.86 C ANISOU 3727 C VAL B 230 10448 10016 12157 1118 -3069 339 C ATOM 3728 O VAL B 230 -25.946 -34.904 37.728 1.00114.86 O ANISOU 3728 O VAL B 230 14076 13811 15755 1066 -3188 393 O ATOM 3729 CB VAL B 230 -26.099 -35.263 34.398 1.00 53.63 C ANISOU 3729 CB VAL B 230 6376 5684 8316 1239 -2773 163 C ATOM 3730 CG1 VAL B 230 -25.448 -33.939 34.738 1.00 41.25 C ANISOU 3730 CG1 VAL B 230 4775 4191 6708 1250 -2803 52 C ATOM 3731 CG2 VAL B 230 -25.174 -36.088 33.510 1.00 44.93 C ANISOU 3731 CG2 VAL B 230 5250 4491 7329 1260 -2706 175 C ATOM 3732 N TYR B 231 -28.026 -34.621 36.937 1.00 46.63 N ANISOU 3732 N TYR B 231 5511 5077 7131 1111 -3053 261 N ATOM 3733 CA TYR B 231 -28.413 -33.749 38.054 1.00 76.27 C ANISOU 3733 CA TYR B 231 9234 9026 10720 1030 -3186 204 C ATOM 3734 C TYR B 231 -28.732 -34.506 39.353 1.00102.90 C ANISOU 3734 C TYR B 231 12609 12582 13905 877 -3354 399 C ATOM 3735 O TYR B 231 -28.982 -33.890 40.392 1.00101.97 O ANISOU 3735 O TYR B 231 12460 12692 13592 743 -3469 349 O ATOM 3736 CB TYR B 231 -29.560 -32.805 37.666 1.00 96.68 C ANISOU 3736 CB TYR B 231 11825 11587 13323 1072 -3113 8 C ATOM 3737 CG TYR B 231 -29.158 -31.752 36.653 1.00115.49 C ANISOU 3737 CG TYR B 231 14176 13855 15850 1177 -2966 -185 C ATOM 3738 CD1 TYR B 231 -29.436 -31.917 35.301 1.00118.52 C ANISOU 3738 CD1 TYR B 231 14604 14060 16368 1249 -2778 -217 C ATOM 3739 CD2 TYR B 231 -28.488 -30.598 37.046 1.00109.46 C ANISOU 3739 CD2 TYR B 231 13331 13190 15067 1170 -3007 -337 C ATOM 3740 CE1 TYR B 231 -29.065 -30.963 34.367 1.00 99.19 C ANISOU 3740 CE1 TYR B 231 12129 11543 14017 1296 -2638 -364 C ATOM 3741 CE2 TYR B 231 -28.111 -29.638 36.118 1.00106.99 C ANISOU 3741 CE2 TYR B 231 12987 12770 14893 1253 -2865 -492 C ATOM 3742 CZ TYR B 231 -28.403 -29.827 34.780 1.00 97.75 C ANISOU 3742 CZ TYR B 231 11872 11429 13839 1306 -2682 -491 C ATOM 3743 OH TYR B 231 -28.035 -28.878 33.853 1.00 85.07 O ANISOU 3743 OH TYR B 231 10238 9755 12329 1336 -2542 -617 O ATOM 3744 N ARG B 232 -28.758 -35.835 39.277 1.00114.38 N ANISOU 3744 N ARG B 232 14092 13955 15412 870 -3356 601 N ATOM 3745 CA ARG B 232 -28.803 -36.679 40.468 1.00112.66 C ANISOU 3745 CA ARG B 232 13863 13903 15041 717 -3505 830 C ATOM 3746 C ARG B 232 -27.415 -36.860 41.052 1.00117.36 C ANISOU 3746 C ARG B 232 14394 14580 15618 670 -3592 939 C ATOM 3747 O ARG B 232 -27.235 -36.834 42.270 1.00130.58 O ANISOU 3747 O ARG B 232 16032 16495 17088 504 -3726 1049 O ATOM 3748 CB ARG B 232 -29.407 -38.049 40.160 1.00124.94 C ANISOU 3748 CB ARG B 232 15459 15325 16689 733 -3470 994 C ATOM 3749 CG ARG B 232 -29.002 -39.128 41.161 1.00129.40 C ANISOU 3749 CG ARG B 232 15988 15992 17187 608 -3602 1255 C ATOM 3750 CD ARG B 232 -29.994 -40.274 41.181 1.00120.01 C ANISOU 3750 CD ARG B 232 14837 14739 16023 577 -3597 1401 C ATOM 3751 NE ARG B 232 -29.372 -41.566 40.915 1.00118.64 N ANISOU 3751 NE ARG B 232 14629 14408 16041 613 -3599 1544 N ATOM 3752 CZ ARG B 232 -29.963 -42.728 41.161 1.00136.16 C ANISOU 3752 CZ ARG B 232 16853 16587 18295 559 -3632 1711 C ATOM 3753 NH1 ARG B 232 -31.180 -42.749 41.685 1.00149.69 N ANISOU 3753 NH1 ARG B 232 18614 18416 19847 466 -3659 1769 N ATOM 3754 NH2 ARG B 232 -29.340 -43.865 40.890 1.00137.76 N ANISOU 3754 NH2 ARG B 232 17007 16636 18700 590 -3643 1813 N ATOM 3755 N GLU B 233 -26.435 -37.060 40.174 1.00117.15 N ANISOU 3755 N GLU B 233 14351 14369 15792 796 -3508 903 N ATOM 3756 CA GLU B 233 -25.059 -37.237 40.624 1.00129.24 C ANISOU 3756 CA GLU B 233 15820 15948 17337 768 -3586 995 C ATOM 3757 C GLU B 233 -24.482 -35.911 41.106 1.00135.71 C ANISOU 3757 C GLU B 233 16600 16938 18027 730 -3629 860 C ATOM 3758 O GLU B 233 -23.520 -35.882 41.876 1.00151.76 O ANISOU 3758 O GLU B 233 18576 19104 19980 652 -3728 947 O ATOM 3759 CB GLU B 233 -24.186 -37.814 39.507 1.00126.96 C ANISOU 3759 CB GLU B 233 15521 15426 17293 897 -3481 966 C ATOM 3760 CG GLU B 233 -23.117 -38.783 40.000 1.00147.41 C ANISOU 3760 CG GLU B 233 18053 18005 19952 856 -3582 1153 C ATOM 3761 CD GLU B 233 -23.538 -40.238 39.882 1.00160.76 C ANISOU 3761 CD GLU B 233 19746 19573 21764 844 -3594 1308 C ATOM 3762 OE1 GLU B 233 -23.483 -40.781 38.759 1.00165.86 O ANISOU 3762 OE1 GLU B 233 20399 20023 22599 938 -3478 1223 O ATOM 3763 OE2 GLU B 233 -23.929 -40.837 40.906 1.00157.63 O ANISOU 3763 OE2 GLU B 233 19338 19290 21266 726 -3717 1506 O ATOM 3764 N ALA B 234 -25.084 -34.816 40.654 1.00125.61 N ANISOU 3764 N ALA B 234 15340 15651 16734 779 -3553 637 N ATOM 3765 CA ALA B 234 -24.618 -33.477 40.999 1.00118.32 C ANISOU 3765 CA ALA B 234 14368 14868 15719 751 -3576 454 C ATOM 3766 C ALA B 234 -25.019 -33.072 42.415 1.00134.68 C ANISOU 3766 C ALA B 234 16406 17261 17505 535 -3712 459 C ATOM 3767 O ALA B 234 -24.400 -32.193 43.014 1.00137.51 O ANISOU 3767 O ALA B 234 16705 17797 17746 452 -3757 344 O ATOM 3768 CB ALA B 234 -25.129 -32.463 39.992 1.00104.18 C ANISOU 3768 CB ALA B 234 12593 12943 14046 876 -3438 199 C ATOM 3769 N LYS B 235 -26.061 -33.708 42.943 1.00150.09 N ANISOU 3769 N LYS B 235 18393 19305 19330 421 -3762 576 N ATOM 3770 CA LYS B 235 -26.480 -33.461 44.318 1.00165.42 C ANISOU 3770 CA LYS B 235 20309 21590 20954 159 -3837 589 C ATOM 3771 C LYS B 235 -25.575 -34.193 45.311 1.00186.04 C ANISOU 3771 C LYS B 235 22870 24378 23438 19 -3973 849 C ATOM 3772 O LYS B 235 -25.328 -33.702 46.415 1.00197.82 O ANISOU 3772 O LYS B 235 24307 26184 24670 -196 -4033 826 O ATOM 3773 CB LYS B 235 -27.936 -33.883 44.534 1.00155.23 C ANISOU 3773 CB LYS B 235 19080 20349 19553 67 -3765 614 C ATOM 3774 CG LYS B 235 -28.961 -32.863 44.053 1.00151.41 C ANISOU 3774 CG LYS B 235 18630 19819 19081 105 -3513 297 C ATOM 3775 CD LYS B 235 -30.379 -33.264 44.452 1.00149.12 C ANISOU 3775 CD LYS B 235 18391 19622 18646 -19 -3448 322 C ATOM 3776 CE LYS B 235 -31.393 -32.203 44.033 1.00131.36 C ANISOU 3776 CE LYS B 235 16157 17328 16427 7 -3200 4 C ATOM 3777 NZ LYS B 235 -32.790 -32.537 44.437 1.00 94.92 N ANISOU 3777 NZ LYS B 235 11588 12808 11671 -118 -3125 6 N ATOM 3778 N GLU B 236 -25.077 -35.360 44.908 1.00179.84 N ANISOU 3778 N GLU B 236 22098 23392 22841 132 -3980 1070 N ATOM 3779 CA GLU B 236 -24.307 -36.228 45.796 1.00167.97 C ANISOU 3779 CA GLU B 236 20549 22004 21269 18 -4086 1329 C ATOM 3780 C GLU B 236 -23.063 -35.554 46.371 1.00151.24 C ANISOU 3780 C GLU B 236 18358 20050 19058 -46 -4140 1289 C ATOM 3781 O GLU B 236 -22.519 -35.995 47.384 1.00160.85 O ANISOU 3781 O GLU B 236 19527 21451 20138 -200 -4238 1472 O ATOM 3782 CB GLU B 236 -23.934 -37.531 45.078 1.00163.23 C ANISOU 3782 CB GLU B 236 19965 21102 20954 169 -4069 1507 C ATOM 3783 CG GLU B 236 -22.434 -37.783 44.972 1.00166.34 C ANISOU 3783 CG GLU B 236 20303 21403 21497 236 -4102 1575 C ATOM 3784 CD GLU B 236 -22.119 -39.097 44.283 1.00174.40 C ANISOU 3784 CD GLU B 236 21326 22136 22801 350 -4080 1712 C ATOM 3785 OE1 GLU B 236 -21.915 -39.089 43.050 1.00165.06 O ANISOU 3785 OE1 GLU B 236 20167 20710 21840 526 -3958 1571 O ATOM 3786 OE2 GLU B 236 -22.070 -40.137 44.975 1.00189.10 O ANISOU 3786 OE2 GLU B 236 23158 24026 24665 245 -4181 1950 O ATOM 3787 N GLN B 237 -22.617 -34.489 45.715 1.00122.00 N ANISOU 3787 N GLN B 237 14644 16273 15438 71 -4072 1050 N ATOM 3788 CA GLN B 237 -21.413 -33.787 46.137 1.00131.09 C ANISOU 3788 CA GLN B 237 15727 17556 16525 31 -4110 988 C ATOM 3789 C GLN B 237 -21.492 -33.292 47.581 1.00146.19 C ANISOU 3789 C GLN B 237 17585 19877 18084 -251 -4184 978 C ATOM 3790 O GLN B 237 -20.692 -33.685 48.433 1.00141.64 O ANISOU 3790 O GLN B 237 16960 19453 17403 -366 -4269 1148 O ATOM 3791 CB GLN B 237 -21.144 -32.605 45.205 1.00128.72 C ANISOU 3791 CB GLN B 237 15427 17118 16364 187 -4009 701 C ATOM 3792 CG GLN B 237 -22.262 -31.575 45.186 1.00140.57 C ANISOU 3792 CG GLN B 237 16942 18706 17763 132 -3955 434 C ATOM 3793 CD GLN B 237 -21.770 -30.200 44.788 1.00173.59 C ANISOU 3793 CD GLN B 237 21082 22863 22012 209 -3883 132 C ATOM 3794 OE1 GLN B 237 -20.696 -30.061 44.200 1.00190.53 O ANISOU 3794 OE1 GLN B 237 23210 24862 24322 349 -3850 133 O ATOM 3795 NE2 GLN B 237 -22.550 -29.174 45.107 1.00179.64 N ANISOU 3795 NE2 GLN B 237 21841 23770 22645 105 -3689 -141 N ATOM 3796 N ILE B 238 -22.472 -32.440 47.851 1.00161.96 N ANISOU 3796 N ILE B 238 19586 22048 19902 -378 -4137 762 N ATOM 3797 CA ILE B 238 -22.610 -31.819 49.161 1.00156.36 C ANISOU 3797 CA ILE B 238 18817 21754 18838 -676 -4146 673 C ATOM 3798 C ILE B 238 -23.586 -32.602 50.032 1.00165.23 C ANISOU 3798 C ILE B 238 19963 23079 19738 -882 -4160 843 C ATOM 3799 O ILE B 238 -23.280 -33.715 50.467 1.00166.19 O ANISOU 3799 O ILE B 238 20089 23189 19866 -910 -4245 1145 O ATOM 3800 CB ILE B 238 -23.064 -30.348 49.043 1.00130.38 C ANISOU 3800 CB ILE B 238 15508 18547 15485 -713 -3965 263 C ATOM 3801 CG1 ILE B 238 -23.995 -30.175 47.837 1.00 88.36 C ANISOU 3801 CG1 ILE B 238 10265 12900 10408 -489 -3794 103 C ATOM 3802 CG2 ILE B 238 -21.856 -29.433 48.908 1.00134.18 C ANISOU 3802 CG2 ILE B 238 15927 19018 16037 -645 -3949 102 C ATOM 3803 CD1 ILE B 238 -24.493 -28.753 47.628 1.00 58.90 C ANISOU 3803 CD1 ILE B 238 6510 9178 6690 -480 -3538 -309 C ATOM 3804 N VAL B 280 -11.272 -29.191 46.019 1.00117.97 N ANISOU 3804 N VAL B 280 13656 16008 15160 341 -4145 500 N ATOM 3805 CA VAL B 280 -11.668 -28.141 46.952 1.00119.37 C ANISOU 3805 CA VAL B 280 13780 16505 15072 155 -4168 324 C ATOM 3806 C VAL B 280 -12.867 -27.339 46.413 1.00 98.16 C ANISOU 3806 C VAL B 280 11130 13755 12413 187 -4061 70 C ATOM 3807 O VAL B 280 -13.965 -27.427 46.964 1.00 65.90 O ANISOU 3807 O VAL B 280 7051 9824 8163 50 -4083 47 O ATOM 3808 CB VAL B 280 -10.451 -27.247 47.358 1.00 61.86 C ANISOU 3808 CB VAL B 280 6420 9366 7718 110 -4184 220 C ATOM 3809 CG1 VAL B 280 -10.900 -25.951 48.028 1.00 62.30 C ANISOU 3809 CG1 VAL B 280 6419 9692 7559 -61 -4154 -62 C ATOM 3810 CG2 VAL B 280 -9.499 -28.031 48.266 1.00 64.32 C ANISOU 3810 CG2 VAL B 280 6686 9826 7927 18 -4316 465 C ATOM 3811 N MET B 281 -12.682 -26.593 45.325 1.00118.60 N ANISOU 3811 N MET B 281 13741 16107 15215 367 -3938 -123 N ATOM 3812 CA MET B 281 -13.789 -25.811 44.767 1.00121.65 C ANISOU 3812 CA MET B 281 14151 16408 15664 422 -3825 -377 C ATOM 3813 C MET B 281 -14.324 -26.364 43.445 1.00106.09 C ANISOU 3813 C MET B 281 12265 14107 13937 624 -3729 -332 C ATOM 3814 O MET B 281 -13.695 -26.227 42.392 1.00 76.57 O ANISOU 3814 O MET B 281 8553 10135 10406 790 -3636 -363 O ATOM 3815 CB MET B 281 -13.374 -24.351 44.570 1.00131.22 C ANISOU 3815 CB MET B 281 15305 17629 16923 456 -3726 -678 C ATOM 3816 CG MET B 281 -13.134 -23.578 45.858 1.00151.90 C ANISOU 3816 CG MET B 281 17832 20594 19288 232 -3770 -825 C ATOM 3817 SD MET B 281 -14.650 -23.182 46.755 1.00206.26 S ANISOU 3817 SD MET B 281 24683 27745 25941 16 -3722 -1044 S ATOM 3818 CE MET B 281 -14.014 -22.074 48.012 1.00161.43 C ANISOU 3818 CE MET B 281 18887 22435 20013 -226 -3671 -1273 C ATOM 3819 N LEU B 282 -15.499 -26.984 43.521 1.00110.17 N ANISOU 3819 N LEU B 282 12825 14625 14411 587 -3745 -267 N ATOM 3820 CA LEU B 282 -16.243 -27.418 42.343 1.00 87.35 C ANISOU 3820 CA LEU B 282 10010 11461 11718 746 -3642 -261 C ATOM 3821 C LEU B 282 -17.386 -26.469 41.982 1.00 95.23 C ANISOU 3821 C LEU B 282 11003 12434 12745 773 -3545 -521 C ATOM 3822 O LEU B 282 -18.090 -26.688 41.001 1.00106.42 O ANISOU 3822 O LEU B 282 12476 13644 14313 894 -3451 -534 O ATOM 3823 CB LEU B 282 -16.783 -28.835 42.539 1.00 94.29 C ANISOU 3823 CB LEU B 282 10939 12317 12570 710 -3710 -4 C ATOM 3824 CG LEU B 282 -15.785 -29.980 42.346 1.00131.14 C ANISOU 3824 CG LEU B 282 15616 16866 17344 760 -3745 234 C ATOM 3825 CD1 LEU B 282 -14.584 -29.855 43.284 1.00144.42 C ANISOU 3825 CD1 LEU B 282 17226 18739 18907 660 -3855 317 C ATOM 3826 CD2 LEU B 282 -16.481 -31.319 42.534 1.00136.14 C ANISOU 3826 CD2 LEU B 282 16287 17465 17974 724 -3797 453 C ATOM 3827 N MET B 283 -17.580 -25.424 42.781 1.00136.16 N ANISOU 3827 N MET B 283 16912 16555 18266 876 -6737 -460 N ATOM 3828 CA MET B 283 -18.707 -24.520 42.574 1.00119.06 C ANISOU 3828 CA MET B 283 15024 14145 16070 808 -6695 -566 C ATOM 3829 C MET B 283 -18.719 -23.988 41.142 1.00119.14 C ANISOU 3829 C MET B 283 14860 14096 16312 632 -6599 -496 C ATOM 3830 O MET B 283 -19.769 -23.948 40.507 1.00130.08 O ANISOU 3830 O MET B 283 16392 15363 17670 674 -6417 -513 O ATOM 3831 CB MET B 283 -18.689 -23.375 43.590 1.00113.40 C ANISOU 3831 CB MET B 283 14533 13283 15270 722 -6954 -719 C ATOM 3832 CG MET B 283 -20.067 -22.959 44.097 1.00110.47 C ANISOU 3832 CG MET B 283 14569 12731 14673 855 -6892 -851 C ATOM 3833 SD MET B 283 -20.974 -24.295 44.907 1.00150.05 S ANISOU 3833 SD MET B 283 19760 17866 19386 1175 -6693 -826 S ATOM 3834 CE MET B 283 -19.867 -24.691 46.259 1.00111.74 C ANISOU 3834 CE MET B 283 14848 13167 14443 1257 -6924 -846 C ATOM 3835 N ARG B 284 -17.551 -23.598 40.633 1.00120.52 N ANISOU 3835 N ARG B 284 14705 14380 16707 440 -6714 -403 N ATOM 3836 CA ARG B 284 -17.431 -23.158 39.243 1.00119.58 C ANISOU 3836 CA ARG B 284 14367 14250 16818 281 -6615 -298 C ATOM 3837 C ARG B 284 -18.091 -24.168 38.313 1.00108.22 C ANISOU 3837 C ARG B 284 12896 12864 15358 476 -6315 -225 C ATOM 3838 O ARG B 284 -18.857 -23.803 37.416 1.00142.03 O ANISOU 3838 O ARG B 284 17246 17017 19701 438 -6177 -229 O ATOM 3839 CB ARG B 284 -15.963 -22.975 38.853 1.00153.01 C ANISOU 3839 CB ARG B 284 18165 18707 21264 103 -6736 -146 C ATOM 3840 CG ARG B 284 -15.304 -21.724 39.419 1.00181.67 C ANISOU 3840 CG ARG B 284 21793 22243 24989 -188 -7041 -190 C ATOM 3841 CD ARG B 284 -15.038 -20.684 38.331 1.00203.76 C ANISOU 3841 CD ARG B 284 24410 24965 28045 -484 -7062 -82 C ATOM 3842 NE ARG B 284 -16.267 -20.232 37.681 1.00213.74 N ANISOU 3842 NE ARG B 284 25944 25969 29299 -468 -6915 -152 N ATOM 3843 CZ ARG B 284 -16.307 -19.388 36.653 1.00210.26 C ANISOU 3843 CZ ARG B 284 25409 25424 29056 -682 -6888 -65 C ATOM 3844 NH1 ARG B 284 -15.182 -18.898 36.147 1.00206.86 N ANISOU 3844 NH1 ARG B 284 24609 25128 28860 -947 -6990 116 N ATOM 3845 NH2 ARG B 284 -17.473 -19.035 36.129 1.00207.53 N ANISOU 3845 NH2 ARG B 284 25327 24860 28666 -629 -6755 -144 N ATOM 3846 N GLU B 285 -17.785 -25.441 38.537 1.00 88.41 N ANISOU 3846 N GLU B 285 10301 10535 12755 692 -6225 -160 N ATOM 3847 CA GLU B 285 -18.393 -26.538 37.791 1.00 93.40 C ANISOU 3847 CA GLU B 285 10957 11191 13340 899 -5964 -98 C ATOM 3848 C GLU B 285 -19.919 -26.440 37.792 1.00 99.71 C ANISOU 3848 C GLU B 285 12107 11769 14011 944 -5836 -201 C ATOM 3849 O GLU B 285 -20.568 -26.672 36.768 1.00 99.10 O ANISOU 3849 O GLU B 285 12036 11639 13979 985 -5643 -167 O ATOM 3850 CB GLU B 285 -17.950 -27.875 38.389 1.00 90.30 C ANISOU 3850 CB GLU B 285 10538 10960 12810 1132 -5938 -42 C ATOM 3851 CG GLU B 285 -18.648 -29.096 37.823 1.00 88.44 C ANISOU 3851 CG GLU B 285 10416 10694 12494 1349 -5703 8 C ATOM 3852 CD GLU B 285 -17.710 -29.976 37.020 1.00122.33 C ANISOU 3852 CD GLU B 285 14426 15197 16856 1508 -5610 152 C ATOM 3853 OE1 GLU B 285 -17.011 -29.447 36.130 1.00144.89 O ANISOU 3853 OE1 GLU B 285 16982 18186 19885 1424 -5602 233 O ATOM 3854 OE2 GLU B 285 -17.665 -31.197 37.282 1.00121.04 O ANISOU 3854 OE2 GLU B 285 14347 15076 16566 1730 -5545 196 O ATOM 3855 N HIS B 286 -20.483 -26.077 38.942 1.00103.75 N ANISOU 3855 N HIS B 286 12899 12175 14346 950 -5942 -321 N ATOM 3856 CA HIS B 286 -21.935 -26.027 39.119 1.00106.10 C ANISOU 3856 CA HIS B 286 13516 12328 14470 1024 -5820 -399 C ATOM 3857 C HIS B 286 -22.618 -24.792 38.529 1.00113.99 C ANISOU 3857 C HIS B 286 14624 13163 15525 888 -5814 -476 C ATOM 3858 O HIS B 286 -23.712 -24.894 37.971 1.00119.72 O ANISOU 3858 O HIS B 286 15478 13824 16186 944 -5637 -483 O ATOM 3859 CB HIS B 286 -22.295 -26.186 40.596 1.00114.93 C ANISOU 3859 CB HIS B 286 14882 13447 15340 1138 -5910 -474 C ATOM 3860 CG HIS B 286 -22.143 -27.591 41.092 1.00122.70 C ANISOU 3860 CG HIS B 286 15853 14555 16213 1316 -5841 -386 C ATOM 3861 ND1 HIS B 286 -23.132 -28.234 41.800 1.00130.53 N ANISOU 3861 ND1 HIS B 286 17079 15540 16975 1460 -5745 -376 N ATOM 3862 CD2 HIS B 286 -21.134 -28.478 40.955 1.00120.25 C ANISOU 3862 CD2 HIS B 286 15327 14383 15981 1382 -5853 -288 C ATOM 3863 CE1 HIS B 286 -22.730 -29.465 42.093 1.00121.93 C ANISOU 3863 CE1 HIS B 286 15940 14547 15842 1589 -5714 -277 C ATOM 3864 NE2 HIS B 286 -21.518 -29.630 41.589 1.00122.31 N ANISOU 3864 NE2 HIS B 286 15726 14680 16066 1560 -5778 -233 N ATOM 3865 N LYS B 287 -21.984 -23.630 38.660 1.00124.58 N ANISOU 3865 N LYS B 287 15924 14434 16978 707 -6018 -527 N ATOM 3866 CA LYS B 287 -22.502 -22.410 38.048 1.00115.86 C ANISOU 3866 CA LYS B 287 14926 13152 15944 568 -6038 -588 C ATOM 3867 C LYS B 287 -22.392 -22.513 36.522 1.00108.37 C ANISOU 3867 C LYS B 287 13725 12237 15212 497 -5879 -473 C ATOM 3868 O LYS B 287 -23.198 -21.934 35.792 1.00100.30 O ANISOU 3868 O LYS B 287 12808 11097 14204 468 -5787 -505 O ATOM 3869 CB LYS B 287 -21.755 -21.174 38.572 1.00115.00 C ANISOU 3869 CB LYS B 287 14848 12930 15916 368 -6323 -653 C ATOM 3870 CG LYS B 287 -22.407 -19.825 38.246 1.00118.93 C ANISOU 3870 CG LYS B 287 15580 13189 16420 257 -6385 -745 C ATOM 3871 CD LYS B 287 -23.568 -19.496 39.187 1.00127.66 C ANISOU 3871 CD LYS B 287 17108 14182 17214 450 -6388 -906 C ATOM 3872 CE LYS B 287 -24.105 -18.083 38.943 1.00127.41 C ANISOU 3872 CE LYS B 287 17341 13906 17164 371 -6481 -1006 C ATOM 3873 NZ LYS B 287 -25.270 -17.746 39.816 1.00120.11 N ANISOU 3873 NZ LYS B 287 16822 12911 15904 613 -6461 -1154 N ATOM 3874 N ALA B 288 -21.397 -23.256 36.042 1.00113.58 N ANISOU 3874 N ALA B 288 14054 13080 16022 501 -5841 -337 N ATOM 3875 CA ALA B 288 -21.268 -23.509 34.608 1.00110.85 C ANISOU 3875 CA ALA B 288 13458 12807 15854 501 -5665 -215 C ATOM 3876 C ALA B 288 -22.220 -24.612 34.143 1.00106.77 C ANISOU 3876 C ALA B 288 13048 12303 15215 725 -5414 -208 C ATOM 3877 O ALA B 288 -22.547 -24.699 32.960 1.00103.64 O ANISOU 3877 O ALA B 288 12559 11906 14912 757 -5247 -154 O ATOM 3878 CB ALA B 288 -19.829 -23.850 34.245 1.00113.04 C ANISOU 3878 CB ALA B 288 13331 13312 16308 460 -5708 -57 C ATOM 3879 N LEU B 289 -22.640 -25.466 35.075 1.00 97.49 N ANISOU 3879 N LEU B 289 12065 11141 13836 873 -5395 -250 N ATOM 3880 CA LEU B 289 -23.587 -26.546 34.783 1.00 76.32 C ANISOU 3880 CA LEU B 289 9519 8450 11029 1046 -5186 -231 C ATOM 3881 C LEU B 289 -25.035 -26.064 34.673 1.00 63.47 C ANISOU 3881 C LEU B 289 8149 6692 9275 1040 -5090 -313 C ATOM 3882 O LEU B 289 -25.747 -26.366 33.705 1.00 61.36 O ANISOU 3882 O LEU B 289 7891 6398 9026 1088 -4912 -287 O ATOM 3883 CB LEU B 289 -23.508 -27.606 35.882 1.00 77.76 C ANISOU 3883 CB LEU B 289 9811 8694 11041 1181 -5217 -217 C ATOM 3884 CG LEU B 289 -24.097 -28.987 35.592 1.00 64.99 C ANISOU 3884 CG LEU B 289 8283 7078 9334 1342 -5043 -149 C ATOM 3885 CD1 LEU B 289 -23.115 -29.781 34.761 1.00 65.70 C ANISOU 3885 CD1 LEU B 289 8138 7270 9554 1442 -4985 -51 C ATOM 3886 CD2 LEU B 289 -24.416 -29.722 36.885 1.00 65.74 C ANISOU 3886 CD2 LEU B 289 8573 7185 9220 1432 -5090 -144 C ATOM 3887 N LYS B 290 -25.468 -25.315 35.681 1.00 91.63 N ANISOU 3887 N LYS B 290 11930 10195 12692 1004 -5209 -413 N ATOM 3888 CA LYS B 290 -26.853 -24.876 35.762 1.00107.43 C ANISOU 3888 CA LYS B 290 14184 12125 14510 1044 -5118 -484 C ATOM 3889 C LYS B 290 -27.204 -24.080 34.517 1.00 99.25 C ANISOU 3889 C LYS B 290 13097 11010 13602 967 -5043 -501 C ATOM 3890 O LYS B 290 -28.305 -24.202 33.975 1.00 99.67 O ANISOU 3890 O LYS B 290 13249 11057 13563 1032 -4876 -503 O ATOM 3891 CB LYS B 290 -27.073 -24.035 37.021 1.00128.77 C ANISOU 3891 CB LYS B 290 17117 14783 17026 1051 -5276 -597 C ATOM 3892 CG LYS B 290 -28.528 -23.726 37.323 1.00142.16 C ANISOU 3892 CG LYS B 290 19078 16476 18461 1158 -5164 -652 C ATOM 3893 CD LYS B 290 -28.668 -22.953 38.627 1.00149.53 C ANISOU 3893 CD LYS B 290 20249 17384 19183 1224 -5318 -765 C ATOM 3894 CE LYS B 290 -30.131 -22.699 38.966 1.00149.01 C ANISOU 3894 CE LYS B 290 20421 17379 18816 1379 -5178 -797 C ATOM 3895 NZ LYS B 290 -30.291 -21.913 40.224 1.00148.88 N ANISOU 3895 NZ LYS B 290 20654 17346 18567 1496 -5316 -914 N ATOM 3896 N THR B 291 -26.248 -23.277 34.060 1.00 87.44 N ANISOU 3896 N THR B 291 11432 9470 12322 821 -5171 -496 N ATOM 3897 CA THR B 291 -26.440 -22.462 32.868 1.00 86.91 C ANISOU 3897 CA THR B 291 11293 9328 12401 736 -5122 -491 C ATOM 3898 C THR B 291 -26.554 -23.320 31.600 1.00 78.20 C ANISOU 3898 C THR B 291 9995 8306 11410 824 -4901 -388 C ATOM 3899 O THR B 291 -27.117 -22.879 30.600 1.00 89.01 O ANISOU 3899 O THR B 291 11356 9631 12831 827 -4794 -390 O ATOM 3900 CB THR B 291 -25.349 -21.367 32.741 1.00 89.18 C ANISOU 3900 CB THR B 291 11434 9547 12904 518 -5332 -476 C ATOM 3901 OG1 THR B 291 -25.447 -20.466 33.853 1.00 69.82 O ANISOU 3901 OG1 THR B 291 9245 6966 10318 455 -5534 -600 O ATOM 3902 CG2 THR B 291 -25.516 -20.573 31.452 1.00 93.99 C ANISOU 3902 CG2 THR B 291 11947 10083 13681 422 -5278 -440 C ATOM 3903 N LEU B 292 -26.045 -24.549 31.640 1.00 59.80 N ANISOU 3903 N LEU B 292 7535 6089 9098 923 -4832 -306 N ATOM 3904 CA LEU B 292 -26.335 -25.487 30.555 1.00 61.77 C ANISOU 3904 CA LEU B 292 7695 6386 9388 1054 -4614 -236 C ATOM 3905 C LEU B 292 -27.750 -26.035 30.716 1.00 76.21 C ANISOU 3905 C LEU B 292 9778 8171 11008 1141 -4482 -280 C ATOM 3906 O LEU B 292 -28.482 -26.179 29.733 1.00 71.87 O ANISOU 3906 O LEU B 292 9242 7601 10464 1194 -4317 -274 O ATOM 3907 CB LEU B 292 -25.320 -26.636 30.479 1.00 59.24 C ANISOU 3907 CB LEU B 292 7190 6188 9129 1158 -4590 -138 C ATOM 3908 CG LEU B 292 -24.117 -26.456 29.547 1.00 69.70 C ANISOU 3908 CG LEU B 292 8174 7638 10672 1156 -4574 -28 C ATOM 3909 CD1 LEU B 292 -23.219 -27.684 29.601 1.00 66.74 C ANISOU 3909 CD1 LEU B 292 7668 7411 10280 1322 -4542 58 C ATOM 3910 CD2 LEU B 292 -24.540 -26.156 28.108 1.00 59.09 C ANISOU 3910 CD2 LEU B 292 6746 6278 9427 1199 -4391 1 C ATOM 3911 N GLY B 293 -28.136 -26.335 31.955 1.00 81.89 N ANISOU 3911 N GLY B 293 10683 8894 11536 1156 -4552 -309 N ATOM 3912 CA GLY B 293 -29.491 -26.797 32.220 1.00 78.10 C ANISOU 3912 CA GLY B 293 10413 8415 10848 1214 -4438 -312 C ATOM 3913 C GLY B 293 -30.519 -25.849 31.627 1.00 83.12 C ANISOU 3913 C GLY B 293 11139 9019 11424 1198 -4354 -373 C ATOM 3914 O GLY B 293 -31.466 -26.260 30.936 1.00 84.53 O ANISOU 3914 O GLY B 293 11356 9212 11551 1241 -4196 -345 O ATOM 3915 N ILE B 294 -30.313 -24.563 31.890 1.00 79.58 N ANISOU 3915 N ILE B 294 10737 8521 10979 1134 -4477 -459 N ATOM 3916 CA ILE B 294 -31.186 -23.525 31.369 1.00 63.12 C ANISOU 3916 CA ILE B 294 8765 6395 8822 1140 -4426 -530 C ATOM 3917 C ILE B 294 -31.424 -23.702 29.878 1.00 68.94 C ANISOU 3917 C ILE B 294 9364 7127 9702 1159 -4239 -486 C ATOM 3918 O ILE B 294 -32.562 -23.743 29.446 1.00 86.04 O ANISOU 3918 O ILE B 294 11624 9332 11735 1215 -4054 -496 O ATOM 3919 CB ILE B 294 -30.598 -22.128 31.616 1.00 73.79 C ANISOU 3919 CB ILE B 294 10168 7635 10233 1042 -4624 -621 C ATOM 3920 CG1 ILE B 294 -30.682 -21.777 33.102 1.00106.79 C ANISOU 3920 CG1 ILE B 294 14568 11807 14200 1067 -4765 -700 C ATOM 3921 CG2 ILE B 294 -31.318 -21.084 30.775 1.00 54.12 C ANISOU 3921 CG2 ILE B 294 7773 5076 7715 1036 -4495 -680 C ATOM 3922 CD1 ILE B 294 -30.169 -20.392 33.431 1.00130.28 C ANISOU 3922 CD1 ILE B 294 17663 14628 17211 967 -4986 -806 C ATOM 3923 N ILE B 295 -30.354 -23.843 29.101 1.00 69.09 N ANISOU 3923 N ILE B 295 9148 7131 9973 1117 -4234 -430 N ATOM 3924 CA ILE B 295 -30.470 -23.935 27.645 1.00 79.14 C ANISOU 3924 CA ILE B 295 10287 8411 11371 1153 -4004 -391 C ATOM 3925 C ILE B 295 -31.536 -24.921 27.192 1.00 96.56 C ANISOU 3925 C ILE B 295 12573 10656 13458 1264 -3832 -377 C ATOM 3926 O ILE B 295 -32.384 -24.595 26.362 1.00102.90 O ANISOU 3926 O ILE B 295 13420 11465 14214 1291 -3644 -407 O ATOM 3927 CB ILE B 295 -29.145 -24.354 27.006 1.00 51.95 C ANISOU 3927 CB ILE B 295 6560 5010 8167 1165 -4026 -294 C ATOM 3928 CG1 ILE B 295 -28.081 -23.315 27.320 1.00 54.03 C ANISOU 3928 CG1 ILE B 295 6697 5253 8580 1004 -4199 -276 C ATOM 3929 CG2 ILE B 295 -29.304 -24.528 25.498 1.00 50.76 C ANISOU 3929 CG2 ILE B 295 6289 4889 8109 1258 -3782 -254 C ATOM 3930 CD1 ILE B 295 -28.523 -21.920 27.009 1.00 53.92 C ANISOU 3930 CD1 ILE B 295 6791 5137 8561 887 -4151 -336 C ATOM 3931 N MET B 296 -31.487 -26.131 27.737 1.00 83.09 N ANISOU 3931 N MET B 296 10895 8972 11702 1313 -3899 -325 N ATOM 3932 CA MET B 296 -32.438 -27.165 27.360 1.00 86.58 C ANISOU 3932 CA MET B 296 11425 9426 12047 1367 -3767 -293 C ATOM 3933 C MET B 296 -33.807 -26.910 27.974 1.00 87.14 C ANISOU 3933 C MET B 296 11677 9548 11883 1345 -3750 -305 C ATOM 3934 O MET B 296 -34.828 -27.322 27.425 1.00 76.23 O ANISOU 3934 O MET B 296 10344 8198 10422 1356 -3617 -283 O ATOM 3935 CB MET B 296 -31.919 -28.535 27.776 1.00 96.46 C ANISOU 3935 CB MET B 296 12680 10664 13306 1392 -3812 -226 C ATOM 3936 CG MET B 296 -30.530 -28.823 27.265 1.00 88.84 C ANISOU 3936 CG MET B 296 11530 9706 12521 1454 -3821 -202 C ATOM 3937 SD MET B 296 -29.885 -30.330 27.987 1.00 84.14 S ANISOU 3937 SD MET B 296 10985 9100 11886 1517 -3905 -135 S ATOM 3938 CE MET B 296 -30.166 -30.001 29.728 1.00150.98 C ANISOU 3938 CE MET B 296 19582 17588 20197 1418 -4063 -134 C ATOM 3939 N GLY B 297 -33.832 -26.236 29.118 1.00 93.57 N ANISOU 3939 N GLY B 297 12589 10398 12567 1314 -3862 -337 N ATOM 3940 CA GLY B 297 -35.110 -25.878 29.703 1.00 83.25 C ANISOU 3940 CA GLY B 297 11442 9194 10994 1335 -3814 -342 C ATOM 3941 C GLY B 297 -35.860 -24.934 28.784 1.00 79.31 C ANISOU 3941 C GLY B 297 10960 8721 10455 1352 -3627 -412 C ATOM 3942 O GLY B 297 -36.970 -25.225 28.330 1.00101.28 O ANISOU 3942 O GLY B 297 13763 11599 13121 1372 -3474 -377 O ATOM 3943 N VAL B 298 -35.227 -23.807 28.486 1.00 47.26 N ANISOU 3943 N VAL B 298 6884 4574 6497 1334 -3651 -501 N ATOM 3944 CA VAL B 298 -35.812 -22.797 27.632 1.00 47.87 C ANISOU 3944 CA VAL B 298 7000 4649 6541 1363 -3487 -568 C ATOM 3945 C VAL B 298 -36.104 -23.383 26.266 1.00 46.15 C ANISOU 3945 C VAL B 298 6650 4448 6436 1382 -3290 -532 C ATOM 3946 O VAL B 298 -37.149 -23.109 25.684 1.00 43.89 O ANISOU 3946 O VAL B 298 6410 4242 6023 1437 -3122 -554 O ATOM 3947 CB VAL B 298 -34.889 -21.578 27.482 1.00 62.25 C ANISOU 3947 CB VAL B 298 8821 6329 8504 1301 -3576 -638 C ATOM 3948 CG1 VAL B 298 -33.449 -22.014 27.364 1.00 72.62 C ANISOU 3948 CG1 VAL B 298 9931 7569 10091 1210 -3701 -580 C ATOM 3949 CG2 VAL B 298 -35.293 -20.757 26.275 1.00 89.43 C ANISOU 3949 CG2 VAL B 298 12257 9742 11981 1327 -3378 -673 C ATOM 3950 N PHE B 299 -35.186 -24.196 25.756 1.00 45.00 N ANISOU 3950 N PHE B 299 6348 4241 6508 1366 -3320 -481 N ATOM 3951 CA PHE B 299 -35.403 -24.826 24.465 1.00 73.78 C ANISOU 3951 CA PHE B 299 9897 7892 10245 1424 -3161 -460 C ATOM 3952 C PHE B 299 -36.703 -25.618 24.507 1.00 72.89 C ANISOU 3952 C PHE B 299 9875 7864 9955 1434 -3097 -430 C ATOM 3953 O PHE B 299 -37.624 -25.361 23.736 1.00 79.84 O ANISOU 3953 O PHE B 299 10769 8811 10754 1470 -2937 -458 O ATOM 3954 CB PHE B 299 -34.237 -25.741 24.107 1.00 80.91 C ANISOU 3954 CB PHE B 299 10654 8736 11352 1460 -3234 -404 C ATOM 3955 CG PHE B 299 -34.302 -26.290 22.710 1.00 71.66 C ANISOU 3955 CG PHE B 299 9401 7558 10267 1571 -3089 -399 C ATOM 3956 CD1 PHE B 299 -34.712 -27.593 22.477 1.00 49.45 C ANISOU 3956 CD1 PHE B 299 6649 4717 7421 1625 -3111 -375 C ATOM 3957 CD2 PHE B 299 -33.946 -25.504 21.633 1.00 43.60 C ANISOU 3957 CD2 PHE B 299 5729 4016 6820 1627 -2945 -415 C ATOM 3958 CE1 PHE B 299 -34.761 -28.095 21.198 1.00 43.38 C ANISOU 3958 CE1 PHE B 299 5842 3948 6691 1718 -2963 -397 C ATOM 3959 CE2 PHE B 299 -33.992 -26.002 20.355 1.00 43.13 C ANISOU 3959 CE2 PHE B 299 5605 3969 6814 1770 -2814 -416 C ATOM 3960 CZ PHE B 299 -34.401 -27.299 20.135 1.00 43.02 C ANISOU 3960 CZ PHE B 299 5672 3949 6725 1799 -2799 -422 C ATOM 3961 N THR B 300 -36.784 -26.563 25.433 1.00 52.57 N ANISOU 3961 N THR B 300 7356 5300 7317 1391 -3228 -357 N ATOM 3962 CA THR B 300 -37.978 -27.379 25.569 1.00 51.38 C ANISOU 3962 CA THR B 300 7274 5235 7012 1351 -3196 -282 C ATOM 3963 C THR B 300 -39.242 -26.522 25.681 1.00 65.11 C ANISOU 3963 C THR B 300 9067 7150 8520 1361 -3066 -299 C ATOM 3964 O THR B 300 -40.272 -26.861 25.122 1.00 51.57 O ANISOU 3964 O THR B 300 7341 5532 6720 1343 -2963 -263 O ATOM 3965 CB THR B 300 -37.872 -28.324 26.776 1.00 65.49 C ANISOU 3965 CB THR B 300 9127 7018 8737 1292 -3364 -172 C ATOM 3966 OG1 THR B 300 -36.721 -29.164 26.623 1.00 45.85 O ANISOU 3966 OG1 THR B 300 6602 4376 6442 1320 -3483 -158 O ATOM 3967 CG2 THR B 300 -39.116 -29.185 26.885 1.00 77.88 C ANISOU 3967 CG2 THR B 300 10748 8679 10164 1207 -3338 -51 C ATOM 3968 N LEU B 301 -39.168 -25.403 26.391 1.00 79.60 N ANISOU 3968 N LEU B 301 10971 9033 10240 1405 -3085 -355 N ATOM 3969 CA LEU B 301 -40.356 -24.569 26.551 1.00 60.17 C ANISOU 3969 CA LEU B 301 8586 6757 7517 1475 -2967 -373 C ATOM 3970 C LEU B 301 -40.699 -23.813 25.285 1.00 60.03 C ANISOU 3970 C LEU B 301 8538 6740 7531 1541 -2787 -461 C ATOM 3971 O LEU B 301 -41.852 -23.438 25.074 1.00 84.23 O ANISOU 3971 O LEU B 301 11628 9986 10388 1608 -2654 -457 O ATOM 3972 CB LEU B 301 -40.188 -23.594 27.709 1.00 44.55 C ANISOU 3972 CB LEU B 301 6748 4807 5371 1549 -3068 -425 C ATOM 3973 CG LEU B 301 -40.381 -24.260 29.070 1.00 49.56 C ANISOU 3973 CG LEU B 301 7435 5554 5842 1540 -3196 -316 C ATOM 3974 CD1 LEU B 301 -40.033 -23.298 30.189 1.00 47.20 C ANISOU 3974 CD1 LEU B 301 7298 5250 5387 1643 -3334 -397 C ATOM 3975 CD2 LEU B 301 -41.809 -24.775 29.203 1.00 58.14 C ANISOU 3975 CD2 LEU B 301 8494 6908 6689 1548 -3076 -176 C ATOM 3976 N CYS B 302 -39.685 -23.560 24.466 1.00 53.42 N ANISOU 3976 N CYS B 302 7634 5725 6938 1537 -2780 -524 N ATOM 3977 CA CYS B 302 -39.865 -22.831 23.214 1.00 71.66 C ANISOU 3977 CA CYS B 302 9910 8020 9296 1610 -2607 -593 C ATOM 3978 C CYS B 302 -40.343 -23.694 22.043 1.00 60.11 C ANISOU 3978 C CYS B 302 8347 6597 7896 1626 -2490 -572 C ATOM 3979 O CYS B 302 -41.236 -23.303 21.295 1.00 52.48 O ANISOU 3979 O CYS B 302 7383 5739 6818 1700 -2334 -606 O ATOM 3980 CB CYS B 302 -38.585 -22.069 22.848 1.00 67.99 C ANISOU 3980 CB CYS B 302 9404 7378 9051 1597 -2641 -638 C ATOM 3981 SG CYS B 302 -38.294 -20.574 23.858 1.00 70.18 S ANISOU 3981 SG CYS B 302 9865 7577 9225 1590 -2763 -709 S ATOM 3982 N TRP B 303 -39.734 -24.857 21.868 1.00 53.45 N ANISOU 3982 N TRP B 303 5487 4604 10217 -1029 -3898 2114 N ATOM 3983 CA TRP B 303 -40.136 -25.745 20.788 1.00 53.29 C ANISOU 3983 CA TRP B 303 5434 4685 10127 -1012 -3854 2117 C ATOM 3984 C TRP B 303 -41.029 -26.925 21.165 1.00 64.55 C ANISOU 3984 C TRP B 303 6845 6194 11488 -976 -3819 2069 C ATOM 3985 O TRP B 303 -41.429 -27.690 20.293 1.00 61.54 O ANISOU 3985 O TRP B 303 6438 5892 11053 -958 -3796 2061 O ATOM 3986 CB TRP B 303 -38.910 -26.229 20.026 1.00 58.31 C ANISOU 3986 CB TRP B 303 6064 5286 10805 -1069 -3822 2194 C ATOM 3987 CG TRP B 303 -38.327 -25.161 19.178 1.00 76.55 C ANISOU 3987 CG TRP B 303 8361 7580 13145 -1095 -3855 2254 C ATOM 3988 CD1 TRP B 303 -37.463 -24.184 19.570 1.00 84.94 C ANISOU 3988 CD1 TRP B 303 9441 8530 14304 -1150 -3895 2308 C ATOM 3989 CD2 TRP B 303 -38.575 -24.946 17.788 1.00 61.64 C ANISOU 3989 CD2 TRP B 303 6434 5796 11192 -1072 -3859 2275 C ATOM 3990 NE1 TRP B 303 -37.149 -23.378 18.503 1.00 75.90 N ANISOU 3990 NE1 TRP B 303 8267 7410 13163 -1171 -3923 2373 N ATOM 3991 CE2 TRP B 303 -37.821 -23.828 17.397 1.00 63.78 C ANISOU 3991 CE2 TRP B 303 6697 6016 11522 -1121 -3900 2355 C ATOM 3992 CE3 TRP B 303 -39.357 -25.596 16.834 1.00 83.50 C ANISOU 3992 CE3 TRP B 303 9171 8699 13856 -1017 -3841 2236 C ATOM 3993 CZ2 TRP B 303 -37.829 -23.346 16.095 1.00 84.70 C ANISOU 3993 CZ2 TRP B 303 9306 8754 14121 -1115 -3919 2407 C ATOM 3994 CZ3 TRP B 303 -39.364 -25.115 15.543 1.00100.36 C ANISOU 3994 CZ3 TRP B 303 11271 10924 15937 -1003 -3862 2274 C ATOM 3995 CH2 TRP B 303 -38.608 -24.002 15.185 1.00 99.13 C ANISOU 3995 CH2 TRP B 303 11106 10725 15833 -1051 -3898 2363 C ATOM 3996 N LEU B 304 -41.302 -27.110 22.453 1.00 82.43 N ANISOU 3996 N LEU B 304 9120 8446 13755 -969 -3820 2043 N ATOM 3997 CA LEU B 304 -42.269 -28.127 22.878 1.00 79.95 C ANISOU 3997 CA LEU B 304 8777 8227 13375 -940 -3795 2010 C ATOM 3998 C LEU B 304 -43.725 -27.773 22.593 1.00 77.50 C ANISOU 3998 C LEU B 304 8414 8055 12976 -863 -3814 1941 C ATOM 3999 O LEU B 304 -44.479 -28.617 22.118 1.00 57.73 O ANISOU 3999 O LEU B 304 5875 5639 10421 -846 -3797 1926 O ATOM 4000 CB LEU B 304 -42.111 -28.494 24.347 1.00 77.98 C ANISOU 4000 CB LEU B 304 8540 7949 13141 -959 -3792 2016 C ATOM 4001 CG LEU B 304 -42.960 -29.698 24.726 1.00 80.07 C ANISOU 4001 CG LEU B 304 8769 8307 13348 -952 -3767 2013 C ATOM 4002 CD1 LEU B 304 -42.533 -30.900 23.909 1.00 52.32 C ANISOU 4002 CD1 LEU B 304 5266 4749 9864 -994 -3742 2055 C ATOM 4003 CD2 LEU B 304 -42.841 -29.977 26.209 1.00107.40 C ANISOU 4003 CD2 LEU B 304 12234 11765 16808 -970 -3771 2029 C ATOM 4004 N PRO B 305 -44.133 -26.531 22.912 1.00 93.11 N ANISOU 4004 N PRO B 305 10383 10052 14943 -811 -3859 1893 N ATOM 4005 CA PRO B 305 -45.521 -26.119 22.673 1.00 89.43 C ANISOU 4005 CA PRO B 305 9858 9724 14398 -725 -3886 1820 C ATOM 4006 C PRO B 305 -45.875 -26.192 21.193 1.00 71.58 C ANISOU 4006 C PRO B 305 7583 7504 12111 -715 -3892 1825 C ATOM 4007 O PRO B 305 -47.024 -26.437 20.840 1.00 55.61 O ANISOU 4007 O PRO B 305 5505 5604 10021 -662 -3899 1778 O ATOM 4008 CB PRO B 305 -45.543 -24.662 23.154 1.00 89.29 C ANISOU 4008 CB PRO B 305 9849 9675 14402 -676 -3950 1773 C ATOM 4009 CG PRO B 305 -44.117 -24.217 23.120 1.00 71.62 C ANISOU 4009 CG PRO B 305 7680 7268 12263 -751 -3961 1837 C ATOM 4010 CD PRO B 305 -43.334 -25.439 23.493 1.00 91.55 C ANISOU 4010 CD PRO B 305 10226 9745 14813 -825 -3901 1898 C ATOM 4011 N PHE B 306 -44.886 -25.966 20.338 1.00 75.54 N ANISOU 4011 N PHE B 306 8123 7917 12660 -765 -3892 1882 N ATOM 4012 CA PHE B 306 -45.068 -26.064 18.895 1.00 70.10 C ANISOU 4012 CA PHE B 306 7418 7281 11934 -756 -3899 1894 C ATOM 4013 C PHE B 306 -45.066 -27.518 18.424 1.00 79.35 C ANISOU 4013 C PHE B 306 8576 8496 13076 -776 -3855 1904 C ATOM 4014 O PHE B 306 -45.922 -27.919 17.636 1.00 81.32 O ANISOU 4014 O PHE B 306 8788 8846 13262 -737 -3867 1869 O ATOM 4015 CB PHE B 306 -43.975 -25.267 18.187 1.00 75.11 C ANISOU 4015 CB PHE B 306 8084 7834 12622 -800 -3919 1961 C ATOM 4016 CG PHE B 306 -43.866 -25.541 16.713 1.00 70.63 C ANISOU 4016 CG PHE B 306 7496 7336 12005 -800 -3917 1991 C ATOM 4017 CD1 PHE B 306 -43.312 -26.724 16.249 1.00 68.93 C ANISOU 4017 CD1 PHE B 306 7274 7143 11774 -825 -3869 2012 C ATOM 4018 CD2 PHE B 306 -44.272 -24.596 15.789 1.00 67.96 C ANISOU 4018 CD2 PHE B 306 7144 7044 11635 -768 -3973 1997 C ATOM 4019 CE1 PHE B 306 -43.188 -26.969 14.891 1.00 62.92 C ANISOU 4019 CE1 PHE B 306 6485 6469 10951 -809 -3873 2027 C ATOM 4020 CE2 PHE B 306 -44.149 -24.839 14.432 1.00 69.84 C ANISOU 4020 CE2 PHE B 306 7359 7367 11811 -762 -3976 2027 C ATOM 4021 CZ PHE B 306 -43.602 -26.024 13.984 1.00 56.01 C ANISOU 4021 CZ PHE B 306 5594 5657 10030 -778 -3924 2038 C ATOM 4022 N PHE B 307 -44.101 -28.300 18.908 1.00 93.67 N ANISOU 4022 N PHE B 307 10419 10228 14942 -834 -3815 1947 N ATOM 4023 CA PHE B 307 -43.991 -29.719 18.555 1.00 69.97 C ANISOU 4023 CA PHE B 307 7410 7244 11930 -852 -3786 1952 C ATOM 4024 C PHE B 307 -44.888 -30.610 19.433 1.00 71.93 C ANISOU 4024 C PHE B 307 7637 7534 12161 -846 -3779 1926 C ATOM 4025 O PHE B 307 -44.866 -31.834 19.315 1.00 56.92 O ANISOU 4025 O PHE B 307 5732 5628 10268 -866 -3769 1932 O ATOM 4026 CB PHE B 307 -42.537 -30.196 18.639 1.00 53.41 C ANISOU 4026 CB PHE B 307 5348 5042 9905 -910 -3758 2010 C ATOM 4027 CG PHE B 307 -41.721 -29.943 17.390 1.00 72.36 C ANISOU 4027 CG PHE B 307 7737 7459 12296 -912 -3758 2038 C ATOM 4028 CD1 PHE B 307 -41.823 -30.785 16.292 1.00 93.22 C ANISOU 4028 CD1 PHE B 307 10349 10186 14884 -882 -3758 2011 C ATOM 4029 CD2 PHE B 307 -40.815 -28.895 17.333 1.00 96.70 C ANISOU 4029 CD2 PHE B 307 10832 10484 15424 -943 -3764 2093 C ATOM 4030 CE1 PHE B 307 -41.054 -30.569 15.146 1.00111.39 C ANISOU 4030 CE1 PHE B 307 12626 12541 17158 -872 -3758 2036 C ATOM 4031 CE2 PHE B 307 -40.042 -28.675 16.190 1.00107.44 C ANISOU 4031 CE2 PHE B 307 12167 11889 16768 -947 -3762 2135 C ATOM 4032 CZ PHE B 307 -40.165 -29.512 15.097 1.00104.17 C ANISOU 4032 CZ PHE B 307 11715 11584 16280 -906 -3756 2105 C ATOM 4033 N LEU B 308 -45.629 -29.997 20.352 1.00 79.58 N ANISOU 4033 N LEU B 308 8585 8545 13108 -817 -3790 1898 N ATOM 4034 CA LEU B 308 -46.786 -30.650 20.949 1.00 69.81 C ANISOU 4034 CA LEU B 308 7294 7408 11824 -796 -3791 1870 C ATOM 4035 C LEU B 308 -47.990 -30.481 20.025 1.00 85.67 C ANISOU 4035 C LEU B 308 9245 9542 13765 -736 -3821 1813 C ATOM 4036 O LEU B 308 -48.761 -31.414 19.807 1.00 87.80 O ANISOU 4036 O LEU B 308 9471 9883 14007 -735 -3826 1799 O ATOM 4037 CB LEU B 308 -47.090 -30.070 22.326 1.00 81.45 C ANISOU 4037 CB LEU B 308 8748 8916 13283 -776 -3792 1855 C ATOM 4038 CG LEU B 308 -46.351 -30.707 23.499 1.00108.27 C ANISOU 4038 CG LEU B 308 12177 12239 16723 -835 -3768 1909 C ATOM 4039 CD1 LEU B 308 -46.515 -29.868 24.762 1.00139.57 C ANISOU 4039 CD1 LEU B 308 16123 16248 20661 -801 -3780 1881 C ATOM 4040 CD2 LEU B 308 -46.849 -32.128 23.714 1.00 91.20 C ANISOU 4040 CD2 LEU B 308 9983 10120 14548 -870 -3757 1941 C ATOM 4041 N VAL B 309 -48.136 -29.279 19.475 1.00108.70 N ANISOU 4041 N VAL B 309 12161 12477 16664 -689 -3851 1784 N ATOM 4042 CA VAL B 309 -49.270 -28.944 18.615 1.00102.74 C ANISOU 4042 CA VAL B 309 11352 11837 15848 -625 -3891 1730 C ATOM 4043 C VAL B 309 -49.402 -29.914 17.455 1.00 85.66 C ANISOU 4043 C VAL B 309 9181 9704 13663 -637 -3897 1730 C ATOM 4044 O VAL B 309 -50.440 -30.554 17.282 1.00 76.49 O ANISOU 4044 O VAL B 309 7961 8637 12463 -616 -3916 1694 O ATOM 4045 CB VAL B 309 -49.147 -27.509 18.045 1.00 79.76 C ANISOU 4045 CB VAL B 309 8460 8908 12939 -585 -3934 1719 C ATOM 4046 CG1 VAL B 309 -50.019 -27.332 16.799 1.00 57.51 C ANISOU 4046 CG1 VAL B 309 5603 6185 10063 -533 -3982 1684 C ATOM 4047 CG2 VAL B 309 -49.500 -26.486 19.111 1.00 63.65 C ANISOU 4047 CG2 VAL B 309 6402 6878 10904 -538 -3957 1680 C ATOM 4048 N ASN B 310 -48.327 -30.046 16.688 1.00 66.47 N ANISOU 4048 N ASN B 310 6799 7201 11254 -670 -3887 1767 N ATOM 4049 CA ASN B 310 -48.365 -30.779 15.437 1.00 69.05 C ANISOU 4049 CA ASN B 310 7116 7575 11544 -661 -3905 1752 C ATOM 4050 C ASN B 310 -48.902 -32.195 15.612 1.00 90.74 C ANISOU 4050 C ASN B 310 9836 10347 14295 -677 -3906 1731 C ATOM 4051 O ASN B 310 -49.309 -32.835 14.644 1.00125.70 O ANISOU 4051 O ASN B 310 14239 14835 18685 -657 -3940 1695 O ATOM 4052 CB ASN B 310 -46.980 -30.805 14.801 1.00 65.05 C ANISOU 4052 CB ASN B 310 6651 7006 11058 -691 -3885 1796 C ATOM 4053 CG ASN B 310 -47.034 -31.006 13.304 1.00 90.88 C ANISOU 4053 CG ASN B 310 9902 10370 14260 -654 -3918 1772 C ATOM 4054 OD1 ASN B 310 -48.085 -30.855 12.682 1.00118.98 O ANISOU 4054 OD1 ASN B 310 13424 14025 17758 -607 -3964 1727 O ATOM 4055 ND2 ASN B 310 -45.895 -31.342 12.712 1.00 92.29 N ANISOU 4055 ND2 ASN B 310 10093 10533 14439 -669 -3900 1798 N ATOM 4056 N ILE B 311 -48.904 -32.687 16.846 1.00 55.97 N ANISOU 4056 N ILE B 311 5434 5897 9935 -716 -3878 1757 N ATOM 4057 CA ILE B 311 -49.526 -33.976 17.125 1.00 67.32 C ANISOU 4057 CA ILE B 311 6839 7356 11385 -741 -3891 1753 C ATOM 4058 C ILE B 311 -51.043 -33.854 17.166 1.00 86.68 C ANISOU 4058 C ILE B 311 9208 9942 13784 -703 -3924 1709 C ATOM 4059 O ILE B 311 -51.757 -34.700 16.629 1.00100.71 O ANISOU 4059 O ILE B 311 10944 11771 15551 -703 -3963 1682 O ATOM 4060 CB ILE B 311 -49.020 -34.592 18.435 1.00 76.89 C ANISOU 4060 CB ILE B 311 8074 8483 12656 -801 -3858 1812 C ATOM 4061 CG1 ILE B 311 -47.718 -35.338 18.174 1.00 66.72 C ANISOU 4061 CG1 ILE B 311 6848 7069 11432 -841 -3847 1844 C ATOM 4062 CG2 ILE B 311 -50.043 -35.563 18.998 1.00 73.24 C ANISOU 4062 CG2 ILE B 311 7553 8082 12193 -824 -3878 1820 C ATOM 4063 CD1 ILE B 311 -47.823 -36.315 17.029 1.00 55.63 C ANISOU 4063 CD1 ILE B 311 5433 5680 10024 -827 -3888 1803 C ATOM 4064 N VAL B 312 -51.533 -32.795 17.800 1.00 83.15 N ANISOU 4064 N VAL B 312 8729 9556 13309 -666 -3916 1694 N ATOM 4065 CA VAL B 312 -52.963 -32.544 17.815 1.00 91.11 C ANISOU 4065 CA VAL B 312 9642 10712 14264 -616 -3950 1643 C ATOM 4066 C VAL B 312 -53.400 -32.233 16.393 1.00 99.06 C ANISOU 4066 C VAL B 312 10638 11767 15233 -568 -4002 1595 C ATOM 4067 O VAL B 312 -54.558 -32.422 16.035 1.00 97.04 O ANISOU 4067 O VAL B 312 10305 11622 14943 -537 -4045 1552 O ATOM 4068 CB VAL B 312 -53.328 -31.383 18.740 1.00 79.16 C ANISOU 4068 CB VAL B 312 8091 9263 12724 -565 -3941 1619 C ATOM 4069 CG1 VAL B 312 -54.814 -31.420 19.057 1.00 78.94 C ANISOU 4069 CG1 VAL B 312 7938 9411 12644 -520 -3968 1569 C ATOM 4070 CG2 VAL B 312 -52.513 -31.458 20.018 1.00 61.18 C ANISOU 4070 CG2 VAL B 312 5852 6913 10479 -609 -3893 1668 C ATOM 4071 N ASN B 313 -52.457 -31.751 15.589 1.00103.31 N ANISOU 4071 N ASN B 313 11247 12232 15774 -564 -4001 1608 N ATOM 4072 CA ASN B 313 -52.674 -31.586 14.160 1.00 97.39 C ANISOU 4072 CA ASN B 313 10495 11532 14978 -525 -4051 1576 C ATOM 4073 C ASN B 313 -53.152 -32.898 13.569 1.00 84.65 C ANISOU 4073 C ASN B 313 8850 9957 13356 -540 -4085 1548 C ATOM 4074 O ASN B 313 -54.059 -32.921 12.744 1.00112.70 O ANISOU 4074 O ASN B 313 12354 13604 16863 -500 -4144 1500 O ATOM 4075 CB ASN B 313 -51.386 -31.123 13.468 1.00114.83 C ANISOU 4075 CB ASN B 313 12775 13667 17188 -535 -4037 1612 C ATOM 4076 CG ASN B 313 -51.426 -31.301 11.954 1.00118.14 C ANISOU 4076 CG ASN B 313 13189 14155 17544 -503 -4086 1586 C ATOM 4077 OD1 ASN B 313 -50.836 -32.236 11.408 1.00100.73 O ANISOU 4077 OD1 ASN B 313 11000 11939 15334 -521 -4083 1582 O ATOM 4078 ND2 ASN B 313 -52.112 -30.392 11.269 1.00132.62 N ANISOU 4078 ND2 ASN B 313 14998 16067 19325 -448 -4139 1565 N ATOM 4079 N VAL B 314 -52.549 -33.997 14.008 1.00 65.51 N ANISOU 4079 N VAL B 314 6453 7453 10983 -598 -4057 1577 N ATOM 4080 CA VAL B 314 -52.956 -35.318 13.544 1.00 79.34 C ANISOU 4080 CA VAL B 314 8180 9218 12747 -618 -4102 1550 C ATOM 4081 C VAL B 314 -54.287 -35.769 14.159 1.00 87.29 C ANISOU 4081 C VAL B 314 9102 10302 13763 -632 -4129 1540 C ATOM 4082 O VAL B 314 -55.181 -36.227 13.452 1.00 78.07 O ANISOU 4082 O VAL B 314 7881 9208 12575 -616 -4194 1493 O ATOM 4083 CB VAL B 314 -51.855 -36.375 13.796 1.00 59.13 C ANISOU 4083 CB VAL B 314 5677 6536 10253 -671 -4079 1583 C ATOM 4084 CG1 VAL B 314 -52.441 -37.768 13.817 1.00 59.87 C ANISOU 4084 CG1 VAL B 314 5738 6619 10389 -706 -4131 1570 C ATOM 4085 CG2 VAL B 314 -50.774 -36.272 12.737 1.00 58.81 C ANISOU 4085 CG2 VAL B 314 5684 6475 10186 -644 -4080 1564 C ATOM 4086 N PHE B 315 -54.420 -35.630 15.473 1.00 91.83 N ANISOU 4086 N PHE B 315 9655 10875 14363 -660 -4084 1584 N ATOM 4087 CA PHE B 315 -55.594 -36.146 16.174 1.00 96.10 C ANISOU 4087 CA PHE B 315 10098 11508 14907 -683 -4104 1588 C ATOM 4088 C PHE B 315 -56.893 -35.375 15.942 1.00118.28 C ANISOU 4088 C PHE B 315 12807 14477 17657 -620 -4139 1530 C ATOM 4089 O PHE B 315 -57.899 -35.958 15.549 1.00121.64 O ANISOU 4089 O PHE B 315 13154 14984 18080 -625 -4196 1501 O ATOM 4090 CB PHE B 315 -55.296 -36.313 17.664 1.00 99.64 C ANISOU 4090 CB PHE B 315 10544 11931 15384 -733 -4048 1656 C ATOM 4091 CG PHE B 315 -54.557 -37.577 17.979 1.00124.78 C ANISOU 4091 CG PHE B 315 13784 14985 18642 -811 -4048 1720 C ATOM 4092 CD1 PHE B 315 -55.015 -38.440 18.956 1.00145.18 C ANISOU 4092 CD1 PHE B 315 16314 17591 21256 -877 -4053 1783 C ATOM 4093 CD2 PHE B 315 -53.419 -37.920 17.267 1.00124.56 C ANISOU 4093 CD2 PHE B 315 13851 14824 18653 -817 -4050 1719 C ATOM 4094 CE1 PHE B 315 -54.338 -39.612 19.236 1.00145.06 C ANISOU 4094 CE1 PHE B 315 16355 17441 21319 -949 -4068 1849 C ATOM 4095 CE2 PHE B 315 -52.740 -39.090 17.540 1.00125.01 C ANISOU 4095 CE2 PHE B 315 13955 14757 18786 -878 -4061 1768 C ATOM 4096 CZ PHE B 315 -53.198 -39.936 18.526 1.00131.66 C ANISOU 4096 CZ PHE B 315 14758 15597 19670 -944 -4075 1836 C ATOM 4097 N ASN B 316 -56.875 -34.072 16.191 1.00137.39 N ANISOU 4097 N ASN B 316 15225 16938 20038 -560 -4115 1510 N ATOM 4098 CA ASN B 316 -58.038 -33.229 15.926 1.00150.70 C ANISOU 4098 CA ASN B 316 16817 18768 21673 -484 -4157 1447 C ATOM 4099 C ASN B 316 -57.629 -31.967 15.173 1.00140.80 C ANISOU 4099 C ASN B 316 15623 17484 20392 -417 -4172 1422 C ATOM 4100 O ASN B 316 -56.902 -31.127 15.705 1.00156.94 O ANISOU 4100 O ASN B 316 17721 19467 22443 -403 -4133 1441 O ATOM 4101 CB ASN B 316 -58.755 -32.864 17.233 1.00172.07 C ANISOU 4101 CB ASN B 316 19420 21602 24358 -464 -4130 1439 C ATOM 4102 CG ASN B 316 -59.600 -34.007 17.783 1.00175.72 C ANISOU 4102 CG ASN B 316 19777 22158 24832 -523 -4139 1458 C ATOM 4103 OD1 ASN B 316 -60.234 -34.743 17.028 1.00185.39 O ANISOU 4103 OD1 ASN B 316 20960 23408 26071 -545 -4195 1443 O ATOM 4104 ND2 ASN B 316 -59.617 -34.153 19.105 1.00168.15 N ANISOU 4104 ND2 ASN B 316 18768 21256 23866 -551 -4092 1493 N ATOM 4105 N ARG B 317 -58.100 -31.830 13.937 1.00105.23 N ANISOU 4105 N ARG B 317 11107 13019 15856 -378 -4238 1383 N ATOM 4106 CA ARG B 317 -57.632 -30.745 13.079 1.00111.90 C ANISOU 4106 CA ARG B 317 12016 13828 16674 -328 -4264 1378 C ATOM 4107 C ARG B 317 -58.117 -29.355 13.496 1.00120.87 C ANISOU 4107 C ARG B 317 13114 15016 17795 -253 -4282 1352 C ATOM 4108 O ARG B 317 -57.310 -28.451 13.715 1.00113.42 O ANISOU 4108 O ARG B 317 12238 13989 16866 -243 -4261 1378 O ATOM 4109 CB ARG B 317 -57.986 -31.011 11.611 1.00109.37 C ANISOU 4109 CB ARG B 317 11693 13550 16312 -306 -4339 1348 C ATOM 4110 CG ARG B 317 -57.207 -32.151 10.974 1.00125.95 C ANISOU 4110 CG ARG B 317 13852 15587 18418 -359 -4333 1363 C ATOM 4111 CD ARG B 317 -57.276 -32.099 9.448 1.00158.25 C ANISOU 4111 CD ARG B 317 17957 19727 22443 -320 -4407 1332 C ATOM 4112 NE ARG B 317 -58.639 -32.236 8.936 1.00182.02 N ANISOU 4112 NE ARG B 317 20881 22851 25427 -283 -4492 1276 N ATOM 4113 CZ ARG B 317 -59.201 -33.392 8.591 1.00180.31 C ANISOU 4113 CZ ARG B 317 20621 22670 25218 -310 -4539 1239 C ATOM 4114 NH1 ARG B 317 -58.521 -34.526 8.701 1.00178.63 N ANISOU 4114 NH1 ARG B 317 20447 22381 25042 -367 -4514 1249 N ATOM 4115 NH2 ARG B 317 -60.447 -33.416 8.135 1.00171.51 N ANISOU 4115 NH2 ARG B 317 19422 21660 24084 -278 -4622 1191 N ATOM 4116 N ASP B 318 -59.430 -29.187 13.617 1.00137.23 N ANISOU 4116 N ASP B 318 15071 17226 19844 -199 -4328 1298 N ATOM 4117 CA ASP B 318 -59.999 -27.867 13.881 1.00142.95 C ANISOU 4117 CA ASP B 318 15748 18013 20554 -108 -4365 1257 C ATOM 4118 C ASP B 318 -60.017 -27.493 15.363 1.00151.48 C ANISOU 4118 C ASP B 318 16782 19130 21642 -88 -4313 1244 C ATOM 4119 O ASP B 318 -60.427 -26.389 15.726 1.00150.58 O ANISOU 4119 O ASP B 318 16626 19069 21519 -4 -4345 1201 O ATOM 4120 CB ASP B 318 -61.393 -27.722 13.251 1.00143.28 C ANISOU 4120 CB ASP B 318 15678 18197 20564 -42 -4450 1198 C ATOM 4121 CG ASP B 318 -62.204 -29.002 13.314 1.00143.43 C ANISOU 4121 CG ASP B 318 15600 18316 20580 -87 -4452 1182 C ATOM 4122 OD1 ASP B 318 -63.004 -29.244 12.383 1.00119.68 O ANISOU 4122 OD1 ASP B 318 12542 15376 17556 -69 -4527 1151 O ATOM 4123 OD2 ASP B 318 -62.045 -29.764 14.290 1.00160.06 O ANISOU 4123 OD2 ASP B 318 17680 20431 22704 -146 -4388 1204 O ATOM 4124 N LEU B 319 -59.568 -28.409 16.216 1.00154.99 N ANISOU 4124 N LEU B 319 17233 19553 22102 -161 -4242 1280 N ATOM 4125 CA LEU B 319 -59.399 -28.095 17.627 1.00151.65 C ANISOU 4125 CA LEU B 319 16779 19165 21675 -149 -4192 1275 C ATOM 4126 C LEU B 319 -58.136 -27.264 17.793 1.00133.32 C ANISOU 4126 C LEU B 319 14586 16681 19388 -154 -4171 1308 C ATOM 4127 O LEU B 319 -57.868 -26.729 18.869 1.00120.80 O ANISOU 4127 O LEU B 319 12994 15103 17801 -128 -4146 1296 O ATOM 4128 CB LEU B 319 -59.326 -29.368 18.481 1.00165.18 C ANISOU 4128 CB LEU B 319 18460 20907 23394 -233 -4133 1317 C ATOM 4129 CG LEU B 319 -60.625 -29.866 19.131 1.00182.36 C ANISOU 4129 CG LEU B 319 20463 23297 25529 -217 -4140 1279 C ATOM 4130 CD1 LEU B 319 -61.576 -30.450 18.097 1.00190.23 C ANISOU 4130 CD1 LEU B 319 21392 24359 26526 -224 -4199 1258 C ATOM 4131 CD2 LEU B 319 -60.338 -30.891 20.222 1.00182.31 C ANISOU 4131 CD2 LEU B 319 20437 23303 25528 -304 -4081 1338 C ATOM 4132 N VAL B 320 -57.360 -27.166 16.715 1.00138.41 N ANISOU 4132 N VAL B 320 15337 17193 20060 -187 -4187 1348 N ATOM 4133 CA VAL B 320 -56.118 -26.404 16.730 1.00134.41 C ANISOU 4133 CA VAL B 320 14944 16531 19594 -206 -4173 1390 C ATOM 4134 C VAL B 320 -56.167 -25.202 15.789 1.00121.95 C ANISOU 4134 C VAL B 320 13398 14919 18019 -150 -4248 1379 C ATOM 4135 O VAL B 320 -55.891 -25.339 14.596 1.00106.43 O ANISOU 4135 O VAL B 320 11477 12917 16045 -174 -4274 1411 O ATOM 4136 CB VAL B 320 -54.956 -27.304 16.259 1.00123.80 C ANISOU 4136 CB VAL B 320 13693 15065 18280 -303 -4126 1462 C ATOM 4137 CG1 VAL B 320 -53.647 -26.534 16.234 1.00108.07 C ANISOU 4137 CG1 VAL B 320 11802 12925 16334 -333 -4114 1512 C ATOM 4138 CG2 VAL B 320 -54.848 -28.538 17.138 1.00128.29 C ANISOU 4138 CG2 VAL B 320 14243 15641 18860 -366 -4066 1485 C ATOM 4139 N PRO B 321 -56.420 -24.005 16.344 1.00117.93 N ANISOU 4139 N PRO B 321 12870 14415 17522 -77 -4290 1338 N ATOM 4140 CA PRO B 321 -56.433 -22.751 15.579 1.00104.21 C ANISOU 4140 CA PRO B 321 11169 12622 15804 -25 -4376 1336 C ATOM 4141 C PRO B 321 -55.135 -22.577 14.800 1.00 97.45 C ANISOU 4141 C PRO B 321 10428 11614 14983 -103 -4370 1424 C ATOM 4142 O PRO B 321 -54.093 -23.010 15.280 1.00110.02 O ANISOU 4142 O PRO B 321 12077 13120 16607 -178 -4302 1471 O ATOM 4143 CB PRO B 321 -56.562 -21.690 16.671 1.00 91.74 C ANISOU 4143 CB PRO B 321 9569 11037 14252 47 -4405 1283 C ATOM 4144 CG PRO B 321 -57.373 -22.373 17.728 1.00111.37 C ANISOU 4144 CG PRO B 321 11941 13686 16688 81 -4357 1224 C ATOM 4145 CD PRO B 321 -56.946 -23.822 17.708 1.00119.71 C ANISOU 4145 CD PRO B 321 13015 14738 17732 -23 -4272 1280 C ATOM 4146 N ASP B 322 -55.202 -21.963 13.620 1.00 98.11 N ANISOU 4146 N ASP B 322 10537 11680 15059 -85 -4444 1450 N ATOM 4147 CA ASP B 322 -54.061 -21.918 12.701 1.00105.38 C ANISOU 4147 CA ASP B 322 11541 12510 15989 -159 -4438 1541 C ATOM 4148 C ASP B 322 -53.156 -20.693 12.873 1.00116.02 C ANISOU 4148 C ASP B 322 12957 13717 17408 -182 -4476 1593 C ATOM 4149 O ASP B 322 -52.087 -20.625 12.268 1.00129.69 O ANISOU 4149 O ASP B 322 14745 15379 19153 -253 -4464 1680 O ATOM 4150 CB ASP B 322 -54.540 -22.030 11.243 1.00112.74 C ANISOU 4150 CB ASP B 322 12459 13521 16855 -137 -4498 1555 C ATOM 4151 CG ASP B 322 -53.409 -22.333 10.267 1.00112.77 C ANISOU 4151 CG ASP B 322 12522 13491 16833 -208 -4475 1643 C ATOM 4152 OD1 ASP B 322 -53.079 -23.524 10.084 1.00119.84 O ANISOU 4152 OD1 ASP B 322 13415 14424 17694 -249 -4410 1645 O ATOM 4153 OD2 ASP B 322 -52.860 -21.385 9.667 1.00110.73 O ANISOU 4153 OD2 ASP B 322 12306 13178 16587 -220 -4528 1711 O ATOM 4154 N TRP B 323 -53.572 -19.725 13.685 1.00120.89 N ANISOU 4154 N TRP B 323 13561 14301 18072 -119 -4530 1540 N ATOM 4155 CA TRP B 323 -52.703 -18.583 13.966 1.00127.44 C ANISOU 4155 CA TRP B 323 14456 14978 18986 -146 -4579 1583 C ATOM 4156 C TRP B 323 -51.669 -18.971 15.022 1.00130.80 C ANISOU 4156 C TRP B 323 14920 15321 19458 -216 -4495 1602 C ATOM 4157 O TRP B 323 -50.509 -18.561 14.956 1.00138.70 O ANISOU 4157 O TRP B 323 15983 16196 20522 -294 -4496 1680 O ATOM 4158 CB TRP B 323 -53.509 -17.340 14.370 1.00135.26 C ANISOU 4158 CB TRP B 323 15425 15952 20017 -43 -4690 1510 C ATOM 4159 CG TRP B 323 -53.880 -17.250 15.824 1.00153.39 C ANISOU 4159 CG TRP B 323 17681 18275 22327 22 -4671 1412 C ATOM 4160 CD1 TRP B 323 -54.494 -18.208 16.579 1.00156.98 C ANISOU 4160 CD1 TRP B 323 18060 18869 22718 53 -4591 1349 C ATOM 4161 CD2 TRP B 323 -53.692 -16.119 16.686 1.00164.96 C ANISOU 4161 CD2 TRP B 323 19171 19641 23867 70 -4745 1364 C ATOM 4162 NE1 TRP B 323 -54.682 -17.750 17.862 1.00161.06 N ANISOU 4162 NE1 TRP B 323 18546 19400 23250 120 -4601 1270 N ATOM 4163 CE2 TRP B 323 -54.200 -16.470 17.952 1.00171.29 C ANISOU 4163 CE2 TRP B 323 19905 20546 24630 137 -4697 1269 C ATOM 4164 CE3 TRP B 323 -53.137 -14.846 16.511 1.00156.50 C ANISOU 4164 CE3 TRP B 323 18169 18403 22892 60 -4855 1395 C ATOM 4165 CZ2 TRP B 323 -54.169 -15.594 19.038 1.00173.32 C ANISOU 4165 CZ2 TRP B 323 20163 20759 24932 209 -4755 1192 C ATOM 4166 CZ3 TRP B 323 -53.107 -13.978 17.591 1.00143.93 C ANISOU 4166 CZ3 TRP B 323 16586 16740 21362 124 -4920 1315 C ATOM 4167 CH2 TRP B 323 -53.619 -14.356 18.836 1.00155.83 C ANISOU 4167 CH2 TRP B 323 18027 18364 22819 204 -4869 1209 C ATOM 4168 N LEU B 324 -52.099 -19.784 15.982 1.00118.96 N ANISOU 4168 N LEU B 324 14667 11849 18684 552 -4412 -946 N ATOM 4169 CA LEU B 324 -51.201 -20.350 16.979 1.00101.35 C ANISOU 4169 CA LEU B 324 12447 9678 16385 556 -4341 -952 C ATOM 4170 C LEU B 324 -50.115 -21.170 16.301 1.00 95.33 C ANISOU 4170 C LEU B 324 11769 8945 15507 583 -4335 -981 C ATOM 4171 O LEU B 324 -48.963 -21.174 16.737 1.00116.39 O ANISOU 4171 O LEU B 324 14474 11672 18076 601 -4277 -1000 O ATOM 4172 CB LEU B 324 -51.981 -21.241 17.942 1.00 87.46 C ANISOU 4172 CB LEU B 324 10604 7884 14741 527 -4348 -922 C ATOM 4173 CG LEU B 324 -51.951 -20.834 19.412 1.00 86.29 C ANISOU 4173 CG LEU B 324 10406 7766 14614 518 -4298 -909 C ATOM 4174 CD1 LEU B 324 -52.340 -19.371 19.564 1.00110.31 C ANISOU 4174 CD1 LEU B 324 13419 10809 17685 514 -4289 -902 C ATOM 4175 CD2 LEU B 324 -52.869 -21.727 20.222 1.00 52.34 C ANISOU 4175 CD2 LEU B 324 6012 3419 10457 489 -4318 -875 C ATOM 4176 N PHE B 325 -50.496 -21.867 15.235 1.00 87.27 N ANISOU 4176 N PHE B 325 10774 7876 14508 588 -4402 -985 N ATOM 4177 CA PHE B 325 -49.577 -22.716 14.483 1.00108.48 C ANISOU 4177 CA PHE B 325 13540 10581 17098 614 -4408 -1011 C ATOM 4178 C PHE B 325 -48.372 -21.899 14.038 1.00103.84 C ANISOU 4178 C PHE B 325 13018 10050 16385 643 -4366 -1039 C ATOM 4179 O PHE B 325 -47.258 -22.412 13.974 1.00132.24 O ANISOU 4179 O PHE B 325 16659 13689 19897 662 -4331 -1058 O ATOM 4180 CB PHE B 325 -50.291 -23.332 13.272 1.00146.22 C ANISOU 4180 CB PHE B 325 18347 15288 21921 620 -4508 -1016 C ATOM 4181 CG PHE B 325 -49.689 -24.631 12.781 1.00130.40 C ANISOU 4181 CG PHE B 325 16400 13286 19860 637 -4524 -1033 C ATOM 4182 CD1 PHE B 325 -49.560 -25.722 13.630 1.00 83.02 C ANISOU 4182 CD1 PHE B 325 10363 7296 13884 622 -4492 -1022 C ATOM 4183 CD2 PHE B 325 -49.294 -24.768 11.455 1.00135.25 C ANISOU 4183 CD2 PHE B 325 17104 13885 20398 670 -4580 -1061 C ATOM 4184 CE1 PHE B 325 -49.022 -26.915 13.173 1.00 78.99 C ANISOU 4184 CE1 PHE B 325 9901 6785 13325 637 -4509 -1038 C ATOM 4185 CE2 PHE B 325 -48.758 -25.958 10.990 1.00118.49 C ANISOU 4185 CE2 PHE B 325 15034 11761 18225 687 -4599 -1077 C ATOM 4186 CZ PHE B 325 -48.621 -27.032 11.850 1.00101.20 C ANISOU 4186 CZ PHE B 325 12803 9584 16063 670 -4561 -1065 C ATOM 4187 N VAL B 326 -48.599 -20.629 13.717 1.00 80.77 N ANISOU 4187 N VAL B 326 10097 7128 13464 646 -4373 -1039 N ATOM 4188 CA VAL B 326 -47.501 -19.718 13.405 1.00 94.11 C ANISOU 4188 CA VAL B 326 11833 8871 15055 670 -4329 -1062 C ATOM 4189 C VAL B 326 -46.839 -19.120 14.661 1.00108.11 C ANISOU 4189 C VAL B 326 13569 10700 16807 664 -4245 -1060 C ATOM 4190 O VAL B 326 -45.603 -19.033 14.758 1.00108.15 O ANISOU 4190 O VAL B 326 13602 10753 16736 683 -4198 -1080 O ATOM 4191 CB VAL B 326 -47.968 -18.597 12.465 1.00 90.90 C ANISOU 4191 CB VAL B 326 11448 8437 14653 680 -4379 -1066 C ATOM 4192 CG1 VAL B 326 -46.806 -17.687 12.120 1.00107.43 C ANISOU 4192 CG1 VAL B 326 13583 10584 16652 703 -4335 -1088 C ATOM 4193 CG2 VAL B 326 -48.573 -19.191 11.204 1.00 91.58 C ANISOU 4193 CG2 VAL B 326 11586 8459 14753 694 -4483 -1074 C ATOM 4194 N ALA B 327 -47.669 -18.722 15.623 1.00108.63 N ANISOU 4194 N ALA B 327 13572 10754 16950 641 -4236 -1037 N ATOM 4195 CA ALA B 327 -47.185 -18.088 16.848 1.00 89.76 C ANISOU 4195 CA ALA B 327 11155 8406 14542 639 -4175 -1039 C ATOM 4196 C ALA B 327 -46.136 -18.936 17.556 1.00 86.42 C ANISOU 4196 C ALA B 327 10752 8021 14063 652 -4137 -1054 C ATOM 4197 O ALA B 327 -45.216 -18.400 18.171 1.00 82.73 O ANISOU 4197 O ALA B 327 10294 7594 13546 666 -4096 -1071 O ATOM 4198 CB ALA B 327 -48.340 -17.782 17.789 1.00 73.33 C ANISOU 4198 CB ALA B 327 9003 6298 12562 612 -4184 -1011 C ATOM 4199 N PHE B 328 -46.289 -20.256 17.482 1.00 92.97 N ANISOU 4199 N PHE B 328 11585 8830 14909 647 -4161 -1050 N ATOM 4200 CA PHE B 328 -45.354 -21.174 18.136 1.00 70.66 C ANISOU 4200 CA PHE B 328 8777 6032 12038 660 -4138 -1064 C ATOM 4201 C PHE B 328 -44.065 -21.414 17.355 1.00 65.28 C ANISOU 4201 C PHE B 328 8149 5379 11275 686 -4124 -1092 C ATOM 4202 O PHE B 328 -43.006 -21.557 17.963 1.00 84.57 O ANISOU 4202 O PHE B 328 10603 7853 13678 702 -4096 -1111 O ATOM 4203 CB PHE B 328 -46.032 -22.497 18.505 1.00 49.18 C ANISOU 4203 CB PHE B 328 6032 3279 9376 644 -4168 -1047 C ATOM 4204 CG PHE B 328 -46.994 -22.379 19.655 1.00 83.55 C ANISOU 4204 CG PHE B 328 10321 7611 13812 621 -4175 -1022 C ATOM 4205 CD1 PHE B 328 -47.020 -21.232 20.438 1.00 91.00 C ANISOU 4205 CD1 PHE B 328 11247 8573 14756 623 -4151 -1023 C ATOM 4206 CD2 PHE B 328 -47.869 -23.409 19.956 1.00 75.42 C ANISOU 4206 CD2 PHE B 328 9247 6541 12870 599 -4208 -999 C ATOM 4207 CE1 PHE B 328 -47.904 -21.115 21.496 1.00 88.54 C ANISOU 4207 CE1 PHE B 328 10876 8240 14525 606 -4164 -1000 C ATOM 4208 CE2 PHE B 328 -48.755 -23.299 21.012 1.00 70.83 C ANISOU 4208 CE2 PHE B 328 8596 5935 12381 579 -4218 -973 C ATOM 4209 CZ PHE B 328 -48.772 -22.152 21.783 1.00 79.99 C ANISOU 4209 CZ PHE B 328 9742 7114 13537 583 -4198 -974 C ATOM 4210 N ASN B 329 -44.144 -21.464 16.024 1.00 48.77 N ANISOU 4210 N ASN B 329 6091 3272 9168 693 -4153 -1096 N ATOM 4211 CA ASN B 329 -42.929 -21.567 15.209 1.00 63.81 C ANISOU 4211 CA ASN B 329 8041 5201 11001 718 -4144 -1122 C ATOM 4212 C ASN B 329 -42.091 -20.297 15.357 1.00 78.13 C ANISOU 4212 C ASN B 329 9849 7050 12786 729 -4104 -1137 C ATOM 4213 O ASN B 329 -40.855 -20.337 15.288 1.00 81.96 O ANISOU 4213 O ASN B 329 10344 7562 13234 747 -4082 -1158 O ATOM 4214 CB ASN B 329 -43.230 -21.874 13.730 1.00 49.04 C ANISOU 4214 CB ASN B 329 6219 3301 9112 729 -4198 -1127 C ATOM 4215 CG ASN B 329 -42.261 -22.904 13.126 1.00 64.08 C ANISOU 4215 CG ASN B 329 8167 5216 10964 750 -4207 -1148 C ATOM 4216 OD1 ASN B 329 -41.124 -23.042 13.576 1.00 73.26 O ANISOU 4216 OD1 ASN B 329 9322 6414 12101 761 -4169 -1164 O ATOM 4217 ND2 ASN B 329 -42.719 -23.634 12.107 1.00 57.76 N ANISOU 4217 ND2 ASN B 329 7412 4379 10155 758 -4267 -1151 N ATOM 4218 N TRP B 330 -42.754 -19.165 15.581 1.00 48.11 N ANISOU 4218 N TRP B 330 6023 3244 9011 718 -4098 -1124 N ATOM 4219 CA TRP B 330 -41.991 -17.957 15.896 1.00 90.79 C ANISOU 4219 CA TRP B 330 11416 8682 14398 726 -4059 -1137 C ATOM 4220 C TRP B 330 -41.475 -17.976 17.342 1.00 97.09 C ANISOU 4220 C TRP B 330 12189 9500 15201 728 -4027 -1144 C ATOM 4221 O TRP B 330 -40.294 -17.724 17.588 1.00 47.25 O ANISOU 4221 O TRP B 330 5875 3211 8866 744 -4006 -1167 O ATOM 4222 CB TRP B 330 -42.760 -16.675 15.547 1.00 69.37 C ANISOU 4222 CB TRP B 330 8692 5958 11706 717 -4067 -1126 C ATOM 4223 CG TRP B 330 -42.768 -16.413 14.060 1.00 63.68 C ANISOU 4223 CG TRP B 330 8012 5223 10960 730 -4105 -1132 C ATOM 4224 CD1 TRP B 330 -43.749 -16.750 13.177 1.00 67.14 C ANISOU 4224 CD1 TRP B 330 8476 5619 11414 728 -4166 -1123 C ATOM 4225 CD2 TRP B 330 -41.731 -15.788 13.285 1.00 78.04 C ANISOU 4225 CD2 TRP B 330 9852 7064 12735 749 -4096 -1153 C ATOM 4226 NE1 TRP B 330 -43.397 -16.364 11.905 1.00 80.54 N ANISOU 4226 NE1 TRP B 330 10224 7311 13066 750 -4202 -1139 N ATOM 4227 CE2 TRP B 330 -42.163 -15.772 11.943 1.00 85.84 C ANISOU 4227 CE2 TRP B 330 10890 8024 13702 762 -4156 -1156 C ATOM 4228 CE3 TRP B 330 -40.483 -15.238 13.595 1.00 71.52 C ANISOU 4228 CE3 TRP B 330 9005 6273 11897 758 -4053 -1171 C ATOM 4229 CZ2 TRP B 330 -41.394 -15.225 10.912 1.00 82.80 C ANISOU 4229 CZ2 TRP B 330 10540 7649 13273 786 -4172 -1175 C ATOM 4230 CZ3 TRP B 330 -39.717 -14.696 12.567 1.00 60.80 C ANISOU 4230 CZ3 TRP B 330 7665 4923 10514 776 -4064 -1187 C ATOM 4231 CH2 TRP B 330 -40.178 -14.694 11.244 1.00 65.84 C ANISOU 4231 CH2 TRP B 330 8358 5537 11121 790 -4122 -1189 C ATOM 4232 N LEU B 331 -42.345 -18.326 18.285 1.00 90.95 N ANISOU 4232 N LEU B 331 11390 8707 14458 713 -4036 -1128 N ATOM 4233 CA LEU B 331 -41.945 -18.438 19.681 1.00 82.74 C ANISOU 4233 CA LEU B 331 10341 7682 13416 721 -4026 -1138 C ATOM 4234 C LEU B 331 -40.658 -19.244 19.744 1.00 87.84 C ANISOU 4234 C LEU B 331 11009 8341 14027 743 -4024 -1164 C ATOM 4235 O LEU B 331 -39.751 -18.930 20.515 1.00 74.45 O ANISOU 4235 O LEU B 331 9312 6658 12316 761 -4018 -1187 O ATOM 4236 CB LEU B 331 -43.040 -19.129 20.499 1.00 72.95 C ANISOU 4236 CB LEU B 331 9080 6416 12221 705 -4049 -1116 C ATOM 4237 CG LEU B 331 -42.952 -19.114 22.030 1.00 56.74 C ANISOU 4237 CG LEU B 331 7022 4368 10168 716 -4057 -1125 C ATOM 4238 CD1 LEU B 331 -44.210 -19.711 22.642 1.00 64.46 C ANISOU 4238 CD1 LEU B 331 7966 5315 11209 695 -4086 -1098 C ATOM 4239 CD2 LEU B 331 -41.727 -19.853 22.534 1.00 47.69 C ANISOU 4239 CD2 LEU B 331 5908 3236 8977 743 -4064 -1155 C ATOM 4240 N GLY B 332 -40.590 -20.283 18.918 1.00104.92 N ANISOU 4240 N GLY B 332 13187 10494 16182 742 -4038 -1161 N ATOM 4241 CA GLY B 332 -39.412 -21.123 18.830 1.00115.14 C ANISOU 4241 CA GLY B 332 14498 11797 17453 761 -4043 -1184 C ATOM 4242 C GLY B 332 -38.255 -20.433 18.133 1.00100.11 C ANISOU 4242 C GLY B 332 12593 9910 15533 776 -4027 -1206 C ATOM 4243 O GLY B 332 -37.102 -20.561 18.563 1.00 73.14 O ANISOU 4243 O GLY B 332 9168 6502 12120 794 -4028 -1231 O ATOM 4244 N TYR B 333 -38.548 -19.707 17.055 1.00 47.37 N ANISOU 4244 N TYR B 333 5919 3232 8848 770 -4022 -1199 N ATOM 4245 CA TYR B 333 -37.492 -18.952 16.396 1.00 71.35 C ANISOU 4245 CA TYR B 333 8946 6283 11879 783 -4010 -1218 C ATOM 4246 C TYR B 333 -36.747 -18.171 17.474 1.00 90.06 C ANISOU 4246 C TYR B 333 11283 8663 14272 789 -3992 -1235 C ATOM 4247 O TYR B 333 -35.516 -18.083 17.453 1.00 97.63 O ANISOU 4247 O TYR B 333 12220 9625 15251 803 -3992 -1259 O ATOM 4248 CB TYR B 333 -38.055 -18.000 15.337 1.00 79.04 C ANISOU 4248 CB TYR B 333 9932 7255 12844 777 -4013 -1208 C ATOM 4249 CG TYR B 333 -38.476 -18.658 14.036 1.00 89.63 C ANISOU 4249 CG TYR B 333 11318 8580 14158 782 -4050 -1203 C ATOM 4250 CD1 TYR B 333 -37.626 -19.517 13.349 1.00 47.63 C ANISOU 4250 CD1 TYR B 333 6018 3262 8817 799 -4068 -1221 C ATOM 4251 CD2 TYR B 333 -39.726 -18.406 13.490 1.00106.79 C ANISOU 4251 CD2 TYR B 333 13514 10730 16330 773 -4079 -1184 C ATOM 4252 CE1 TYR B 333 -38.022 -20.109 12.162 1.00 47.94 C ANISOU 4252 CE1 TYR B 333 6111 3283 8822 810 -4114 -1221 C ATOM 4253 CE2 TYR B 333 -40.125 -18.993 12.310 1.00 94.86 C ANISOU 4253 CE2 TYR B 333 12055 9196 14793 783 -4130 -1186 C ATOM 4254 CZ TYR B 333 -39.272 -19.840 11.651 1.00 48.21 C ANISOU 4254 CZ TYR B 333 6176 3291 8850 803 -4147 -1204 C ATOM 4255 OH TYR B 333 -39.686 -20.411 10.475 1.00 48.68 O ANISOU 4255 OH TYR B 333 6300 3324 8874 818 -4208 -1209 O ATOM 4256 N ALA B 334 -37.504 -17.648 18.438 1.00 99.81 N ANISOU 4256 N ALA B 334 12513 9898 15514 781 -3985 -1224 N ATOM 4257 CA ALA B 334 -36.950 -16.836 19.522 1.00103.52 C ANISOU 4257 CA ALA B 334 12963 10372 15998 791 -3979 -1242 C ATOM 4258 C ALA B 334 -35.771 -17.510 20.224 1.00 83.45 C ANISOU 4258 C ALA B 334 10418 7823 13468 814 -4002 -1273 C ATOM 4259 O ALA B 334 -34.867 -16.838 20.726 1.00 70.44 O ANISOU 4259 O ALA B 334 8747 6171 11845 828 -4009 -1298 O ATOM 4260 CB ALA B 334 -38.040 -16.492 20.531 1.00 91.22 C ANISOU 4260 CB ALA B 334 11411 8811 14439 784 -3982 -1227 C ATOM 4261 N ASN B 335 -35.769 -18.837 20.240 1.00 47.61 N ANISOU 4261 N ASN B 335 5896 3276 8917 818 -4022 -1271 N ATOM 4262 CA ASN B 335 -34.701 -19.562 20.893 1.00 47.99 C ANISOU 4262 CA ASN B 335 5942 3311 8980 841 -4055 -1301 C ATOM 4263 C ASN B 335 -33.386 -18.964 20.417 1.00 48.19 C ANISOU 4263 C ASN B 335 5928 3333 9049 850 -4055 -1327 C ATOM 4264 O ASN B 335 -32.578 -18.515 21.220 1.00 48.57 O ANISOU 4264 O ASN B 335 5957 3367 9132 868 -4080 -1355 O ATOM 4265 CB ASN B 335 -34.798 -21.056 20.556 1.00 48.06 C ANISOU 4265 CB ASN B 335 5971 3314 8975 841 -4071 -1294 C ATOM 4266 CG ASN B 335 -33.948 -21.931 21.470 1.00 56.28 C ANISOU 4266 CG ASN B 335 7018 4337 10029 867 -4118 -1323 C ATOM 4267 OD1 ASN B 335 -33.316 -22.886 21.019 1.00 48.71 O ANISOU 4267 OD1 ASN B 335 6056 3371 9081 874 -4135 -1332 O ATOM 4268 ND2 ASN B 335 -33.932 -21.609 22.758 1.00 48.79 N ANISOU 4268 ND2 ASN B 335 6082 3378 9077 885 -4147 -1339 N ATOM 4269 N SER B 336 -33.215 -18.890 19.103 1.00 69.05 N ANISOU 4269 N SER B 336 8555 5983 11697 839 -4035 -1318 N ATOM 4270 CA SER B 336 -31.956 -18.446 18.512 1.00 80.68 C ANISOU 4270 CA SER B 336 9979 7448 13228 846 -4039 -1342 C ATOM 4271 C SER B 336 -31.429 -17.167 19.162 1.00 82.13 C ANISOU 4271 C SER B 336 10124 7623 13459 849 -4038 -1360 C ATOM 4272 O SER B 336 -30.267 -17.105 19.563 1.00 98.97 O ANISOU 4272 O SER B 336 12213 9731 15661 863 -4069 -1391 O ATOM 4273 CB SER B 336 -32.121 -18.240 17.002 1.00 70.92 C ANISOU 4273 CB SER B 336 8743 6224 11979 835 -4021 -1327 C ATOM 4274 OG SER B 336 -31.091 -18.891 16.281 1.00 48.31 O ANISOU 4274 OG SER B 336 5853 3349 9155 846 -4043 -1346 O ATOM 4275 N ALA B 337 -32.284 -16.155 19.275 1.00 63.34 N ANISOU 4275 N ALA B 337 7757 5258 11051 838 -4011 -1342 N ATOM 4276 CA ALA B 337 -31.873 -14.880 19.855 1.00 71.42 C ANISOU 4276 CA ALA B 337 8748 6274 12116 841 -4010 -1358 C ATOM 4277 C ALA B 337 -31.762 -14.988 21.369 1.00 87.87 C ANISOU 4277 C ALA B 337 10850 8339 14196 863 -4049 -1380 C ATOM 4278 O ALA B 337 -31.140 -14.145 22.016 1.00115.43 O ANISOU 4278 O ALA B 337 14316 11812 17731 875 -4071 -1406 O ATOM 4279 CB ALA B 337 -32.840 -13.769 19.466 1.00 47.86 C ANISOU 4279 CB ALA B 337 5772 3310 9102 823 -3973 -1333 C ATOM 4280 N MET B 338 -32.370 -16.028 21.928 1.00 62.56 N ANISOU 4280 N MET B 338 7692 5136 10942 870 -4067 -1372 N ATOM 4281 CA MET B 338 -32.322 -16.251 23.368 1.00 72.77 C ANISOU 4281 CA MET B 338 9017 6411 12221 897 -4117 -1396 C ATOM 4282 C MET B 338 -30.972 -16.847 23.784 1.00 91.43 C ANISOU 4282 C MET B 338 11362 8740 14639 924 -4178 -1437 C ATOM 4283 O MET B 338 -30.471 -16.565 24.870 1.00103.23 O ANISOU 4283 O MET B 338 12867 10205 16151 954 -4237 -1471 O ATOM 4284 CB MET B 338 -33.473 -17.165 23.822 1.00 72.10 C ANISOU 4284 CB MET B 338 8984 6337 12073 894 -4120 -1372 C ATOM 4285 CG MET B 338 -34.878 -16.594 23.619 1.00 69.06 C ANISOU 4285 CG MET B 338 8611 5974 11655 869 -4078 -1335 C ATOM 4286 SD MET B 338 -36.212 -17.799 23.869 1.00 85.83 S ANISOU 4286 SD MET B 338 10770 8100 13743 856 -4083 -1304 S ATOM 4287 CE MET B 338 -36.413 -17.733 25.644 1.00 58.06 C ANISOU 4287 CE MET B 338 7293 4567 10200 888 -4141 -1327 C ATOM 4288 N ASN B 339 -30.380 -17.659 22.913 1.00 90.35 N ANISOU 4288 N ASN B 339 11197 8599 14534 917 -4174 -1436 N ATOM 4289 CA ASN B 339 -29.172 -18.405 23.269 1.00 94.97 C ANISOU 4289 CA ASN B 339 11759 9145 15180 943 -4238 -1474 C ATOM 4290 C ASN B 339 -27.948 -17.586 23.698 1.00105.14 C ANISOU 4290 C ASN B 339 12990 10390 16567 960 -4288 -1516 C ATOM 4291 O ASN B 339 -27.458 -17.753 24.815 1.00105.84 O ANISOU 4291 O ASN B 339 13098 10442 16675 995 -4366 -1554 O ATOM 4292 CB ASN B 339 -28.799 -19.399 22.167 1.00 93.28 C ANISOU 4292 CB ASN B 339 11519 8935 14987 931 -4223 -1464 C ATOM 4293 CG ASN B 339 -29.465 -20.746 22.354 1.00 84.42 C ANISOU 4293 CG ASN B 339 10453 7823 13798 935 -4232 -1448 C ATOM 4294 OD1 ASN B 339 -30.378 -20.894 23.170 1.00 50.22 O ANISOU 4294 OD1 ASN B 339 6177 3502 9404 940 -4237 -1437 O ATOM 4295 ND2 ASN B 339 -29.009 -21.741 21.600 1.00 77.04 N ANISOU 4295 ND2 ASN B 339 9503 6885 12885 933 -4237 -1448 N ATOM 4296 N PRO B 340 -27.451 -16.696 22.821 1.00101.19 N ANISOU 4296 N PRO B 340 12421 9890 16136 939 -4252 -1514 N ATOM 4297 CA PRO B 340 -26.218 -15.974 23.157 1.00 67.61 C ANISOU 4297 CA PRO B 340 8097 5585 12007 953 -4304 -1556 C ATOM 4298 C PRO B 340 -26.351 -15.231 24.470 1.00 60.62 C ANISOU 4298 C PRO B 340 7249 4679 11104 980 -4355 -1582 C ATOM 4299 O PRO B 340 -25.340 -14.978 25.116 1.00 69.66 O ANISOU 4299 O PRO B 340 8358 5767 12344 1005 -4435 -1628 O ATOM 4300 CB PRO B 340 -26.067 -14.968 22.010 1.00 63.53 C ANISOU 4300 CB PRO B 340 7512 5083 11544 920 -4240 -1538 C ATOM 4301 CG PRO B 340 -27.427 -14.838 21.431 1.00 96.35 C ANISOU 4301 CG PRO B 340 11729 9299 15581 899 -4167 -1491 C ATOM 4302 CD PRO B 340 -28.056 -16.194 21.578 1.00105.49 C ANISOU 4302 CD PRO B 340 12953 10475 16654 906 -4173 -1476 C ATOM 4303 N ILE B 341 -27.582 -14.904 24.855 1.00 65.12 N ANISOU 4303 N ILE B 341 7890 5289 11563 977 -4320 -1556 N ATOM 4304 CA ILE B 341 -27.845 -14.114 26.056 1.00 56.01 C ANISOU 4304 CA ILE B 341 6781 4121 10381 1004 -4365 -1578 C ATOM 4305 C ILE B 341 -27.996 -14.976 27.307 1.00 53.16 C ANISOU 4305 C ILE B 341 6498 3739 9960 1046 -4447 -1602 C ATOM 4306 O ILE B 341 -28.152 -14.459 28.409 1.00 53.64 O ANISOU 4306 O ILE B 341 6610 3782 9989 1079 -4505 -1628 O ATOM 4307 CB ILE B 341 -29.097 -13.225 25.898 1.00 51.69 C ANISOU 4307 CB ILE B 341 6262 3621 9755 980 -4292 -1539 C ATOM 4308 CG1 ILE B 341 -29.347 -12.899 24.421 1.00 74.75 C ANISOU 4308 CG1 ILE B 341 9133 6576 12691 937 -4203 -1500 C ATOM 4309 CG2 ILE B 341 -28.955 -11.954 26.730 1.00 52.17 C ANISOU 4309 CG2 ILE B 341 6327 3660 9835 1000 -4329 -1567 C ATOM 4310 CD1 ILE B 341 -30.565 -12.028 24.171 1.00 50.07 C ANISOU 4310 CD1 ILE B 341 6031 3492 9503 914 -4141 -1464 C ATOM 4311 N ILE B 342 -27.964 -16.291 27.136 1.00 53.12 N ANISOU 4311 N ILE B 342 6510 3737 9936 1048 -4457 -1596 N ATOM 4312 CA ILE B 342 -27.843 -17.182 28.282 1.00 95.50 C ANISOU 4312 CA ILE B 342 11945 9073 15266 1094 -4551 -1628 C ATOM 4313 C ILE B 342 -26.352 -17.373 28.569 1.00 83.58 C ANISOU 4313 C ILE B 342 10391 7496 13871 1126 -4651 -1683 C ATOM 4314 O ILE B 342 -25.954 -17.916 29.603 1.00 62.27 O ANISOU 4314 O ILE B 342 7744 4752 11164 1175 -4760 -1725 O ATOM 4315 CB ILE B 342 -28.527 -18.539 28.029 1.00 94.39 C ANISOU 4315 CB ILE B 342 11844 8962 15058 1084 -4522 -1597 C ATOM 4316 CG1 ILE B 342 -29.946 -18.331 27.498 1.00 90.58 C ANISOU 4316 CG1 ILE B 342 11380 8537 14500 1044 -4424 -1541 C ATOM 4317 CG2 ILE B 342 -28.561 -19.367 29.303 1.00104.42 C ANISOU 4317 CG2 ILE B 342 13197 10203 16275 1135 -4621 -1627 C ATOM 4318 CD1 ILE B 342 -30.792 -19.589 27.490 1.00102.54 C ANISOU 4318 CD1 ILE B 342 12939 10072 15951 1038 -4411 -1513 C ATOM 4319 N TYR B 343 -25.532 -16.900 27.640 1.00 85.35 N ANISOU 4319 N TYR B 343 10516 7706 14208 1099 -4621 -1685 N ATOM 4320 CA TYR B 343 -24.089 -16.985 27.777 1.00 85.00 C ANISOU 4320 CA TYR B 343 10400 7588 14308 1121 -4714 -1736 C ATOM 4321 C TYR B 343 -23.527 -15.728 28.416 1.00 80.08 C ANISOU 4321 C TYR B 343 9750 6916 13761 1142 -4778 -1777 C ATOM 4322 O TYR B 343 -22.317 -15.588 28.585 1.00101.96 O ANISOU 4322 O TYR B 343 12450 9613 16677 1160 -4866 -1824 O ATOM 4323 CB TYR B 343 -23.450 -17.222 26.418 1.00 98.25 C ANISOU 4323 CB TYR B 343 11973 9268 16088 1080 -4654 -1718 C ATOM 4324 CG TYR B 343 -23.820 -18.550 25.829 1.00 97.55 C ANISOU 4324 CG TYR B 343 11909 9214 15940 1068 -4616 -1688 C ATOM 4325 CD1 TYR B 343 -23.359 -19.729 26.402 1.00107.45 C ANISOU 4325 CD1 TYR B 343 13190 10432 17206 1101 -4702 -1716 C ATOM 4326 CD2 TYR B 343 -24.633 -18.632 24.703 1.00 83.37 C ANISOU 4326 CD2 TYR B 343 10115 7483 14078 1027 -4504 -1634 C ATOM 4327 CE1 TYR B 343 -23.696 -20.958 25.870 1.00131.31 C ANISOU 4327 CE1 TYR B 343 16233 13482 20176 1091 -4669 -1690 C ATOM 4328 CE2 TYR B 343 -24.977 -19.856 24.161 1.00105.77 C ANISOU 4328 CE2 TYR B 343 12978 10346 16863 1018 -4477 -1610 C ATOM 4329 CZ TYR B 343 -24.508 -21.021 24.748 1.00119.93 C ANISOU 4329 CZ TYR B 343 14792 12105 18671 1048 -4556 -1637 C ATOM 4330 OH TYR B 343 -24.844 -22.251 24.213 1.00 78.94 O ANISOU 4330 OH TYR B 343 9625 6937 13432 1041 -4532 -1614 O ATOM 4331 N CYS B 344 -24.416 -14.810 28.771 1.00 66.45 N ANISOU 4331 N CYS B 344 8076 5225 11946 1140 -4739 -1760 N ATOM 4332 CA CYS B 344 -24.014 -13.645 29.538 1.00108.27 C ANISOU 4332 CA CYS B 344 13369 10476 17294 1168 -4810 -1801 C ATOM 4333 C CYS B 344 -23.697 -14.072 30.963 1.00151.85 C ANISOU 4333 C CYS B 344 18973 15936 22786 1237 -4961 -1858 C ATOM 4334 O CYS B 344 -23.247 -13.265 31.776 1.00180.24 O ANISOU 4334 O CYS B 344 22581 19477 26426 1275 -5057 -1905 O ATOM 4335 CB CYS B 344 -25.109 -12.579 29.532 1.00101.58 C ANISOU 4335 CB CYS B 344 12559 9684 16354 1148 -4728 -1766 C ATOM 4336 SG CYS B 344 -25.140 -11.544 28.047 1.00103.83 S ANISOU 4336 SG CYS B 344 12736 10007 16709 1083 -4597 -1723 S ATOM 4337 N ARG B 345 -23.947 -15.343 31.262 1.00152.89 N ANISOU 4337 N ARG B 345 19170 16077 22845 1256 -4988 -1855 N ATOM 4338 CA ARG B 345 -23.751 -15.877 32.610 1.00151.08 C ANISOU 4338 CA ARG B 345 19042 15795 22566 1328 -5135 -1907 C ATOM 4339 C ARG B 345 -22.311 -16.295 32.962 1.00157.58 C ANISOU 4339 C ARG B 345 19820 16520 23532 1369 -5284 -1973 C ATOM 4340 O ARG B 345 -21.972 -16.412 34.142 1.00173.36 O ANISOU 4340 O ARG B 345 21901 18456 25511 1439 -5435 -2030 O ATOM 4341 CB ARG B 345 -24.733 -17.028 32.877 1.00123.11 C ANISOU 4341 CB ARG B 345 15599 12302 18877 1336 -5105 -1876 C ATOM 4342 CG ARG B 345 -26.140 -16.555 33.211 1.00 99.94 C ANISOU 4342 CG ARG B 345 12745 9430 15799 1328 -5032 -1837 C ATOM 4343 CD ARG B 345 -27.065 -17.715 33.547 1.00 90.60 C ANISOU 4343 CD ARG B 345 11650 8282 14493 1338 -5019 -1812 C ATOM 4344 NE ARG B 345 -28.075 -17.319 34.525 1.00110.46 N ANISOU 4344 NE ARG B 345 14274 10814 16882 1370 -5037 -1810 N ATOM 4345 CZ ARG B 345 -29.168 -16.618 34.236 1.00122.56 C ANISOU 4345 CZ ARG B 345 15801 12402 18363 1330 -4934 -1764 C ATOM 4346 NH1 ARG B 345 -30.026 -16.304 35.199 1.00114.03 N ANISOU 4346 NH1 ARG B 345 14820 11330 17175 1365 -4965 -1768 N ATOM 4347 NH2 ARG B 345 -29.403 -16.228 32.989 1.00121.36 N ANISOU 4347 NH2 ARG B 345 15550 12294 18266 1261 -4809 -1717 N ATOM 4348 N SER B 346 -21.474 -16.524 31.952 1.00164.13 N ANISOU 4348 N SER B 346 18444 23858 20060 -4193 245 -1758 N ATOM 4349 CA SER B 346 -20.079 -16.893 32.195 1.00146.29 C ANISOU 4349 CA SER B 346 16473 21491 17619 -4144 94 -1640 C ATOM 4350 C SER B 346 -19.138 -15.696 32.077 1.00159.56 C ANISOU 4350 C SER B 346 18214 23222 19188 -3948 -39 -1690 C ATOM 4351 O SER B 346 -19.114 -15.021 31.048 1.00167.03 O ANISOU 4351 O SER B 346 19019 24209 20237 -3832 -158 -1796 O ATOM 4352 CB SER B 346 -19.628 -18.008 31.245 1.00110.99 C ANISOU 4352 CB SER B 346 12017 16863 13293 -4181 -63 -1612 C ATOM 4353 OG SER B 346 -19.690 -19.276 31.875 1.00112.91 O ANISOU 4353 OG SER B 346 12395 16963 13541 -4345 10 -1469 O ATOM 4354 N PRO B 347 -18.363 -15.428 33.140 1.00164.45 N ANISOU 4354 N PRO B 347 19070 23833 19579 -3942 -40 -1599 N ATOM 4355 CA PRO B 347 -17.351 -14.367 33.116 1.00165.35 C ANISOU 4355 CA PRO B 347 19259 23978 19590 -3785 -181 -1637 C ATOM 4356 C PRO B 347 -16.197 -14.731 32.183 1.00162.39 C ANISOU 4356 C PRO B 347 18876 23478 19346 -3684 -412 -1616 C ATOM 4357 O PRO B 347 -15.565 -13.832 31.621 1.00147.75 O ANISOU 4357 O PRO B 347 16988 21651 17500 -3554 -507 -1705 O ATOM 4358 CB PRO B 347 -16.874 -14.302 34.569 1.00169.87 C ANISOU 4358 CB PRO B 347 20122 24549 19872 -3888 -156 -1514 C ATOM 4359 CG PRO B 347 -17.154 -15.657 35.116 1.00170.77 C ANISOU 4359 CG PRO B 347 20360 24562 19963 -4077 -118 -1341 C ATOM 4360 CD PRO B 347 -18.409 -16.119 34.440 1.00165.65 C ANISOU 4360 CD PRO B 347 19466 23941 19533 -4129 68 -1441 C ATOM 4361 N ASP B 348 -15.933 -16.029 32.028 1.00169.44 N ANISOU 4361 N ASP B 348 19800 24213 20366 -3756 -464 -1516 N ATOM 4362 CA ASP B 348 -14.988 -16.508 31.024 1.00157.64 C ANISOU 4362 CA ASP B 348 18258 22560 19079 -3683 -587 -1555 C ATOM 4363 C ASP B 348 -15.379 -15.865 29.713 1.00137.84 C ANISOU 4363 C ASP B 348 15616 20139 16617 -3645 -564 -1749 C ATOM 4364 O ASP B 348 -14.539 -15.377 28.954 1.00124.00 O ANISOU 4364 O ASP B 348 13860 18352 14904 -3563 -628 -1842 O ATOM 4365 CB ASP B 348 -15.088 -18.028 30.846 1.00158.65 C ANISOU 4365 CB ASP B 348 18394 22487 19397 -3790 -565 -1481 C ATOM 4366 CG ASP B 348 -14.842 -18.797 32.130 1.00154.93 C ANISOU 4366 CG ASP B 348 18089 21895 18883 -3868 -626 -1234 C ATOM 4367 OD1 ASP B 348 -14.202 -18.249 33.051 1.00145.72 O ANISOU 4367 OD1 ASP B 348 17049 20761 17557 -3832 -750 -1113 O ATOM 4368 OD2 ASP B 348 -15.289 -19.962 32.207 1.00153.38 O ANISOU 4368 OD2 ASP B 348 17922 21558 18797 -3993 -571 -1149 O ATOM 4369 N PHE B 349 -16.682 -15.887 29.463 1.00137.39 N ANISOU 4369 N PHE B 349 15453 20185 16564 -3732 -482 -1796 N ATOM 4370 CA PHE B 349 -17.254 -15.358 28.244 1.00130.26 C ANISOU 4370 CA PHE B 349 14433 19356 15704 -3742 -535 -1928 C ATOM 4371 C PHE B 349 -17.290 -13.831 28.236 1.00137.57 C ANISOU 4371 C PHE B 349 15315 20411 16546 -3609 -584 -1975 C ATOM 4372 O PHE B 349 -16.860 -13.212 27.269 1.00147.79 O ANISOU 4372 O PHE B 349 16635 21701 17816 -3571 -691 -2048 O ATOM 4373 CB PHE B 349 -18.659 -15.924 28.052 1.00111.63 C ANISOU 4373 CB PHE B 349 11925 17041 13447 -3889 -487 -1934 C ATOM 4374 CG PHE B 349 -19.270 -15.580 26.731 1.00120.67 C ANISOU 4374 CG PHE B 349 12967 18235 14647 -3951 -634 -2027 C ATOM 4375 CD1 PHE B 349 -18.541 -14.901 25.771 1.00122.63 C ANISOU 4375 CD1 PHE B 349 13318 18472 14803 -3906 -764 -2097 C ATOM 4376 CD2 PHE B 349 -20.574 -15.927 26.451 1.00125.56 C ANISOU 4376 CD2 PHE B 349 13398 18903 15407 -4088 -662 -2030 C ATOM 4377 CE1 PHE B 349 -19.102 -14.577 24.558 1.00118.04 C ANISOU 4377 CE1 PHE B 349 12712 17926 14210 -4014 -947 -2146 C ATOM 4378 CE2 PHE B 349 -21.143 -15.605 25.239 1.00123.80 C ANISOU 4378 CE2 PHE B 349 13097 18717 15224 -4178 -884 -2077 C ATOM 4379 CZ PHE B 349 -20.408 -14.932 24.290 1.00118.03 C ANISOU 4379 CZ PHE B 349 12529 17974 14343 -4150 -1041 -2123 C ATOM 4380 N ARG B 350 -17.793 -13.224 29.308 1.00126.06 N ANISOU 4380 N ARG B 350 13818 19043 15036 -3562 -476 -1945 N ATOM 4381 CA ARG B 350 -17.960 -11.775 29.335 1.00103.97 C ANISOU 4381 CA ARG B 350 10960 16328 12217 -3435 -487 -2009 C ATOM 4382 C ARG B 350 -16.626 -11.046 29.192 1.00111.96 C ANISOU 4382 C ARG B 350 12125 17307 13107 -3331 -588 -2028 C ATOM 4383 O ARG B 350 -16.570 -9.962 28.619 1.00117.04 O ANISOU 4383 O ARG B 350 12741 17971 13757 -3246 -666 -2085 O ATOM 4384 CB ARG B 350 -18.711 -11.320 30.595 1.00105.58 C ANISOU 4384 CB ARG B 350 11117 16598 12400 -3434 -267 -2022 C ATOM 4385 CG ARG B 350 -19.226 -9.883 30.516 1.00123.00 C ANISOU 4385 CG ARG B 350 13182 18843 14710 -3302 -235 -2119 C ATOM 4386 CD ARG B 350 -20.416 -9.636 31.445 1.00134.85 C ANISOU 4386 CD ARG B 350 14521 20376 16341 -3334 61 -2191 C ATOM 4387 NE ARG B 350 -21.029 -8.327 31.207 1.00158.83 N ANISOU 4387 NE ARG B 350 17343 23389 19616 -3184 86 -2291 N ATOM 4388 CZ ARG B 350 -22.171 -7.915 31.755 1.00162.78 C ANISOU 4388 CZ ARG B 350 17596 23872 20382 -3171 355 -2396 C ATOM 4389 NH1 ARG B 350 -22.841 -8.708 32.580 1.00157.34 N ANISOU 4389 NH1 ARG B 350 16870 23212 19700 -3333 653 -2424 N ATOM 4390 NH2 ARG B 350 -22.648 -6.708 31.476 1.00164.13 N ANISOU 4390 NH2 ARG B 350 17546 23969 20848 -3004 347 -2476 N ATOM 4391 N LYS B 351 -15.554 -11.646 29.705 1.00118.39 N ANISOU 4391 N LYS B 351 13084 18049 13850 -3346 -606 -1965 N ATOM 4392 CA LYS B 351 -14.221 -11.048 29.599 1.00129.38 C ANISOU 4392 CA LYS B 351 14572 19393 15192 -3265 -703 -1984 C ATOM 4393 C LYS B 351 -13.759 -10.975 28.152 1.00120.23 C ANISOU 4393 C LYS B 351 13394 18174 14114 -3266 -767 -2074 C ATOM 4394 O LYS B 351 -13.068 -10.037 27.756 1.00115.71 O ANISOU 4394 O LYS B 351 12864 17598 13502 -3209 -812 -2134 O ATOM 4395 CB LYS B 351 -13.198 -11.829 30.427 1.00140.16 C ANISOU 4395 CB LYS B 351 16038 20659 16558 -3287 -763 -1868 C ATOM 4396 CG LYS B 351 -13.272 -11.561 31.919 1.00145.86 C ANISOU 4396 CG LYS B 351 16898 21442 17082 -3328 -749 -1774 C ATOM 4397 CD LYS B 351 -13.035 -10.091 32.229 1.00140.32 C ANISOU 4397 CD LYS B 351 16252 20827 16237 -3262 -746 -1864 C ATOM 4398 CE LYS B 351 -13.222 -9.806 33.710 1.00126.38 C ANISOU 4398 CE LYS B 351 14683 19122 14214 -3363 -681 -1814 C ATOM 4399 NZ LYS B 351 -13.123 -8.353 34.018 1.00103.86 N ANISOU 4399 NZ LYS B 351 11898 16333 11230 -3317 -626 -1945 N ATOM 4400 N ALA B 352 -14.137 -11.980 27.372 1.00110.87 N ANISOU 4400 N ALA B 352 12178 16930 13019 -3370 -751 -2095 N ATOM 4401 CA ALA B 352 -13.845 -11.990 25.948 1.00100.19 C ANISOU 4401 CA ALA B 352 10874 15518 11675 -3448 -774 -2205 C ATOM 4402 C ALA B 352 -14.901 -11.191 25.184 1.00100.51 C ANISOU 4402 C ALA B 352 10886 15662 11642 -3488 -881 -2220 C ATOM 4403 O ALA B 352 -14.708 -10.862 24.018 1.00100.72 O ANISOU 4403 O ALA B 352 11019 15661 11588 -3582 -947 -2286 O ATOM 4404 CB ALA B 352 -13.775 -13.415 25.435 1.00101.15 C ANISOU 4404 CB ALA B 352 11015 15506 11913 -3579 -700 -2246 C ATOM 4405 N PHE B 353 -16.016 -10.891 25.850 1.00101.10 N ANISOU 4405 N PHE B 353 10819 15832 11763 -3436 -897 -2154 N ATOM 4406 CA PHE B 353 -17.099 -10.101 25.265 1.00105.09 C ANISOU 4406 CA PHE B 353 11213 16399 12317 -3438 -1040 -2137 C ATOM 4407 C PHE B 353 -16.786 -8.615 25.323 1.00139.49 C ANISOU 4407 C PHE B 353 15598 20765 16636 -3298 -1097 -2139 C ATOM 4408 O PHE B 353 -17.158 -7.855 24.429 1.00159.42 O ANISOU 4408 O PHE B 353 18126 23275 19170 -3314 -1281 -2112 O ATOM 4409 CB PHE B 353 -18.435 -10.367 25.974 1.00104.19 C ANISOU 4409 CB PHE B 353 10865 16346 12377 -3432 -982 -2094 C ATOM 4410 CG PHE B 353 -19.570 -9.492 25.486 1.00144.69 C ANISOU 4410 CG PHE B 353 15788 21501 17687 -3395 -1150 -2062 C ATOM 4411 CD1 PHE B 353 -20.202 -9.759 24.280 1.00167.05 C ANISOU 4411 CD1 PHE B 353 18580 24321 20569 -3544 -1404 -2022 C ATOM 4412 CD2 PHE B 353 -20.004 -8.403 26.232 1.00146.94 C ANISOU 4412 CD2 PHE B 353 15920 21793 18117 -3225 -1068 -2071 C ATOM 4413 CE1 PHE B 353 -21.240 -8.958 23.827 1.00170.35 C ANISOU 4413 CE1 PHE B 353 18778 24733 21215 -3508 -1641 -1947 C ATOM 4414 CE2 PHE B 353 -21.044 -7.598 25.782 1.00141.13 C ANISOU 4414 CE2 PHE B 353 14938 21027 17658 -3162 -1239 -2029 C ATOM 4415 CZ PHE B 353 -21.659 -7.876 24.579 1.00154.59 C ANISOU 4415 CZ PHE B 353 16573 22718 19448 -3295 -1559 -1945 C ATOM 4416 N LYS B 354 -16.095 -8.203 26.379 1.00141.16 N ANISOU 4416 N LYS B 354 15853 20983 16799 -3183 -965 -2156 N ATOM 4417 CA LYS B 354 -15.792 -6.794 26.568 1.00126.52 C ANISOU 4417 CA LYS B 354 14035 19120 14918 -3060 -988 -2178 C ATOM 4418 C LYS B 354 -14.716 -6.354 25.579 1.00121.06 C ANISOU 4418 C LYS B 354 13523 18367 14109 -3106 -1080 -2207 C ATOM 4419 O LYS B 354 -14.972 -5.530 24.700 1.00114.11 O ANISOU 4419 O LYS B 354 12685 17453 13220 -3119 -1225 -2183 O ATOM 4420 CB LYS B 354 -15.382 -6.501 28.018 1.00103.47 C ANISOU 4420 CB LYS B 354 11153 16225 11937 -2982 -826 -2205 C ATOM 4421 CG LYS B 354 -14.311 -7.421 28.588 1.00 99.38 C ANISOU 4421 CG LYS B 354 10752 15692 11315 -3040 -789 -2180 C ATOM 4422 CD LYS B 354 -13.291 -6.637 29.403 1.00 99.03 C ANISOU 4422 CD LYS B 354 10832 15639 11156 -2991 -784 -2203 C ATOM 4423 CE LYS B 354 -13.970 -5.705 30.396 1.00100.16 C ANISOU 4423 CE LYS B 354 10984 15827 11244 -2944 -662 -2254 C ATOM 4424 NZ LYS B 354 -12.994 -4.835 31.114 1.00100.14 N ANISOU 4424 NZ LYS B 354 11140 15810 11098 -2934 -677 -2298 N ATOM 4425 N ARG B 355 -13.523 -6.922 25.717 1.00104.34 N ANISOU 4425 N ARG B 355 11503 16212 11929 -3145 -997 -2249 N ATOM 4426 CA ARG B 355 -12.401 -6.584 24.851 1.00100.97 C ANISOU 4426 CA ARG B 355 11222 15711 11432 -3211 -999 -2313 C ATOM 4427 C ARG B 355 -12.718 -6.861 23.390 1.00121.54 C ANISOU 4427 C ARG B 355 13938 18282 13960 -3387 -1065 -2334 C ATOM 4428 O ARG B 355 -12.102 -6.291 22.488 1.00139.34 O ANISOU 4428 O ARG B 355 16363 20479 16100 -3488 -1069 -2381 O ATOM 4429 CB ARG B 355 -11.171 -7.383 25.256 1.00 97.68 C ANISOU 4429 CB ARG B 355 10802 15227 11086 -3222 -887 -2359 C ATOM 4430 CG ARG B 355 -11.337 -8.140 26.549 1.00103.32 C ANISOU 4430 CG ARG B 355 11421 15968 11868 -3156 -871 -2281 C ATOM 4431 CD ARG B 355 -10.152 -9.044 26.781 1.00127.56 C ANISOU 4431 CD ARG B 355 14460 18919 15087 -3170 -834 -2285 C ATOM 4432 NE ARG B 355 -9.880 -9.879 25.618 1.00140.55 N ANISOU 4432 NE ARG B 355 16115 20450 16838 -3279 -731 -2383 N ATOM 4433 CZ ARG B 355 -8.704 -10.455 25.384 1.00158.82 C ANISOU 4433 CZ ARG B 355 18376 22601 19367 -3296 -637 -2455 C ATOM 4434 NH1 ARG B 355 -7.697 -10.288 26.233 1.00168.74 N ANISOU 4434 NH1 ARG B 355 19536 23801 20777 -3202 -706 -2401 N ATOM 4435 NH2 ARG B 355 -8.523 -11.199 24.304 1.00165.95 N ANISOU 4435 NH2 ARG B 355 19313 23379 20360 -3423 -473 -2592 N ATOM 4436 N LEU B 356 -13.674 -7.752 23.163 1.00118.41 N ANISOU 4436 N LEU B 356 13475 17915 13600 -3465 -1112 -2303 N ATOM 4437 CA LEU B 356 -14.082 -8.093 21.812 1.00124.82 C ANISOU 4437 CA LEU B 356 14429 18701 14297 -3686 -1215 -2320 C ATOM 4438 C LEU B 356 -14.521 -6.853 21.037 1.00126.64 C ANISOU 4438 C LEU B 356 14767 18933 14418 -3725 -1448 -2233 C ATOM 4439 O LEU B 356 -13.868 -6.444 20.077 1.00125.27 O ANISOU 4439 O LEU B 356 14849 18697 14049 -3886 -1454 -2273 O ATOM 4440 CB LEU B 356 -15.222 -9.102 21.859 1.00135.18 C ANISOU 4440 CB LEU B 356 15610 20055 15699 -3756 -1279 -2279 C ATOM 4441 CG LEU B 356 -15.680 -9.626 20.504 1.00146.73 C ANISOU 4441 CG LEU B 356 17244 21491 17017 -4039 -1413 -2305 C ATOM 4442 CD1 LEU B 356 -14.504 -10.252 19.776 1.00134.05 C ANISOU 4442 CD1 LEU B 356 15888 19773 15272 -4221 -1186 -2480 C ATOM 4443 CD2 LEU B 356 -16.812 -10.621 20.683 1.00161.21 C ANISOU 4443 CD2 LEU B 356 18905 23364 18982 -4108 -1480 -2267 C TER 4444 LEU B 356 CONECT 586 1265 CONECT 1213 1259 CONECT 1259 1213 CONECT 1265 586 CONECT 2804 3483 CONECT 3431 3477 CONECT 3477 3431 CONECT 3483 2804 MASTER 588 0 0 30 0 0 0 6 4442 2 8 50 END