HEADER SIGNALING PROTEIN 06-JAN-15 4S0V TITLE CRYSTAL STRUCTURE OF THE HUMAN OX2 OREXIN RECEPTOR BOUND TO THE TITLE 2 INSOMNIA DRUG SUVOREXANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN OREXIN RECEPTOR TYPE 2 FUSION PROTEIN TO P. ABYSII COMPND 3 GLYCOGEN SYNTHASE; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: UNP O43614 RESIDUES 3-254, 294-388, AND UNP Q9V2J8 RESIDUES COMPND 6 218-413; COMPND 7 SYNONYM: OX-2-R, OX2-R, OX2R, HYPOCRETIN RECEPTOR TYPE 2, GLYCOGEN COMPND 8 SYNTHASE; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI GE5; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 272844; SOURCE 5 GENE: HCRTR2, PAB2292, PYRAB00770; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: FASTBAC BACULOVIRUS; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1 KEYWDS G PROTEIN-COUPLED RECEPTOR, OREXIN NEUROTRANSMITTERS, OREXIN KEYWDS 2 RECEPTOR, OREXIN-A, OREXIN-B, SUVOREXANT, N-LINKED GLYCOSYLATION, KEYWDS 3 SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.YIN,P.KOLB,J.C.MOBAREC,D.M.ROSENBAUM REVDAT 4 23-AUG-17 4S0V 1 SOURCE REMARK REVDAT 3 25-MAR-15 4S0V 1 JRNL REVDAT 2 18-MAR-15 4S0V 1 JRNL REVDAT 1 14-JAN-15 4S0V 0 SPRSDE 14-JAN-15 4S0V 4RNB JRNL AUTH J.YIN,J.C.MOBAREC,P.KOLB,D.M.ROSENBAUM JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN OX2 OREXIN RECEPTOR BOUND TO JRNL TITL 2 THE INSOMNIA DRUG SUVOREXANT. JRNL REF NATURE V. 519 247 2015 JRNL REFN ISSN 0028-0836 JRNL PMID 25533960 JRNL DOI 10.1038/NATURE14035 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1839) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.2 REMARK 3 NUMBER OF REFLECTIONS : 18772 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 REMARK 3 FREE R VALUE TEST SET COUNT : 955 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 43.7170 - 4.7589 1.00 3087 162 0.1895 0.2102 REMARK 3 2 4.7589 - 3.7779 1.00 3018 168 0.1711 0.2290 REMARK 3 3 3.7779 - 3.3006 1.00 3029 171 0.1953 0.2437 REMARK 3 4 3.3006 - 2.9989 1.00 3003 156 0.2202 0.2841 REMARK 3 5 2.9989 - 2.7840 0.92 2758 146 0.2311 0.2691 REMARK 3 6 2.7840 - 2.6199 0.65 1928 112 0.2329 0.2919 REMARK 3 7 2.6199 - 2.5000 0.32 994 40 0.2457 0.2862 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.920 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 3939 REMARK 3 ANGLE : 0.745 5331 REMARK 3 CHIRALITY : 0.025 611 REMARK 3 PLANARITY : 0.003 648 REMARK 3 DIHEDRAL : 12.360 1437 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 20 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND RESID 50:54) REMARK 3 ORIGIN FOR THE GROUP (A): 54.1433 26.5207 61.3854 REMARK 3 T TENSOR REMARK 3 T11: 0.7827 T22: 0.7261 REMARK 3 T33: 0.6222 T12: -0.0884 REMARK 3 T13: -0.0849 T23: -0.1524 REMARK 3 L TENSOR REMARK 3 L11: 1.5733 L22: 1.5019 REMARK 3 L33: 4.0685 L12: -1.3406 REMARK 3 L13: 2.4012 L23: -1.8665 REMARK 3 S TENSOR REMARK 3 S11: 0.0033 S12: -0.2999 S13: 0.4044 REMARK 3 S21: 0.1249 S22: -0.0290 S23: 0.3229 REMARK 3 S31: 0.0657 S32: 0.8761 S33: 0.0510 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND RESID 55:85) REMARK 3 ORIGIN FOR THE GROUP (A): 42.9114 18.3464 37.8261 REMARK 3 T TENSOR REMARK 3 T11: 0.2395 T22: 0.1739 REMARK 3 T33: 0.2615 T12: 0.0094 REMARK 3 T13: -0.0408 T23: 0.0355 REMARK 3 L TENSOR REMARK 3 L11: 0.7113 L22: 2.3959 REMARK 3 L33: 4.5987 L12: 0.0596 REMARK 3 L13: 0.0573 L23: 1.4319 REMARK 3 S TENSOR REMARK 3 S11: -0.1748 S12: 0.1335 S13: 0.3600 REMARK 3 S21: -0.1194 S22: -0.2977 S23: 0.4591 REMARK 3 S31: -0.2642 S32: 0.0790 S33: 0.0951 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN A AND RESID 86:124) REMARK 3 ORIGIN FOR THE GROUP (A): 44.8382 10.9817 46.5369 REMARK 3 T TENSOR REMARK 3 T11: 0.1485 T22: 0.2252 REMARK 3 T33: 0.2608 T12: -0.0087 REMARK 3 T13: 0.0135 T23: -0.0279 REMARK 3 L TENSOR REMARK 3 L11: 0.5902 L22: 1.0389 REMARK 3 L33: 4.1422 L12: -0.7036 REMARK 3 L13: -0.9380 L23: -0.8921 REMARK 3 S TENSOR REMARK 3 S11: 0.0527 S12: -0.1299 S13: 0.0552 REMARK 3 S21: -0.0086 S22: -0.0900 S23: 0.1935 REMARK 3 S31: -0.2621 S32: -0.0433 S33: 0.0266 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN A AND RESID 125:156) REMARK 3 ORIGIN FOR THE GROUP (A): 50.6997 2.3116 39.8424 REMARK 3 T TENSOR REMARK 3 T11: 0.1293 T22: 0.1977 REMARK 3 T33: 0.2436 T12: 0.0323 REMARK 3 T13: -0.0086 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 2.0526 L22: 1.4177 REMARK 3 L33: 4.5032 L12: 0.3682 REMARK 3 L13: -1.9058 L23: 0.2164 REMARK 3 S TENSOR REMARK 3 S11: 0.1570 S12: -0.0876 S13: -0.0872 REMARK 3 S21: -0.0870 S22: 0.0211 S23: -0.1786 REMARK 3 S31: -0.0756 S32: 0.3297 S33: -0.1102 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN A AND RESID 157:168) REMARK 3 ORIGIN FOR THE GROUP (A): 51.1587 -3.7330 21.8609 REMARK 3 T TENSOR REMARK 3 T11: 0.5549 T22: 0.6739 REMARK 3 T33: 0.6300 T12: 0.0837 REMARK 3 T13: -0.0520 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 4.4988 L22: 0.6239 REMARK 3 L33: 0.5012 L12: 1.6653 REMARK 3 L13: -0.7524 L23: -0.3477 REMARK 3 S TENSOR REMARK 3 S11: -0.6997 S12: -0.8659 S13: -0.9418 REMARK 3 S21: -0.8499 S22: 0.5674 S23: -0.0502 REMARK 3 S31: 0.2777 S32: 0.6708 S33: 0.0532 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN A AND RESID 169:206) REMARK 3 ORIGIN FOR THE GROUP (A): 46.6293 0.3098 52.9248 REMARK 3 T TENSOR REMARK 3 T11: 0.1625 T22: 0.2275 REMARK 3 T33: 0.3020 T12: -0.0321 REMARK 3 T13: 0.0375 T23: 0.0130 REMARK 3 L TENSOR REMARK 3 L11: 1.1427 L22: 2.2363 REMARK 3 L33: 3.7473 L12: -0.4149 REMARK 3 L13: -0.2518 L23: 0.8566 REMARK 3 S TENSOR REMARK 3 S11: -0.0950 S12: -0.1175 S13: -0.0982 REMARK 3 S21: 0.2434 S22: -0.1962 S23: 0.4236 REMARK 3 S31: 0.4354 S32: 0.1066 S33: 0.1956 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN A AND RESID 207:220) REMARK 3 ORIGIN FOR THE GROUP (A): 54.8882 0.8035 64.3297 REMARK 3 T TENSOR REMARK 3 T11: 0.3928 T22: 0.4823 REMARK 3 T33: 0.3340 T12: 0.0444 REMARK 3 T13: -0.0897 T23: 0.0539 REMARK 3 L TENSOR REMARK 3 L11: 8.5317 L22: 6.1611 REMARK 3 L33: 2.1299 L12: -5.5758 REMARK 3 L13: -2.8312 L23: 0.8551 REMARK 3 S TENSOR REMARK 3 S11: 0.0116 S12: -0.8554 S13: 0.2132 REMARK 3 S21: 0.3643 S22: 0.4551 S23: -0.8422 REMARK 3 S31: 0.0113 S32: 0.2012 S33: 0.0382 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN A AND RESID 221:252) REMARK 3 ORIGIN FOR THE GROUP (A): 63.1872 2.4894 36.7223 REMARK 3 T TENSOR REMARK 3 T11: 0.2736 T22: 0.3630 REMARK 3 T33: 0.2829 T12: 0.0962 REMARK 3 T13: 0.0335 T23: 0.0247 REMARK 3 L TENSOR REMARK 3 L11: 0.3971 L22: 2.3335 REMARK 3 L33: 6.0142 L12: 0.3001 REMARK 3 L13: 0.3854 L23: -0.4464 REMARK 3 S TENSOR REMARK 3 S11: 0.0260 S12: 0.1252 S13: -0.1344 REMARK 3 S21: -0.2654 S22: 0.0250 S23: -0.1805 REMARK 3 S31: 0.2978 S32: 0.4550 S33: 0.0365 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN A AND (RESID 253:254) OR (RESID 1001: 1012)) REMARK 3 ORIGIN FOR THE GROUP (A): 65.4489 15.1024 2.9480 REMARK 3 T TENSOR REMARK 3 T11: 0.5509 T22: 0.4787 REMARK 3 T33: 0.3124 T12: 0.0531 REMARK 3 T13: 0.0812 T23: -0.0777 REMARK 3 L TENSOR REMARK 3 L11: 2.4840 L22: 5.6862 REMARK 3 L33: 3.7463 L12: 0.2528 REMARK 3 L13: 0.0814 L23: -2.8700 REMARK 3 S TENSOR REMARK 3 S11: 0.0015 S12: -0.6536 S13: 0.3041 REMARK 3 S21: 0.5902 S22: 0.2686 S23: 1.0732 REMARK 3 S31: 0.0472 S32: -0.5921 S33: -0.0761 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN A AND RESID 1013:1031) REMARK 3 ORIGIN FOR THE GROUP (A): 68.5030 11.4582 -17.7986 REMARK 3 T TENSOR REMARK 3 T11: 0.3063 T22: 0.2569 REMARK 3 T33: 0.2317 T12: -0.0670 REMARK 3 T13: 0.0105 T23: -0.0032 REMARK 3 L TENSOR REMARK 3 L11: 5.6591 L22: 4.0350 REMARK 3 L33: 4.0781 L12: -2.0191 REMARK 3 L13: -1.8966 L23: 0.9885 REMARK 3 S TENSOR REMARK 3 S11: -0.2262 S12: 0.5537 S13: 0.3664 REMARK 3 S21: -0.4563 S22: -0.0209 S23: 0.0465 REMARK 3 S31: -0.0107 S32: 0.1254 S33: 0.2046 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN A AND RESID 1032:1053) REMARK 3 ORIGIN FOR THE GROUP (A): 72.9179 -4.8110 -4.3800 REMARK 3 T TENSOR REMARK 3 T11: 0.5993 T22: 0.3313 REMARK 3 T33: 0.2986 T12: 0.0890 REMARK 3 T13: -0.0111 T23: 0.0725 REMARK 3 L TENSOR REMARK 3 L11: 3.0099 L22: 3.0154 REMARK 3 L33: 1.7347 L12: -1.1395 REMARK 3 L13: -0.3394 L23: -1.9594 REMARK 3 S TENSOR REMARK 3 S11: -0.5026 S12: -0.6766 S13: -0.2029 REMARK 3 S21: 0.3263 S22: -0.0923 S23: -0.6194 REMARK 3 S31: 0.4844 S32: 0.4420 S33: 0.4157 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN A AND RESID 1054:1069) REMARK 3 ORIGIN FOR THE GROUP (A): 68.2344 -7.9264 -18.4300 REMARK 3 T TENSOR REMARK 3 T11: 0.7080 T22: 0.0902 REMARK 3 T33: 0.3789 T12: -0.0328 REMARK 3 T13: 0.1539 T23: -0.0975 REMARK 3 L TENSOR REMARK 3 L11: 2.7684 L22: 6.2111 REMARK 3 L33: 1.1261 L12: 0.1383 REMARK 3 L13: -0.4952 L23: -0.5193 REMARK 3 S TENSOR REMARK 3 S11: -0.4934 S12: 0.8921 S13: -0.3220 REMARK 3 S21: -0.6056 S22: -0.1996 S23: 0.3426 REMARK 3 S31: 1.2292 S32: 0.0455 S33: 0.0972 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: (CHAIN A AND RESID 1070:1087) REMARK 3 ORIGIN FOR THE GROUP (A): 81.0025 -5.0721 -7.6087 REMARK 3 T TENSOR REMARK 3 T11: 0.3520 T22: 0.5308 REMARK 3 T33: 0.6059 T12: 0.3117 REMARK 3 T13: 0.1249 T23: 0.1442 REMARK 3 L TENSOR REMARK 3 L11: 1.3292 L22: 2.8743 REMARK 3 L33: 2.3530 L12: -1.6263 REMARK 3 L13: 0.7880 L23: -2.0888 REMARK 3 S TENSOR REMARK 3 S11: -0.5179 S12: -0.3250 S13: -0.5503 REMARK 3 S21: 0.4228 S22: -0.3974 S23: -0.9302 REMARK 3 S31: 0.7418 S32: 1.2697 S33: -0.5681 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: (CHAIN A AND RESID 1088:1107) REMARK 3 ORIGIN FOR THE GROUP (A): 77.1556 5.6670 -9.3649 REMARK 3 T TENSOR REMARK 3 T11: 0.2512 T22: 0.3869 REMARK 3 T33: 0.3538 T12: -0.0238 REMARK 3 T13: 0.0232 T23: 0.0512 REMARK 3 L TENSOR REMARK 3 L11: 2.1047 L22: 5.1534 REMARK 3 L33: 3.8327 L12: -0.2233 REMARK 3 L13: -0.1527 L23: 3.1557 REMARK 3 S TENSOR REMARK 3 S11: 0.0171 S12: -0.2748 S13: 0.0713 REMARK 3 S21: -0.7739 S22: 0.2874 S23: -0.7054 REMARK 3 S31: -0.4081 S32: 0.9169 S33: 0.0094 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: (CHAIN A AND RESID 1108:1121) REMARK 3 ORIGIN FOR THE GROUP (A): 66.8164 0.9472 -4.3766 REMARK 3 T TENSOR REMARK 3 T11: 0.3626 T22: 0.2957 REMARK 3 T33: 0.1381 T12: 0.0394 REMARK 3 T13: 0.0153 T23: 0.0074 REMARK 3 L TENSOR REMARK 3 L11: 1.6844 L22: 2.0340 REMARK 3 L33: 0.3814 L12: 0.5376 REMARK 3 L13: -0.0726 L23: 0.8378 REMARK 3 S TENSOR REMARK 3 S11: -0.1927 S12: -0.3272 S13: 0.3334 REMARK 3 S21: 0.0190 S22: 0.0121 S23: 0.2284 REMARK 3 S31: 0.8389 S32: 0.5111 S33: 0.0766 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: (CHAIN A AND RESID 1122:1127) REMARK 3 ORIGIN FOR THE GROUP (A): 66.3898 1.4947 7.1544 REMARK 3 T TENSOR REMARK 3 T11: 0.6726 T22: 0.4077 REMARK 3 T33: 0.6237 T12: -0.0482 REMARK 3 T13: -0.0451 T23: 0.0155 REMARK 3 L TENSOR REMARK 3 L11: 2.5842 L22: 1.9208 REMARK 3 L33: 6.9009 L12: -0.3115 REMARK 3 L13: 0.8848 L23: 2.0824 REMARK 3 S TENSOR REMARK 3 S11: 0.5588 S12: -0.5880 S13: -0.1672 REMARK 3 S21: 0.9042 S22: -0.4147 S23: 0.1123 REMARK 3 S31: 0.1911 S32: -0.7602 S33: 0.2783 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: (CHAIN A AND RESID 1128:1182) REMARK 3 ORIGIN FOR THE GROUP (A): 59.3061 -2.0919 -5.3341 REMARK 3 T TENSOR REMARK 3 T11: 0.3308 T22: 0.2855 REMARK 3 T33: 0.3590 T12: -0.0460 REMARK 3 T13: 0.0748 T23: 0.0194 REMARK 3 L TENSOR REMARK 3 L11: 2.2123 L22: 2.7287 REMARK 3 L33: 3.2468 L12: -1.0506 REMARK 3 L13: 0.5994 L23: 1.6961 REMARK 3 S TENSOR REMARK 3 S11: -0.0401 S12: -0.3816 S13: -0.2659 REMARK 3 S21: 0.3202 S22: -0.2745 S23: 0.5688 REMARK 3 S31: 0.6299 S32: -0.4847 S33: 0.2450 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: (CHAIN A AND (RESID 1183:1196) OR (RESID 294:304)) REMARK 3 ORIGIN FOR THE GROUP (A): 55.7137 10.2582 6.9053 REMARK 3 T TENSOR REMARK 3 T11: 0.3435 T22: 0.3994 REMARK 3 T33: 0.2512 T12: 0.0054 REMARK 3 T13: 0.0414 T23: 0.0159 REMARK 3 L TENSOR REMARK 3 L11: 0.5991 L22: 0.7704 REMARK 3 L33: 3.4917 L12: 0.3748 REMARK 3 L13: 0.8839 L23: 1.7578 REMARK 3 S TENSOR REMARK 3 S11: -0.2773 S12: 0.1231 S13: 0.1139 REMARK 3 S21: -0.0193 S22: -0.1442 S23: -0.0290 REMARK 3 S31: -0.4923 S32: -0.2171 S33: 0.2366 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: (CHAIN A AND RESID 305:340) REMARK 3 ORIGIN FOR THE GROUP (A): 61.9975 10.7862 49.4395 REMARK 3 T TENSOR REMARK 3 T11: 0.1900 T22: 0.3673 REMARK 3 T33: 0.3083 T12: -0.0389 REMARK 3 T13: -0.0173 T23: 0.0036 REMARK 3 L TENSOR REMARK 3 L11: 0.8095 L22: 2.6163 REMARK 3 L33: 1.3894 L12: 0.2174 REMARK 3 L13: -0.7682 L23: -0.6913 REMARK 3 S TENSOR REMARK 3 S11: -0.1134 S12: -0.2731 S13: 0.0903 REMARK 3 S21: 0.3497 S22: -0.2711 S23: -0.3922 REMARK 3 S31: -0.3538 S32: 0.6439 S33: 0.3697 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: (CHAIN A AND RESID 341:381) REMARK 3 ORIGIN FOR THE GROUP (A): 50.4615 19.1727 38.4349 REMARK 3 T TENSOR REMARK 3 T11: 0.2847 T22: 0.2269 REMARK 3 T33: 0.2718 T12: -0.0040 REMARK 3 T13: 0.0018 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: 0.5420 L22: 1.5576 REMARK 3 L33: 3.2189 L12: 0.0760 REMARK 3 L13: 0.1832 L23: -0.3129 REMARK 3 S TENSOR REMARK 3 S11: 0.1773 S12: -0.1539 S13: 0.1453 REMARK 3 S21: -0.0755 S22: -0.1464 S23: 0.0835 REMARK 3 S31: -0.4567 S32: -0.1967 S33: -0.1169 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4S0V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-15. REMARK 100 THE DEPOSITION ID IS D_1000088038. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUL-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.9 REMARK 200 NUMBER OF CRYSTALS USED : 52 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22305 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 4DKL AND 2BFW REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 31% PEG 400, 0.1 M SODIUM CITRATE, 0.2 REMARK 280 M SODIUM FORMATE, 3%(W/V) HEXANEDIOL, PH 5.9, LIPIDIC CUBIC REMARK 280 PHASE (LCP), TEMPERATURE 293K 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 47.17900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.90950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 47.17900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.90950 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A -5 REMARK 465 TYR A -4 REMARK 465 LYS A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ASP A 0 REMARK 465 ALA A 1 REMARK 465 MET A 2 REMARK 465 GLY A 3 REMARK 465 THR A 4 REMARK 465 LYS A 5 REMARK 465 LEU A 6 REMARK 465 GLU A 7 REMARK 465 ASP A 8 REMARK 465 SER A 9 REMARK 465 PRO A 10 REMARK 465 PRO A 11 REMARK 465 CYS A 12 REMARK 465 ARG A 13 REMARK 465 ASN A 14 REMARK 465 TRP A 15 REMARK 465 SER A 16 REMARK 465 SER A 17 REMARK 465 ALA A 18 REMARK 465 SER A 19 REMARK 465 GLU A 20 REMARK 465 LEU A 21 REMARK 465 ASN A 22 REMARK 465 GLU A 23 REMARK 465 THR A 24 REMARK 465 GLN A 25 REMARK 465 GLU A 26 REMARK 465 PRO A 27 REMARK 465 PHE A 28 REMARK 465 LEU A 29 REMARK 465 ASN A 30 REMARK 465 PRO A 31 REMARK 465 THR A 32 REMARK 465 ASP A 33 REMARK 465 TYR A 34 REMARK 465 ASP A 35 REMARK 465 ASP A 36 REMARK 465 GLU A 37 REMARK 465 GLU A 38 REMARK 465 PHE A 39 REMARK 465 LEU A 40 REMARK 465 ARG A 41 REMARK 465 TYR A 42 REMARK 465 LEU A 43 REMARK 465 TRP A 44 REMARK 465 ARG A 45 REMARK 465 GLU A 46 REMARK 465 TYR A 47 REMARK 465 LEU A 48 REMARK 465 HIS A 49 REMARK 465 LEU A 160 REMARK 465 MET A 161 REMARK 465 PHE A 162 REMARK 465 LYS A 163 REMARK 465 PRO A 198 REMARK 465 GLY A 199 REMARK 465 LEU A 200 REMARK 465 ALA A 201 REMARK 465 ASN A 202 REMARK 465 THR A 336 REMARK 465 GLU A 337 REMARK 465 CYS A 382 REMARK 465 CYS A 383 REMARK 465 LEU A 384 REMARK 465 GLY A 385 REMARK 465 VAL A 386 REMARK 465 HIS A 387 REMARK 465 HIS A 388 REMARK 465 HIS A 389 REMARK 465 HIS A 390 REMARK 465 HIS A 391 REMARK 465 HIS A 392 REMARK 465 HIS A 393 REMARK 465 HIS A 394 REMARK 465 HIS A 395 REMARK 465 HIS A 396 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 203 CG CD CE NZ REMARK 470 HIS A 335 CG ND1 CD2 CE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LYS A 1061 O HOH A 4026 2.10 REMARK 500 OD1 ASN A 90 O HOH A 4027 2.11 REMARK 500 O ILE A 1116 O HOH A 4012 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR A 53 17.53 47.19 REMARK 500 TYR A 232 -75.01 -138.51 REMARK 500 GLN A1045 -72.63 -136.82 REMARK 500 PRO A1118 39.26 -88.83 REMARK 500 GLU A1122 86.56 -155.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 2002 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUV A 2001 DBREF 4S0V A 3 254 UNP O43614 OX2R_HUMAN 3 254 DBREF 4S0V A 1001 1196 UNP Q9V2J8 Q9V2J8_PYRAB 218 413 DBREF 4S0V A 294 388 UNP O43614 OX2R_HUMAN 294 388 SEQADV 4S0V ASP A -5 UNP O43614 EXPRESSION TAG SEQADV 4S0V TYR A -4 UNP O43614 EXPRESSION TAG SEQADV 4S0V LYS A -3 UNP O43614 EXPRESSION TAG SEQADV 4S0V ASP A -2 UNP O43614 EXPRESSION TAG SEQADV 4S0V ASP A -1 UNP O43614 EXPRESSION TAG SEQADV 4S0V ASP A 0 UNP O43614 EXPRESSION TAG SEQADV 4S0V ALA A 1 UNP O43614 EXPRESSION TAG SEQADV 4S0V MET A 2 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 389 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 390 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 391 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 392 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 393 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 394 UNP O43614 EXPRESSION TAG SEQADV 4S0V HIS A 395 UNP O43614 EXPRESSION TAG SEQRES 1 A 559 ASP TYR LYS ASP ASP ASP ALA MET GLY THR LYS LEU GLU SEQRES 2 A 559 ASP SER PRO PRO CYS ARG ASN TRP SER SER ALA SER GLU SEQRES 3 A 559 LEU ASN GLU THR GLN GLU PRO PHE LEU ASN PRO THR ASP SEQRES 4 A 559 TYR ASP ASP GLU GLU PHE LEU ARG TYR LEU TRP ARG GLU SEQRES 5 A 559 TYR LEU HIS PRO LYS GLU TYR GLU TRP VAL LEU ILE ALA SEQRES 6 A 559 GLY TYR ILE ILE VAL PHE VAL VAL ALA LEU ILE GLY ASN SEQRES 7 A 559 VAL LEU VAL CYS VAL ALA VAL TRP LYS ASN HIS HIS MET SEQRES 8 A 559 ARG THR VAL THR ASN TYR PHE ILE VAL ASN LEU SER LEU SEQRES 9 A 559 ALA ASP VAL LEU VAL THR ILE THR CYS LEU PRO ALA THR SEQRES 10 A 559 LEU VAL VAL ASP ILE THR GLU THR TRP PHE PHE GLY GLN SEQRES 11 A 559 SER LEU CYS LYS VAL ILE PRO TYR LEU GLN THR VAL SER SEQRES 12 A 559 VAL SER VAL SER VAL LEU THR LEU SER CYS ILE ALA LEU SEQRES 13 A 559 ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU MET PHE LYS SEQRES 14 A 559 SER THR ALA LYS ARG ALA ARG ASN SER ILE VAL ILE ILE SEQRES 15 A 559 TRP ILE VAL SER CYS ILE ILE MET ILE PRO GLN ALA ILE SEQRES 16 A 559 VAL MET GLU CYS SER THR VAL PHE PRO GLY LEU ALA ASN SEQRES 17 A 559 LYS THR THR LEU PHE THR VAL CYS ASP GLU ARG TRP GLY SEQRES 18 A 559 GLY GLU ILE TYR PRO LYS MET TYR HIS ILE CYS PHE PHE SEQRES 19 A 559 LEU VAL THR TYR MET ALA PRO LEU CYS LEU MET VAL LEU SEQRES 20 A 559 ALA TYR LEU GLN ILE PHE ARG LYS LEU TRP CYS ARG GLN SEQRES 21 A 559 GLY ILE ASP CYS SER PHE TRP ASN GLU SER TYR LEU THR SEQRES 22 A 559 GLY SER ARG ASP GLU ARG LYS LYS SER LEU LEU SER LYS SEQRES 23 A 559 PHE GLY MET ASP GLU GLY VAL THR PHE MET PHE ILE GLY SEQRES 24 A 559 ARG PHE ASP ARG GLY GLN LYS GLY VAL ASP VAL LEU LEU SEQRES 25 A 559 LYS ALA ILE GLU ILE LEU SER SER LYS LYS GLU PHE GLN SEQRES 26 A 559 GLU MET ARG PHE ILE ILE ILE GLY LYS GLY ASP PRO GLU SEQRES 27 A 559 LEU GLU GLY TRP ALA ARG SER LEU GLU GLU LYS HIS GLY SEQRES 28 A 559 ASN VAL LYS VAL ILE THR GLU MET LEU SER ARG GLU PHE SEQRES 29 A 559 VAL ARG GLU LEU TYR GLY SER VAL ASP PHE VAL ILE ILE SEQRES 30 A 559 PRO SER TYR PHE GLU PRO PHE GLY LEU VAL ALA LEU GLU SEQRES 31 A 559 ALA MET CYS LEU GLY ALA ILE PRO ILE ALA SER ALA VAL SEQRES 32 A 559 GLY GLY LEU ARG ASP ILE ILE THR ASN GLU THR GLY ILE SEQRES 33 A 559 LEU VAL LYS ALA GLY ASP PRO GLY GLU LEU ALA ASN ALA SEQRES 34 A 559 ILE LEU LYS ALA LEU GLU LEU SER ARG SER ASP LEU SER SEQRES 35 A 559 LYS PHE ARG GLU ASN CYS LYS LYS ARG ALA MET SER PHE SEQRES 36 A 559 SER LYS GLN ILE ARG ALA ARG ARG LYS THR ALA ARG MET SEQRES 37 A 559 LEU MET VAL VAL LEU LEU VAL PHE ALA ILE CYS TYR LEU SEQRES 38 A 559 PRO ILE SER ILE LEU ASN VAL LEU LYS ARG VAL PHE GLY SEQRES 39 A 559 MET PHE ALA HIS THR GLU ASP ARG GLU THR VAL TYR ALA SEQRES 40 A 559 TRP PHE THR PHE SER HIS TRP LEU VAL TYR ALA ASN SER SEQRES 41 A 559 ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER GLY LYS SEQRES 42 A 559 PHE ARG GLU GLU PHE LYS ALA ALA PHE SER CYS CYS CYS SEQRES 43 A 559 LEU GLY VAL HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HET SUV A2001 32 HET OLA A2002 8 HETNAM SUV [(7R)-4-(5-CHLORO-1,3-BENZOXAZOL-2-YL)-7-METHYL-1,4- HETNAM 2 SUV DIAZEPAN-1-YL][5-METHYL-2-(2H-1,2,3-TRIAZOL-2-YL) HETNAM 3 SUV PHENYL]METHANONE HETNAM OLA OLEIC ACID HETSYN SUV SUVOREXANT FORMUL 2 SUV C23 H23 CL N6 O2 FORMUL 3 OLA C18 H34 O2 FORMUL 4 HOH *28(H2 O) HELIX 1 1 TYR A 53 ASN A 82 1 30 HELIX 2 2 HIS A 83 ARG A 86 5 4 HELIX 3 3 THR A 87 CYS A 107 1 21 HELIX 4 4 CYS A 107 GLU A 118 1 12 HELIX 5 5 GLY A 123 CYS A 157 1 35 HELIX 6 6 THR A 165 MET A 184 1 20 HELIX 7 7 MET A 184 VAL A 190 1 7 HELIX 8 8 GLU A 217 TYR A 232 1 16 HELIX 9 9 TYR A 232 CYS A 252 1 21 HELIX 10 10 ASN A 1008 LEU A 1012 5 5 HELIX 11 11 SER A 1015 GLY A 1028 1 14 HELIX 12 12 GLY A 1047 SER A 1059 1 13 HELIX 13 13 SER A 1060 GLN A 1065 5 6 HELIX 14 14 ASP A 1076 HIS A 1090 1 15 HELIX 15 15 SER A 1101 GLY A 1110 1 10 HELIX 16 16 GLY A 1125 CYS A 1133 1 9 HELIX 17 17 GLY A 1145 ILE A 1150 1 6 HELIX 18 18 ASP A 1162 ARG A 1178 1 17 HELIX 19 19 LEU A 1181 VAL A 329 1 52 HELIX 20 20 ARG A 339 SER A 368 1 30 HELIX 21 21 SER A 368 PHE A 379 1 12 SHEET 1 A 2 MET A 191 VAL A 196 0 SHEET 2 A 2 PHE A 207 GLU A 212 -1 O PHE A 207 N VAL A 196 SHEET 1 B 6 VAL A1093 ILE A1096 0 SHEET 2 B 6 MET A1067 ILE A1072 1 N ILE A1071 O ILE A1096 SHEET 3 B 6 VAL A1033 PHE A1037 1 N PHE A1037 O ILE A1070 SHEET 4 B 6 PHE A1114 ILE A1117 1 O ILE A1116 N MET A1036 SHEET 5 B 6 ILE A1137 SER A1141 1 O ILE A1139 N VAL A1115 SHEET 6 B 6 ILE A1156 VAL A1158 1 O ILE A1156 N PRO A1138 SSBOND 1 CYS A 127 CYS A 210 1555 1555 2.04 CISPEP 1 PRO A 50 LYS A 51 0 -2.87 SITE 1 AC1 12 THR A 111 VAL A 114 TRP A 120 ILE A 130 SITE 2 AC1 12 PRO A 131 GLN A 134 THR A 135 GLN A 187 SITE 3 AC1 12 GLU A 212 ILE A 320 ASN A 324 HOH A4025 CRYST1 94.358 75.819 96.335 90.00 111.71 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010598 0.000000 0.004220 0.00000 SCALE2 0.000000 0.013189 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011173 0.00000 ATOM 1 N PRO A 50 52.480 26.848 67.575 1.00 92.84 N ANISOU 1 N PRO A 50 12541 12020 10715 -751 -425 -1950 N ATOM 2 CA PRO A 50 52.585 26.352 66.199 1.00 82.32 C ANISOU 2 CA PRO A 50 11209 10610 9458 -775 -508 -1819 C ATOM 3 C PRO A 50 51.693 27.121 65.224 1.00 77.84 C ANISOU 3 C PRO A 50 10646 9763 9167 -877 -543 -1799 C ATOM 4 O PRO A 50 50.566 27.446 65.591 1.00 81.16 O ANISOU 4 O PRO A 50 11076 10021 9742 -863 -473 -1812 O ATOM 5 CB PRO A 50 52.124 24.896 66.317 1.00 80.95 C ANISOU 5 CB PRO A 50 11091 10430 9236 -629 -481 -1680 C ATOM 6 CG PRO A 50 51.225 24.886 67.509 1.00 85.01 C ANISOU 6 CG PRO A 50 11592 10926 9780 -579 -358 -1694 C ATOM 7 CD PRO A 50 51.827 25.873 68.466 1.00 90.12 C ANISOU 7 CD PRO A 50 12213 11720 10310 -605 -315 -1881 C ATOM 8 N LYS A 51 52.171 27.421 64.015 1.00 76.69 N ANISOU 8 N LYS A 51 10483 9583 9071 -962 -644 -1757 N ATOM 9 CA LYS A 51 53.530 27.117 63.561 1.00 77.59 C ANISOU 9 CA LYS A 51 10551 9950 8978 -953 -716 -1716 C ATOM 10 C LYS A 51 53.908 28.081 62.443 1.00 79.95 C ANISOU 10 C LYS A 51 10791 10208 9376 -1108 -812 -1692 C ATOM 11 O LYS A 51 53.033 28.661 61.802 1.00 78.94 O ANISOU 11 O LYS A 51 10693 9816 9486 -1187 -832 -1689 O ATOM 12 CB LYS A 51 53.640 25.670 63.059 1.00 65.27 C ANISOU 12 CB LYS A 51 9057 8443 7298 -768 -739 -1587 C ATOM 13 CG LYS A 51 55.067 25.159 62.918 1.00 65.01 C ANISOU 13 CG LYS A 51 8979 8749 6972 -672 -782 -1552 C ATOM 14 CD LYS A 51 55.816 25.266 64.240 1.00 76.02 C ANISOU 14 CD LYS A 51 10315 10393 8177 -683 -727 -1645 C ATOM 15 CE LYS A 51 57.259 24.812 64.110 1.00 79.00 C ANISOU 15 CE LYS A 51 10616 11144 8257 -588 -768 -1593 C ATOM 16 NZ LYS A 51 57.998 24.937 65.397 1.00 78.70 N ANISOU 16 NZ LYS A 51 10519 11343 8042 -613 -730 -1680 N ATOM 17 N GLU A 52 55.203 28.257 62.196 1.00 79.87 N ANISOU 17 N GLU A 52 10683 10478 9185 -1156 -876 -1652 N ATOM 18 CA GLU A 52 55.612 28.955 60.986 1.00 84.20 C ANISOU 18 CA GLU A 52 11152 11039 9802 -1284 -971 -1564 C ATOM 19 C GLU A 52 55.407 27.998 59.819 1.00 85.67 C ANISOU 19 C GLU A 52 11387 11194 9971 -1105 -979 -1437 C ATOM 20 O GLU A 52 55.025 26.844 60.020 1.00 95.78 O ANISOU 20 O GLU A 52 12775 12434 11184 -908 -942 -1422 O ATOM 21 CB GLU A 52 57.065 29.440 61.058 1.00 87.15 C ANISOU 21 CB GLU A 52 11368 11766 9980 -1402 -1046 -1506 C ATOM 22 CG GLU A 52 58.114 28.364 60.834 1.00 91.30 C ANISOU 22 CG GLU A 52 11815 12668 10205 -1201 -1027 -1387 C ATOM 23 CD GLU A 52 58.537 27.688 62.118 1.00 96.05 C ANISOU 23 CD GLU A 52 12438 13452 10605 -1089 -966 -1465 C ATOM 24 OE1 GLU A 52 58.215 28.215 63.202 1.00 99.32 O ANISOU 24 OE1 GLU A 52 12896 13752 11090 -1198 -949 -1602 O ATOM 25 OE2 GLU A 52 59.189 26.628 62.044 1.00 97.13 O ANISOU 25 OE2 GLU A 52 12562 13848 10495 -869 -941 -1393 O ATOM 26 N TYR A 53 55.647 28.491 58.607 1.00 70.28 N ANISOU 26 N TYR A 53 9375 9249 8077 -1173 -1050 -1339 N ATOM 27 CA TYR A 53 55.387 27.763 57.360 1.00 71.99 C ANISOU 27 CA TYR A 53 9667 9397 8291 -998 -1085 -1228 C ATOM 28 C TYR A 53 54.002 27.097 57.298 1.00 72.12 C ANISOU 28 C TYR A 53 9866 9038 8497 -902 -1074 -1259 C ATOM 29 O TYR A 53 53.766 26.233 56.456 1.00 84.50 O ANISOU 29 O TYR A 53 11552 10525 10030 -718 -1133 -1177 O ATOM 30 CB TYR A 53 56.497 26.718 57.092 1.00 67.09 C ANISOU 30 CB TYR A 53 9022 9147 7324 -742 -1097 -1129 C ATOM 31 CG TYR A 53 56.533 25.474 57.972 1.00 70.05 C ANISOU 31 CG TYR A 53 9514 9584 7519 -526 -1061 -1175 C ATOM 32 CD1 TYR A 53 55.680 24.400 57.736 1.00 65.46 C ANISOU 32 CD1 TYR A 53 9146 8748 6979 -338 -1101 -1165 C ATOM 33 CD2 TYR A 53 57.459 25.353 59.004 1.00 78.16 C ANISOU 33 CD2 TYR A 53 10445 10924 8328 -517 -1015 -1210 C ATOM 34 CE1 TYR A 53 55.718 23.264 58.524 1.00 62.12 C ANISOU 34 CE1 TYR A 53 8841 8368 6394 -161 -1098 -1186 C ATOM 35 CE2 TYR A 53 57.505 24.215 59.797 1.00 77.67 C ANISOU 35 CE2 TYR A 53 10496 10919 8097 -320 -989 -1247 C ATOM 36 CZ TYR A 53 56.633 23.175 59.549 1.00 69.16 C ANISOU 36 CZ TYR A 53 9633 9575 7068 -145 -1033 -1232 C ATOM 37 OH TYR A 53 56.670 22.042 60.328 1.00 68.30 O ANISOU 37 OH TYR A 53 9650 9505 6796 31 -1036 -1249 O ATOM 38 N GLU A 54 53.080 27.522 58.158 1.00 54.70 N ANISOU 38 N GLU A 54 7687 6611 6484 -1018 -1016 -1359 N ATOM 39 CA GLU A 54 51.751 26.920 58.195 1.00 53.91 C ANISOU 39 CA GLU A 54 7713 6204 6567 -953 -1004 -1342 C ATOM 40 C GLU A 54 50.853 27.471 57.092 1.00 53.50 C ANISOU 40 C GLU A 54 7696 5849 6783 -1039 -1060 -1302 C ATOM 41 O GLU A 54 50.151 26.716 56.417 1.00 57.27 O ANISOU 41 O GLU A 54 8289 6126 7346 -941 -1126 -1213 O ATOM 42 CB GLU A 54 51.097 27.138 59.562 1.00 65.34 C ANISOU 42 CB GLU A 54 9146 7593 8087 -1006 -901 -1435 C ATOM 43 CG GLU A 54 49.724 26.488 59.696 1.00 72.33 C ANISOU 43 CG GLU A 54 10111 8222 9149 -952 -883 -1364 C ATOM 44 CD GLU A 54 49.189 26.524 61.115 1.00 79.02 C ANISOU 44 CD GLU A 54 10920 9107 9997 -947 -763 -1418 C ATOM 45 OE1 GLU A 54 50.004 26.565 62.061 1.00 82.54 O ANISOU 45 OE1 GLU A 54 11328 9791 10241 -921 -708 -1506 O ATOM 46 OE2 GLU A 54 47.950 26.514 61.283 1.00 78.44 O ANISOU 46 OE2 GLU A 54 10845 8844 10116 -957 -723 -1360 O ATOM 47 N TRP A 55 50.879 28.788 56.910 1.00 35.13 N ANISOU 47 N TRP A 55 5784 3470 4094 -1360 -623 -197 N ATOM 48 CA TRP A 55 50.049 29.435 55.900 1.00 37.11 C ANISOU 48 CA TRP A 55 6067 3515 4518 -1346 -645 -182 C ATOM 49 C TRP A 55 50.467 29.034 54.486 1.00 33.53 C ANISOU 49 C TRP A 55 5449 3219 4073 -1361 -678 -25 C ATOM 50 O TRP A 55 49.622 28.895 53.602 1.00 36.39 O ANISOU 50 O TRP A 55 5787 3476 4562 -1245 -649 -14 O ATOM 51 CB TRP A 55 50.094 30.962 56.059 1.00 44.46 C ANISOU 51 CB TRP A 55 7189 4226 5479 -1521 -770 -215 C ATOM 52 CG TRP A 55 51.471 31.562 55.986 1.00 48.47 C ANISOU 52 CG TRP A 55 7685 4885 5845 -1797 -896 -119 C ATOM 53 CD1 TRP A 55 52.299 31.846 57.035 1.00 43.38 C ANISOU 53 CD1 TRP A 55 7085 4337 5061 -1948 -947 -167 C ATOM 54 CD2 TRP A 55 52.173 31.962 54.802 1.00 52.52 C ANISOU 54 CD2 TRP A 55 8136 5485 6333 -1977 -981 26 C ATOM 55 NE1 TRP A 55 53.476 32.389 56.575 1.00 45.97 N ANISOU 55 NE1 TRP A 55 7353 4827 5288 -2221 -1057 -71 N ATOM 56 CE2 TRP A 55 53.423 32.472 55.208 1.00 50.01 C ANISOU 56 CE2 TRP A 55 7806 5333 5865 -2253 -1068 50 C ATOM 57 CE3 TRP A 55 51.866 31.935 53.437 1.00 51.18 C ANISOU 57 CE3 TRP A 55 7926 5276 6243 -1943 -989 131 C ATOM 58 CZ2 TRP A 55 54.367 32.951 54.297 1.00 47.76 C ANISOU 58 CZ2 TRP A 55 7443 5199 5507 -2478 -1125 172 C ATOM 59 CZ3 TRP A 55 52.805 32.409 52.535 1.00 51.94 C ANISOU 59 CZ3 TRP A 55 7989 5488 6257 -2183 -1062 264 C ATOM 60 CH2 TRP A 55 54.039 32.911 52.969 1.00 49.25 C ANISOU 60 CH2 TRP A 55 7609 5339 5766 -2431 -1108 280 C ATOM 61 N VAL A 56 51.766 28.837 54.275 1.00 34.31 N ANISOU 61 N VAL A 56 5424 3587 4027 -1497 -737 83 N ATOM 62 CA VAL A 56 52.263 28.429 52.963 1.00 37.97 C ANISOU 62 CA VAL A 56 5724 4229 4473 -1519 -752 226 C ATOM 63 C VAL A 56 51.913 26.961 52.711 1.00 38.06 C ANISOU 63 C VAL A 56 5611 4367 4484 -1279 -631 237 C ATOM 64 O VAL A 56 51.747 26.534 51.565 1.00 34.93 O ANISOU 64 O VAL A 56 5126 4017 4130 -1220 -610 320 O ATOM 65 CB VAL A 56 53.795 28.655 52.830 1.00 41.10 C ANISOU 65 CB VAL A 56 5990 4918 4708 -1745 -837 313 C ATOM 66 CG1 VAL A 56 54.571 27.743 53.766 1.00 46.37 C ANISOU 66 CG1 VAL A 56 6534 5861 5223 -1659 -816 275 C ATOM 67 CG2 VAL A 56 54.251 28.452 51.395 1.00 49.90 C ANISOU 67 CG2 VAL A 56 6962 6189 5808 -1803 -843 452 C ATOM 68 N LEU A 57 51.777 26.199 53.793 1.00 32.65 N ANISOU 68 N LEU A 57 4955 3715 3734 -1148 -549 149 N ATOM 69 CA LEU A 57 51.399 24.794 53.697 1.00 29.85 C ANISOU 69 CA LEU A 57 4550 3436 3355 -934 -421 147 C ATOM 70 C LEU A 57 49.924 24.665 53.339 1.00 33.86 C ANISOU 70 C LEU A 57 5117 3708 4040 -822 -323 70 C ATOM 71 O LEU A 57 49.552 23.893 52.458 1.00 26.40 O ANISOU 71 O LEU A 57 4095 2801 3136 -719 -263 113 O ATOM 72 CB LEU A 57 51.686 24.065 55.009 1.00 27.32 C ANISOU 72 CB LEU A 57 4305 3190 2885 -840 -364 75 C ATOM 73 CG LEU A 57 51.579 22.545 54.921 1.00 36.39 C ANISOU 73 CG LEU A 57 5444 4436 3947 -634 -245 94 C ATOM 74 CD1 LEU A 57 52.640 22.012 53.972 1.00 43.98 C ANISOU 74 CD1 LEU A 57 6222 5679 4811 -603 -309 227 C ATOM 75 CD2 LEU A 57 51.704 21.906 56.296 1.00 41.94 C ANISOU 75 CD2 LEU A 57 6303 5143 4490 -537 -186 14 C ATOM 76 N ILE A 58 49.088 25.427 54.035 1.00 40.41 N ANISOU 76 N ILE A 58 6076 4308 4971 -840 -309 -58 N ATOM 77 CA ILE A 58 47.660 25.454 53.758 1.00 35.21 C ANISOU 77 CA ILE A 58 5439 3448 4489 -734 -229 -167 C ATOM 78 C ILE A 58 47.404 25.951 52.340 1.00 37.78 C ANISOU 78 C ILE A 58 5697 3724 4932 -742 -328 -85 C ATOM 79 O ILE A 58 46.643 25.342 51.584 1.00 43.05 O ANISOU 79 O ILE A 58 6287 4382 5687 -629 -270 -101 O ATOM 80 CB ILE A 58 46.914 26.350 54.765 1.00 29.33 C ANISOU 80 CB ILE A 58 4836 2483 3824 -746 -214 -331 C ATOM 81 CG1 ILE A 58 47.038 25.774 56.177 1.00 24.78 C ANISOU 81 CG1 ILE A 58 4357 1940 3120 -729 -95 -421 C ATOM 82 CG2 ILE A 58 45.452 26.498 54.374 1.00 31.36 C ANISOU 82 CG2 ILE A 58 5071 2569 4277 -623 -154 -463 C ATOM 83 CD1 ILE A 58 46.699 26.766 57.272 1.00 29.40 C ANISOU 83 CD1 ILE A 58 5099 2346 3727 -779 -104 -560 C ATOM 84 N ALA A 59 48.059 27.053 51.984 1.00 31.00 N ANISOU 84 N ALA A 59 4889 2834 4057 -892 -478 -2 N ATOM 85 CA ALA A 59 47.910 27.645 50.658 1.00 38.12 C ANISOU 85 CA ALA A 59 5788 3662 5033 -920 -585 89 C ATOM 86 C ALA A 59 48.341 26.671 49.568 1.00 39.41 C ANISOU 86 C ALA A 59 5799 4033 5141 -886 -557 220 C ATOM 87 O ALA A 59 47.607 26.437 48.604 1.00 32.90 O ANISOU 87 O ALA A 59 4939 3152 4411 -782 -560 228 O ATOM 88 CB ALA A 59 48.707 28.933 50.562 1.00 26.33 C ANISOU 88 CB ALA A 59 4418 2102 3482 -1136 -729 166 C ATOM 89 N GLY A 60 49.532 26.102 49.734 1.00 40.34 N ANISOU 89 N GLY A 60 5826 4401 5100 -959 -538 309 N ATOM 90 CA GLY A 60 50.057 25.137 48.784 1.00 36.28 C ANISOU 90 CA GLY A 60 5169 4106 4510 -911 -503 424 C ATOM 91 C GLY A 60 49.160 23.925 48.631 1.00 28.97 C ANISOU 91 C GLY A 60 4203 3166 3636 -707 -378 363 C ATOM 92 O GLY A 60 48.942 23.441 47.520 1.00 36.11 O ANISOU 92 O GLY A 60 5044 4111 4564 -646 -370 425 O ATOM 93 N TYR A 61 48.628 23.439 49.749 1.00 26.30 N ANISOU 93 N TYR A 61 3921 2766 3305 -621 -273 236 N ATOM 94 CA TYR A 61 47.744 22.280 49.725 1.00 21.20 C ANISOU 94 CA TYR A 61 3266 2094 2694 -471 -130 159 C ATOM 95 C TYR A 61 46.437 22.597 49.009 1.00 34.11 C ANISOU 95 C TYR A 61 4883 3558 4520 -419 -136 78 C ATOM 96 O TYR A 61 45.906 21.758 48.286 1.00 44.90 O ANISOU 96 O TYR A 61 6190 4953 5917 -336 -73 71 O ATOM 97 CB TYR A 61 47.467 21.777 51.144 1.00 20.01 C ANISOU 97 CB TYR A 61 3217 1898 2488 -427 -2 34 C ATOM 98 CG TYR A 61 48.348 20.615 51.549 1.00 28.92 C ANISOU 98 CG TYR A 61 4368 3207 3412 -358 62 96 C ATOM 99 CD1 TYR A 61 49.593 20.829 52.125 1.00 31.39 C ANISOU 99 CD1 TYR A 61 4679 3675 3572 -401 -23 161 C ATOM 100 CD2 TYR A 61 47.941 19.305 51.343 1.00 38.06 C ANISOU 100 CD2 TYR A 61 5559 4380 4520 -243 198 79 C ATOM 101 CE1 TYR A 61 50.404 19.770 52.491 1.00 38.35 C ANISOU 101 CE1 TYR A 61 5585 4731 4258 -291 10 205 C ATOM 102 CE2 TYR A 61 48.745 18.238 51.706 1.00 42.06 C ANISOU 102 CE2 TYR A 61 6132 5026 4822 -144 244 134 C ATOM 103 CZ TYR A 61 49.976 18.478 52.278 1.00 42.21 C ANISOU 103 CZ TYR A 61 6141 5205 4692 -149 141 196 C ATOM 104 OH TYR A 61 50.783 17.425 52.642 1.00 38.99 O ANISOU 104 OH TYR A 61 5801 4944 4070 -6 161 240 O ATOM 105 N ILE A 62 45.925 23.809 49.202 1.00 33.92 N ANISOU 105 N ILE A 62 4916 3359 4615 -458 -224 7 N ATOM 106 CA ILE A 62 44.709 24.232 48.512 1.00 32.30 C ANISOU 106 CA ILE A 62 4686 3001 4585 -373 -268 -83 C ATOM 107 C ILE A 62 44.940 24.323 47.001 1.00 33.73 C ANISOU 107 C ILE A 62 4824 3226 4768 -373 -385 59 C ATOM 108 O ILE A 62 44.163 23.773 46.208 1.00 30.59 O ANISOU 108 O ILE A 62 4350 2829 4445 -272 -368 20 O ATOM 109 CB ILE A 62 44.202 25.587 49.041 1.00 24.76 C ANISOU 109 CB ILE A 62 3834 1838 3735 -382 -360 -187 C ATOM 110 CG1 ILE A 62 43.663 25.430 50.462 1.00 28.00 C ANISOU 110 CG1 ILE A 62 4279 2192 4166 -356 -219 -367 C ATOM 111 CG2 ILE A 62 43.111 26.138 48.143 1.00 23.15 C ANISOU 111 CG2 ILE A 62 3609 1495 3694 -262 -462 -259 C ATOM 112 CD1 ILE A 62 43.222 26.731 51.091 1.00 25.36 C ANISOU 112 CD1 ILE A 62 4060 1657 3917 -351 -297 -482 C ATOM 113 N ILE A 63 46.013 25.011 46.613 1.00 23.08 N ANISOU 113 N ILE A 63 3528 1918 3325 -504 -498 214 N ATOM 114 CA ILE A 63 46.387 25.135 45.205 1.00 26.65 C ANISOU 114 CA ILE A 63 3969 2419 3740 -538 -595 364 C ATOM 115 C ILE A 63 46.514 23.766 44.543 1.00 35.62 C ANISOU 115 C ILE A 63 4981 3740 4814 -461 -497 415 C ATOM 116 O ILE A 63 45.884 23.496 43.513 1.00 36.22 O ANISOU 116 O ILE A 63 5028 3788 4945 -378 -528 421 O ATOM 117 CB ILE A 63 47.719 25.888 45.033 1.00 25.84 C ANISOU 117 CB ILE A 63 3923 2392 3503 -743 -678 518 C ATOM 118 CG1 ILE A 63 47.619 27.299 45.611 1.00 33.32 C ANISOU 118 CG1 ILE A 63 5041 3124 4494 -843 -783 473 C ATOM 119 CG2 ILE A 63 48.111 25.947 43.563 1.00 22.70 C ANISOU 119 CG2 ILE A 63 3526 2055 3045 -795 -747 670 C ATOM 120 CD1 ILE A 63 46.581 28.159 44.935 1.00 44.25 C ANISOU 120 CD1 ILE A 63 6562 4248 6003 -751 -908 431 C ATOM 121 N VAL A 64 47.329 22.908 45.151 1.00 32.49 N ANISOU 121 N VAL A 64 4529 3526 4288 -475 -391 446 N ATOM 122 CA VAL A 64 47.546 21.560 44.646 1.00 22.07 C ANISOU 122 CA VAL A 64 3131 2371 2881 -386 -292 491 C ATOM 123 C VAL A 64 46.228 20.808 44.535 1.00 21.88 C ANISOU 123 C VAL A 64 3096 2247 2968 -259 -205 358 C ATOM 124 O VAL A 64 45.971 20.164 43.528 1.00 37.11 O ANISOU 124 O VAL A 64 4985 4221 4894 -200 -195 391 O ATOM 125 CB VAL A 64 48.523 20.769 45.543 1.00 23.60 C ANISOU 125 CB VAL A 64 3306 2746 2914 -373 -201 513 C ATOM 126 CG1 VAL A 64 48.427 19.277 45.266 1.00 19.95 C ANISOU 126 CG1 VAL A 64 2828 2379 2373 -234 -78 511 C ATOM 127 CG2 VAL A 64 49.944 21.260 45.330 1.00 26.92 C ANISOU 127 CG2 VAL A 64 3667 3357 3203 -495 -283 646 C ATOM 128 N PHE A 65 45.392 20.911 45.563 1.00 22.16 N ANISOU 128 N PHE A 65 3166 2157 3098 -234 -136 197 N ATOM 129 CA PHE A 65 44.101 20.226 45.587 1.00 29.55 C ANISOU 129 CA PHE A 65 4069 3020 4140 -153 -30 35 C ATOM 130 C PHE A 65 43.226 20.619 44.394 1.00 27.91 C ANISOU 130 C PHE A 65 3794 2743 4068 -99 -142 5 C ATOM 131 O PHE A 65 42.773 19.761 43.623 1.00 27.64 O ANISOU 131 O PHE A 65 3705 2758 4039 -49 -100 -13 O ATOM 132 CB PHE A 65 43.374 20.527 46.904 1.00 27.63 C ANISOU 132 CB PHE A 65 3862 2659 3976 -159 59 -146 C ATOM 133 CG PHE A 65 42.014 19.897 47.013 1.00 20.32 C ANISOU 133 CG PHE A 65 2877 1681 3162 -112 190 -343 C ATOM 134 CD1 PHE A 65 41.875 18.581 47.429 1.00 21.65 C ANISOU 134 CD1 PHE A 65 3088 1900 3237 -124 385 -394 C ATOM 135 CD2 PHE A 65 40.872 20.627 46.720 1.00 23.11 C ANISOU 135 CD2 PHE A 65 3140 1937 3705 -59 119 -491 C ATOM 136 CE1 PHE A 65 40.624 18.000 47.535 1.00 27.30 C ANISOU 136 CE1 PHE A 65 3747 2579 4047 -130 526 -590 C ATOM 137 CE2 PHE A 65 39.617 20.052 46.824 1.00 32.44 C ANISOU 137 CE2 PHE A 65 4221 3114 4992 -33 245 -701 C ATOM 138 CZ PHE A 65 39.493 18.737 47.232 1.00 27.63 C ANISOU 138 CZ PHE A 65 3646 2565 4289 -92 459 -752 C ATOM 139 N VAL A 66 43.007 21.921 44.240 1.00 28.23 N ANISOU 139 N VAL A 66 3864 2660 4204 -103 -297 -2 N ATOM 140 CA VAL A 66 42.148 22.429 43.176 1.00 33.72 C ANISOU 140 CA VAL A 66 4527 3267 5019 -17 -440 -40 C ATOM 141 C VAL A 66 42.697 22.099 41.787 1.00 35.44 C ANISOU 141 C VAL A 66 4748 3574 5142 -26 -517 132 C ATOM 142 O VAL A 66 41.975 21.576 40.927 1.00 40.06 O ANISOU 142 O VAL A 66 5266 4177 5775 56 -536 83 O ATOM 143 CB VAL A 66 41.955 23.951 43.294 1.00 31.50 C ANISOU 143 CB VAL A 66 4344 2807 4818 -4 -608 -59 C ATOM 144 CG1 VAL A 66 41.132 24.471 42.127 1.00 30.65 C ANISOU 144 CG1 VAL A 66 4238 2604 4805 120 -786 -86 C ATOM 145 CG2 VAL A 66 41.288 24.297 44.620 1.00 37.00 C ANISOU 145 CG2 VAL A 66 5033 3411 5615 27 -530 -255 C ATOM 146 N VAL A 67 43.979 22.390 41.578 1.00 22.45 N ANISOU 146 N VAL A 67 3172 2001 3356 -134 -553 320 N ATOM 147 CA VAL A 67 44.605 22.159 40.279 1.00 29.28 C ANISOU 147 CA VAL A 67 4049 2963 4112 -161 -610 486 C ATOM 148 C VAL A 67 44.634 20.674 39.907 1.00 35.57 C ANISOU 148 C VAL A 67 4763 3915 4839 -103 -478 488 C ATOM 149 O VAL A 67 44.384 20.314 38.756 1.00 36.64 O ANISOU 149 O VAL A 67 4889 4075 4956 -55 -523 527 O ATOM 150 CB VAL A 67 46.035 22.724 40.244 1.00 29.92 C ANISOU 150 CB VAL A 67 4190 3133 4046 -320 -641 663 C ATOM 151 CG1 VAL A 67 46.742 22.323 38.960 1.00 25.57 C ANISOU 151 CG1 VAL A 67 3630 2723 3361 -356 -654 821 C ATOM 152 CG2 VAL A 67 45.998 24.237 40.379 1.00 40.38 C ANISOU 152 CG2 VAL A 67 5654 4271 5419 -403 -787 677 C ATOM 153 N ALA A 68 44.923 19.814 40.879 1.00 26.35 N ANISOU 153 N ALA A 68 3566 2831 3614 -100 -319 442 N ATOM 154 CA ALA A 68 44.956 18.374 40.633 1.00 31.95 C ANISOU 154 CA ALA A 68 4251 3653 4236 -38 -186 436 C ATOM 155 C ALA A 68 43.566 17.855 40.292 1.00 35.94 C ANISOU 155 C ALA A 68 4717 4074 4865 28 -155 277 C ATOM 156 O ALA A 68 43.394 17.105 39.326 1.00 49.99 O ANISOU 156 O ALA A 68 6486 5905 6601 68 -146 300 O ATOM 157 CB ALA A 68 45.516 17.629 41.835 1.00 16.37 C ANISOU 157 CB ALA A 68 2311 1751 2159 -34 -37 414 C ATOM 158 N LEU A 69 42.578 18.263 41.084 1.00 30.33 N ANISOU 158 N LEU A 69 3975 3247 4302 34 -137 103 N ATOM 159 CA LEU A 69 41.207 17.816 40.866 1.00 36.85 C ANISOU 159 CA LEU A 69 4718 4027 5257 78 -99 -88 C ATOM 160 C LEU A 69 40.705 18.223 39.479 1.00 35.88 C ANISOU 160 C LEU A 69 4547 3887 5199 142 -280 -70 C ATOM 161 O LEU A 69 40.388 17.361 38.640 1.00 34.03 O ANISOU 161 O LEU A 69 4285 3713 4933 162 -259 -85 O ATOM 162 CB LEU A 69 40.283 18.375 41.947 1.00 32.19 C ANISOU 162 CB LEU A 69 4075 3339 4817 77 -57 -289 C ATOM 163 CG LEU A 69 38.957 17.631 42.101 1.00 35.39 C ANISOU 163 CG LEU A 69 4371 3749 5327 77 68 -526 C ATOM 164 CD1 LEU A 69 39.210 16.206 42.560 1.00 39.96 C ANISOU 164 CD1 LEU A 69 5035 4383 5766 -1 295 -530 C ATOM 165 CD2 LEU A 69 38.036 18.355 43.066 1.00 39.19 C ANISOU 165 CD2 LEU A 69 4770 4156 5964 91 95 -738 C ATOM 166 N ILE A 70 40.653 19.534 39.242 1.00 28.31 N ANISOU 166 N ILE A 70 3611 2834 4313 175 -465 -37 N ATOM 167 CA ILE A 70 40.174 20.065 37.967 1.00 28.76 C ANISOU 167 CA ILE A 70 3668 2844 4414 258 -666 -16 C ATOM 168 C ILE A 70 40.970 19.490 36.798 1.00 31.72 C ANISOU 168 C ILE A 70 4108 3316 4630 229 -685 171 C ATOM 169 O ILE A 70 40.398 19.025 35.812 1.00 33.27 O ANISOU 169 O ILE A 70 4270 3540 4832 289 -744 135 O ATOM 170 CB ILE A 70 40.258 21.608 37.914 1.00 36.67 C ANISOU 170 CB ILE A 70 4774 3696 5463 290 -863 36 C ATOM 171 CG1 ILE A 70 39.512 22.239 39.094 1.00 34.90 C ANISOU 171 CG1 ILE A 70 4500 3372 5389 337 -845 -155 C ATOM 172 CG2 ILE A 70 39.707 22.128 36.592 1.00 30.72 C ANISOU 172 CG2 ILE A 70 4066 2873 4733 402 -1086 54 C ATOM 173 CD1 ILE A 70 38.046 21.880 39.156 1.00 45.96 C ANISOU 173 CD1 ILE A 70 5720 4789 6953 454 -831 -418 C ATOM 174 N GLY A 71 42.292 19.512 36.931 1.00 21.29 N ANISOU 174 N GLY A 71 2866 2064 3160 138 -632 355 N ATOM 175 CA GLY A 71 43.186 19.058 35.882 1.00 22.57 C ANISOU 175 CA GLY A 71 3080 2339 3154 107 -634 533 C ATOM 176 C GLY A 71 42.984 17.612 35.475 1.00 31.00 C ANISOU 176 C GLY A 71 4106 3512 4161 151 -511 491 C ATOM 177 O GLY A 71 42.805 17.315 34.291 1.00 27.23 O ANISOU 177 O GLY A 71 3652 3059 3636 187 -579 531 O ATOM 178 N ASN A 72 43.008 16.705 36.446 1.00 17.72 N ANISOU 178 N ASN A 72 2396 1874 2463 143 -331 411 N ATOM 179 CA ASN A 72 42.875 15.287 36.126 1.00 28.96 C ANISOU 179 CA ASN A 72 3835 3368 3801 173 -200 374 C ATOM 180 C ASN A 72 41.466 14.943 35.642 1.00 34.23 C ANISOU 180 C ASN A 72 4438 3974 4592 200 -231 195 C ATOM 181 O ASN A 72 41.293 14.100 34.744 1.00 38.05 O ANISOU 181 O ASN A 72 4948 4503 5006 219 -217 194 O ATOM 182 CB ASN A 72 43.259 14.430 37.331 1.00 27.72 C ANISOU 182 CB ASN A 72 3722 3242 3570 161 -5 336 C ATOM 183 CG ASN A 72 44.750 14.474 37.622 1.00 34.13 C ANISOU 183 CG ASN A 72 4575 4173 4219 165 20 507 C ATOM 184 OD1 ASN A 72 45.545 13.832 36.935 1.00 47.56 O ANISOU 184 OD1 ASN A 72 6312 5994 5765 211 47 618 O ATOM 185 ND2 ASN A 72 45.136 15.235 38.640 1.00 28.05 N ANISOU 185 ND2 ASN A 72 3789 3386 3480 121 9 513 N ATOM 186 N VAL A 73 40.463 15.608 36.215 1.00 33.20 N ANISOU 186 N VAL A 73 4216 3757 4643 203 -279 29 N ATOM 187 CA VAL A 73 39.096 15.443 35.725 1.00 22.27 C ANISOU 187 CA VAL A 73 2720 2351 3390 235 -339 -167 C ATOM 188 C VAL A 73 39.009 15.863 34.254 1.00 28.29 C ANISOU 188 C VAL A 73 3499 3117 4132 309 -554 -85 C ATOM 189 O VAL A 73 38.378 15.181 33.439 1.00 31.41 O ANISOU 189 O VAL A 73 3858 3554 4523 325 -579 -166 O ATOM 190 CB VAL A 73 38.087 16.247 36.570 1.00 19.99 C ANISOU 190 CB VAL A 73 2304 1992 3300 257 -373 -368 C ATOM 191 CG1 VAL A 73 36.760 16.387 35.843 1.00 21.52 C ANISOU 191 CG1 VAL A 73 2345 2197 3635 332 -511 -562 C ATOM 192 CG2 VAL A 73 37.884 15.577 37.919 1.00 27.86 C ANISOU 192 CG2 VAL A 73 3285 2991 4309 165 -130 -499 C ATOM 193 N LEU A 74 39.668 16.966 33.911 1.00 30.40 N ANISOU 193 N LEU A 74 3848 3335 4367 337 -706 78 N ATOM 194 CA LEU A 74 39.692 17.441 32.528 1.00 34.74 C ANISOU 194 CA LEU A 74 4474 3865 4861 398 -909 182 C ATOM 195 C LEU A 74 40.471 16.504 31.614 1.00 33.49 C ANISOU 195 C LEU A 74 4401 3811 4512 363 -839 327 C ATOM 196 O LEU A 74 40.175 16.412 30.425 1.00 28.92 O ANISOU 196 O LEU A 74 3864 3238 3884 412 -963 348 O ATOM 197 CB LEU A 74 40.288 18.846 32.439 1.00 21.39 C ANISOU 197 CB LEU A 74 2904 2072 3150 398 -1061 330 C ATOM 198 CG LEU A 74 39.395 20.000 32.889 1.00 30.68 C ANISOU 198 CG LEU A 74 4053 3105 4498 491 -1218 197 C ATOM 199 CD1 LEU A 74 39.940 21.315 32.358 1.00 39.02 C ANISOU 199 CD1 LEU A 74 5313 4029 5485 493 -1405 366 C ATOM 200 CD2 LEU A 74 37.958 19.786 32.441 1.00 25.27 C ANISOU 200 CD2 LEU A 74 3232 2423 3948 628 -1333 -26 C ATOM 201 N VAL A 75 41.477 15.828 32.162 1.00 22.69 N ANISOU 201 N VAL A 75 3067 2529 3026 298 -650 421 N ATOM 202 CA VAL A 75 42.221 14.835 31.393 1.00 24.33 C ANISOU 202 CA VAL A 75 3349 2847 3046 294 -562 534 C ATOM 203 C VAL A 75 41.282 13.706 30.989 1.00 26.38 C ANISOU 203 C VAL A 75 3584 3114 3323 319 -512 380 C ATOM 204 O VAL A 75 41.163 13.354 29.800 1.00 36.01 O ANISOU 204 O VAL A 75 4858 4362 4461 350 -585 412 O ATOM 205 CB VAL A 75 43.408 14.263 32.191 1.00 26.79 C ANISOU 205 CB VAL A 75 3688 3260 3232 263 -375 629 C ATOM 206 CG1 VAL A 75 43.985 13.046 31.489 1.00 20.90 C ANISOU 206 CG1 VAL A 75 3016 2623 2301 302 -269 694 C ATOM 207 CG2 VAL A 75 44.478 15.328 32.390 1.00 40.67 C ANISOU 207 CG2 VAL A 75 5459 5054 4940 207 -428 788 C ATOM 208 N CYS A 76 40.599 13.159 31.990 1.00 28.36 N ANISOU 208 N CYS A 76 3766 3336 3672 287 -384 205 N ATOM 209 CA CYS A 76 39.637 12.087 31.756 1.00 28.30 C ANISOU 209 CA CYS A 76 3734 3332 3686 261 -312 28 C ATOM 210 C CYS A 76 38.542 12.498 30.769 1.00 38.08 C ANISOU 210 C CYS A 76 4878 4559 5031 302 -516 -88 C ATOM 211 O CYS A 76 38.206 11.740 29.858 1.00 43.95 O ANISOU 211 O CYS A 76 5655 5338 5706 299 -535 -130 O ATOM 212 CB CYS A 76 39.017 11.642 33.079 1.00 29.28 C ANISOU 212 CB CYS A 76 3801 3419 3906 184 -136 -154 C ATOM 213 SG CYS A 76 40.233 11.021 34.259 1.00 44.76 S ANISOU 213 SG CYS A 76 5912 5384 5713 164 89 -35 S ATOM 214 N VAL A 77 37.996 13.698 30.950 1.00 34.02 N ANISOU 214 N VAL A 77 4261 3992 4673 357 -682 -147 N ATOM 215 CA VAL A 77 36.965 14.213 30.049 1.00 39.70 C ANISOU 215 CA VAL A 77 4892 4702 5489 444 -916 -263 C ATOM 216 C VAL A 77 37.487 14.329 28.616 1.00 40.94 C ANISOU 216 C VAL A 77 5199 4866 5490 501 -1071 -85 C ATOM 217 O VAL A 77 36.818 13.921 27.660 1.00 35.04 O ANISOU 217 O VAL A 77 4434 4155 4727 535 -1180 -172 O ATOM 218 CB VAL A 77 36.446 15.591 30.520 1.00 40.43 C ANISOU 218 CB VAL A 77 4895 4716 5750 537 -1082 -334 C ATOM 219 CG1 VAL A 77 35.604 16.252 29.438 1.00 38.26 C ANISOU 219 CG1 VAL A 77 4586 4421 5530 683 -1374 -407 C ATOM 220 CG2 VAL A 77 35.649 15.442 31.805 1.00 41.73 C ANISOU 220 CG2 VAL A 77 4880 4894 6082 490 -940 -567 C ATOM 221 N ALA A 78 38.691 14.877 28.481 1.00 35.38 N ANISOU 221 N ALA A 78 4643 4139 4662 494 -1073 156 N ATOM 222 CA ALA A 78 39.327 15.055 27.182 1.00 34.29 C ANISOU 222 CA ALA A 78 4669 4010 4351 520 -1187 342 C ATOM 223 C ALA A 78 39.465 13.731 26.445 1.00 41.05 C ANISOU 223 C ALA A 78 5577 4956 5063 495 -1082 343 C ATOM 224 O ALA A 78 39.135 13.635 25.262 1.00 42.49 O ANISOU 224 O ALA A 78 5829 5144 5172 542 -1223 348 O ATOM 225 CB ALA A 78 40.692 15.712 27.345 1.00 29.89 C ANISOU 225 CB ALA A 78 4231 3450 3673 462 -1137 577 C ATOM 226 N VAL A 79 39.951 12.709 27.143 1.00 33.15 N ANISOU 226 N VAL A 79 4572 4014 4008 431 -842 337 N ATOM 227 CA VAL A 79 40.121 11.408 26.502 1.00 33.31 C ANISOU 227 CA VAL A 79 4683 4097 3876 418 -731 334 C ATOM 228 C VAL A 79 38.774 10.746 26.191 1.00 36.93 C ANISOU 228 C VAL A 79 5065 4545 4423 399 -777 100 C ATOM 229 O VAL A 79 38.594 10.151 25.127 1.00 32.28 O ANISOU 229 O VAL A 79 4557 3982 3725 411 -829 91 O ATOM 230 CB VAL A 79 40.970 10.464 27.373 1.00 30.07 C ANISOU 230 CB VAL A 79 4328 3731 3368 385 -473 378 C ATOM 231 CG1 VAL A 79 40.915 9.035 26.843 1.00 24.88 C ANISOU 231 CG1 VAL A 79 3788 3097 2567 381 -354 328 C ATOM 232 CG2 VAL A 79 42.407 10.956 27.434 1.00 30.69 C ANISOU 232 CG2 VAL A 79 4462 3878 3319 406 -434 602 C ATOM 233 N TRP A 80 37.823 10.870 27.110 1.00 29.05 N ANISOU 233 N TRP A 80 3903 3520 3616 360 -756 -100 N ATOM 234 CA TRP A 80 36.555 10.156 26.988 1.00 24.32 C ANISOU 234 CA TRP A 80 3192 2944 3104 298 -755 -356 C ATOM 235 C TRP A 80 35.611 10.742 25.937 1.00 31.52 C ANISOU 235 C TRP A 80 4007 3880 4089 381 -1039 -460 C ATOM 236 O TRP A 80 34.870 10.003 25.288 1.00 37.97 O ANISOU 236 O TRP A 80 4791 4747 4888 338 -1075 -612 O ATOM 237 CB TRP A 80 35.849 10.111 28.345 1.00 33.66 C ANISOU 237 CB TRP A 80 4214 4115 4461 211 -618 -555 C ATOM 238 CG TRP A 80 36.468 9.137 29.306 1.00 41.61 C ANISOU 238 CG TRP A 80 5348 5092 5370 110 -327 -521 C ATOM 239 CD1 TRP A 80 37.273 8.079 28.994 1.00 38.11 C ANISOU 239 CD1 TRP A 80 5121 4642 4718 93 -187 -403 C ATOM 240 CD2 TRP A 80 36.339 9.134 30.735 1.00 36.99 C ANISOU 240 CD2 TRP A 80 4711 4471 4873 34 -152 -609 C ATOM 241 NE1 TRP A 80 37.649 7.415 30.137 1.00 36.34 N ANISOU 241 NE1 TRP A 80 4996 4371 4442 27 51 -410 N ATOM 242 CE2 TRP A 80 37.091 8.044 31.220 1.00 37.72 C ANISOU 242 CE2 TRP A 80 5015 4526 4792 -22 79 -530 C ATOM 243 CE3 TRP A 80 35.660 9.946 31.649 1.00 38.74 C ANISOU 243 CE3 TRP A 80 4745 4685 5290 21 -170 -751 C ATOM 244 CZ2 TRP A 80 37.182 7.744 32.579 1.00 29.14 C ANISOU 244 CZ2 TRP A 80 3975 3385 3712 -98 285 -580 C ATOM 245 CZ3 TRP A 80 35.753 9.648 32.999 1.00 41.63 C ANISOU 245 CZ3 TRP A 80 5142 5008 5669 -71 52 -804 C ATOM 246 CH2 TRP A 80 36.508 8.555 33.450 1.00 36.47 C ANISOU 246 CH2 TRP A 80 4718 4308 4830 -134 274 -715 C ATOM 247 N LYS A 81 35.639 12.060 25.762 1.00 30.11 N ANISOU 247 N LYS A 81 3804 3659 3978 504 -1251 -382 N ATOM 248 CA LYS A 81 34.663 12.715 24.892 1.00 32.04 C ANISOU 248 CA LYS A 81 3963 3912 4297 626 -1549 -500 C ATOM 249 C LYS A 81 35.160 12.926 23.465 1.00 40.82 C ANISOU 249 C LYS A 81 5287 5001 5220 707 -1729 -314 C ATOM 250 O LYS A 81 34.364 13.173 22.560 1.00 55.34 O ANISOU 250 O LYS A 81 7100 6857 7070 808 -1975 -414 O ATOM 251 CB LYS A 81 34.236 14.054 25.497 1.00 42.30 C ANISOU 251 CB LYS A 81 5149 5151 5772 744 -1704 -554 C ATOM 252 CG LYS A 81 33.577 13.905 26.859 1.00 63.50 C ANISOU 252 CG LYS A 81 7605 7873 8651 673 -1541 -774 C ATOM 253 CD LYS A 81 32.543 12.783 26.833 1.00 74.99 C ANISOU 253 CD LYS A 81 8878 9451 10165 562 -1451 -1049 C ATOM 254 CE LYS A 81 32.294 12.206 28.219 1.00 67.33 C ANISOU 254 CE LYS A 81 7783 8505 9293 399 -1162 -1201 C ATOM 255 NZ LYS A 81 31.486 10.956 28.152 1.00 55.35 N ANISOU 255 NZ LYS A 81 6162 7089 7779 225 -1022 -1435 N ATOM 256 N ASN A 82 36.469 12.828 23.261 1.00 38.66 N ANISOU 256 N ASN A 82 5221 4703 4765 666 -1607 -57 N ATOM 257 CA ASN A 82 37.035 12.967 21.924 1.00 36.48 C ANISOU 257 CA ASN A 82 5163 4415 4282 714 -1731 125 C ATOM 258 C ASN A 82 37.709 11.674 21.484 1.00 41.43 C ANISOU 258 C ASN A 82 5909 5113 4719 631 -1530 194 C ATOM 259 O ASN A 82 38.651 11.207 22.126 1.00 35.29 O ANISOU 259 O ASN A 82 5169 4362 3876 566 -1293 298 O ATOM 260 CB ASN A 82 38.024 14.130 21.880 1.00 33.34 C ANISOU 260 CB ASN A 82 4922 3939 3807 736 -1782 369 C ATOM 261 CG ASN A 82 37.455 15.394 22.487 1.00 40.25 C ANISOU 261 CG ASN A 82 5715 4716 4863 815 -1940 304 C ATOM 262 OD1 ASN A 82 37.702 15.698 23.655 1.00 50.69 O ANISOU 262 OD1 ASN A 82 6948 6017 6297 773 -1826 299 O ATOM 263 ND2 ASN A 82 36.680 16.133 21.702 1.00 33.24 N ANISOU 263 ND2 ASN A 82 4850 3774 4006 904 -2117 230 N ATOM 264 N HIS A 83 37.223 11.096 20.390 1.00 31.77 N ANISOU 264 N HIS A 83 4753 3920 3399 652 -1635 127 N ATOM 265 CA HIS A 83 37.652 9.763 19.982 1.00 36.18 C ANISOU 265 CA HIS A 83 5428 4532 3786 583 -1451 141 C ATOM 266 C HIS A 83 39.081 9.730 19.450 1.00 40.34 C ANISOU 266 C HIS A 83 6166 5080 4080 594 -1341 405 C ATOM 267 O HIS A 83 39.763 8.712 19.564 1.00 41.36 O ANISOU 267 O HIS A 83 6377 5255 4082 560 -1121 446 O ATOM 268 CB HIS A 83 36.703 9.196 18.928 1.00 29.57 C ANISOU 268 CB HIS A 83 4609 3722 2903 593 -1610 -17 C ATOM 269 CG HIS A 83 36.816 7.714 18.755 1.00 50.59 C ANISOU 269 CG HIS A 83 7367 6417 5438 499 -1411 -83 C ATOM 270 ND1 HIS A 83 36.274 6.821 19.654 1.00 59.62 N ANISOU 270 ND1 HIS A 83 8404 7565 6684 380 -1233 -275 N ATOM 271 CD2 HIS A 83 37.415 6.968 17.797 1.00 50.42 C ANISOU 271 CD2 HIS A 83 7568 6410 5180 505 -1355 15 C ATOM 272 CE1 HIS A 83 36.530 5.589 19.254 1.00 60.58 C ANISOU 272 CE1 HIS A 83 8701 7684 6634 318 -1084 -289 C ATOM 273 NE2 HIS A 83 37.220 5.649 18.130 1.00 53.58 N ANISOU 273 NE2 HIS A 83 8005 6808 5544 404 -1157 -119 N ATOM 274 N HIS A 84 39.537 10.835 18.869 1.00 41.70 N ANISOU 274 N HIS A 84 6434 5222 4187 641 -1485 574 N ATOM 275 CA HIS A 84 40.898 10.893 18.344 1.00 37.96 C ANISOU 275 CA HIS A 84 6017 4821 3587 574 -1261 763 C ATOM 276 C HIS A 84 41.916 10.852 19.485 1.00 39.87 C ANISOU 276 C HIS A 84 6177 5120 3852 526 -1043 851 C ATOM 277 O HIS A 84 43.112 10.649 19.262 1.00 49.33 O ANISOU 277 O HIS A 84 7351 6428 4962 472 -852 966 O ATOM 278 CB HIS A 84 41.096 12.146 17.481 1.00 34.76 C ANISOU 278 CB HIS A 84 5640 4383 3182 560 -1346 859 C ATOM 279 CG HIS A 84 41.033 13.428 18.249 1.00 42.98 C ANISOU 279 CG HIS A 84 6617 5347 4364 557 -1413 882 C ATOM 280 ND1 HIS A 84 42.150 14.014 18.808 1.00 48.28 N ANISOU 280 ND1 HIS A 84 7251 6063 5030 483 -1251 1012 N ATOM 281 CD2 HIS A 84 39.992 14.239 18.554 1.00 33.62 C ANISOU 281 CD2 HIS A 84 5395 4049 3329 627 -1627 776 C ATOM 282 CE1 HIS A 84 41.797 15.130 19.424 1.00 51.91 C ANISOU 282 CE1 HIS A 84 7690 6417 5615 492 -1360 994 C ATOM 283 NE2 HIS A 84 40.494 15.287 19.284 1.00 48.69 N ANISOU 283 NE2 HIS A 84 7280 5912 5309 586 -1582 853 N ATOM 284 N MET A 85 41.428 11.031 20.709 1.00 28.18 N ANISOU 284 N MET A 85 4631 3578 2497 550 -1093 778 N ATOM 285 CA MET A 85 42.261 10.943 21.899 1.00 28.40 C ANISOU 285 CA MET A 85 4595 3649 2545 518 -902 839 C ATOM 286 C MET A 85 42.450 9.500 22.349 1.00 32.70 C ANISOU 286 C MET A 85 5152 4246 3026 524 -682 763 C ATOM 287 O MET A 85 43.238 9.227 23.251 1.00 43.30 O ANISOU 287 O MET A 85 6465 5639 4347 523 -508 812 O ATOM 288 CB MET A 85 41.649 11.758 23.041 1.00 31.56 C ANISOU 288 CB MET A 85 4843 3969 3179 502 -965 747 C ATOM 289 CG MET A 85 41.502 13.235 22.745 1.00 39.72 C ANISOU 289 CG MET A 85 5902 4919 4271 515 -1178 821 C ATOM 290 SD MET A 85 43.101 14.043 22.615 1.00 41.68 S ANISOU 290 SD MET A 85 6146 5262 4426 415 -989 1017 S ATOM 291 CE MET A 85 43.802 13.635 24.213 1.00 37.11 C ANISOU 291 CE MET A 85 5475 4744 3882 385 -814 1035 C ATOM 292 N ARG A 86 41.728 8.575 21.725 1.00 30.87 N ANISOU 292 N ARG A 86 4470 3628 3630 1499 -1090 -322 N ATOM 293 CA ARG A 86 41.720 7.195 22.199 1.00 35.31 C ANISOU 293 CA ARG A 86 5094 4143 4179 1284 -1131 -364 C ATOM 294 C ARG A 86 42.901 6.390 21.685 1.00 36.28 C ANISOU 294 C ARG A 86 5474 4081 4232 1340 -1081 -302 C ATOM 295 O ARG A 86 42.820 5.718 20.658 1.00 44.86 O ANISOU 295 O ARG A 86 6738 5110 5198 1380 -1163 -331 O ATOM 296 CB ARG A 86 40.407 6.511 21.821 1.00 36.21 C ANISOU 296 CB ARG A 86 5152 4385 4220 1143 -1299 -475 C ATOM 297 CG ARG A 86 39.214 7.141 22.512 1.00 57.54 C ANISOU 297 CG ARG A 86 7571 7307 6983 1073 -1337 -517 C ATOM 298 CD ARG A 86 37.963 6.294 22.406 1.00 74.32 C ANISOU 298 CD ARG A 86 9601 9591 9047 860 -1495 -615 C ATOM 299 NE ARG A 86 36.843 6.940 23.084 1.00 84.29 N ANISOU 299 NE ARG A 86 10568 11097 10361 823 -1518 -630 N ATOM 300 CZ ARG A 86 36.635 6.885 24.396 1.00 79.99 C ANISOU 300 CZ ARG A 86 9883 10590 9920 682 -1449 -620 C ATOM 301 NH1 ARG A 86 37.471 6.209 25.174 1.00 74.01 N ANISOU 301 NH1 ARG A 86 9247 9648 9225 561 -1358 -602 N ATOM 302 NH2 ARG A 86 35.592 7.506 24.930 1.00 78.27 N ANISOU 302 NH2 ARG A 86 9403 10605 9729 685 -1464 -620 N ATOM 303 N THR A 87 44.002 6.473 22.421 1.00 39.30 N ANISOU 303 N THR A 87 5874 4382 4674 1351 -942 -211 N ATOM 304 CA THR A 87 45.170 5.642 22.180 1.00 25.99 C ANISOU 304 CA THR A 87 4404 2554 2917 1408 -868 -127 C ATOM 305 C THR A 87 45.476 4.870 23.458 1.00 30.08 C ANISOU 305 C THR A 87 4898 3054 3479 1240 -798 -114 C ATOM 306 O THR A 87 44.970 5.214 24.528 1.00 23.78 O ANISOU 306 O THR A 87 3905 2346 2784 1104 -790 -153 O ATOM 307 CB THR A 87 46.394 6.479 21.758 1.00 30.01 C ANISOU 307 CB THR A 87 4855 3113 3433 1446 -679 -18 C ATOM 308 OG1 THR A 87 46.806 7.318 22.845 1.00 37.59 O ANISOU 308 OG1 THR A 87 5645 4127 4511 1386 -584 31 O ATOM 309 CG2 THR A 87 46.057 7.346 20.555 1.00 22.68 C ANISOU 309 CG2 THR A 87 3908 2240 2471 1529 -691 -38 C ATOM 310 N VAL A 88 46.293 3.827 23.345 1.00 30.99 N ANISOU 310 N VAL A 88 5224 3053 3500 1271 -740 -52 N ATOM 311 CA VAL A 88 46.679 3.026 24.502 1.00 30.19 C ANISOU 311 CA VAL A 88 5131 2929 3412 1152 -655 -23 C ATOM 312 C VAL A 88 47.355 3.904 25.553 1.00 31.55 C ANISOU 312 C VAL A 88 5096 3195 3698 1154 -549 54 C ATOM 313 O VAL A 88 47.020 3.852 26.750 1.00 43.62 O ANISOU 313 O VAL A 88 6483 4782 5307 1001 -528 18 O ATOM 314 CB VAL A 88 47.617 1.876 24.092 1.00 24.86 C ANISOU 314 CB VAL A 88 4740 2121 2586 1253 -576 63 C ATOM 315 CG1 VAL A 88 48.130 1.142 25.314 1.00 28.59 C ANISOU 315 CG1 VAL A 88 5223 2580 3058 1183 -465 118 C ATOM 316 CG2 VAL A 88 46.895 0.917 23.166 1.00 24.27 C ANISOU 316 CG2 VAL A 88 4919 1922 2382 1215 -685 -29 C ATOM 317 N THR A 89 48.294 4.723 25.085 1.00 26.82 N ANISOU 317 N THR A 89 4437 2651 3101 1253 -460 144 N ATOM 318 CA THR A 89 48.988 5.689 25.929 1.00 40.89 C ANISOU 318 CA THR A 89 6033 4526 4976 1223 -368 211 C ATOM 319 C THR A 89 48.007 6.544 26.723 1.00 34.20 C ANISOU 319 C THR A 89 5038 3709 4246 1166 -437 127 C ATOM 320 O THR A 89 48.152 6.709 27.932 1.00 34.72 O ANISOU 320 O THR A 89 4977 3836 4378 1053 -385 130 O ATOM 321 CB THR A 89 49.894 6.615 25.092 1.00 38.57 C ANISOU 321 CB THR A 89 5673 4300 4680 1246 -283 278 C ATOM 322 OG1 THR A 89 50.881 5.832 24.410 1.00 51.70 O ANISOU 322 OG1 THR A 89 7427 5975 6242 1278 -209 342 O ATOM 323 CG2 THR A 89 50.587 7.635 25.983 1.00 34.95 C ANISOU 323 CG2 THR A 89 5071 3906 4304 1208 -213 340 C ATOM 324 N ASN A 90 46.996 7.068 26.037 1.00 27.40 N ANISOU 324 N ASN A 90 4154 2857 3399 1193 -530 42 N ATOM 325 CA ASN A 90 46.023 7.953 26.667 1.00 28.23 C ANISOU 325 CA ASN A 90 4082 3048 3597 1114 -561 -36 C ATOM 326 C ASN A 90 45.071 7.240 27.623 1.00 30.85 C ANISOU 326 C ASN A 90 4318 3435 3967 932 -609 -122 C ATOM 327 O ASN A 90 44.622 7.833 28.600 1.00 36.52 O ANISOU 327 O ASN A 90 4885 4227 4767 855 -586 -151 O ATOM 328 CB ASN A 90 45.222 8.692 25.599 1.00 26.49 C ANISOU 328 CB ASN A 90 3862 2850 3354 1235 -638 -83 C ATOM 329 CG ASN A 90 45.968 9.886 25.037 1.00 27.89 C ANISOU 329 CG ASN A 90 4055 3013 3530 1334 -536 -6 C ATOM 330 OD1 ASN A 90 47.117 10.140 25.400 1.00 36.02 O ANISOU 330 OD1 ASN A 90 5080 4027 4579 1286 -422 79 O ATOM 331 ND2 ASN A 90 45.320 10.625 24.144 1.00 24.04 N ANISOU 331 ND2 ASN A 90 3559 2563 3011 1408 -557 -36 N ATOM 332 N TYR A 91 44.753 5.979 27.340 1.00 29.32 N ANISOU 332 N TYR A 91 4233 3198 3708 862 -668 -160 N ATOM 333 CA TYR A 91 43.967 5.175 28.271 1.00 20.64 C ANISOU 333 CA TYR A 91 3066 2137 2640 668 -694 -228 C ATOM 334 C TYR A 91 44.744 5.013 29.575 1.00 27.48 C ANISOU 334 C TYR A 91 3889 2999 3554 610 -576 -169 C ATOM 335 O TYR A 91 44.208 5.210 30.680 1.00 41.11 O ANISOU 335 O TYR A 91 5461 4800 5360 497 -560 -205 O ATOM 336 CB TYR A 91 43.635 3.804 27.678 1.00 23.60 C ANISOU 336 CB TYR A 91 3624 2430 2913 588 -761 -274 C ATOM 337 CG TYR A 91 42.454 3.786 26.729 1.00 39.28 C ANISOU 337 CG TYR A 91 5594 4475 4853 549 -911 -369 C ATOM 338 CD1 TYR A 91 41.182 4.137 27.165 1.00 42.25 C ANISOU 338 CD1 TYR A 91 5751 5011 5291 428 -986 -444 C ATOM 339 CD2 TYR A 91 42.606 3.387 25.405 1.00 36.23 C ANISOU 339 CD2 TYR A 91 5411 4006 4348 640 -977 -377 C ATOM 340 CE1 TYR A 91 40.097 4.112 26.304 1.00 50.65 C ANISOU 340 CE1 TYR A 91 6769 6179 6297 390 -1129 -521 C ATOM 341 CE2 TYR A 91 41.526 3.358 24.536 1.00 38.28 C ANISOU 341 CE2 TYR A 91 5648 4347 4550 596 -1126 -468 C ATOM 342 CZ TYR A 91 40.274 3.722 24.991 1.00 47.02 C ANISOU 342 CZ TYR A 91 6508 5641 5717 466 -1205 -538 C ATOM 343 OH TYR A 91 39.195 3.696 24.136 1.00 39.33 O ANISOU 343 OH TYR A 91 5479 4796 4669 420 -1360 -619 O ATOM 344 N PHE A 92 46.018 4.660 29.431 1.00 19.25 N ANISOU 344 N PHE A 92 2976 1887 2451 704 -491 -71 N ATOM 345 CA PHE A 92 46.912 4.552 30.576 1.00 22.17 C ANISOU 345 CA PHE A 92 3297 2287 2842 678 -379 3 C ATOM 346 C PHE A 92 46.969 5.867 31.352 1.00 24.01 C ANISOU 346 C PHE A 92 3338 2611 3173 652 -348 4 C ATOM 347 O PHE A 92 46.878 5.885 32.584 1.00 19.25 O ANISOU 347 O PHE A 92 2627 2064 2623 551 -307 -10 O ATOM 348 CB PHE A 92 48.310 4.147 30.117 1.00 24.60 C ANISOU 348 CB PHE A 92 3747 2551 3047 823 -295 132 C ATOM 349 CG PHE A 92 48.474 2.670 29.901 1.00 37.23 C ANISOU 349 CG PHE A 92 5564 4051 4529 842 -269 154 C ATOM 350 CD1 PHE A 92 47.960 1.765 30.813 1.00 42.30 C ANISOU 350 CD1 PHE A 92 6225 4673 5174 704 -251 104 C ATOM 351 CD2 PHE A 92 49.137 2.185 28.786 1.00 37.82 C ANISOU 351 CD2 PHE A 92 5850 4040 4478 1005 -251 228 C ATOM 352 CE1 PHE A 92 48.104 0.404 30.620 1.00 40.49 C ANISOU 352 CE1 PHE A 92 6243 4323 4820 719 -209 123 C ATOM 353 CE2 PHE A 92 49.286 0.824 28.588 1.00 28.76 C ANISOU 353 CE2 PHE A 92 4954 2775 3198 1036 -213 249 C ATOM 354 CZ PHE A 92 48.768 -0.066 29.504 1.00 31.38 C ANISOU 354 CZ PHE A 92 5323 3071 3529 887 -189 194 C ATOM 355 N ILE A 93 47.108 6.964 30.615 1.00 25.06 N ANISOU 355 N ILE A 93 3455 2746 3320 749 -362 18 N ATOM 356 CA ILE A 93 47.142 8.301 31.197 1.00 25.58 C ANISOU 356 CA ILE A 93 3398 2863 3457 730 -326 14 C ATOM 357 C ILE A 93 45.869 8.585 31.996 1.00 24.17 C ANISOU 357 C ILE A 93 3094 2739 3349 635 -365 -82 C ATOM 358 O ILE A 93 45.921 9.170 33.082 1.00 33.23 O ANISOU 358 O ILE A 93 4152 3928 4547 567 -314 -88 O ATOM 359 CB ILE A 93 47.335 9.370 30.100 1.00 28.02 C ANISOU 359 CB ILE A 93 3756 3136 3753 861 -329 40 C ATOM 360 CG1 ILE A 93 48.783 9.355 29.602 1.00 27.21 C ANISOU 360 CG1 ILE A 93 3734 3010 3593 940 -258 163 C ATOM 361 CG2 ILE A 93 46.975 10.746 30.613 1.00 23.18 C ANISOU 361 CG2 ILE A 93 3063 2545 3200 841 -299 7 C ATOM 362 CD1 ILE A 93 49.035 10.249 28.411 1.00 21.30 C ANISOU 362 CD1 ILE A 93 3059 2213 2822 1078 -251 201 C ATOM 363 N VAL A 94 44.731 8.147 31.466 1.00 18.13 N ANISOU 363 N VAL A 94 2323 1988 2576 628 -456 -153 N ATOM 364 CA VAL A 94 43.463 8.268 32.177 1.00 23.99 C ANISOU 364 CA VAL A 94 2925 2817 3372 543 -495 -228 C ATOM 365 C VAL A 94 43.522 7.523 33.498 1.00 23.71 C ANISOU 365 C VAL A 94 2837 2801 3371 403 -446 -230 C ATOM 366 O VAL A 94 43.127 8.059 34.532 1.00 27.33 O ANISOU 366 O VAL A 94 3180 3319 3885 358 -410 -249 O ATOM 367 CB VAL A 94 42.283 7.735 31.348 1.00 25.27 C ANISOU 367 CB VAL A 94 3073 3029 3501 527 -612 -294 C ATOM 368 CG1 VAL A 94 41.081 7.453 32.240 1.00 20.30 C ANISOU 368 CG1 VAL A 94 2283 2513 2918 395 -642 -350 C ATOM 369 CG2 VAL A 94 41.917 8.730 30.280 1.00 30.37 C ANISOU 369 CG2 VAL A 94 3718 3704 4117 684 -657 -299 C ATOM 370 N ASN A 95 44.021 6.289 33.462 1.00 18.23 N ANISOU 370 N ASN A 95 2247 2048 2631 354 -433 -207 N ATOM 371 CA ASN A 95 44.205 5.519 34.692 1.00 21.06 C ANISOU 371 CA ASN A 95 2583 2414 3005 247 -367 -196 C ATOM 372 C ASN A 95 45.027 6.294 35.724 1.00 28.25 C ANISOU 372 C ASN A 95 3420 3366 3949 260 -280 -149 C ATOM 373 O ASN A 95 44.662 6.385 36.908 1.00 37.19 O ANISOU 373 O ASN A 95 4450 4551 5129 183 -245 -172 O ATOM 374 CB ASN A 95 44.874 4.182 34.381 1.00 18.21 C ANISOU 374 CB ASN A 95 2400 1963 2557 247 -337 -154 C ATOM 375 CG ASN A 95 44.875 3.242 35.566 1.00 25.35 C ANISOU 375 CG ASN A 95 3305 2865 3460 146 -265 -148 C ATOM 376 OD1 ASN A 95 43.824 2.773 36.000 1.00 30.44 O ANISOU 376 OD1 ASN A 95 3900 3526 4141 16 -294 -213 O ATOM 377 ND2 ASN A 95 46.060 2.951 36.090 1.00 27.04 N ANISOU 377 ND2 ASN A 95 3572 3077 3625 209 -166 -61 N ATOM 378 N LEU A 96 46.128 6.868 35.251 1.00 24.06 N ANISOU 378 N LEU A 96 2940 2816 3384 350 -246 -81 N ATOM 379 CA LEU A 96 47.000 7.695 36.080 1.00 24.66 C ANISOU 379 CA LEU A 96 2955 2941 3472 337 -176 -36 C ATOM 380 C LEU A 96 46.232 8.848 36.735 1.00 25.21 C ANISOU 380 C LEU A 96 2930 3041 3610 298 -180 -100 C ATOM 381 O LEU A 96 46.344 9.085 37.944 1.00 22.63 O ANISOU 381 O LEU A 96 2537 2759 3303 226 -134 -107 O ATOM 382 CB LEU A 96 48.155 8.234 35.232 1.00 21.98 C ANISOU 382 CB LEU A 96 2679 2587 3084 424 -151 46 C ATOM 383 CG LEU A 96 49.368 8.825 35.946 1.00 30.52 C ANISOU 383 CG LEU A 96 3710 3742 4144 382 -79 118 C ATOM 384 CD1 LEU A 96 49.906 7.842 36.960 1.00 28.15 C ANISOU 384 CD1 LEU A 96 3372 3521 3804 339 -29 162 C ATOM 385 CD2 LEU A 96 50.439 9.176 34.932 1.00 40.03 C ANISOU 385 CD2 LEU A 96 4973 4944 5294 465 -56 214 C ATOM 386 N SER A 97 45.441 9.551 35.929 1.00 30.12 N ANISOU 386 N SER A 97 3557 3639 4248 365 -230 -141 N ATOM 387 CA SER A 97 44.650 10.677 36.414 1.00 29.79 C ANISOU 387 CA SER A 97 3458 3619 4243 376 -221 -189 C ATOM 388 C SER A 97 43.589 10.248 37.423 1.00 30.01 C ANISOU 388 C SER A 97 3375 3716 4312 308 -228 -237 C ATOM 389 O SER A 97 43.262 10.997 38.340 1.00 27.38 O ANISOU 389 O SER A 97 2999 3406 3998 299 -185 -256 O ATOM 390 CB SER A 97 43.985 11.406 35.244 1.00 21.26 C ANISOU 390 CB SER A 97 2411 2520 3149 502 -265 -208 C ATOM 391 OG SER A 97 44.936 12.141 34.498 1.00 29.78 O ANISOU 391 OG SER A 97 3594 3526 4194 569 -231 -160 O ATOM 392 N LEU A 98 43.050 9.046 37.244 1.00 25.43 N ANISOU 392 N LEU A 98 2767 3161 3736 256 -277 -255 N ATOM 393 CA LEU A 98 42.061 8.509 38.171 1.00 26.19 C ANISOU 393 CA LEU A 98 2752 3327 3870 170 -278 -290 C ATOM 394 C LEU A 98 42.701 8.228 39.526 1.00 29.82 C ANISOU 394 C LEU A 98 3201 3788 4343 99 -196 -268 C ATOM 395 O LEU A 98 42.138 8.572 40.570 1.00 26.29 O ANISOU 395 O LEU A 98 2669 3392 3927 76 -160 -286 O ATOM 396 CB LEU A 98 41.425 7.235 37.610 1.00 25.71 C ANISOU 396 CB LEU A 98 2694 3277 3797 94 -345 -314 C ATOM 397 CG LEU A 98 40.495 7.420 36.407 1.00 31.69 C ANISOU 397 CG LEU A 98 3422 4084 4533 139 -446 -349 C ATOM 398 CD1 LEU A 98 39.958 6.082 35.927 1.00 24.72 C ANISOU 398 CD1 LEU A 98 2569 3202 3623 13 -516 -382 C ATOM 399 CD2 LEU A 98 39.354 8.366 36.749 1.00 27.42 C ANISOU 399 CD2 LEU A 98 2726 3672 4020 193 -455 -368 C ATOM 400 N ALA A 99 43.877 7.604 39.505 1.00 28.12 N ANISOU 400 N ALA A 99 3069 3529 4087 85 -162 -220 N ATOM 401 CA ALA A 99 44.627 7.370 40.738 1.00 24.67 C ANISOU 401 CA ALA A 99 2616 3119 3639 39 -85 -188 C ATOM 402 C ALA A 99 44.927 8.694 41.444 1.00 33.79 C ANISOU 402 C ALA A 99 3737 4299 4802 44 -51 -196 C ATOM 403 O ALA A 99 44.781 8.815 42.673 1.00 25.01 O ANISOU 403 O ALA A 99 2573 3229 3702 1 -7 -210 O ATOM 404 CB ALA A 99 45.918 6.619 40.445 1.00 20.82 C ANISOU 404 CB ALA A 99 2217 2614 3080 63 -50 -115 C ATOM 405 N ASP A 100 45.335 9.688 40.656 1.00 31.83 N ANISOU 405 N ASP A 100 3543 4014 4538 95 -67 -187 N ATOM 406 CA ASP A 100 45.646 11.009 41.194 1.00 32.64 C ANISOU 406 CA ASP A 100 3666 4105 4629 82 -30 -199 C ATOM 407 C ASP A 100 44.422 11.687 41.818 1.00 29.15 C ANISOU 407 C ASP A 100 3191 3667 4219 110 -20 -256 C ATOM 408 O ASP A 100 44.531 12.324 42.866 1.00 22.79 O ANISOU 408 O ASP A 100 2398 2863 3397 73 27 -273 O ATOM 409 CB ASP A 100 46.245 11.896 40.102 1.00 35.18 C ANISOU 409 CB ASP A 100 4077 4366 4924 129 -38 -175 C ATOM 410 CG ASP A 100 47.684 11.528 39.779 1.00 58.71 C ANISOU 410 CG ASP A 100 7080 7373 7856 96 -22 -98 C ATOM 411 OD1 ASP A 100 48.369 10.974 40.665 1.00 57.60 O ANISOU 411 OD1 ASP A 100 6889 7311 7687 28 7 -66 O ATOM 412 OD2 ASP A 100 48.131 11.795 38.643 1.00 74.68 O ANISOU 412 OD2 ASP A 100 9163 9354 9858 154 -34 -59 O ATOM 413 N VAL A 101 43.264 11.547 41.178 1.00 19.72 N ANISOU 413 N VAL A 101 1953 2486 3052 181 -64 -279 N ATOM 414 CA VAL A 101 42.016 12.076 41.727 1.00 28.36 C ANISOU 414 CA VAL A 101 2988 3625 4163 237 -49 -310 C ATOM 415 C VAL A 101 41.688 11.385 43.047 1.00 29.71 C ANISOU 415 C VAL A 101 3071 3857 4361 163 -15 -315 C ATOM 416 O VAL A 101 41.298 12.031 44.025 1.00 35.20 O ANISOU 416 O VAL A 101 3762 4566 5047 189 38 -327 O ATOM 417 CB VAL A 101 40.832 11.897 40.745 1.00 23.17 C ANISOU 417 CB VAL A 101 2258 3029 3517 317 -114 -319 C ATOM 418 CG1 VAL A 101 39.504 12.112 41.457 1.00 24.78 C ANISOU 418 CG1 VAL A 101 2345 3338 3732 366 -95 -328 C ATOM 419 CG2 VAL A 101 40.962 12.848 39.572 1.00 25.30 C ANISOU 419 CG2 VAL A 101 2622 3244 3747 437 -129 -313 C ATOM 420 N LEU A 102 41.857 10.065 43.063 1.00 26.44 N ANISOU 420 N LEU A 102 2612 3467 3968 83 -34 -303 N ATOM 421 CA LEU A 102 41.635 9.266 44.261 1.00 33.74 C ANISOU 421 CA LEU A 102 3469 4437 4912 14 11 -300 C ATOM 422 C LEU A 102 42.445 9.787 45.446 1.00 36.00 C ANISOU 422 C LEU A 102 3796 4716 5167 -4 76 -295 C ATOM 423 O LEU A 102 41.885 10.152 46.492 1.00 35.66 O ANISOU 423 O LEU A 102 3717 4704 5130 11 121 -309 O ATOM 424 CB LEU A 102 41.987 7.802 43.991 1.00 29.37 C ANISOU 424 CB LEU A 102 2930 3871 4358 -61 0 -280 C ATOM 425 CG LEU A 102 42.022 6.876 45.209 1.00 32.79 C ANISOU 425 CG LEU A 102 3333 4331 4796 -124 68 -265 C ATOM 426 CD1 LEU A 102 40.658 6.822 45.886 1.00 27.00 C ANISOU 426 CD1 LEU A 102 2482 3663 4112 -145 83 -284 C ATOM 427 CD2 LEU A 102 42.485 5.484 44.808 1.00 30.19 C ANISOU 427 CD2 LEU A 102 3078 3956 4437 -173 76 -238 C ATOM 428 N VAL A 103 43.764 9.833 45.273 1.00 22.41 N ANISOU 428 N VAL A 103 2145 2968 3402 -35 80 -271 N ATOM 429 CA VAL A 103 44.644 10.253 46.358 1.00 27.45 C ANISOU 429 CA VAL A 103 2808 3630 3991 -82 127 -266 C ATOM 430 C VAL A 103 44.437 11.737 46.700 1.00 34.94 C ANISOU 430 C VAL A 103 3827 4533 4916 -64 144 -306 C ATOM 431 O VAL A 103 44.647 12.155 47.839 1.00 27.43 O ANISOU 431 O VAL A 103 2899 3596 3925 -99 184 -324 O ATOM 432 CB VAL A 103 46.133 9.980 46.013 1.00 23.83 C ANISOU 432 CB VAL A 103 2382 3198 3474 -124 124 -214 C ATOM 433 CG1 VAL A 103 46.589 10.819 44.826 1.00 28.13 C ANISOU 433 CG1 VAL A 103 2997 3686 4006 -109 89 -205 C ATOM 434 CG2 VAL A 103 47.024 10.222 47.223 1.00 19.06 C ANISOU 434 CG2 VAL A 103 1769 2669 2805 -191 162 -205 C ATOM 435 N THR A 104 43.998 12.525 45.722 1.00 31.75 N ANISOU 435 N THR A 104 3478 4066 4520 3 121 -319 N ATOM 436 CA THR A 104 43.721 13.939 45.958 1.00 31.66 C ANISOU 436 CA THR A 104 3580 3983 4466 46 157 -351 C ATOM 437 C THR A 104 42.516 14.122 46.881 1.00 38.65 C ANISOU 437 C THR A 104 4431 4896 5358 125 200 -370 C ATOM 438 O THR A 104 42.550 14.926 47.815 1.00 40.82 O ANISOU 438 O THR A 104 4803 5129 5577 126 253 -395 O ATOM 439 CB THR A 104 43.468 14.692 44.635 1.00 26.47 C ANISOU 439 CB THR A 104 3000 3255 3804 136 139 -349 C ATOM 440 OG1 THR A 104 44.662 14.677 43.842 1.00 41.35 O ANISOU 440 OG1 THR A 104 4932 5108 5673 67 114 -322 O ATOM 441 CG2 THR A 104 43.066 16.135 44.900 1.00 21.30 C ANISOU 441 CG2 THR A 104 2500 2507 3087 211 200 -376 C ATOM 442 N ILE A 105 41.455 13.368 46.619 1.00 30.55 N ANISOU 442 N ILE A 105 3271 3945 4390 185 178 -355 N ATOM 443 CA ILE A 105 40.233 13.487 47.406 1.00 33.66 C ANISOU 443 CA ILE A 105 3599 4401 4790 272 221 -351 C ATOM 444 C ILE A 105 40.359 12.859 48.793 1.00 33.17 C ANISOU 444 C ILE A 105 3487 4380 4734 208 265 -350 C ATOM 445 O ILE A 105 39.962 13.463 49.792 1.00 24.57 O ANISOU 445 O ILE A 105 2443 3287 3605 269 327 -356 O ATOM 446 CB ILE A 105 39.036 12.842 46.679 1.00 32.42 C ANISOU 446 CB ILE A 105 3283 4350 4686 326 177 -328 C ATOM 447 CG1 ILE A 105 38.695 13.631 45.415 1.00 40.91 C ANISOU 447 CG1 ILE A 105 4403 5408 5733 440 144 -325 C ATOM 448 CG2 ILE A 105 37.825 12.770 47.595 1.00 30.93 C ANISOU 448 CG2 ILE A 105 2981 4268 4505 396 227 -304 C ATOM 449 CD1 ILE A 105 37.506 13.080 44.658 1.00 50.60 C ANISOU 449 CD1 ILE A 105 5461 6774 6989 486 85 -304 C ATOM 450 N THR A 106 40.922 11.656 48.860 1.00 37.74 N ANISOU 450 N THR A 106 3996 4993 5349 104 243 -338 N ATOM 451 CA THR A 106 40.860 10.883 50.099 1.00 38.14 C ANISOU 451 CA THR A 106 3985 5097 5408 67 293 -327 C ATOM 452 C THR A 106 42.043 11.063 51.053 1.00 42.94 C ANISOU 452 C THR A 106 4674 5691 5950 8 323 -338 C ATOM 453 O THR A 106 41.912 10.810 52.250 1.00 46.30 O ANISOU 453 O THR A 106 5078 6154 6359 15 377 -336 O ATOM 454 CB THR A 106 40.732 9.381 49.799 1.00 32.69 C ANISOU 454 CB THR A 106 3199 4450 4773 -2 277 -300 C ATOM 455 OG1 THR A 106 41.909 8.926 49.118 1.00 29.01 O ANISOU 455 OG1 THR A 106 2791 3947 4283 -59 243 -291 O ATOM 456 CG2 THR A 106 39.509 9.114 48.935 1.00 21.08 C ANISOU 456 CG2 THR A 106 1631 3023 3357 17 236 -294 C ATOM 457 N CYS A 107 43.191 11.497 50.543 1.00 32.24 N ANISOU 457 N CYS A 107 3400 4299 4550 -51 289 -346 N ATOM 458 CA CYS A 107 44.410 11.473 51.352 1.00 28.21 C ANISOU 458 CA CYS A 107 2924 3829 3966 -133 301 -345 C ATOM 459 C CYS A 107 44.994 12.850 51.651 1.00 26.40 C ANISOU 459 C CYS A 107 2832 3546 3654 -185 299 -387 C ATOM 460 O CYS A 107 45.405 13.124 52.781 1.00 25.82 O ANISOU 460 O CYS A 107 2798 3503 3508 -232 322 -410 O ATOM 461 CB CYS A 107 45.469 10.611 50.664 1.00 32.07 C ANISOU 461 CB CYS A 107 3373 4367 4446 -185 270 -298 C ATOM 462 SG CYS A 107 44.943 8.909 50.394 1.00 39.12 S ANISOU 462 SG CYS A 107 4175 5288 5402 -148 288 -253 S ATOM 463 N LEU A 108 45.041 13.704 50.634 1.00 30.77 N ANISOU 463 N LEU A 108 3472 4014 4206 -183 274 -399 N ATOM 464 CA LEU A 108 45.597 15.051 50.767 1.00 25.41 C ANISOU 464 CA LEU A 108 2963 3250 3440 -255 282 -441 C ATOM 465 C LEU A 108 45.051 15.845 51.975 1.00 27.71 C ANISOU 465 C LEU A 108 3379 3485 3664 -224 336 -490 C ATOM 466 O LEU A 108 45.842 16.395 52.750 1.00 45.69 O ANISOU 466 O LEU A 108 5758 5758 5846 -346 338 -526 O ATOM 467 CB LEU A 108 45.367 15.825 49.461 1.00 22.02 C ANISOU 467 CB LEU A 108 2627 2712 3028 -206 272 -441 C ATOM 468 CG LEU A 108 45.866 17.263 49.300 1.00 24.03 C ANISOU 468 CG LEU A 108 3100 2838 3194 -278 296 -478 C ATOM 469 CD1 LEU A 108 46.213 17.518 47.848 1.00 24.60 C ANISOU 469 CD1 LEU A 108 3198 2856 3291 -273 272 -449 C ATOM 470 CD2 LEU A 108 44.823 18.271 49.769 1.00 27.77 C ANISOU 470 CD2 LEU A 108 3746 3190 3617 -155 365 -518 C ATOM 471 N PRO A 109 43.713 15.907 52.153 1.00 26.83 N ANISOU 471 N PRO A 109 3261 3346 3589 -63 381 -487 N ATOM 472 CA PRO A 109 43.223 16.717 53.279 1.00 31.28 C ANISOU 472 CA PRO A 109 3970 3847 4067 -5 446 -523 C ATOM 473 C PRO A 109 43.645 16.163 54.638 1.00 37.19 C ANISOU 473 C PRO A 109 4671 4681 4777 -70 455 -535 C ATOM 474 O PRO A 109 44.085 16.921 55.513 1.00 37.22 O ANISOU 474 O PRO A 109 4840 4633 4669 -136 473 -584 O ATOM 475 CB PRO A 109 41.697 16.657 53.125 1.00 24.44 C ANISOU 475 CB PRO A 109 3041 2992 3252 202 494 -486 C ATOM 476 CG PRO A 109 41.462 16.236 51.710 1.00 34.91 C ANISOU 476 CG PRO A 109 4249 4348 4665 229 443 -453 C ATOM 477 CD PRO A 109 42.597 15.327 51.383 1.00 28.13 C ANISOU 477 CD PRO A 109 3292 3547 3849 70 376 -447 C ATOM 478 N ALA A 110 43.505 14.850 54.802 1.00 39.35 N ANISOU 478 N ALA A 110 4742 5078 5132 -53 445 -491 N ATOM 479 CA ALA A 110 43.919 14.172 56.024 1.00 31.66 C ANISOU 479 CA ALA A 110 3708 4201 4122 -90 462 -489 C ATOM 480 C ALA A 110 45.377 14.481 56.331 1.00 30.73 C ANISOU 480 C ALA A 110 3651 4125 3901 -260 416 -519 C ATOM 481 O ALA A 110 45.733 14.776 57.472 1.00 45.57 O ANISOU 481 O ALA A 110 5602 6032 5681 -304 428 -554 O ATOM 482 CB ALA A 110 43.706 12.669 55.899 1.00 22.60 C ANISOU 482 CB ALA A 110 2360 3157 3068 -60 467 -430 C ATOM 483 N THR A 111 46.210 14.427 55.297 1.00 20.58 N ANISOU 483 N THR A 111 2330 2859 2629 -356 360 -500 N ATOM 484 CA THR A 111 47.633 14.697 55.435 1.00 21.01 C ANISOU 484 CA THR A 111 2402 2996 2585 -532 311 -508 C ATOM 485 C THR A 111 47.885 16.133 55.869 1.00 29.93 C ANISOU 485 C THR A 111 3753 4018 3599 -646 309 -585 C ATOM 486 O THR A 111 48.746 16.388 56.707 1.00 26.18 O ANISOU 486 O THR A 111 3312 3628 3008 -789 281 -616 O ATOM 487 CB THR A 111 48.384 14.427 54.125 1.00 22.56 C ANISOU 487 CB THR A 111 2523 3230 2820 -591 265 -457 C ATOM 488 OG1 THR A 111 48.161 13.070 53.722 1.00 28.99 O ANISOU 488 OG1 THR A 111 3177 4119 3719 -487 274 -390 O ATOM 489 CG2 THR A 111 49.874 14.656 54.312 1.00 30.01 C ANISOU 489 CG2 THR A 111 3442 4309 3650 -776 218 -445 C ATOM 490 N LEU A 112 47.135 17.073 55.300 1.00 32.73 N ANISOU 490 N LEU A 112 4274 4191 3970 -584 341 -616 N ATOM 491 CA LEU A 112 47.254 18.466 55.719 1.00 31.61 C ANISOU 491 CA LEU A 112 4407 3902 3704 -674 362 -691 C ATOM 492 C LEU A 112 46.933 18.612 57.208 1.00 37.71 C ANISOU 492 C LEU A 112 5271 4675 4383 -642 397 -737 C ATOM 493 O LEU A 112 47.695 19.228 57.964 1.00 37.53 O ANISOU 493 O LEU A 112 5387 4650 4222 -816 372 -798 O ATOM 494 CB LEU A 112 46.337 19.366 54.893 1.00 24.75 C ANISOU 494 CB LEU A 112 3715 2834 2856 -544 419 -699 C ATOM 495 CG LEU A 112 46.338 20.829 55.343 1.00 37.70 C ANISOU 495 CG LEU A 112 5703 4275 4345 -605 470 -774 C ATOM 496 CD1 LEU A 112 47.727 21.435 55.190 1.00 44.42 C ANISOU 496 CD1 LEU A 112 6657 5119 5102 -903 417 -815 C ATOM 497 CD2 LEU A 112 45.304 21.642 54.581 1.00 34.31 C ANISOU 497 CD2 LEU A 112 5452 3662 3920 -407 552 -764 C ATOM 498 N VAL A 113 45.811 18.030 57.623 1.00 34.61 N ANISOU 498 N VAL A 113 4797 4295 4060 -430 451 -705 N ATOM 499 CA VAL A 113 45.389 18.100 59.021 1.00 33.45 C ANISOU 499 CA VAL A 113 4729 4148 3832 -358 498 -734 C ATOM 500 C VAL A 113 46.427 17.500 59.968 1.00 32.82 C ANISOU 500 C VAL A 113 4549 4241 3681 -497 446 -747 C ATOM 501 O VAL A 113 46.783 18.110 60.973 1.00 34.84 O ANISOU 501 O VAL A 113 4969 4476 3793 -581 443 -811 O ATOM 502 CB VAL A 113 44.048 17.381 59.242 1.00 29.85 C ANISOU 502 CB VAL A 113 4142 3722 3479 -115 568 -673 C ATOM 503 CG1 VAL A 113 43.683 17.397 60.719 1.00 33.59 C ANISOU 503 CG1 VAL A 113 4690 4208 3866 -30 624 -691 C ATOM 504 CG2 VAL A 113 42.955 18.033 58.415 1.00 31.36 C ANISOU 504 CG2 VAL A 113 4419 3786 3711 48 622 -651 C ATOM 505 N VAL A 114 46.907 16.304 59.641 1.00 32.92 N ANISOU 505 N VAL A 114 4306 4426 3776 -512 411 -684 N ATOM 506 CA VAL A 114 47.907 15.628 60.462 1.00 32.60 C ANISOU 506 CA VAL A 114 4143 4586 3658 -605 371 -674 C ATOM 507 C VAL A 114 49.214 16.414 60.528 1.00 42.79 C ANISOU 507 C VAL A 114 5517 5936 4805 -859 292 -724 C ATOM 508 O VAL A 114 49.779 16.595 61.603 1.00 48.83 O ANISOU 508 O VAL A 114 6324 6797 5431 -954 264 -767 O ATOM 509 CB VAL A 114 48.197 14.208 59.935 1.00 31.35 C ANISOU 509 CB VAL A 114 3728 4585 3598 -548 366 -582 C ATOM 510 CG1 VAL A 114 49.368 13.585 60.681 1.00 27.41 C ANISOU 510 CG1 VAL A 114 3107 4318 2988 -627 332 -556 C ATOM 511 CG2 VAL A 114 46.961 13.343 60.068 1.00 28.16 C ANISOU 511 CG2 VAL A 114 3243 4143 3315 -344 444 -537 C ATOM 512 N ASP A 115 49.688 16.890 59.381 1.00 38.54 N ANISOU 512 N ASP A 115 5001 5350 4294 -978 254 -717 N ATOM 513 CA ASP A 115 50.944 17.631 59.337 1.00 40.07 C ANISOU 513 CA ASP A 115 5255 5613 4357 -1252 180 -753 C ATOM 514 C ASP A 115 50.834 18.974 60.053 1.00 43.37 C ANISOU 514 C ASP A 115 5986 5860 4631 -1380 186 -865 C ATOM 515 O ASP A 115 51.838 19.531 60.496 1.00 46.77 O ANISOU 515 O ASP A 115 6482 6376 4913 -1635 121 -914 O ATOM 516 CB ASP A 115 51.397 17.843 57.892 1.00 35.98 C ANISOU 516 CB ASP A 115 4699 5063 3907 -1335 156 -710 C ATOM 517 CG ASP A 115 51.934 16.573 57.259 1.00 48.06 C ANISOU 517 CG ASP A 115 5942 6801 5516 -1269 135 -599 C ATOM 518 OD1 ASP A 115 52.083 15.564 57.982 1.00 55.43 O ANISOU 518 OD1 ASP A 115 6714 7913 6433 -1183 140 -557 O ATOM 519 OD2 ASP A 115 52.221 16.585 56.043 1.00 44.42 O ANISOU 519 OD2 ASP A 115 5438 6320 5121 -1291 123 -550 O ATOM 520 N ILE A 116 49.616 19.490 60.172 1.00 41.13 N ANISOU 520 N ILE A 116 5905 5344 4377 -1204 267 -900 N ATOM 521 CA ILE A 116 49.398 20.740 60.892 1.00 45.15 C ANISOU 521 CA ILE A 116 6765 5657 4732 -1278 297 -1001 C ATOM 522 C ILE A 116 49.276 20.521 62.405 1.00 44.36 C ANISOU 522 C ILE A 116 6701 5631 4523 -1232 301 -1041 C ATOM 523 O ILE A 116 49.862 21.260 63.200 1.00 42.35 O ANISOU 523 O ILE A 116 6647 5358 4088 -1428 262 -1128 O ATOM 524 CB ILE A 116 48.136 21.465 60.377 1.00 40.58 C ANISOU 524 CB ILE A 116 6415 4804 4200 -1068 400 -1005 C ATOM 525 CG1 ILE A 116 48.430 22.154 59.046 1.00 49.55 C ANISOU 525 CG1 ILE A 116 7647 5814 5366 -1171 399 -1001 C ATOM 526 CG2 ILE A 116 47.649 22.493 61.382 1.00 51.50 C ANISOU 526 CG2 ILE A 116 8164 5989 5414 -1036 464 -1089 C ATOM 527 CD1 ILE A 116 47.261 22.942 58.506 1.00 59.94 C ANISOU 527 CD1 ILE A 116 9200 6877 6696 -952 506 -998 C ATOM 528 N THR A 117 48.531 19.492 62.796 1.00 34.04 N ANISOU 528 N THR A 117 5204 4411 3318 -985 347 -977 N ATOM 529 CA THR A 117 48.183 19.280 64.198 1.00 30.81 C ANISOU 529 CA THR A 117 4843 4042 2820 -879 379 -1002 C ATOM 530 C THR A 117 49.020 18.202 64.885 1.00 31.48 C ANISOU 530 C THR A 117 4666 4418 2876 -927 320 -968 C ATOM 531 O THR A 117 49.041 18.124 66.114 1.00 31.30 O ANISOU 531 O THR A 117 4696 4458 2738 -894 326 -1002 O ATOM 532 CB THR A 117 46.699 18.896 64.340 1.00 34.59 C ANISOU 532 CB THR A 117 5305 4425 3413 -555 492 -946 C ATOM 533 OG1 THR A 117 46.462 17.646 63.680 1.00 28.86 O ANISOU 533 OG1 THR A 117 4262 3834 2869 -447 499 -848 O ATOM 534 CG2 THR A 117 45.811 19.967 63.723 1.00 31.70 C ANISOU 534 CG2 THR A 117 5195 3802 3048 -456 564 -963 C ATOM 535 N GLU A 118 49.691 17.374 64.088 1.00 39.81 N ANISOU 535 N GLU A 118 5454 5650 4022 -981 274 -895 N ATOM 536 CA GLU A 118 50.488 16.248 64.586 1.00 39.65 C ANISOU 536 CA GLU A 118 5174 5921 3971 -981 239 -835 C ATOM 537 C GLU A 118 49.655 15.259 65.403 1.00 43.03 C ANISOU 537 C GLU A 118 5511 6382 4455 -720 326 -787 C ATOM 538 O GLU A 118 50.185 14.550 66.258 1.00 48.72 O ANISOU 538 O GLU A 118 6108 7310 5093 -691 318 -761 O ATOM 539 CB GLU A 118 51.672 16.746 65.419 1.00 43.29 C ANISOU 539 CB GLU A 118 5677 6555 4216 -1221 145 -898 C ATOM 540 CG GLU A 118 52.582 17.712 64.681 1.00 52.97 C ANISOU 540 CG GLU A 118 6984 7770 5371 -1525 59 -942 C ATOM 541 CD GLU A 118 53.861 18.005 65.439 1.00 73.82 C ANISOU 541 CD GLU A 118 9590 10662 7797 -1794 -50 -985 C ATOM 542 OE1 GLU A 118 54.124 17.323 66.452 1.00 78.01 O ANISOU 542 OE1 GLU A 118 9992 11411 8239 -1716 -63 -966 O ATOM 543 OE2 GLU A 118 54.603 18.919 65.021 1.00 82.98 O ANISOU 543 OE2 GLU A 118 10849 11811 8869 -2090 -121 -1034 O ATOM 544 N THR A 119 48.353 15.217 65.134 1.00 39.22 N ANISOU 544 N THR A 119 5084 5712 4106 -529 415 -767 N ATOM 545 CA THR A 119 47.457 14.265 65.784 1.00 44.43 C ANISOU 545 CA THR A 119 5647 6394 4841 -294 510 -709 C ATOM 546 C THR A 119 46.503 13.638 64.772 1.00 43.41 C ANISOU 546 C THR A 119 5401 6184 4911 -162 569 -636 C ATOM 547 O THR A 119 46.357 14.129 63.652 1.00 43.74 O ANISOU 547 O THR A 119 5477 6120 5022 -216 541 -642 O ATOM 548 CB THR A 119 46.626 14.924 66.910 1.00 48.63 C ANISOU 548 CB THR A 119 6387 6800 5288 -175 574 -759 C ATOM 549 OG1 THR A 119 45.918 16.052 66.387 1.00 54.01 O ANISOU 549 OG1 THR A 119 7283 7257 5982 -163 595 -801 O ATOM 550 CG2 THR A 119 47.522 15.377 68.055 1.00 49.56 C ANISOU 550 CG2 THR A 119 6620 7015 5194 -296 515 -835 C ATOM 551 N TRP A 120 45.854 12.550 65.176 1.00 34.28 N ANISOU 551 N TRP A 120 4112 5079 3835 3 650 -567 N ATOM 552 CA TRP A 120 44.897 11.865 64.317 1.00 28.94 C ANISOU 552 CA TRP A 120 3318 4342 3333 103 703 -500 C ATOM 553 C TRP A 120 43.490 11.970 64.904 1.00 31.07 C ANISOU 553 C TRP A 120 3630 4524 3651 280 802 -480 C ATOM 554 O TRP A 120 43.189 11.355 65.925 1.00 32.33 O ANISOU 554 O TRP A 120 3750 4742 3791 388 876 -447 O ATOM 555 CB TRP A 120 45.299 10.398 64.132 1.00 22.97 C ANISOU 555 CB TRP A 120 2376 3718 2635 123 726 -423 C ATOM 556 CG TRP A 120 44.463 9.665 63.125 1.00 23.57 C ANISOU 556 CG TRP A 120 2349 3732 2875 169 761 -366 C ATOM 557 CD1 TRP A 120 43.406 8.841 63.379 1.00 26.89 C ANISOU 557 CD1 TRP A 120 2695 4133 3389 280 854 -312 C ATOM 558 CD2 TRP A 120 44.613 9.697 61.701 1.00 20.80 C ANISOU 558 CD2 TRP A 120 1964 3338 2603 90 700 -360 C ATOM 559 NE1 TRP A 120 42.888 8.356 62.202 1.00 20.74 N ANISOU 559 NE1 TRP A 120 1838 3307 2735 254 844 -279 N ATOM 560 CE2 TRP A 120 43.614 8.865 61.157 1.00 27.87 C ANISOU 560 CE2 TRP A 120 2769 4191 3630 151 750 -309 C ATOM 561 CE3 TRP A 120 45.497 10.343 60.835 1.00 23.84 C ANISOU 561 CE3 TRP A 120 2387 3719 2953 -35 609 -389 C ATOM 562 CZ2 TRP A 120 43.474 8.667 59.784 1.00 31.48 C ANISOU 562 CZ2 TRP A 120 3182 4601 4177 101 703 -295 C ATOM 563 CZ3 TRP A 120 45.358 10.144 59.473 1.00 32.54 C ANISOU 563 CZ3 TRP A 120 3443 4768 4151 -63 575 -366 C ATOM 564 CH2 TRP A 120 44.354 9.313 58.961 1.00 26.45 C ANISOU 564 CH2 TRP A 120 2592 3955 3504 9 618 -323 C ATOM 565 N PHE A 121 42.635 12.756 64.254 1.00 43.25 N ANISOU 565 N PHE A 121 5248 5941 5245 324 810 -488 N ATOM 566 CA PHE A 121 41.287 13.014 64.757 1.00 41.57 C ANISOU 566 CA PHE A 121 5071 5670 5055 509 907 -453 C ATOM 567 C PHE A 121 40.291 11.977 64.269 1.00 39.08 C ANISOU 567 C PHE A 121 4543 5408 4899 586 962 -364 C ATOM 568 O PHE A 121 39.221 11.800 64.852 1.00 41.19 O ANISOU 568 O PHE A 121 4766 5691 5194 733 1055 -307 O ATOM 569 CB PHE A 121 40.817 14.405 64.337 1.00 39.32 C ANISOU 569 CB PHE A 121 4983 5242 4716 552 906 -491 C ATOM 570 CG PHE A 121 41.642 15.519 64.905 1.00 49.47 C ANISOU 570 CG PHE A 121 6532 6440 5826 463 868 -585 C ATOM 571 CD1 PHE A 121 41.350 16.048 66.151 1.00 49.62 C ANISOU 571 CD1 PHE A 121 6733 6410 5712 571 930 -609 C ATOM 572 CD2 PHE A 121 42.708 16.040 64.192 1.00 49.76 C ANISOU 572 CD2 PHE A 121 6645 6443 5819 260 771 -648 C ATOM 573 CE1 PHE A 121 42.108 17.075 66.677 1.00 50.46 C ANISOU 573 CE1 PHE A 121 7109 6424 5638 460 889 -707 C ATOM 574 CE2 PHE A 121 43.470 17.067 64.711 1.00 53.88 C ANISOU 574 CE2 PHE A 121 7415 6887 6169 133 733 -740 C ATOM 575 CZ PHE A 121 43.169 17.586 65.956 1.00 57.24 C ANISOU 575 CZ PHE A 121 8039 7254 6456 224 788 -775 C ATOM 576 N PHE A 122 40.650 11.298 63.189 1.00 38.49 N ANISOU 576 N PHE A 122 4342 5363 4918 477 905 -348 N ATOM 577 CA PHE A 122 39.752 10.350 62.551 1.00 40.44 C ANISOU 577 CA PHE A 122 4412 5649 5307 501 938 -278 C ATOM 578 C PHE A 122 39.800 9.009 63.271 1.00 46.15 C ANISOU 578 C PHE A 122 5028 6448 6059 510 1009 -227 C ATOM 579 O PHE A 122 40.523 8.852 64.252 1.00 65.52 O ANISOU 579 O PHE A 122 7536 8937 8419 525 1031 -242 O ATOM 580 CB PHE A 122 40.120 10.218 61.078 1.00 37.63 C ANISOU 580 CB PHE A 122 4007 5272 5019 386 849 -290 C ATOM 581 CG PHE A 122 40.578 11.514 60.469 1.00 39.84 C ANISOU 581 CG PHE A 122 4431 5469 5236 349 779 -351 C ATOM 582 CD1 PHE A 122 39.693 12.568 60.308 1.00 38.43 C ANISOU 582 CD1 PHE A 122 4339 5224 5039 457 803 -354 C ATOM 583 CD2 PHE A 122 41.899 11.691 60.088 1.00 50.94 C ANISOU 583 CD2 PHE A 122 5896 6870 6587 216 702 -394 C ATOM 584 CE1 PHE A 122 40.111 13.769 59.762 1.00 40.28 C ANISOU 584 CE1 PHE A 122 4746 5356 5203 426 759 -409 C ATOM 585 CE2 PHE A 122 42.325 12.889 59.540 1.00 51.26 C ANISOU 585 CE2 PHE A 122 6084 6825 6568 159 649 -447 C ATOM 586 CZ PHE A 122 41.428 13.930 59.377 1.00 45.05 C ANISOU 586 CZ PHE A 122 5413 5939 5764 262 681 -460 C ATOM 587 N GLY A 123 39.021 8.047 62.799 1.00 40.83 N ANISOU 587 N GLY A 123 4214 5800 5500 496 1047 -167 N ATOM 588 CA GLY A 123 38.885 6.792 63.515 1.00 48.30 C ANISOU 588 CA GLY A 123 5089 6791 6471 511 1142 -111 C ATOM 589 C GLY A 123 40.072 5.857 63.398 1.00 45.52 C ANISOU 589 C GLY A 123 4755 6456 6084 438 1131 -112 C ATOM 590 O GLY A 123 41.121 6.217 62.863 1.00 37.52 O ANISOU 590 O GLY A 123 3795 5444 5016 375 1043 -154 O ATOM 591 N GLN A 124 39.899 4.649 63.924 1.00 47.87 N ANISOU 591 N GLN A 124 5036 6766 6386 443 1200 -65 N ATOM 592 CA GLN A 124 40.851 3.564 63.736 1.00 45.19 C ANISOU 592 CA GLN A 124 4737 6432 6001 396 1198 -49 C ATOM 593 C GLN A 124 40.794 3.099 62.286 1.00 37.85 C ANISOU 593 C GLN A 124 3769 5455 5157 295 1170 -35 C ATOM 594 O GLN A 124 41.824 2.882 61.626 1.00 42.64 O ANISOU 594 O GLN A 124 4406 6068 5728 265 1142 -36 O ATOM 595 CB GLN A 124 40.527 2.404 64.682 1.00 50.15 C ANISOU 595 CB GLN A 124 5407 7047 6601 426 1266 -8 C ATOM 596 CG GLN A 124 41.639 2.042 65.644 1.00 59.92 C ANISOU 596 CG GLN A 124 6727 8324 7715 490 1277 -11 C ATOM 597 CD GLN A 124 42.736 1.220 64.996 1.00 67.00 C ANISOU 597 CD GLN A 124 7670 9228 8558 463 1265 11 C ATOM 598 OE1 GLN A 124 42.595 0.752 63.866 1.00 82.79 O ANISOU 598 OE1 GLN A 124 9660 11183 10614 398 1267 32 O ATOM 599 NE2 GLN A 124 43.837 1.038 65.713 1.00 58.95 N ANISOU 599 NE2 GLN A 124 6706 8269 7425 521 1256 17 N ATOM 600 N SER A 125 39.562 2.959 61.805 1.00 28.36 N ANISOU 600 N SER A 125 3561 4091 3124 -774 168 200 N ATOM 601 CA SER A 125 39.296 2.487 60.460 1.00 29.43 C ANISOU 601 CA SER A 125 3631 4135 3415 -651 127 239 C ATOM 602 C SER A 125 39.983 3.361 59.429 1.00 37.31 C ANISOU 602 C SER A 125 4591 5099 4484 -594 130 172 C ATOM 603 O SER A 125 40.672 2.849 58.563 1.00 30.35 O ANISOU 603 O SER A 125 3663 4206 3663 -521 30 209 O ATOM 604 CB SER A 125 37.793 2.441 60.193 1.00 29.06 C ANISOU 604 CB SER A 125 3559 4034 3447 -627 227 237 C ATOM 605 OG SER A 125 37.189 1.386 60.918 1.00 42.98 O ANISOU 605 OG SER A 125 5356 5813 5160 -689 219 306 O ATOM 606 N LEU A 126 39.807 4.674 59.529 1.00 40.22 N ANISOU 606 N LEU A 126 5000 5440 4844 -629 267 74 N ATOM 607 CA LEU A 126 40.428 5.583 58.572 1.00 30.21 C ANISOU 607 CA LEU A 126 3731 4114 3634 -589 305 10 C ATOM 608 C LEU A 126 41.947 5.578 58.717 1.00 39.48 C ANISOU 608 C LEU A 126 4886 5384 4729 -671 209 -22 C ATOM 609 O LEU A 126 42.673 5.785 57.739 1.00 33.34 O ANISOU 609 O LEU A 126 4072 4583 4011 -628 179 -40 O ATOM 610 CB LEU A 126 39.877 6.997 58.737 1.00 27.11 C ANISOU 610 CB LEU A 126 3429 3634 3236 -605 511 -82 C ATOM 611 CG LEU A 126 38.422 7.152 58.294 1.00 29.81 C ANISOU 611 CG LEU A 126 3749 3909 3669 -465 611 -41 C ATOM 612 CD1 LEU A 126 37.935 8.573 58.509 1.00 26.62 C ANISOU 612 CD1 LEU A 126 3457 3403 3255 -441 839 -118 C ATOM 613 CD2 LEU A 126 38.265 6.741 56.839 1.00 35.16 C ANISOU 613 CD2 LEU A 126 4334 4561 4463 -316 529 25 C ATOM 614 N CYS A 127 42.422 5.325 59.936 1.00 20.95 N ANISOU 614 N CYS A 127 2551 3172 2237 -789 161 -26 N ATOM 615 CA CYS A 127 43.852 5.181 60.182 1.00 21.63 C ANISOU 615 CA CYS A 127 2574 3424 2220 -859 45 -43 C ATOM 616 C CYS A 127 44.384 3.980 59.409 1.00 36.51 C ANISOU 616 C CYS A 127 4366 5329 4179 -709 -115 76 C ATOM 617 O CYS A 127 45.546 3.963 59.006 1.00 33.03 O ANISOU 617 O CYS A 127 3841 4988 3720 -702 -193 61 O ATOM 618 CB CYS A 127 44.137 5.041 61.682 1.00 28.64 C ANISOU 618 CB CYS A 127 3479 4492 2910 -995 10 -47 C ATOM 619 SG CYS A 127 45.857 4.651 62.153 1.00 52.27 S ANISOU 619 SG CYS A 127 6340 7788 5731 -1054 -169 -33 S ATOM 620 N LYS A 128 43.534 2.980 59.193 1.00 20.30 N ANISOU 620 N LYS A 128 2329 3180 2205 -600 -146 183 N ATOM 621 CA LYS A 128 43.901 1.887 58.293 1.00 28.15 C ANISOU 621 CA LYS A 128 3274 4134 3289 -459 -253 276 C ATOM 622 C LYS A 128 43.771 2.309 56.825 1.00 30.06 C ANISOU 622 C LYS A 128 3487 4258 3676 -389 -213 228 C ATOM 623 O LYS A 128 44.702 2.160 56.033 1.00 43.64 O ANISOU 623 O LYS A 128 5147 6000 5434 -329 -273 226 O ATOM 624 CB LYS A 128 43.029 0.653 58.542 1.00 35.96 C ANISOU 624 CB LYS A 128 4320 5043 4301 -405 -274 389 C ATOM 625 CG LYS A 128 42.822 0.301 60.004 1.00 53.90 C ANISOU 625 CG LYS A 128 6655 7398 6427 -478 -277 446 C ATOM 626 CD LYS A 128 44.094 -0.203 60.640 1.00 46.25 C ANISOU 626 CD LYS A 128 5652 6594 5325 -438 -400 524 C ATOM 627 CE LYS A 128 44.015 -1.692 60.927 1.00 29.39 C ANISOU 627 CE LYS A 128 3593 4403 3170 -327 -454 691 C ATOM 628 NZ LYS A 128 45.240 -2.168 61.622 1.00 27.98 N ANISOU 628 NZ LYS A 128 3375 4417 2840 -243 -573 796 N ATOM 629 N VAL A 129 42.607 2.855 56.490 1.00 17.96 N ANISOU 629 N VAL A 129 1991 2622 2210 -388 -105 193 N ATOM 630 CA VAL A 129 42.169 3.077 55.115 1.00 25.66 C ANISOU 630 CA VAL A 129 2943 3500 3307 -296 -72 180 C ATOM 631 C VAL A 129 42.985 4.106 54.342 1.00 29.63 C ANISOU 631 C VAL A 129 3441 3987 3832 -293 -29 106 C ATOM 632 O VAL A 129 43.471 3.825 53.247 1.00 36.01 O ANISOU 632 O VAL A 129 4207 4770 4705 -220 -78 117 O ATOM 633 CB VAL A 129 40.689 3.519 55.088 1.00 33.73 C ANISOU 633 CB VAL A 129 3983 4468 4366 -278 37 171 C ATOM 634 CG1 VAL A 129 40.283 3.967 53.690 1.00 16.39 C ANISOU 634 CG1 VAL A 129 1752 2214 2261 -170 74 163 C ATOM 635 CG2 VAL A 129 39.788 2.394 55.584 1.00 17.23 C ANISOU 635 CG2 VAL A 129 1886 2391 2270 -297 5 235 C ATOM 636 N ILE A 130 43.122 5.300 54.905 1.00 27.79 N ANISOU 636 N ILE A 130 3267 3756 3537 -386 84 23 N ATOM 637 CA ILE A 130 43.768 6.403 54.198 1.00 30.78 C ANISOU 637 CA ILE A 130 3682 4085 3930 -410 174 -57 C ATOM 638 C ILE A 130 45.236 6.123 53.813 1.00 29.36 C ANISOU 638 C ILE A 130 3424 4002 3729 -448 78 -81 C ATOM 639 O ILE A 130 45.636 6.414 52.680 1.00 35.10 O ANISOU 639 O ILE A 130 4144 4674 4518 -399 100 -98 O ATOM 640 CB ILE A 130 43.665 7.705 55.024 1.00 25.35 C ANISOU 640 CB ILE A 130 3109 3359 3162 -538 346 -159 C ATOM 641 CG1 ILE A 130 42.205 8.168 55.068 1.00 23.92 C ANISOU 641 CG1 ILE A 130 2999 3062 3026 -443 478 -132 C ATOM 642 CG2 ILE A 130 44.561 8.790 54.448 1.00 19.19 C ANISOU 642 CG2 ILE A 130 2393 2527 2371 -617 455 -258 C ATOM 643 CD1 ILE A 130 41.967 9.393 55.921 1.00 25.11 C ANISOU 643 CD1 ILE A 130 3293 3143 3105 -546 679 -229 C ATOM 644 N PRO A 131 46.042 5.549 54.731 1.00 27.60 N ANISOU 644 N PRO A 131 3133 3944 3410 -522 -27 -75 N ATOM 645 CA PRO A 131 47.387 5.172 54.273 1.00 27.16 C ANISOU 645 CA PRO A 131 2966 4013 3341 -515 -125 -81 C ATOM 646 C PRO A 131 47.348 4.090 53.196 1.00 29.03 C ANISOU 646 C PRO A 131 3153 4185 3691 -337 -215 13 C ATOM 647 O PRO A 131 48.150 4.117 52.255 1.00 34.78 O ANISOU 647 O PRO A 131 3825 4929 4462 -302 -229 -12 O ATOM 648 CB PRO A 131 48.058 4.650 55.546 1.00 19.89 C ANISOU 648 CB PRO A 131 1970 3309 2279 -581 -231 -58 C ATOM 649 CG PRO A 131 47.328 5.330 56.655 1.00 20.46 C ANISOU 649 CG PRO A 131 2141 3368 2263 -714 -137 -111 C ATOM 650 CD PRO A 131 45.907 5.393 56.191 1.00 19.30 C ANISOU 650 CD PRO A 131 2096 3002 2235 -620 -48 -72 C ATOM 651 N TYR A 132 46.418 3.151 53.340 1.00 22.78 N ANISOU 651 N TYR A 132 2393 3323 2941 -248 -259 106 N ATOM 652 CA TYR A 132 46.227 2.102 52.349 1.00 16.54 C ANISOU 652 CA TYR A 132 1587 2448 2248 -112 -317 176 C ATOM 653 C TYR A 132 45.925 2.702 50.981 1.00 21.49 C ANISOU 653 C TYR A 132 2230 2972 2963 -74 -249 130 C ATOM 654 O TYR A 132 46.550 2.340 49.985 1.00 23.34 O ANISOU 654 O TYR A 132 2425 3196 3247 -7 -282 130 O ATOM 655 CB TYR A 132 45.103 1.156 52.774 1.00 16.44 C ANISOU 655 CB TYR A 132 1630 2363 2252 -80 -334 255 C ATOM 656 CG TYR A 132 44.778 0.099 51.743 1.00 16.01 C ANISOU 656 CG TYR A 132 1587 2208 2287 14 -365 299 C ATOM 657 CD1 TYR A 132 45.598 -1.005 51.574 1.00 21.79 C ANISOU 657 CD1 TYR A 132 2313 2938 3029 103 -434 359 C ATOM 658 CD2 TYR A 132 43.649 0.206 50.941 1.00 20.44 C ANISOU 658 CD2 TYR A 132 2165 2689 2911 16 -315 277 C ATOM 659 CE1 TYR A 132 45.308 -1.974 50.634 1.00 23.07 C ANISOU 659 CE1 TYR A 132 2514 2984 3265 168 -434 379 C ATOM 660 CE2 TYR A 132 43.350 -0.758 49.998 1.00 17.26 C ANISOU 660 CE2 TYR A 132 1774 2216 2568 62 -337 293 C ATOM 661 CZ TYR A 132 44.184 -1.845 49.848 1.00 18.38 C ANISOU 661 CZ TYR A 132 1939 2320 2723 126 -387 336 C ATOM 662 OH TYR A 132 43.895 -2.808 48.913 1.00 24.91 O ANISOU 662 OH TYR A 132 2808 3053 3603 151 -382 333 O ATOM 663 N LEU A 133 44.972 3.628 50.941 1.00 27.40 N ANISOU 663 N LEU A 133 3039 3651 3720 -102 -146 99 N ATOM 664 CA LEU A 133 44.615 4.305 49.698 1.00 23.96 C ANISOU 664 CA LEU A 133 2629 3131 3342 -41 -73 79 C ATOM 665 C LEU A 133 45.806 5.065 49.127 1.00 24.31 C ANISOU 665 C LEU A 133 2674 3185 3376 -81 -29 13 C ATOM 666 O LEU A 133 46.001 5.109 47.911 1.00 26.44 O ANISOU 666 O LEU A 133 2941 3413 3692 -16 -20 13 O ATOM 667 CB LEU A 133 43.439 5.256 49.922 1.00 22.86 C ANISOU 667 CB LEU A 133 2557 2932 3198 -31 47 74 C ATOM 668 CG LEU A 133 42.092 4.582 50.187 1.00 26.67 C ANISOU 668 CG LEU A 133 3011 3425 3697 14 21 132 C ATOM 669 CD1 LEU A 133 41.000 5.616 50.436 1.00 19.24 C ANISOU 669 CD1 LEU A 133 2115 2452 2745 52 155 130 C ATOM 670 CD2 LEU A 133 41.724 3.677 49.021 1.00 28.25 C ANISOU 670 CD2 LEU A 133 3153 3630 3952 92 -56 170 C ATOM 671 N GLN A 134 46.599 5.661 50.013 1.00 20.45 N ANISOU 671 N GLN A 134 2189 2770 2812 -210 5 -53 N ATOM 672 CA GLN A 134 47.816 6.358 49.605 1.00 22.43 C ANISOU 672 CA GLN A 134 2424 3063 3034 -298 56 -138 C ATOM 673 C GLN A 134 48.758 5.422 48.847 1.00 21.27 C ANISOU 673 C GLN A 134 2161 2997 2924 -226 -55 -114 C ATOM 674 O GLN A 134 49.105 5.673 47.685 1.00 23.12 O ANISOU 674 O GLN A 134 2403 3181 3201 -192 -13 -134 O ATOM 675 CB GLN A 134 48.527 6.950 50.826 1.00 23.30 C ANISOU 675 CB GLN A 134 2525 3299 3031 -484 88 -226 C ATOM 676 CG GLN A 134 49.884 7.560 50.523 1.00 38.78 C ANISOU 676 CG GLN A 134 4434 5361 4940 -622 133 -334 C ATOM 677 CD GLN A 134 49.783 8.846 49.727 1.00 51.36 C ANISOU 677 CD GLN A 134 6178 6781 6554 -684 329 -406 C ATOM 678 OE1 GLN A 134 48.931 9.693 49.997 1.00 51.67 O ANISOU 678 OE1 GLN A 134 6378 6667 6589 -703 471 -420 O ATOM 679 NE2 GLN A 134 50.655 8.999 48.736 1.00 59.07 N ANISOU 679 NE2 GLN A 134 7117 7775 7551 -702 355 -444 N ATOM 680 N THR A 135 49.152 4.334 49.506 1.00 27.55 N ANISOU 680 N THR A 135 2861 3912 3695 -187 -184 -61 N ATOM 681 CA THR A 135 50.086 3.376 48.919 1.00 29.14 C ANISOU 681 CA THR A 135 2955 4190 3926 -88 -275 -28 C ATOM 682 C THR A 135 49.542 2.735 47.644 1.00 31.03 C ANISOU 682 C THR A 135 3237 4285 4268 42 -279 15 C ATOM 683 O THR A 135 50.280 2.545 46.678 1.00 38.03 O ANISOU 683 O THR A 135 4076 5183 5189 91 -278 -6 O ATOM 684 CB THR A 135 50.446 2.259 49.913 1.00 30.00 C ANISOU 684 CB THR A 135 2988 4424 3986 -22 -397 55 C ATOM 685 OG1 THR A 135 49.249 1.624 50.377 1.00 33.34 O ANISOU 685 OG1 THR A 135 3505 4732 4431 26 -416 134 O ATOM 686 CG2 THR A 135 51.201 2.825 51.095 1.00 28.85 C ANISOU 686 CG2 THR A 135 2762 4494 3708 -155 -416 6 C ATOM 687 N VAL A 136 48.256 2.399 47.649 1.00 28.00 N ANISOU 687 N VAL A 136 2932 3787 3919 83 -279 66 N ATOM 688 CA VAL A 136 47.608 1.820 46.478 1.00 26.56 C ANISOU 688 CA VAL A 136 2784 3500 3806 170 -281 90 C ATOM 689 C VAL A 136 47.672 2.786 45.300 1.00 27.45 C ANISOU 689 C VAL A 136 2925 3572 3934 167 -200 40 C ATOM 690 O VAL A 136 47.980 2.390 44.176 1.00 31.15 O ANISOU 690 O VAL A 136 3383 4017 4435 224 -207 32 O ATOM 691 CB VAL A 136 46.136 1.453 46.767 1.00 31.34 C ANISOU 691 CB VAL A 136 3444 4041 4423 175 -285 134 C ATOM 692 CG1 VAL A 136 45.366 1.231 45.471 1.00 20.85 C ANISOU 692 CG1 VAL A 136 2134 2654 3133 223 -273 131 C ATOM 693 CG2 VAL A 136 46.064 0.220 47.657 1.00 35.52 C ANISOU 693 CG2 VAL A 136 3980 4573 4944 189 -353 195 C ATOM 694 N SER A 137 47.390 4.058 45.571 1.00 18.50 N ANISOU 694 N SER A 137 1845 2417 2766 102 -106 10 N ATOM 695 CA SER A 137 47.474 5.097 44.554 1.00 24.25 C ANISOU 695 CA SER A 137 2637 3084 3493 106 0 -21 C ATOM 696 C SER A 137 48.887 5.182 43.982 1.00 29.18 C ANISOU 696 C SER A 137 3215 3760 4113 62 15 -81 C ATOM 697 O SER A 137 49.071 5.224 42.762 1.00 40.79 O ANISOU 697 O SER A 137 4704 5194 5601 111 44 -85 O ATOM 698 CB SER A 137 47.053 6.450 45.131 1.00 35.87 C ANISOU 698 CB SER A 137 4211 4495 4924 44 133 -44 C ATOM 699 OG SER A 137 46.999 7.442 44.121 1.00 50.71 O ANISOU 699 OG SER A 137 6190 6281 6796 77 257 -47 O ATOM 700 N VAL A 138 49.880 5.194 44.868 1.00 15.62 N ANISOU 700 N VAL A 138 1421 2156 2357 -34 -6 -129 N ATOM 701 CA VAL A 138 51.280 5.223 44.445 1.00 24.48 C ANISOU 701 CA VAL A 138 2451 3384 3465 -84 3 -194 C ATOM 702 C VAL A 138 51.626 4.039 43.532 1.00 35.52 C ANISOU 702 C VAL A 138 3780 4795 4922 52 -75 -157 C ATOM 703 O VAL A 138 52.205 4.218 42.455 1.00 27.12 O ANISOU 703 O VAL A 138 2710 3723 3871 58 -22 -195 O ATOM 704 CB VAL A 138 52.226 5.222 45.661 1.00 17.39 C ANISOU 704 CB VAL A 138 1433 2677 2496 -194 -41 -241 C ATOM 705 CG1 VAL A 138 53.671 5.071 45.212 1.00 25.74 C ANISOU 705 CG1 VAL A 138 2344 3901 3536 -222 -50 -300 C ATOM 706 CG2 VAL A 138 52.042 6.496 46.473 1.00 17.98 C ANISOU 706 CG2 VAL A 138 1596 2737 2497 -374 70 -315 C ATOM 707 N SER A 139 51.253 2.836 43.966 1.00 32.41 N ANISOU 707 N SER A 139 3355 4403 4556 154 -181 -86 N ATOM 708 CA SER A 139 51.491 1.615 43.198 1.00 25.46 C ANISOU 708 CA SER A 139 2447 3497 3730 283 -231 -54 C ATOM 709 C SER A 139 50.838 1.666 41.817 1.00 26.22 C ANISOU 709 C SER A 139 2632 3473 3859 316 -184 -65 C ATOM 710 O SER A 139 51.466 1.329 40.809 1.00 17.42 O ANISOU 710 O SER A 139 1497 2358 2765 362 -161 -95 O ATOM 711 CB SER A 139 50.978 0.396 43.969 1.00 31.18 C ANISOU 711 CB SER A 139 3185 4190 4470 367 -316 28 C ATOM 712 OG SER A 139 51.074 -0.785 43.189 1.00 35.55 O ANISOU 712 OG SER A 139 3763 4669 5077 481 -328 50 O ATOM 713 N VAL A 140 49.576 2.084 41.780 1.00 26.52 N ANISOU 713 N VAL A 140 2756 3433 3888 298 -168 -38 N ATOM 714 CA VAL A 140 48.857 2.224 40.521 1.00 24.65 C ANISOU 714 CA VAL A 140 2584 3132 3650 333 -135 -37 C ATOM 715 C VAL A 140 49.599 3.180 39.597 1.00 22.77 C ANISOU 715 C VAL A 140 2368 2897 3387 308 -42 -81 C ATOM 716 O VAL A 140 49.794 2.885 38.419 1.00 28.89 O ANISOU 716 O VAL A 140 3157 3659 4160 346 -27 -98 O ATOM 717 CB VAL A 140 47.418 2.733 40.732 1.00 23.76 C ANISOU 717 CB VAL A 140 2526 2989 3513 335 -126 8 C ATOM 718 CG1 VAL A 140 46.794 3.133 39.402 1.00 14.02 C ANISOU 718 CG1 VAL A 140 1339 1745 2245 385 -90 21 C ATOM 719 CG2 VAL A 140 46.575 1.674 41.420 1.00 20.42 C ANISOU 719 CG2 VAL A 140 2086 2564 3109 339 -204 41 C ATOM 720 N SER A 141 50.027 4.315 40.145 1.00 19.29 N ANISOU 720 N SER A 141 1945 2467 2917 224 35 -108 N ATOM 721 CA SER A 141 50.753 5.315 39.364 1.00 19.52 C ANISOU 721 CA SER A 141 2023 2479 2914 167 156 -155 C ATOM 722 C SER A 141 52.017 4.728 38.746 1.00 26.12 C ANISOU 722 C SER A 141 2764 3395 3767 162 148 -213 C ATOM 723 O SER A 141 52.227 4.798 37.530 1.00 40.44 O ANISOU 723 O SER A 141 4617 5179 5568 188 202 -226 O ATOM 724 CB SER A 141 51.110 6.520 40.237 1.00 21.04 C ANISOU 724 CB SER A 141 2260 2668 3068 33 259 -201 C ATOM 725 OG SER A 141 49.944 7.195 40.679 1.00 28.02 O ANISOU 725 OG SER A 141 3256 3456 3935 58 305 -149 O ATOM 726 N VAL A 142 52.847 4.137 39.595 1.00 26.15 N ANISOU 726 N VAL A 142 2635 3514 3786 144 84 -238 N ATOM 727 CA VAL A 142 54.108 3.551 39.159 1.00 27.85 C ANISOU 727 CA VAL A 142 2726 3839 4017 168 80 -286 C ATOM 728 C VAL A 142 53.935 2.471 38.090 1.00 30.09 C ANISOU 728 C VAL A 142 3031 4059 4343 300 51 -265 C ATOM 729 O VAL A 142 54.631 2.474 37.072 1.00 26.11 O ANISOU 729 O VAL A 142 2510 3573 3836 306 116 -313 O ATOM 730 CB VAL A 142 54.858 2.942 40.346 1.00 31.33 C ANISOU 730 CB VAL A 142 3008 4442 4455 183 -7 -281 C ATOM 731 CG1 VAL A 142 56.129 2.304 39.874 1.00 32.30 C ANISOU 731 CG1 VAL A 142 2982 4699 4592 252 -6 -316 C ATOM 732 CG2 VAL A 142 55.152 4.008 41.376 1.00 47.41 C ANISOU 732 CG2 VAL A 142 5012 6577 6423 14 28 -331 C ATOM 733 N LEU A 143 53.011 1.545 38.327 1.00 28.80 N ANISOU 733 N LEU A 143 2911 3820 4210 385 -30 -205 N ATOM 734 CA LEU A 143 52.785 0.449 37.392 1.00 23.03 C ANISOU 734 CA LEU A 143 2223 3017 3509 478 -42 -204 C ATOM 735 C LEU A 143 52.162 0.948 36.089 1.00 38.20 C ANISOU 735 C LEU A 143 4246 4880 5389 450 12 -224 C ATOM 736 O LEU A 143 52.372 0.359 35.027 1.00 23.00 O ANISOU 736 O LEU A 143 2346 2931 3461 486 40 -261 O ATOM 737 CB LEU A 143 51.899 -0.620 38.028 1.00 25.75 C ANISOU 737 CB LEU A 143 2610 3289 3882 531 -120 -149 C ATOM 738 CG LEU A 143 52.487 -1.288 39.274 1.00 34.17 C ANISOU 738 CG LEU A 143 3601 4408 4975 596 -174 -103 C ATOM 739 CD1 LEU A 143 51.523 -2.324 39.835 1.00 29.86 C ANISOU 739 CD1 LEU A 143 3140 3755 4449 631 -222 -45 C ATOM 740 CD2 LEU A 143 53.843 -1.913 38.966 1.00 17.94 C ANISOU 740 CD2 LEU A 143 1452 2420 2945 704 -147 -122 C ATOM 741 N THR A 144 51.398 2.034 36.174 1.00 24.92 N ANISOU 741 N THR A 144 2627 3179 3663 397 35 -193 N ATOM 742 CA THR A 144 50.817 2.648 34.987 1.00 22.56 C ANISOU 742 CA THR A 144 2422 2850 3301 399 88 -182 C ATOM 743 C THR A 144 51.919 3.256 34.130 1.00 22.25 C ANISOU 743 C THR A 144 2392 2827 3234 362 195 -234 C ATOM 744 O THR A 144 51.953 3.055 32.915 1.00 20.95 O ANISOU 744 O THR A 144 2273 2659 3028 386 228 -253 O ATOM 745 CB THR A 144 49.783 3.731 35.346 1.00 23.87 C ANISOU 745 CB THR A 144 2658 2988 3423 395 109 -115 C ATOM 746 OG1 THR A 144 48.679 3.127 36.030 1.00 17.39 O ANISOU 746 OG1 THR A 144 1815 2173 2619 423 16 -74 O ATOM 747 CG2 THR A 144 49.267 4.407 34.091 1.00 21.43 C ANISOU 747 CG2 THR A 144 2445 2670 3029 437 168 -78 C ATOM 748 N LEU A 145 52.824 3.992 34.770 1.00 20.06 N ANISOU 748 N LEU A 145 2072 2583 2966 283 258 -268 N ATOM 749 CA LEU A 145 53.982 4.541 34.070 1.00 22.03 C ANISOU 749 CA LEU A 145 2311 2869 3189 213 375 -335 C ATOM 750 C LEU A 145 54.821 3.427 33.448 1.00 27.90 C ANISOU 750 C LEU A 145 2958 3677 3968 271 357 -389 C ATOM 751 O LEU A 145 55.317 3.555 32.323 1.00 34.82 O ANISOU 751 O LEU A 145 3866 4555 4809 258 443 -430 O ATOM 752 CB LEU A 145 54.838 5.380 35.020 1.00 18.72 C ANISOU 752 CB LEU A 145 1830 2516 2766 79 439 -387 C ATOM 753 CG LEU A 145 54.209 6.690 35.496 1.00 22.96 C ANISOU 753 CG LEU A 145 2509 2956 3259 -4 524 -359 C ATOM 754 CD1 LEU A 145 55.218 7.529 36.260 1.00 27.29 C ANISOU 754 CD1 LEU A 145 3010 3577 3782 -192 622 -451 C ATOM 755 CD2 LEU A 145 53.651 7.470 34.315 1.00 20.14 C ANISOU 755 CD2 LEU A 145 2338 2476 2840 30 635 -308 C ATOM 756 N SER A 146 54.965 2.330 34.188 1.00 24.92 N ANISOU 756 N SER A 146 2477 3338 3653 348 260 -382 N ATOM 757 CA SER A 146 55.734 1.180 33.724 1.00 23.16 C ANISOU 757 CA SER A 146 2176 3151 3472 443 259 -421 C ATOM 758 C SER A 146 55.101 0.535 32.498 1.00 22.99 C ANISOU 758 C SER A 146 2274 3032 3431 491 273 -431 C ATOM 759 O SER A 146 55.803 0.128 31.573 1.00 19.52 O ANISOU 759 O SER A 146 1824 2606 2988 521 344 -491 O ATOM 760 CB SER A 146 55.872 0.146 34.841 1.00 18.91 C ANISOU 760 CB SER A 146 1546 2643 2995 544 165 -381 C ATOM 761 OG SER A 146 56.638 0.661 35.912 1.00 31.05 O ANISOU 761 OG SER A 146 2943 4328 4526 497 147 -383 O ATOM 762 N CYS A 147 53.775 0.440 32.497 1.00 18.23 N ANISOU 762 N CYS A 147 1771 2353 2802 488 209 -383 N ATOM 763 CA CYS A 147 53.052 -0.135 31.369 1.00 23.71 C ANISOU 763 CA CYS A 147 2565 2997 3446 499 211 -404 C ATOM 764 C CYS A 147 53.096 0.786 30.160 1.00 27.12 C ANISOU 764 C CYS A 147 3067 3455 3783 453 290 -417 C ATOM 765 O CYS A 147 53.127 0.324 29.021 1.00 33.11 O ANISOU 765 O CYS A 147 3880 4213 4488 455 329 -467 O ATOM 766 CB CYS A 147 51.603 -0.428 31.752 1.00 31.95 C ANISOU 766 CB CYS A 147 3661 4008 4470 488 118 -354 C ATOM 767 SG CYS A 147 51.427 -1.834 32.858 1.00 52.95 S ANISOU 767 SG CYS A 147 6301 6597 7221 533 52 -346 S ATOM 768 N ILE A 148 53.090 2.090 30.415 1.00 22.21 N ANISOU 768 N ILE A 148 2464 2846 3127 408 330 -371 N ATOM 769 CA ILE A 148 53.254 3.068 29.350 1.00 22.17 C ANISOU 769 CA ILE A 148 2553 2844 3027 373 435 -364 C ATOM 770 C ILE A 148 54.604 2.880 28.676 1.00 28.40 C ANISOU 770 C ILE A 148 3298 3668 3825 341 539 -455 C ATOM 771 O ILE A 148 54.685 2.721 27.454 1.00 42.75 O ANISOU 771 O ILE A 148 5182 5492 5568 343 594 -485 O ATOM 772 CB ILE A 148 53.143 4.509 29.875 1.00 20.35 C ANISOU 772 CB ILE A 148 2383 2579 2771 327 502 -304 C ATOM 773 CG1 ILE A 148 51.700 4.812 30.274 1.00 23.57 C ANISOU 773 CG1 ILE A 148 2848 2961 3146 388 426 -203 C ATOM 774 CG2 ILE A 148 53.613 5.494 28.818 1.00 19.74 C ANISOU 774 CG2 ILE A 148 2422 2479 2600 282 652 -302 C ATOM 775 CD1 ILE A 148 51.499 6.172 30.908 1.00 18.26 C ANISOU 775 CD1 ILE A 148 2261 2221 2458 366 511 -142 C ATOM 776 N ALA A 149 55.659 2.887 29.487 1.00 24.75 N ANISOU 776 N ALA A 149 2709 3254 3441 311 564 -500 N ATOM 777 CA ALA A 149 57.020 2.712 28.984 1.00 33.40 C ANISOU 777 CA ALA A 149 3716 4426 4551 287 666 -590 C ATOM 778 C ALA A 149 57.174 1.387 28.241 1.00 34.89 C ANISOU 778 C ALA A 149 3892 4604 4760 385 657 -640 C ATOM 779 O ALA A 149 57.827 1.319 27.201 1.00 29.63 O ANISOU 779 O ALA A 149 3240 3963 4054 372 762 -705 O ATOM 780 CB ALA A 149 58.019 2.796 30.128 1.00 30.80 C ANISOU 780 CB ALA A 149 3205 4209 4290 255 661 -624 C ATOM 781 N LEU A 150 56.563 0.340 28.783 1.00 38.61 N ANISOU 781 N LEU A 150 4357 5025 5288 474 551 -615 N ATOM 782 CA LEU A 150 56.617 -0.986 28.183 1.00 25.78 C ANISOU 782 CA LEU A 150 2762 3347 3685 558 565 -669 C ATOM 783 C LEU A 150 55.949 -0.976 26.814 1.00 30.15 C ANISOU 783 C LEU A 150 3464 3866 4126 505 602 -702 C ATOM 784 O LEU A 150 56.469 -1.535 25.848 1.00 33.18 O ANISOU 784 O LEU A 150 3879 4242 4484 519 693 -784 O ATOM 785 CB LEU A 150 55.939 -2.011 29.092 1.00 27.66 C ANISOU 785 CB LEU A 150 3011 3508 3991 632 464 -629 C ATOM 786 CG LEU A 150 56.390 -3.462 28.956 1.00 35.25 C ANISOU 786 CG LEU A 150 3985 4393 5016 750 512 -677 C ATOM 787 CD1 LEU A 150 57.809 -3.612 29.478 1.00 39.64 C ANISOU 787 CD1 LEU A 150 4371 5043 5647 868 561 -678 C ATOM 788 CD2 LEU A 150 55.436 -4.384 29.700 1.00 43.01 C ANISOU 788 CD2 LEU A 150 5048 5259 6037 780 433 -634 C ATOM 789 N ASP A 151 54.790 -0.331 26.746 1.00 25.04 N ANISOU 789 N ASP A 151 2900 3215 3400 451 533 -634 N ATOM 790 CA ASP A 151 54.024 -0.236 25.512 1.00 30.91 C ANISOU 790 CA ASP A 151 3763 3978 4002 408 541 -643 C ATOM 791 C ASP A 151 54.811 0.505 24.437 1.00 29.56 C ANISOU 791 C ASP A 151 3636 3849 3747 370 669 -671 C ATOM 792 O ASP A 151 54.913 0.046 23.294 1.00 34.95 O ANISOU 792 O ASP A 151 4386 4549 4344 350 728 -741 O ATOM 793 CB ASP A 151 52.688 0.464 25.773 1.00 42.49 C ANISOU 793 CB ASP A 151 5272 5476 5396 396 442 -539 C ATOM 794 CG ASP A 151 51.859 0.629 24.516 1.00 58.03 C ANISOU 794 CG ASP A 151 7335 7525 7190 370 431 -527 C ATOM 795 OD1 ASP A 151 51.163 -0.336 24.145 1.00 59.95 O ANISOU 795 OD1 ASP A 151 7596 7800 7384 336 373 -584 O ATOM 796 OD2 ASP A 151 51.895 1.721 23.907 1.00 57.55 O ANISOU 796 OD2 ASP A 151 7339 7502 7027 377 488 -461 O ATOM 797 N ARG A 152 55.371 1.652 24.812 1.00 28.39 N ANISOU 797 N ARG A 152 3462 3713 3613 341 729 -627 N ATOM 798 CA ARG A 152 56.162 2.446 23.879 1.00 31.23 C ANISOU 798 CA ARG A 152 3877 4100 3891 281 877 -652 C ATOM 799 C ARG A 152 57.390 1.680 23.415 1.00 24.43 C ANISOU 799 C ARG A 152 2933 3270 3078 283 976 -775 C ATOM 800 O ARG A 152 57.762 1.742 22.246 1.00 33.88 O ANISOU 800 O ARG A 152 4201 4490 4181 248 1083 -825 O ATOM 801 CB ARG A 152 56.578 3.779 24.511 1.00 29.02 C ANISOU 801 CB ARG A 152 3595 3806 3625 214 949 -602 C ATOM 802 CG ARG A 152 55.434 4.764 24.739 1.00 22.80 C ANISOU 802 CG ARG A 152 2933 2964 2765 230 909 -471 C ATOM 803 CD ARG A 152 54.764 5.176 23.432 1.00 23.64 C ANISOU 803 CD ARG A 152 3205 3079 2699 261 945 -403 C ATOM 804 NE ARG A 152 53.755 4.215 22.997 1.00 36.08 N ANISOU 804 NE ARG A 152 4772 4718 4218 327 808 -397 N ATOM 805 CZ ARG A 152 53.462 3.963 21.726 1.00 42.61 C ANISOU 805 CZ ARG A 152 5678 5614 4895 331 818 -406 C ATOM 806 NH1 ARG A 152 54.101 4.604 20.756 1.00 54.03 N ANISOU 806 NH1 ARG A 152 7229 7061 6237 295 961 -404 N ATOM 807 NH2 ARG A 152 52.530 3.068 21.425 1.00 39.15 N ANISOU 807 NH2 ARG A 152 5220 5257 4399 351 694 -425 N ATOM 808 N TRP A 153 58.014 0.949 24.332 1.00 27.53 N ANISOU 808 N TRP A 153 3175 3676 3609 342 946 -815 N ATOM 809 CA TRP A 153 59.207 0.180 24.001 1.00 32.13 C ANISOU 809 CA TRP A 153 3655 4304 4248 392 1046 -917 C ATOM 810 C TRP A 153 58.874 -0.941 23.024 1.00 30.02 C ANISOU 810 C TRP A 153 3493 3973 3939 441 1071 -985 C ATOM 811 O TRP A 153 59.639 -1.225 22.103 1.00 27.55 O ANISOU 811 O TRP A 153 3186 3686 3595 441 1202 -1075 O ATOM 812 CB TRP A 153 59.846 -0.390 25.267 1.00 38.70 C ANISOU 812 CB TRP A 153 4300 5182 5221 488 995 -914 C ATOM 813 CG TRP A 153 61.120 -1.129 25.009 1.00 45.66 C ANISOU 813 CG TRP A 153 5046 6141 6162 582 1103 -1000 C ATOM 814 CD1 TRP A 153 62.357 -0.586 24.813 1.00 42.21 C ANISOU 814 CD1 TRP A 153 4461 5856 5721 534 1222 -1060 C ATOM 815 CD2 TRP A 153 61.287 -2.549 24.920 1.00 48.15 C ANISOU 815 CD2 TRP A 153 5362 6389 6545 748 1122 -1035 C ATOM 816 NE1 TRP A 153 63.282 -1.579 24.607 1.00 46.08 N ANISOU 816 NE1 TRP A 153 4832 6403 6274 683 1302 -1124 N ATOM 817 CE2 TRP A 153 62.651 -2.794 24.667 1.00 48.66 C ANISOU 817 CE2 TRP A 153 5264 6577 6648 828 1251 -1105 C ATOM 818 CE3 TRP A 153 60.415 -3.636 25.028 1.00 55.80 C ANISOU 818 CE3 TRP A 153 6463 7198 7541 829 1063 -1020 C ATOM 819 CZ2 TRP A 153 63.164 -4.081 24.522 1.00 55.70 C ANISOU 819 CZ2 TRP A 153 6132 7422 7610 1025 1326 -1144 C ATOM 820 CZ3 TRP A 153 60.926 -4.914 24.883 1.00 62.47 C ANISOU 820 CZ3 TRP A 153 7313 7971 8454 993 1149 -1069 C ATOM 821 CH2 TRP A 153 62.287 -5.125 24.633 1.00 57.91 C ANISOU 821 CH2 TRP A 153 6583 7503 7919 1109 1281 -1122 C ATOM 822 N TYR A 154 57.722 -1.569 23.231 1.00 28.69 N ANISOU 822 N TYR A 154 3411 3728 3763 461 957 -954 N ATOM 823 CA TYR A 154 57.276 -2.655 22.370 1.00 34.46 C ANISOU 823 CA TYR A 154 4262 4395 4438 463 983 -1037 C ATOM 824 C TYR A 154 56.891 -2.148 20.985 1.00 44.30 C ANISOU 824 C TYR A 154 5636 5697 5499 360 1030 -1064 C ATOM 825 O TYR A 154 57.119 -2.826 19.988 1.00 41.85 O ANISOU 825 O TYR A 154 5404 5373 5123 339 1126 -1172 O ATOM 826 CB TYR A 154 56.095 -3.392 23.007 1.00 37.23 C ANISOU 826 CB TYR A 154 4665 4668 4812 466 855 -1008 C ATOM 827 CG TYR A 154 56.492 -4.534 23.919 1.00 40.00 C ANISOU 827 CG TYR A 154 4971 4913 5314 584 864 -1025 C ATOM 828 CD1 TYR A 154 57.430 -5.476 23.517 1.00 49.80 C ANISOU 828 CD1 TYR A 154 6223 6089 6610 679 1004 -1116 C ATOM 829 CD2 TYR A 154 55.928 -4.669 25.182 1.00 40.91 C ANISOU 829 CD2 TYR A 154 5046 4990 5509 618 746 -939 C ATOM 830 CE1 TYR A 154 57.795 -6.523 24.346 1.00 47.27 C ANISOU 830 CE1 TYR A 154 5883 5660 6418 829 1028 -1105 C ATOM 831 CE2 TYR A 154 56.287 -5.712 26.018 1.00 56.25 C ANISOU 831 CE2 TYR A 154 6970 6830 7573 745 762 -931 C ATOM 832 CZ TYR A 154 57.222 -6.636 25.595 1.00 61.93 C ANISOU 832 CZ TYR A 154 7709 7479 8343 861 904 -1006 C ATOM 833 OH TYR A 154 57.583 -7.678 26.423 1.00 71.82 O ANISOU 833 OH TYR A 154 8963 8619 9708 1028 936 -973 O ATOM 834 N ALA A 155 56.312 -0.953 20.922 1.00 48.66 N ANISOU 834 N ALA A 155 6221 6310 5957 307 975 -961 N ATOM 835 CA ALA A 155 55.834 -0.418 19.648 1.00 46.99 C ANISOU 835 CA ALA A 155 6139 6172 5545 238 1005 -950 C ATOM 836 C ALA A 155 56.945 0.243 18.829 1.00 51.98 C ANISOU 836 C ALA A 155 6793 6834 6121 201 1174 -984 C ATOM 837 O ALA A 155 56.900 0.245 17.597 1.00 48.24 O ANISOU 837 O ALA A 155 6430 6411 5487 151 1244 -1024 O ATOM 838 CB ALA A 155 54.702 0.570 19.887 1.00 38.77 C ANISOU 838 CB ALA A 155 5139 5180 4413 238 891 -802 C ATOM 839 N ILE A 156 57.938 0.797 19.517 1.00 49.79 N ANISOU 839 N ILE A 156 6410 6547 5963 208 1244 -975 N ATOM 840 CA ILE A 156 58.993 1.574 18.870 1.00 35.15 C ANISOU 840 CA ILE A 156 4565 4733 4058 140 1418 -1006 C ATOM 841 C ILE A 156 60.243 0.748 18.578 1.00 46.22 C ANISOU 841 C ILE A 156 5859 6164 5539 162 1548 -1149 C ATOM 842 O ILE A 156 60.768 0.772 17.462 1.00 47.54 O ANISOU 842 O ILE A 156 6090 6366 5606 112 1689 -1221 O ATOM 843 CB ILE A 156 59.391 2.786 19.737 1.00 31.68 C ANISOU 843 CB ILE A 156 4071 4291 3675 88 1448 -934 C ATOM 844 CG1 ILE A 156 58.252 3.807 19.769 1.00 31.90 C ANISOU 844 CG1 ILE A 156 4252 4274 3596 81 1383 -785 C ATOM 845 CG2 ILE A 156 60.678 3.418 19.227 1.00 32.57 C ANISOU 845 CG2 ILE A 156 4157 4456 3763 -15 1649 -1004 C ATOM 846 CD1 ILE A 156 58.397 4.849 20.852 1.00 35.75 C ANISOU 846 CD1 ILE A 156 4711 4718 4156 37 1398 -719 C ATOM 847 N CYS A 157 60.719 0.022 19.583 1.00 62.51 N ANISOU 847 N CYS A 157 7288 9814 6650 318 365 -1966 N ATOM 848 CA CYS A 157 61.949 -0.747 19.441 1.00 71.06 C ANISOU 848 CA CYS A 157 8259 10945 7796 441 668 -1972 C ATOM 849 C CYS A 157 61.710 -2.098 18.771 1.00 79.76 C ANISOU 849 C CYS A 157 9499 11607 9201 445 859 -1893 C ATOM 850 O CYS A 157 62.641 -2.708 18.247 1.00 79.56 O ANISOU 850 O CYS A 157 9492 11477 9261 442 1116 -1988 O ATOM 851 CB CYS A 157 62.609 -0.946 20.806 1.00 65.31 C ANISOU 851 CB CYS A 157 7045 10707 7062 797 775 -1739 C ATOM 852 SG CYS A 157 63.130 0.592 21.601 1.00 52.62 S ANISOU 852 SG CYS A 157 5233 9669 5092 780 619 -1892 S ATOM 853 N HIS A 158 60.466 -2.567 18.792 1.00 81.86 N ANISOU 853 N HIS A 158 9849 11612 9643 447 746 -1736 N ATOM 854 CA HIS A 158 60.126 -3.841 18.161 1.00 81.92 C ANISOU 854 CA HIS A 158 9987 11182 9959 432 925 -1679 C ATOM 855 C HIS A 158 58.741 -3.821 17.514 1.00 82.23 C ANISOU 855 C HIS A 158 10346 10859 10040 193 721 -1707 C ATOM 856 O HIS A 158 57.824 -4.488 17.990 1.00 88.59 O ANISOU 856 O HIS A 158 11059 11538 11062 345 683 -1460 O ATOM 857 CB HIS A 158 60.196 -4.975 19.186 1.00 87.68 C ANISOU 857 CB HIS A 158 10323 11996 10994 827 1103 -1314 C ATOM 858 CG HIS A 158 61.486 -5.022 19.942 1.00 98.04 C ANISOU 858 CG HIS A 158 11267 13709 12274 1081 1284 -1215 C ATOM 859 ND1 HIS A 158 62.633 -5.582 19.425 1.00111.73 N ANISOU 859 ND1 HIS A 158 12981 15347 14125 1092 1579 -1327 N ATOM 860 CD2 HIS A 158 61.812 -4.566 21.175 1.00100.63 C ANISOU 860 CD2 HIS A 158 11219 14556 12459 1317 1215 -1020 C ATOM 861 CE1 HIS A 158 63.610 -5.475 20.308 1.00114.51 C ANISOU 861 CE1 HIS A 158 12960 16133 14414 1336 1674 -1178 C ATOM 862 NE2 HIS A 158 63.138 -4.862 21.378 1.00110.26 N ANISOU 862 NE2 HIS A 158 12200 15989 13704 1467 1456 -992 N ATOM 863 N PRO A 159 58.589 -3.067 16.414 1.00 80.34 N ANISOU 863 N PRO A 159 10472 10460 9595 -193 588 -1988 N ATOM 864 CA PRO A 159 57.284 -2.928 15.757 1.00 80.06 C ANISOU 864 CA PRO A 159 10736 10117 9566 -456 368 -2004 C ATOM 865 C PRO A 159 56.856 -4.189 15.005 1.00 82.32 C ANISOU 865 C PRO A 159 11189 9982 10107 -550 545 -2011 C ATOM 866 O PRO A 159 57.080 -5.306 15.475 1.00 77.59 O ANISOU 866 O PRO A 159 10375 9311 9793 -280 781 -1852 O ATOM 867 CB PRO A 159 57.503 -1.765 14.775 1.00 80.54 C ANISOU 867 CB PRO A 159 11090 10184 9325 -847 208 -2286 C ATOM 868 CG PRO A 159 58.822 -1.144 15.161 1.00 75.21 C ANISOU 868 CG PRO A 159 10234 9867 8475 -740 304 -2400 C ATOM 869 CD PRO A 159 59.621 -2.258 15.745 1.00 77.67 C ANISOU 869 CD PRO A 159 10268 10249 8995 -411 619 -2282 C ATOM 870 N SER A 164 49.740 -3.851 20.207 1.00 69.13 N ANISOU 870 N SER A 164 8701 8603 8961 399 -702 -455 N ATOM 871 CA SER A 164 49.134 -3.369 21.444 1.00 70.00 C ANISOU 871 CA SER A 164 8519 9033 9044 604 -871 -277 C ATOM 872 C SER A 164 47.728 -2.830 21.207 1.00 60.00 C ANISOU 872 C SER A 164 7443 7560 7795 422 -1156 -264 C ATOM 873 O SER A 164 47.551 -1.763 20.621 1.00 60.20 O ANISOU 873 O SER A 164 7670 7522 7680 161 -1335 -461 O ATOM 874 CB SER A 164 50.004 -2.288 22.082 1.00 75.87 C ANISOU 874 CB SER A 164 9044 10234 9550 663 -894 -414 C ATOM 875 OG SER A 164 51.171 -2.842 22.667 1.00 82.44 O ANISOU 875 OG SER A 164 9589 11356 10380 907 -649 -332 O ATOM 876 N THR A 165 46.732 -3.573 21.675 1.00 55.54 N ANISOU 876 N THR A 165 6795 6887 7421 563 -1199 -11 N ATOM 877 CA THR A 165 45.339 -3.198 21.479 1.00 58.32 C ANISOU 877 CA THR A 165 7311 7025 7823 410 -1459 36 C ATOM 878 C THR A 165 44.748 -2.557 22.731 1.00 65.82 C ANISOU 878 C THR A 165 7950 8316 8742 592 -1622 151 C ATOM 879 O THR A 165 45.353 -2.593 23.803 1.00 67.03 O ANISOU 879 O THR A 165 7743 8886 8840 850 -1521 232 O ATOM 880 CB THR A 165 44.486 -4.416 21.092 1.00 53.83 C ANISOU 880 CB THR A 165 6883 6081 7490 407 -1415 220 C ATOM 881 OG1 THR A 165 44.538 -5.387 22.144 1.00 47.92 O ANISOU 881 OG1 THR A 165 5798 5503 6907 758 -1268 498 O ATOM 882 CG2 THR A 165 45.007 -5.041 19.807 1.00 52.70 C ANISOU 882 CG2 THR A 165 7046 5596 7381 185 -1239 57 C ATOM 883 N ALA A 166 43.562 -1.973 22.586 1.00 60.35 N ANISOU 883 N ALA A 166 7382 7460 8087 444 -1870 157 N ATOM 884 CA ALA A 166 42.876 -1.336 23.704 1.00 46.67 C ANISOU 884 CA ALA A 166 5368 6012 6351 582 -2027 231 C ATOM 885 C ALA A 166 42.367 -2.376 24.700 1.00 48.51 C ANISOU 885 C ALA A 166 5330 6382 6722 875 -1962 540 C ATOM 886 O ALA A 166 42.229 -2.090 25.890 1.00 54.61 O ANISOU 886 O ALA A 166 5749 7552 7447 1066 -1995 618 O ATOM 887 CB ALA A 166 41.729 -0.475 23.201 1.00 44.15 C ANISOU 887 CB ALA A 166 5258 5433 6084 336 -2300 165 C ATOM 888 N LYS A 167 42.085 -3.578 24.206 1.00 43.53 N ANISOU 888 N LYS A 167 4850 5427 6262 894 -1865 709 N ATOM 889 CA LYS A 167 41.690 -4.691 25.066 1.00 44.41 C ANISOU 889 CA LYS A 167 4705 5630 6540 1172 -1779 1034 C ATOM 890 C LYS A 167 42.846 -5.108 25.959 1.00 47.84 C ANISOU 890 C LYS A 167 4765 6487 6924 1448 -1561 1145 C ATOM 891 O LYS A 167 42.681 -5.301 27.168 1.00 55.04 O ANISOU 891 O LYS A 167 5298 7780 7835 1687 -1561 1365 O ATOM 892 CB LYS A 167 41.218 -5.881 24.230 1.00 48.28 C ANISOU 892 CB LYS A 167 5451 5637 7256 1106 -1696 1156 C ATOM 893 CG LYS A 167 39.760 -5.796 23.801 1.00 63.41 C ANISOU 893 CG LYS A 167 7600 7227 9267 933 -1921 1203 C ATOM 894 CD LYS A 167 38.854 -6.472 24.821 1.00 68.70 C ANISOU 894 CD LYS A 167 8009 7998 10095 1177 -1964 1525 C ATOM 895 CE LYS A 167 37.395 -6.052 24.651 1.00 64.73 C ANISOU 895 CE LYS A 167 7665 7290 9641 1026 -2231 1556 C ATOM 896 NZ LYS A 167 37.173 -4.582 24.879 1.00 55.89 N ANISOU 896 NZ LYS A 167 6510 6368 8357 912 -2441 1368 N ATOM 897 N ARG A 168 44.016 -5.248 25.345 1.00 47.66 N ANISOU 897 N ARG A 168 4840 6413 6855 1399 -1375 1000 N ATOM 898 CA ARG A 168 45.240 -5.569 26.063 1.00 51.97 C ANISOU 898 CA ARG A 168 5048 7351 7348 1632 -1164 1090 C ATOM 899 C ARG A 168 45.512 -4.513 27.125 1.00 52.74 C ANISOU 899 C ARG A 168 4824 8016 7198 1713 -1258 1022 C ATOM 900 O ARG A 168 45.936 -4.826 28.239 1.00 63.52 O ANISOU 900 O ARG A 168 5773 9837 8525 1959 -1167 1233 O ATOM 901 CB ARG A 168 46.419 -5.667 25.092 1.00 60.63 C ANISOU 901 CB ARG A 168 6350 8273 8414 1512 -974 875 C ATOM 902 CG ARG A 168 47.754 -5.939 25.759 1.00 80.66 C ANISOU 902 CG ARG A 168 8544 11205 10898 1738 -754 959 C ATOM 903 CD ARG A 168 48.914 -5.494 24.880 1.00 89.75 C ANISOU 903 CD ARG A 168 9897 12290 11914 1569 -635 648 C ATOM 904 NE ARG A 168 50.164 -5.411 25.631 1.00 91.09 N ANISOU 904 NE ARG A 168 9717 12931 11964 1763 -477 694 N ATOM 905 CZ ARG A 168 51.058 -6.391 25.710 1.00 97.05 C ANISOU 905 CZ ARG A 168 10297 13695 12881 1943 -218 860 C ATOM 906 NH1 ARG A 168 50.846 -7.538 25.077 1.00 93.81 N ANISOU 906 NH1 ARG A 168 10032 12828 12785 1953 -70 968 N ATOM 907 NH2 ARG A 168 52.167 -6.225 26.419 1.00102.18 N ANISOU 907 NH2 ARG A 168 10613 14811 13400 2105 -98 916 N ATOM 908 N ALA A 169 45.248 -3.259 26.772 1.00 36.20 N ANISOU 908 N ALA A 169 5086 4431 4238 933 -1601 -742 N ATOM 909 CA ALA A 169 45.454 -2.144 27.685 1.00 31.06 C ANISOU 909 CA ALA A 169 4297 3833 3673 883 -1544 -611 C ATOM 910 C ALA A 169 44.474 -2.203 28.851 1.00 42.15 C ANISOU 910 C ALA A 169 5499 5191 5325 747 -1555 -707 C ATOM 911 O ALA A 169 44.838 -1.910 29.987 1.00 42.81 O ANISOU 911 O ALA A 169 5478 5288 5499 677 -1425 -611 O ATOM 912 CB ALA A 169 45.324 -0.822 26.947 1.00 28.69 C ANISOU 912 CB ALA A 169 4048 3582 3271 962 -1677 -554 C ATOM 913 N ARG A 170 43.234 -2.587 28.563 1.00 42.40 N ANISOU 913 N ARG A 170 5472 5180 5460 705 -1707 -905 N ATOM 914 CA ARG A 170 42.209 -2.722 29.593 1.00 41.56 C ANISOU 914 CA ARG A 170 5160 5042 5588 561 -1708 -1021 C ATOM 915 C ARG A 170 42.618 -3.801 30.593 1.00 33.25 C ANISOU 915 C ARG A 170 4110 3914 4611 450 -1499 -997 C ATOM 916 O ARG A 170 42.550 -3.603 31.815 1.00 44.02 O ANISOU 916 O ARG A 170 5347 5272 6106 357 -1386 -950 O ATOM 917 CB ARG A 170 40.858 -3.053 28.955 1.00 49.66 C ANISOU 917 CB ARG A 170 6113 6061 6695 530 -1910 -1260 C ATOM 918 CG ARG A 170 39.650 -2.664 29.790 1.00 61.68 C ANISOU 918 CG ARG A 170 7378 7612 8447 421 -1965 -1386 C ATOM 919 CD ARG A 170 38.502 -2.197 28.900 1.00 81.62 C ANISOU 919 CD ARG A 170 9826 10204 10984 492 -2188 -1536 C ATOM 920 NE ARG A 170 38.845 -0.986 28.153 1.00 87.14 N ANISOU 920 NE ARG A 170 10639 10947 11522 678 -2277 -1406 N ATOM 921 CZ ARG A 170 38.685 -0.839 26.840 1.00 80.74 C ANISOU 921 CZ ARG A 170 9968 10154 10557 809 -2413 -1434 C ATOM 922 NH1 ARG A 170 38.181 -1.827 26.113 1.00 76.06 N ANISOU 922 NH1 ARG A 170 9400 9551 9948 781 -2492 -1592 N ATOM 923 NH2 ARG A 170 39.028 0.300 26.254 1.00 73.22 N ANISOU 923 NH2 ARG A 170 9144 9217 9460 958 -2459 -1302 N ATOM 924 N ASN A 171 43.055 -4.938 30.058 1.00 28.91 N ANISOU 924 N ASN A 171 3730 3296 3959 477 -1448 -1027 N ATOM 925 CA ASN A 171 43.598 -6.014 30.877 1.00 37.60 C ANISOU 925 CA ASN A 171 4900 4304 5082 419 -1251 -984 C ATOM 926 C ASN A 171 44.744 -5.518 31.750 1.00 31.58 C ANISOU 926 C ASN A 171 4117 3606 4276 469 -1091 -771 C ATOM 927 O ASN A 171 44.803 -5.818 32.944 1.00 41.62 O ANISOU 927 O ASN A 171 5333 4836 5646 385 -957 -732 O ATOM 928 CB ASN A 171 44.074 -7.172 29.997 1.00 46.48 C ANISOU 928 CB ASN A 171 6254 5349 6057 496 -1230 -1030 C ATOM 929 CG ASN A 171 42.927 -7.961 29.399 1.00 58.54 C ANISOU 929 CG ASN A 171 7810 6780 7651 395 -1357 -1265 C ATOM 930 OD1 ASN A 171 41.914 -8.202 30.057 1.00 61.10 O ANISOU 930 OD1 ASN A 171 7999 7051 8164 218 -1362 -1391 O ATOM 931 ND2 ASN A 171 43.079 -8.367 28.143 1.00 66.84 N ANISOU 931 ND2 ASN A 171 9035 7819 8544 497 -1455 -1335 N ATOM 932 N SER A 172 45.645 -4.750 31.143 1.00 26.70 N ANISOU 932 N SER A 172 3547 3095 3501 597 -1105 -640 N ATOM 933 CA SER A 172 46.770 -4.162 31.860 1.00 30.60 C ANISOU 933 CA SER A 172 3999 3682 3945 633 -972 -451 C ATOM 934 C SER A 172 46.291 -3.320 33.039 1.00 34.47 C ANISOU 934 C SER A 172 4310 4190 4599 520 -960 -426 C ATOM 935 O SER A 172 46.785 -3.478 34.154 1.00 25.09 O ANISOU 935 O SER A 172 3074 3009 3451 483 -825 -344 O ATOM 936 CB SER A 172 47.625 -3.310 30.918 1.00 33.78 C ANISOU 936 CB SER A 172 4467 4201 4168 746 -1001 -338 C ATOM 937 OG SER A 172 48.215 -4.106 29.904 1.00 34.51 O ANISOU 937 OG SER A 172 4728 4293 4090 865 -980 -348 O ATOM 938 N ILE A 173 45.327 -2.438 32.784 1.00 42.38 N ANISOU 938 N ILE A 173 5220 5200 5681 485 -1107 -503 N ATOM 939 CA ILE A 173 44.736 -1.597 33.825 1.00 40.42 C ANISOU 939 CA ILE A 173 4806 4965 5588 394 -1108 -504 C ATOM 940 C ILE A 173 44.215 -2.432 34.989 1.00 43.15 C ANISOU 940 C ILE A 173 5072 5235 6086 270 -998 -573 C ATOM 941 O ILE A 173 44.604 -2.227 36.150 1.00 46.20 O ANISOU 941 O ILE A 173 5401 5637 6517 221 -875 -483 O ATOM 942 CB ILE A 173 43.566 -0.749 33.279 1.00 33.22 C ANISOU 942 CB ILE A 173 3813 4061 4748 405 -1303 -621 C ATOM 943 CG1 ILE A 173 44.021 0.142 32.123 1.00 24.38 C ANISOU 943 CG1 ILE A 173 2813 2992 3459 532 -1414 -544 C ATOM 944 CG2 ILE A 173 42.950 0.083 34.391 1.00 23.43 C ANISOU 944 CG2 ILE A 173 2403 2833 3666 330 -1291 -633 C ATOM 945 CD1 ILE A 173 45.044 1.163 32.509 1.00 35.74 C ANISOU 945 CD1 ILE A 173 4276 4485 4818 543 -1326 -358 C ATOM 946 N VAL A 174 43.333 -3.375 34.664 1.00 24.41 N ANISOU 946 N VAL A 174 2709 2780 3785 208 -1040 -736 N ATOM 947 CA VAL A 174 42.719 -4.228 35.676 1.00 28.75 C ANISOU 947 CA VAL A 174 3206 3239 4477 60 -925 -816 C ATOM 948 C VAL A 174 43.774 -4.928 36.529 1.00 26.10 C ANISOU 948 C VAL A 174 2986 2858 4072 74 -730 -677 C ATOM 949 O VAL A 174 43.715 -4.898 37.765 1.00 35.05 O ANISOU 949 O VAL A 174 4057 3975 5285 -6 -611 -635 O ATOM 950 CB VAL A 174 41.803 -5.281 35.035 1.00 32.66 C ANISOU 950 CB VAL A 174 3738 3643 5030 -23 -986 -1011 C ATOM 951 CG1 VAL A 174 41.263 -6.228 36.095 1.00 37.76 C ANISOU 951 CG1 VAL A 174 4368 4174 5807 -201 -831 -1080 C ATOM 952 CG2 VAL A 174 40.667 -4.603 34.285 1.00 27.63 C ANISOU 952 CG2 VAL A 174 2952 3074 4470 -29 -1197 -1170 C ATOM 953 N ILE A 175 44.745 -5.542 35.859 1.00 25.22 N ANISOU 953 N ILE A 175 3047 2737 3799 196 -703 -609 N ATOM 954 CA ILE A 175 45.853 -6.201 36.541 1.00 33.77 C ANISOU 954 CA ILE A 175 4244 3800 4788 263 -540 -476 C ATOM 955 C ILE A 175 46.584 -5.242 37.482 1.00 28.63 C ANISOU 955 C ILE A 175 3484 3270 4123 286 -480 -324 C ATOM 956 O ILE A 175 46.864 -5.587 38.633 1.00 28.48 O ANISOU 956 O ILE A 175 3475 3223 4125 259 -355 -262 O ATOM 957 CB ILE A 175 46.854 -6.792 35.533 1.00 26.65 C ANISOU 957 CB ILE A 175 3514 2914 3698 431 -537 -427 C ATOM 958 CG1 ILE A 175 46.223 -7.978 34.799 1.00 32.46 C ANISOU 958 CG1 ILE A 175 4405 3495 4435 403 -568 -580 C ATOM 959 CG2 ILE A 175 48.128 -7.228 36.236 1.00 27.14 C ANISOU 959 CG2 ILE A 175 3651 3012 3650 547 -389 -277 C ATOM 960 CD1 ILE A 175 47.094 -8.554 33.704 1.00 35.61 C ANISOU 960 CD1 ILE A 175 4986 3901 4642 579 -573 -557 C ATOM 961 N ILE A 176 46.872 -4.039 36.987 1.00 26.53 N ANISOU 961 N ILE A 176 3136 3129 3816 330 -570 -269 N ATOM 962 CA ILE A 176 47.537 -3.002 37.774 1.00 35.25 C ANISOU 962 CA ILE A 176 4140 4347 4908 327 -530 -142 C ATOM 963 C ILE A 176 46.791 -2.730 39.078 1.00 30.69 C ANISOU 963 C ILE A 176 3452 3727 4481 202 -483 -174 C ATOM 964 O ILE A 176 47.387 -2.742 40.162 1.00 26.17 O ANISOU 964 O ILE A 176 2866 3187 3892 196 -377 -85 O ATOM 965 CB ILE A 176 47.664 -1.679 36.978 1.00 37.87 C ANISOU 965 CB ILE A 176 4425 4772 5191 354 -644 -105 C ATOM 966 CG1 ILE A 176 48.719 -1.806 35.877 1.00 34.98 C ANISOU 966 CG1 ILE A 176 4165 4484 4641 475 -643 -29 C ATOM 967 CG2 ILE A 176 48.022 -0.524 37.903 1.00 19.20 C ANISOU 967 CG2 ILE A 176 1955 2486 2855 300 -615 -13 C ATOM 968 CD1 ILE A 176 48.808 -0.587 34.977 1.00 20.66 C ANISOU 968 CD1 ILE A 176 2356 2735 2759 493 -743 9 C ATOM 969 N TRP A 177 45.484 -2.505 38.974 1.00 32.06 N ANISOU 969 N TRP A 177 3543 3842 4795 111 -562 -311 N ATOM 970 CA TRP A 177 44.684 -2.200 40.160 1.00 26.06 C ANISOU 970 CA TRP A 177 2664 3055 4181 -6 -509 -359 C ATOM 971 C TRP A 177 44.590 -3.376 41.138 1.00 32.32 C ANISOU 971 C TRP A 177 3523 3748 5007 -80 -350 -368 C ATOM 972 O TRP A 177 44.677 -3.182 42.357 1.00 27.48 O ANISOU 972 O TRP A 177 2875 3142 4424 -129 -248 -315 O ATOM 973 CB TRP A 177 43.283 -1.749 39.753 1.00 28.41 C ANISOU 973 CB TRP A 177 2836 3338 4622 -69 -631 -523 C ATOM 974 CG TRP A 177 43.209 -0.295 39.384 1.00 27.29 C ANISOU 974 CG TRP A 177 2618 3276 4474 -8 -760 -500 C ATOM 975 CD1 TRP A 177 43.274 0.237 38.131 1.00 30.06 C ANISOU 975 CD1 TRP A 177 3014 3660 4746 89 -910 -503 C ATOM 976 CD2 TRP A 177 43.056 0.813 40.282 1.00 28.99 C ANISOU 976 CD2 TRP A 177 2735 3531 4750 -33 -746 -468 C ATOM 977 NE1 TRP A 177 43.168 1.606 38.190 1.00 33.89 N ANISOU 977 NE1 TRP A 177 3450 4189 5239 125 -989 -469 N ATOM 978 CE2 TRP A 177 43.034 1.984 39.500 1.00 27.81 C ANISOU 978 CE2 TRP A 177 2589 3421 4558 51 -892 -452 C ATOM 979 CE3 TRP A 177 42.936 0.926 41.672 1.00 30.34 C ANISOU 979 CE3 TRP A 177 2838 3696 4993 -115 -622 -452 C ATOM 980 CZ2 TRP A 177 42.894 3.254 40.059 1.00 19.73 C ANISOU 980 CZ2 TRP A 177 1509 2417 3568 57 -918 -425 C ATOM 981 CZ3 TRP A 177 42.798 2.188 42.226 1.00 23.43 C ANISOU 981 CZ3 TRP A 177 1892 2859 4152 -109 -650 -432 C ATOM 982 CH2 TRP A 177 42.778 3.335 41.421 1.00 20.57 C ANISOU 982 CH2 TRP A 177 1540 2522 3753 -24 -797 -421 C ATOM 983 N ILE A 178 44.415 -4.588 40.613 1.00 28.80 N ANISOU 983 N ILE A 178 3200 3198 4544 -88 -326 -434 N ATOM 984 CA ILE A 178 44.352 -5.777 41.466 1.00 32.12 C ANISOU 984 CA ILE A 178 3741 3488 4976 -156 -167 -435 C ATOM 985 C ILE A 178 45.656 -5.987 42.240 1.00 41.25 C ANISOU 985 C ILE A 178 5006 4677 5992 -39 -59 -261 C ATOM 986 O ILE A 178 45.650 -6.114 43.473 1.00 42.60 O ANISOU 986 O ILE A 178 5190 4816 6180 -90 59 -214 O ATOM 987 CB ILE A 178 44.050 -7.049 40.654 1.00 30.54 C ANISOU 987 CB ILE A 178 3697 3148 4759 -176 -165 -535 C ATOM 988 CG1 ILE A 178 42.659 -6.969 40.026 1.00 25.11 C ANISOU 988 CG1 ILE A 178 2883 2436 4221 -318 -271 -734 C ATOM 989 CG2 ILE A 178 44.150 -8.280 41.540 1.00 28.23 C ANISOU 989 CG2 ILE A 178 3589 2691 4445 -229 14 -508 C ATOM 990 CD1 ILE A 178 42.271 -8.214 39.257 1.00 28.86 C ANISOU 990 CD1 ILE A 178 3510 2767 4689 -374 -276 -859 C ATOM 991 N VAL A 179 46.768 -6.022 41.509 1.00 30.86 N ANISOU 991 N VAL A 179 3759 3437 4528 124 -100 -173 N ATOM 992 CA VAL A 179 48.088 -6.163 42.115 1.00 31.70 C ANISOU 992 CA VAL A 179 3929 3622 4492 262 -23 -20 C ATOM 993 C VAL A 179 48.324 -5.089 43.171 1.00 36.37 C ANISOU 993 C VAL A 179 4379 4332 5108 222 -10 55 C ATOM 994 O VAL A 179 48.734 -5.392 44.297 1.00 32.62 O ANISOU 994 O VAL A 179 3951 3853 4588 243 87 128 O ATOM 995 CB VAL A 179 49.207 -6.089 41.055 1.00 34.56 C ANISOU 995 CB VAL A 179 4321 4104 4705 432 -80 47 C ATOM 996 CG1 VAL A 179 50.562 -5.861 41.715 1.00 37.08 C ANISOU 996 CG1 VAL A 179 4611 4579 4897 558 -26 192 C ATOM 997 CG2 VAL A 179 49.223 -7.354 40.211 1.00 33.40 C ANISOU 997 CG2 VAL A 179 4366 3833 4493 514 -64 -10 C ATOM 998 N SER A 180 48.049 -3.839 42.805 1.00 32.11 N ANISOU 998 N SER A 180 3687 3887 4627 170 -111 34 N ATOM 999 CA SER A 180 48.239 -2.717 43.719 1.00 32.04 C ANISOU 999 CA SER A 180 3557 3976 4640 123 -110 90 C ATOM 1000 C SER A 180 47.431 -2.885 45.007 1.00 34.10 C ANISOU 1000 C SER A 180 3805 4151 5000 12 -17 48 C ATOM 1001 O SER A 180 47.948 -2.671 46.102 1.00 30.64 O ANISOU 1001 O SER A 180 3364 3765 4513 20 48 126 O ATOM 1002 CB SER A 180 47.865 -1.403 43.034 1.00 25.81 C ANISOU 1002 CB SER A 180 2651 3249 3906 82 -235 55 C ATOM 1003 OG SER A 180 48.716 -1.150 41.929 1.00 29.26 O ANISOU 1003 OG SER A 180 3115 3775 4229 174 -299 113 O ATOM 1004 N CYS A 181 46.168 -3.278 44.876 1.00 28.34 N ANISOU 1004 N CYS A 181 3065 3302 4402 -97 -6 -80 N ATOM 1005 CA CYS A 181 45.320 -3.460 46.049 1.00 28.57 C ANISOU 1005 CA CYS A 181 3074 3254 4528 -222 106 -131 C ATOM 1006 C CYS A 181 45.791 -4.617 46.926 1.00 38.49 C ANISOU 1006 C CYS A 181 4512 4419 5693 -198 257 -57 C ATOM 1007 O CYS A 181 45.667 -4.565 48.152 1.00 26.54 O ANISOU 1007 O CYS A 181 3015 2890 4180 -250 361 -26 O ATOM 1008 CB CYS A 181 43.866 -3.683 45.635 1.00 20.74 C ANISOU 1008 CB CYS A 181 2005 2176 3701 -356 89 -303 C ATOM 1009 SG CYS A 181 43.032 -2.193 45.050 1.00 40.52 S ANISOU 1009 SG CYS A 181 4285 4782 6328 -374 -75 -405 S ATOM 1010 N ILE A 182 46.329 -5.661 46.304 1.00 39.03 N ANISOU 1010 N ILE A 182 4740 4420 5669 -106 269 -28 N ATOM 1011 CA ILE A 182 46.764 -6.827 47.066 1.00 32.88 C ANISOU 1011 CA ILE A 182 4178 3527 4789 -54 406 44 C ATOM 1012 C ILE A 182 48.077 -6.585 47.813 1.00 32.31 C ANISOU 1012 C ILE A 182 4135 3583 4557 108 417 196 C ATOM 1013 O ILE A 182 48.175 -6.877 49.004 1.00 44.40 O ANISOU 1013 O ILE A 182 5762 5073 6036 108 520 254 O ATOM 1014 CB ILE A 182 46.918 -8.062 46.160 1.00 38.13 C ANISOU 1014 CB ILE A 182 5032 4059 5396 13 416 17 C ATOM 1015 CG1 ILE A 182 45.545 -8.519 45.666 1.00 24.20 C ANISOU 1015 CG1 ILE A 182 3264 2146 3786 -182 430 -149 C ATOM 1016 CG2 ILE A 182 47.609 -9.197 46.909 1.00 29.57 C ANISOU 1016 CG2 ILE A 182 4207 2861 4167 129 542 118 C ATOM 1017 CD1 ILE A 182 45.596 -9.712 44.751 1.00 31.48 C ANISOU 1017 CD1 ILE A 182 4386 2917 4658 -143 433 -199 C ATOM 1018 N ILE A 183 49.079 -6.041 47.129 1.00 28.40 N ANISOU 1018 N ILE A 183 3557 3255 3980 240 311 256 N ATOM 1019 CA ILE A 183 50.398 -5.890 47.743 1.00 30.05 C ANISOU 1019 CA ILE A 183 3768 3615 4034 397 311 383 C ATOM 1020 C ILE A 183 50.434 -4.829 48.843 1.00 33.04 C ANISOU 1020 C ILE A 183 4020 4103 4429 324 306 413 C ATOM 1021 O ILE A 183 51.372 -4.791 49.637 1.00 35.79 O ANISOU 1021 O ILE A 183 4381 4564 4653 429 316 503 O ATOM 1022 CB ILE A 183 51.481 -5.541 46.695 1.00 37.06 C ANISOU 1022 CB ILE A 183 4571 4679 4832 533 215 428 C ATOM 1023 CG1 ILE A 183 51.259 -4.137 46.126 1.00 35.92 C ANISOU 1023 CG1 ILE A 183 4228 4647 4772 422 113 393 C ATOM 1024 CG2 ILE A 183 51.520 -6.589 45.588 1.00 21.14 C ANISOU 1024 CG2 ILE A 183 2696 2561 2776 629 219 395 C ATOM 1025 CD1 ILE A 183 52.340 -3.700 45.159 1.00 32.24 C ANISOU 1025 CD1 ILE A 183 3683 4359 4209 523 44 445 C ATOM 1026 N MET A 184 49.418 -3.975 48.901 1.00 19.34 N ANISOU 1026 N MET A 184 2164 2341 2841 156 285 329 N ATOM 1027 CA MET A 184 49.396 -2.916 49.904 1.00 23.35 C ANISOU 1027 CA MET A 184 2567 2938 3365 87 281 344 C ATOM 1028 C MET A 184 48.559 -3.284 51.127 1.00 37.58 C ANISOU 1028 C MET A 184 4452 4619 5209 -6 410 315 C ATOM 1029 O MET A 184 48.324 -2.448 52.000 1.00 36.05 O ANISOU 1029 O MET A 184 4185 4474 5038 -76 422 304 O ATOM 1030 CB MET A 184 48.887 -1.613 49.289 1.00 21.45 C ANISOU 1030 CB MET A 184 2156 2753 3241 -10 178 275 C ATOM 1031 CG MET A 184 49.812 -1.054 48.226 1.00 22.20 C ANISOU 1031 CG MET A 184 2182 2981 3271 63 68 322 C ATOM 1032 SD MET A 184 51.517 -1.004 48.809 1.00 42.48 S ANISOU 1032 SD MET A 184 4740 5747 5653 186 66 452 S ATOM 1033 CE MET A 184 52.394 -0.626 47.295 1.00 36.18 C ANISOU 1033 CE MET A 184 3869 5080 4797 247 -22 483 C ATOM 1034 N ILE A 185 48.121 -4.538 51.191 1.00 31.48 N ANISOU 1034 N ILE A 185 3848 3679 4433 -14 516 301 N ATOM 1035 CA ILE A 185 47.411 -5.044 52.366 1.00 34.23 C ANISOU 1035 CA ILE A 185 4315 3898 4791 -107 672 289 C ATOM 1036 C ILE A 185 48.258 -4.991 53.655 1.00 33.93 C ANISOU 1036 C ILE A 185 4370 3933 4588 -6 713 402 C ATOM 1037 O ILE A 185 47.732 -4.622 54.715 1.00 30.79 O ANISOU 1037 O ILE A 185 3974 3519 4207 -99 795 385 O ATOM 1038 CB ILE A 185 46.906 -6.490 52.130 1.00 30.17 C ANISOU 1038 CB ILE A 185 4010 3170 4284 -142 788 262 C ATOM 1039 CG1 ILE A 185 45.744 -6.488 51.135 1.00 23.02 C ANISOU 1039 CG1 ILE A 185 2992 2191 3565 -300 763 113 C ATOM 1040 CG2 ILE A 185 46.468 -7.137 53.436 1.00 24.32 C ANISOU 1040 CG2 ILE A 185 3455 2291 3495 -214 973 290 C ATOM 1041 CD1 ILE A 185 45.247 -7.871 50.772 1.00 24.60 C ANISOU 1041 CD1 ILE A 185 3389 2178 3779 -365 864 65 C ATOM 1042 N PRO A 186 49.561 -5.352 53.582 1.00 27.42 N ANISOU 1042 N PRO A 186 3619 3203 3598 193 654 508 N ATOM 1043 CA PRO A 186 50.391 -5.194 54.785 1.00 33.89 C ANISOU 1043 CA PRO A 186 4494 4127 4254 301 658 601 C ATOM 1044 C PRO A 186 50.355 -3.787 55.384 1.00 38.15 C ANISOU 1044 C PRO A 186 4849 4816 4831 208 598 572 C ATOM 1045 O PRO A 186 50.343 -3.645 56.611 1.00 43.92 O ANISOU 1045 O PRO A 186 5650 5554 5482 202 655 599 O ATOM 1046 CB PRO A 186 51.795 -5.522 54.279 1.00 35.10 C ANISOU 1046 CB PRO A 186 4649 4426 4261 527 559 685 C ATOM 1047 CG PRO A 186 51.562 -6.510 53.206 1.00 34.64 C ANISOU 1047 CG PRO A 186 4700 4223 4240 565 587 662 C ATOM 1048 CD PRO A 186 50.297 -6.070 52.521 1.00 28.03 C ANISOU 1048 CD PRO A 186 3753 3287 3611 345 596 542 C ATOM 1049 N GLN A 187 50.330 -2.770 54.527 1.00 31.33 N ANISOU 1049 N GLN A 187 3778 4050 4073 142 487 518 N ATOM 1050 CA GLN A 187 50.253 -1.389 54.984 1.00 25.00 C ANISOU 1050 CA GLN A 187 2827 3359 3315 47 427 482 C ATOM 1051 C GLN A 187 49.030 -1.183 55.869 1.00 31.95 C ANISOU 1051 C GLN A 187 3737 4119 4282 -89 541 410 C ATOM 1052 O GLN A 187 49.133 -0.634 56.964 1.00 41.54 O ANISOU 1052 O GLN A 187 4963 5388 5432 -108 561 418 O ATOM 1053 CB GLN A 187 50.208 -0.427 53.797 1.00 25.46 C ANISOU 1053 CB GLN A 187 2709 3481 3482 -11 310 432 C ATOM 1054 CG GLN A 187 50.366 1.027 54.193 1.00 25.15 C ANISOU 1054 CG GLN A 187 2548 3550 3459 -90 236 408 C ATOM 1055 CD GLN A 187 51.747 1.322 54.743 1.00 42.26 C ANISOU 1055 CD GLN A 187 4689 5904 5463 -15 172 486 C ATOM 1056 OE1 GLN A 187 52.753 1.130 54.058 1.00 43.61 O ANISOU 1056 OE1 GLN A 187 4812 6197 5561 71 108 540 O ATOM 1057 NE2 GLN A 187 51.806 1.782 55.990 1.00 35.98 N ANISOU 1057 NE2 GLN A 187 3918 5147 4605 -46 190 481 N ATOM 1058 N ALA A 188 47.877 -1.642 55.391 1.00 30.78 N ANISOU 1058 N ALA A 188 3597 3822 4276 -186 618 329 N ATOM 1059 CA ALA A 188 46.631 -1.539 56.142 1.00 29.47 C ANISOU 1059 CA ALA A 188 3433 3556 4208 -326 747 244 C ATOM 1060 C ALA A 188 46.695 -2.337 57.443 1.00 28.39 C ANISOU 1060 C ALA A 188 3504 3346 3937 -309 903 309 C ATOM 1061 O ALA A 188 46.159 -1.914 58.467 1.00 28.74 O ANISOU 1061 O ALA A 188 3557 3383 3980 -384 994 276 O ATOM 1062 CB ALA A 188 45.460 -2.009 55.292 1.00 20.98 C ANISOU 1062 CB ALA A 188 2307 2359 3307 -435 793 136 C ATOM 1063 N ILE A 189 47.351 -3.492 57.401 1.00 24.89 N ANISOU 1063 N ILE A 189 3249 2841 3366 -196 935 402 N ATOM 1064 CA ILE A 189 47.489 -4.318 58.595 1.00 35.57 C ANISOU 1064 CA ILE A 189 4849 4106 4559 -151 1076 482 C ATOM 1065 C ILE A 189 48.294 -3.617 59.693 1.00 38.11 C ANISOU 1065 C ILE A 189 5180 4579 4721 -59 1021 544 C ATOM 1066 O ILE A 189 47.888 -3.597 60.854 1.00 41.91 O ANISOU 1066 O ILE A 189 5772 5015 5135 -107 1141 548 O ATOM 1067 CB ILE A 189 48.158 -5.665 58.269 1.00 33.35 C ANISOU 1067 CB ILE A 189 4793 3727 4153 -2 1096 576 C ATOM 1068 CG1 ILE A 189 47.268 -6.488 57.339 1.00 35.68 C ANISOU 1068 CG1 ILE A 189 5129 3836 4590 -119 1175 503 C ATOM 1069 CG2 ILE A 189 48.440 -6.443 59.543 1.00 37.89 C ANISOU 1069 CG2 ILE A 189 5657 4213 4525 86 1220 678 C ATOM 1070 CD1 ILE A 189 47.873 -7.811 56.932 1.00 38.91 C ANISOU 1070 CD1 ILE A 189 5784 4119 4882 27 1197 582 C ATOM 1071 N VAL A 190 49.423 -3.026 59.316 1.00 29.73 N ANISOU 1071 N VAL A 190 3996 3704 3594 61 843 584 N ATOM 1072 CA VAL A 190 50.360 -2.470 60.291 1.00 23.69 C ANISOU 1072 CA VAL A 190 3238 3106 2659 159 766 639 C ATOM 1073 C VAL A 190 49.882 -1.164 60.952 1.00 26.19 C ANISOU 1073 C VAL A 190 3433 3486 3033 25 756 559 C ATOM 1074 O VAL A 190 50.160 -0.925 62.130 1.00 24.05 O ANISOU 1074 O VAL A 190 3248 3271 2619 58 771 583 O ATOM 1075 CB VAL A 190 51.740 -2.238 59.633 1.00 35.50 C ANISOU 1075 CB VAL A 190 4609 4804 4076 304 585 690 C ATOM 1076 CG1 VAL A 190 52.722 -1.652 60.623 1.00 54.39 C ANISOU 1076 CG1 VAL A 190 6977 7393 6296 388 489 726 C ATOM 1077 CG2 VAL A 190 52.283 -3.547 59.098 1.00 44.75 C ANISOU 1077 CG2 VAL A 190 5920 5920 5161 478 598 768 C ATOM 1078 N MET A 191 49.156 -0.331 60.209 1.00 29.83 N ANISOU 1078 N MET A 191 3711 3933 3689 -109 726 461 N ATOM 1079 CA MET A 191 48.702 0.960 60.735 1.00 26.69 C ANISOU 1079 CA MET A 191 3207 3582 3349 -213 708 377 C ATOM 1080 C MET A 191 47.840 0.797 61.981 1.00 31.41 C ANISOU 1080 C MET A 191 3935 4086 3912 -276 882 345 C ATOM 1081 O MET A 191 46.885 0.024 61.987 1.00 34.08 O ANISOU 1081 O MET A 191 4345 4279 4325 -344 1041 319 O ATOM 1082 CB MET A 191 47.917 1.740 59.674 1.00 27.17 C ANISOU 1082 CB MET A 191 3086 3612 3625 -317 658 276 C ATOM 1083 CG MET A 191 48.716 2.096 58.432 1.00 30.72 C ANISOU 1083 CG MET A 191 3415 4154 4102 -275 494 303 C ATOM 1084 SD MET A 191 50.293 2.883 58.813 1.00 41.67 S ANISOU 1084 SD MET A 191 4759 5752 5321 -214 345 368 S ATOM 1085 CE MET A 191 49.729 4.350 59.669 1.00 40.84 C ANISOU 1085 CE MET A 191 4616 5645 5255 -332 338 271 C ATOM 1086 N GLU A 192 48.190 1.523 63.040 1.00 30.55 N ANISOU 1086 N GLU A 192 3859 4065 3683 -264 858 341 N ATOM 1087 CA GLU A 192 47.431 1.475 64.287 1.00 34.06 C ANISOU 1087 CA GLU A 192 4436 4438 4069 -316 1027 309 C ATOM 1088 C GLU A 192 47.333 2.846 64.952 1.00 29.87 C ANISOU 1088 C GLU A 192 3832 3988 3530 -366 977 225 C ATOM 1089 O GLU A 192 48.192 3.713 64.760 1.00 37.09 O ANISOU 1089 O GLU A 192 4655 5028 4408 -341 800 222 O ATOM 1090 CB GLU A 192 48.059 0.477 65.269 1.00 44.52 C ANISOU 1090 CB GLU A 192 6012 5751 5153 -199 1093 425 C ATOM 1091 CG GLU A 192 48.060 -0.977 64.808 1.00 42.16 C ANISOU 1091 CG GLU A 192 5859 5325 4836 -143 1179 510 C ATOM 1092 CD GLU A 192 46.677 -1.602 64.803 1.00 45.73 C ANISOU 1092 CD GLU A 192 6373 5583 5418 -293 1407 456 C ATOM 1093 OE1 GLU A 192 45.743 -1.005 65.376 1.00 42.49 O ANISOU 1093 OE1 GLU A 192 5913 5153 5079 -417 1522 363 O ATOM 1094 OE2 GLU A 192 46.525 -2.699 64.225 1.00 62.88 O ANISOU 1094 OE2 GLU A 192 8643 7628 7621 -292 1476 496 O ATOM 1095 N CYS A 193 46.273 3.032 65.732 1.00 29.25 N ANISOU 1095 N CYS A 193 3799 3832 3483 -445 1144 149 N ATOM 1096 CA CYS A 193 46.114 4.228 66.545 1.00 34.34 C ANISOU 1096 CA CYS A 193 4425 4531 4090 -475 1127 64 C ATOM 1097 C CYS A 193 46.701 3.998 67.928 1.00 32.77 C ANISOU 1097 C CYS A 193 4439 4379 3631 -407 1166 124 C ATOM 1098 O CYS A 193 46.471 2.956 68.541 1.00 35.20 O ANISOU 1098 O CYS A 193 4931 4611 3832 -383 1327 190 O ATOM 1099 CB CYS A 193 44.640 4.622 66.662 1.00 42.01 C ANISOU 1099 CB CYS A 193 5317 5416 5228 -575 1288 -67 C ATOM 1100 SG CYS A 193 43.984 5.542 65.255 1.00 47.12 S ANISOU 1100 SG CYS A 193 5700 6052 6151 -621 1172 -182 S ATOM 1101 N SER A 194 47.463 4.970 68.415 1.00 35.69 N ANISOU 1101 N SER A 194 4802 4868 3890 -381 1018 99 N ATOM 1102 CA SER A 194 48.046 4.878 69.747 1.00 33.73 C ANISOU 1102 CA SER A 194 4749 4687 3381 -308 1024 138 C ATOM 1103 C SER A 194 47.744 6.131 70.563 1.00 30.66 C ANISOU 1103 C SER A 194 4367 4325 2956 -364 1018 18 C ATOM 1104 O SER A 194 47.862 7.259 70.071 1.00 32.14 O ANISOU 1104 O SER A 194 4410 4549 3252 -422 887 -65 O ATOM 1105 CB SER A 194 49.556 4.645 69.660 1.00 40.87 C ANISOU 1105 CB SER A 194 5660 5746 4123 -193 818 231 C ATOM 1106 OG SER A 194 50.173 5.587 68.801 1.00 68.07 O ANISOU 1106 OG SER A 194 8898 9293 7673 -243 623 186 O ATOM 1107 N THR A 195 47.340 5.913 71.810 1.00 41.06 N ANISOU 1107 N THR A 195 5879 5610 4111 -345 1173 10 N ATOM 1108 CA THR A 195 46.982 6.993 72.717 1.00 47.05 C ANISOU 1108 CA THR A 195 6686 6383 4808 -383 1198 -109 C ATOM 1109 C THR A 195 48.186 7.416 73.549 1.00 48.26 C ANISOU 1109 C THR A 195 6949 6679 4708 -316 1018 -95 C ATOM 1110 O THR A 195 48.878 6.583 74.134 1.00 61.53 O ANISOU 1110 O THR A 195 8786 8419 6173 -211 999 9 O ATOM 1111 CB THR A 195 45.826 6.581 73.651 1.00 54.04 C ANISOU 1111 CB THR A 195 7723 7165 5645 -407 1485 -140 C ATOM 1112 OG1 THR A 195 44.685 6.210 72.865 1.00 66.45 O ANISOU 1112 OG1 THR A 195 9155 8629 7464 -489 1646 -176 O ATOM 1113 CG2 THR A 195 45.445 7.726 74.573 1.00 47.98 C ANISOU 1113 CG2 THR A 195 7008 6415 4808 -429 1517 -275 C ATOM 1114 N VAL A 196 48.429 8.721 73.589 1.00 45.73 N ANISOU 1114 N VAL A 196 6553 6411 4413 -375 880 -207 N ATOM 1115 CA VAL A 196 49.571 9.291 74.287 1.00 55.71 C ANISOU 1115 CA VAL A 196 7882 7823 5462 -350 684 -227 C ATOM 1116 C VAL A 196 49.115 10.341 75.299 1.00 53.29 C ANISOU 1116 C VAL A 196 7693 7488 5068 -393 727 -367 C ATOM 1117 O VAL A 196 48.184 11.113 75.039 1.00 55.82 O ANISOU 1117 O VAL A 196 7953 7697 5559 -461 813 -474 O ATOM 1118 CB VAL A 196 50.570 9.933 73.301 1.00 58.17 C ANISOU 1118 CB VAL A 196 7993 8241 5869 -409 441 -236 C ATOM 1119 CG1 VAL A 196 51.922 10.136 73.967 1.00 66.19 C ANISOU 1119 CG1 VAL A 196 9047 9455 6647 -375 233 -234 C ATOM 1120 CG2 VAL A 196 50.718 9.076 72.053 1.00 51.60 C ANISOU 1120 CG2 VAL A 196 7016 7400 5190 -382 432 -127 C ATOM 1121 N PHE A 197 49.784 10.361 76.449 1.00 54.34 N ANISOU 1121 N PHE A 197 7999 7725 4923 -334 658 -371 N ATOM 1122 CA PHE A 197 49.439 11.259 77.547 1.00 47.66 C ANISOU 1122 CA PHE A 197 7307 6859 3941 -357 698 -503 C ATOM 1123 C PHE A 197 50.548 12.273 77.810 1.00 54.87 C ANISOU 1123 C PHE A 197 8205 7907 4737 -412 433 -590 C ATOM 1124 O PHE A 197 50.412 13.455 77.494 1.00 60.56 O ANISOU 1124 O PHE A 197 8858 8574 5579 -522 366 -713 O ATOM 1125 CB PHE A 197 49.155 10.455 78.817 1.00 44.61 C ANISOU 1125 CB PHE A 197 7185 6469 3297 -251 866 -452 C ATOM 1126 CG PHE A 197 47.944 9.572 78.717 1.00 57.04 C ANISOU 1126 CG PHE A 197 8801 7897 4977 -242 1166 -394 C ATOM 1127 CD1 PHE A 197 47.999 8.370 78.026 1.00 51.09 C ANISOU 1127 CD1 PHE A 197 8001 7113 4298 -205 1218 -249 C ATOM 1128 CD2 PHE A 197 46.752 9.941 79.317 1.00 60.72 C ANISOU 1128 CD2 PHE A 197 9348 8259 5464 -277 1403 -494 C ATOM 1129 CE1 PHE A 197 46.885 7.559 77.931 1.00 52.44 C ANISOU 1129 CE1 PHE A 197 8209 7145 4569 -231 1497 -208 C ATOM 1130 CE2 PHE A 197 45.637 9.133 79.228 1.00 61.52 C ANISOU 1130 CE2 PHE A 197 9459 8246 5669 -297 1688 -455 C ATOM 1131 CZ PHE A 197 45.703 7.940 78.532 1.00 57.80 C ANISOU 1131 CZ PHE A 197 8945 7739 5278 -288 1734 -313 C ATOM 1132 N LYS A 203 46.628 12.730 84.692 1.00 67.84 N ANISOU 1132 N LYS A 203 11193 9271 5311 -140 1506 -953 N ATOM 1133 CA LYS A 203 46.518 13.196 83.314 1.00 70.25 C ANISOU 1133 CA LYS A 203 11192 9528 5970 -231 1409 -980 C ATOM 1134 C LYS A 203 45.210 13.948 83.090 1.00 74.39 C ANISOU 1134 C LYS A 203 11629 9923 6713 -272 1610 -1121 C ATOM 1135 O LYS A 203 44.153 13.528 83.560 1.00 75.42 O ANISOU 1135 O LYS A 203 11828 9995 6835 -245 1908 -1131 O ATOM 1136 CB LYS A 203 46.624 12.022 82.336 1.00 65.98 C ANISOU 1136 CB LYS A 203 10497 8984 5589 -229 1431 -805 C ATOM 1137 N THR A 204 45.288 15.063 82.370 1.00 79.98 N ANISOU 1137 N THR A 204 12188 10590 7612 -332 1450 -1233 N ATOM 1138 CA THR A 204 44.108 15.864 82.069 1.00 85.26 C ANISOU 1138 CA THR A 204 12765 11139 8492 -335 1599 -1375 C ATOM 1139 C THR A 204 43.634 15.616 80.642 1.00 83.74 C ANISOU 1139 C THR A 204 12288 10890 8640 -371 1609 -1323 C ATOM 1140 O THR A 204 42.434 15.544 80.378 1.00 89.26 O ANISOU 1140 O THR A 204 12875 11525 9516 -347 1823 -1375 O ATOM 1141 CB THR A 204 44.378 17.370 82.257 1.00 87.20 C ANISOU 1141 CB THR A 204 13086 11336 8709 -358 1430 -1550 C ATOM 1142 OG1 THR A 204 45.475 17.769 81.425 1.00 80.46 O ANISOU 1142 OG1 THR A 204 12128 10512 7930 -448 1131 -1516 O ATOM 1143 CG2 THR A 204 44.711 17.677 83.709 1.00 90.34 C ANISOU 1143 CG2 THR A 204 13777 11784 8766 -320 1433 -1632 C ATOM 1144 N THR A 205 44.585 15.488 79.722 1.00 79.70 N ANISOU 1144 N THR A 205 11652 10419 8211 -425 1375 -1229 N ATOM 1145 CA THR A 205 44.263 15.265 78.318 1.00 82.75 C ANISOU 1145 CA THR A 205 11786 10757 8897 -457 1353 -1176 C ATOM 1146 C THR A 205 45.017 14.072 77.739 1.00 74.02 C ANISOU 1146 C THR A 205 10601 9729 7792 -473 1279 -991 C ATOM 1147 O THR A 205 45.889 13.493 78.386 1.00 77.25 O ANISOU 1147 O THR A 205 11143 10236 7972 -448 1212 -905 O ATOM 1148 CB THR A 205 44.579 16.508 77.458 1.00 82.08 C ANISOU 1148 CB THR A 205 11610 10612 8967 -508 1139 -1261 C ATOM 1149 OG1 THR A 205 45.974 16.821 77.557 1.00 75.19 O ANISOU 1149 OG1 THR A 205 10800 9822 7945 -577 888 -1230 O ATOM 1150 CG2 THR A 205 43.760 17.705 77.919 1.00 88.43 C ANISOU 1150 CG2 THR A 205 12502 11309 9788 -465 1213 -1448 C ATOM 1151 N LEU A 206 44.661 13.713 76.511 1.00 65.84 N ANISOU 1151 N LEU A 206 9356 8652 7010 -496 1285 -939 N ATOM 1152 CA LEU A 206 45.354 12.670 75.768 1.00 70.34 C ANISOU 1152 CA LEU A 206 9836 9279 7612 -504 1202 -778 C ATOM 1153 C LEU A 206 45.153 12.908 74.281 1.00 60.46 C ANISOU 1153 C LEU A 206 8355 7976 6642 -545 1115 -776 C ATOM 1154 O LEU A 206 44.104 13.403 73.867 1.00 55.61 O ANISOU 1154 O LEU A 206 7642 7272 6215 -543 1207 -873 O ATOM 1155 CB LEU A 206 44.852 11.277 76.170 1.00 75.95 C ANISOU 1155 CB LEU A 206 10619 9978 8260 -468 1430 -676 C ATOM 1156 CG LEU A 206 43.354 10.952 76.091 1.00 80.10 C ANISOU 1156 CG LEU A 206 11071 10411 8952 -488 1711 -733 C ATOM 1157 CD1 LEU A 206 42.920 10.536 74.695 1.00 74.28 C ANISOU 1157 CD1 LEU A 206 10098 9630 8497 -527 1703 -701 C ATOM 1158 CD2 LEU A 206 43.002 9.862 77.086 1.00 89.88 C ANISOU 1158 CD2 LEU A 206 12501 11640 10010 -473 1956 -660 C ATOM 1159 N PHE A 207 46.153 12.569 73.476 1.00 75.47 N ANISOU 1159 N PHE A 207 10387 11666 6621 1673 -106 -904 N ATOM 1160 CA PHE A 207 45.993 12.677 72.030 1.00 70.68 C ANISOU 1160 CA PHE A 207 9712 10672 6471 1330 202 -597 C ATOM 1161 C PHE A 207 46.273 11.334 71.375 1.00 60.86 C ANISOU 1161 C PHE A 207 8463 9462 5200 1236 94 -217 C ATOM 1162 O PHE A 207 46.985 10.511 71.930 1.00 56.81 O ANISOU 1162 O PHE A 207 7919 9160 4506 1361 -214 -320 O ATOM 1163 CB PHE A 207 46.901 13.771 71.448 1.00 77.99 C ANISOU 1163 CB PHE A 207 10391 11186 8054 1112 327 -1083 C ATOM 1164 CG PHE A 207 48.374 13.513 71.622 1.00 84.61 C ANISOU 1164 CG PHE A 207 10983 11996 9168 1066 1 -1580 C ATOM 1165 CD1 PHE A 207 49.093 12.833 70.650 1.00 91.68 C ANISOU 1165 CD1 PHE A 207 11769 12720 10347 879 9 -1400 C ATOM 1166 CD2 PHE A 207 49.046 13.976 72.742 1.00 88.97 C ANISOU 1166 CD2 PHE A 207 11391 12706 9707 1238 -326 -2271 C ATOM 1167 CE1 PHE A 207 50.450 12.603 70.802 1.00101.18 C ANISOU 1167 CE1 PHE A 207 12717 13886 11843 839 -275 -1846 C ATOM 1168 CE2 PHE A 207 50.403 13.750 72.899 1.00101.50 C ANISOU 1168 CE2 PHE A 207 12695 14284 11587 1210 -659 -2773 C ATOM 1169 CZ PHE A 207 51.106 13.065 71.927 1.00106.00 C ANISOU 1169 CZ PHE A 207 13149 14654 12471 997 -616 -2535 C ATOM 1170 N THR A 208 45.699 11.106 70.202 1.00 55.84 N ANISOU 1170 N THR A 208 7849 8639 4727 1056 338 202 N ATOM 1171 CA THR A 208 45.922 9.853 69.496 1.00 48.33 C ANISOU 1171 CA THR A 208 6877 7691 3797 964 240 501 C ATOM 1172 C THR A 208 46.682 10.098 68.201 1.00 43.19 C ANISOU 1172 C THR A 208 6089 6733 3589 757 363 414 C ATOM 1173 O THR A 208 46.353 11.011 67.445 1.00 39.36 O ANISOU 1173 O THR A 208 5594 6038 3324 696 671 459 O ATOM 1174 CB THR A 208 44.592 9.133 69.188 1.00 49.28 C ANISOU 1174 CB THR A 208 7071 7821 3833 933 348 986 C ATOM 1175 OG1 THR A 208 43.947 8.776 70.417 1.00 64.37 O ANISOU 1175 OG1 THR A 208 9016 9812 5630 1038 271 1037 O ATOM 1176 CG2 THR A 208 44.837 7.872 68.372 1.00 40.61 C ANISOU 1176 CG2 THR A 208 5885 6595 2949 776 232 1134 C ATOM 1177 N VAL A 209 47.711 9.293 67.952 1.00 46.45 N ANISOU 1177 N VAL A 209 6402 7121 4125 697 164 325 N ATOM 1178 CA VAL A 209 48.426 9.382 66.684 1.00 33.65 C ANISOU 1178 CA VAL A 209 4670 5225 2892 552 317 313 C ATOM 1179 C VAL A 209 48.254 8.099 65.880 1.00 31.36 C ANISOU 1179 C VAL A 209 4428 4991 2498 525 240 643 C ATOM 1180 O VAL A 209 48.048 7.022 66.443 1.00 45.16 O ANISOU 1180 O VAL A 209 6220 6926 4012 576 17 782 O ATOM 1181 CB VAL A 209 49.924 9.667 66.892 1.00 37.32 C ANISOU 1181 CB VAL A 209 4916 5533 3732 489 198 -140 C ATOM 1182 CG1 VAL A 209 50.107 10.955 67.681 1.00 39.00 C ANISOU 1182 CG1 VAL A 209 5016 5652 4148 508 247 -585 C ATOM 1183 CG2 VAL A 209 50.602 8.504 67.596 1.00 43.95 C ANISOU 1183 CG2 VAL A 209 5720 6606 4371 559 -201 -221 C ATOM 1184 N CYS A 210 48.319 8.225 64.559 1.00 37.23 N ANISOU 1184 N CYS A 210 5156 5565 3425 486 454 769 N ATOM 1185 CA CYS A 210 48.180 7.081 63.666 1.00 34.03 C ANISOU 1185 CA CYS A 210 4777 5207 2946 487 369 985 C ATOM 1186 C CYS A 210 49.535 6.730 63.070 1.00 39.57 C ANISOU 1186 C CYS A 210 5374 5748 3914 442 344 841 C ATOM 1187 O CYS A 210 50.133 7.539 62.360 1.00 48.67 O ANISOU 1187 O CYS A 210 6466 6689 5338 458 615 775 O ATOM 1188 CB CYS A 210 47.161 7.381 62.560 1.00 35.84 C ANISOU 1188 CB CYS A 210 5079 5459 3078 579 586 1219 C ATOM 1189 SG CYS A 210 46.989 6.103 61.281 1.00 46.85 S ANISOU 1189 SG CYS A 210 6462 6910 4430 623 442 1316 S ATOM 1190 N ASP A 211 50.028 5.530 63.362 1.00 32.18 N ANISOU 1190 N ASP A 211 4405 4884 2939 410 71 827 N ATOM 1191 CA ASP A 211 51.350 5.144 62.880 1.00 41.12 C ANISOU 1191 CA ASP A 211 5425 5870 4330 375 37 691 C ATOM 1192 C ASP A 211 51.516 3.632 62.762 1.00 43.60 C ANISOU 1192 C ASP A 211 5746 6255 4564 372 -196 796 C ATOM 1193 O ASP A 211 50.744 2.857 63.328 1.00 41.58 O ANISOU 1193 O ASP A 211 5546 6139 4114 387 -343 948 O ATOM 1194 CB ASP A 211 52.436 5.711 63.801 1.00 47.41 C ANISOU 1194 CB ASP A 211 6056 6602 5354 334 -57 354 C ATOM 1195 CG ASP A 211 53.783 5.851 63.106 1.00 62.64 C ANISOU 1195 CG ASP A 211 7806 8279 7714 288 59 191 C ATOM 1196 OD1 ASP A 211 53.971 5.250 62.026 1.00 45.69 O ANISOU 1196 OD1 ASP A 211 5705 6057 5599 318 166 372 O ATOM 1197 OD2 ASP A 211 54.658 6.561 63.646 1.00 79.93 O ANISOU 1197 OD2 ASP A 211 9786 10342 10242 239 45 -147 O ATOM 1198 N GLU A 212 52.537 3.228 62.015 1.00 39.83 N ANISOU 1198 N GLU A 212 5196 5641 4297 365 -175 730 N ATOM 1199 CA GLU A 212 52.880 1.824 61.858 1.00 35.93 C ANISOU 1199 CA GLU A 212 4689 5159 3804 364 -367 790 C ATOM 1200 C GLU A 212 53.252 1.196 63.193 1.00 37.18 C ANISOU 1200 C GLU A 212 4791 5434 3903 373 -621 765 C ATOM 1201 O GLU A 212 54.071 1.737 63.936 1.00 41.04 O ANISOU 1201 O GLU A 212 5173 5951 4467 390 -703 555 O ATOM 1202 CB GLU A 212 54.035 1.670 60.870 1.00 39.10 C ANISOU 1202 CB GLU A 212 5019 5386 4451 385 -262 708 C ATOM 1203 CG GLU A 212 53.725 2.187 59.480 1.00 50.57 C ANISOU 1203 CG GLU A 212 6557 6773 5884 500 26 789 C ATOM 1204 CD GLU A 212 54.946 2.214 58.585 1.00 56.71 C ANISOU 1204 CD GLU A 212 7267 7364 6917 578 223 749 C ATOM 1205 OE1 GLU A 212 56.075 2.152 59.117 1.00 49.02 O ANISOU 1205 OE1 GLU A 212 6128 6269 6227 491 162 611 O ATOM 1206 OE2 GLU A 212 54.776 2.296 57.350 1.00 67.64 O ANISOU 1206 OE2 GLU A 212 8751 8745 8204 771 442 853 O ATOM 1207 N ARG A 213 52.642 0.055 63.495 1.00 29.29 N ANISOU 1207 N ARG A 213 3838 4500 2791 401 -730 968 N ATOM 1208 CA ARG A 213 52.961 -0.677 64.712 1.00 30.81 C ANISOU 1208 CA ARG A 213 4002 4817 2887 508 -904 1049 C ATOM 1209 C ARG A 213 53.736 -1.935 64.354 1.00 37.77 C ANISOU 1209 C ARG A 213 4816 5583 3950 519 -981 1104 C ATOM 1210 O ARG A 213 53.193 -2.861 63.755 1.00 35.47 O ANISOU 1210 O ARG A 213 4540 5165 3772 474 -932 1248 O ATOM 1211 CB ARG A 213 51.692 -1.026 65.495 1.00 31.23 C ANISOU 1211 CB ARG A 213 4142 4984 2742 585 -867 1325 C ATOM 1212 CG ARG A 213 51.945 -1.408 66.945 1.00 33.63 C ANISOU 1212 CG ARG A 213 4459 5499 2821 822 -977 1448 C ATOM 1213 CD ARG A 213 50.656 -1.393 67.752 1.00 47.79 C ANISOU 1213 CD ARG A 213 6357 7316 4484 885 -820 1641 C ATOM 1214 NE ARG A 213 49.802 -2.538 67.450 1.00 62.30 N ANISOU 1214 NE ARG A 213 8166 8954 6550 830 -665 1921 N ATOM 1215 CZ ARG A 213 48.595 -2.730 67.975 1.00 69.36 C ANISOU 1215 CZ ARG A 213 9081 9796 7477 855 -477 2105 C ATOM 1216 NH1 ARG A 213 48.092 -1.848 68.828 1.00 69.19 N ANISOU 1216 NH1 ARG A 213 9148 9903 7236 931 -421 2037 N ATOM 1217 NH2 ARG A 213 47.890 -3.804 67.644 1.00 70.86 N ANISOU 1217 NH2 ARG A 213 9163 9794 7968 812 -339 2371 N ATOM 1218 N TRP A 214 55.013 -1.960 64.712 1.00 49.61 N ANISOU 1218 N TRP A 214 6210 7116 5523 584 -1110 947 N ATOM 1219 CA TRP A 214 55.861 -3.094 64.379 1.00 53.07 C ANISOU 1219 CA TRP A 214 6576 7441 6147 613 -1168 997 C ATOM 1220 C TRP A 214 56.212 -3.905 65.620 1.00 60.79 C ANISOU 1220 C TRP A 214 7524 8592 6983 837 -1318 1159 C ATOM 1221 O TRP A 214 56.412 -3.358 66.698 1.00 61.99 O ANISOU 1221 O TRP A 214 7655 9001 6897 1007 -1457 1071 O ATOM 1222 CB TRP A 214 57.133 -2.621 63.671 1.00 41.27 C ANISOU 1222 CB TRP A 214 4951 5824 4904 551 -1158 734 C ATOM 1223 CG TRP A 214 56.863 -2.006 62.339 1.00 42.87 C ANISOU 1223 CG TRP A 214 5208 5854 5227 437 -932 674 C ATOM 1224 CD1 TRP A 214 56.859 -0.677 62.039 1.00 35.55 C ANISOU 1224 CD1 TRP A 214 4260 4884 4363 389 -770 532 C ATOM 1225 CD2 TRP A 214 56.540 -2.694 61.123 1.00 37.13 C ANISOU 1225 CD2 TRP A 214 4564 4991 4554 423 -823 756 C ATOM 1226 NE1 TRP A 214 56.561 -0.493 60.713 1.00 33.45 N ANISOU 1226 NE1 TRP A 214 4083 4492 4135 392 -537 591 N ATOM 1227 CE2 TRP A 214 56.359 -1.715 60.128 1.00 37.85 C ANISOU 1227 CE2 TRP A 214 4707 5024 4651 426 -602 691 C ATOM 1228 CE3 TRP A 214 56.386 -4.042 60.780 1.00 43.43 C ANISOU 1228 CE3 TRP A 214 5382 5706 5413 441 -883 854 C ATOM 1229 CZ2 TRP A 214 56.036 -2.039 58.812 1.00 36.17 C ANISOU 1229 CZ2 TRP A 214 4589 4756 4399 505 -482 709 C ATOM 1230 CZ3 TRP A 214 56.065 -4.360 59.471 1.00 39.41 C ANISOU 1230 CZ3 TRP A 214 4937 5101 4936 460 -793 795 C ATOM 1231 CH2 TRP A 214 55.892 -3.363 58.506 1.00 31.36 C ANISOU 1231 CH2 TRP A 214 3991 4107 3818 520 -616 719 C ATOM 1232 N GLY A 215 56.281 -5.219 65.456 1.00 48.96 N ANISOU 1232 N GLY A 215 6018 6959 5625 884 -1277 1389 N ATOM 1233 CA GLY A 215 56.654 -6.105 66.542 1.00 56.11 C ANISOU 1233 CA GLY A 215 6900 8005 6412 1165 -1345 1632 C ATOM 1234 C GLY A 215 58.122 -6.484 66.498 1.00 61.53 C ANISOU 1234 C GLY A 215 7446 8708 7224 1261 -1496 1494 C ATOM 1235 O GLY A 215 58.476 -7.660 66.597 1.00 69.72 O ANISOU 1235 O GLY A 215 8455 9654 8381 1394 -1453 1730 O ATOM 1236 N GLY A 216 58.982 -5.485 66.336 1.00 56.90 N ANISOU 1236 N GLY A 216 6740 8200 6678 1193 -1643 1112 N ATOM 1237 CA GLY A 216 60.407 -5.723 66.206 1.00 61.50 C ANISOU 1237 CA GLY A 216 7130 8771 7464 1255 -1781 930 C ATOM 1238 C GLY A 216 61.092 -4.593 65.467 1.00 58.72 C ANISOU 1238 C GLY A 216 6627 8292 7393 1044 -1773 533 C ATOM 1239 O GLY A 216 60.439 -3.650 65.021 1.00 59.01 O ANISOU 1239 O GLY A 216 6734 8245 7442 869 -1636 433 O ATOM 1240 N GLU A 217 62.411 -4.688 65.338 1.00 55.95 N ANISOU 1240 N GLU A 217 6046 7902 7310 1082 -1878 335 N ATOM 1241 CA GLU A 217 63.194 -3.665 64.658 1.00 61.74 C ANISOU 1241 CA GLU A 217 6569 8445 8446 905 -1797 -10 C ATOM 1242 C GLU A 217 63.534 -4.078 63.231 1.00 60.99 C ANISOU 1242 C GLU A 217 6508 8006 8658 770 -1510 109 C ATOM 1243 O GLU A 217 63.930 -3.249 62.413 1.00 77.03 O ANISOU 1243 O GLU A 217 8437 9815 11015 643 -1289 -44 O ATOM 1244 CB GLU A 217 64.480 -3.375 65.432 1.00 70.85 C ANISOU 1244 CB GLU A 217 7368 9760 9791 1042 -2091 -375 C ATOM 1245 CG GLU A 217 64.292 -2.496 66.652 1.00 83.98 C ANISOU 1245 CG GLU A 217 8930 11750 11230 1174 -2378 -702 C ATOM 1246 CD GLU A 217 65.060 -1.196 66.538 1.00 95.28 C ANISOU 1246 CD GLU A 217 9999 13025 13178 1016 -2400 -1242 C ATOM 1247 OE1 GLU A 217 65.176 -0.674 65.409 1.00 95.82 O ANISOU 1247 OE1 GLU A 217 10027 12688 13693 760 -2035 -1227 O ATOM 1248 OE2 GLU A 217 65.556 -0.703 67.574 1.00100.14 O ANISOU 1248 OE2 GLU A 217 10351 13917 13780 1184 -2766 -1692 O ATOM 1249 N ILE A 218 63.373 -5.363 62.940 1.00 43.24 N ANISOU 1249 N ILE A 218 4400 5705 6324 837 -1479 388 N ATOM 1250 CA ILE A 218 63.760 -5.910 61.644 1.00 44.32 C ANISOU 1250 CA ILE A 218 4576 5561 6703 780 -1252 459 C ATOM 1251 C ILE A 218 62.650 -5.758 60.605 1.00 40.82 C ANISOU 1251 C ILE A 218 4378 4995 6139 681 -1024 547 C ATOM 1252 O ILE A 218 62.902 -5.393 59.449 1.00 48.20 O ANISOU 1252 O ILE A 218 5338 5758 7219 663 -784 496 O ATOM 1253 CB ILE A 218 64.137 -7.396 61.769 1.00 47.01 C ANISOU 1253 CB ILE A 218 4926 5867 7067 912 -1323 658 C ATOM 1254 CG1 ILE A 218 65.077 -7.602 62.959 1.00 57.63 C ANISOU 1254 CG1 ILE A 218 6047 7438 8412 1104 -1592 612 C ATOM 1255 CG2 ILE A 218 64.767 -7.897 60.482 1.00 47.48 C ANISOU 1255 CG2 ILE A 218 4990 5653 7399 892 -1112 655 C ATOM 1256 CD1 ILE A 218 65.525 -9.031 63.146 1.00 67.59 C ANISOU 1256 CD1 ILE A 218 7304 8665 9713 1288 -1620 859 C ATOM 1257 N TYR A 219 61.422 -6.039 61.030 1.00 40.30 N ANISOU 1257 N TYR A 219 4476 5035 5801 665 -1090 686 N ATOM 1258 CA TYR A 219 60.256 -5.963 60.155 1.00 39.45 C ANISOU 1258 CA TYR A 219 4558 4864 5569 598 -948 726 C ATOM 1259 C TYR A 219 60.083 -4.601 59.461 1.00 45.20 C ANISOU 1259 C TYR A 219 5320 5582 6270 559 -756 609 C ATOM 1260 O TYR A 219 59.882 -4.565 58.248 1.00 43.46 O ANISOU 1260 O TYR A 219 5205 5275 6033 613 -574 597 O ATOM 1261 CB TYR A 219 58.986 -6.318 60.937 1.00 44.66 C ANISOU 1261 CB TYR A 219 5311 5634 6025 579 -1041 885 C ATOM 1262 CG TYR A 219 58.979 -7.720 61.500 1.00 51.91 C ANISOU 1262 CG TYR A 219 6204 6489 7032 656 -1109 1086 C ATOM 1263 CD1 TYR A 219 59.549 -7.996 62.736 1.00 68.89 C ANISOU 1263 CD1 TYR A 219 8271 8788 9116 807 -1231 1221 C ATOM 1264 CD2 TYR A 219 58.397 -8.769 60.798 1.00 52.44 C ANISOU 1264 CD2 TYR A 219 6309 6345 7271 619 -1039 1125 C ATOM 1265 CE1 TYR A 219 59.543 -9.277 63.256 1.00 80.56 C ANISOU 1265 CE1 TYR A 219 9732 10190 10688 941 -1212 1487 C ATOM 1266 CE2 TYR A 219 58.386 -10.054 61.310 1.00 64.02 C ANISOU 1266 CE2 TYR A 219 7721 7671 8933 689 -1022 1333 C ATOM 1267 CZ TYR A 219 58.961 -10.301 62.540 1.00 81.45 C ANISOU 1267 CZ TYR A 219 9872 10012 11062 860 -1075 1563 C ATOM 1268 OH TYR A 219 58.955 -11.577 63.056 1.00 89.91 O ANISOU 1268 OH TYR A 219 10896 10928 12337 993 -982 1850 O ATOM 1269 N PRO A 220 60.160 -3.479 60.212 1.00 48.61 N ANISOU 1269 N PRO A 220 5663 6107 6699 511 -777 516 N ATOM 1270 CA PRO A 220 60.001 -2.201 59.503 1.00 40.71 C ANISOU 1270 CA PRO A 220 4682 5027 5759 492 -508 451 C ATOM 1271 C PRO A 220 61.105 -1.946 58.476 1.00 42.40 C ANISOU 1271 C PRO A 220 4796 5019 6297 558 -231 414 C ATOM 1272 O PRO A 220 60.828 -1.417 57.395 1.00 52.06 O ANISOU 1272 O PRO A 220 6133 6162 7487 659 79 494 O ATOM 1273 CB PRO A 220 60.056 -1.162 60.631 1.00 42.06 C ANISOU 1273 CB PRO A 220 4716 5288 5977 422 -604 293 C ATOM 1274 CG PRO A 220 60.756 -1.842 61.750 1.00 39.86 C ANISOU 1274 CG PRO A 220 4288 5144 5713 464 -923 210 C ATOM 1275 CD PRO A 220 60.331 -3.272 61.663 1.00 36.82 C ANISOU 1275 CD PRO A 220 4053 4800 5135 524 -1018 449 C ATOM 1276 N LYS A 221 62.334 -2.327 58.812 1.00 34.91 N ANISOU 1276 N LYS A 221 5550 3933 3782 676 -461 789 N ATOM 1277 CA LYS A 221 63.457 -2.178 57.893 1.00 38.26 C ANISOU 1277 CA LYS A 221 5773 4474 4290 832 -537 762 C ATOM 1278 C LYS A 221 63.205 -2.949 56.599 1.00 36.69 C ANISOU 1278 C LYS A 221 5537 4262 4141 904 -499 726 C ATOM 1279 O LYS A 221 63.339 -2.400 55.498 1.00 27.77 O ANISOU 1279 O LYS A 221 4200 3254 3098 934 -446 692 O ATOM 1280 CB LYS A 221 64.758 -2.652 58.547 1.00 34.37 C ANISOU 1280 CB LYS A 221 5329 3982 3748 982 -715 787 C ATOM 1281 CG LYS A 221 65.153 -1.870 59.793 1.00 31.80 C ANISOU 1281 CG LYS A 221 5046 3678 3358 897 -784 826 C ATOM 1282 CD LYS A 221 66.499 -2.337 60.331 1.00 34.31 C ANISOU 1282 CD LYS A 221 5360 4047 3630 1056 -985 857 C ATOM 1283 CE LYS A 221 66.791 -1.762 61.713 1.00 43.06 C ANISOU 1283 CE LYS A 221 6587 5135 4640 945 -1080 903 C ATOM 1284 NZ LYS A 221 66.927 -0.280 61.703 1.00 44.30 N ANISOU 1284 NZ LYS A 221 6594 5420 4818 783 -1038 899 N ATOM 1285 N MET A 222 62.826 -4.217 56.740 1.00 29.64 N ANISOU 1285 N MET A 222 4886 3202 3172 914 -529 734 N ATOM 1286 CA MET A 222 62.545 -5.056 55.579 1.00 29.83 C ANISOU 1286 CA MET A 222 4958 3170 3205 960 -507 701 C ATOM 1287 C MET A 222 61.397 -4.496 54.743 1.00 35.55 C ANISOU 1287 C MET A 222 5542 3975 3992 791 -369 683 C ATOM 1288 O MET A 222 61.503 -4.381 53.515 1.00 42.19 O ANISOU 1288 O MET A 222 6247 4885 4898 850 -340 645 O ATOM 1289 CB MET A 222 62.224 -6.486 56.017 1.00 41.27 C ANISOU 1289 CB MET A 222 6774 4386 4519 945 -570 721 C ATOM 1290 CG MET A 222 63.406 -7.221 56.630 1.00 59.89 C ANISOU 1290 CG MET A 222 9305 6650 6801 1185 -728 735 C ATOM 1291 SD MET A 222 63.032 -8.932 57.058 1.00 77.28 S ANISOU 1291 SD MET A 222 12034 8521 8806 1178 -811 757 S ATOM 1292 CE MET A 222 61.796 -8.707 58.334 1.00 72.29 C ANISOU 1292 CE MET A 222 11547 7826 8093 819 -736 814 C ATOM 1293 N TYR A 223 60.307 -4.135 55.414 1.00 33.34 N ANISOU 1293 N TYR A 223 5287 3700 3679 594 -284 713 N ATOM 1294 CA TYR A 223 59.129 -3.637 54.717 1.00 33.35 C ANISOU 1294 CA TYR A 223 5141 3809 3723 453 -161 708 C ATOM 1295 C TYR A 223 59.419 -2.362 53.945 1.00 32.26 C ANISOU 1295 C TYR A 223 4736 3829 3693 532 -114 678 C ATOM 1296 O TYR A 223 58.910 -2.173 52.845 1.00 31.95 O ANISOU 1296 O TYR A 223 4574 3862 3702 510 -65 657 O ATOM 1297 CB TYR A 223 57.974 -3.377 55.686 1.00 29.76 C ANISOU 1297 CB TYR A 223 4720 3385 3201 268 -63 750 C ATOM 1298 CG TYR A 223 56.751 -2.815 54.988 1.00 36.14 C ANISOU 1298 CG TYR A 223 5328 4357 4047 161 58 751 C ATOM 1299 CD1 TYR A 223 55.876 -3.650 54.304 1.00 47.14 C ANISOU 1299 CD1 TYR A 223 6746 5762 5405 9 70 761 C ATOM 1300 CD2 TYR A 223 56.481 -1.451 54.995 1.00 33.94 C ANISOU 1300 CD2 TYR A 223 4854 4221 3820 216 147 746 C ATOM 1301 CE1 TYR A 223 54.763 -3.147 53.654 1.00 49.28 C ANISOU 1301 CE1 TYR A 223 6800 6220 5704 -81 161 770 C ATOM 1302 CE2 TYR A 223 55.369 -0.937 54.345 1.00 40.13 C ANISOU 1302 CE2 TYR A 223 5451 5169 4629 166 246 751 C ATOM 1303 CZ TYR A 223 54.514 -1.792 53.677 1.00 48.14 C ANISOU 1303 CZ TYR A 223 6440 6230 5619 20 249 766 C ATOM 1304 OH TYR A 223 53.405 -1.293 53.029 1.00 48.59 O ANISOU 1304 OH TYR A 223 6279 6489 5695 -26 328 779 O ATOM 1305 N HIS A 224 60.221 -1.476 54.522 1.00 25.76 N ANISOU 1305 N HIS A 224 3848 3050 2888 603 -140 680 N ATOM 1306 CA HIS A 224 60.458 -0.193 53.877 1.00 36.83 C ANISOU 1306 CA HIS A 224 5054 4579 4361 637 -95 659 C ATOM 1307 C HIS A 224 61.515 -0.293 52.785 1.00 37.33 C ANISOU 1307 C HIS A 224 5001 4698 4484 756 -151 624 C ATOM 1308 O HIS A 224 61.477 0.466 51.808 1.00 30.33 O ANISOU 1308 O HIS A 224 3972 3902 3648 759 -100 601 O ATOM 1309 CB HIS A 224 60.831 0.859 54.915 1.00 28.22 C ANISOU 1309 CB HIS A 224 3983 3506 3235 616 -100 678 C ATOM 1310 CG HIS A 224 59.644 1.425 55.629 1.00 35.71 C ANISOU 1310 CG HIS A 224 4991 4449 4127 531 13 699 C ATOM 1311 ND1 HIS A 224 58.889 2.456 55.112 1.00 33.93 N ANISOU 1311 ND1 HIS A 224 4667 4306 3919 533 118 689 N ATOM 1312 CD2 HIS A 224 59.059 1.082 56.801 1.00 38.34 C ANISOU 1312 CD2 HIS A 224 5474 4718 4374 460 46 731 C ATOM 1313 CE1 HIS A 224 57.902 2.736 55.944 1.00 32.99 C ANISOU 1313 CE1 HIS A 224 4614 4191 3729 494 216 712 C ATOM 1314 NE2 HIS A 224 57.983 1.917 56.977 1.00 32.29 N ANISOU 1314 NE2 HIS A 224 4672 4020 3576 433 183 737 N ATOM 1315 N ILE A 225 62.445 -1.233 52.938 1.00 31.09 N ANISOU 1315 N ILE A 225 4280 3860 3672 871 -250 622 N ATOM 1316 CA ILE A 225 63.326 -1.574 51.828 1.00 25.87 C ANISOU 1316 CA ILE A 225 3517 3264 3049 1016 -278 587 C ATOM 1317 C ILE A 225 62.484 -2.055 50.647 1.00 34.70 C ANISOU 1317 C ILE A 225 4665 4339 4182 987 -214 556 C ATOM 1318 O ILE A 225 62.614 -1.546 49.526 1.00 29.50 O ANISOU 1318 O ILE A 225 3865 3773 3572 1007 -166 526 O ATOM 1319 CB ILE A 225 64.347 -2.659 52.208 1.00 33.11 C ANISOU 1319 CB ILE A 225 4532 4132 3917 1200 -391 590 C ATOM 1320 CG1 ILE A 225 65.427 -2.080 53.118 1.00 28.02 C ANISOU 1320 CG1 ILE A 225 3782 3600 3264 1242 -479 621 C ATOM 1321 CG2 ILE A 225 64.993 -3.242 50.964 1.00 28.08 C ANISOU 1321 CG2 ILE A 225 3835 3540 3293 1382 -389 547 C ATOM 1322 CD1 ILE A 225 66.430 -3.109 53.585 1.00 35.74 C ANISOU 1322 CD1 ILE A 225 4837 4559 4184 1460 -608 635 C ATOM 1323 N CYS A 226 61.606 -3.022 50.910 1.00 35.20 N ANISOU 1323 N CYS A 226 4928 4260 4185 910 -218 568 N ATOM 1324 CA CYS A 226 60.741 -3.570 49.868 1.00 26.09 C ANISOU 1324 CA CYS A 226 3833 3062 3019 834 -181 548 C ATOM 1325 C CYS A 226 59.859 -2.500 49.230 1.00 37.74 C ANISOU 1325 C CYS A 226 5117 4668 4554 719 -93 548 C ATOM 1326 O CYS A 226 59.709 -2.462 48.012 1.00 33.92 O ANISOU 1326 O CYS A 226 4576 4220 4094 728 -72 518 O ATOM 1327 CB CYS A 226 59.866 -4.690 50.431 1.00 28.98 C ANISOU 1327 CB CYS A 226 4457 3271 3285 695 -206 576 C ATOM 1328 SG CYS A 226 60.768 -6.198 50.838 1.00 46.87 S ANISOU 1328 SG CYS A 226 7056 5316 5437 859 -325 570 S ATOM 1329 N PHE A 227 59.280 -1.632 50.055 1.00 32.94 N ANISOU 1329 N PHE A 227 4435 4124 3956 633 -43 580 N ATOM 1330 CA PHE A 227 58.406 -0.573 49.561 1.00 31.30 C ANISOU 1330 CA PHE A 227 4068 4039 3785 573 38 585 C ATOM 1331 C PHE A 227 59.180 0.377 48.660 1.00 30.83 C ANISOU 1331 C PHE A 227 3879 4054 3782 669 46 553 C ATOM 1332 O PHE A 227 58.689 0.782 47.602 1.00 26.16 O ANISOU 1332 O PHE A 227 3204 3523 3212 658 78 539 O ATOM 1333 CB PHE A 227 57.769 0.201 50.719 1.00 31.92 C ANISOU 1333 CB PHE A 227 4129 4161 3837 519 99 621 C ATOM 1334 CG PHE A 227 56.618 1.074 50.303 1.00 23.45 C ANISOU 1334 CG PHE A 227 2921 3217 2773 490 186 633 C ATOM 1335 CD1 PHE A 227 56.834 2.369 49.862 1.00 22.81 C ANISOU 1335 CD1 PHE A 227 2755 3191 2720 579 216 619 C ATOM 1336 CD2 PHE A 227 55.320 0.596 50.350 1.00 24.27 C ANISOU 1336 CD2 PHE A 227 2986 3396 2839 374 230 665 C ATOM 1337 CE1 PHE A 227 55.773 3.171 49.475 1.00 22.96 C ANISOU 1337 CE1 PHE A 227 2672 3321 2730 603 286 632 C ATOM 1338 CE2 PHE A 227 54.257 1.392 49.966 1.00 27.44 C ANISOU 1338 CE2 PHE A 227 3227 3958 3242 386 302 682 C ATOM 1339 CZ PHE A 227 54.483 2.681 49.528 1.00 29.49 C ANISOU 1339 CZ PHE A 227 3420 4254 3530 527 328 664 C ATOM 1340 N PHE A 228 60.394 0.725 49.081 1.00 22.90 N ANISOU 1340 N PHE A 228 2858 3055 2786 746 8 547 N ATOM 1341 CA PHE A 228 61.246 1.595 48.281 1.00 22.55 C ANISOU 1341 CA PHE A 228 2695 3100 2773 794 16 524 C ATOM 1342 C PHE A 228 61.607 0.962 46.938 1.00 22.77 C ANISOU 1342 C PHE A 228 2691 3143 2817 863 14 485 C ATOM 1343 O PHE A 228 61.593 1.632 45.908 1.00 33.14 O ANISOU 1343 O PHE A 228 3927 4519 4145 854 55 466 O ATOM 1344 CB PHE A 228 62.521 1.954 49.042 1.00 29.60 C ANISOU 1344 CB PHE A 228 3556 4037 3654 826 -39 535 C ATOM 1345 CG PHE A 228 63.509 2.730 48.222 1.00 35.60 C ANISOU 1345 CG PHE A 228 4182 4919 4426 833 -33 518 C ATOM 1346 CD1 PHE A 228 63.229 4.027 47.825 1.00 38.98 C ANISOU 1346 CD1 PHE A 228 4593 5378 4841 746 18 521 C ATOM 1347 CD2 PHE A 228 64.715 2.164 47.842 1.00 39.05 C ANISOU 1347 CD2 PHE A 228 4521 5450 4868 934 -72 503 C ATOM 1348 CE1 PHE A 228 64.132 4.746 47.065 1.00 41.06 C ANISOU 1348 CE1 PHE A 228 4761 5751 5091 707 27 511 C ATOM 1349 CE2 PHE A 228 65.623 2.878 47.083 1.00 40.20 C ANISOU 1349 CE2 PHE A 228 4517 5748 5009 911 -50 494 C ATOM 1350 CZ PHE A 228 65.331 4.171 46.694 1.00 44.25 C ANISOU 1350 CZ PHE A 228 5031 6278 5503 772 -2 499 C ATOM 1351 N LEU A 229 61.931 -0.327 46.951 1.00 30.83 N ANISOU 1351 N LEU A 229 3811 4088 3815 942 -32 472 N ATOM 1352 CA LEU A 229 62.317 -1.024 45.727 1.00 31.53 C ANISOU 1352 CA LEU A 229 3922 4167 3891 1037 -28 429 C ATOM 1353 C LEU A 229 61.152 -1.178 44.755 1.00 38.36 C ANISOU 1353 C LEU A 229 4840 4990 4746 938 2 418 C ATOM 1354 O LEU A 229 61.293 -0.942 43.553 1.00 31.93 O ANISOU 1354 O LEU A 229 3979 4219 3933 963 34 387 O ATOM 1355 CB LEU A 229 62.888 -2.404 46.058 1.00 32.18 C ANISOU 1355 CB LEU A 229 4167 4142 3920 1177 -90 418 C ATOM 1356 CG LEU A 229 64.195 -2.432 46.848 1.00 37.41 C ANISOU 1356 CG LEU A 229 4757 4877 4579 1328 -143 429 C ATOM 1357 CD1 LEU A 229 64.573 -3.864 47.199 1.00 39.92 C ANISOU 1357 CD1 LEU A 229 5292 5054 4820 1500 -215 422 C ATOM 1358 CD2 LEU A 229 65.307 -1.755 46.061 1.00 40.80 C ANISOU 1358 CD2 LEU A 229 4960 5506 5037 1419 -103 407 C ATOM 1359 N VAL A 230 60.001 -1.578 45.286 1.00 41.10 N ANISOU 1359 N VAL A 230 5276 5270 5068 810 -12 448 N ATOM 1360 CA VAL A 230 58.831 -1.876 44.470 1.00 39.76 C ANISOU 1360 CA VAL A 230 5146 5089 4872 684 -8 450 C ATOM 1361 C VAL A 230 58.161 -0.616 43.934 1.00 37.50 C ANISOU 1361 C VAL A 230 4684 4935 4628 635 38 462 C ATOM 1362 O VAL A 230 57.853 -0.530 42.745 1.00 35.31 O ANISOU 1362 O VAL A 230 4391 4684 4342 617 37 444 O ATOM 1363 CB VAL A 230 57.790 -2.700 45.266 1.00 41.51 C ANISOU 1363 CB VAL A 230 5491 5245 5036 523 -36 490 C ATOM 1364 CG1 VAL A 230 56.482 -2.807 44.495 1.00 34.73 C ANISOU 1364 CG1 VAL A 230 4602 4449 4147 349 -40 508 C ATOM 1365 CG2 VAL A 230 58.340 -4.083 45.588 1.00 42.43 C ANISOU 1365 CG2 VAL A 230 5870 5180 5073 565 -99 476 C ATOM 1366 N THR A 231 57.945 0.364 44.806 1.00 36.56 N ANISOU 1366 N THR A 231 4468 4886 4538 630 74 492 N ATOM 1367 CA THR A 231 57.190 1.551 44.417 1.00 28.08 C ANISOU 1367 CA THR A 231 3275 3917 3478 620 115 509 C ATOM 1368 C THR A 231 58.059 2.637 43.797 1.00 25.03 C ANISOU 1368 C THR A 231 2846 3556 3109 701 137 485 C ATOM 1369 O THR A 231 57.543 3.638 43.307 1.00 25.90 O ANISOU 1369 O THR A 231 2910 3720 3209 715 160 494 O ATOM 1370 CB THR A 231 56.443 2.165 45.615 1.00 31.47 C ANISOU 1370 CB THR A 231 3661 4399 3897 601 159 551 C ATOM 1371 OG1 THR A 231 57.386 2.752 46.521 1.00 35.05 O ANISOU 1371 OG1 THR A 231 4153 4808 4354 658 170 549 O ATOM 1372 CG2 THR A 231 55.632 1.103 46.340 1.00 44.48 C ANISOU 1372 CG2 THR A 231 5349 6041 5509 484 152 582 C ATOM 1373 N TYR A 232 59.374 2.454 43.815 1.00 26.50 N ANISOU 1373 N TYR A 232 3050 3716 3304 753 127 459 N ATOM 1374 CA TYR A 232 60.248 3.494 43.290 1.00 33.10 C ANISOU 1374 CA TYR A 232 3838 4603 4135 777 152 445 C ATOM 1375 C TYR A 232 61.405 2.948 42.461 1.00 38.63 C ANISOU 1375 C TYR A 232 4515 5331 4832 834 154 406 C ATOM 1376 O TYR A 232 61.384 3.032 41.236 1.00 47.58 O ANISOU 1376 O TYR A 232 5650 6482 5947 837 178 382 O ATOM 1377 CB TYR A 232 60.793 4.355 44.433 1.00 30.85 C ANISOU 1377 CB TYR A 232 3551 4331 3841 757 153 469 C ATOM 1378 CG TYR A 232 61.463 5.630 43.967 1.00 33.53 C ANISOU 1378 CG TYR A 232 3882 4715 4144 716 175 467 C ATOM 1379 CD1 TYR A 232 60.721 6.780 43.736 1.00 33.53 C ANISOU 1379 CD1 TYR A 232 3953 4688 4101 699 201 482 C ATOM 1380 CD2 TYR A 232 62.835 5.681 43.757 1.00 31.57 C ANISOU 1380 CD2 TYR A 232 3564 4547 3884 694 168 456 C ATOM 1381 CE1 TYR A 232 61.326 7.947 43.308 1.00 35.81 C ANISOU 1381 CE1 TYR A 232 4300 4981 4324 636 214 484 C ATOM 1382 CE2 TYR A 232 63.449 6.843 43.330 1.00 33.39 C ANISOU 1382 CE2 TYR A 232 3802 4828 4057 599 188 462 C ATOM 1383 CZ TYR A 232 62.690 7.974 43.107 1.00 40.85 C ANISOU 1383 CZ TYR A 232 4875 5698 4948 557 208 475 C ATOM 1384 OH TYR A 232 63.298 9.135 42.681 1.00 39.28 O ANISOU 1384 OH TYR A 232 4748 5514 4661 438 221 484 O ATOM 1385 N MET A 233 62.402 2.383 43.134 1.00 27.42 N ANISOU 1385 N MET A 233 3073 3927 3417 895 131 403 N ATOM 1386 CA MET A 233 63.692 2.102 42.510 1.00 30.61 C ANISOU 1386 CA MET A 233 3402 4422 3808 984 149 373 C ATOM 1387 C MET A 233 63.638 1.198 41.274 1.00 35.54 C ANISOU 1387 C MET A 233 4092 5009 4404 1069 174 328 C ATOM 1388 O MET A 233 64.042 1.618 40.190 1.00 47.83 O ANISOU 1388 O MET A 233 5600 6639 5934 1070 230 305 O ATOM 1389 CB MET A 233 64.643 1.488 43.536 1.00 30.12 C ANISOU 1389 CB MET A 233 3300 4396 3747 1079 99 384 C ATOM 1390 CG MET A 233 66.115 1.688 43.201 1.00 41.13 C ANISOU 1390 CG MET A 233 4522 5982 5123 1149 119 375 C ATOM 1391 SD MET A 233 66.620 3.425 43.240 1.00 61.33 S ANISOU 1391 SD MET A 233 6953 8688 7663 944 143 408 S ATOM 1392 CE MET A 233 66.555 3.885 41.507 1.00 63.38 C ANISOU 1392 CE MET A 233 7202 8991 7887 904 242 373 C ATOM 1393 N ALA A 234 63.154 -0.032 41.432 1.00 32.52 N ANISOU 1393 N ALA A 234 3855 4497 4003 1124 134 317 N ATOM 1394 CA ALA A 234 63.180 -1.007 40.336 1.00 36.16 C ANISOU 1394 CA ALA A 234 4446 4886 4406 1211 149 271 C ATOM 1395 C ALA A 234 62.405 -0.556 39.082 1.00 44.38 C ANISOU 1395 C ALA A 234 5517 5918 5426 1108 176 257 C ATOM 1396 O ALA A 234 62.967 -0.564 37.975 1.00 52.19 O ANISOU 1396 O ALA A 234 6512 6946 6371 1175 231 218 O ATOM 1397 CB ALA A 234 62.663 -2.367 40.825 1.00 26.49 C ANISOU 1397 CB ALA A 234 3444 3484 3135 1237 83 270 C ATOM 1398 N PRO A 235 61.127 -0.151 39.238 1.00 38.48 N ANISOU 1398 N PRO A 235 4781 5139 4700 958 140 291 N ATOM 1399 CA PRO A 235 60.412 0.297 38.037 1.00 38.93 C ANISOU 1399 CA PRO A 235 4857 5206 4728 880 145 285 C ATOM 1400 C PRO A 235 61.020 1.556 37.424 1.00 47.60 C ANISOU 1400 C PRO A 235 5848 6408 5829 887 207 280 C ATOM 1401 O PRO A 235 60.943 1.737 36.210 1.00 53.19 O ANISOU 1401 O PRO A 235 6606 7117 6486 873 227 258 O ATOM 1402 CB PRO A 235 59.001 0.575 38.555 1.00 29.84 C ANISOU 1402 CB PRO A 235 3678 4059 3600 752 94 334 C ATOM 1403 CG PRO A 235 59.195 0.869 40.001 1.00 22.79 C ANISOU 1403 CG PRO A 235 2711 3189 2758 766 102 365 C ATOM 1404 CD PRO A 235 60.278 -0.043 40.439 1.00 32.48 C ANISOU 1404 CD PRO A 235 4003 4361 3976 867 100 339 C ATOM 1405 N LEU A 236 61.619 2.408 38.252 1.00 44.46 N ANISOU 1405 N LEU A 236 5338 6086 5469 885 230 304 N ATOM 1406 CA LEU A 236 62.274 3.611 37.754 1.00 41.57 C ANISOU 1406 CA LEU A 236 4908 5809 5078 845 283 306 C ATOM 1407 C LEU A 236 63.476 3.242 36.895 1.00 45.30 C ANISOU 1407 C LEU A 236 5346 6363 5505 913 352 264 C ATOM 1408 O LEU A 236 63.656 3.780 35.803 1.00 45.80 O ANISOU 1408 O LEU A 236 5431 6461 5510 871 403 250 O ATOM 1409 CB LEU A 236 62.710 4.514 38.907 1.00 48.02 C ANISOU 1409 CB LEU A 236 5650 6677 5918 796 280 342 C ATOM 1410 CG LEU A 236 62.703 6.014 38.616 1.00 52.43 C ANISOU 1410 CG LEU A 236 6240 7256 6427 693 301 365 C ATOM 1411 CD1 LEU A 236 61.281 6.492 38.367 1.00 55.63 C ANISOU 1411 CD1 LEU A 236 6741 7575 6822 694 269 384 C ATOM 1412 CD2 LEU A 236 63.341 6.786 39.758 1.00 49.93 C ANISOU 1412 CD2 LEU A 236 5891 6976 6102 622 291 396 C ATOM 1413 N CYS A 237 64.294 2.321 37.394 1.00 30.48 N ANISOU 1413 N CYS A 237 3419 4522 3639 1034 358 247 N ATOM 1414 CA CYS A 237 65.450 1.833 36.650 1.00 35.44 C ANISOU 1414 CA CYS A 237 3992 5260 4215 1159 436 206 C ATOM 1415 C CYS A 237 65.031 1.233 35.315 1.00 33.41 C ANISOU 1415 C CYS A 237 3899 4909 3888 1204 470 160 C ATOM 1416 O CYS A 237 65.574 1.584 34.259 1.00 39.95 O ANISOU 1416 O CYS A 237 4704 5824 4649 1203 557 135 O ATOM 1417 CB CYS A 237 66.213 0.793 37.468 1.00 47.36 C ANISOU 1417 CB CYS A 237 5457 6802 5737 1343 416 198 C ATOM 1418 SG CYS A 237 66.972 1.441 38.964 1.00 64.52 S ANISOU 1418 SG CYS A 237 7427 9122 7967 1295 368 252 S ATOM 1419 N LEU A 238 64.055 0.332 35.372 1.00 26.64 N ANISOU 1419 N LEU A 238 3220 3874 3028 1216 397 151 N ATOM 1420 CA LEU A 238 63.562 -0.327 34.167 1.00 35.18 C ANISOU 1420 CA LEU A 238 4504 4841 4023 1228 401 110 C ATOM 1421 C LEU A 238 63.030 0.679 33.147 1.00 32.23 C ANISOU 1421 C LEU A 238 4137 4489 3620 1088 414 119 C ATOM 1422 O LEU A 238 63.344 0.595 31.958 1.00 36.58 O ANISOU 1422 O LEU A 238 4775 5041 4081 1117 477 80 O ATOM 1423 CB LEU A 238 62.480 -1.345 34.527 1.00 33.71 C ANISOU 1423 CB LEU A 238 4511 4471 3826 1184 296 116 C ATOM 1424 CG LEU A 238 63.021 -2.539 35.318 1.00 45.37 C ANISOU 1424 CG LEU A 238 6086 5868 5283 1344 278 99 C ATOM 1425 CD1 LEU A 238 61.908 -3.499 35.713 1.00 52.02 C ANISOU 1425 CD1 LEU A 238 7153 6520 6090 1235 171 115 C ATOM 1426 CD2 LEU A 238 64.096 -3.254 34.508 1.00 35.81 C ANISOU 1426 CD2 LEU A 238 4975 4660 3973 1574 365 36 C ATOM 1427 N MET A 239 62.241 1.637 33.620 1.00 31.09 N ANISOU 1427 N MET A 239 3921 4357 3535 956 358 170 N ATOM 1428 CA MET A 239 61.678 2.662 32.748 1.00 28.09 C ANISOU 1428 CA MET A 239 3571 3985 3116 852 350 187 C ATOM 1429 C MET A 239 62.756 3.559 32.152 1.00 35.44 C ANISOU 1429 C MET A 239 4444 5025 3995 836 455 177 C ATOM 1430 O MET A 239 62.626 4.021 31.021 1.00 47.64 O ANISOU 1430 O MET A 239 6085 6558 5458 783 477 167 O ATOM 1431 CB MET A 239 60.659 3.512 33.504 1.00 29.82 C ANISOU 1431 CB MET A 239 3733 4201 3394 773 275 245 C ATOM 1432 CG MET A 239 59.293 2.871 33.629 1.00 24.04 C ANISOU 1432 CG MET A 239 3051 3408 2676 730 173 266 C ATOM 1433 SD MET A 239 58.101 4.006 34.354 1.00 47.94 S ANISOU 1433 SD MET A 239 5979 6487 5747 693 114 334 S ATOM 1434 CE MET A 239 58.559 3.917 36.086 1.00 44.86 C ANISOU 1434 CE MET A 239 5489 6114 5441 724 145 350 C ATOM 1435 N VAL A 240 63.814 3.809 32.916 1.00 37.12 N ANISOU 1435 N VAL A 240 4504 5358 4241 859 511 184 N ATOM 1436 CA VAL A 240 64.920 4.623 32.427 1.00 31.17 C ANISOU 1436 CA VAL A 240 3667 4753 3423 798 614 183 C ATOM 1437 C VAL A 240 65.647 3.894 31.304 1.00 34.97 C ANISOU 1437 C VAL A 240 4175 5295 3816 898 720 128 C ATOM 1438 O VAL A 240 65.908 4.475 30.248 1.00 39.26 O ANISOU 1438 O VAL A 240 4773 5881 4263 818 794 119 O ATOM 1439 CB VAL A 240 65.911 4.980 33.555 1.00 33.30 C ANISOU 1439 CB VAL A 240 3740 5176 3738 775 632 211 C ATOM 1440 CG1 VAL A 240 67.250 5.410 32.979 1.00 32.72 C ANISOU 1440 CG1 VAL A 240 3532 5320 3580 719 753 205 C ATOM 1441 CG2 VAL A 240 65.330 6.078 34.436 1.00 28.66 C ANISOU 1441 CG2 VAL A 240 3180 4527 3184 640 557 264 C ATOM 1442 N LEU A 241 65.956 2.619 31.528 1.00 40.63 N ANISOU 1442 N LEU A 241 4890 6000 4547 1084 730 90 N ATOM 1443 CA LEU A 241 66.580 1.795 30.491 1.00 41.52 C ANISOU 1443 CA LEU A 241 5076 6143 4555 1236 836 29 C ATOM 1444 C LEU A 241 65.728 1.762 29.220 1.00 41.61 C ANISOU 1444 C LEU A 241 5336 5997 4477 1168 822 4 C ATOM 1445 O LEU A 241 66.223 1.992 28.105 1.00 45.56 O ANISOU 1445 O LEU A 241 5884 6563 4865 1161 933 -24 O ATOM 1446 CB LEU A 241 66.807 0.373 31.003 1.00 45.83 C ANISOU 1446 CB LEU A 241 5677 6627 5112 1472 818 -6 C ATOM 1447 CG LEU A 241 67.734 0.220 32.210 1.00 52.74 C ANISOU 1447 CG LEU A 241 6320 7664 6056 1589 821 16 C ATOM 1448 CD1 LEU A 241 67.833 -1.239 32.624 1.00 56.39 C ANISOU 1448 CD1 LEU A 241 6919 8007 6498 1846 786 -19 C ATOM 1449 CD2 LEU A 241 69.110 0.788 31.903 1.00 54.64 C ANISOU 1449 CD2 LEU A 241 6296 8215 6249 1617 960 18 C ATOM 1450 N ALA A 242 64.441 1.484 29.406 1.00 40.55 N ANISOU 1450 N ALA A 242 5349 5676 4381 1103 683 20 N ATOM 1451 CA ALA A 242 63.493 1.407 28.301 1.00 32.97 C ANISOU 1451 CA ALA A 242 4615 4576 3337 1020 626 8 C ATOM 1452 C ALA A 242 63.445 2.711 27.517 1.00 36.99 C ANISOU 1452 C ALA A 242 5121 5140 3792 881 655 33 C ATOM 1453 O ALA A 242 63.477 2.704 26.288 1.00 39.96 O ANISOU 1453 O ALA A 242 5657 5481 4046 862 700 3 O ATOM 1454 CB ALA A 242 62.106 1.054 28.819 1.00 28.55 C ANISOU 1454 CB ALA A 242 4130 3881 2836 937 460 42 C ATOM 1455 N TYR A 243 63.383 3.829 28.232 1.00 29.35 N ANISOU 1455 N TYR A 243 4014 4241 2897 785 629 87 N ATOM 1456 CA TYR A 243 63.239 5.130 27.593 1.00 28.47 C ANISOU 1456 CA TYR A 243 3962 4139 2716 650 634 119 C ATOM 1457 C TYR A 243 64.526 5.637 26.955 1.00 40.47 C ANISOU 1457 C TYR A 243 5442 5800 4134 600 795 102 C ATOM 1458 O TYR A 243 64.474 6.453 26.038 1.00 42.95 O ANISOU 1458 O TYR A 243 5890 6094 4337 487 819 113 O ATOM 1459 CB TYR A 243 62.721 6.159 28.598 1.00 30.32 C ANISOU 1459 CB TYR A 243 4123 4367 3029 578 552 181 C ATOM 1460 CG TYR A 243 61.215 6.214 28.673 1.00 30.77 C ANISOU 1460 CG TYR A 243 4260 4313 3120 583 401 213 C ATOM 1461 CD1 TYR A 243 60.443 6.180 27.518 1.00 36.55 C ANISOU 1461 CD1 TYR A 243 5156 4969 3763 562 335 211 C ATOM 1462 CD2 TYR A 243 60.563 6.289 29.895 1.00 29.96 C ANISOU 1462 CD2 TYR A 243 4053 4206 3124 610 326 250 C ATOM 1463 CE1 TYR A 243 59.065 6.227 27.578 1.00 26.87 C ANISOU 1463 CE1 TYR A 243 3952 3699 2559 567 188 250 C ATOM 1464 CE2 TYR A 243 59.183 6.335 29.966 1.00 35.94 C ANISOU 1464 CE2 TYR A 243 4833 4921 3902 622 202 286 C ATOM 1465 CZ TYR A 243 58.441 6.303 28.803 1.00 32.95 C ANISOU 1465 CZ TYR A 243 4581 4500 3439 601 129 288 C ATOM 1466 OH TYR A 243 57.069 6.348 28.868 1.00 40.45 O ANISOU 1466 OH TYR A 243 5505 5463 4403 614 -3 332 O ATOM 1467 N LEU A 244 65.680 5.175 27.429 1.00 39.31 N ANISOU 1467 N LEU A 244 5107 5816 4012 680 904 80 N ATOM 1468 CA LEU A 244 66.928 5.579 26.789 1.00 43.63 C ANISOU 1468 CA LEU A 244 5567 6561 4448 625 1072 68 C ATOM 1469 C LEU A 244 67.143 4.748 25.524 1.00 44.44 C ANISOU 1469 C LEU A 244 5810 6646 4428 742 1176 3 C ATOM 1470 O LEU A 244 67.647 5.257 24.514 1.00 44.08 O ANISOU 1470 O LEU A 244 5823 6680 4244 648 1294 -5 O ATOM 1471 CB LEU A 244 68.121 5.465 27.750 1.00 44.16 C ANISOU 1471 CB LEU A 244 5337 6870 4574 670 1147 79 C ATOM 1472 CG LEU A 244 68.503 4.166 28.462 1.00 54.77 C ANISOU 1472 CG LEU A 244 6550 8263 5997 924 1148 45 C ATOM 1473 CD1 LEU A 244 69.328 3.242 27.575 1.00 73.31 C ANISOU 1473 CD1 LEU A 244 8889 10726 8238 1130 1304 -19 C ATOM 1474 CD2 LEU A 244 69.252 4.480 29.749 1.00 49.61 C ANISOU 1474 CD2 LEU A 244 5623 7797 5429 896 1130 89 C ATOM 1475 N GLN A 245 66.741 3.479 25.567 1.00 39.70 N ANISOU 1475 N GLN A 245 5305 5923 3856 933 1131 -42 N ATOM 1476 CA GLN A 245 66.750 2.666 24.352 1.00 35.11 C ANISOU 1476 CA GLN A 245 4946 5258 3134 1041 1203 -106 C ATOM 1477 C GLN A 245 65.784 3.251 23.321 1.00 34.77 C ANISOU 1477 C GLN A 245 5158 5051 3002 873 1123 -93 C ATOM 1478 O GLN A 245 66.098 3.330 22.128 1.00 46.85 O ANISOU 1478 O GLN A 245 6839 6587 4373 853 1228 -125 O ATOM 1479 CB GLN A 245 66.386 1.216 24.664 1.00 36.51 C ANISOU 1479 CB GLN A 245 5254 5283 3336 1243 1138 -151 C ATOM 1480 CG GLN A 245 67.389 0.512 25.559 1.00 52.65 C ANISOU 1480 CG GLN A 245 7097 7474 5435 1467 1216 -169 C ATOM 1481 CD GLN A 245 66.915 -0.856 25.999 1.00 65.63 C ANISOU 1481 CD GLN A 245 8933 8914 7091 1643 1122 -203 C ATOM 1482 OE1 GLN A 245 66.421 -1.644 25.193 1.00 68.05 O ANISOU 1482 OE1 GLN A 245 9555 9021 7280 1690 1100 -250 O ATOM 1483 NE2 GLN A 245 67.054 -1.143 27.288 1.00 73.38 N ANISOU 1483 NE2 GLN A 245 9760 9928 8195 1719 1057 -176 N ATOM 1484 N ILE A 246 64.612 3.667 23.797 1.00 33.06 N ANISOU 1484 N ILE A 246 4983 4704 2876 768 938 -43 N ATOM 1485 CA ILE A 246 63.614 4.325 22.961 1.00 32.84 C ANISOU 1485 CA ILE A 246 5159 4546 2773 631 827 -15 C ATOM 1486 C ILE A 246 64.168 5.617 22.365 1.00 41.00 C ANISOU 1486 C ILE A 246 6212 5662 3705 489 919 12 C ATOM 1487 O ILE A 246 63.975 5.891 21.184 1.00 44.79 O ANISOU 1487 O ILE A 246 6911 6071 4037 420 929 3 O ATOM 1488 CB ILE A 246 62.323 4.637 23.755 1.00 36.81 C ANISOU 1488 CB ILE A 246 5628 4961 3398 581 625 44 C ATOM 1489 CG1 ILE A 246 61.508 3.363 23.981 1.00 40.89 C ANISOU 1489 CG1 ILE A 246 6213 5367 3955 644 510 25 C ATOM 1490 CG2 ILE A 246 61.464 5.660 23.024 1.00 34.35 C ANISOU 1490 CG2 ILE A 246 5469 4575 3008 468 518 90 C ATOM 1491 CD1 ILE A 246 60.282 3.572 24.850 1.00 34.41 C ANISOU 1491 CD1 ILE A 246 5301 4521 3251 594 335 86 C ATOM 1492 N PHE A 247 64.857 6.403 23.185 1.00 36.40 N ANISOU 1492 N PHE A 247 5428 5218 3182 421 977 48 N ATOM 1493 CA PHE A 247 65.480 7.638 22.720 1.00 37.57 C ANISOU 1493 CA PHE A 247 5614 5448 3213 238 1067 80 C ATOM 1494 C PHE A 247 66.460 7.355 21.591 1.00 41.80 C ANISOU 1494 C PHE A 247 6195 6103 3584 228 1264 32 C ATOM 1495 O PHE A 247 66.422 8.008 20.545 1.00 51.21 O ANISOU 1495 O PHE A 247 7598 7244 4614 95 1299 41 O ATOM 1496 CB PHE A 247 66.197 8.356 23.870 1.00 40.20 C ANISOU 1496 CB PHE A 247 5722 5932 3622 144 1100 123 C ATOM 1497 CG PHE A 247 67.089 9.483 23.419 1.00 51.88 C ANISOU 1497 CG PHE A 247 7229 7533 4951 -89 1219 154 C ATOM 1498 CD1 PHE A 247 66.569 10.745 23.182 1.00 56.47 C ANISOU 1498 CD1 PHE A 247 8051 7969 5438 -264 1135 207 C ATOM 1499 CD2 PHE A 247 68.450 9.282 23.235 1.00 58.18 C ANISOU 1499 CD2 PHE A 247 7821 8603 5682 -134 1413 135 C ATOM 1500 CE1 PHE A 247 67.386 11.783 22.766 1.00 63.15 C ANISOU 1500 CE1 PHE A 247 8977 8903 6115 -521 1238 240 C ATOM 1501 CE2 PHE A 247 69.270 10.315 22.818 1.00 64.11 C ANISOU 1501 CE2 PHE A 247 8591 9495 6275 -403 1526 172 C ATOM 1502 CZ PHE A 247 68.737 11.567 22.585 1.00 61.08 C ANISOU 1502 CZ PHE A 247 8492 8929 5788 -618 1435 225 C ATOM 1503 N ARG A 248 67.336 6.378 21.808 1.00 41.08 N ANISOU 1503 N ARG A 248 5916 6173 3521 388 1397 -17 N ATOM 1504 CA ARG A 248 68.337 6.028 20.808 1.00 46.53 C ANISOU 1504 CA ARG A 248 6610 7020 4049 431 1615 -66 C ATOM 1505 C ARG A 248 67.673 5.551 19.518 1.00 53.61 C ANISOU 1505 C ARG A 248 7852 7711 4805 476 1597 -112 C ATOM 1506 O ARG A 248 68.165 5.817 18.421 1.00 53.83 O ANISOU 1506 O ARG A 248 8007 7797 4649 402 1744 -132 O ATOM 1507 CB ARG A 248 69.284 4.952 21.343 1.00 55.89 C ANISOU 1507 CB ARG A 248 7541 8405 5289 678 1740 -112 C ATOM 1508 CG ARG A 248 70.687 5.038 20.765 1.00 80.03 C ANISOU 1508 CG ARG A 248 10417 11787 8203 684 2000 -132 C ATOM 1509 CD ARG A 248 71.544 3.850 21.174 1.00 96.51 C ANISOU 1509 CD ARG A 248 12282 14066 10321 1013 2117 -183 C ATOM 1510 NE ARG A 248 72.955 4.071 20.863 1.00105.45 N ANISOU 1510 NE ARG A 248 13122 15606 11339 1015 2363 -183 N ATOM 1511 CZ ARG A 248 73.882 3.118 20.863 1.00103.45 C ANISOU 1511 CZ ARG A 248 12686 15541 11080 1305 2490 -235 C ATOM 1512 NH1 ARG A 248 73.552 1.866 21.149 1.00 99.21 N ANISOU 1512 NH1 ARG A 248 12279 14814 10604 1635 2415 -291 N ATOM 1513 NH2 ARG A 248 75.141 3.416 20.570 1.00105.01 N ANISOU 1513 NH2 ARG A 248 12608 16044 11248 1224 2639 -229 N ATOM 1514 N LYS A 249 66.546 4.858 19.658 1.00 46.15 N ANISOU 1514 N LYS A 249 7066 6535 3934 570 1414 -125 N ATOM 1515 CA LYS A 249 65.817 4.332 18.506 1.00 48.23 C ANISOU 1515 CA LYS A 249 7671 6594 4061 589 1355 -163 C ATOM 1516 C LYS A 249 65.132 5.437 17.695 1.00 48.68 C ANISOU 1516 C LYS A 249 7945 6538 4013 381 1258 -115 C ATOM 1517 O LYS A 249 65.251 5.488 16.472 1.00 45.10 O ANISOU 1517 O LYS A 249 7734 6035 3367 332 1332 -141 O ATOM 1518 CB LYS A 249 64.780 3.307 18.972 1.00 54.11 C ANISOU 1518 CB LYS A 249 8505 7150 4904 692 1165 -176 C ATOM 1519 CG LYS A 249 64.032 2.599 17.855 1.00 61.77 C ANISOU 1519 CG LYS A 249 9838 7910 5722 692 1082 -215 C ATOM 1520 CD LYS A 249 64.749 1.334 17.419 1.00 66.60 C ANISOU 1520 CD LYS A 249 10590 8500 6215 898 1236 -305 C ATOM 1521 CE LYS A 249 63.861 0.484 16.522 1.00 64.79 C ANISOU 1521 CE LYS A 249 10762 8016 5838 877 1107 -342 C ATOM 1522 NZ LYS A 249 64.584 -0.694 15.970 1.00 65.05 N ANISOU 1522 NZ LYS A 249 11022 7990 5706 1096 1272 -437 N ATOM 1523 N LEU A 250 64.421 6.322 18.387 1.00 47.47 N ANISOU 1523 N LEU A 250 7727 6338 3970 279 1095 -44 N ATOM 1524 CA LEU A 250 63.603 7.347 17.743 1.00 44.85 C ANISOU 1524 CA LEU A 250 7622 5874 3544 137 959 10 C ATOM 1525 C LEU A 250 64.391 8.553 17.245 1.00 45.36 C ANISOU 1525 C LEU A 250 7760 6014 3462 -41 1092 39 C ATOM 1526 O LEU A 250 64.077 9.113 16.192 1.00 51.72 O ANISOU 1526 O LEU A 250 8850 6707 4093 -142 1059 54 O ATOM 1527 CB LEU A 250 62.517 7.834 18.705 1.00 36.01 C ANISOU 1527 CB LEU A 250 6419 4684 2580 145 741 74 C ATOM 1528 CG LEU A 250 61.152 7.149 18.656 1.00 35.40 C ANISOU 1528 CG LEU A 250 6414 4481 2555 216 522 82 C ATOM 1529 CD1 LEU A 250 60.222 7.778 19.678 1.00 33.99 C ANISOU 1529 CD1 LEU A 250 6098 4298 2519 238 353 151 C ATOM 1530 CD2 LEU A 250 60.556 7.242 17.263 1.00 36.76 C ANISOU 1530 CD2 LEU A 250 6899 4528 2539 156 433 83 C ATOM 1531 N TRP A 251 65.404 8.963 17.998 1.00 39.12 N ANISOU 1531 N TRP A 251 6728 5412 2724 -103 1231 52 N ATOM 1532 CA TRP A 251 66.100 10.204 17.691 1.00 42.64 C ANISOU 1532 CA TRP A 251 7246 5931 3025 -336 1333 96 C ATOM 1533 C TRP A 251 67.402 9.994 16.911 1.00 47.54 C ANISOU 1533 C TRP A 251 7812 6766 3483 -411 1604 55 C ATOM 1534 O TRP A 251 67.748 10.790 16.033 1.00 62.03 O ANISOU 1534 O TRP A 251 9852 8603 5112 -615 1692 77 O ATOM 1535 CB TRP A 251 66.380 10.956 18.984 1.00 45.09 C ANISOU 1535 CB TRP A 251 7353 6325 3455 -424 1300 149 C ATOM 1536 CG TRP A 251 65.156 11.335 19.714 1.00 54.90 C ANISOU 1536 CG TRP A 251 8664 7377 4819 -350 1066 192 C ATOM 1537 CD1 TRP A 251 64.450 10.572 20.626 1.00 55.41 C ANISOU 1537 CD1 TRP A 251 8556 7410 5086 -161 945 182 C ATOM 1538 CD2 TRP A 251 64.452 12.588 19.615 1.00 60.08 C ANISOU 1538 CD2 TRP A 251 9589 7852 5385 -446 927 256 C ATOM 1539 NE1 TRP A 251 63.359 11.292 21.092 1.00 49.56 N ANISOU 1539 NE1 TRP A 251 7924 6516 4391 -135 755 236 N ATOM 1540 CE2 TRP A 251 63.342 12.522 20.490 1.00 60.15 C ANISOU 1540 CE2 TRP A 251 9540 7758 5556 -281 738 280 C ATOM 1541 CE3 TRP A 251 64.655 13.753 18.877 1.00 58.67 C ANISOU 1541 CE3 TRP A 251 9717 7587 4988 -648 948 297 C ATOM 1542 CZ2 TRP A 251 62.437 13.585 20.644 1.00 63.38 C ANISOU 1542 CZ2 TRP A 251 10168 7997 5918 -265 574 340 C ATOM 1543 CZ3 TRP A 251 63.751 14.800 19.036 1.00 67.09 C ANISOU 1543 CZ3 TRP A 251 11046 8444 6003 -639 769 357 C ATOM 1544 CH2 TRP A 251 62.656 14.706 19.912 1.00 68.16 C ANISOU 1544 CH2 TRP A 251 11097 8496 6306 -426 587 376 C ATOM 1545 N CYS A 252 68.110 8.912 17.215 1.00 56.51 N ANISOU 1545 N CYS A 252 8689 8088 4696 -233 1741 -2 N ATOM 1546 CA CYS A 252 69.429 8.697 16.635 1.00 57.38 C ANISOU 1546 CA CYS A 252 8665 8475 4662 -258 2020 -36 C ATOM 1547 C CYS A 252 69.400 7.790 15.409 1.00 64.27 C ANISOU 1547 C CYS A 252 9758 9279 5382 -104 2126 -113 C ATOM 1548 O CYS A 252 70.115 8.032 14.436 1.00 71.43 O ANISOU 1548 O CYS A 252 10748 10313 6080 -207 2329 -128 O ATOM 1549 CB CYS A 252 70.372 8.120 17.689 1.00 62.38 C ANISOU 1549 CB CYS A 252 8867 9397 5438 -121 2125 -49 C ATOM 1550 SG CYS A 252 70.534 9.150 19.166 1.00 69.39 S ANISOU 1550 SG CYS A 252 9506 10380 6478 -322 2010 38 S ATOM 1551 N ARG A 253 68.572 6.752 15.451 1.00 68.21 N ANISOU 1551 N ARG A 253 11016 10248 4654 39 1485 93 N ATOM 1552 CA ARG A 253 68.552 5.762 14.379 1.00 50.82 C ANISOU 1552 CA ARG A 253 8762 7909 2637 -7 1396 260 C ATOM 1553 C ARG A 253 67.383 5.946 13.409 1.00 58.40 C ANISOU 1553 C ARG A 253 9642 8771 3776 -11 1584 267 C ATOM 1554 O ARG A 253 67.478 5.572 12.240 1.00 57.77 O ANISOU 1554 O ARG A 253 9552 8536 3863 -41 1455 315 O ATOM 1555 CB ARG A 253 68.532 4.355 14.976 1.00 51.91 C ANISOU 1555 CB ARG A 253 8968 8085 2670 -86 1416 524 C ATOM 1556 CG ARG A 253 69.877 3.928 15.548 1.00 62.94 C ANISOU 1556 CG ARG A 253 10430 9530 3954 -82 1170 579 C ATOM 1557 CD ARG A 253 69.789 2.599 16.278 1.00 77.99 C ANISOU 1557 CD ARG A 253 12410 11483 5741 -146 1214 846 C ATOM 1558 NE ARG A 253 68.992 2.698 17.497 1.00 92.93 N ANISOU 1558 NE ARG A 253 14353 13551 7406 -174 1457 884 N ATOM 1559 CZ ARG A 253 68.836 1.708 18.371 1.00 99.22 C ANISOU 1559 CZ ARG A 253 15217 14432 8049 -233 1529 1114 C ATOM 1560 NH1 ARG A 253 69.427 0.539 18.162 1.00 97.02 N ANISOU 1560 NH1 ARG A 253 14966 14062 7836 -265 1368 1323 N ATOM 1561 NH2 ARG A 253 68.092 1.888 19.454 1.00106.35 N ANISOU 1561 NH2 ARG A 253 16168 15502 8738 -253 1776 1140 N ATOM 1562 N GLN A 254 66.285 6.519 13.889 1.00 64.18 N ANISOU 1562 N GLN A 254 10322 9587 4474 20 1905 236 N ATOM 1563 CA GLN A 254 65.165 6.842 13.012 1.00 61.17 C ANISOU 1563 CA GLN A 254 9820 9131 4290 28 2128 269 C ATOM 1564 C GLN A 254 65.226 8.302 12.587 1.00 65.96 C ANISOU 1564 C GLN A 254 10369 9699 4995 163 2126 -3 C ATOM 1565 O GLN A 254 65.953 9.102 13.179 1.00 67.48 O ANISOU 1565 O GLN A 254 10625 9933 5082 229 2006 -207 O ATOM 1566 CB GLN A 254 63.827 6.555 13.694 1.00 73.19 C ANISOU 1566 CB GLN A 254 11232 10761 5815 2 2549 468 C ATOM 1567 CG GLN A 254 63.486 5.084 13.819 1.00 76.37 C ANISOU 1567 CG GLN A 254 11650 11157 6212 -175 2581 801 C ATOM 1568 CD GLN A 254 62.135 4.856 14.464 1.00 95.74 C ANISOU 1568 CD GLN A 254 13910 13725 8740 -211 3011 1043 C ATOM 1569 OE1 GLN A 254 61.260 5.721 14.420 1.00109.64 O ANISOU 1569 OE1 GLN A 254 15458 15533 10666 -99 3310 1013 O ATOM 1570 NE2 GLN A 254 61.958 3.689 15.073 1.00104.38 N ANISOU 1570 NE2 GLN A 254 15037 14865 9756 -353 3044 1307 N ATOM 1571 N GLY A1001 64.457 8.644 11.559 1.00 57.08 N ANISOU 1571 N GLY A1001 9125 8481 4081 187 2260 21 N ATOM 1572 CA GLY A1001 64.394 10.012 11.088 1.00 60.12 C ANISOU 1572 CA GLY A1001 9418 8810 4616 328 2268 -211 C ATOM 1573 C GLY A1001 65.007 10.186 9.716 1.00 68.62 C ANISOU 1573 C GLY A1001 10431 9732 5910 292 1893 -282 C ATOM 1574 O GLY A1001 65.615 9.265 9.170 1.00 69.77 O ANISOU 1574 O GLY A1001 10655 9809 6046 182 1638 -181 O ATOM 1575 N ILE A1002 64.848 11.382 9.161 1.00 61.17 N ANISOU 1575 N ILE A1002 9367 8721 5156 402 1885 -450 N ATOM 1576 CA ILE A1002 65.346 11.692 7.830 1.00 57.85 C ANISOU 1576 CA ILE A1002 8880 8158 4943 383 1565 -511 C ATOM 1577 C ILE A1002 65.423 13.205 7.667 1.00 51.31 C ANISOU 1577 C ILE A1002 8021 7276 4198 535 1603 -741 C ATOM 1578 O ILE A1002 64.545 13.928 8.137 1.00 68.82 O ANISOU 1578 O ILE A1002 10120 9520 6508 650 1888 -783 O ATOM 1579 CB ILE A1002 64.443 11.074 6.733 1.00 60.85 C ANISOU 1579 CB ILE A1002 8992 8451 5678 255 1448 -301 C ATOM 1580 CG1 ILE A1002 64.929 11.460 5.337 1.00 49.07 C ANISOU 1580 CG1 ILE A1002 7481 6808 4356 244 1135 -371 C ATOM 1581 CG2 ILE A1002 62.991 11.490 6.929 1.00 71.74 C ANISOU 1581 CG2 ILE A1002 10044 9881 7335 291 1717 -188 C ATOM 1582 CD1 ILE A1002 63.999 11.016 4.230 1.00 53.66 C ANISOU 1582 CD1 ILE A1002 7840 7289 5259 102 980 -184 C ATOM 1583 N ASP A1003 66.483 13.686 7.027 1.00 44.52 N ANISOU 1583 N ASP A1003 7273 6330 3313 549 1337 -873 N ATOM 1584 CA ASP A1003 66.622 15.114 6.773 1.00 55.17 C ANISOU 1584 CA ASP A1003 8605 7595 4763 669 1330 -1076 C ATOM 1585 C ASP A1003 65.603 15.555 5.722 1.00 54.39 C ANISOU 1585 C ASP A1003 8188 7403 5073 698 1330 -999 C ATOM 1586 O ASP A1003 65.918 15.634 4.533 1.00 58.35 O ANISOU 1586 O ASP A1003 8621 7806 5743 652 1071 -969 O ATOM 1587 CB ASP A1003 68.046 15.448 6.320 1.00 67.53 C ANISOU 1587 CB ASP A1003 10265 9102 6293 620 1003 -1159 C ATOM 1588 CG ASP A1003 68.387 16.919 6.493 1.00 76.41 C ANISOU 1588 CG ASP A1003 11375 10153 7502 672 971 -1350 C ATOM 1589 OD1 ASP A1003 67.470 17.764 6.401 1.00 78.72 O ANISOU 1589 OD1 ASP A1003 11621 10375 7915 812 1175 -1449 O ATOM 1590 OD2 ASP A1003 69.575 17.230 6.723 1.00 78.82 O ANISOU 1590 OD2 ASP A1003 11717 10462 7768 580 763 -1383 O ATOM 1591 N CYS A1004 64.384 15.837 6.172 1.00 48.36 N ANISOU 1591 N CYS A1004 7230 6677 4467 780 1628 -942 N ATOM 1592 CA CYS A1004 63.292 16.214 5.279 1.00 50.70 C ANISOU 1592 CA CYS A1004 7169 6906 5189 804 1633 -808 C ATOM 1593 C CYS A1004 63.549 17.538 4.567 1.00 52.19 C ANISOU 1593 C CYS A1004 7326 6953 5551 921 1522 -964 C ATOM 1594 O CYS A1004 63.047 17.764 3.465 1.00 53.28 O ANISOU 1594 O CYS A1004 7222 7010 6010 894 1359 -844 O ATOM 1595 CB CYS A1004 61.974 16.297 6.053 1.00 52.73 C ANISOU 1595 CB CYS A1004 7193 7246 5595 905 2034 -683 C ATOM 1596 SG CYS A1004 61.306 14.702 6.566 1.00 66.19 S ANISOU 1596 SG CYS A1004 8793 9100 7258 725 2141 -384 S ATOM 1597 N SER A1005 64.330 18.410 5.197 1.00 42.57 N ANISOU 1597 N SER A1005 6369 5694 4113 1030 1584 -1216 N ATOM 1598 CA SER A1005 64.639 19.712 4.614 1.00 50.41 C ANISOU 1598 CA SER A1005 7366 6528 5259 1132 1483 -1369 C ATOM 1599 C SER A1005 65.600 19.580 3.436 1.00 55.04 C ANISOU 1599 C SER A1005 7988 7050 5875 1009 1090 -1344 C ATOM 1600 O SER A1005 65.718 20.492 2.617 1.00 60.48 O ANISOU 1600 O SER A1005 8605 7608 6765 1058 958 -1385 O ATOM 1601 CB SER A1005 65.228 20.650 5.671 1.00 55.34 C ANISOU 1601 CB SER A1005 8309 7098 5618 1246 1633 -1648 C ATOM 1602 OG SER A1005 66.471 20.167 6.152 1.00 55.47 O ANISOU 1602 OG SER A1005 8578 7189 5308 1090 1422 -1709 O ATOM 1603 N PHE A1006 66.283 18.440 3.352 1.00 46.16 N ANISOU 1603 N PHE A1006 6982 6007 4550 867 928 -1261 N ATOM 1604 CA PHE A1006 67.242 18.198 2.279 1.00 39.13 C ANISOU 1604 CA PHE A1006 6155 5058 3655 780 617 -1219 C ATOM 1605 C PHE A1006 66.682 17.271 1.205 1.00 51.16 C ANISOU 1605 C PHE A1006 7541 6562 5336 669 471 -1007 C ATOM 1606 O PHE A1006 66.881 17.497 0.011 1.00 48.62 O ANISOU 1606 O PHE A1006 7187 6142 5146 642 264 -960 O ATOM 1607 CB PHE A1006 68.538 17.609 2.841 1.00 32.06 C ANISOU 1607 CB PHE A1006 5513 4233 2434 725 529 -1260 C ATOM 1608 CG PHE A1006 69.533 17.222 1.784 1.00 29.67 C ANISOU 1608 CG PHE A1006 5266 3880 2129 670 277 -1178 C ATOM 1609 CD1 PHE A1006 70.378 18.168 1.231 1.00 28.75 C ANISOU 1609 CD1 PHE A1006 5146 3682 2095 692 136 -1234 C ATOM 1610 CD2 PHE A1006 69.625 15.912 1.346 1.00 39.43 C ANISOU 1610 CD2 PHE A1006 6549 5134 3301 592 205 -1019 C ATOM 1611 CE1 PHE A1006 71.294 17.817 0.256 1.00 35.71 C ANISOU 1611 CE1 PHE A1006 6026 4527 3015 647 -34 -1105 C ATOM 1612 CE2 PHE A1006 70.539 15.554 0.372 1.00 39.53 C ANISOU 1612 CE2 PHE A1006 6624 5081 3314 573 33 -934 C ATOM 1613 CZ PHE A1006 71.374 16.509 -0.173 1.00 37.21 C ANISOU 1613 CZ PHE A1006 6269 4732 3136 601 -66 -958 C ATOM 1614 N TRP A1007 65.988 16.221 1.633 1.00 50.44 N ANISOU 1614 N TRP A1007 7399 6553 5215 587 569 -872 N ATOM 1615 CA TRP A1007 65.484 15.220 0.702 1.00 37.84 C ANISOU 1615 CA TRP A1007 5735 4913 3731 435 394 -672 C ATOM 1616 C TRP A1007 64.084 15.554 0.197 1.00 42.57 C ANISOU 1616 C TRP A1007 6010 5482 4682 406 398 -525 C ATOM 1617 O TRP A1007 63.116 14.883 0.548 1.00 52.13 O ANISOU 1617 O TRP A1007 7056 6753 5997 318 491 -357 O ATOM 1618 CB TRP A1007 65.482 13.835 1.357 1.00 33.49 C ANISOU 1618 CB TRP A1007 5300 4436 2990 325 453 -566 C ATOM 1619 CG TRP A1007 66.841 13.366 1.789 1.00 45.05 C ANISOU 1619 CG TRP A1007 7051 5927 4138 350 419 -648 C ATOM 1620 CD1 TRP A1007 67.322 13.311 3.065 1.00 40.88 C ANISOU 1620 CD1 TRP A1007 6645 5515 3371 403 581 -723 C ATOM 1621 CD2 TRP A1007 67.895 12.887 0.944 1.00 29.96 C ANISOU 1621 CD2 TRP A1007 5336 3925 2122 331 214 -634 C ATOM 1622 NE1 TRP A1007 68.607 12.827 3.067 1.00 32.52 N ANISOU 1622 NE1 TRP A1007 5803 4452 2100 406 456 -733 N ATOM 1623 CE2 TRP A1007 68.983 12.560 1.777 1.00 29.51 C ANISOU 1623 CE2 TRP A1007 5459 3944 1809 381 259 -676 C ATOM 1624 CE3 TRP A1007 68.024 12.703 -0.435 1.00 37.33 C ANISOU 1624 CE3 TRP A1007 6325 4717 3141 286 9 -577 C ATOM 1625 CZ2 TRP A1007 70.182 12.060 1.278 1.00 28.09 C ANISOU 1625 CZ2 TRP A1007 5409 3709 1556 398 129 -625 C ATOM 1626 CZ3 TRP A1007 69.217 12.207 -0.930 1.00 36.60 C ANISOU 1626 CZ3 TRP A1007 6463 4560 2884 325 -85 -570 C ATOM 1627 CH2 TRP A1007 70.279 11.891 -0.076 1.00 33.89 C ANISOU 1627 CH2 TRP A1007 6202 4300 2376 389 -10 -578 C ATOM 1628 N ASN A1008 63.977 16.594 -0.624 1.00 40.18 N ANISOU 1628 N ASN A1008 5594 5087 4584 474 289 -556 N ATOM 1629 CA ASN A1008 62.715 16.899 -1.288 1.00 57.68 C ANISOU 1629 CA ASN A1008 7485 7265 7165 435 221 -369 C ATOM 1630 C ASN A1008 62.944 17.436 -2.700 1.00 54.60 C ANISOU 1630 C ASN A1008 7113 6743 6891 403 -83 -343 C ATOM 1631 O ASN A1008 64.032 17.908 -3.029 1.00 37.62 O ANISOU 1631 O ASN A1008 5176 4534 4582 470 -155 -496 O ATOM 1632 CB ASN A1008 61.887 17.888 -0.461 1.00 66.38 C ANISOU 1632 CB ASN A1008 8323 8411 8486 626 540 -389 C ATOM 1633 CG ASN A1008 62.584 19.213 -0.261 1.00 70.31 C ANISOU 1633 CG ASN A1008 8940 8834 8942 825 630 -630 C ATOM 1634 OD1 ASN A1008 62.407 20.143 -1.046 1.00 75.41 O ANISOU 1634 OD1 ASN A1008 9463 9370 9820 892 518 -615 O ATOM 1635 ND2 ASN A1008 63.377 19.312 0.799 1.00 74.29 N ANISOU 1635 ND2 ASN A1008 9698 9384 9146 903 810 -841 N ATOM 1636 N GLU A1009 61.906 17.353 -3.527 1.00 65.02 N ANISOU 1636 N GLU A1009 8196 8020 8487 287 -269 -121 N ATOM 1637 CA GLU A1009 62.015 17.625 -4.958 1.00 65.13 C ANISOU 1637 CA GLU A1009 8269 7910 8567 203 -607 -49 C ATOM 1638 C GLU A1009 62.348 19.083 -5.281 1.00 54.04 C ANISOU 1638 C GLU A1009 6805 6436 7290 390 -584 -154 C ATOM 1639 O GLU A1009 62.893 19.376 -6.347 1.00 41.67 O ANISOU 1639 O GLU A1009 5395 4772 5665 358 -814 -157 O ATOM 1640 CB GLU A1009 60.710 17.218 -5.657 1.00 81.08 C ANISOU 1640 CB GLU A1009 10027 9909 10872 6 -845 247 C ATOM 1641 CG GLU A1009 60.792 17.121 -7.179 1.00 94.14 C ANISOU 1641 CG GLU A1009 11845 11429 12494 -160 -1261 347 C ATOM 1642 CD GLU A1009 60.506 18.440 -7.877 1.00100.52 C ANISOU 1642 CD GLU A1009 12450 12178 13564 -49 -1361 406 C ATOM 1643 OE1 GLU A1009 59.931 19.345 -7.235 1.00104.43 O ANISOU 1643 OE1 GLU A1009 12601 12722 14355 134 -1132 429 O ATOM 1644 OE2 GLU A1009 60.860 18.571 -9.068 1.00 95.04 O ANISOU 1644 OE2 GLU A1009 11963 11377 12769 -131 -1653 435 O ATOM 1645 N SER A1010 62.034 19.989 -4.358 1.00 50.54 N ANISOU 1645 N SER A1010 6171 6025 7006 589 -293 -238 N ATOM 1646 CA SER A1010 62.171 21.426 -4.600 1.00 47.95 C ANISOU 1646 CA SER A1010 5770 5595 6855 770 -258 -320 C ATOM 1647 C SER A1010 63.575 21.844 -5.037 1.00 41.77 C ANISOU 1647 C SER A1010 5302 4735 5833 791 -372 -499 C ATOM 1648 O SER A1010 63.742 22.843 -5.736 1.00 55.54 O ANISOU 1648 O SER A1010 7017 6365 7720 858 -479 -496 O ATOM 1649 CB SER A1010 61.776 22.213 -3.347 1.00 57.04 C ANISOU 1649 CB SER A1010 6786 6763 8122 996 129 -440 C ATOM 1650 OG SER A1010 60.417 21.993 -3.010 1.00 60.29 O ANISOU 1650 OG SER A1010 6840 7243 8825 1020 281 -227 O ATOM 1651 N TYR A1011 64.581 21.075 -4.635 1.00 38.48 N ANISOU 1651 N TYR A1011 5164 4381 5078 733 -348 -621 N ATOM 1652 CA TYR A1011 65.964 21.416 -4.949 1.00 47.66 C ANISOU 1652 CA TYR A1011 6578 5492 6039 757 -427 -749 C ATOM 1653 C TYR A1011 66.366 21.009 -6.365 1.00 50.16 C ANISOU 1653 C TYR A1011 7034 5745 6280 647 -697 -624 C ATOM 1654 O TYR A1011 67.317 21.552 -6.929 1.00 48.66 O ANISOU 1654 O TYR A1011 6975 5491 6022 685 -770 -663 O ATOM 1655 CB TYR A1011 66.904 20.776 -3.929 1.00 40.95 C ANISOU 1655 CB TYR A1011 5938 4739 4883 755 -294 -888 C ATOM 1656 CG TYR A1011 66.797 21.407 -2.564 1.00 47.65 C ANISOU 1656 CG TYR A1011 6758 5621 5724 872 -42 -1055 C ATOM 1657 CD1 TYR A1011 67.569 22.510 -2.227 1.00 51.90 C ANISOU 1657 CD1 TYR A1011 7396 6082 6240 959 -15 -1222 C ATOM 1658 CD2 TYR A1011 65.910 20.914 -1.617 1.00 59.76 C ANISOU 1658 CD2 TYR A1011 8195 7250 7263 887 169 -1039 C ATOM 1659 CE1 TYR A1011 67.469 23.099 -0.980 1.00 63.82 C ANISOU 1659 CE1 TYR A1011 8964 7589 7695 1056 204 -1399 C ATOM 1660 CE2 TYR A1011 65.802 21.496 -0.368 1.00 63.80 C ANISOU 1660 CE2 TYR A1011 8744 7780 7716 1010 432 -1202 C ATOM 1661 CZ TYR A1011 66.584 22.588 -0.055 1.00 60.40 C ANISOU 1661 CZ TYR A1011 8469 7252 7226 1094 441 -1397 C ATOM 1662 OH TYR A1011 66.482 23.170 1.185 1.00 66.67 O ANISOU 1662 OH TYR A1011 9385 8032 7916 1206 690 -1583 O ATOM 1663 N LEU A1012 65.642 20.056 -6.939 1.00 43.78 N ANISOU 1663 N LEU A1012 6218 4943 5473 502 -844 -466 N ATOM 1664 CA LEU A1012 65.912 19.630 -8.305 1.00 49.99 C ANISOU 1664 CA LEU A1012 7209 5643 6143 389 -1101 -356 C ATOM 1665 C LEU A1012 65.215 20.557 -9.291 1.00 56.82 C ANISOU 1665 C LEU A1012 7908 6419 7262 379 -1295 -220 C ATOM 1666 O LEU A1012 64.168 21.126 -8.986 1.00 62.07 O ANISOU 1666 O LEU A1012 8253 7096 8236 413 -1267 -142 O ATOM 1667 CB LEU A1012 65.461 18.185 -8.521 1.00 44.37 C ANISOU 1667 CB LEU A1012 6634 4933 5289 205 -1219 -253 C ATOM 1668 CG LEU A1012 66.024 17.160 -7.535 1.00 37.67 C ANISOU 1668 CG LEU A1012 5939 4163 4212 209 -1037 -347 C ATOM 1669 CD1 LEU A1012 65.581 15.763 -7.920 1.00 35.42 C ANISOU 1669 CD1 LEU A1012 5835 3826 3799 12 -1187 -234 C ATOM 1670 CD2 LEU A1012 67.540 17.247 -7.469 1.00 34.73 C ANISOU 1670 CD2 LEU A1012 5801 3791 3604 334 -933 -474 C ATOM 1671 N THR A1013 65.800 20.709 -10.473 1.00 52.73 N ANISOU 1671 N THR A1013 6634 5210 8190 -415 -569 -657 N ATOM 1672 CA THR A1013 65.227 21.576 -11.493 1.00 53.49 C ANISOU 1672 CA THR A1013 6776 5090 8456 -434 -587 -424 C ATOM 1673 C THR A1013 64.846 20.785 -12.738 1.00 52.33 C ANISOU 1673 C THR A1013 6684 5105 8095 -433 -578 -168 C ATOM 1674 O THR A1013 65.462 19.766 -13.052 1.00 54.46 O ANISOU 1674 O THR A1013 6962 5582 8149 -495 -527 -148 O ATOM 1675 CB THR A1013 66.199 22.701 -11.889 1.00 55.21 C ANISOU 1675 CB THR A1013 6984 5057 8938 -588 -548 -359 C ATOM 1676 OG1 THR A1013 67.419 22.129 -12.378 1.00 52.28 O ANISOU 1676 OG1 THR A1013 6578 4838 8446 -735 -479 -296 O ATOM 1677 CG2 THR A1013 66.504 23.587 -10.689 1.00 59.14 C ANISOU 1677 CG2 THR A1013 7411 5397 9661 -598 -569 -670 C ATOM 1678 N GLY A1014 63.826 21.261 -13.442 1.00 54.04 N ANISOU 1678 N GLY A1014 6931 5240 8363 -341 -637 6 N ATOM 1679 CA GLY A1014 63.361 20.607 -14.649 1.00 27.35 C ANISOU 1679 CA GLY A1014 3584 2047 4760 -318 -671 205 C ATOM 1680 C GLY A1014 62.515 19.389 -14.344 1.00 36.69 C ANISOU 1680 C GLY A1014 4710 3455 5774 -266 -692 55 C ATOM 1681 O GLY A1014 62.483 18.912 -13.208 1.00 40.78 O ANISOU 1681 O GLY A1014 5190 3999 6306 -251 -638 -156 O ATOM 1682 N SER A1015 61.825 18.886 -15.362 1.00 34.08 N ANISOU 1682 N SER A1015 4371 3293 5284 -234 -762 158 N ATOM 1683 CA SER A1015 61.002 17.692 -15.218 1.00 31.39 C ANISOU 1683 CA SER A1015 3953 3142 4833 -229 -763 -3 C ATOM 1684 C SER A1015 61.864 16.468 -14.942 1.00 42.41 C ANISOU 1684 C SER A1015 5397 4640 6076 -341 -624 -112 C ATOM 1685 O SER A1015 63.080 16.492 -15.140 1.00 38.33 O ANISOU 1685 O SER A1015 4958 4117 5490 -413 -562 -42 O ATOM 1686 CB SER A1015 60.167 17.461 -16.476 1.00 33.19 C ANISOU 1686 CB SER A1015 4136 3554 4920 -185 -899 85 C ATOM 1687 OG SER A1015 61.000 17.125 -17.572 1.00 35.72 O ANISOU 1687 OG SER A1015 4562 3999 5009 -256 -888 215 O ATOM 1688 N ARG A1016 61.228 15.392 -14.493 1.00 40.37 N ANISOU 1688 N ARG A1016 5085 4465 5789 -349 -553 -274 N ATOM 1689 CA ARG A1016 61.948 14.158 -14.223 1.00 34.16 C ANISOU 1689 CA ARG A1016 4363 3744 4875 -417 -393 -356 C ATOM 1690 C ARG A1016 62.501 13.554 -15.514 1.00 31.28 C ANISOU 1690 C ARG A1016 4063 3509 4312 -503 -401 -290 C ATOM 1691 O ARG A1016 63.570 12.945 -15.508 1.00 31.36 O ANISOU 1691 O ARG A1016 4153 3550 4212 -541 -283 -285 O ATOM 1692 CB ARG A1016 61.044 13.151 -13.509 1.00 26.93 C ANISOU 1692 CB ARG A1016 3386 2833 4014 -408 -267 -514 C ATOM 1693 CG ARG A1016 61.775 11.906 -13.049 1.00 25.60 C ANISOU 1693 CG ARG A1016 3311 2674 3742 -429 -57 -566 C ATOM 1694 CD ARG A1016 60.877 10.974 -12.254 1.00 33.77 C ANISOU 1694 CD ARG A1016 4304 3656 4872 -415 132 -680 C ATOM 1695 NE ARG A1016 61.677 10.074 -11.429 1.00 30.17 N ANISOU 1695 NE ARG A1016 3971 3167 4325 -346 356 -668 N ATOM 1696 CZ ARG A1016 62.046 10.343 -10.182 1.00 19.70 C ANISOU 1696 CZ ARG A1016 2690 1828 2967 -192 431 -647 C ATOM 1697 NH1 ARG A1016 61.671 11.479 -9.609 1.00 22.81 N ANISOU 1697 NH1 ARG A1016 3017 2211 3437 -119 312 -672 N ATOM 1698 NH2 ARG A1016 62.782 9.475 -9.504 1.00 19.09 N ANISOU 1698 NH2 ARG A1016 2728 1760 2766 -84 622 -610 N ATOM 1699 N ASP A1017 61.777 13.729 -16.616 1.00 29.25 N ANISOU 1699 N ASP A1017 3766 3357 3991 -506 -543 -248 N ATOM 1700 CA ASP A1017 62.216 13.213 -17.913 1.00 37.15 C ANISOU 1700 CA ASP A1017 4837 4524 4756 -560 -564 -205 C ATOM 1701 C ASP A1017 63.549 13.818 -18.326 1.00 42.38 C ANISOU 1701 C ASP A1017 5609 5166 5326 -569 -516 -3 C ATOM 1702 O ASP A1017 64.453 13.117 -18.793 1.00 46.55 O ANISOU 1702 O ASP A1017 6215 5781 5692 -623 -406 -4 O ATOM 1703 CB ASP A1017 61.176 13.498 -18.996 1.00 42.70 C ANISOU 1703 CB ASP A1017 5466 5393 5365 -509 -770 -188 C ATOM 1704 CG ASP A1017 59.829 12.895 -18.681 1.00 55.90 C ANISOU 1704 CG ASP A1017 6966 7110 7163 -527 -823 -422 C ATOM 1705 OD1 ASP A1017 59.642 11.687 -18.941 1.00 46.23 O ANISOU 1705 OD1 ASP A1017 5716 5968 5883 -634 -757 -634 O ATOM 1706 OD2 ASP A1017 58.956 13.632 -18.179 1.00 72.77 O ANISOU 1706 OD2 ASP A1017 8982 9185 9481 -439 -912 -407 O ATOM 1707 N GLU A1018 63.657 15.130 -18.151 1.00 31.40 N ANISOU 1707 N GLU A1018 4214 3643 4072 -519 -575 163 N ATOM 1708 CA GLU A1018 64.861 15.858 -18.512 1.00 31.49 C ANISOU 1708 CA GLU A1018 4298 3590 4078 -557 -503 359 C ATOM 1709 C GLU A1018 66.034 15.436 -17.633 1.00 33.19 C ANISOU 1709 C GLU A1018 4502 3757 4350 -629 -356 256 C ATOM 1710 O GLU A1018 67.156 15.260 -18.117 1.00 44.88 O ANISOU 1710 O GLU A1018 6016 5300 5734 -689 -248 335 O ATOM 1711 CB GLU A1018 64.614 17.363 -18.405 1.00 38.05 C ANISOU 1711 CB GLU A1018 5121 4217 5120 -498 -572 530 C ATOM 1712 CG GLU A1018 63.548 17.868 -19.368 1.00 59.75 C ANISOU 1712 CG GLU A1018 7883 7037 7781 -366 -724 691 C ATOM 1713 CD GLU A1018 63.074 19.272 -19.044 1.00 79.03 C ANISOU 1713 CD GLU A1018 10313 9229 10484 -262 -781 831 C ATOM 1714 OE1 GLU A1018 63.534 19.838 -18.030 1.00 83.80 O ANISOU 1714 OE1 GLU A1018 10895 9596 11351 -320 -706 753 O ATOM 1715 OE2 GLU A1018 62.238 19.808 -19.802 1.00 83.10 O ANISOU 1715 OE2 GLU A1018 10841 9795 10939 -104 -906 1005 O ATOM 1716 N ARG A1019 65.766 15.258 -16.343 1.00 29.70 N ANISOU 1716 N ARG A1019 4003 3237 4046 -598 -348 81 N ATOM 1717 CA ARG A1019 66.797 14.830 -15.405 1.00 21.84 C ANISOU 1717 CA ARG A1019 2986 2248 3066 -607 -241 -28 C ATOM 1718 C ARG A1019 67.283 13.424 -15.726 1.00 25.48 C ANISOU 1718 C ARG A1019 3497 2859 3325 -611 -116 -77 C ATOM 1719 O ARG A1019 68.470 13.136 -15.621 1.00 20.01 O ANISOU 1719 O ARG A1019 2794 2227 2580 -620 -24 -73 O ATOM 1720 CB ARG A1019 66.281 14.888 -13.967 1.00 20.95 C ANISOU 1720 CB ARG A1019 2826 2060 3075 -520 -255 -194 C ATOM 1721 CG ARG A1019 66.048 16.294 -13.448 1.00 26.39 C ANISOU 1721 CG ARG A1019 3464 2578 3986 -505 -353 -204 C ATOM 1722 CD ARG A1019 65.665 16.281 -11.976 1.00 37.33 C ANISOU 1722 CD ARG A1019 4813 3935 5434 -395 -348 -398 C ATOM 1723 NE ARG A1019 64.332 16.833 -11.755 1.00 43.79 N ANISOU 1723 NE ARG A1019 5607 4647 6383 -324 -412 -422 N ATOM 1724 CZ ARG A1019 63.294 16.127 -11.324 1.00 33.69 C ANISOU 1724 CZ ARG A1019 4313 3419 5068 -247 -361 -493 C ATOM 1725 NH1 ARG A1019 63.435 14.840 -11.052 1.00 25.43 N ANISOU 1725 NH1 ARG A1019 3302 2489 3871 -235 -229 -535 N ATOM 1726 NH2 ARG A1019 62.116 16.710 -11.154 1.00 52.36 N ANISOU 1726 NH2 ARG A1019 6618 5700 7575 -176 -418 -518 N ATOM 1727 N LYS A1020 66.359 12.550 -16.112 1.00 26.66 N ANISOU 1727 N LYS A1020 3684 3060 3387 -604 -109 -144 N ATOM 1728 CA LYS A1020 66.707 11.179 -16.467 1.00 29.01 C ANISOU 1728 CA LYS A1020 4046 3447 3529 -613 30 -219 C ATOM 1729 C LYS A1020 67.531 11.153 -17.748 1.00 29.05 C ANISOU 1729 C LYS A1020 4103 3575 3359 -663 56 -114 C ATOM 1730 O LYS A1020 68.474 10.367 -17.881 1.00 34.39 O ANISOU 1730 O LYS A1020 4820 4317 3932 -650 199 -135 O ATOM 1731 CB LYS A1020 65.451 10.328 -16.635 1.00 26.60 C ANISOU 1731 CB LYS A1020 3742 3136 3229 -635 35 -362 C ATOM 1732 CG LYS A1020 65.744 8.876 -16.959 1.00 28.69 C ANISOU 1732 CG LYS A1020 4086 3427 3390 -657 208 -477 C ATOM 1733 CD LYS A1020 64.515 8.180 -17.501 1.00 21.50 C ANISOU 1733 CD LYS A1020 3144 2522 2504 -740 183 -653 C ATOM 1734 CE LYS A1020 64.818 6.736 -17.820 1.00 32.82 C ANISOU 1734 CE LYS A1020 4667 3922 3880 -777 381 -803 C ATOM 1735 NZ LYS A1020 63.658 6.047 -18.448 1.00 38.22 N ANISOU 1735 NZ LYS A1020 5291 4614 4616 -900 349 -1042 N ATOM 1736 N LYS A1021 67.168 12.022 -18.688 1.00 30.33 N ANISOU 1736 N LYS A1021 4270 3778 3475 -691 -67 17 N ATOM 1737 CA LYS A1021 67.907 12.133 -19.937 1.00 37.51 C ANISOU 1737 CA LYS A1021 5243 4820 4187 -715 -21 161 C ATOM 1738 C LYS A1021 69.335 12.594 -19.657 1.00 41.63 C ANISOU 1738 C LYS A1021 5727 5307 4784 -746 105 274 C ATOM 1739 O LYS A1021 70.297 12.025 -20.180 1.00 55.84 O ANISOU 1739 O LYS A1021 7552 7221 6444 -754 248 293 O ATOM 1740 CB LYS A1021 67.207 13.095 -20.897 1.00 42.88 C ANISOU 1740 CB LYS A1021 5950 5549 4794 -687 -167 334 C ATOM 1741 CG LYS A1021 67.602 12.911 -22.352 1.00 46.88 C ANISOU 1741 CG LYS A1021 6556 6266 4990 -669 -125 451 C ATOM 1742 CD LYS A1021 66.929 13.938 -23.248 1.00 54.08 C ANISOU 1742 CD LYS A1021 7510 7242 5795 -581 -268 678 C ATOM 1743 CE LYS A1021 67.300 13.715 -24.707 1.00 57.25 C ANISOU 1743 CE LYS A1021 8032 7904 5814 -522 -218 801 C ATOM 1744 NZ LYS A1021 66.757 14.782 -25.592 1.00 68.94 N ANISOU 1744 NZ LYS A1021 9580 9464 7150 -382 -333 1093 N ATOM 1745 N SER A1022 69.466 13.620 -18.817 1.00 29.72 N ANISOU 1745 N SER A1022 4135 3644 3514 -765 54 316 N ATOM 1746 CA SER A1022 70.779 14.103 -18.394 1.00 33.16 C ANISOU 1746 CA SER A1022 4474 4044 4082 -821 148 353 C ATOM 1747 C SER A1022 71.576 13.003 -17.701 1.00 33.94 C ANISOU 1747 C SER A1022 4525 4248 4123 -765 247 195 C ATOM 1748 O SER A1022 72.769 12.848 -17.937 1.00 40.47 O ANISOU 1748 O SER A1022 5284 5170 4924 -787 367 229 O ATOM 1749 CB SER A1022 70.638 15.306 -17.460 1.00 31.18 C ANISOU 1749 CB SER A1022 4133 3596 4119 -853 54 330 C ATOM 1750 OG SER A1022 70.022 16.394 -18.122 1.00 57.76 O ANISOU 1750 OG SER A1022 7551 6827 7569 -877 -5 517 O ATOM 1751 N LEU A1023 70.899 12.245 -16.848 1.00 26.89 N ANISOU 1751 N LEU A1023 3663 3337 3218 -673 215 40 N ATOM 1752 CA LEU A1023 71.512 11.157 -16.101 1.00 34.39 C ANISOU 1752 CA LEU A1023 4601 4363 4102 -561 322 -73 C ATOM 1753 C LEU A1023 72.127 10.123 -17.031 1.00 33.77 C ANISOU 1753 C LEU A1023 4590 4403 3839 -542 478 -51 C ATOM 1754 O LEU A1023 73.322 9.815 -16.947 1.00 27.83 O ANISOU 1754 O LEU A1023 3763 3755 3055 -489 582 -45 O ATOM 1755 CB LEU A1023 70.476 10.487 -15.198 1.00 31.07 C ANISOU 1755 CB LEU A1023 4246 3868 3692 -464 316 -188 C ATOM 1756 CG LEU A1023 70.915 9.202 -14.493 1.00 34.47 C ANISOU 1756 CG LEU A1023 4723 4341 4034 -305 471 -255 C ATOM 1757 CD1 LEU A1023 71.940 9.505 -13.414 1.00 27.20 C ANISOU 1757 CD1 LEU A1023 3685 3517 3133 -180 445 -282 C ATOM 1758 CD2 LEU A1023 69.717 8.464 -13.913 1.00 27.73 C ANISOU 1758 CD2 LEU A1023 3963 3367 3206 -248 535 -325 C ATOM 1759 N LEU A1024 71.299 9.593 -17.923 1.00 30.72 N ANISOU 1759 N LEU A1024 4325 4015 3332 -576 488 -69 N ATOM 1760 CA LEU A1024 71.745 8.563 -18.847 1.00 35.65 C ANISOU 1760 CA LEU A1024 5035 4740 3769 -554 637 -102 C ATOM 1761 C LEU A1024 72.817 9.095 -19.790 1.00 25.94 C ANISOU 1761 C LEU A1024 3763 3645 2447 -600 706 44 C ATOM 1762 O LEU A1024 73.740 8.371 -20.158 1.00 31.34 O ANISOU 1762 O LEU A1024 4453 4431 3023 -541 872 27 O ATOM 1763 CB LEU A1024 70.557 8.007 -19.629 1.00 29.12 C ANISOU 1763 CB LEU A1024 4320 3906 2839 -603 594 -210 C ATOM 1764 CG LEU A1024 69.585 7.274 -18.704 1.00 29.06 C ANISOU 1764 CG LEU A1024 4334 3746 2963 -576 606 -364 C ATOM 1765 CD1 LEU A1024 68.409 6.705 -19.470 1.00 36.58 C ANISOU 1765 CD1 LEU A1024 5337 4696 3865 -659 558 -529 C ATOM 1766 CD2 LEU A1024 70.327 6.180 -17.948 1.00 25.73 C ANISOU 1766 CD2 LEU A1024 3954 3261 2560 -449 816 -413 C ATOM 1767 N SER A1025 72.702 10.364 -20.168 1.00 25.62 N ANISOU 1767 N SER A1025 3681 3587 2466 -692 610 200 N ATOM 1768 CA SER A1025 73.722 10.985 -21.006 1.00 26.82 C ANISOU 1768 CA SER A1025 3785 3832 2574 -749 724 381 C ATOM 1769 C SER A1025 75.063 11.049 -20.278 1.00 27.44 C ANISOU 1769 C SER A1025 3679 3939 2809 -746 828 363 C ATOM 1770 O SER A1025 76.112 10.807 -20.873 1.00 45.90 O ANISOU 1770 O SER A1025 5961 6409 5070 -742 1003 421 O ATOM 1771 CB SER A1025 73.291 12.386 -21.435 1.00 32.31 C ANISOU 1771 CB SER A1025 4485 4438 3355 -836 634 585 C ATOM 1772 OG SER A1025 74.285 12.988 -22.245 1.00 37.41 O ANISOU 1772 OG SER A1025 5092 5142 3981 -900 801 794 O ATOM 1773 N LYS A1026 75.019 11.374 -18.989 1.00 26.50 N ANISOU 1773 N LYS A1026 3449 3725 2895 -731 715 262 N ATOM 1774 CA LYS A1026 76.222 11.475 -18.169 1.00 33.02 C ANISOU 1774 CA LYS A1026 4059 4623 3864 -707 751 192 C ATOM 1775 C LYS A1026 76.859 10.112 -17.942 1.00 29.75 C ANISOU 1775 C LYS A1026 3645 4358 3303 -526 871 97 C ATOM 1776 O LYS A1026 78.081 9.992 -17.886 1.00 37.12 O ANISOU 1776 O LYS A1026 4399 5436 4268 -487 968 88 O ATOM 1777 CB LYS A1026 75.903 12.125 -16.818 1.00 43.28 C ANISOU 1777 CB LYS A1026 5260 5822 5362 -700 572 67 C ATOM 1778 CG LYS A1026 75.571 13.608 -16.884 1.00 52.81 C ANISOU 1778 CG LYS A1026 6420 6850 6797 -873 479 136 C ATOM 1779 CD LYS A1026 74.972 14.090 -15.566 1.00 50.60 C ANISOU 1779 CD LYS A1026 6099 6463 6662 -831 299 -32 C ATOM 1780 CE LYS A1026 74.414 15.499 -15.686 1.00 51.45 C ANISOU 1780 CE LYS A1026 6210 6336 7004 -975 220 33 C ATOM 1781 NZ LYS A1026 73.747 15.941 -14.429 1.00 56.65 N ANISOU 1781 NZ LYS A1026 6847 6894 7784 -913 57 -156 N ATOM 1782 N PHE A1027 76.026 9.085 -17.805 1.00 32.89 N ANISOU 1782 N PHE A1027 4227 4704 3567 -411 880 24 N ATOM 1783 CA PHE A1027 76.527 7.739 -17.538 1.00 34.30 C ANISOU 1783 CA PHE A1027 4445 4954 3633 -211 1024 -50 C ATOM 1784 C PHE A1027 76.882 6.974 -18.810 1.00 30.78 C ANISOU 1784 C PHE A1027 4101 4581 3014 -202 1214 -29 C ATOM 1785 O PHE A1027 77.400 5.860 -18.742 1.00 42.94 O ANISOU 1785 O PHE A1027 5679 6161 4476 -29 1370 -86 O ATOM 1786 CB PHE A1027 75.504 6.946 -16.723 1.00 32.68 C ANISOU 1786 CB PHE A1027 4394 4606 3415 -95 1004 -137 C ATOM 1787 CG PHE A1027 75.679 7.085 -15.242 1.00 34.19 C ANISOU 1787 CG PHE A1027 4490 4818 3683 54 918 -176 C ATOM 1788 CD1 PHE A1027 75.128 8.159 -14.562 1.00 32.73 C ANISOU 1788 CD1 PHE A1027 4237 4580 3619 -32 731 -201 C ATOM 1789 CD2 PHE A1027 76.405 6.147 -14.529 1.00 46.82 C ANISOU 1789 CD2 PHE A1027 6073 6506 5212 314 1026 -190 C ATOM 1790 CE1 PHE A1027 75.294 8.291 -13.196 1.00 34.15 C ANISOU 1790 CE1 PHE A1027 4335 4820 3821 128 644 -270 C ATOM 1791 CE2 PHE A1027 76.574 6.273 -13.164 1.00 48.03 C ANISOU 1791 CE2 PHE A1027 6145 6735 5369 498 931 -222 C ATOM 1792 CZ PHE A1027 76.018 7.346 -12.496 1.00 39.00 C ANISOU 1792 CZ PHE A1027 4935 5564 4319 399 735 -277 C ATOM 1793 N GLY A1028 76.609 7.574 -19.964 1.00 32.26 N ANISOU 1793 N GLY A1028 4342 4791 3124 -359 1210 58 N ATOM 1794 CA GLY A1028 76.904 6.943 -21.238 1.00 28.14 C ANISOU 1794 CA GLY A1028 3928 4377 2385 -343 1383 61 C ATOM 1795 C GLY A1028 76.011 5.747 -21.506 1.00 41.38 C ANISOU 1795 C GLY A1028 5820 5970 3934 -281 1416 -111 C ATOM 1796 O GLY A1028 76.477 4.683 -21.917 1.00 39.08 O ANISOU 1796 O GLY A1028 5603 5716 3529 -168 1601 -208 O ATOM 1797 N MET A1029 74.717 5.924 -21.266 1.00 39.42 N ANISOU 1797 N MET A1029 5652 5593 3733 -359 1249 -170 N ATOM 1798 CA MET A1029 73.739 4.867 -21.487 1.00 37.29 C ANISOU 1798 CA MET A1029 5542 5218 3406 -354 1272 -371 C ATOM 1799 C MET A1029 72.638 5.329 -22.431 1.00 35.53 C ANISOU 1799 C MET A1029 5385 5054 3060 -484 1105 -411 C ATOM 1800 O MET A1029 72.346 6.522 -22.519 1.00 28.16 O ANISOU 1800 O MET A1029 4388 4163 2147 -555 944 -252 O ATOM 1801 CB MET A1029 73.125 4.418 -20.161 1.00 41.23 C ANISOU 1801 CB MET A1029 6046 5512 4108 -299 1256 -441 C ATOM 1802 CG MET A1029 74.018 3.536 -19.308 1.00 53.44 C ANISOU 1802 CG MET A1029 7589 7002 5713 -98 1446 -437 C ATOM 1803 SD MET A1029 73.271 3.217 -17.697 1.00 69.70 S ANISOU 1803 SD MET A1029 9671 8852 7959 0 1440 -442 S ATOM 1804 CE MET A1029 74.179 1.767 -17.178 1.00 67.47 C ANISOU 1804 CE MET A1029 9418 8497 7721 268 1624 -414 C ATOM 1805 N ASP A1030 72.032 4.381 -23.140 1.00 37.87 N ANISOU 1805 N ASP A1030 5802 5354 3234 -502 1141 -638 N ATOM 1806 CA ASP A1030 70.859 4.679 -23.951 1.00 41.57 C ANISOU 1806 CA ASP A1030 6304 5916 3577 -600 942 -738 C ATOM 1807 C ASP A1030 69.662 4.862 -23.028 1.00 48.35 C ANISOU 1807 C ASP A1030 7092 6600 4679 -669 791 -798 C ATOM 1808 O ASP A1030 69.719 4.494 -21.854 1.00 47.20 O ANISOU 1808 O ASP A1030 6920 6254 4760 -637 886 -801 O ATOM 1809 CB ASP A1030 70.582 3.564 -24.964 1.00 41.30 C ANISOU 1809 CB ASP A1030 6387 5958 3347 -610 1011 -1041 C ATOM 1810 CG ASP A1030 71.772 3.272 -25.860 1.00 53.57 C ANISOU 1810 CG ASP A1030 8013 7685 4656 -509 1194 -1002 C ATOM 1811 OD1 ASP A1030 72.648 4.149 -26.003 1.00 65.55 O ANISOU 1811 OD1 ASP A1030 9487 9331 6089 -470 1239 -721 O ATOM 1812 OD2 ASP A1030 71.826 2.161 -26.428 1.00 58.67 O ANISOU 1812 OD2 ASP A1030 8711 8304 5278 -445 1267 -1224 O ATOM 1813 N GLU A1031 68.580 5.429 -23.551 1.00 58.04 N ANISOU 1813 N GLU A1031 8283 7926 5843 -736 564 -835 N ATOM 1814 CA GLU A1031 67.363 5.578 -22.766 1.00 58.32 C ANISOU 1814 CA GLU A1031 8225 7821 6114 -800 431 -917 C ATOM 1815 C GLU A1031 66.804 4.202 -22.421 1.00 53.19 C ANISOU 1815 C GLU A1031 7596 6992 5621 -865 570 -1223 C ATOM 1816 O GLU A1031 67.065 3.222 -23.120 1.00 44.57 O ANISOU 1816 O GLU A1031 6595 5925 4416 -881 692 -1432 O ATOM 1817 CB GLU A1031 66.316 6.407 -23.515 1.00 72.67 C ANISOU 1817 CB GLU A1031 9974 9820 7816 -825 151 -910 C ATOM 1818 CG GLU A1031 65.751 5.737 -24.759 1.00 81.26 C ANISOU 1818 CG GLU A1031 11092 11123 8661 -859 59 -1186 C ATOM 1819 CD GLU A1031 64.467 6.389 -25.237 1.00 93.33 C ANISOU 1819 CD GLU A1031 12501 12833 10129 -859 -249 -1237 C ATOM 1820 OE1 GLU A1031 63.710 6.910 -24.389 1.00 95.04 O ANISOU 1820 OE1 GLU A1031 12590 12915 10604 -879 -341 -1180 O ATOM 1821 OE2 GLU A1031 64.214 6.383 -26.461 1.00 98.02 O ANISOU 1821 OE2 GLU A1031 13121 13726 10395 -812 -400 -1336 O ATOM 1822 N GLY A1032 66.039 4.136 -21.337 1.00 43.08 N ANISOU 1822 N GLY A1032 6948 4607 4813 -786 302 -399 N ATOM 1823 CA GLY A1032 65.472 2.884 -20.873 1.00 38.33 C ANISOU 1823 CA GLY A1032 6438 4015 4109 -765 322 -405 C ATOM 1824 C GLY A1032 65.185 2.961 -19.389 1.00 28.76 C ANISOU 1824 C GLY A1032 5102 2847 2979 -753 214 -399 C ATOM 1825 O GLY A1032 65.651 3.877 -18.717 1.00 25.47 O ANISOU 1825 O GLY A1032 4554 2439 2682 -738 120 -403 O ATOM 1826 N VAL A1033 64.415 2.008 -18.875 1.00 27.19 N ANISOU 1826 N VAL A1033 4955 2656 2719 -766 227 -389 N ATOM 1827 CA VAL A1033 64.075 1.996 -17.457 1.00 31.90 C ANISOU 1827 CA VAL A1033 5487 3281 3355 -748 158 -384 C ATOM 1828 C VAL A1033 65.344 1.824 -16.620 1.00 36.78 C ANISOU 1828 C VAL A1033 6182 3801 3994 -663 146 -396 C ATOM 1829 O VAL A1033 66.162 0.948 -16.891 1.00 41.24 O ANISOU 1829 O VAL A1033 6922 4239 4506 -602 247 -386 O ATOM 1830 CB VAL A1033 63.052 0.884 -17.133 1.00 17.56 C ANISOU 1830 CB VAL A1033 3757 1448 1466 -791 202 -363 C ATOM 1831 CG1 VAL A1033 63.557 -0.475 -17.603 1.00 36.02 C ANISOU 1831 CG1 VAL A1033 6308 3657 3721 -770 311 -367 C ATOM 1832 CG2 VAL A1033 62.734 0.865 -15.650 1.00 17.32 C ANISOU 1832 CG2 VAL A1033 3707 1428 1446 -771 157 -355 C ATOM 1833 N THR A1034 65.522 2.677 -15.617 1.00 27.73 N ANISOU 1833 N THR A1034 4917 2694 2924 -644 24 -415 N ATOM 1834 CA THR A1034 66.760 2.662 -14.844 1.00 33.40 C ANISOU 1834 CA THR A1034 5712 3307 3672 -573 -37 -426 C ATOM 1835 C THR A1034 66.554 2.235 -13.395 1.00 30.61 C ANISOU 1835 C THR A1034 5424 2960 3247 -534 -94 -438 C ATOM 1836 O THR A1034 65.690 2.757 -12.691 1.00 29.93 O ANISOU 1836 O THR A1034 5230 2982 3161 -556 -157 -459 O ATOM 1837 CB THR A1034 67.447 4.040 -14.861 1.00 32.30 C ANISOU 1837 CB THR A1034 5411 3168 3695 -589 -187 -444 C ATOM 1838 OG1 THR A1034 66.629 4.997 -14.180 1.00 44.73 O ANISOU 1838 OG1 THR A1034 6796 4885 5315 -611 -290 -485 O ATOM 1839 CG2 THR A1034 67.667 4.497 -16.287 1.00 17.54 C ANISOU 1839 CG2 THR A1034 3497 1267 1900 -632 -115 -411 C ATOM 1840 N PHE A1035 67.368 1.279 -12.964 1.00 35.57 N ANISOU 1840 N PHE A1035 6256 3449 3811 -450 -47 -415 N ATOM 1841 CA PHE A1035 67.334 0.771 -11.604 1.00 34.35 C ANISOU 1841 CA PHE A1035 6206 3289 3556 -383 -93 -412 C ATOM 1842 C PHE A1035 68.592 1.191 -10.861 1.00 35.41 C ANISOU 1842 C PHE A1035 6185 3490 3781 -247 -244 -335 C ATOM 1843 O PHE A1035 69.646 1.384 -11.470 1.00 32.82 O ANISOU 1843 O PHE A1035 5726 3146 3597 -184 -244 -243 O ATOM 1844 CB PHE A1035 67.196 -0.749 -11.605 1.00 27.71 C ANISOU 1844 CB PHE A1035 5572 2333 2624 -337 96 -352 C ATOM 1845 CG PHE A1035 66.018 -1.243 -12.386 1.00 33.57 C ANISOU 1845 CG PHE A1035 6290 3112 3352 -451 209 -342 C ATOM 1846 CD1 PHE A1035 64.773 -1.353 -11.789 1.00 39.58 C ANISOU 1846 CD1 PHE A1035 7028 3938 4073 -522 199 -334 C ATOM 1847 CD2 PHE A1035 66.151 -1.592 -13.721 1.00 39.17 C ANISOU 1847 CD2 PHE A1035 7008 3788 4088 -474 312 -332 C ATOM 1848 CE1 PHE A1035 63.683 -1.805 -12.506 1.00 48.74 C ANISOU 1848 CE1 PHE A1035 8166 5118 5237 -626 270 -314 C ATOM 1849 CE2 PHE A1035 65.065 -2.044 -14.445 1.00 45.09 C ANISOU 1849 CE2 PHE A1035 7740 4578 4813 -574 366 -329 C ATOM 1850 CZ PHE A1035 63.828 -2.151 -13.836 1.00 50.41 C ANISOU 1850 CZ PHE A1035 8381 5307 5467 -654 336 -318 C ATOM 1851 N MET A1036 68.484 1.329 -9.545 1.00 33.86 N ANISOU 1851 N MET A1036 5998 3371 3496 -196 -375 -358 N ATOM 1852 CA MET A1036 69.596 1.830 -8.752 1.00 26.22 C ANISOU 1852 CA MET A1036 4884 2481 2599 -90 -576 -308 C ATOM 1853 C MET A1036 69.758 1.096 -7.424 1.00 33.25 C ANISOU 1853 C MET A1036 5869 3430 3333 41 -612 -249 C ATOM 1854 O MET A1036 68.790 0.887 -6.693 1.00 31.72 O ANISOU 1854 O MET A1036 5814 3273 2965 35 -585 -312 O ATOM 1855 CB MET A1036 69.416 3.327 -8.499 1.00 22.41 C ANISOU 1855 CB MET A1036 4266 2062 2187 -171 -802 -442 C ATOM 1856 CG MET A1036 70.458 3.937 -7.580 1.00 29.91 C ANISOU 1856 CG MET A1036 5077 3082 3205 -91 -1068 -429 C ATOM 1857 SD MET A1036 70.109 5.670 -7.233 1.00 44.15 S ANISOU 1857 SD MET A1036 6772 4916 5089 -194 -1330 -627 S ATOM 1858 CE MET A1036 71.326 6.014 -5.965 1.00 48.04 C ANISOU 1858 CE MET A1036 7168 5483 5602 -91 -1662 -619 C ATOM 1859 N PHE A1037 70.994 0.699 -7.133 1.00 25.48 N ANISOU 1859 N PHE A1037 4797 2466 2419 172 -660 -100 N ATOM 1860 CA PHE A1037 71.365 0.180 -5.822 1.00 28.87 C ANISOU 1860 CA PHE A1037 5268 2988 2712 313 -746 -21 C ATOM 1861 C PHE A1037 72.416 1.103 -5.220 1.00 28.52 C ANISOU 1861 C PHE A1037 5029 3046 2761 352 -1057 -15 C ATOM 1862 O PHE A1037 73.272 1.617 -5.938 1.00 33.60 O ANISOU 1862 O PHE A1037 5480 3652 3634 322 -1125 45 O ATOM 1863 CB PHE A1037 71.893 -1.252 -5.925 1.00 29.90 C ANISOU 1863 CB PHE A1037 5469 3050 2843 442 -527 182 C ATOM 1864 CG PHE A1037 72.354 -1.829 -4.614 1.00 36.04 C ANISOU 1864 CG PHE A1037 6266 3937 3490 605 -604 306 C ATOM 1865 CD1 PHE A1037 71.459 -2.462 -3.766 1.00 41.94 C ANISOU 1865 CD1 PHE A1037 7190 4719 4025 653 -515 300 C ATOM 1866 CD2 PHE A1037 73.685 -1.745 -4.231 1.00 31.74 C ANISOU 1866 CD2 PHE A1037 5547 3470 3043 715 -765 456 C ATOM 1867 CE1 PHE A1037 71.882 -2.996 -2.560 1.00 45.61 C ANISOU 1867 CE1 PHE A1037 7672 5306 4352 822 -576 435 C ATOM 1868 CE2 PHE A1037 74.113 -2.276 -3.028 1.00 45.17 C ANISOU 1868 CE2 PHE A1037 7261 5295 4609 869 -849 585 C ATOM 1869 CZ PHE A1037 73.210 -2.903 -2.192 1.00 46.47 C ANISOU 1869 CZ PHE A1037 7617 5504 4536 930 -749 571 C ATOM 1870 N ILE A1038 72.358 1.312 -3.909 1.00 36.56 N ANISOU 1870 N ILE A1038 6097 4192 3605 421 -1251 -69 N ATOM 1871 CA ILE A1038 73.220 2.301 -3.263 1.00 42.04 C ANISOU 1871 CA ILE A1038 6631 4976 4367 430 -1602 -115 C ATOM 1872 C ILE A1038 73.916 1.741 -2.013 1.00 60.81 C ANISOU 1872 C ILE A1038 9022 7491 6590 593 -1749 3 C ATOM 1873 O ILE A1038 74.944 2.263 -1.578 1.00 79.74 O ANISOU 1873 O ILE A1038 11255 9958 9085 613 -2039 40 O ATOM 1874 CB ILE A1038 72.404 3.570 -2.896 1.00 43.51 C ANISOU 1874 CB ILE A1038 6866 5186 4479 328 -1785 -380 C ATOM 1875 CG1 ILE A1038 73.300 4.679 -2.331 1.00 49.27 C ANISOU 1875 CG1 ILE A1038 7438 5966 5318 307 -2175 -462 C ATOM 1876 CG2 ILE A1038 71.290 3.225 -1.928 1.00 56.16 C ANISOU 1876 CG2 ILE A1038 8712 6868 5757 401 -1709 -470 C ATOM 1877 CD1 ILE A1038 74.319 5.212 -3.311 1.00 49.73 C ANISOU 1877 CD1 ILE A1038 7218 5934 5745 222 -2257 -359 C ATOM 1878 N GLY A1039 73.373 0.664 -1.455 1.00 34.15 N ANISOU 1878 N GLY A1039 5829 4156 2991 708 -1553 84 N ATOM 1879 CA GLY A1039 73.908 0.082 -0.231 1.00 58.27 C ANISOU 1879 CA GLY A1039 8912 7364 5863 882 -1665 213 C ATOM 1880 C GLY A1039 75.335 -0.451 -0.277 1.00 55.78 C ANISOU 1880 C GLY A1039 8405 7074 5714 977 -1723 471 C ATOM 1881 O GLY A1039 76.018 -0.367 -1.298 1.00 62.26 O ANISOU 1881 O GLY A1039 9057 7785 6816 919 -1669 565 O ATOM 1882 N ARG A1040 75.782 -1.003 0.849 1.00 58.87 N ANISOU 1882 N ARG A1040 8818 7623 5928 1140 -1825 607 N ATOM 1883 CA ARG A1040 77.121 -1.579 0.976 1.00 54.77 C ANISOU 1883 CA ARG A1040 8109 7156 5545 1255 -1885 891 C ATOM 1884 C ARG A1040 77.172 -2.980 0.363 1.00 56.81 C ANISOU 1884 C ARG A1040 8410 7291 5886 1356 -1475 1137 C ATOM 1885 O ARG A1040 76.140 -3.636 0.225 1.00 59.93 O ANISOU 1885 O ARG A1040 9010 7602 6158 1361 -1193 1092 O ATOM 1886 CB ARG A1040 77.535 -1.631 2.451 1.00 61.45 C ANISOU 1886 CB ARG A1040 8968 8237 6143 1398 -2164 948 C ATOM 1887 CG ARG A1040 79.002 -1.952 2.696 1.00 79.78 C ANISOU 1887 CG ARG A1040 11044 10650 8618 1495 -2331 1235 C ATOM 1888 CD ARG A1040 79.229 -2.451 4.116 1.00 92.55 C ANISOU 1888 CD ARG A1040 12723 12506 9934 1681 -2486 1356 C ATOM 1889 NE ARG A1040 80.646 -2.656 4.408 1.00105.37 N ANISOU 1889 NE ARG A1040 14086 14241 11708 1762 -2698 1638 N ATOM 1890 CZ ARG A1040 81.315 -3.775 4.144 1.00108.61 C ANISOU 1890 CZ ARG A1040 14382 14623 12261 1900 -2448 1994 C ATOM 1891 NH1 ARG A1040 80.700 -4.802 3.575 1.00114.43 N ANISOU 1891 NH1 ARG A1040 15264 15204 13009 1967 -1985 2084 N ATOM 1892 NH2 ARG A1040 82.604 -3.866 4.447 1.00103.33 N ANISOU 1892 NH2 ARG A1040 13448 14063 11750 1954 -2657 2257 N ATOM 1893 N PHE A1041 78.367 -3.440 -0.001 1.00 57.80 N ANISOU 1893 N PHE A1041 8339 7391 6230 1437 -1440 1403 N ATOM 1894 CA PHE A1041 78.521 -4.763 -0.605 1.00 52.46 C ANISOU 1894 CA PHE A1041 7712 6573 5648 1552 -1044 1637 C ATOM 1895 C PHE A1041 78.736 -5.839 0.455 1.00 58.87 C ANISOU 1895 C PHE A1041 8575 7500 6293 1757 -972 1871 C ATOM 1896 O PHE A1041 79.866 -6.109 0.864 1.00 56.13 O ANISOU 1896 O PHE A1041 8041 7257 6028 1886 -1080 2130 O ATOM 1897 CB PHE A1041 79.683 -4.781 -1.602 1.00 56.11 C ANISOU 1897 CB PHE A1041 7947 6934 6439 1572 -976 1838 C ATOM 1898 CG PHE A1041 79.405 -4.039 -2.885 1.00 50.28 C ANISOU 1898 CG PHE A1041 7185 6045 5876 1408 -912 1666 C ATOM 1899 CD1 PHE A1041 78.238 -3.309 -3.054 1.00 49.46 C ANISOU 1899 CD1 PHE A1041 7227 5912 5651 1239 -962 1350 C ATOM 1900 CD2 PHE A1041 80.313 -4.086 -3.928 1.00 41.83 C ANISOU 1900 CD2 PHE A1041 5939 4867 5087 1444 -783 1848 C ATOM 1901 CE1 PHE A1041 77.991 -2.632 -4.234 1.00 43.78 C ANISOU 1901 CE1 PHE A1041 6474 5072 5089 1098 -902 1218 C ATOM 1902 CE2 PHE A1041 80.073 -3.414 -5.109 1.00 40.95 C ANISOU 1902 CE2 PHE A1041 5804 4636 5118 1316 -713 1715 C ATOM 1903 CZ PHE A1041 78.910 -2.686 -5.263 1.00 43.91 C ANISOU 1903 CZ PHE A1041 6320 4993 5369 1138 -780 1398 C ATOM 1904 N ASP A1042 77.642 -6.451 0.893 1.00 65.00 N ANISOU 1904 N ASP A1042 9587 8261 6850 1791 -785 1806 N ATOM 1905 CA ASP A1042 77.697 -7.489 1.915 1.00 56.93 C ANISOU 1905 CA ASP A1042 8627 7346 5659 1995 -685 2037 C ATOM 1906 C ASP A1042 77.098 -8.796 1.414 1.00 66.08 C ANISOU 1906 C ASP A1042 9951 8284 6871 2050 -238 2151 C ATOM 1907 O ASP A1042 76.361 -8.813 0.428 1.00 75.99 O ANISOU 1907 O ASP A1042 11327 9331 8216 1908 -47 1984 O ATOM 1908 CB ASP A1042 76.950 -7.046 3.176 1.00 50.34 C ANISOU 1908 CB ASP A1042 7916 6727 4484 2026 -891 1895 C ATOM 1909 CG ASP A1042 77.432 -5.714 3.708 1.00 78.31 C ANISOU 1909 CG ASP A1042 11343 10460 7950 1959 -1354 1725 C ATOM 1910 OD1 ASP A1042 78.415 -5.700 4.478 1.00 91.87 O ANISOU 1910 OD1 ASP A1042 12917 12367 9623 2073 -1601 1891 O ATOM 1911 OD2 ASP A1042 76.817 -4.681 3.366 1.00 84.99 O ANISOU 1911 OD2 ASP A1042 12242 11262 8789 1789 -1479 1427 O ATOM 1912 N ARG A1043 77.413 -9.889 2.099 1.00 64.10 N ANISOU 1912 N ARG A1043 9689 8077 6590 2224 -85 2409 N ATOM 1913 CA ARG A1043 76.702 -11.141 1.885 1.00 61.52 C ANISOU 1913 CA ARG A1043 9496 7554 6324 2227 304 2447 C ATOM 1914 C ARG A1043 75.791 -11.404 3.074 1.00 54.88 C ANISOU 1914 C ARG A1043 8750 6857 5245 2273 302 2424 C ATOM 1915 O ARG A1043 76.252 -11.791 4.145 1.00 66.17 O ANISOU 1915 O ARG A1043 10082 8475 6584 2405 236 2584 O ATOM 1916 CB ARG A1043 77.669 -12.312 1.685 1.00 66.04 C ANISOU 1916 CB ARG A1043 9938 8033 7121 2332 534 2684 C ATOM 1917 CG ARG A1043 78.241 -12.436 0.278 1.00 64.23 C ANISOU 1917 CG ARG A1043 9673 7577 7156 2278 701 2674 C ATOM 1918 CD ARG A1043 78.875 -13.801 0.073 1.00 62.15 C ANISOU 1918 CD ARG A1043 9347 7189 7077 2382 1008 2851 C ATOM 1919 NE ARG A1043 79.661 -13.875 -1.157 1.00 61.90 N ANISOU 1919 NE ARG A1043 9246 7001 7272 2368 1146 2859 N ATOM 1920 CZ ARG A1043 79.203 -14.345 -2.314 1.00 66.21 C ANISOU 1920 CZ ARG A1043 9945 7295 7916 2292 1406 2704 C ATOM 1921 NH1 ARG A1043 77.957 -14.789 -2.403 1.00 64.79 N ANISOU 1921 NH1 ARG A1043 9983 6975 7661 2201 1540 2536 N ATOM 1922 NH2 ARG A1043 79.991 -14.370 -3.380 1.00 71.10 N ANISOU 1922 NH2 ARG A1043 10495 7815 8707 2307 1525 2716 N ATOM 1923 N GLY A1044 74.497 -11.174 2.886 1.00 54.01 N ANISOU 1923 N GLY A1044 8817 6662 5041 2161 378 2230 N ATOM 1924 CA GLY A1044 73.520 -11.448 3.922 1.00 63.02 C ANISOU 1924 CA GLY A1044 10033 7915 5996 2201 425 2215 C ATOM 1925 C GLY A1044 73.094 -10.230 4.719 1.00 70.34 C ANISOU 1925 C GLY A1044 10994 9085 6648 2186 124 2031 C ATOM 1926 O GLY A1044 72.613 -10.361 5.844 1.00 78.14 O ANISOU 1926 O GLY A1044 11996 10238 7455 2271 111 2051 O ATOM 1927 N GLN A1045 73.264 -9.042 4.144 1.00 72.44 N ANISOU 1927 N GLN A1045 11269 9362 6892 2081 -112 1839 N ATOM 1928 CA GLN A1045 72.906 -7.804 4.835 1.00 62.20 C ANISOU 1928 CA GLN A1045 9997 8268 5367 2042 -415 1608 C ATOM 1929 C GLN A1045 72.179 -6.819 3.917 1.00 51.85 C ANISOU 1929 C GLN A1045 8786 6836 4080 1859 -471 1341 C ATOM 1930 O GLN A1045 70.973 -6.614 4.052 1.00 47.62 O ANISOU 1930 O GLN A1045 8355 6279 3462 1785 -374 1199 O ATOM 1931 CB GLN A1045 74.156 -7.149 5.430 1.00 69.76 C ANISOU 1931 CB GLN A1045 10798 9437 6271 2103 -779 1625 C ATOM 1932 CG GLN A1045 74.851 -8.001 6.487 1.00 78.68 C ANISOU 1932 CG GLN A1045 11826 10728 7342 2271 -767 1875 C ATOM 1933 CD GLN A1045 76.304 -7.623 6.688 1.00 84.53 C ANISOU 1933 CD GLN A1045 12367 11602 8147 2303 -1079 1975 C ATOM 1934 OE1 GLN A1045 76.660 -6.445 6.680 1.00 88.76 O ANISOU 1934 OE1 GLN A1045 12846 12218 8661 2206 -1421 1787 O ATOM 1935 NE2 GLN A1045 77.156 -8.628 6.863 1.00 87.61 N ANISOU 1935 NE2 GLN A1045 12631 12001 8654 2422 -961 2273 N ATOM 1936 N LYS A1046 72.912 -6.209 2.990 1.00 49.51 N ANISOU 1936 N LYS A1046 8356 6451 4003 1724 -601 1245 N ATOM 1937 CA LYS A1046 72.313 -5.272 2.042 1.00 43.67 C ANISOU 1937 CA LYS A1046 7628 5588 3376 1502 -638 977 C ATOM 1938 C LYS A1046 71.847 -5.988 0.776 1.00 42.96 C ANISOU 1938 C LYS A1046 7589 5234 3500 1384 -316 998 C ATOM 1939 O LYS A1046 71.034 -5.462 0.016 1.00 45.24 O ANISOU 1939 O LYS A1046 7927 5416 3847 1209 -275 806 O ATOM 1940 CB LYS A1046 73.298 -4.158 1.689 1.00 42.47 C ANISOU 1940 CB LYS A1046 7294 5480 3361 1415 -949 864 C ATOM 1941 CG LYS A1046 73.627 -3.245 2.856 1.00 47.40 C ANISOU 1941 CG LYS A1046 7895 6338 3777 1481 -1324 761 C ATOM 1942 CD LYS A1046 72.363 -2.645 3.445 1.00 46.66 C ANISOU 1942 CD LYS A1046 7988 6309 3430 1464 -1347 542 C ATOM 1943 CE LYS A1046 72.664 -1.839 4.692 1.00 62.52 C ANISOU 1943 CE LYS A1046 9944 8525 5285 1500 -1639 412 C ATOM 1944 NZ LYS A1046 71.421 -1.327 5.332 1.00 71.28 N ANISOU 1944 NZ LYS A1046 11159 9670 6256 1466 -1548 219 N ATOM 1945 N GLY A1047 72.377 -7.186 0.555 1.00 44.61 N ANISOU 1945 N GLY A1047 7791 5335 3822 1487 -95 1232 N ATOM 1946 CA GLY A1047 71.896 -8.055 -0.503 1.00 48.37 C ANISOU 1946 CA GLY A1047 8367 5547 4465 1403 221 1254 C ATOM 1947 C GLY A1047 72.257 -7.650 -1.919 1.00 45.81 C ANISOU 1947 C GLY A1047 7986 5064 4353 1257 241 1138 C ATOM 1948 O GLY A1047 71.446 -7.798 -2.834 1.00 44.91 O ANISOU 1948 O GLY A1047 7983 4774 4306 1110 398 1014 O ATOM 1949 N VAL A1048 73.473 -7.151 -2.114 1.00 36.74 N ANISOU 1949 N VAL A1048 6660 3985 3316 1302 81 1195 N ATOM 1950 CA VAL A1048 73.928 -6.822 -3.459 1.00 36.24 C ANISOU 1950 CA VAL A1048 6527 3783 3461 1206 132 1138 C ATOM 1951 C VAL A1048 74.193 -8.114 -4.233 1.00 38.89 C ANISOU 1951 C VAL A1048 6961 3894 3922 1285 470 1291 C ATOM 1952 O VAL A1048 74.162 -8.128 -5.463 1.00 41.85 O ANISOU 1952 O VAL A1048 7381 4104 4415 1204 607 1212 O ATOM 1953 CB VAL A1048 75.195 -5.934 -3.446 1.00 36.36 C ANISOU 1953 CB VAL A1048 6292 3925 3600 1241 -125 1199 C ATOM 1954 CG1 VAL A1048 76.422 -6.742 -3.041 1.00 47.41 C ANISOU 1954 CG1 VAL A1048 7576 5359 5079 1448 -75 1508 C ATOM 1955 CG2 VAL A1048 75.406 -5.285 -4.808 1.00 34.92 C ANISOU 1955 CG2 VAL A1048 6030 3628 3608 1119 -99 1104 C ATOM 1956 N ASP A1049 74.433 -9.202 -3.503 1.00 42.50 N ANISOU 1956 N ASP A1049 7464 4341 4342 1453 610 1507 N ATOM 1957 CA ASP A1049 74.633 -10.513 -4.113 1.00 44.36 C ANISOU 1957 CA ASP A1049 7821 4337 4697 1545 948 1653 C ATOM 1958 C ASP A1049 73.357 -10.983 -4.806 1.00 40.37 C ANISOU 1958 C ASP A1049 7540 3616 4181 1381 1137 1464 C ATOM 1959 O ASP A1049 73.400 -11.563 -5.897 1.00 50.89 O ANISOU 1959 O ASP A1049 8927 4769 5642 1327 1328 1380 O ATOM 1960 CB ASP A1049 75.079 -11.536 -3.063 1.00 55.84 C ANISOU 1960 CB ASP A1049 9214 5866 6138 1727 1034 1891 C ATOM 1961 CG ASP A1049 74.282 -11.440 -1.772 1.00 67.06 C ANISOU 1961 CG ASP A1049 10686 7452 7341 1750 917 1900 C ATOM 1962 OD1 ASP A1049 73.228 -10.771 -1.764 1.00 77.71 O ANISOU 1962 OD1 ASP A1049 12140 8820 8566 1608 825 1701 O ATOM 1963 OD2 ASP A1049 74.709 -12.040 -0.763 1.00 67.79 O ANISOU 1963 OD2 ASP A1049 10684 7678 7394 1898 920 2087 O ATOM 1964 N VAL A1050 72.224 -10.715 -4.164 1.00 36.98 N ANISOU 1964 N VAL A1050 7186 3259 3607 1283 1054 1357 N ATOM 1965 CA VAL A1050 70.918 -11.027 -4.729 1.00 42.13 C ANISOU 1965 CA VAL A1050 8013 3736 4260 1101 1181 1190 C ATOM 1966 C VAL A1050 70.706 -10.270 -6.034 1.00 37.09 C ANISOU 1966 C VAL A1050 7398 3019 3676 920 1134 967 C ATOM 1967 O VAL A1050 70.219 -10.832 -7.018 1.00 48.33 O ANISOU 1967 O VAL A1050 8933 4256 5176 806 1285 847 O ATOM 1968 CB VAL A1050 69.781 -10.680 -3.748 1.00 39.68 C ANISOU 1968 CB VAL A1050 7729 3559 3787 1043 1081 1144 C ATOM 1969 CG1 VAL A1050 68.430 -11.018 -4.358 1.00 44.62 C ANISOU 1969 CG1 VAL A1050 8485 4009 4458 839 1199 998 C ATOM 1970 CG2 VAL A1050 69.972 -11.418 -2.436 1.00 37.54 C ANISOU 1970 CG2 VAL A1050 7412 3403 3447 1236 1128 1366 C ATOM 1971 N LEU A1051 71.087 -8.996 -6.039 1.00 32.98 N ANISOU 1971 N LEU A1051 6713 2688 3131 883 895 878 N ATOM 1972 CA LEU A1051 70.936 -8.161 -7.225 1.00 34.16 C ANISOU 1972 CA LEU A1051 6841 2800 3338 727 839 691 C ATOM 1973 C LEU A1051 71.847 -8.611 -8.360 1.00 39.46 C ANISOU 1973 C LEU A1051 7533 3316 4143 800 1007 753 C ATOM 1974 O LEU A1051 71.424 -8.651 -9.511 1.00 46.36 O ANISOU 1974 O LEU A1051 8523 4050 5041 688 1107 617 O ATOM 1975 CB LEU A1051 71.210 -6.692 -6.898 1.00 30.85 C ANISOU 1975 CB LEU A1051 6223 2602 2897 685 548 609 C ATOM 1976 CG LEU A1051 71.178 -5.762 -8.116 1.00 36.98 C ANISOU 1976 CG LEU A1051 6939 3354 3760 546 494 457 C ATOM 1977 CD1 LEU A1051 69.837 -5.853 -8.835 1.00 27.54 C ANISOU 1977 CD1 LEU A1051 5905 2046 2513 356 586 283 C ATOM 1978 CD2 LEU A1051 71.480 -4.328 -7.717 1.00 28.16 C ANISOU 1978 CD2 LEU A1051 5616 2426 2657 507 205 388 C ATOM 1979 N LEU A1052 73.096 -8.938 -8.044 1.00 35.48 N ANISOU 1979 N LEU A1052 6916 2846 3717 1000 1041 968 N ATOM 1980 CA LEU A1052 74.033 -9.381 -9.072 1.00 43.58 C ANISOU 1980 CA LEU A1052 7955 3730 4874 1113 1234 1066 C ATOM 1981 C LEU A1052 73.563 -10.699 -9.685 1.00 47.45 C ANISOU 1981 C LEU A1052 8602 4057 5369 1081 1488 968 C ATOM 1982 O LEU A1052 73.546 -10.863 -10.913 1.00 52.46 O ANISOU 1982 O LEU A1052 9311 4598 6022 1034 1608 846 O ATOM 1983 CB LEU A1052 75.443 -9.524 -8.493 1.00 42.92 C ANISOU 1983 CB LEU A1052 7662 3753 4893 1331 1211 1339 C ATOM 1984 CG LEU A1052 76.074 -8.236 -7.953 1.00 40.47 C ANISOU 1984 CG LEU A1052 7074 3685 4618 1321 890 1379 C ATOM 1985 CD1 LEU A1052 77.456 -8.505 -7.378 1.00 44.27 C ANISOU 1985 CD1 LEU A1052 7351 4256 5215 1533 863 1685 C ATOM 1986 CD2 LEU A1052 76.139 -7.163 -9.029 1.00 38.12 C ANISOU 1986 CD2 LEU A1052 6682 3396 4405 1204 810 1245 C ATOM 1987 N LYS A1053 73.158 -11.626 -8.822 1.00 51.85 N ANISOU 1987 N LYS A1053 9215 4589 5898 1112 1558 1027 N ATOM 1988 CA LYS A1053 72.647 -12.915 -9.273 1.00 60.34 C ANISOU 1988 CA LYS A1053 10436 5496 6992 1076 1772 945 C ATOM 1989 C LYS A1053 71.403 -12.747 -10.151 1.00 59.15 C ANISOU 1989 C LYS A1053 10435 5264 6774 840 1749 687 C ATOM 1990 O LYS A1053 71.279 -13.387 -11.201 1.00 65.35 O ANISOU 1990 O LYS A1053 11337 5933 7562 792 1882 576 O ATOM 1991 CB LYS A1053 72.332 -13.808 -8.072 1.00 58.27 C ANISOU 1991 CB LYS A1053 10175 5233 6731 1142 1825 1075 C ATOM 1992 CG LYS A1053 72.060 -15.259 -8.423 1.00 60.73 C ANISOU 1992 CG LYS A1053 10607 5358 7109 1144 2054 1049 C ATOM 1993 CD LYS A1053 73.236 -15.877 -9.161 1.00 66.50 C ANISOU 1993 CD LYS A1053 11331 6016 7921 1299 2240 1121 C ATOM 1994 CE LYS A1053 73.256 -17.391 -8.999 1.00 69.35 C ANISOU 1994 CE LYS A1053 11770 6222 8358 1378 2465 1193 C ATOM 1995 NZ LYS A1053 71.947 -18.013 -9.342 1.00 67.50 N ANISOU 1995 NZ LYS A1053 11710 5828 8108 1184 2496 1016 N ATOM 1996 N ALA A1054 70.491 -11.876 -9.723 1.00 39.75 N ANISOU 1996 N ALA A1054 7615 2800 4690 261 1949 -50 N ATOM 1997 CA ALA A1054 69.266 -11.615 -10.477 1.00 46.76 C ANISOU 1997 CA ALA A1054 8403 3704 5662 87 1924 -174 C ATOM 1998 C ALA A1054 69.567 -10.948 -11.819 1.00 40.54 C ANISOU 1998 C ALA A1054 7486 2990 4927 94 1767 -203 C ATOM 1999 O ALA A1054 68.873 -11.178 -12.811 1.00 44.35 O ANISOU 1999 O ALA A1054 7964 3440 5447 -17 1765 -323 O ATOM 2000 CB ALA A1054 68.314 -10.755 -9.661 1.00 46.97 C ANISOU 2000 CB ALA A1054 8315 3783 5749 -2 1856 -199 C ATOM 2001 N ILE A1055 70.603 -10.117 -11.840 1.00 31.65 N ANISOU 2001 N ILE A1055 6263 1955 3809 225 1629 -101 N ATOM 2002 CA ILE A1055 71.049 -9.475 -13.067 1.00 37.50 C ANISOU 2002 CA ILE A1055 6902 2756 4589 258 1513 -101 C ATOM 2003 C ILE A1055 71.551 -10.539 -14.029 1.00 46.87 C ANISOU 2003 C ILE A1055 8256 3853 5701 301 1682 -132 C ATOM 2004 O ILE A1055 71.281 -10.481 -15.231 1.00 54.88 O ANISOU 2004 O ILE A1055 9288 4860 6705 244 1659 -222 O ATOM 2005 CB ILE A1055 72.152 -8.430 -12.797 1.00 34.96 C ANISOU 2005 CB ILE A1055 6425 2532 4327 399 1356 32 C ATOM 2006 CG1 ILE A1055 71.526 -7.119 -12.318 1.00 33.76 C ANISOU 2006 CG1 ILE A1055 6080 2468 4281 324 1146 34 C ATOM 2007 CG2 ILE A1055 72.986 -8.182 -14.044 1.00 29.84 C ANISOU 2007 CG2 ILE A1055 5737 1908 3694 488 1345 74 C ATOM 2008 CD1 ILE A1055 72.534 -6.026 -12.030 1.00 28.01 C ANISOU 2008 CD1 ILE A1055 5173 1821 3650 432 961 162 C ATOM 2009 N GLU A1056 72.266 -11.524 -13.493 1.00 47.17 N ANISOU 2009 N GLU A1056 8429 3806 5687 403 1849 -67 N ATOM 2010 CA GLU A1056 72.714 -12.645 -14.311 1.00 50.96 C ANISOU 2010 CA GLU A1056 9077 4170 6115 444 2042 -98 C ATOM 2011 C GLU A1056 71.529 -13.449 -14.845 1.00 51.65 C ANISOU 2011 C GLU A1056 9286 4160 6179 264 2128 -270 C ATOM 2012 O GLU A1056 71.539 -13.880 -15.997 1.00 60.43 O ANISOU 2012 O GLU A1056 10493 5216 7253 237 2186 -370 O ATOM 2013 CB GLU A1056 73.658 -13.550 -13.519 1.00 49.41 C ANISOU 2013 CB GLU A1056 8984 3882 5907 591 2194 7 C ATOM 2014 CG GLU A1056 75.045 -12.959 -13.339 1.00 60.66 C ANISOU 2014 CG GLU A1056 10280 5370 7397 789 2117 152 C ATOM 2015 CD GLU A1056 75.988 -13.889 -12.609 1.00 79.51 C ANISOU 2015 CD GLU A1056 12752 7646 9811 942 2238 245 C ATOM 2016 OE1 GLU A1056 77.217 -13.699 -12.728 1.00 87.87 O ANISOU 2016 OE1 GLU A1056 13707 8710 10969 1110 2219 355 O ATOM 2017 OE2 GLU A1056 75.503 -14.807 -11.914 1.00 88.40 O ANISOU 2017 OE2 GLU A1056 14036 8667 10884 896 2351 213 O ATOM 2018 N ILE A1057 70.509 -13.642 -14.013 1.00 46.21 N ANISOU 2018 N ILE A1057 8592 3446 5520 144 2137 -316 N ATOM 2019 CA ILE A1057 69.301 -14.338 -14.452 1.00 45.56 C ANISOU 2019 CA ILE A1057 8573 3270 5466 -34 2196 -491 C ATOM 2020 C ILE A1057 68.621 -13.584 -15.596 1.00 56.83 C ANISOU 2020 C ILE A1057 9898 4765 6929 -142 2002 -632 C ATOM 2021 O ILE A1057 68.136 -14.189 -16.553 1.00 71.24 O ANISOU 2021 O ILE A1057 11815 6515 8737 -235 2018 -800 O ATOM 2022 CB ILE A1057 68.295 -14.522 -13.294 1.00 47.06 C ANISOU 2022 CB ILE A1057 8739 3427 5714 -135 2254 -505 C ATOM 2023 CG1 ILE A1057 68.895 -15.401 -12.195 1.00 49.61 C ANISOU 2023 CG1 ILE A1057 9216 3660 5974 -34 2454 -388 C ATOM 2024 CG2 ILE A1057 66.993 -15.132 -13.800 1.00 40.62 C ANISOU 2024 CG2 ILE A1057 7937 2516 4982 -320 2290 -701 C ATOM 2025 CD1 ILE A1057 67.948 -15.674 -11.042 1.00 40.67 C ANISOU 2025 CD1 ILE A1057 8109 2475 4869 -123 2566 -399 C ATOM 2026 N LEU A1058 68.607 -12.258 -15.498 1.00 49.45 N ANISOU 2026 N LEU A1058 8780 3967 6042 -126 1803 -573 N ATOM 2027 CA LEU A1058 67.928 -11.417 -16.480 1.00 35.09 C ANISOU 2027 CA LEU A1058 6850 2210 4272 -226 1588 -692 C ATOM 2028 C LEU A1058 68.720 -11.237 -17.772 1.00 44.10 C ANISOU 2028 C LEU A1058 8134 3347 5274 -167 1613 -709 C ATOM 2029 O LEU A1058 68.140 -10.981 -18.826 1.00 52.66 O ANISOU 2029 O LEU A1058 9296 4414 6298 -287 1534 -857 O ATOM 2030 CB LEU A1058 67.631 -10.044 -15.878 1.00 31.75 C ANISOU 2030 CB LEU A1058 6198 1901 3964 -233 1395 -611 C ATOM 2031 CG LEU A1058 66.554 -9.966 -14.799 1.00 31.80 C ANISOU 2031 CG LEU A1058 6102 1892 4087 -331 1404 -631 C ATOM 2032 CD1 LEU A1058 66.575 -8.602 -14.139 1.00 33.14 C ANISOU 2032 CD1 LEU A1058 6072 2172 4348 -296 1244 -528 C ATOM 2033 CD2 LEU A1058 65.189 -10.246 -15.397 1.00 39.56 C ANISOU 2033 CD2 LEU A1058 7048 2803 5181 -508 1332 -819 C ATOM 2034 N SER A1059 70.040 -11.377 -17.689 1.00 43.99 N ANISOU 2034 N SER A1059 8206 3327 5182 10 1760 -559 N ATOM 2035 CA SER A1059 70.922 -11.094 -18.822 1.00 45.24 C ANISOU 2035 CA SER A1059 8541 3459 5189 104 1870 -528 C ATOM 2036 C SER A1059 70.655 -11.980 -20.043 1.00 46.85 C ANISOU 2036 C SER A1059 9006 3560 5235 18 1993 -721 C ATOM 2037 O SER A1059 71.051 -11.643 -21.158 1.00 41.62 O ANISOU 2037 O SER A1059 8523 2893 4399 47 2053 -755 O ATOM 2038 CB SER A1059 72.386 -11.237 -18.396 1.00 49.49 C ANISOU 2038 CB SER A1059 9075 3994 5734 334 2021 -323 C ATOM 2039 OG SER A1059 72.668 -12.558 -17.969 1.00 66.04 O ANISOU 2039 OG SER A1059 11256 5994 7843 369 2179 -329 O ATOM 2040 N SER A1060 69.984 -13.107 -19.830 1.00 56.58 N ANISOU 2040 N SER A1060 10270 4714 6513 -82 2030 -855 N ATOM 2041 CA SER A1060 69.664 -14.020 -20.923 1.00 57.40 C ANISOU 2041 CA SER A1060 10605 4723 6481 -174 2118 -1070 C ATOM 2042 C SER A1060 68.348 -13.643 -21.597 1.00 57.50 C ANISOU 2042 C SER A1060 10610 4772 6467 -392 1890 -1293 C ATOM 2043 O SER A1060 68.070 -14.069 -22.716 1.00 67.72 O ANISOU 2043 O SER A1060 12115 6028 7588 -487 1890 -1494 O ATOM 2044 CB SER A1060 69.599 -15.460 -20.414 1.00 57.70 C ANISOU 2044 CB SER A1060 10689 4636 6598 -169 2269 -1115 C ATOM 2045 OG SER A1060 68.575 -15.608 -19.447 1.00 54.29 O ANISOU 2045 OG SER A1060 10073 4212 6342 -271 2147 -1142 O ATOM 2046 N LYS A1061 67.543 -12.840 -20.908 1.00 48.80 N ANISOU 2046 N LYS A1061 9260 3741 5541 -471 1680 -1261 N ATOM 2047 CA LYS A1061 66.238 -12.432 -21.419 1.00 51.14 C ANISOU 2047 CA LYS A1061 9485 4055 5890 -679 1425 -1451 C ATOM 2048 C LYS A1061 66.333 -11.233 -22.359 1.00 54.45 C ANISOU 2048 C LYS A1061 9981 4564 6141 -741 1264 -1462 C ATOM 2049 O LYS A1061 67.214 -10.384 -22.214 1.00 66.16 O ANISOU 2049 O LYS A1061 11462 6107 7568 -612 1314 -1277 O ATOM 2050 CB LYS A1061 65.296 -12.106 -20.258 1.00 50.52 C ANISOU 2050 CB LYS A1061 9087 3996 6113 -726 1279 -1401 C ATOM 2051 CG LYS A1061 64.997 -13.284 -19.344 1.00 54.52 C ANISOU 2051 CG LYS A1061 9557 4413 6747 -700 1416 -1404 C ATOM 2052 CD LYS A1061 64.073 -12.872 -18.206 1.00 63.31 C ANISOU 2052 CD LYS A1061 10449 5528 8079 -763 1358 -1344 C ATOM 2053 CE LYS A1061 63.611 -14.072 -17.394 1.00 69.36 C ANISOU 2053 CE LYS A1061 11293 6153 8907 -810 1594 -1374 C ATOM 2054 NZ LYS A1061 64.768 -14.829 -16.853 1.00 75.16 N ANISOU 2054 NZ LYS A1061 12195 6856 9506 -669 1864 -1233 N ATOM 2055 N LYS A1062 65.408 -11.162 -23.312 1.00 53.80 N ANISOU 2055 N LYS A1062 9974 4490 5980 -945 1046 -1674 N ATOM 2056 CA LYS A1062 65.385 -10.077 -24.289 1.00 59.08 C ANISOU 2056 CA LYS A1062 10757 5262 6428 -1052 836 -1693 C ATOM 2057 C LYS A1062 65.054 -8.734 -23.634 1.00 59.30 C ANISOU 2057 C LYS A1062 10486 5353 6694 -1090 623 -1537 C ATOM 2058 O LYS A1062 65.404 -7.676 -24.160 1.00 54.13 O ANISOU 2058 O LYS A1062 9916 4781 5869 -1126 489 -1451 O ATOM 2059 CB LYS A1062 64.379 -10.380 -25.405 1.00 66.97 C ANISOU 2059 CB LYS A1062 11878 6275 7292 -1289 577 -1951 C ATOM 2060 CG LYS A1062 62.939 -10.483 -24.930 1.00 76.32 C ANISOU 2060 CG LYS A1062 12733 7395 8871 -1447 328 -2064 C ATOM 2061 CD LYS A1062 61.979 -10.655 -26.095 1.00 84.48 C ANISOU 2061 CD LYS A1062 13859 8445 9793 -1681 11 -2306 C ATOM 2062 CE LYS A1062 60.540 -10.714 -25.611 1.00 89.48 C ANISOU 2062 CE LYS A1062 14110 8982 10908 -1809 -236 -2406 C ATOM 2063 NZ LYS A1062 59.571 -10.847 -26.733 1.00 99.64 N ANISOU 2063 NZ LYS A1062 15434 10282 12142 -2039 -586 -2640 N ATOM 2064 N GLU A1063 64.388 -8.779 -22.483 1.00 53.34 N ANISOU 2064 N GLU A1063 9387 4560 6321 -1076 589 -1491 N ATOM 2065 CA GLU A1063 64.010 -7.559 -21.773 1.00 47.29 C ANISOU 2065 CA GLU A1063 8284 3849 5834 -1091 403 -1342 C ATOM 2066 C GLU A1063 65.214 -6.855 -21.151 1.00 35.18 C ANISOU 2066 C GLU A1063 6742 2359 4264 -895 546 -1101 C ATOM 2067 O GLU A1063 65.159 -5.660 -20.854 1.00 37.87 O ANISOU 2067 O GLU A1063 6872 2753 4763 -910 381 -963 O ATOM 2068 CB GLU A1063 62.979 -7.865 -20.684 1.00 42.27 C ANISOU 2068 CB GLU A1063 7323 3162 5574 -1087 350 -1351 C ATOM 2069 CG GLU A1063 61.548 -8.007 -21.183 1.00 58.53 C ANISOU 2069 CG GLU A1063 9243 5156 7839 -1283 86 -1533 C ATOM 2070 CD GLU A1063 61.198 -9.427 -21.583 1.00 78.63 C ANISOU 2070 CD GLU A1063 11988 7589 10300 -1334 173 -1738 C ATOM 2071 OE1 GLU A1063 62.107 -10.284 -21.616 1.00 80.74 O ANISOU 2071 OE1 GLU A1063 12514 7842 10321 -1228 448 -1743 O ATOM 2072 OE2 GLU A1063 60.007 -9.686 -21.859 1.00 88.26 O ANISOU 2072 OE2 GLU A1063 13087 8715 11733 -1476 -48 -1884 O ATOM 2073 N PHE A1064 66.298 -7.602 -20.961 1.00 35.25 N ANISOU 2073 N PHE A1064 6948 2338 4107 -707 833 -1038 N ATOM 2074 CA PHE A1064 67.503 -7.078 -20.327 1.00 44.21 C ANISOU 2074 CA PHE A1064 8047 3503 5247 -487 961 -804 C ATOM 2075 C PHE A1064 68.079 -5.892 -21.090 1.00 45.83 C ANISOU 2075 C PHE A1064 8374 3713 5328 -471 876 -697 C ATOM 2076 O PHE A1064 68.653 -4.981 -20.492 1.00 45.48 O ANISOU 2076 O PHE A1064 8146 3698 5435 -343 831 -475 O ATOM 2077 CB PHE A1064 68.558 -8.179 -20.203 1.00 45.77 C ANISOU 2077 CB PHE A1064 8429 3659 5304 -302 1260 -755 C ATOM 2078 CG PHE A1064 69.769 -7.772 -19.412 1.00 44.70 C ANISOU 2078 CG PHE A1064 8188 3566 5231 -70 1352 -511 C ATOM 2079 CD1 PHE A1064 69.680 -7.557 -18.046 1.00 34.86 C ANISOU 2079 CD1 PHE A1064 6663 2397 4185 -32 1255 -411 C ATOM 2080 CD2 PHE A1064 70.999 -7.616 -20.032 1.00 43.47 C ANISOU 2080 CD2 PHE A1064 8202 3385 4930 118 1526 -389 C ATOM 2081 CE1 PHE A1064 70.793 -7.186 -17.314 1.00 29.72 C ANISOU 2081 CE1 PHE A1064 5894 1813 3584 155 1271 -219 C ATOM 2082 CE2 PHE A1064 72.116 -7.246 -19.305 1.00 31.07 C ANISOU 2082 CE2 PHE A1064 6461 1875 3471 335 1567 -162 C ATOM 2083 CZ PHE A1064 72.013 -7.030 -17.944 1.00 28.90 C ANISOU 2083 CZ PHE A1064 5896 1694 3389 333 1407 -93 C ATOM 2084 N GLN A1065 67.911 -5.906 -22.410 1.00 49.83 N ANISOU 2084 N GLN A1065 9190 4206 5536 -604 818 -845 N ATOM 2085 CA GLN A1065 68.407 -4.832 -23.267 1.00 51.40 C ANISOU 2085 CA GLN A1065 9276 4680 5575 -552 651 -613 C ATOM 2086 C GLN A1065 67.671 -3.516 -23.025 1.00 43.07 C ANISOU 2086 C GLN A1065 7815 3765 4787 -694 268 -458 C ATOM 2087 O GLN A1065 68.179 -2.445 -23.359 1.00 36.17 O ANISOU 2087 O GLN A1065 6720 3115 3907 -605 133 -179 O ATOM 2088 CB GLN A1065 68.289 -5.230 -24.741 1.00 53.31 C ANISOU 2088 CB GLN A1065 9825 5047 5385 -653 620 -758 C ATOM 2089 CG GLN A1065 69.092 -6.464 -25.108 1.00 67.57 C ANISOU 2089 CG GLN A1065 12044 6716 6913 -498 1034 -910 C ATOM 2090 CD GLN A1065 70.566 -6.311 -24.787 1.00 78.26 C ANISOU 2090 CD GLN A1065 13332 8094 8310 -158 1345 -634 C ATOM 2091 OE1 GLN A1065 71.133 -7.097 -24.027 1.00 77.74 O ANISOU 2091 OE1 GLN A1065 13355 7803 8380 11 1642 -667 O ATOM 2092 NE2 GLN A1065 71.196 -5.296 -25.369 1.00 83.28 N ANISOU 2092 NE2 GLN A1065 13798 8987 8860 -57 1272 -347 N ATOM 2093 N GLU A1066 66.475 -3.598 -22.449 1.00 44.61 N ANISOU 2093 N GLU A1066 7899 3805 5247 -912 116 -635 N ATOM 2094 CA GLU A1066 65.694 -2.402 -22.152 1.00 45.36 C ANISOU 2094 CA GLU A1066 7593 3984 5659 -1050 -215 -511 C ATOM 2095 C GLU A1066 66.069 -1.800 -20.801 1.00 41.52 C ANISOU 2095 C GLU A1066 6866 3409 5500 -906 -125 -340 C ATOM 2096 O GLU A1066 65.779 -0.633 -20.531 1.00 38.55 O ANISOU 2096 O GLU A1066 6146 3125 5375 -946 -351 -172 O ATOM 2097 CB GLU A1066 64.196 -2.716 -22.174 1.00 43.82 C ANISOU 2097 CB GLU A1066 7291 3693 5665 -1317 -398 -757 C ATOM 2098 CG GLU A1066 63.604 -2.854 -23.562 1.00 49.71 C ANISOU 2098 CG GLU A1066 8221 4523 6144 -1554 -692 -896 C ATOM 2099 CD GLU A1066 62.109 -3.110 -23.531 1.00 63.75 C ANISOU 2099 CD GLU A1066 9666 6315 8240 -1677 -832 -1063 C ATOM 2100 OE1 GLU A1066 61.658 -3.905 -22.680 1.00 61.92 O ANISOU 2100 OE1 GLU A1066 9295 5958 8275 -1581 -598 -1195 O ATOM 2101 OE2 GLU A1066 61.384 -2.512 -24.354 1.00 77.06 O ANISOU 2101 OE2 GLU A1066 11213 8137 9930 -1843 -1190 -1040 O ATOM 2102 N MET A1067 66.715 -2.600 -19.958 1.00 36.11 N ANISOU 2102 N MET A1067 6270 2643 4807 -697 178 -363 N ATOM 2103 CA MET A1067 67.014 -2.186 -18.591 1.00 36.27 C ANISOU 2103 CA MET A1067 5961 2740 5080 -520 202 -222 C ATOM 2104 C MET A1067 68.366 -1.486 -18.465 1.00 34.85 C ANISOU 2104 C MET A1067 5757 2609 4875 -316 232 45 C ATOM 2105 O MET A1067 69.264 -1.688 -19.281 1.00 35.14 O ANISOU 2105 O MET A1067 6064 2601 4686 -210 362 143 O ATOM 2106 CB MET A1067 66.975 -3.393 -17.653 1.00 36.81 C ANISOU 2106 CB MET A1067 6058 2812 5115 -420 375 -331 C ATOM 2107 CG MET A1067 65.674 -4.176 -17.693 1.00 35.38 C ANISOU 2107 CG MET A1067 5862 2585 4997 -567 346 -534 C ATOM 2108 SD MET A1067 65.843 -5.788 -16.903 1.00 44.18 S ANISOU 2108 SD MET A1067 7128 3670 5987 -470 596 -604 S ATOM 2109 CE MET A1067 64.207 -6.466 -17.157 1.00 48.88 C ANISOU 2109 CE MET A1067 7677 4180 6715 -652 504 -805 C ATOM 2110 N ARG A1068 68.483 -0.657 -17.433 1.00 32.39 N ANISOU 2110 N ARG A1068 5091 2404 4811 -243 102 169 N ATOM 2111 CA ARG A1068 69.718 0.035 -17.083 1.00 32.92 C ANISOU 2111 CA ARG A1068 5016 2582 4911 -67 33 400 C ATOM 2112 C ARG A1068 69.971 -0.181 -15.597 1.00 36.25 C ANISOU 2112 C ARG A1068 5349 3093 5329 -6 -30 331 C ATOM 2113 O ARG A1068 69.031 -0.178 -14.807 1.00 38.15 O ANISOU 2113 O ARG A1068 5564 3339 5594 -88 -65 216 O ATOM 2114 CB ARG A1068 69.623 1.532 -17.390 1.00 27.29 C ANISOU 2114 CB ARG A1068 4202 2010 4156 -78 -14 529 C ATOM 2115 CG ARG A1068 69.106 1.861 -18.778 1.00 28.12 C ANISOU 2115 CG ARG A1068 4241 2105 4339 -241 -241 640 C ATOM 2116 CD ARG A1068 70.131 1.516 -19.835 1.00 21.91 C ANISOU 2116 CD ARG A1068 3627 1391 3306 -107 -148 801 C ATOM 2117 NE ARG A1068 69.608 1.689 -21.185 1.00 23.96 N ANISOU 2117 NE ARG A1068 3913 1841 3348 -254 -292 786 N ATOM 2118 CZ ARG A1068 69.081 0.711 -21.915 1.00 26.19 C ANISOU 2118 CZ ARG A1068 4501 2097 3354 -374 -224 549 C ATOM 2119 NH1 ARG A1068 69.000 -0.518 -21.423 1.00 26.51 N ANISOU 2119 NH1 ARG A1068 4821 1917 3334 -363 15 308 N ATOM 2120 NH2 ARG A1068 68.635 0.962 -23.140 1.00 28.39 N ANISOU 2120 NH2 ARG A1068 4820 2557 3408 -510 -408 554 N ATOM 2121 N PHE A1069 71.227 -0.368 -15.208 1.00 33.00 N ANISOU 2121 N PHE A1069 4956 2725 4857 140 15 414 N ATOM 2122 CA PHE A1069 71.535 -0.625 -13.805 1.00 24.80 C ANISOU 2122 CA PHE A1069 3934 1688 3803 198 73 378 C ATOM 2123 C PHE A1069 72.658 0.268 -13.288 1.00 30.83 C ANISOU 2123 C PHE A1069 4629 2530 4555 288 -69 492 C ATOM 2124 O PHE A1069 73.704 0.397 -13.922 1.00 38.26 O ANISOU 2124 O PHE A1069 5541 3527 5471 390 -49 593 O ATOM 2125 CB PHE A1069 71.907 -2.097 -13.597 1.00 19.84 C ANISOU 2125 CB PHE A1069 3509 999 3031 278 334 306 C ATOM 2126 CG PHE A1069 70.784 -3.059 -13.881 1.00 30.75 C ANISOU 2126 CG PHE A1069 5053 2302 4329 176 481 141 C ATOM 2127 CD1 PHE A1069 69.884 -3.410 -12.886 1.00 35.13 C ANISOU 2127 CD1 PHE A1069 5657 2823 4866 100 546 45 C ATOM 2128 CD2 PHE A1069 70.635 -3.623 -15.138 1.00 40.27 C ANISOU 2128 CD2 PHE A1069 6385 3456 5460 150 568 80 C ATOM 2129 CE1 PHE A1069 68.852 -4.300 -13.144 1.00 40.68 C ANISOU 2129 CE1 PHE A1069 6480 3457 5519 -7 674 -94 C ATOM 2130 CE2 PHE A1069 69.606 -4.515 -15.401 1.00 37.89 C ANISOU 2130 CE2 PHE A1069 6234 3074 5090 32 677 -91 C ATOM 2131 CZ PHE A1069 68.715 -4.853 -14.404 1.00 33.95 C ANISOU 2131 CZ PHE A1069 5718 2561 4622 -47 709 -169 C ATOM 2132 N ILE A1070 72.425 0.885 -12.133 1.00 33.80 N ANISOU 2132 N ILE A1070 4106 4130 4604 491 644 -582 N ATOM 2133 CA ILE A1070 73.441 1.687 -11.461 1.00 31.73 C ANISOU 2133 CA ILE A1070 3667 4029 4360 616 594 -543 C ATOM 2134 C ILE A1070 73.743 1.114 -10.077 1.00 32.81 C ANISOU 2134 C ILE A1070 3771 4171 4523 883 626 -500 C ATOM 2135 O ILE A1070 73.008 1.366 -9.122 1.00 24.36 O ANISOU 2135 O ILE A1070 2873 3004 3379 848 604 -545 O ATOM 2136 CB ILE A1070 73.001 3.156 -11.305 1.00 32.98 C ANISOU 2136 CB ILE A1070 3781 4250 4498 341 390 -712 C ATOM 2137 CG1 ILE A1070 72.408 3.690 -12.611 1.00 31.69 C ANISOU 2137 CG1 ILE A1070 3634 4056 4352 59 328 -745 C ATOM 2138 CG2 ILE A1070 74.173 4.014 -10.850 1.00 26.38 C ANISOU 2138 CG2 ILE A1070 2554 3715 3753 426 150 -777 C ATOM 2139 CD1 ILE A1070 73.435 3.982 -13.673 1.00 37.96 C ANISOU 2139 CD1 ILE A1070 4276 4929 5220 67 323 -747 C ATOM 2140 N ILE A1071 74.819 0.340 -9.971 1.00 33.26 N ANISOU 2140 N ILE A1071 3617 4254 4767 1060 671 -391 N ATOM 2141 CA ILE A1071 75.192 -0.270 -8.695 1.00 40.45 C ANISOU 2141 CA ILE A1071 4570 5140 5661 1322 681 -147 C ATOM 2142 C ILE A1071 76.279 0.541 -7.995 1.00 36.65 C ANISOU 2142 C ILE A1071 3839 4952 5136 1427 344 82 C ATOM 2143 O ILE A1071 77.376 0.696 -8.520 1.00 35.87 O ANISOU 2143 O ILE A1071 3425 5034 5170 1471 272 234 O ATOM 2144 CB ILE A1071 75.684 -1.722 -8.874 1.00 42.38 C ANISOU 2144 CB ILE A1071 4848 5275 5979 1444 851 -25 C ATOM 2145 CG1 ILE A1071 74.548 -2.626 -9.356 1.00 38.10 C ANISOU 2145 CG1 ILE A1071 4556 4521 5399 1278 973 -189 C ATOM 2146 CG2 ILE A1071 76.245 -2.256 -7.570 1.00 48.12 C ANISOU 2146 CG2 ILE A1071 5580 6035 6667 1721 824 249 C ATOM 2147 CD1 ILE A1071 74.460 -2.756 -10.857 1.00 43.40 C ANISOU 2147 CD1 ILE A1071 5210 5203 6077 1134 974 -329 C ATOM 2148 N ILE A1072 75.972 1.044 -6.803 1.00 32.25 N ANISOU 2148 N ILE A1072 3449 4431 4376 1389 76 107 N ATOM 2149 CA ILE A1072 76.885 1.930 -6.088 1.00 33.57 C ANISOU 2149 CA ILE A1072 3459 4837 4458 1348 -378 274 C ATOM 2150 C ILE A1072 77.259 1.388 -4.714 1.00 37.64 C ANISOU 2150 C ILE A1072 4084 5363 4853 1590 -505 504 C ATOM 2151 O ILE A1072 76.390 0.960 -3.953 1.00 32.69 O ANISOU 2151 O ILE A1072 3768 4578 4072 1686 -385 457 O ATOM 2152 CB ILE A1072 76.271 3.334 -5.906 1.00 38.45 C ANISOU 2152 CB ILE A1072 4205 5512 4892 1062 -698 73 C ATOM 2153 CG1 ILE A1072 75.705 3.852 -7.230 1.00 38.39 C ANISOU 2153 CG1 ILE A1072 4137 5471 4980 822 -543 -181 C ATOM 2154 CG2 ILE A1072 77.297 4.303 -5.331 1.00 30.98 C ANISOU 2154 CG2 ILE A1072 3084 4793 3895 987 -1214 239 C ATOM 2155 CD1 ILE A1072 74.843 5.085 -7.077 1.00 34.01 C ANISOU 2155 CD1 ILE A1072 3771 4920 4230 564 -771 -409 C ATOM 2156 N GLY A1073 78.550 1.412 -4.395 1.00 39.38 N ANISOU 2156 N GLY A1073 4039 5775 5149 1695 -748 775 N ATOM 2157 CA GLY A1073 79.004 1.041 -3.067 1.00 44.14 C ANISOU 2157 CA GLY A1073 4753 6385 5634 1859 -924 975 C ATOM 2158 C GLY A1073 80.317 0.283 -3.028 1.00 55.56 C ANISOU 2158 C GLY A1073 5960 7883 7265 1975 -884 1218 C ATOM 2159 O GLY A1073 80.801 -0.205 -4.049 1.00 57.57 O ANISOU 2159 O GLY A1073 5998 8155 7720 2008 -632 1254 O ATOM 2160 N LYS A1074 80.894 0.191 -1.833 1.00 55.44 N ANISOU 2160 N LYS A1074 6019 7882 7161 2033 -1130 1362 N ATOM 2161 CA LYS A1074 82.122 -0.562 -1.617 1.00 50.17 C ANISOU 2161 CA LYS A1074 5163 7274 6625 2174 -1111 1585 C ATOM 2162 C LYS A1074 81.834 -1.776 -0.743 1.00 54.13 C ANISOU 2162 C LYS A1074 5868 7665 7036 2445 -879 1687 C ATOM 2163 O LYS A1074 80.690 -2.010 -0.354 1.00 47.15 O ANISOU 2163 O LYS A1074 5270 6646 5998 2514 -719 1579 O ATOM 2164 CB LYS A1074 83.189 0.311 -0.956 1.00 48.29 C ANISOU 2164 CB LYS A1074 4840 7123 6384 2024 -1606 1647 C ATOM 2165 CG LYS A1074 83.196 1.757 -1.411 1.00 57.37 C ANISOU 2165 CG LYS A1074 5965 8306 7525 1735 -1910 1446 C ATOM 2166 CD LYS A1074 84.113 2.590 -0.531 1.00 77.33 C ANISOU 2166 CD LYS A1074 8547 10891 9944 1697 -2350 1407 C ATOM 2167 CE LYS A1074 84.003 4.070 -0.851 1.00 85.12 C ANISOU 2167 CE LYS A1074 9558 12011 10771 1506 -2483 1147 C ATOM 2168 NZ LYS A1074 84.855 4.891 0.055 1.00 88.92 N ANISOU 2168 NZ LYS A1074 10026 12692 11068 1501 -2722 1167 N ATOM 2169 N GLY A1075 82.874 -2.540 -0.427 1.00 55.84 N ANISOU 2169 N GLY A1075 5946 7932 7340 2591 -850 1890 N ATOM 2170 CA GLY A1075 82.727 -3.669 0.473 1.00 62.19 C ANISOU 2170 CA GLY A1075 6931 8638 8059 2828 -661 1994 C ATOM 2171 C GLY A1075 83.573 -4.870 0.105 1.00 60.47 C ANISOU 2171 C GLY A1075 6547 8436 7994 3013 -373 2166 C ATOM 2172 O GLY A1075 84.778 -4.752 -0.117 1.00 64.52 O ANISOU 2172 O GLY A1075 6790 9098 8628 2998 -510 2315 O ATOM 2173 N ASP A1076 82.931 -6.033 0.051 1.00 60.99 N ANISOU 2173 N ASP A1076 6795 8333 8045 3171 26 2140 N ATOM 2174 CA ASP A1076 83.605 -7.286 -0.264 1.00 69.31 C ANISOU 2174 CA ASP A1076 7766 9361 9206 3345 322 2281 C ATOM 2175 C ASP A1076 84.264 -7.220 -1.639 1.00 68.43 C ANISOU 2175 C ASP A1076 7409 9325 9265 3285 442 2288 C ATOM 2176 O ASP A1076 83.580 -7.053 -2.649 1.00 66.02 O ANISOU 2176 O ASP A1076 7159 8923 9002 3173 609 2100 O ATOM 2177 CB ASP A1076 82.608 -8.447 -0.202 1.00 80.64 C ANISOU 2177 CB ASP A1076 9489 10555 10595 3443 700 2196 C ATOM 2178 CG ASP A1076 83.278 -9.804 -0.298 1.00 97.90 C ANISOU 2178 CG ASP A1076 11650 12699 12849 3630 962 2349 C ATOM 2179 OD1 ASP A1076 84.458 -9.920 0.093 1.00104.60 O ANISOU 2179 OD1 ASP A1076 12301 13712 13729 3744 834 2560 O ATOM 2180 OD2 ASP A1076 82.616 -10.760 -0.756 1.00104.82 O ANISOU 2180 OD2 ASP A1076 12712 13369 13746 3646 1276 2259 O ATOM 2181 N PRO A1077 85.603 -7.343 -1.679 1.00 73.46 N ANISOU 2181 N PRO A1077 7785 10135 9992 3354 356 2505 N ATOM 2182 CA PRO A1077 86.375 -7.285 -2.926 1.00 68.98 C ANISOU 2182 CA PRO A1077 6978 9666 9566 3317 475 2557 C ATOM 2183 C PRO A1077 85.929 -8.336 -3.938 1.00 74.84 C ANISOU 2183 C PRO A1077 7878 10224 10333 3404 905 2456 C ATOM 2184 O PRO A1077 86.053 -8.121 -5.145 1.00 78.71 O ANISOU 2184 O PRO A1077 8286 10727 10894 3325 1016 2385 O ATOM 2185 CB PRO A1077 87.814 -7.546 -2.464 1.00 66.12 C ANISOU 2185 CB PRO A1077 6372 9488 9264 3433 355 2849 C ATOM 2186 CG PRO A1077 87.680 -8.212 -1.132 1.00 65.95 C ANISOU 2186 CG PRO A1077 6520 9402 9135 3591 312 2926 C ATOM 2187 CD PRO A1077 86.469 -7.592 -0.514 1.00 72.00 C ANISOU 2187 CD PRO A1077 7531 10055 9770 3477 153 2722 C ATOM 2188 N GLU A1078 85.413 -9.457 -3.445 1.00 78.28 N ANISOU 2188 N GLU A1078 8563 10478 10701 3547 1120 2443 N ATOM 2189 CA GLU A1078 84.879 -10.497 -4.313 1.00 72.82 C ANISOU 2189 CA GLU A1078 8084 9563 10020 3587 1466 2319 C ATOM 2190 C GLU A1078 83.593 -10.015 -4.983 1.00 64.56 C ANISOU 2190 C GLU A1078 7218 8350 8962 3373 1501 2018 C ATOM 2191 O GLU A1078 83.404 -10.193 -6.189 1.00 65.84 O ANISOU 2191 O GLU A1078 7429 8419 9169 3299 1649 1881 O ATOM 2192 CB GLU A1078 84.628 -11.782 -3.521 1.00 69.19 C ANISOU 2192 CB GLU A1078 7843 8948 9500 3757 1643 2389 C ATOM 2193 CG GLU A1078 84.290 -12.990 -4.380 1.00 82.68 C ANISOU 2193 CG GLU A1078 9759 10429 11227 3804 1953 2302 C ATOM 2194 CD GLU A1078 84.280 -14.285 -3.588 1.00 97.93 C ANISOU 2194 CD GLU A1078 11856 12238 13115 3985 2113 2422 C ATOM 2195 OE1 GLU A1078 84.460 -14.231 -2.353 1.00101.99 O ANISOU 2195 OE1 GLU A1078 12337 12841 13574 4072 1998 2558 O ATOM 2196 OE2 GLU A1078 84.096 -15.358 -4.203 1.00 97.60 O ANISOU 2196 OE2 GLU A1078 11985 12010 13089 4041 2337 2377 O ATOM 2197 N LEU A1079 82.717 -9.395 -4.197 1.00 51.23 N ANISOU 2197 N LEU A1079 5638 6627 7202 3275 1352 1919 N ATOM 2198 CA LEU A1079 81.473 -8.840 -4.721 1.00 51.34 C ANISOU 2198 CA LEU A1079 5808 6499 7199 3062 1367 1646 C ATOM 2199 C LEU A1079 81.737 -7.619 -5.602 1.00 61.07 C ANISOU 2199 C LEU A1079 6831 7883 8492 2905 1213 1559 C ATOM 2200 O LEU A1079 81.030 -7.389 -6.587 1.00 61.75 O ANISOU 2200 O LEU A1079 7001 7857 8603 2737 1297 1333 O ATOM 2201 CB LEU A1079 80.523 -8.470 -3.580 1.00 49.25 C ANISOU 2201 CB LEU A1079 5718 6178 6817 3027 1254 1598 C ATOM 2202 CG LEU A1079 79.983 -9.640 -2.755 1.00 65.16 C ANISOU 2202 CG LEU A1079 7974 8018 8767 3135 1429 1652 C ATOM 2203 CD1 LEU A1079 78.982 -9.151 -1.721 1.00 64.28 C ANISOU 2203 CD1 LEU A1079 8042 7865 8518 3088 1328 1600 C ATOM 2204 CD2 LEU A1079 79.357 -10.696 -3.656 1.00 67.02 C ANISOU 2204 CD2 LEU A1079 8380 8013 9072 3058 1698 1522 C ATOM 2205 N GLU A1080 82.754 -6.839 -5.242 1.00 63.07 N ANISOU 2205 N GLU A1080 6806 8388 8770 2931 961 1740 N ATOM 2206 CA GLU A1080 83.166 -5.701 -6.058 1.00 58.94 C ANISOU 2206 CA GLU A1080 6045 8032 8319 2768 797 1701 C ATOM 2207 C GLU A1080 83.656 -6.183 -7.417 1.00 51.94 C ANISOU 2207 C GLU A1080 5095 7124 7516 2781 1030 1684 C ATOM 2208 O GLU A1080 83.320 -5.604 -8.449 1.00 48.95 O ANISOU 2208 O GLU A1080 4701 6730 7168 2622 1052 1507 O ATOM 2209 CB GLU A1080 84.261 -4.888 -5.361 1.00 61.85 C ANISOU 2209 CB GLU A1080 6133 8658 8708 2749 438 1922 C ATOM 2210 CG GLU A1080 83.763 -4.016 -4.218 1.00 72.04 C ANISOU 2210 CG GLU A1080 7504 9983 9883 2660 91 1885 C ATOM 2211 CD GLU A1080 84.853 -3.144 -3.625 1.00 80.02 C ANISOU 2211 CD GLU A1080 8288 11203 10912 2560 -336 2048 C ATOM 2212 OE1 GLU A1080 84.720 -1.903 -3.684 1.00 78.93 O ANISOU 2212 OE1 GLU A1080 8103 11134 10753 2329 -643 1940 O ATOM 2213 OE2 GLU A1080 85.840 -3.697 -3.096 1.00 82.67 O ANISOU 2213 OE2 GLU A1080 8516 11614 11280 2694 -374 2265 O ATOM 2214 N GLY A1081 84.446 -7.252 -7.405 1.00 49.29 N ANISOU 2214 N GLY A1081 4743 6786 7197 2982 1198 1869 N ATOM 2215 CA GLY A1081 84.963 -7.839 -8.627 1.00 50.55 C ANISOU 2215 CA GLY A1081 4888 6918 7400 3046 1419 1883 C ATOM 2216 C GLY A1081 83.865 -8.454 -9.473 1.00 53.03 C ANISOU 2216 C GLY A1081 5510 6960 7678 2974 1623 1604 C ATOM 2217 O GLY A1081 83.913 -8.397 -10.702 1.00 48.09 O ANISOU 2217 O GLY A1081 4894 6308 7071 2918 1708 1496 O ATOM 2218 N TRP A1082 82.880 -9.053 -8.811 1.00 47.53 N ANISOU 2218 N TRP A1082 5068 6062 6929 2964 1680 1495 N ATOM 2219 CA TRP A1082 81.715 -9.607 -9.494 1.00 47.78 C ANISOU 2219 CA TRP A1082 5386 5830 6938 2837 1809 1231 C ATOM 2220 C TRP A1082 80.958 -8.485 -10.206 1.00 48.31 C ANISOU 2220 C TRP A1082 5443 5903 7010 2578 1691 980 C ATOM 2221 O TRP A1082 80.578 -8.608 -11.380 1.00 47.09 O ANISOU 2221 O TRP A1082 5381 5651 6859 2470 1751 796 O ATOM 2222 CB TRP A1082 80.812 -10.333 -8.491 1.00 47.39 C ANISOU 2222 CB TRP A1082 5569 5595 6843 2845 1860 1207 C ATOM 2223 CG TRP A1082 79.671 -11.103 -9.095 1.00 44.34 C ANISOU 2223 CG TRP A1082 5453 4941 6452 2713 1974 993 C ATOM 2224 CD1 TRP A1082 79.405 -11.278 -10.422 1.00 43.68 C ANISOU 2224 CD1 TRP A1082 5440 4768 6390 2612 2019 817 C ATOM 2225 CD2 TRP A1082 78.643 -11.805 -8.384 1.00 49.02 C ANISOU 2225 CD2 TRP A1082 6265 5339 7021 2665 2030 954 C ATOM 2226 NE1 TRP A1082 78.274 -12.042 -10.581 1.00 44.36 N ANISOU 2226 NE1 TRP A1082 5761 4619 6473 2497 2074 671 N ATOM 2227 CE2 TRP A1082 77.787 -12.378 -9.345 1.00 43.24 C ANISOU 2227 CE2 TRP A1082 5706 4409 6314 2521 2092 760 C ATOM 2228 CE3 TRP A1082 78.362 -12.002 -7.027 1.00 47.43 C ANISOU 2228 CE3 TRP A1082 6124 5122 6776 2736 2027 1079 C ATOM 2229 CZ2 TRP A1082 76.671 -13.136 -8.995 1.00 44.07 C ANISOU 2229 CZ2 TRP A1082 6013 4308 6425 2431 2149 704 C ATOM 2230 CZ3 TRP A1082 77.252 -12.754 -6.681 1.00 44.27 C ANISOU 2230 CZ3 TRP A1082 5940 4512 6371 2653 2111 1020 C ATOM 2231 CH2 TRP A1082 76.421 -13.312 -7.661 1.00 44.49 C ANISOU 2231 CH2 TRP A1082 6109 4349 6447 2496 2171 841 C ATOM 2232 N ALA A1083 80.761 -7.382 -9.489 1.00 40.58 N ANISOU 2232 N ALA A1083 4351 5048 6019 2488 1505 980 N ATOM 2233 CA ALA A1083 80.099 -6.210 -10.045 1.00 42.08 C ANISOU 2233 CA ALA A1083 4510 5270 6207 2251 1381 759 C ATOM 2234 C ALA A1083 80.867 -5.651 -11.242 1.00 46.17 C ANISOU 2234 C ALA A1083 4832 5931 6779 2207 1361 752 C ATOM 2235 O ALA A1083 80.270 -5.297 -12.257 1.00 45.99 O ANISOU 2235 O ALA A1083 4882 5849 6744 2032 1366 520 O ATOM 2236 CB ALA A1083 79.932 -5.142 -8.979 1.00 36.26 C ANISOU 2236 CB ALA A1083 3673 4664 5439 2213 1167 809 C ATOM 2237 N ARG A1084 82.190 -5.578 -11.122 1.00 45.10 N ANISOU 2237 N ARG A1084 4447 5995 6693 2358 1326 1021 N ATOM 2238 CA ARG A1084 83.025 -5.054 -12.200 1.00 50.18 C ANISOU 2238 CA ARG A1084 4891 6790 7387 2328 1315 1069 C ATOM 2239 C ARG A1084 83.032 -5.980 -13.414 1.00 49.77 C ANISOU 2239 C ARG A1084 5000 6595 7314 2400 1537 981 C ATOM 2240 O ARG A1084 83.154 -5.522 -14.552 1.00 46.95 O ANISOU 2240 O ARG A1084 4598 6280 6963 2318 1545 886 O ATOM 2241 CB ARG A1084 84.458 -4.824 -11.711 1.00 56.60 C ANISOU 2241 CB ARG A1084 5394 7853 8260 2456 1210 1415 C ATOM 2242 CG ARG A1084 84.612 -3.649 -10.753 1.00 58.41 C ANISOU 2242 CG ARG A1084 5418 8263 8514 2326 888 1498 C ATOM 2243 CD ARG A1084 84.293 -2.327 -11.434 1.00 65.69 C ANISOU 2243 CD ARG A1084 6250 9255 9456 2069 730 1327 C ATOM 2244 NE ARG A1084 84.266 -1.214 -10.487 1.00 75.91 N ANISOU 2244 NE ARG A1084 7418 10679 10747 1914 380 1362 N ATOM 2245 CZ ARG A1084 83.958 0.038 -10.810 1.00 73.22 C ANISOU 2245 CZ ARG A1084 7016 10397 10406 1666 178 1216 C ATOM 2246 NH1 ARG A1084 83.651 0.348 -12.063 1.00 63.87 N ANISOU 2246 NH1 ARG A1084 5866 9166 9234 1556 313 1031 N ATOM 2247 NH2 ARG A1084 83.956 0.984 -9.880 1.00 71.48 N ANISOU 2247 NH2 ARG A1084 6743 10265 10151 1519 -179 1235 N ATOM 2248 N SER A1085 82.904 -7.281 -13.170 1.00 50.78 N ANISOU 2248 N SER A1085 5325 6558 7412 2558 1700 1018 N ATOM 2249 CA SER A1085 82.861 -8.253 -14.257 1.00 48.24 C ANISOU 2249 CA SER A1085 5183 6085 7060 2639 1881 938 C ATOM 2250 C SER A1085 81.547 -8.115 -15.009 1.00 41.84 C ANISOU 2250 C SER A1085 4588 5098 6212 2418 1855 612 C ATOM 2251 O SER A1085 81.516 -8.143 -16.241 1.00 58.90 O ANISOU 2251 O SER A1085 6812 7218 8348 2419 1943 547 O ATOM 2252 CB SER A1085 83.028 -9.678 -13.728 1.00 49.91 C ANISOU 2252 CB SER A1085 5554 6161 7251 2855 2042 1069 C ATOM 2253 OG SER A1085 81.914 -10.065 -12.946 1.00 63.46 O ANISOU 2253 OG SER A1085 7473 7691 8946 2758 2020 937 O ATOM 2254 N LEU A1086 80.460 -7.958 -14.261 1.00 39.39 N ANISOU 2254 N LEU A1086 4397 4685 5885 2257 1762 465 N ATOM 2255 CA LEU A1086 79.159 -7.728 -14.876 1.00 36.98 C ANISOU 2255 CA LEU A1086 4278 4233 5539 2043 1743 229 C ATOM 2256 C LEU A1086 79.133 -6.398 -15.627 1.00 40.13 C ANISOU 2256 C LEU A1086 4537 4780 5931 1878 1626 115 C ATOM 2257 O LEU A1086 78.466 -6.272 -16.653 1.00 48.58 O ANISOU 2257 O LEU A1086 5727 5766 6967 1762 1648 -30 O ATOM 2258 CB LEU A1086 78.053 -7.766 -13.822 1.00 35.06 C ANISOU 2258 CB LEU A1086 4167 3879 5274 1911 1671 149 C ATOM 2259 CG LEU A1086 77.674 -9.165 -13.336 1.00 55.36 C ANISOU 2259 CG LEU A1086 6945 6240 7847 2016 1808 216 C ATOM 2260 CD1 LEU A1086 76.712 -9.091 -12.163 1.00 45.28 C ANISOU 2260 CD1 LEU A1086 5758 4895 6552 1904 1738 188 C ATOM 2261 CD2 LEU A1086 77.072 -9.974 -14.477 1.00 61.17 C ANISOU 2261 CD2 LEU A1086 7890 6773 8576 1986 1934 122 C ATOM 2262 N GLU A1087 79.865 -5.413 -15.115 1.00 47.34 N ANISOU 2262 N GLU A1087 5192 5914 6880 1865 1490 194 N ATOM 2263 CA GLU A1087 79.944 -4.100 -15.751 1.00 45.21 C ANISOU 2263 CA GLU A1087 4765 5802 6612 1708 1371 107 C ATOM 2264 C GLU A1087 80.703 -4.177 -17.070 1.00 44.56 C ANISOU 2264 C GLU A1087 4619 5770 6544 1802 1488 182 C ATOM 2265 O GLU A1087 80.291 -3.593 -18.072 1.00 53.13 O ANISOU 2265 O GLU A1087 5735 6857 7594 1679 1474 45 O ATOM 2266 CB GLU A1087 80.618 -3.084 -14.826 1.00 45.43 C ANISOU 2266 CB GLU A1087 4526 6039 6698 1686 1201 242 C ATOM 2267 CG GLU A1087 80.724 -1.687 -15.426 1.00 55.15 C ANISOU 2267 CG GLU A1087 5585 7430 7940 1497 1051 151 C ATOM 2268 CD GLU A1087 81.539 -0.737 -14.569 1.00 68.25 C ANISOU 2268 CD GLU A1087 6962 9294 9676 1484 860 377 C ATOM 2269 OE1 GLU A1087 82.561 -1.176 -14.002 1.00 82.54 O ANISOU 2269 OE1 GLU A1087 8626 11198 11538 1663 859 671 O ATOM 2270 OE2 GLU A1087 81.156 0.449 -14.462 1.00 60.54 O ANISOU 2270 OE2 GLU A1087 5916 8392 8695 1281 677 264 O ATOM 2271 N GLU A1088 81.819 -4.897 -17.059 1.00 50.33 N ANISOU 2271 N GLU A1088 5333 6801 6990 990 1302 -50 N ATOM 2272 CA GLU A1088 82.616 -5.078 -18.264 1.00 61.67 C ANISOU 2272 CA GLU A1088 6797 8233 8403 900 1649 -265 C ATOM 2273 C GLU A1088 81.868 -5.936 -19.280 1.00 61.61 C ANISOU 2273 C GLU A1088 7158 7989 8264 1018 1630 -189 C ATOM 2274 O GLU A1088 82.083 -5.816 -20.487 1.00 56.16 O ANISOU 2274 O GLU A1088 6711 7209 7420 882 1913 -296 O ATOM 2275 CB GLU A1088 83.964 -5.718 -17.927 1.00 66.18 C ANISOU 2275 CB GLU A1088 6855 9046 9246 1044 1730 -534 C ATOM 2276 CG GLU A1088 84.959 -5.706 -19.076 1.00 81.04 C ANISOU 2276 CG GLU A1088 8679 10976 11137 888 2164 -828 C ATOM 2277 CD GLU A1088 85.962 -6.837 -18.987 1.00 94.29 C ANISOU 2277 CD GLU A1088 9923 12812 13092 1160 2166 -1086 C ATOM 2278 OE1 GLU A1088 85.624 -7.884 -18.393 1.00 96.94 O ANISOU 2278 OE1 GLU A1088 10194 13104 13535 1505 1826 -969 O ATOM 2279 OE2 GLU A1088 87.086 -6.682 -19.509 1.00102.66 O ANISOU 2279 OE2 GLU A1088 10713 14024 14267 1027 2517 -1421 O ATOM 2280 N LYS A1089 80.986 -6.799 -18.784 1.00 59.78 N ANISOU 2280 N LYS A1089 6981 7649 8084 1256 1309 -16 N ATOM 2281 CA LYS A1089 80.250 -7.716 -19.646 1.00 48.19 C ANISOU 2281 CA LYS A1089 5814 5959 6535 1384 1255 29 C ATOM 2282 C LYS A1089 79.064 -7.038 -20.333 1.00 43.99 C ANISOU 2282 C LYS A1089 5753 5215 5744 1241 1202 158 C ATOM 2283 O LYS A1089 78.785 -7.301 -21.502 1.00 38.75 O ANISOU 2283 O LYS A1089 5407 4396 4921 1232 1296 105 O ATOM 2284 CB LYS A1089 79.766 -8.921 -18.841 1.00 52.83 C ANISOU 2284 CB LYS A1089 6290 6487 7297 1667 959 143 C ATOM 2285 CG LYS A1089 79.504 -10.164 -19.671 1.00 57.45 C ANISOU 2285 CG LYS A1089 7034 6891 7902 1840 957 92 C ATOM 2286 CD LYS A1089 80.222 -11.366 -19.077 1.00 65.29 C ANISOU 2286 CD LYS A1089 7730 7938 9138 2122 873 27 C ATOM 2287 CE LYS A1089 79.841 -11.566 -17.617 1.00 66.27 C ANISOU 2287 CE LYS A1089 7732 8080 9368 2247 588 219 C ATOM 2288 NZ LYS A1089 80.597 -12.684 -16.986 1.00 67.72 N ANISOU 2288 NZ LYS A1089 7681 8294 9757 2554 471 168 N ATOM 2289 N HIS A1090 78.371 -6.165 -19.609 1.00 37.80 N ANISOU 2289 N HIS A1090 5018 4426 4917 1149 1033 305 N ATOM 2290 CA HIS A1090 77.171 -5.528 -20.143 1.00 39.65 C ANISOU 2290 CA HIS A1090 5669 4458 4940 1067 909 408 C ATOM 2291 C HIS A1090 77.266 -4.002 -20.138 1.00 42.00 C ANISOU 2291 C HIS A1090 6111 4769 5077 825 1011 432 C ATOM 2292 O HIS A1090 77.669 -3.396 -19.145 1.00 45.99 O ANISOU 2292 O HIS A1090 6347 5435 5691 744 1008 450 O ATOM 2293 CB HIS A1090 75.941 -5.978 -19.352 1.00 43.47 C ANISOU 2293 CB HIS A1090 6131 4857 5528 1206 573 546 C ATOM 2294 CG HIS A1090 75.827 -7.465 -19.209 1.00 48.19 C ANISOU 2294 CG HIS A1090 6605 5408 6296 1421 482 539 C ATOM 2295 ND1 HIS A1090 75.930 -8.105 -17.994 1.00 45.86 N ANISOU 2295 ND1 HIS A1090 6025 5198 6201 1546 359 615 N ATOM 2296 CD2 HIS A1090 75.629 -8.437 -20.132 1.00 50.86 C ANISOU 2296 CD2 HIS A1090 7103 5601 6621 1535 498 463 C ATOM 2297 CE1 HIS A1090 75.794 -9.409 -18.172 1.00 49.79 C ANISOU 2297 CE1 HIS A1090 6528 5584 6807 1723 310 599 C ATOM 2298 NE2 HIS A1090 75.611 -9.635 -19.460 1.00 50.81 N ANISOU 2298 NE2 HIS A1090 6901 5579 6825 1716 393 496 N ATOM 2299 N GLY A1091 76.885 -3.389 -21.255 1.00 47.60 N ANISOU 2299 N GLY A1091 7279 5290 5515 718 1089 428 N ATOM 2300 CA GLY A1091 76.954 -1.946 -21.403 1.00 53.03 C ANISOU 2300 CA GLY A1091 8210 5923 6014 488 1201 458 C ATOM 2301 C GLY A1091 75.857 -1.208 -20.660 1.00 49.91 C ANISOU 2301 C GLY A1091 7882 5457 5625 509 886 588 C ATOM 2302 O GLY A1091 75.953 -0.001 -20.435 1.00 45.27 O ANISOU 2302 O GLY A1091 7399 4849 4951 335 943 618 O ATOM 2303 N ASN A1092 74.810 -1.935 -20.280 1.00 46.49 N ANISOU 2303 N ASN A1092 7382 4977 5307 711 572 644 N ATOM 2304 CA ASN A1092 73.691 -1.350 -19.548 1.00 37.69 C ANISOU 2304 CA ASN A1092 6279 3808 4234 744 278 725 C ATOM 2305 C ASN A1092 73.848 -1.540 -18.043 1.00 32.84 C ANISOU 2305 C ASN A1092 5204 3403 3870 761 209 771 C ATOM 2306 O ASN A1092 72.872 -1.511 -17.293 1.00 29.52 O ANISOU 2306 O ASN A1092 4706 2967 3545 825 -26 819 O ATOM 2307 CB ASN A1092 72.365 -1.952 -20.021 1.00 35.09 C ANISOU 2307 CB ASN A1092 6145 3297 3891 924 -10 712 C ATOM 2308 CG ASN A1092 72.311 -3.461 -19.847 1.00 41.60 C ANISOU 2308 CG ASN A1092 6730 4167 4909 1075 -43 687 C ATOM 2309 OD1 ASN A1092 73.306 -4.159 -20.048 1.00 40.38 O ANISOU 2309 OD1 ASN A1092 6446 4102 4796 1087 167 653 O ATOM 2310 ND2 ASN A1092 71.143 -3.971 -19.471 1.00 35.19 N ANISOU 2310 ND2 ASN A1092 5858 3282 4233 1187 -297 681 N ATOM 2311 N VAL A1093 75.089 -1.738 -17.612 1.00 33.36 N ANISOU 2311 N VAL A1093 4971 3670 4036 708 416 732 N ATOM 2312 CA VAL A1093 75.404 -1.881 -16.197 1.00 27.07 C ANISOU 2312 CA VAL A1093 3771 3081 3433 741 343 766 C ATOM 2313 C VAL A1093 76.597 -1.004 -15.831 1.00 30.12 C ANISOU 2313 C VAL A1093 3961 3650 3835 564 548 687 C ATOM 2314 O VAL A1093 77.673 -1.132 -16.417 1.00 33.39 O ANISOU 2314 O VAL A1093 4304 4133 4248 498 800 567 O ATOM 2315 CB VAL A1093 75.714 -3.345 -15.828 1.00 28.83 C ANISOU 2315 CB VAL A1093 3751 3380 3822 941 304 768 C ATOM 2316 CG1 VAL A1093 76.267 -3.428 -14.417 1.00 28.07 C ANISOU 2316 CG1 VAL A1093 3290 3503 3872 987 238 794 C ATOM 2317 CG2 VAL A1093 74.469 -4.206 -15.969 1.00 25.32 C ANISOU 2317 CG2 VAL A1093 3459 2756 3405 1082 105 834 C ATOM 2318 N LYS A1094 76.398 -0.108 -14.870 1.00 32.38 N ANISOU 2318 N LYS A1094 4142 4014 4147 475 453 722 N ATOM 2319 CA LYS A1094 77.462 0.780 -14.416 1.00 33.29 C ANISOU 2319 CA LYS A1094 4043 4304 4302 292 625 620 C ATOM 2320 C LYS A1094 77.704 0.630 -12.920 1.00 33.36 C ANISOU 2320 C LYS A1094 3663 4544 4469 375 464 626 C ATOM 2321 O LYS A1094 76.762 0.636 -12.124 1.00 25.53 O ANISOU 2321 O LYS A1094 2689 3530 3483 451 240 736 O ATOM 2322 CB LYS A1094 77.130 2.234 -14.751 1.00 28.34 C ANISOU 2322 CB LYS A1094 3716 3530 3522 70 690 628 C ATOM 2323 CG LYS A1094 77.471 2.636 -16.175 1.00 36.68 C ANISOU 2323 CG LYS A1094 5147 4401 4387 -84 958 578 C ATOM 2324 CD LYS A1094 78.973 2.723 -16.384 1.00 51.89 C ANISOU 2324 CD LYS A1094 6839 6492 6385 -264 1315 400 C ATOM 2325 CE LYS A1094 79.303 3.168 -17.799 1.00 67.72 C ANISOU 2325 CE LYS A1094 9273 8294 8163 -462 1641 350 C ATOM 2326 NZ LYS A1094 78.837 2.175 -18.803 1.00 71.88 N ANISOU 2326 NZ LYS A1094 10061 8681 8569 -283 1601 398 N ATOM 2327 N VAL A1095 78.973 0.497 -12.547 1.00 45.23 N ANISOU 2327 N VAL A1095 4818 6272 6096 363 581 483 N ATOM 2328 CA VAL A1095 79.352 0.317 -11.150 1.00 40.78 C ANISOU 2328 CA VAL A1095 3899 5940 5655 475 403 465 C ATOM 2329 C VAL A1095 80.143 1.512 -10.630 1.00 42.22 C ANISOU 2329 C VAL A1095 3866 6293 5883 262 502 307 C ATOM 2330 O VAL A1095 81.143 1.912 -11.225 1.00 52.23 O ANISOU 2330 O VAL A1095 5020 7623 7201 94 763 118 O ATOM 2331 CB VAL A1095 80.187 -0.963 -10.953 1.00 41.00 C ANISOU 2331 CB VAL A1095 3650 6108 5820 717 360 394 C ATOM 2332 CG1 VAL A1095 80.659 -1.078 -9.510 1.00 31.34 C ANISOU 2332 CG1 VAL A1095 2103 5119 4685 855 146 363 C ATOM 2333 CG2 VAL A1095 79.379 -2.186 -11.356 1.00 46.93 C ANISOU 2333 CG2 VAL A1095 4617 6672 6543 923 256 547 C ATOM 2334 N ILE A1096 79.681 2.077 -9.520 1.00 34.54 N ANISOU 2334 N ILE A1096 2837 5391 4895 251 315 365 N ATOM 2335 CA ILE A1096 80.348 3.200 -8.876 1.00 41.26 C ANISOU 2335 CA ILE A1096 3474 6407 5798 60 368 207 C ATOM 2336 C ILE A1096 80.836 2.802 -7.486 1.00 48.83 C ANISOU 2336 C ILE A1096 4072 7635 6845 241 135 150 C ATOM 2337 O ILE A1096 80.037 2.611 -6.569 1.00 50.05 O ANISOU 2337 O ILE A1096 4296 7793 6928 367 -96 300 O ATOM 2338 CB ILE A1096 79.416 4.424 -8.752 1.00 36.98 C ANISOU 2338 CB ILE A1096 3200 5707 5142 -125 344 287 C ATOM 2339 CG1 ILE A1096 78.672 4.674 -10.067 1.00 31.92 C ANISOU 2339 CG1 ILE A1096 3005 4755 4366 -213 470 387 C ATOM 2340 CG2 ILE A1096 80.201 5.655 -8.318 1.00 34.30 C ANISOU 2340 CG2 ILE A1096 2675 5492 4863 -372 463 94 C ATOM 2341 CD1 ILE A1096 79.582 4.922 -11.249 1.00 50.54 C ANISOU 2341 CD1 ILE A1096 5447 7049 6707 -402 803 259 C ATOM 2342 N THR A1097 82.150 2.675 -7.334 1.00 47.91 N ANISOU 2342 N THR A1097 3580 7746 6879 258 194 -86 N ATOM 2343 CA THR A1097 82.733 2.327 -6.045 1.00 45.31 C ANISOU 2343 CA THR A1097 2925 7671 6621 462 -68 -175 C ATOM 2344 C THR A1097 83.245 3.567 -5.315 1.00 50.80 C ANISOU 2344 C THR A1097 3495 8449 7357 246 -61 -348 C ATOM 2345 O THR A1097 83.584 3.509 -4.133 1.00 55.35 O ANISOU 2345 O THR A1097 4022 9075 7933 362 -289 -371 O ATOM 2346 CB THR A1097 83.887 1.321 -6.206 1.00 43.60 C ANISOU 2346 CB THR A1097 2518 7491 6556 649 -82 -321 C ATOM 2347 OG1 THR A1097 84.810 1.808 -7.187 1.00 47.35 O ANISOU 2347 OG1 THR A1097 2799 8032 7160 431 242 -575 O ATOM 2348 CG2 THR A1097 83.358 -0.034 -6.647 1.00 37.04 C ANISOU 2348 CG2 THR A1097 1857 6531 5685 910 -157 -139 C ATOM 2349 N GLU A1098 83.294 4.688 -6.026 1.00 54.87 N ANISOU 2349 N GLU A1098 4004 8954 7890 -85 218 -466 N ATOM 2350 CA GLU A1098 83.800 5.934 -5.462 1.00 53.99 C ANISOU 2350 CA GLU A1098 3813 8877 7826 -316 262 -637 C ATOM 2351 C GLU A1098 82.763 6.577 -4.546 1.00 45.87 C ANISOU 2351 C GLU A1098 2948 7815 6664 -330 67 -492 C ATOM 2352 O GLU A1098 81.584 6.227 -4.588 1.00 54.55 O ANISOU 2352 O GLU A1098 4285 8812 7628 -229 -37 -253 O ATOM 2353 CB GLU A1098 84.199 6.895 -6.584 1.00 67.85 C ANISOU 2353 CB GLU A1098 5620 10532 9630 -696 669 -796 C ATOM 2354 CG GLU A1098 85.253 7.918 -6.194 1.00 90.28 C ANISOU 2354 CG GLU A1098 8310 13419 12574 -903 762 -1048 C ATOM 2355 CD GLU A1098 85.956 8.514 -7.399 1.00106.90 C ANISOU 2355 CD GLU A1098 10488 15399 14732 -1230 1190 -1220 C ATOM 2356 OE1 GLU A1098 86.028 7.834 -8.445 1.00106.35 O ANISOU 2356 OE1 GLU A1098 10493 15262 14653 -1223 1389 -1194 O ATOM 2357 OE2 GLU A1098 86.436 9.663 -7.301 1.00114.06 O ANISOU 2357 OE2 GLU A1098 11411 16253 15673 -1495 1338 -1383 O ATOM 2358 N MET A1099 83.207 7.513 -3.714 1.00 47.62 N ANISOU 2358 N MET A1099 3090 8084 6917 -445 17 -634 N ATOM 2359 CA MET A1099 82.318 8.187 -2.774 1.00 59.18 C ANISOU 2359 CA MET A1099 4701 9516 8268 -461 -151 -541 C ATOM 2360 C MET A1099 81.522 9.291 -3.466 1.00 59.83 C ANISOU 2360 C MET A1099 4968 9462 8303 -760 37 -517 C ATOM 2361 O MET A1099 82.077 10.078 -4.232 1.00 61.22 O ANISOU 2361 O MET A1099 5148 9558 8555 -1046 315 -668 O ATOM 2362 CB MET A1099 83.117 8.770 -1.607 1.00 71.71 C ANISOU 2362 CB MET A1099 6135 11215 9895 -464 -274 -717 C ATOM 2363 CG MET A1099 82.264 9.282 -0.458 1.00 82.74 C ANISOU 2363 CG MET A1099 7679 12595 11165 -429 -463 -633 C ATOM 2364 SD MET A1099 81.754 7.971 0.670 1.00 91.81 S ANISOU 2364 SD MET A1099 8949 13767 12168 -78 -759 -437 S ATOM 2365 CE MET A1099 83.316 7.577 1.453 1.00 87.30 C ANISOU 2365 CE MET A1099 8109 13388 11674 63 -899 -634 C ATOM 2366 N LEU A1100 80.223 9.346 -3.189 1.00 56.20 N ANISOU 2366 N LEU A1100 4760 8887 7706 -688 -106 -312 N ATOM 2367 CA LEU A1100 79.350 10.355 -3.783 1.00 47.52 C ANISOU 2367 CA LEU A1100 4028 7487 6539 -875 3 -236 C ATOM 2368 C LEU A1100 78.791 11.294 -2.720 1.00 55.48 C ANISOU 2368 C LEU A1100 5037 8529 7513 -932 -142 -286 C ATOM 2369 O LEU A1100 78.501 10.870 -1.600 1.00 60.45 O ANISOU 2369 O LEU A1100 5526 9346 8094 -759 -362 -260 O ATOM 2370 CB LEU A1100 78.202 9.690 -4.545 1.00 34.07 C ANISOU 2370 CB LEU A1100 2673 5541 4731 -723 -38 11 C ATOM 2371 CG LEU A1100 78.601 8.618 -5.562 1.00 37.74 C ANISOU 2371 CG LEU A1100 3166 5966 5209 -626 76 76 C ATOM 2372 CD1 LEU A1100 77.367 7.919 -6.114 1.00 26.41 C ANISOU 2372 CD1 LEU A1100 2039 4317 3680 -455 -22 294 C ATOM 2373 CD2 LEU A1100 79.436 9.222 -6.684 1.00 38.30 C ANISOU 2373 CD2 LEU A1100 3322 5918 5311 -878 391 -46 C ATOM 2374 N SER A1101 78.642 12.567 -3.073 1.00 56.96 N ANISOU 2374 N SER A1101 5417 8516 7709 -1175 -10 -361 N ATOM 2375 CA SER A1101 78.071 13.552 -2.160 1.00 47.49 C ANISOU 2375 CA SER A1101 4246 7310 6489 -1237 -133 -430 C ATOM 2376 C SER A1101 76.568 13.343 -2.019 1.00 54.33 C ANISOU 2376 C SER A1101 5365 8025 7254 -1057 -307 -246 C ATOM 2377 O SER A1101 75.946 12.690 -2.857 1.00 60.42 O ANISOU 2377 O SER A1101 6353 8623 7979 -938 -305 -78 O ATOM 2378 CB SER A1101 78.358 14.974 -2.647 1.00 41.80 C ANISOU 2378 CB SER A1101 3697 6368 5815 -1548 68 -567 C ATOM 2379 OG SER A1101 77.757 15.209 -3.909 1.00 40.52 O ANISOU 2379 OG SER A1101 3982 5838 5576 -1590 188 -418 O ATOM 2380 N ARG A1102 75.991 13.895 -0.956 1.00 54.51 N ANISOU 2380 N ARG A1102 5338 8118 7254 -1042 -453 -312 N ATOM 2381 CA ARG A1102 74.552 13.803 -0.737 1.00 39.74 C ANISOU 2381 CA ARG A1102 3654 6121 5323 -898 -593 -206 C ATOM 2382 C ARG A1102 73.780 14.459 -1.874 1.00 33.77 C ANISOU 2382 C ARG A1102 3271 4989 4572 -940 -550 -155 C ATOM 2383 O ARG A1102 72.709 13.994 -2.249 1.00 37.00 O ANISOU 2383 O ARG A1102 3844 5257 4957 -783 -644 -47 O ATOM 2384 CB ARG A1102 74.154 14.450 0.591 1.00 39.89 C ANISOU 2384 CB ARG A1102 3553 6281 5322 -913 -714 -337 C ATOM 2385 CG ARG A1102 74.354 13.570 1.810 1.00 50.02 C ANISOU 2385 CG ARG A1102 4695 7776 6535 -726 -794 -304 C ATOM 2386 CD ARG A1102 73.339 13.910 2.892 1.00 62.35 C ANISOU 2386 CD ARG A1102 6334 9316 8041 -662 -869 -341 C ATOM 2387 NE ARG A1102 73.329 15.335 3.213 1.00 71.51 N ANISOU 2387 NE ARG A1102 7498 10426 9246 -815 -868 -516 N ATOM 2388 CZ ARG A1102 72.472 15.906 4.055 1.00 69.41 C ANISOU 2388 CZ ARG A1102 7287 10133 8954 -796 -915 -591 C ATOM 2389 NH1 ARG A1102 71.547 15.173 4.663 1.00 64.26 N ANISOU 2389 NH1 ARG A1102 6673 9516 8227 -664 -944 -519 N ATOM 2390 NH2 ARG A1102 72.538 17.211 4.288 1.00 59.90 N ANISOU 2390 NH2 ARG A1102 6095 8866 7799 -929 -913 -758 N ATOM 2391 N GLU A1103 74.328 15.542 -2.413 1.00 34.60 N ANISOU 2391 N GLU A1103 3522 4919 4704 -1151 -413 -246 N ATOM 2392 CA GLU A1103 73.675 16.274 -3.492 1.00 42.85 C ANISOU 2392 CA GLU A1103 5001 5568 5713 -1182 -390 -195 C ATOM 2393 C GLU A1103 73.583 15.416 -4.750 1.00 44.07 C ANISOU 2393 C GLU A1103 5369 5574 5799 -1084 -334 -27 C ATOM 2394 O GLU A1103 72.540 15.371 -5.414 1.00 50.50 O ANISOU 2394 O GLU A1103 6478 6146 6564 -936 -460 57 O ATOM 2395 CB GLU A1103 74.423 17.578 -3.789 1.00 39.28 C ANISOU 2395 CB GLU A1103 4706 4937 5280 -1463 -208 -318 C ATOM 2396 CG GLU A1103 74.319 18.633 -2.688 1.00 42.80 C ANISOU 2396 CG GLU A1103 5030 5440 5792 -1559 -282 -502 C ATOM 2397 CD GLU A1103 75.144 18.295 -1.456 1.00 57.62 C ANISOU 2397 CD GLU A1103 6422 7741 7732 -1603 -293 -641 C ATOM 2398 OE1 GLU A1103 76.066 17.457 -1.565 1.00 57.70 O ANISOU 2398 OE1 GLU A1103 6198 7967 7758 -1613 -201 -627 O ATOM 2399 OE2 GLU A1103 74.868 18.866 -0.378 1.00 58.31 O ANISOU 2399 OE2 GLU A1103 6369 7942 7845 -1609 -410 -779 O ATOM 2400 N PHE A1104 74.673 14.724 -5.064 1.00 33.27 N ANISOU 2400 N PHE A1104 3837 4364 4441 -1154 -161 -10 N ATOM 2401 CA PHE A1104 74.701 13.841 -6.222 1.00 34.49 C ANISOU 2401 CA PHE A1104 4166 4409 4530 -1068 -86 127 C ATOM 2402 C PHE A1104 73.716 12.686 -6.059 1.00 32.46 C ANISOU 2402 C PHE A1104 3852 4215 4266 -791 -292 246 C ATOM 2403 O PHE A1104 72.965 12.369 -6.981 1.00 28.67 O ANISOU 2403 O PHE A1104 3655 3514 3724 -672 -354 343 O ATOM 2404 CB PHE A1104 76.109 13.297 -6.459 1.00 37.15 C ANISOU 2404 CB PHE A1104 4262 4939 4912 -1188 144 71 C ATOM 2405 CG PHE A1104 76.217 12.419 -7.671 1.00 53.17 C ANISOU 2405 CG PHE A1104 6473 6857 6872 -1117 253 187 C ATOM 2406 CD1 PHE A1104 76.155 12.963 -8.943 1.00 59.35 C ANISOU 2406 CD1 PHE A1104 7711 7310 7529 -1235 414 235 C ATOM 2407 CD2 PHE A1104 76.371 11.050 -7.541 1.00 58.66 C ANISOU 2407 CD2 PHE A1104 6925 7757 7605 -924 192 247 C ATOM 2408 CE1 PHE A1104 76.247 12.159 -10.060 1.00 60.66 C ANISOU 2408 CE1 PHE A1104 8065 7379 7605 -1168 515 327 C ATOM 2409 CE2 PHE A1104 76.466 10.240 -8.656 1.00 51.49 C ANISOU 2409 CE2 PHE A1104 6182 6745 6639 -857 293 332 C ATOM 2410 CZ PHE A1104 76.403 10.795 -9.915 1.00 52.76 C ANISOU 2410 CZ PHE A1104 6775 6601 6670 -981 456 365 C ATOM 2411 N VAL A1105 73.724 12.061 -4.885 1.00 24.15 N ANISOU 2411 N VAL A1105 2454 3452 3269 -697 -394 228 N ATOM 2412 CA VAL A1105 72.796 10.972 -4.594 1.00 28.84 C ANISOU 2412 CA VAL A1105 2997 4099 3863 -478 -546 329 C ATOM 2413 C VAL A1105 71.346 11.454 -4.681 1.00 27.81 C ANISOU 2413 C VAL A1105 3073 3756 3738 -396 -703 313 C ATOM 2414 O VAL A1105 70.471 10.740 -5.175 1.00 29.93 O ANISOU 2414 O VAL A1105 3445 3914 4013 -248 -791 377 O ATOM 2415 CB VAL A1105 73.061 10.364 -3.202 1.00 31.29 C ANISOU 2415 CB VAL A1105 2976 4727 4187 -413 -614 313 C ATOM 2416 CG1 VAL A1105 71.981 9.355 -2.842 1.00 32.18 C ANISOU 2416 CG1 VAL A1105 3092 4845 4290 -236 -727 409 C ATOM 2417 CG2 VAL A1105 74.438 9.715 -3.162 1.00 23.19 C ANISOU 2417 CG2 VAL A1105 1725 3911 3175 -419 -522 306 C ATOM 2418 N ARG A1106 71.106 12.676 -4.216 1.00 24.14 N ANISOU 2418 N ARG A1106 2651 3230 3290 -489 -746 195 N ATOM 2419 CA ARG A1106 69.784 13.283 -4.292 1.00 22.07 C ANISOU 2419 CA ARG A1106 2565 2760 3061 -397 -913 127 C ATOM 2420 C ARG A1106 69.364 13.448 -5.745 1.00 32.53 C ANISOU 2420 C ARG A1106 4276 3751 4334 -325 -960 182 C ATOM 2421 O ARG A1106 68.209 13.206 -6.098 1.00 29.47 O ANISOU 2421 O ARG A1106 3991 3225 3982 -151 -1135 158 O ATOM 2422 CB ARG A1106 69.762 14.635 -3.575 1.00 25.18 C ANISOU 2422 CB ARG A1106 2952 3131 3484 -512 -939 -24 C ATOM 2423 CG ARG A1106 68.409 15.331 -3.617 1.00 32.36 C ANISOU 2423 CG ARG A1106 4020 3822 4452 -390 -1132 -137 C ATOM 2424 CD ARG A1106 68.365 16.536 -2.701 1.00 35.74 C ANISOU 2424 CD ARG A1106 4385 4268 4925 -488 -1159 -307 C ATOM 2425 NE ARG A1106 69.298 17.580 -3.116 1.00 42.36 N ANISOU 2425 NE ARG A1106 5428 4947 5719 -677 -1044 -319 N ATOM 2426 CZ ARG A1106 69.443 18.743 -2.490 1.00 41.59 C ANISOU 2426 CZ ARG A1106 5330 4811 5660 -799 -1041 -469 C ATOM 2427 NH1 ARG A1106 68.713 19.016 -1.419 1.00 45.34 N ANISOU 2427 NH1 ARG A1106 5608 5412 6207 -734 -1157 -622 N ATOM 2428 NH2 ARG A1106 70.316 19.634 -2.937 1.00 38.52 N ANISOU 2428 NH2 ARG A1106 5148 4249 5238 -1004 -898 -482 N ATOM 2429 N GLU A1107 70.308 13.857 -6.587 1.00 27.67 N ANISOU 2429 N GLU A1107 3878 3006 3628 -463 -800 235 N ATOM 2430 CA GLU A1107 70.041 13.945 -8.019 1.00 27.16 C ANISOU 2430 CA GLU A1107 4247 2620 3451 -401 -822 309 C ATOM 2431 C GLU A1107 69.737 12.566 -8.604 1.00 30.67 C ANISOU 2431 C GLU A1107 4656 3112 3886 -237 -861 403 C ATOM 2432 O GLU A1107 68.885 12.429 -9.484 1.00 25.03 O ANISOU 2432 O GLU A1107 4217 2170 3121 -74 -1022 417 O ATOM 2433 CB GLU A1107 71.223 14.579 -8.753 1.00 39.86 C ANISOU 2433 CB GLU A1107 6103 4097 4946 -633 -562 344 C ATOM 2434 CG GLU A1107 71.427 16.051 -8.448 1.00 64.30 C ANISOU 2434 CG GLU A1107 9359 7034 8038 -808 -518 249 C ATOM 2435 CD GLU A1107 72.618 16.636 -9.179 1.00 88.10 C ANISOU 2435 CD GLU A1107 12620 9904 10950 -1089 -199 265 C ATOM 2436 OE1 GLU A1107 73.336 15.869 -9.857 1.00 96.73 O ANISOU 2436 OE1 GLU A1107 13704 11063 11985 -1146 -3 333 O ATOM 2437 OE2 GLU A1107 72.836 17.862 -9.077 1.00 97.57 O ANISOU 2437 OE2 GLU A1107 14024 10913 12134 -1267 -122 194 O ATOM 2438 N LEU A1108 70.437 11.547 -8.112 1.00 28.31 N ANISOU 2438 N LEU A1108 2216 4437 4104 -236 -541 -65 N ATOM 2439 CA LEU A1108 70.223 10.178 -8.572 1.00 21.03 C ANISOU 2439 CA LEU A1108 1606 3488 2895 -174 -502 29 C ATOM 2440 C LEU A1108 68.805 9.726 -8.275 1.00 21.73 C ANISOU 2440 C LEU A1108 1827 3385 3046 -295 -527 7 C ATOM 2441 O LEU A1108 68.088 9.291 -9.172 1.00 28.04 O ANISOU 2441 O LEU A1108 2825 4000 3830 -393 -571 102 O ATOM 2442 CB LEU A1108 71.223 9.225 -7.923 1.00 20.06 C ANISOU 2442 CB LEU A1108 1609 3542 2469 77 -385 4 C ATOM 2443 CG LEU A1108 72.637 9.285 -8.495 1.00 32.86 C ANISOU 2443 CG LEU A1108 3194 5318 3971 217 -342 48 C ATOM 2444 CD1 LEU A1108 73.588 8.419 -7.687 1.00 39.05 C ANISOU 2444 CD1 LEU A1108 4061 6273 4502 472 -248 1 C ATOM 2445 CD2 LEU A1108 72.622 8.854 -9.947 1.00 22.10 C ANISOU 2445 CD2 LEU A1108 2055 3833 2510 162 -344 194 C ATOM 2446 N TYR A1109 68.410 9.839 -7.010 1.00 21.86 N ANISOU 2446 N TYR A1109 1728 3446 3132 -294 -495 -130 N ATOM 2447 CA TYR A1109 67.059 9.489 -6.583 1.00 17.94 C ANISOU 2447 CA TYR A1109 1321 2773 2723 -419 -498 -183 C ATOM 2448 C TYR A1109 65.984 10.205 -7.398 1.00 27.18 C ANISOU 2448 C TYR A1109 2435 3726 4164 -639 -603 -156 C ATOM 2449 O TYR A1109 64.917 9.651 -7.653 1.00 21.83 O ANISOU 2449 O TYR A1109 1922 2854 3518 -735 -623 -139 O ATOM 2450 CB TYR A1109 66.868 9.819 -5.107 1.00 18.02 C ANISOU 2450 CB TYR A1109 1151 2886 2812 -416 -446 -356 C ATOM 2451 CG TYR A1109 67.568 8.885 -4.151 1.00 29.63 C ANISOU 2451 CG TYR A1109 2774 4525 3959 -203 -326 -382 C ATOM 2452 CD1 TYR A1109 67.864 7.577 -4.512 1.00 18.81 C ANISOU 2452 CD1 TYR A1109 1739 3130 2279 -58 -261 -266 C ATOM 2453 CD2 TYR A1109 67.923 9.312 -2.876 1.00 27.84 C ANISOU 2453 CD2 TYR A1109 2358 4480 3742 -150 -286 -526 C ATOM 2454 CE1 TYR A1109 68.498 6.722 -3.630 1.00 32.04 C ANISOU 2454 CE1 TYR A1109 3556 4946 3672 141 -167 -280 C ATOM 2455 CE2 TYR A1109 68.557 8.465 -1.989 1.00 25.77 C ANISOU 2455 CE2 TYR A1109 2245 4370 3178 45 -197 -539 C ATOM 2456 CZ TYR A1109 68.842 7.173 -2.369 1.00 28.14 C ANISOU 2456 CZ TYR A1109 2878 4631 3183 193 -143 -410 C ATOM 2457 OH TYR A1109 69.473 6.332 -1.483 1.00 36.89 O ANISOU 2457 OH TYR A1109 4136 5878 4004 391 -70 -413 O ATOM 2458 N GLY A1110 66.271 11.440 -7.798 1.00 25.41 N ANISOU 2458 N GLY A1110 2158 3560 3934 -630 -550 -151 N ATOM 2459 CA GLY A1110 65.319 12.239 -8.546 1.00 21.48 C ANISOU 2459 CA GLY A1110 1757 2915 3488 -700 -534 -136 C ATOM 2460 C GLY A1110 65.339 11.997 -10.044 1.00 29.88 C ANISOU 2460 C GLY A1110 2919 3836 4596 -727 -627 -12 C ATOM 2461 O GLY A1110 64.542 12.577 -10.778 1.00 31.78 O ANISOU 2461 O GLY A1110 3230 3959 4887 -757 -638 17 O ATOM 2462 N SER A1111 66.242 11.133 -10.501 1.00 35.20 N ANISOU 2462 N SER A1111 3613 4551 5211 -724 -722 109 N ATOM 2463 CA SER A1111 66.392 10.874 -11.930 1.00 28.22 C ANISOU 2463 CA SER A1111 2865 3579 4279 -799 -832 291 C ATOM 2464 C SER A1111 66.041 9.436 -12.309 1.00 32.28 C ANISOU 2464 C SER A1111 3670 4005 4591 -825 -862 383 C ATOM 2465 O SER A1111 65.377 9.200 -13.320 1.00 33.27 O ANISOU 2465 O SER A1111 3963 3959 4719 -941 -952 477 O ATOM 2466 CB SER A1111 67.820 11.190 -12.377 1.00 18.59 C ANISOU 2466 CB SER A1111 1531 2543 2987 -759 -849 376 C ATOM 2467 OG SER A1111 68.112 12.564 -12.199 1.00 62.29 O ANISOU 2467 OG SER A1111 6923 8109 8634 -694 -749 255 O ATOM 2468 N VAL A1112 66.494 8.481 -11.504 1.00 26.39 N ANISOU 2468 N VAL A1112 3050 3370 3606 -643 -716 328 N ATOM 2469 CA VAL A1112 66.247 7.071 -11.782 1.00 27.10 C ANISOU 2469 CA VAL A1112 3486 3381 3432 -566 -640 378 C ATOM 2470 C VAL A1112 64.764 6.730 -11.687 1.00 25.41 C ANISOU 2470 C VAL A1112 3366 2938 3350 -710 -693 342 C ATOM 2471 O VAL A1112 63.978 7.481 -11.112 1.00 30.95 O ANISOU 2471 O VAL A1112 3858 3567 4333 -840 -760 250 O ATOM 2472 CB VAL A1112 67.027 6.155 -10.820 1.00 21.37 C ANISOU 2472 CB VAL A1112 2860 2813 2448 -336 -481 327 C ATOM 2473 CG1 VAL A1112 68.523 6.338 -11.012 1.00 19.03 C ANISOU 2473 CG1 VAL A1112 2492 2728 2009 -178 -426 358 C ATOM 2474 CG2 VAL A1112 66.622 6.434 -9.381 1.00 18.39 C ANISOU 2474 CG2 VAL A1112 2316 2480 2193 -334 -450 188 C ATOM 2475 N ASP A1113 64.391 5.589 -12.254 1.00 25.07 N ANISOU 2475 N ASP A1113 3630 2777 3117 -689 -657 402 N ATOM 2476 CA ASP A1113 63.007 5.139 -12.227 1.00 18.55 C ANISOU 2476 CA ASP A1113 2916 1727 2405 -817 -696 363 C ATOM 2477 C ASP A1113 62.720 4.365 -10.950 1.00 25.12 C ANISOU 2477 C ASP A1113 3819 2570 3157 -727 -554 260 C ATOM 2478 O ASP A1113 61.772 4.669 -10.226 1.00 38.60 O ANISOU 2478 O ASP A1113 5408 4179 5078 -840 -569 152 O ATOM 2479 CB ASP A1113 62.705 4.281 -13.454 1.00 31.33 C ANISOU 2479 CB ASP A1113 4830 3209 3866 -847 -725 467 C ATOM 2480 CG ASP A1113 62.813 5.063 -14.748 1.00 42.41 C ANISOU 2480 CG ASP A1113 6187 4578 5350 -972 -880 574 C ATOM 2481 OD1 ASP A1113 62.267 6.183 -14.811 1.00 52.50 O ANISOU 2481 OD1 ASP A1113 7197 5866 6886 -1036 -973 529 O ATOM 2482 OD2 ASP A1113 63.451 4.566 -15.698 1.00 48.40 O ANISOU 2482 OD2 ASP A1113 7137 5378 5875 -916 -854 673 O ATOM 2483 N PHE A1114 63.552 3.367 -10.675 1.00 21.65 N ANISOU 2483 N PHE A1114 3571 2246 2410 -525 -416 292 N ATOM 2484 CA PHE A1114 63.380 2.539 -9.491 1.00 18.93 C ANISOU 2484 CA PHE A1114 3332 1916 1944 -424 -278 221 C ATOM 2485 C PHE A1114 64.661 2.446 -8.680 1.00 24.11 C ANISOU 2485 C PHE A1114 3938 2815 2408 -211 -184 212 C ATOM 2486 O PHE A1114 65.763 2.563 -9.218 1.00 25.21 O ANISOU 2486 O PHE A1114 4059 3090 2429 -99 -190 278 O ATOM 2487 CB PHE A1114 62.921 1.133 -9.876 1.00 19.35 C ANISOU 2487 CB PHE A1114 3728 1816 1810 -384 -201 270 C ATOM 2488 CG PHE A1114 61.641 1.103 -10.650 1.00 19.30 C ANISOU 2488 CG PHE A1114 3787 1565 1980 -583 -294 268 C ATOM 2489 CD1 PHE A1114 61.653 1.172 -12.032 1.00 32.05 C ANISOU 2489 CD1 PHE A1114 5480 3109 3587 -650 -400 360 C ATOM 2490 CD2 PHE A1114 60.427 0.995 -9.998 1.00 25.97 C ANISOU 2490 CD2 PHE A1114 4620 2249 2998 -707 -276 166 C ATOM 2491 CE1 PHE A1114 60.473 1.142 -12.750 1.00 36.07 C ANISOU 2491 CE1 PHE A1114 6010 3439 4257 -804 -497 343 C ATOM 2492 CE2 PHE A1114 59.244 0.964 -10.707 1.00 33.58 C ANISOU 2492 CE2 PHE A1114 5544 3074 4142 -826 -351 141 C ATOM 2493 CZ PHE A1114 59.266 1.037 -12.085 1.00 30.41 C ANISOU 2493 CZ PHE A1114 5148 2684 3721 -833 -452 220 C ATOM 2494 N VAL A1115 64.503 2.232 -7.379 1.00 24.70 N ANISOU 2494 N VAL A1115 3992 2942 2452 -160 -99 125 N ATOM 2495 CA VAL A1115 65.632 1.969 -6.500 1.00 28.24 C ANISOU 2495 CA VAL A1115 4431 3607 2690 54 -16 116 C ATOM 2496 C VAL A1115 65.467 0.585 -5.871 1.00 30.74 C ANISOU 2496 C VAL A1115 5043 3870 2767 176 111 137 C ATOM 2497 O VAL A1115 64.448 0.289 -5.245 1.00 28.26 O ANISOU 2497 O VAL A1115 4799 3430 2509 76 162 78 O ATOM 2498 CB VAL A1115 65.766 3.046 -5.405 1.00 29.14 C ANISOU 2498 CB VAL A1115 4240 3873 2959 20 -36 -7 C ATOM 2499 CG1 VAL A1115 64.411 3.347 -4.778 1.00 35.65 C ANISOU 2499 CG1 VAL A1115 4995 4552 3998 -178 -32 -118 C ATOM 2500 CG2 VAL A1115 66.782 2.617 -4.353 1.00 25.55 C ANISOU 2500 CG2 VAL A1115 3814 3627 2266 241 46 -24 C ATOM 2501 N ILE A1116 66.465 -0.269 -6.063 1.00 36.40 N ANISOU 2501 N ILE A1116 5933 4670 3227 386 168 221 N ATOM 2502 CA ILE A1116 66.400 -1.636 -5.563 1.00 31.89 C ANISOU 2502 CA ILE A1116 5621 4034 2464 507 276 256 C ATOM 2503 C ILE A1116 67.029 -1.744 -4.178 1.00 28.01 C ANISOU 2503 C ILE A1116 5034 3706 1903 635 315 211 C ATOM 2504 O ILE A1116 68.194 -1.391 -3.990 1.00 28.40 O ANISOU 2504 O ILE A1116 4931 3939 1922 760 280 208 O ATOM 2505 CB ILE A1116 67.099 -2.612 -6.526 1.00 36.75 C ANISOU 2505 CB ILE A1116 6281 4605 3076 597 279 320 C ATOM 2506 CG1 ILE A1116 66.473 -2.508 -7.918 1.00 32.46 C ANISOU 2506 CG1 ILE A1116 5819 3912 2600 461 233 357 C ATOM 2507 CG2 ILE A1116 67.012 -4.036 -5.999 1.00 35.92 C ANISOU 2507 CG2 ILE A1116 6309 4402 2936 681 355 325 C ATOM 2508 CD1 ILE A1116 67.131 -3.384 -8.955 1.00 34.00 C ANISOU 2508 CD1 ILE A1116 6056 4082 2781 533 248 391 C ATOM 2509 N ILE A1117 66.246 -2.221 -3.213 1.00 24.41 N ANISOU 2509 N ILE A1117 4675 3173 1427 589 384 173 N ATOM 2510 CA ILE A1117 66.715 -2.389 -1.840 1.00 27.35 C ANISOU 2510 CA ILE A1117 4986 3681 1724 680 413 140 C ATOM 2511 C ILE A1117 66.536 -3.837 -1.388 1.00 39.73 C ANISOU 2511 C ILE A1117 6727 5121 3249 733 473 194 C ATOM 2512 O ILE A1117 65.610 -4.151 -0.641 1.00 40.94 O ANISOU 2512 O ILE A1117 6980 5186 3389 651 542 163 O ATOM 2513 CB ILE A1117 65.966 -1.459 -0.869 1.00 28.93 C ANISOU 2513 CB ILE A1117 5121 3945 1926 564 451 17 C ATOM 2514 CG1 ILE A1117 65.755 -0.084 -1.503 1.00 35.54 C ANISOU 2514 CG1 ILE A1117 5680 4804 3020 411 356 -59 C ATOM 2515 CG2 ILE A1117 66.723 -1.335 0.442 1.00 24.45 C ANISOU 2515 CG2 ILE A1117 4432 3582 1277 663 449 -23 C ATOM 2516 CD1 ILE A1117 64.863 0.823 -0.695 1.00 38.35 C ANISOU 2516 CD1 ILE A1117 5824 5151 3596 209 359 -210 C ATOM 2517 N PRO A1118 67.435 -4.725 -1.835 1.00 41.14 N ANISOU 2517 N PRO A1118 6947 5282 3401 874 456 263 N ATOM 2518 CA PRO A1118 67.303 -6.168 -1.631 1.00 39.67 C ANISOU 2518 CA PRO A1118 6943 4953 3178 943 510 311 C ATOM 2519 C PRO A1118 67.927 -6.657 -0.328 1.00 38.87 C ANISOU 2519 C PRO A1118 6857 4940 2970 1062 520 327 C ATOM 2520 O PRO A1118 68.529 -7.731 -0.305 1.00 39.68 O ANISOU 2520 O PRO A1118 7063 4990 3024 1200 532 378 O ATOM 2521 CB PRO A1118 68.045 -6.749 -2.838 1.00 43.51 C ANISOU 2521 CB PRO A1118 7456 5390 3686 1037 490 354 C ATOM 2522 CG PRO A1118 69.027 -5.658 -3.266 1.00 33.38 C ANISOU 2522 CG PRO A1118 5981 4286 2417 1073 420 340 C ATOM 2523 CD PRO A1118 68.702 -4.394 -2.504 1.00 36.02 C ANISOU 2523 CD PRO A1118 6177 4754 2755 987 394 283 C ATOM 2524 N SER A1119 67.773 -5.880 0.739 1.00 36.69 N ANISOU 2524 N SER A1119 6490 4796 2653 1008 517 276 N ATOM 2525 CA SER A1119 68.377 -6.206 2.026 1.00 40.52 C ANISOU 2525 CA SER A1119 6986 5386 3023 1107 513 287 C ATOM 2526 C SER A1119 67.872 -7.528 2.596 1.00 45.55 C ANISOU 2526 C SER A1119 7838 5874 3595 1128 582 341 C ATOM 2527 O SER A1119 66.709 -7.883 2.419 1.00 48.42 O ANISOU 2527 O SER A1119 8318 6076 4005 1010 653 333 O ATOM 2528 CB SER A1119 68.107 -5.086 3.035 1.00 38.92 C ANISOU 2528 CB SER A1119 6651 5347 2788 1008 510 199 C ATOM 2529 OG SER A1119 68.566 -3.838 2.551 1.00 50.47 O ANISOU 2529 OG SER A1119 7914 6948 4314 999 450 138 O ATOM 2530 N TYR A1120 68.756 -8.255 3.275 1.00 45.77 N ANISOU 2530 N TYR A1120 7927 5946 3518 1287 564 393 N ATOM 2531 CA TYR A1120 68.345 -9.395 4.087 1.00 42.62 C ANISOU 2531 CA TYR A1120 7727 5437 3029 1311 627 443 C ATOM 2532 C TYR A1120 67.825 -8.872 5.416 1.00 45.95 C ANISOU 2532 C TYR A1120 8127 5966 3366 1200 652 401 C ATOM 2533 O TYR A1120 66.924 -9.450 6.024 1.00 48.35 O ANISOU 2533 O TYR A1120 8576 6166 3628 1120 734 412 O ATOM 2534 CB TYR A1120 69.504 -10.364 4.331 1.00 36.48 C ANISOU 2534 CB TYR A1120 7037 4666 2157 1531 595 514 C ATOM 2535 CG TYR A1120 69.982 -11.134 3.121 1.00 45.76 C ANISOU 2535 CG TYR A1120 8274 5719 3394 1649 599 547 C ATOM 2536 CD1 TYR A1120 70.739 -10.517 2.133 1.00 53.04 C ANISOU 2536 CD1 TYR A1120 9049 6715 4388 1701 545 521 C ATOM 2537 CD2 TYR A1120 69.704 -12.487 2.983 1.00 42.01 C ANISOU 2537 CD2 TYR A1120 8009 5059 2893 1711 664 595 C ATOM 2538 CE1 TYR A1120 71.191 -11.223 1.035 1.00 60.51 C ANISOU 2538 CE1 TYR A1120 10057 7562 5374 1802 560 541 C ATOM 2539 CE2 TYR A1120 70.152 -13.201 1.888 1.00 48.58 C ANISOU 2539 CE2 TYR A1120 8901 5789 3770 1817 678 608 C ATOM 2540 CZ TYR A1120 70.895 -12.564 0.917 1.00 55.09 C ANISOU 2540 CZ TYR A1120 9577 6696 4659 1859 627 581 C ATOM 2541 OH TYR A1120 71.343 -13.271 -0.175 1.00 62.37 O ANISOU 2541 OH TYR A1120 10564 7523 5610 1958 651 587 O ATOM 2542 N PHE A1121 68.417 -7.766 5.854 1.00 49.44 N ANISOU 2542 N PHE A1121 8386 6617 3782 1198 589 344 N ATOM 2543 CA PHE A1121 68.096 -7.152 7.135 1.00 55.24 C ANISOU 2543 CA PHE A1121 9073 7493 4424 1097 608 280 C ATOM 2544 C PHE A1121 68.125 -5.629 7.013 1.00 50.43 C ANISOU 2544 C PHE A1121 8234 7045 3883 1003 574 163 C ATOM 2545 O PHE A1121 69.111 -5.051 6.548 1.00 49.07 O ANISOU 2545 O PHE A1121 7921 6975 3749 1108 490 153 O ATOM 2546 CB PHE A1121 69.076 -7.631 8.208 1.00 57.18 C ANISOU 2546 CB PHE A1121 9373 7845 4506 1243 558 333 C ATOM 2547 CG PHE A1121 68.890 -6.971 9.543 1.00 67.19 C ANISOU 2547 CG PHE A1121 10589 9283 5658 1143 569 261 C ATOM 2548 CD1 PHE A1121 67.830 -7.321 10.364 1.00 71.92 C ANISOU 2548 CD1 PHE A1121 11308 9836 6182 1000 669 249 C ATOM 2549 CD2 PHE A1121 69.785 -6.010 9.985 1.00 72.95 C ANISOU 2549 CD2 PHE A1121 11149 10216 6352 1196 485 196 C ATOM 2550 CE1 PHE A1121 67.660 -6.717 11.598 1.00 63.23 C ANISOU 2550 CE1 PHE A1121 10157 8904 4961 895 691 168 C ATOM 2551 CE2 PHE A1121 69.621 -5.404 11.219 1.00 73.46 C ANISOU 2551 CE2 PHE A1121 11171 10437 6305 1096 499 114 C ATOM 2552 CZ PHE A1121 68.556 -5.757 12.025 1.00 59.47 C ANISOU 2552 CZ PHE A1121 9520 8632 4446 935 605 97 C ATOM 2553 N GLU A1122 67.039 -4.984 7.426 1.00 65.31 N ANISOU 2553 N GLU A1122 10076 5896 8841 -1281 -1482 858 N ATOM 2554 CA GLU A1122 66.909 -3.537 7.294 1.00 48.23 C ANISOU 2554 CA GLU A1122 7647 3974 6706 -1103 -1232 696 C ATOM 2555 C GLU A1122 65.938 -2.978 8.329 1.00 50.07 C ANISOU 2555 C GLU A1122 7890 4456 6678 -1349 -938 673 C ATOM 2556 O GLU A1122 64.752 -2.818 8.045 1.00 50.62 O ANISOU 2556 O GLU A1122 7739 4765 6728 -1428 -697 580 O ATOM 2557 CB GLU A1122 66.439 -3.172 5.883 1.00 50.70 C ANISOU 2557 CB GLU A1122 7609 4397 7259 -862 -1121 552 C ATOM 2558 CG GLU A1122 66.366 -1.677 5.600 1.00 65.41 C ANISOU 2558 CG GLU A1122 9262 6436 9154 -625 -898 395 C ATOM 2559 CD GLU A1122 67.645 -1.130 4.997 1.00 83.00 C ANISOU 2559 CD GLU A1122 11464 8529 11541 -350 -1042 360 C ATOM 2560 OE1 GLU A1122 68.703 -1.779 5.146 1.00 81.59 O ANISOU 2560 OE1 GLU A1122 11431 8176 11393 -347 -1312 440 O ATOM 2561 OE2 GLU A1122 67.590 -0.051 4.367 1.00 94.30 O ANISOU 2561 OE2 GLU A1122 12737 10042 13050 -137 -887 244 O ATOM 2562 N PRO A1123 66.442 -2.670 9.533 1.00 51.29 N ANISOU 2562 N PRO A1123 8278 4596 6614 -1453 -963 731 N ATOM 2563 CA PRO A1123 65.592 -2.167 10.618 1.00 55.18 C ANISOU 2563 CA PRO A1123 8800 5346 6821 -1685 -696 700 C ATOM 2564 C PRO A1123 65.090 -0.753 10.341 1.00 59.13 C ANISOU 2564 C PRO A1123 9018 6094 7354 -1463 -423 474 C ATOM 2565 O PRO A1123 64.022 -0.372 10.819 1.00 67.07 O ANISOU 2565 O PRO A1123 9914 7396 8175 -1585 -158 380 O ATOM 2566 CB PRO A1123 66.524 -2.193 11.831 1.00 54.76 C ANISOU 2566 CB PRO A1123 9081 5171 6553 -1773 -860 810 C ATOM 2567 CG PRO A1123 67.885 -2.013 11.253 1.00 56.54 C ANISOU 2567 CG PRO A1123 9306 5181 6996 -1468 -1125 784 C ATOM 2568 CD PRO A1123 67.865 -2.705 9.915 1.00 53.08 C ANISOU 2568 CD PRO A1123 8716 4612 6840 -1327 -1244 793 C ATOM 2569 N PHE A1124 65.856 0.010 9.570 1.00 49.62 N ANISOU 2569 N PHE A1124 7713 4774 6365 -1136 -491 382 N ATOM 2570 CA PHE A1124 65.472 1.370 9.214 1.00 52.47 C ANISOU 2570 CA PHE A1124 7890 5282 6762 -890 -269 183 C ATOM 2571 C PHE A1124 65.677 1.628 7.726 1.00 56.39 C ANISOU 2571 C PHE A1124 8188 5688 7549 -585 -309 120 C ATOM 2572 O PHE A1124 66.801 1.846 7.272 1.00 60.68 O ANISOU 2572 O PHE A1124 8780 6034 8240 -444 -470 141 O ATOM 2573 CB PHE A1124 66.267 2.381 10.038 1.00 59.58 C ANISOU 2573 CB PHE A1124 8964 6123 7550 -844 -269 122 C ATOM 2574 CG PHE A1124 66.252 2.101 11.509 1.00 85.92 C ANISOU 2574 CG PHE A1124 12522 9538 10587 -1123 -270 193 C ATOM 2575 CD1 PHE A1124 65.099 2.297 12.250 1.00103.73 C ANISOU 2575 CD1 PHE A1124 14736 12082 12595 -1269 -22 121 C ATOM 2576 CD2 PHE A1124 67.387 1.636 12.153 1.00 85.83 C ANISOU 2576 CD2 PHE A1124 12750 9347 10514 -1225 -522 317 C ATOM 2577 CE1 PHE A1124 65.079 2.035 13.604 1.00107.17 C ANISOU 2577 CE1 PHE A1124 15385 12612 12722 -1540 -10 193 C ATOM 2578 CE2 PHE A1124 67.372 1.374 13.507 1.00 87.92 C ANISOU 2578 CE2 PHE A1124 13247 9686 10472 -1467 -533 393 C ATOM 2579 CZ PHE A1124 66.218 1.575 14.233 1.00 99.05 C ANISOU 2579 CZ PHE A1124 14633 11370 11631 -1638 -268 341 C ATOM 2580 N GLY A1125 64.585 1.603 6.970 1.00 56.06 N ANISOU 2580 N GLY A1125 7906 5830 7564 -490 -159 32 N ATOM 2581 CA GLY A1125 64.649 1.830 5.538 1.00 58.50 C ANISOU 2581 CA GLY A1125 8028 6087 8113 -190 -186 -28 C ATOM 2582 C GLY A1125 64.794 3.299 5.195 1.00 43.47 C ANISOU 2582 C GLY A1125 6123 4166 6229 111 -58 -162 C ATOM 2583 O GLY A1125 63.939 3.876 4.523 1.00 43.62 O ANISOU 2583 O GLY A1125 5976 4334 6263 353 93 -293 O ATOM 2584 N LEU A1126 65.880 3.906 5.661 1.00 47.86 N ANISOU 2584 N LEU A1126 6883 4533 6769 98 -128 -138 N ATOM 2585 CA LEU A1126 66.124 5.322 5.424 1.00 45.70 C ANISOU 2585 CA LEU A1126 6693 4174 6496 320 -15 -253 C ATOM 2586 C LEU A1126 66.392 5.582 3.946 1.00 43.55 C ANISOU 2586 C LEU A1126 6318 3799 6429 580 -45 -255 C ATOM 2587 O LEU A1126 65.978 6.608 3.409 1.00 43.65 O ANISOU 2587 O LEU A1126 6353 3799 6433 835 94 -356 O ATOM 2588 CB LEU A1126 67.294 5.820 6.275 1.00 49.01 C ANISOU 2588 CB LEU A1126 7347 4425 6849 175 -97 -236 C ATOM 2589 CG LEU A1126 67.143 5.625 7.786 1.00 62.06 C ANISOU 2589 CG LEU A1126 9135 6177 8267 -71 -82 -231 C ATOM 2590 CD1 LEU A1126 68.280 6.299 8.538 1.00 60.80 C ANISOU 2590 CD1 LEU A1126 9191 5872 8038 -171 -159 -262 C ATOM 2591 CD2 LEU A1126 65.792 6.138 8.271 1.00 68.03 C ANISOU 2591 CD2 LEU A1126 9844 7167 8837 -6 159 -367 C ATOM 2592 N VAL A1127 67.083 4.647 3.299 1.00 43.16 N ANISOU 2592 N VAL A1127 6181 3675 6542 533 -235 -147 N ATOM 2593 CA VAL A1127 67.338 4.727 1.864 1.00 45.89 C ANISOU 2593 CA VAL A1127 6402 3967 7065 761 -271 -145 C ATOM 2594 C VAL A1127 66.017 4.796 1.109 1.00 44.06 C ANISOU 2594 C VAL A1127 5991 3911 6840 992 -137 -227 C ATOM 2595 O VAL A1127 65.840 5.614 0.200 1.00 44.88 O ANISOU 2595 O VAL A1127 6087 3990 6976 1268 -50 -283 O ATOM 2596 CB VAL A1127 68.156 3.517 1.365 1.00 44.44 C ANISOU 2596 CB VAL A1127 6121 3731 7033 689 -512 -47 C ATOM 2597 CG1 VAL A1127 68.211 3.498 -0.153 1.00 35.88 C ANISOU 2597 CG1 VAL A1127 4869 2656 6107 936 -531 -61 C ATOM 2598 CG2 VAL A1127 69.557 3.543 1.956 1.00 47.25 C ANISOU 2598 CG2 VAL A1127 6611 3964 7378 535 -665 -4 C ATOM 2599 N ALA A1128 65.089 3.935 1.514 1.00 25.65 N ANISOU 2599 N ALA A1128 3322 3543 2881 491 384 191 N ATOM 2600 CA ALA A1128 63.748 3.908 0.949 1.00 23.72 C ANISOU 2600 CA ALA A1128 2985 3299 2729 355 472 146 C ATOM 2601 C ALA A1128 63.069 5.263 1.085 1.00 35.42 C ANISOU 2601 C ALA A1128 4277 4882 4299 382 412 -29 C ATOM 2602 O ALA A1128 62.515 5.774 0.122 1.00 41.49 O ANISOU 2602 O ALA A1128 4936 5609 5219 349 358 -99 O ATOM 2603 CB ALA A1128 62.910 2.824 1.619 1.00 25.34 C ANISOU 2603 CB ALA A1128 3291 3534 2803 239 663 214 C ATOM 2604 N LEU A1129 63.122 5.845 2.281 1.00 30.75 N ANISOU 2604 N LEU A1129 3662 4420 3603 466 406 -109 N ATOM 2605 CA LEU A1129 62.467 7.124 2.545 1.00 25.79 C ANISOU 2605 CA LEU A1129 2863 3891 3044 517 339 -297 C ATOM 2606 C LEU A1129 63.066 8.257 1.717 1.00 27.47 C ANISOU 2606 C LEU A1129 3003 4000 3436 585 149 -360 C ATOM 2607 O LEU A1129 62.340 9.061 1.125 1.00 44.23 O ANISOU 2607 O LEU A1129 5013 6105 5687 584 84 -471 O ATOM 2608 CB LEU A1129 62.547 7.462 4.034 1.00 26.48 C ANISOU 2608 CB LEU A1129 2961 4139 2961 616 360 -372 C ATOM 2609 CG LEU A1129 61.633 6.626 4.932 1.00 44.20 C ANISOU 2609 CG LEU A1129 5255 6519 5020 537 579 -342 C ATOM 2610 CD1 LEU A1129 61.914 6.893 6.403 1.00 55.36 C ANISOU 2610 CD1 LEU A1129 6726 8090 6218 666 593 -393 C ATOM 2611 CD2 LEU A1129 60.175 6.906 4.605 1.00 40.00 C ANISOU 2611 CD2 LEU A1129 4538 6074 4585 437 664 -475 C ATOM 2612 N GLU A1130 64.393 8.311 1.679 1.00 29.69 N ANISOU 2612 N GLU A1130 3352 4208 3720 644 62 -293 N ATOM 2613 CA GLU A1130 65.110 9.314 0.902 1.00 31.72 C ANISOU 2613 CA GLU A1130 3556 4351 4144 674 -87 -328 C ATOM 2614 C GLU A1130 64.758 9.223 -0.576 1.00 33.77 C ANISOU 2614 C GLU A1130 3817 4485 4529 596 -88 -265 C ATOM 2615 O GLU A1130 64.512 10.237 -1.233 1.00 31.53 O ANISOU 2615 O GLU A1130 3478 4126 4375 609 -184 -334 O ATOM 2616 CB GLU A1130 66.618 9.152 1.093 1.00 22.18 C ANISOU 2616 CB GLU A1130 2401 3109 2918 726 -146 -268 C ATOM 2617 CG GLU A1130 67.088 9.445 2.508 1.00 35.26 C ANISOU 2617 CG GLU A1130 4051 4884 4461 840 -198 -364 C ATOM 2618 CD GLU A1130 68.513 8.999 2.752 1.00 44.83 C ANISOU 2618 CD GLU A1130 5314 6089 5628 907 -253 -317 C ATOM 2619 OE1 GLU A1130 68.974 8.070 2.057 1.00 48.23 O ANISOU 2619 OE1 GLU A1130 5819 6456 6050 870 -203 -184 O ATOM 2620 OE2 GLU A1130 69.172 9.581 3.639 1.00 62.51 O ANISOU 2620 OE2 GLU A1130 7511 8395 7845 1012 -360 -434 O ATOM 2621 N ALA A1131 64.728 7.999 -1.092 1.00 26.74 N ANISOU 2621 N ALA A1131 3009 3562 3590 530 10 -138 N ATOM 2622 CA ALA A1131 64.418 7.777 -2.496 1.00 25.40 C ANISOU 2622 CA ALA A1131 2853 3285 3513 474 6 -84 C ATOM 2623 C ALA A1131 62.959 8.110 -2.819 1.00 28.82 C ANISOU 2623 C ALA A1131 3197 3748 4004 448 6 -197 C ATOM 2624 O ALA A1131 62.665 8.711 -3.852 1.00 31.59 O ANISOU 2624 O ALA A1131 3529 4016 4457 466 -79 -227 O ATOM 2625 CB ALA A1131 64.730 6.345 -2.874 1.00 26.35 C ANISOU 2625 CB ALA A1131 3083 3364 3564 423 96 53 C ATOM 2626 N MET A1132 62.052 7.720 -1.929 1.00 23.20 N ANISOU 2626 N MET A1132 2435 3163 3219 412 104 -264 N ATOM 2627 CA MET A1132 60.624 7.941 -2.130 1.00 26.77 C ANISOU 2627 CA MET A1132 2761 3682 3727 385 118 -405 C ATOM 2628 C MET A1132 60.276 9.422 -2.060 1.00 35.88 C ANISOU 2628 C MET A1132 3813 4857 4962 496 -25 -570 C ATOM 2629 O MET A1132 59.377 9.887 -2.756 1.00 41.28 O ANISOU 2629 O MET A1132 4417 5530 5737 526 -99 -684 O ATOM 2630 CB MET A1132 59.809 7.159 -1.100 1.00 23.76 C ANISOU 2630 CB MET A1132 2338 3449 3240 298 293 -438 C ATOM 2631 CG MET A1132 59.800 5.658 -1.336 1.00 33.70 C ANISOU 2631 CG MET A1132 3703 4652 4450 166 432 -295 C ATOM 2632 SD MET A1132 59.178 4.718 0.071 1.00 34.45 S ANISOU 2632 SD MET A1132 3825 4885 4380 47 669 -270 S ATOM 2633 CE MET A1132 57.417 5.020 -0.056 1.00 31.83 C ANISOU 2633 CE MET A1132 3241 4700 4153 -43 739 -493 C ATOM 2634 N CYS A1133 60.997 10.162 -1.223 1.00 26.50 N ANISOU 2634 N CYS A1133 2635 3691 3743 571 -83 -596 N ATOM 2635 CA CYS A1133 60.792 11.603 -1.120 1.00 33.88 C ANISOU 2635 CA CYS A1133 3501 4610 4764 683 -238 -753 C ATOM 2636 C CYS A1133 61.149 12.312 -2.423 1.00 30.26 C ANISOU 2636 C CYS A1133 3108 3955 4437 711 -378 -710 C ATOM 2637 O CYS A1133 60.723 13.441 -2.665 1.00 42.30 O ANISOU 2637 O CYS A1133 4603 5420 6046 801 -519 -833 O ATOM 2638 CB CYS A1133 61.617 12.185 0.030 1.00 23.81 C ANISOU 2638 CB CYS A1133 2232 3380 3435 752 -282 -794 C ATOM 2639 SG CYS A1133 60.938 11.879 1.676 1.00 46.73 S ANISOU 2639 SG CYS A1133 5055 6537 6162 784 -159 -912 S ATOM 2640 N LEU A1134 61.930 11.640 -3.261 1.00 32.43 N ANISOU 2640 N LEU A1134 3486 4124 4713 643 -337 -534 N ATOM 2641 CA LEU A1134 62.395 12.225 -4.509 1.00 40.48 C ANISOU 2641 CA LEU A1134 4594 4963 5823 656 -434 -460 C ATOM 2642 C LEU A1134 61.770 11.547 -5.723 1.00 39.01 C ANISOU 2642 C LEU A1134 4447 4736 5640 634 -413 -410 C ATOM 2643 O LEU A1134 62.204 11.756 -6.855 1.00 45.51 O ANISOU 2643 O LEU A1134 5373 5424 6496 641 -461 -315 O ATOM 2644 CB LEU A1134 63.919 12.158 -4.576 1.00 36.42 C ANISOU 2644 CB LEU A1134 4155 4371 5312 611 -411 -320 C ATOM 2645 CG LEU A1134 64.571 13.096 -3.559 1.00 42.64 C ANISOU 2645 CG LEU A1134 4899 5165 6136 648 -482 -403 C ATOM 2646 CD1 LEU A1134 66.019 12.732 -3.324 1.00 48.03 C ANISOU 2646 CD1 LEU A1134 5603 5841 6805 603 -440 -305 C ATOM 2647 CD2 LEU A1134 64.450 14.538 -4.027 1.00 43.53 C ANISOU 2647 CD2 LEU A1134 5040 5126 6375 693 -627 -473 C ATOM 2648 N GLY A1135 60.747 10.736 -5.481 1.00 21.29 N ANISOU 2648 N GLY A1135 2118 2613 3358 602 -338 -483 N ATOM 2649 CA GLY A1135 59.954 10.175 -6.558 1.00 41.06 C ANISOU 2649 CA GLY A1135 4623 5093 5885 594 -348 -497 C ATOM 2650 C GLY A1135 60.407 8.820 -7.067 1.00 39.04 C ANISOU 2650 C GLY A1135 4445 4809 5580 501 -240 -351 C ATOM 2651 O GLY A1135 59.725 8.207 -7.888 1.00 37.66 O ANISOU 2651 O GLY A1135 4262 4623 5424 486 -245 -380 O ATOM 2652 N ALA A1136 61.556 8.351 -6.593 1.00 28.97 N ANISOU 2652 N ALA A1136 3242 3521 4246 456 -161 -214 N ATOM 2653 CA ALA A1136 62.041 7.032 -6.983 1.00 26.06 C ANISOU 2653 CA ALA A1136 2958 3121 3823 391 -71 -86 C ATOM 2654 C ALA A1136 61.170 5.945 -6.362 1.00 27.44 C ANISOU 2654 C ALA A1136 3085 3378 3961 297 46 -126 C ATOM 2655 O ALA A1136 60.827 6.011 -5.182 1.00 40.64 O ANISOU 2655 O ALA A1136 4695 5155 5592 268 115 -181 O ATOM 2656 CB ALA A1136 63.493 6.850 -6.575 1.00 29.47 C ANISOU 2656 CB ALA A1136 3468 3531 4200 395 -36 40 C ATOM 2657 N ILE A1137 60.810 4.949 -7.166 1.00 20.20 N ANISOU 2657 N ILE A1137 2206 2411 3059 244 75 -102 N ATOM 2658 CA ILE A1137 59.959 3.859 -6.706 1.00 26.55 C ANISOU 2658 CA ILE A1137 2974 3259 3853 119 196 -136 C ATOM 2659 C ILE A1137 60.803 2.691 -6.203 1.00 33.48 C ANISOU 2659 C ILE A1137 4002 4085 4635 62 302 23 C ATOM 2660 O ILE A1137 61.673 2.196 -6.915 1.00 20.39 O ANISOU 2660 O ILE A1137 2461 2329 2958 103 265 125 O ATOM 2661 CB ILE A1137 59.020 3.377 -7.825 1.00 22.95 C ANISOU 2661 CB ILE A1137 2468 2765 3485 87 153 -229 C ATOM 2662 CG1 ILE A1137 58.083 4.509 -8.256 1.00 25.39 C ANISOU 2662 CG1 ILE A1137 2633 3134 3878 174 29 -411 C ATOM 2663 CG2 ILE A1137 58.229 2.163 -7.371 1.00 23.97 C ANISOU 2663 CG2 ILE A1137 2564 2914 3629 -81 296 -258 C ATOM 2664 CD1 ILE A1137 57.344 4.233 -9.548 1.00 28.27 C ANISOU 2664 CD1 ILE A1137 2968 3456 4318 205 -73 -514 C ATOM 2665 N PRO A1138 60.554 2.254 -4.961 1.00 28.24 N ANISOU 2665 N PRO A1138 3346 3489 3895 -18 431 39 N ATOM 2666 CA PRO A1138 61.369 1.207 -4.337 1.00 22.32 C ANISOU 2666 CA PRO A1138 2776 2680 3027 -43 515 194 C ATOM 2667 C PRO A1138 60.960 -0.215 -4.711 1.00 28.64 C ANISOU 2667 C PRO A1138 3674 3368 3838 -167 599 248 C ATOM 2668 O PRO A1138 59.777 -0.551 -4.690 1.00 37.93 O ANISOU 2668 O PRO A1138 4762 4569 5081 -307 684 162 O ATOM 2669 CB PRO A1138 61.146 1.448 -2.844 1.00 23.36 C ANISOU 2669 CB PRO A1138 2892 2934 3051 -65 618 183 C ATOM 2670 CG PRO A1138 59.772 2.013 -2.770 1.00 24.24 C ANISOU 2670 CG PRO A1138 2804 3160 3245 -139 658 15 C ATOM 2671 CD PRO A1138 59.586 2.839 -4.017 1.00 24.58 C ANISOU 2671 CD PRO A1138 2738 3173 3430 -60 497 -88 C ATOM 2672 N ILE A1139 61.946 -1.033 -5.064 1.00 29.21 N ANISOU 2672 N ILE A1139 3921 3318 3859 -115 568 372 N ATOM 2673 CA ILE A1139 61.761 -2.474 -5.175 1.00 32.10 C ANISOU 2673 CA ILE A1139 4440 3547 4212 -218 642 445 C ATOM 2674 C ILE A1139 62.560 -3.109 -4.049 1.00 35.90 C ANISOU 2674 C ILE A1139 5125 3989 4525 -184 708 591 C ATOM 2675 O ILE A1139 63.764 -3.328 -4.182 1.00 52.90 O ANISOU 2675 O ILE A1139 7399 6091 6610 -39 621 668 O ATOM 2676 CB ILE A1139 62.230 -3.029 -6.537 1.00 30.47 C ANISOU 2676 CB ILE A1139 4296 3215 4064 -153 533 456 C ATOM 2677 CG1 ILE A1139 61.576 -2.263 -7.688 1.00 30.94 C ANISOU 2677 CG1 ILE A1139 4181 3322 4253 -134 439 316 C ATOM 2678 CG2 ILE A1139 61.923 -4.516 -6.646 1.00 24.78 C ANISOU 2678 CG2 ILE A1139 3734 2329 3352 -268 597 506 C ATOM 2679 CD1 ILE A1139 62.057 -2.701 -9.054 1.00 25.24 C ANISOU 2679 CD1 ILE A1139 3526 2504 3561 -45 331 320 C ATOM 2680 N ALA A1140 61.897 -3.388 -2.932 1.00 28.93 N ANISOU 2680 N ALA A1140 4282 3143 3566 -305 860 618 N ATOM 2681 CA ALA A1140 62.613 -3.764 -1.718 1.00 30.43 C ANISOU 2681 CA ALA A1140 4675 3327 3560 -239 912 749 C ATOM 2682 C ALA A1140 62.153 -5.085 -1.119 1.00 33.29 C ANISOU 2682 C ALA A1140 5263 3550 3836 -393 1073 871 C ATOM 2683 O ALA A1140 61.048 -5.556 -1.384 1.00 30.97 O ANISOU 2683 O ALA A1140 4913 3209 3646 -603 1191 831 O ATOM 2684 CB ALA A1140 62.483 -2.659 -0.683 1.00 29.23 C ANISOU 2684 CB ALA A1140 4405 3371 3330 -191 943 689 C ATOM 2685 N SER A1141 63.019 -5.673 -0.299 1.00 43.34 N ANISOU 2685 N SER A1141 6798 4753 4918 -285 1073 1014 N ATOM 2686 CA SER A1141 62.696 -6.901 0.413 1.00 43.76 C ANISOU 2686 CA SER A1141 7132 4648 4847 -412 1227 1164 C ATOM 2687 C SER A1141 61.615 -6.660 1.452 1.00 44.94 C ANISOU 2687 C SER A1141 7230 4923 4923 -594 1452 1162 C ATOM 2688 O SER A1141 61.501 -5.564 2.003 1.00 45.00 O ANISOU 2688 O SER A1141 7060 5151 4888 -528 1455 1073 O ATOM 2689 CB SER A1141 63.939 -7.473 1.088 1.00 33.92 C ANISOU 2689 CB SER A1141 6195 3308 3384 -200 1142 1308 C ATOM 2690 OG SER A1141 64.899 -7.874 0.130 1.00 45.90 O ANISOU 2690 OG SER A1141 7751 4721 4966 -32 948 1295 O ATOM 2691 N ALA A1142 60.824 -7.691 1.721 1.00 37.64 N ANISOU 2691 N ALA A1142 6459 3857 3985 -829 1647 1255 N ATOM 2692 CA ALA A1142 59.777 -7.597 2.726 1.00 41.03 C ANISOU 2692 CA ALA A1142 6850 4408 4331 -1032 1905 1264 C ATOM 2693 C ALA A1142 60.336 -7.889 4.113 1.00 46.66 C ANISOU 2693 C ALA A1142 7848 5136 4745 -915 1957 1426 C ATOM 2694 O ALA A1142 59.845 -8.772 4.814 1.00 45.67 O ANISOU 2694 O ALA A1142 7858 4946 4548 -1051 2078 1519 O ATOM 2695 CB ALA A1142 58.638 -8.547 2.399 1.00 42.31 C ANISOU 2695 CB ALA A1142 6998 4435 4642 -1352 2080 1262 C ATOM 2696 N VAL A1143 61.372 -7.150 4.499 1.00 49.21 N ANISOU 2696 N VAL A1143 8217 5562 4919 -636 1812 1429 N ATOM 2697 CA VAL A1143 61.941 -7.268 5.836 1.00 49.55 C ANISOU 2697 CA VAL A1143 8476 5666 4686 -475 1801 1527 C ATOM 2698 C VAL A1143 61.501 -6.083 6.690 1.00 56.69 C ANISOU 2698 C VAL A1143 9223 6855 5463 -450 1923 1439 C ATOM 2699 O VAL A1143 61.356 -4.968 6.185 1.00 53.41 O ANISOU 2699 O VAL A1143 8470 6607 5218 -405 1820 1246 O ATOM 2700 CB VAL A1143 63.481 -7.352 5.800 1.00 45.25 C ANISOU 2700 CB VAL A1143 8095 5050 4047 -152 1533 1561 C ATOM 2701 CG1 VAL A1143 63.922 -8.634 5.116 1.00 41.80 C ANISOU 2701 CG1 VAL A1143 7825 4352 3706 -155 1419 1629 C ATOM 2702 CG2 VAL A1143 64.072 -6.144 5.096 1.00 47.15 C ANISOU 2702 CG2 VAL A1143 8080 5427 4409 13 1361 1411 C ATOM 2703 N GLY A1144 61.279 -6.340 7.978 1.00 67.20 N ANISOU 2703 N GLY A1144 10687 8269 6577 -453 2028 1510 N ATOM 2704 CA GLY A1144 60.755 -5.346 8.901 1.00 64.98 C ANISOU 2704 CA GLY A1144 10265 8271 6154 -435 2158 1418 C ATOM 2705 C GLY A1144 61.499 -4.026 8.878 1.00 60.45 C ANISOU 2705 C GLY A1144 9523 7873 5574 -165 1957 1261 C ATOM 2706 O GLY A1144 62.670 -3.957 9.242 1.00 72.61 O ANISOU 2706 O GLY A1144 11227 9391 6972 101 1764 1297 O ATOM 2707 N GLY A1145 60.806 -2.975 8.457 1.00 43.70 N ANISOU 2707 N GLY A1145 7021 5929 3653 -228 1947 1049 N ATOM 2708 CA GLY A1145 61.425 -1.683 8.231 1.00 43.86 C ANISOU 2708 CA GLY A1145 6807 6083 3776 -9 1699 863 C ATOM 2709 C GLY A1145 61.046 -1.214 6.841 1.00 52.87 C ANISOU 2709 C GLY A1145 7654 7183 5253 -104 1602 727 C ATOM 2710 O GLY A1145 60.323 -0.231 6.681 1.00 57.40 O ANISOU 2710 O GLY A1145 7939 7916 5954 -135 1600 541 O ATOM 2711 N LEU A1146 61.537 -1.927 5.832 1.00 43.90 N ANISOU 2711 N LEU A1146 6605 5831 4245 -130 1511 813 N ATOM 2712 CA LEU A1146 61.059 -1.742 4.469 1.00 45.84 C ANISOU 2712 CA LEU A1146 6627 6015 4776 -242 1451 713 C ATOM 2713 C LEU A1146 59.621 -2.233 4.397 1.00 48.49 C ANISOU 2713 C LEU A1146 6871 6369 5185 -519 1684 686 C ATOM 2714 O LEU A1146 58.783 -1.670 3.691 1.00 53.46 O ANISOU 2714 O LEU A1146 7222 7074 6016 -606 1673 519 O ATOM 2715 CB LEU A1146 61.934 -2.500 3.471 1.00 47.72 C ANISOU 2715 CB LEU A1146 7005 6029 5098 -194 1314 812 C ATOM 2716 CG LEU A1146 63.430 -2.191 3.484 1.00 46.56 C ANISOU 2716 CG LEU A1146 6941 5861 4890 63 1098 835 C ATOM 2717 CD1 LEU A1146 64.174 -3.137 2.554 1.00 41.70 C ANISOU 2717 CD1 LEU A1146 6473 5036 4334 97 1003 931 C ATOM 2718 CD2 LEU A1146 63.679 -0.744 3.094 1.00 47.79 C ANISOU 2718 CD2 LEU A1146 6823 6149 5185 170 942 662 C ATOM 2719 N ARG A1147 59.354 -3.297 5.146 1.00 48.46 N ANISOU 2719 N ARG A1147 7111 6290 5011 -654 1894 849 N ATOM 2720 CA ARG A1147 58.027 -3.886 5.243 1.00 51.47 C ANISOU 2720 CA ARG A1147 7427 6684 5446 -954 2160 840 C ATOM 2721 C ARG A1147 57.044 -2.887 5.849 1.00 59.60 C ANISOU 2721 C ARG A1147 8167 8010 6469 -998 2281 651 C ATOM 2722 O ARG A1147 55.856 -2.891 5.525 1.00 67.51 O ANISOU 2722 O ARG A1147 8931 9092 7629 -1211 2421 518 O ATOM 2723 CB ARG A1147 58.090 -5.167 6.081 1.00 47.51 C ANISOU 2723 CB ARG A1147 7302 6028 4721 -1077 2370 1084 C ATOM 2724 CG ARG A1147 56.826 -6.004 6.091 1.00 60.27 C ANISOU 2724 CG ARG A1147 8862 7600 6436 -1409 2610 1093 C ATOM 2725 CD ARG A1147 57.003 -7.212 6.999 1.00 78.74 C ANISOU 2725 CD ARG A1147 11531 9792 8593 -1441 2673 1315 C ATOM 2726 NE ARG A1147 55.806 -8.046 7.056 1.00 99.10 N ANISOU 2726 NE ARG A1147 14040 12325 11290 -1743 2869 1322 N ATOM 2727 CZ ARG A1147 55.591 -9.097 6.271 1.00110.08 C ANISOU 2727 CZ ARG A1147 15498 13466 12861 -1903 2848 1362 C ATOM 2728 NH1 ARG A1147 56.494 -9.444 5.363 1.00109.76 N ANISOU 2728 NH1 ARG A1147 15597 13211 12897 -1777 2638 1401 N ATOM 2729 NH2 ARG A1147 54.473 -9.800 6.393 1.00112.97 N ANISOU 2729 NH2 ARG A1147 15787 13804 13333 -2181 3036 1353 N ATOM 2730 N ASP A1148 57.555 -2.025 6.724 1.00 58.38 N ANISOU 2730 N ASP A1148 8021 8025 6137 -781 2212 615 N ATOM 2731 CA ASP A1148 56.741 -1.011 7.388 1.00 65.58 C ANISOU 2731 CA ASP A1148 8676 9227 7013 -769 2299 421 C ATOM 2732 C ASP A1148 56.410 0.157 6.462 1.00 60.13 C ANISOU 2732 C ASP A1148 7632 8629 6587 -689 2098 169 C ATOM 2733 O ASP A1148 55.254 0.563 6.342 1.00 64.06 O ANISOU 2733 O ASP A1148 7850 9288 7202 -804 2195 -20 O ATOM 2734 CB ASP A1148 57.457 -0.488 8.637 1.00 77.13 C ANISOU 2734 CB ASP A1148 10288 10828 8191 -538 2262 454 C ATOM 2735 CG ASP A1148 57.656 -1.561 9.691 1.00 96.68 C ANISOU 2735 CG ASP A1148 13135 13242 10356 -594 2475 696 C ATOM 2736 OD1 ASP A1148 56.730 -2.374 9.898 1.00103.16 O ANISOU 2736 OD1 ASP A1148 14003 14049 11145 -866 2766 776 O ATOM 2737 OD2 ASP A1148 58.739 -1.592 10.313 1.00103.18 O ANISOU 2737 OD2 ASP A1148 14210 14027 10966 -365 2349 802 O ATOM 2738 N ILE A1149 57.436 0.694 5.812 1.00 46.64 N ANISOU 2738 N ILE A1149 5942 6817 4964 -488 1820 163 N ATOM 2739 CA ILE A1149 57.289 1.874 4.969 1.00 44.87 C ANISOU 2739 CA ILE A1149 5447 6644 4956 -382 1610 -44 C ATOM 2740 C ILE A1149 56.504 1.592 3.691 1.00 46.24 C ANISOU 2740 C ILE A1149 5457 6733 5378 -533 1598 -123 C ATOM 2741 O ILE A1149 55.583 2.331 3.338 1.00 42.73 O ANISOU 2741 O ILE A1149 4742 6418 5077 -543 1568 -338 O ATOM 2742 CB ILE A1149 58.665 2.447 4.581 1.00 47.13 C ANISOU 2742 CB ILE A1149 5820 6820 5266 -160 1344 -5 C ATOM 2743 CG1 ILE A1149 59.477 2.774 5.834 1.00 50.03 C ANISOU 2743 CG1 ILE A1149 6328 7280 5403 13 1318 35 C ATOM 2744 CG2 ILE A1149 58.507 3.679 3.701 1.00 48.48 C ANISOU 2744 CG2 ILE A1149 5755 7014 5651 -65 1141 -193 C ATOM 2745 CD1 ILE A1149 60.920 3.116 5.549 1.00 46.54 C ANISOU 2745 CD1 ILE A1149 5979 6724 4978 203 1083 82 C ATOM 2746 N ILE A1150 56.873 0.513 3.009 1.00 41.68 N ANISOU 2746 N ILE A1150 5049 5940 4847 -628 1605 34 N ATOM 2747 CA ILE A1150 56.369 0.234 1.668 1.00 37.10 C ANISOU 2747 CA ILE A1150 4348 5252 4498 -725 1537 -39 C ATOM 2748 C ILE A1150 55.105 -0.624 1.653 1.00 49.52 C ANISOU 2748 C ILE A1150 5825 6844 6147 -999 1761 -89 C ATOM 2749 O ILE A1150 55.038 -1.668 2.304 1.00 50.32 O ANISOU 2749 O ILE A1150 6111 6877 6130 -1164 1970 66 O ATOM 2750 CB ILE A1150 57.453 -0.462 0.821 1.00 37.29 C ANISOU 2750 CB ILE A1150 4588 5033 4548 -667 1404 126 C ATOM 2751 CG1 ILE A1150 58.693 0.426 0.716 1.00 29.43 C ANISOU 2751 CG1 ILE A1150 3640 4028 3515 -421 1190 148 C ATOM 2752 CG2 ILE A1150 56.924 -0.805 -0.565 1.00 36.15 C ANISOU 2752 CG2 ILE A1150 4336 4780 4619 -753 1331 45 C ATOM 2753 CD1 ILE A1150 59.881 -0.271 0.114 1.00 40.63 C ANISOU 2753 CD1 ILE A1150 5270 5252 4916 -347 1086 308 C ATOM 2754 N THR A1151 54.106 -0.166 0.905 1.00 58.28 N ANISOU 2754 N THR A1151 6645 8041 7457 -1046 1712 -315 N ATOM 2755 CA THR A1151 52.898 -0.942 0.655 1.00 61.86 C ANISOU 2755 CA THR A1151 6949 8509 8044 -1310 1886 -413 C ATOM 2756 C THR A1151 52.809 -1.266 -0.834 1.00 69.20 C ANISOU 2756 C THR A1151 7828 9277 9188 -1315 1709 -480 C ATOM 2757 O THR A1151 53.666 -0.851 -1.614 1.00 64.89 O ANISOU 2757 O THR A1151 7369 8625 8661 -1114 1477 -437 O ATOM 2758 CB THR A1151 51.632 -0.192 1.102 1.00 60.34 C ANISOU 2758 CB THR A1151 6414 8603 7909 -1362 1988 -678 C ATOM 2759 OG1 THR A1151 51.432 0.955 0.267 1.00 57.14 O ANISOU 2759 OG1 THR A1151 5792 8271 7648 -1156 1727 -897 O ATOM 2760 CG2 THR A1151 51.765 0.256 2.553 1.00 59.28 C ANISOU 2760 CG2 THR A1151 6327 8654 7541 -1313 2141 -632 C ATOM 2761 N ASN A1152 51.774 -2.000 -1.232 1.00 80.41 N ANISOU 2761 N ASN A1152 9103 10684 10766 -1547 1823 -594 N ATOM 2762 CA ASN A1152 51.631 -2.412 -2.626 1.00 78.59 C ANISOU 2762 CA ASN A1152 8830 10301 10729 -1552 1654 -676 C ATOM 2763 C ASN A1152 51.263 -1.249 -3.545 1.00 77.43 C ANISOU 2763 C ASN A1152 8441 10268 10709 -1341 1402 -917 C ATOM 2764 O ASN A1152 51.279 -1.389 -4.769 1.00 78.88 O ANISOU 2764 O ASN A1152 8615 10339 11017 -1272 1216 -984 O ATOM 2765 CB ASN A1152 50.587 -3.524 -2.750 1.00 76.72 C ANISOU 2765 CB ASN A1152 8490 10018 10645 -1871 1841 -760 C ATOM 2766 CG ASN A1152 49.181 -3.038 -2.468 1.00 86.61 C ANISOU 2766 CG ASN A1152 9352 11536 12019 -1994 1955 -1052 C ATOM 2767 OD1 ASN A1152 48.791 -2.864 -1.313 1.00 92.74 O ANISOU 2767 OD1 ASN A1152 10062 12489 12688 -2099 2185 -1049 O ATOM 2768 ND2 ASN A1152 48.407 -2.822 -3.526 1.00 90.13 N ANISOU 2768 ND2 ASN A1152 9536 12028 12683 -1967 1790 -1322 N ATOM 2769 N GLU A1153 50.932 -0.104 -2.952 1.00 72.28 N ANISOU 2769 N GLU A1153 7615 9835 10013 -1222 1387 -1050 N ATOM 2770 CA GLU A1153 50.632 1.101 -3.719 1.00 64.30 C ANISOU 2770 CA GLU A1153 6420 8915 9098 -990 1134 -1265 C ATOM 2771 C GLU A1153 51.845 2.022 -3.806 1.00 55.16 C ANISOU 2771 C GLU A1153 5450 7683 7824 -731 947 -1126 C ATOM 2772 O GLU A1153 51.864 2.958 -4.605 1.00 63.67 O ANISOU 2772 O GLU A1153 6471 8755 8964 -529 716 -1236 O ATOM 2773 CB GLU A1153 49.454 1.862 -3.104 1.00 72.00 C ANISOU 2773 CB GLU A1153 7069 10169 10119 -996 1200 -1541 C ATOM 2774 CG GLU A1153 48.107 1.166 -3.233 1.00 89.39 C ANISOU 2774 CG GLU A1153 8993 12482 12489 -1236 1347 -1763 C ATOM 2775 CD GLU A1153 47.809 0.235 -2.072 1.00 99.52 C ANISOU 2775 CD GLU A1153 10296 13822 13693 -1542 1710 -1655 C ATOM 2776 OE1 GLU A1153 48.691 0.059 -1.205 1.00103.32 O ANISOU 2776 OE1 GLU A1153 11044 14242 13972 -1544 1828 -1393 O ATOM 2777 OE2 GLU A1153 46.688 -0.316 -2.026 1.00 97.51 O ANISOU 2777 OE2 GLU A1153 9890 13627 13531 -1721 1814 -1790 O ATOM 2778 N THR A1154 52.853 1.759 -2.980 1.00 41.52 N ANISOU 2778 N THR A1154 3952 5894 5930 -739 1046 -890 N ATOM 2779 CA THR A1154 54.027 2.623 -2.918 1.00 48.40 C ANISOU 2779 CA THR A1154 4973 6712 6704 -521 892 -776 C ATOM 2780 C THR A1154 55.337 1.858 -3.096 1.00 54.26 C ANISOU 2780 C THR A1154 6003 7255 7357 -513 884 -515 C ATOM 2781 O THR A1154 56.330 2.150 -2.429 1.00 55.23 O ANISOU 2781 O THR A1154 6267 7368 7349 -418 875 -384 O ATOM 2782 CB THR A1154 54.085 3.387 -1.583 1.00 56.13 C ANISOU 2782 CB THR A1154 5912 7862 7553 -460 968 -803 C ATOM 2783 OG1 THR A1154 54.121 2.452 -0.497 1.00 63.14 O ANISOU 2783 OG1 THR A1154 6910 8781 8299 -625 1216 -667 O ATOM 2784 CG2 THR A1154 52.870 4.291 -1.431 1.00 59.04 C ANISOU 2784 CG2 THR A1154 5985 8441 8005 -417 943 -1088 C ATOM 2785 N GLY A1155 55.336 0.881 -3.997 1.00 50.80 N ANISOU 2785 N GLY A1155 5641 6668 6994 -598 873 -463 N ATOM 2786 CA GLY A1155 56.540 0.133 -4.304 1.00 30.74 C ANISOU 2786 CA GLY A1155 3357 3943 4380 -564 843 -248 C ATOM 2787 C GLY A1155 56.281 -1.333 -4.586 1.00 34.93 C ANISOU 2787 C GLY A1155 3992 4332 4949 -745 949 -181 C ATOM 2788 O GLY A1155 55.132 -1.766 -4.676 1.00 44.13 O ANISOU 2788 O GLY A1155 5011 5533 6225 -917 1042 -312 O ATOM 2789 N ILE A1156 57.359 -2.097 -4.729 1.00 37.00 N ANISOU 2789 N ILE A1156 4500 4430 5130 -704 927 6 N ATOM 2790 CA ILE A1156 57.267 -3.527 -4.996 1.00 35.20 C ANISOU 2790 CA ILE A1156 4422 4023 4930 -853 1003 85 C ATOM 2791 C ILE A1156 58.054 -4.315 -3.953 1.00 43.41 C ANISOU 2791 C ILE A1156 5731 4969 5793 -878 1123 300 C ATOM 2792 O ILE A1156 59.242 -4.066 -3.744 1.00 49.83 O ANISOU 2792 O ILE A1156 6683 5766 6485 -699 1037 414 O ATOM 2793 CB ILE A1156 57.794 -3.876 -6.403 1.00 37.71 C ANISOU 2793 CB ILE A1156 4808 4199 5321 -745 826 83 C ATOM 2794 CG1 ILE A1156 57.010 -3.112 -7.471 1.00 36.53 C ANISOU 2794 CG1 ILE A1156 4428 4133 5316 -691 690 -127 C ATOM 2795 CG2 ILE A1156 57.710 -5.372 -6.650 1.00 40.92 C ANISOU 2795 CG2 ILE A1156 5382 4403 5763 -887 886 148 C ATOM 2796 CD1 ILE A1156 57.884 -2.341 -8.431 1.00 40.24 C ANISOU 2796 CD1 ILE A1156 4933 4596 5760 -459 498 -109 C ATOM 2797 N LEU A1157 57.390 -5.263 -3.300 1.00 42.53 N ANISOU 2797 N LEU A1157 5698 4793 5667 -1101 1320 351 N ATOM 2798 CA LEU A1157 58.031 -6.058 -2.258 1.00 45.08 C ANISOU 2798 CA LEU A1157 6320 5010 5800 -1124 1440 565 C ATOM 2799 C LEU A1157 58.414 -7.447 -2.755 1.00 47.75 C ANISOU 2799 C LEU A1157 6916 5071 6156 -1180 1421 684 C ATOM 2800 O LEU A1157 57.737 -8.021 -3.607 1.00 48.20 O ANISOU 2800 O LEU A1157 6901 5023 6388 -1320 1414 590 O ATOM 2801 CB LEU A1157 57.118 -6.170 -1.035 1.00 41.92 C ANISOU 2801 CB LEU A1157 5893 4713 5322 -1331 1700 580 C ATOM 2802 CG LEU A1157 57.002 -4.899 -0.193 1.00 37.15 C ANISOU 2802 CG LEU A1157 5120 4377 4621 -1228 1725 502 C ATOM 2803 CD1 LEU A1157 55.979 -5.078 0.914 1.00 42.53 C ANISOU 2803 CD1 LEU A1157 5751 5181 5226 -1449 2007 494 C ATOM 2804 CD2 LEU A1157 58.359 -4.520 0.384 1.00 41.39 C ANISOU 2804 CD2 LEU A1157 5848 4919 4959 -975 1610 634 C ATOM 2805 N VAL A1158 59.511 -7.974 -2.218 1.00 54.27 N ANISOU 2805 N VAL A1158 8041 5778 6801 -1050 1394 870 N ATOM 2806 CA VAL A1158 60.018 -9.288 -2.605 1.00 50.18 C ANISOU 2806 CA VAL A1158 7809 4982 6274 -1054 1351 987 C ATOM 2807 C VAL A1158 60.570 -10.052 -1.413 1.00 56.73 C ANISOU 2807 C VAL A1158 8994 5685 6875 -1038 1451 1204 C ATOM 2808 O VAL A1158 60.814 -9.475 -0.355 1.00 65.05 O ANISOU 2808 O VAL A1158 10075 6888 7754 -962 1514 1263 O ATOM 2809 CB VAL A1158 61.135 -9.183 -3.660 1.00 45.86 C ANISOU 2809 CB VAL A1158 7281 4393 5753 -796 1105 961 C ATOM 2810 CG1 VAL A1158 60.564 -8.786 -5.002 1.00 39.02 C ANISOU 2810 CG1 VAL A1158 6156 3573 5096 -820 1004 775 C ATOM 2811 CG2 VAL A1158 62.201 -8.197 -3.204 1.00 43.48 C ANISOU 2811 CG2 VAL A1158 6950 4260 5311 -548 1007 989 C ATOM 2812 N LYS A1159 60.772 -11.354 -1.593 1.00 65.62 N ANISOU 2812 N LYS A1159 10365 6564 8003 -1070 1418 1292 N ATOM 2813 CA LYS A1159 61.411 -12.165 -0.566 1.00 66.22 C ANISOU 2813 CA LYS A1159 10711 6569 7879 -964 1398 1442 C ATOM 2814 C LYS A1159 62.878 -11.755 -0.465 1.00 68.16 C ANISOU 2814 C LYS A1159 11042 6879 7977 -623 1200 1471 C ATOM 2815 O LYS A1159 63.535 -11.523 -1.482 1.00 68.87 O ANISOU 2815 O LYS A1159 11066 6954 8148 -470 1037 1401 O ATOM 2816 CB LYS A1159 61.269 -13.656 -0.875 1.00 63.88 C ANISOU 2816 CB LYS A1159 10603 6015 7653 -1055 1368 1489 C ATOM 2817 CG LYS A1159 61.390 -14.545 0.351 1.00 68.32 C ANISOU 2817 CG LYS A1159 11431 6492 8037 -1066 1441 1645 C ATOM 2818 CD LYS A1159 60.614 -15.845 0.183 1.00 75.05 C ANISOU 2818 CD LYS A1159 12398 7110 9008 -1302 1524 1683 C ATOM 2819 CE LYS A1159 61.258 -16.762 -0.843 1.00 74.73 C ANISOU 2819 CE LYS A1159 12482 6849 9064 -1180 1320 1652 C ATOM 2820 NZ LYS A1159 60.547 -18.067 -0.929 1.00 77.49 N ANISOU 2820 NZ LYS A1159 12969 6947 9526 -1404 1392 1695 N ATOM 2821 N ALA A1160 63.374 -11.671 0.767 1.00 72.17 N ANISOU 2821 N ALA A1160 11682 7468 8271 -504 1215 1559 N ATOM 2822 CA ALA A1160 64.657 -11.037 1.079 1.00 63.67 C ANISOU 2822 CA ALA A1160 10624 6511 7055 -199 1050 1551 C ATOM 2823 C ALA A1160 65.845 -11.536 0.254 1.00 68.59 C ANISOU 2823 C ALA A1160 11304 7045 7714 29 819 1509 C ATOM 2824 O ALA A1160 66.602 -10.732 -0.295 1.00 73.46 O ANISOU 2824 O ALA A1160 11776 7775 8361 203 693 1430 O ATOM 2825 CB ALA A1160 64.960 -11.203 2.558 1.00 54.54 C ANISOU 2825 CB ALA A1160 9651 5407 5663 -114 1090 1645 C ATOM 2826 N GLY A1161 66.019 -12.851 0.174 1.00 56.15 N ANISOU 2826 N GLY A1161 9929 5274 6134 30 771 1555 N ATOM 2827 CA GLY A1161 67.180 -13.401 -0.502 1.00 57.94 C ANISOU 2827 CA GLY A1161 10210 5434 6368 260 561 1499 C ATOM 2828 C GLY A1161 66.863 -14.319 -1.666 1.00 62.30 C ANISOU 2828 C GLY A1161 10788 5800 7083 174 520 1462 C ATOM 2829 O GLY A1161 67.529 -15.337 -1.855 1.00 65.90 O ANISOU 2829 O GLY A1161 11408 6125 7508 300 400 1460 O ATOM 2830 N ASP A1162 65.850 -13.959 -2.449 1.00 56.94 N ANISOU 2830 N ASP A1162 9951 5108 6576 -31 610 1416 N ATOM 2831 CA ASP A1162 65.462 -14.755 -3.610 1.00 53.36 C ANISOU 2831 CA ASP A1162 9506 4477 6290 -117 563 1356 C ATOM 2832 C ASP A1162 65.694 -13.970 -4.899 1.00 55.18 C ANISOU 2832 C ASP A1162 9525 4800 6639 -24 464 1230 C ATOM 2833 O ASP A1162 64.891 -13.106 -5.255 1.00 56.41 O ANISOU 2833 O ASP A1162 9509 5026 6899 -165 554 1182 O ATOM 2834 CB ASP A1162 63.995 -15.186 -3.503 1.00 55.02 C ANISOU 2834 CB ASP A1162 9720 4562 6624 -453 748 1381 C ATOM 2835 CG ASP A1162 63.648 -16.339 -4.436 1.00 68.96 C ANISOU 2835 CG ASP A1162 11565 6092 8546 -541 687 1331 C ATOM 2836 OD1 ASP A1162 64.213 -16.409 -5.549 1.00 69.61 O ANISOU 2836 OD1 ASP A1162 11604 6151 8695 -381 523 1231 O ATOM 2837 OD2 ASP A1162 62.808 -17.181 -4.050 1.00 69.77 O ANISOU 2837 OD2 ASP A1162 11772 6036 8704 -769 806 1385 O ATOM 2838 N PRO A1163 66.796 -14.275 -5.604 1.00 49.07 N ANISOU 2838 N PRO A1163 8766 4033 5845 216 285 1168 N ATOM 2839 CA PRO A1163 67.163 -13.594 -6.852 1.00 38.04 C ANISOU 2839 CA PRO A1163 7184 2736 4531 335 187 1053 C ATOM 2840 C PRO A1163 66.121 -13.787 -7.950 1.00 49.19 C ANISOU 2840 C PRO A1163 8546 4020 6124 171 208 975 C ATOM 2841 O PRO A1163 65.962 -12.915 -8.804 1.00 57.94 O ANISOU 2841 O PRO A1163 9492 5217 7307 197 186 894 O ATOM 2842 CB PRO A1163 68.489 -14.258 -7.241 1.00 38.81 C ANISOU 2842 CB PRO A1163 7346 2845 4555 594 19 1002 C ATOM 2843 CG PRO A1163 69.011 -14.853 -5.972 1.00 38.97 C ANISOU 2843 CG PRO A1163 7552 2831 4425 656 18 1088 C ATOM 2844 CD PRO A1163 67.794 -15.285 -5.217 1.00 43.55 C ANISOU 2844 CD PRO A1163 8262 3261 5026 397 173 1194 C ATOM 2845 N GLY A1164 65.424 -14.919 -7.925 1.00 45.93 N ANISOU 2845 N GLY A1164 8275 3391 5784 8 243 988 N ATOM 2846 CA GLY A1164 64.366 -15.180 -8.884 1.00 40.84 C ANISOU 2846 CA GLY A1164 7579 2608 5331 -172 256 883 C ATOM 2847 C GLY A1164 63.215 -14.211 -8.702 1.00 47.04 C ANISOU 2847 C GLY A1164 8180 3479 6212 -407 412 848 C ATOM 2848 O GLY A1164 62.734 -13.610 -9.666 1.00 59.41 O ANISOU 2848 O GLY A1164 9493 5179 7902 -416 357 691 O ATOM 2849 N GLU A1165 62.781 -14.057 -7.455 1.00 53.92 N ANISOU 2849 N GLU A1165 9083 4384 7019 -566 584 959 N ATOM 2850 CA GLU A1165 61.711 -13.127 -7.116 1.00 53.53 C ANISOU 2850 CA GLU A1165 8774 4517 7048 -770 734 896 C ATOM 2851 C GLU A1165 62.101 -11.690 -7.441 1.00 54.85 C ANISOU 2851 C GLU A1165 8671 4980 7191 -593 655 816 C ATOM 2852 O GLU A1165 61.276 -10.906 -7.913 1.00 60.58 O ANISOU 2852 O GLU A1165 9122 5856 8039 -676 666 675 O ATOM 2853 CB GLU A1165 61.344 -13.247 -5.634 1.00 59.80 C ANISOU 2853 CB GLU A1165 9696 5297 7727 -937 943 1047 C ATOM 2854 CG GLU A1165 60.643 -14.544 -5.261 1.00 74.65 C ANISOU 2854 CG GLU A1165 11705 6995 9665 -1154 1029 1090 C ATOM 2855 CD GLU A1165 59.222 -14.622 -5.794 1.00 86.49 C ANISOU 2855 CD GLU A1165 13003 8457 11403 -1464 1140 940 C ATOM 2856 OE1 GLU A1165 58.693 -13.588 -6.255 1.00 91.45 O ANISOU 2856 OE1 GLU A1165 13353 9259 12134 -1507 1160 792 O ATOM 2857 OE2 GLU A1165 58.631 -15.722 -5.749 1.00 91.99 O ANISOU 2857 OE2 GLU A1165 13778 8982 12192 -1646 1184 946 O ATOM 2858 N LEU A1166 63.361 -11.348 -7.190 1.00 42.93 N ANISOU 2858 N LEU A1166 7242 3543 5526 -347 568 896 N ATOM 2859 CA LEU A1166 63.851 -10.005 -7.479 1.00 39.40 C ANISOU 2859 CA LEU A1166 6564 3345 5060 -191 498 833 C ATOM 2860 C LEU A1166 63.871 -9.738 -8.983 1.00 41.41 C ANISOU 2860 C LEU A1166 6669 3641 5426 -103 367 697 C ATOM 2861 O LEU A1166 63.485 -8.660 -9.430 1.00 35.14 O ANISOU 2861 O LEU A1166 5645 3013 4694 -103 350 604 O ATOM 2862 CB LEU A1166 65.247 -9.796 -6.888 1.00 29.44 C ANISOU 2862 CB LEU A1166 5414 2144 3629 39 433 929 C ATOM 2863 CG LEU A1166 65.880 -8.434 -7.188 1.00 29.60 C ANISOU 2863 CG LEU A1166 5207 2397 3644 184 364 867 C ATOM 2864 CD1 LEU A1166 64.942 -7.299 -6.801 1.00 26.26 C ANISOU 2864 CD1 LEU A1166 4563 2132 3281 47 453 809 C ATOM 2865 CD2 LEU A1166 67.215 -8.289 -6.476 1.00 29.48 C ANISOU 2865 CD2 LEU A1166 5279 2444 3480 387 306 935 C ATOM 2866 N ALA A1167 64.323 -10.719 -9.758 1.00 28.75 N ANISOU 2866 N ALA A1167 5215 1878 3829 -12 266 684 N ATOM 2867 CA ALA A1167 64.353 -10.589 -11.211 1.00 32.22 C ANISOU 2867 CA ALA A1167 5546 2353 4343 89 142 554 C ATOM 2868 C ALA A1167 62.937 -10.457 -11.770 1.00 40.23 C ANISOU 2868 C ALA A1167 6397 3367 5522 -95 162 414 C ATOM 2869 O ALA A1167 62.689 -9.670 -12.694 1.00 45.61 O ANISOU 2869 O ALA A1167 6902 4179 6249 -28 89 303 O ATOM 2870 CB ALA A1167 65.063 -11.772 -11.835 1.00 28.94 C ANISOU 2870 CB ALA A1167 5337 1764 3896 228 31 552 C ATOM 2871 N ASN A1168 62.013 -11.225 -11.200 1.00 38.43 N ANISOU 2871 N ASN A1168 6232 2992 5380 -325 261 415 N ATOM 2872 CA ASN A1168 60.604 -11.120 -11.564 1.00 36.22 C ANISOU 2872 CA ASN A1168 5760 2729 5275 -525 294 256 C ATOM 2873 C ASN A1168 60.051 -9.735 -11.257 1.00 43.64 C ANISOU 2873 C ASN A1168 6441 3911 6227 -554 348 200 C ATOM 2874 O ASN A1168 59.297 -9.168 -12.050 1.00 51.50 O ANISOU 2874 O ASN A1168 7234 5007 7329 -554 277 32 O ATOM 2875 CB ASN A1168 59.778 -12.182 -10.838 1.00 36.09 C ANISOU 2875 CB ASN A1168 5852 2514 5347 -805 434 283 C ATOM 2876 CG ASN A1168 60.084 -13.584 -11.316 1.00 49.47 C ANISOU 2876 CG ASN A1168 7794 3925 7075 -798 354 294 C ATOM 2877 OD1 ASN A1168 60.479 -13.787 -12.464 1.00 57.28 O ANISOU 2877 OD1 ASN A1168 8792 4889 8084 -622 181 195 O ATOM 2878 ND2 ASN A1168 59.902 -14.562 -10.437 1.00 58.63 N ANISOU 2878 ND2 ASN A1168 9178 4866 8235 -983 480 414 N ATOM 2879 N ALA A1169 60.435 -9.194 -10.105 1.00 34.09 N ANISOU 2879 N ALA A1169 5253 2793 4904 -556 454 329 N ATOM 2880 CA ALA A1169 60.002 -7.859 -9.701 1.00 32.57 C ANISOU 2880 CA ALA A1169 4839 2824 4714 -562 496 277 C ATOM 2881 C ALA A1169 60.565 -6.784 -10.626 1.00 35.98 C ANISOU 2881 C ALA A1169 5163 3386 5121 -343 348 225 C ATOM 2882 O ALA A1169 59.901 -5.791 -10.911 1.00 47.29 O ANISOU 2882 O ALA A1169 6397 4955 6616 -338 316 108 O ATOM 2883 CB ALA A1169 60.412 -7.583 -8.272 1.00 30.36 C ANISOU 2883 CB ALA A1169 4633 2602 4299 -583 624 421 C ATOM 2884 N ILE A1170 61.797 -6.983 -11.079 1.00 31.11 N ANISOU 2884 N ILE A1170 4685 2728 4409 -162 264 311 N ATOM 2885 CA ILE A1170 62.432 -6.055 -12.006 1.00 32.48 C ANISOU 2885 CA ILE A1170 4785 3009 4545 27 153 285 C ATOM 2886 C ILE A1170 61.705 -6.076 -13.351 1.00 32.99 C ANISOU 2886 C ILE A1170 4771 3063 4700 54 44 133 C ATOM 2887 O ILE A1170 61.417 -5.021 -13.928 1.00 29.93 O ANISOU 2887 O ILE A1170 4257 2788 4326 125 -19 61 O ATOM 2888 CB ILE A1170 63.924 -6.392 -12.195 1.00 27.43 C ANISOU 2888 CB ILE A1170 4294 2342 3786 202 108 393 C ATOM 2889 CG1 ILE A1170 64.700 -6.069 -10.917 1.00 22.77 C ANISOU 2889 CG1 ILE A1170 3744 1806 3100 222 178 511 C ATOM 2890 CG2 ILE A1170 64.509 -5.628 -13.366 1.00 22.08 C ANISOU 2890 CG2 ILE A1170 3554 1760 3077 366 18 360 C ATOM 2891 CD1 ILE A1170 66.162 -6.469 -10.968 1.00 34.34 C ANISOU 2891 CD1 ILE A1170 5333 3258 4458 398 129 589 C ATOM 2892 N LEU A1171 61.400 -7.278 -13.837 1.00 25.47 N ANISOU 2892 N LEU A1171 3909 1963 3804 6 10 77 N ATOM 2893 CA LEU A1171 60.606 -7.433 -15.056 1.00 28.09 C ANISOU 2893 CA LEU A1171 4165 2278 4229 29 -108 -99 C ATOM 2894 C LEU A1171 59.247 -6.736 -14.927 1.00 37.00 C ANISOU 2894 C LEU A1171 5074 3505 5480 -91 -98 -250 C ATOM 2895 O LEU A1171 58.803 -6.023 -15.839 1.00 45.06 O ANISOU 2895 O LEU A1171 5988 4614 6521 18 -217 -377 O ATOM 2896 CB LEU A1171 60.408 -8.917 -15.381 1.00 28.47 C ANISOU 2896 CB LEU A1171 4342 2128 4346 -40 -139 -151 C ATOM 2897 CG LEU A1171 61.621 -9.692 -15.903 1.00 27.83 C ANISOU 2897 CG LEU A1171 4467 1950 4158 135 -210 -75 C ATOM 2898 CD1 LEU A1171 61.369 -11.186 -15.836 1.00 29.87 C ANISOU 2898 CD1 LEU A1171 4881 1971 4498 28 -220 -106 C ATOM 2899 CD2 LEU A1171 61.948 -9.277 -17.328 1.00 27.22 C ANISOU 2899 CD2 LEU A1171 4363 1964 4017 355 -350 -163 C ATOM 2900 N LYS A1172 58.601 -6.938 -13.782 1.00 39.98 N ANISOU 2900 N LYS A1172 5392 3874 5926 -302 43 -239 N ATOM 2901 CA LYS A1172 57.305 -6.329 -13.506 1.00 41.87 C ANISOU 2901 CA LYS A1172 5396 4230 6285 -427 76 -400 C ATOM 2902 C LYS A1172 57.416 -4.807 -13.492 1.00 38.15 C ANISOU 2902 C LYS A1172 4810 3936 5751 -282 26 -406 C ATOM 2903 O LYS A1172 56.514 -4.108 -13.952 1.00 46.67 O ANISOU 2903 O LYS A1172 5712 5115 6907 -247 -60 -583 O ATOM 2904 CB LYS A1172 56.749 -6.840 -12.171 1.00 45.38 C ANISOU 2904 CB LYS A1172 5818 4647 6777 -684 279 -357 C ATOM 2905 CG LYS A1172 55.249 -6.633 -11.979 1.00 55.61 C ANISOU 2905 CG LYS A1172 6848 6043 8237 -865 334 -570 C ATOM 2906 CD LYS A1172 54.924 -5.277 -11.365 1.00 66.91 C ANISOU 2906 CD LYS A1172 8098 7692 9634 -815 364 -612 C ATOM 2907 CE LYS A1172 53.422 -5.043 -11.295 1.00 77.25 C ANISOU 2907 CE LYS A1172 9110 9130 11110 -958 394 -869 C ATOM 2908 NZ LYS A1172 52.794 -5.051 -12.646 1.00 81.84 N ANISOU 2908 NZ LYS A1172 9570 9710 11814 -861 188 -1100 N ATOM 2909 N ALA A1173 58.527 -4.305 -12.961 1.00 39.00 N ANISOU 2909 N ALA A1173 5024 4072 5724 -190 68 -226 N ATOM 2910 CA ALA A1173 58.783 -2.870 -12.903 1.00 30.52 C ANISOU 2910 CA ALA A1173 3873 3128 4594 -63 24 -212 C ATOM 2911 C ALA A1173 59.000 -2.306 -14.298 1.00 31.06 C ANISOU 2911 C ALA A1173 3962 3206 4634 129 -140 -262 C ATOM 2912 O ALA A1173 58.662 -1.157 -14.567 1.00 33.16 O ANISOU 2912 O ALA A1173 4142 3556 4902 220 -217 -327 O ATOM 2913 CB ALA A1173 59.987 -2.578 -12.024 1.00 22.85 C ANISOU 2913 CB ALA A1173 3007 2171 3504 -24 102 -25 C ATOM 2914 N LEU A1174 59.579 -3.118 -15.175 1.00 32.74 N ANISOU 2914 N LEU A1174 4310 3327 4803 203 -194 -227 N ATOM 2915 CA LEU A1174 59.768 -2.736 -16.569 1.00 28.18 C ANISOU 2915 CA LEU A1174 3779 2759 4169 389 -335 -271 C ATOM 2916 C LEU A1174 58.423 -2.595 -17.277 1.00 33.83 C ANISOU 2916 C LEU A1174 4368 3503 4983 406 -462 -495 C ATOM 2917 O LEU A1174 58.092 -1.530 -17.833 1.00 43.46 O ANISOU 2917 O LEU A1174 5546 4792 6174 538 -567 -559 O ATOM 2918 CB LEU A1174 60.647 -3.767 -17.282 1.00 27.64 C ANISOU 2918 CB LEU A1174 3875 2601 4026 467 -357 -208 C ATOM 2919 CG LEU A1174 60.704 -3.758 -18.812 1.00 35.12 C ANISOU 2919 CG LEU A1174 4890 3552 4904 652 -497 -282 C ATOM 2920 CD1 LEU A1174 61.115 -2.401 -19.357 1.00 41.22 C ANISOU 2920 CD1 LEU A1174 5681 4413 5567 798 -532 -216 C ATOM 2921 CD2 LEU A1174 61.659 -4.830 -19.297 1.00 25.33 C ANISOU 2921 CD2 LEU A1174 3801 2238 3586 726 -496 -223 C ATOM 2922 N GLU A1175 57.645 -3.676 -17.242 1.00 37.47 N ANISOU 2922 N GLU A1175 4774 3900 5564 275 -459 -624 N ATOM 2923 CA GLU A1175 56.329 -3.678 -17.873 1.00 44.39 C ANISOU 2923 CA GLU A1175 5493 4811 6561 277 -586 -879 C ATOM 2924 C GLU A1175 55.474 -2.553 -17.307 1.00 41.54 C ANISOU 2924 C GLU A1175 4939 4584 6261 258 -588 -982 C ATOM 2925 O GLU A1175 54.660 -1.959 -18.013 1.00 60.30 O ANISOU 2925 O GLU A1175 7210 7029 8671 381 -746 -1171 O ATOM 2926 CB GLU A1175 55.630 -5.026 -17.678 1.00 54.10 C ANISOU 2926 CB GLU A1175 6666 5942 7947 74 -543 -1001 C ATOM 2927 CG GLU A1175 56.488 -6.242 -18.015 1.00 67.45 C ANISOU 2927 CG GLU A1175 8564 7473 9591 77 -533 -897 C ATOM 2928 CD GLU A1175 57.015 -6.231 -19.442 1.00 72.39 C ANISOU 2928 CD GLU A1175 9314 8091 10102 332 -706 -928 C ATOM 2929 OE1 GLU A1175 56.336 -5.678 -20.334 1.00 69.91 O ANISOU 2929 OE1 GLU A1175 8914 7853 9794 467 -864 -1100 O ATOM 2930 OE2 GLU A1175 58.115 -6.781 -19.668 1.00 68.31 O ANISOU 2930 OE2 GLU A1175 8983 7499 9474 412 -686 -786 O ATOM 2931 N LEU A1176 55.679 -2.257 -16.029 1.00 35.16 N ANISOU 2931 N LEU A1176 4094 3815 5452 128 -425 -867 N ATOM 2932 CA LEU A1176 54.990 -1.158 -15.370 1.00 38.45 C ANISOU 2932 CA LEU A1176 4336 4366 5909 124 -417 -957 C ATOM 2933 C LEU A1176 55.520 0.186 -15.869 1.00 45.12 C ANISOU 2933 C LEU A1176 5260 5245 6638 350 -536 -892 C ATOM 2934 O LEU A1176 54.795 1.181 -15.897 1.00 47.86 O ANISOU 2934 O LEU A1176 5487 5679 7018 439 -632 -1030 O ATOM 2935 CB LEU A1176 55.153 -1.268 -13.852 1.00 39.77 C ANISOU 2935 CB LEU A1176 4469 4565 6077 -63 -207 -845 C ATOM 2936 CG LEU A1176 53.982 -0.830 -12.973 1.00 43.41 C ANISOU 2936 CG LEU A1176 4683 5170 6640 -181 -135 -1016 C ATOM 2937 CD1 LEU A1176 52.683 -1.424 -13.484 1.00 56.72 C ANISOU 2937 CD1 LEU A1176 6173 6884 8493 -273 -187 -1281 C ATOM 2938 CD2 LEU A1176 54.228 -1.262 -11.541 1.00 45.16 C ANISOU 2938 CD2 LEU A1176 4927 5402 6829 -376 96 -879 C ATOM 2939 N SER A1177 56.789 0.204 -16.270 1.00 42.73 N ANISOU 2939 N SER A1177 5162 4868 6205 441 -527 -688 N ATOM 2940 CA SER A1177 57.435 1.432 -16.721 1.00 34.66 C ANISOU 2940 CA SER A1177 4244 3853 5074 615 -601 -590 C ATOM 2941 C SER A1177 57.097 1.713 -18.177 1.00 39.13 C ANISOU 2941 C SER A1177 4881 4400 5586 813 -788 -685 C ATOM 2942 O SER A1177 57.453 2.761 -18.712 1.00 36.70 O ANISOU 2942 O SER A1177 4681 4081 5182 965 -864 -617 O ATOM 2943 CB SER A1177 58.953 1.353 -16.545 1.00 25.35 C ANISOU 2943 CB SER A1177 3226 2623 3782 615 -495 -347 C ATOM 2944 OG SER A1177 59.543 0.559 -17.560 1.00 40.75 O ANISOU 2944 OG SER A1177 5313 4513 5658 688 -525 -297 O ATOM 2945 N ARG A1178 56.416 0.773 -18.823 1.00 38.97 N ANISOU 2945 N ARG A1178 4816 4366 5623 811 -865 -843 N ATOM 2946 CA ARG A1178 55.924 1.028 -20.178 1.00 41.11 C ANISOU 2946 CA ARG A1178 5142 4638 5839 1024 -1071 -978 C ATOM 2947 C ARG A1178 54.835 2.114 -20.221 1.00 46.62 C ANISOU 2947 C ARG A1178 5716 5410 6586 1138 -1222 -1166 C ATOM 2948 O ARG A1178 54.561 2.685 -21.279 1.00 45.37 O ANISOU 2948 O ARG A1178 5654 5246 6338 1364 -1409 -1239 O ATOM 2949 CB ARG A1178 55.395 -0.261 -20.804 1.00 33.00 C ANISOU 2949 CB ARG A1178 4073 3581 4883 995 -1138 -1143 C ATOM 2950 CG ARG A1178 56.414 -1.378 -20.817 1.00 41.78 C ANISOU 2950 CG ARG A1178 5321 4605 5947 914 -1020 -986 C ATOM 2951 CD ARG A1178 56.040 -2.485 -21.784 1.00 51.67 C ANISOU 2951 CD ARG A1178 6597 5806 7231 963 -1139 -1148 C ATOM 2952 NE ARG A1178 56.947 -3.620 -21.647 1.00 61.65 N ANISOU 2952 NE ARG A1178 7982 6973 8470 879 -1030 -1017 N ATOM 2953 CZ ARG A1178 58.177 -3.658 -22.150 1.00 60.17 C ANISOU 2953 CZ ARG A1178 7986 6766 8110 1005 -998 -840 C ATOM 2954 NH1 ARG A1178 58.651 -2.624 -22.834 1.00 57.37 N ANISOU 2954 NH1 ARG A1178 7734 6474 7591 1192 -1043 -751 N ATOM 2955 NH2 ARG A1178 58.933 -4.733 -21.974 1.00 51.41 N ANISOU 2955 NH2 ARG A1178 6971 5572 6990 945 -919 -756 N ATOM 2956 N SER A1179 54.218 2.398 -19.076 1.00 43.56 N ANISOU 2956 N SER A1179 5129 5096 6326 1001 -1148 -1250 N ATOM 2957 CA SER A1179 53.189 3.435 -19.002 1.00 42.52 C ANISOU 2957 CA SER A1179 4857 5050 6249 1120 -1292 -1451 C ATOM 2958 C SER A1179 53.533 4.524 -17.988 1.00 40.29 C ANISOU 2958 C SER A1179 4568 4789 5951 1097 -1211 -1339 C ATOM 2959 O SER A1179 54.602 4.502 -17.376 1.00 46.98 O ANISOU 2959 O SER A1179 5519 5587 6742 992 -1049 -1105 O ATOM 2960 CB SER A1179 51.829 2.822 -18.657 1.00 39.05 C ANISOU 2960 CB SER A1179 4118 4720 6001 1005 -1313 -1754 C ATOM 2961 OG SER A1179 51.250 2.197 -19.789 1.00 54.22 O ANISOU 2961 OG SER A1179 6023 6632 7949 1107 -1484 -1945 O ATOM 2962 N ASP A1180 52.614 5.472 -17.823 1.00 35.67 N ANISOU 2962 N ASP A1180 3854 4279 5418 1214 -1344 -1532 N ATOM 2963 CA ASP A1180 52.788 6.598 -16.907 1.00 40.10 C ANISOU 2963 CA ASP A1180 4400 4861 5975 1227 -1310 -1479 C ATOM 2964 C ASP A1180 52.960 6.135 -15.461 1.00 50.09 C ANISOU 2964 C ASP A1180 5518 6202 7312 977 -1073 -1424 C ATOM 2965 O ASP A1180 52.179 5.325 -14.963 1.00 59.89 O ANISOU 2965 O ASP A1180 6545 7547 8664 821 -984 -1577 O ATOM 2966 CB ASP A1180 51.594 7.554 -17.020 1.00 44.38 C ANISOU 2966 CB ASP A1180 4804 5485 6575 1419 -1521 -1756 C ATOM 2967 CG ASP A1180 51.679 8.722 -16.053 1.00 60.37 C ANISOU 2967 CG ASP A1180 6803 7530 8606 1449 -1507 -1740 C ATOM 2968 OD1 ASP A1180 52.806 9.125 -15.690 1.00 65.93 O ANISOU 2968 OD1 ASP A1180 7683 8133 9235 1398 -1405 -1486 O ATOM 2969 OD2 ASP A1180 50.613 9.242 -15.660 1.00 62.66 O ANISOU 2969 OD2 ASP A1180 6887 7943 8978 1525 -1604 -2000 O ATOM 2970 N LEU A1181 53.987 6.659 -14.795 1.00 44.68 N ANISOU 2970 N LEU A1181 4954 5465 6559 938 -969 -1209 N ATOM 2971 CA LEU A1181 54.302 6.278 -13.419 1.00 40.46 C ANISOU 2971 CA LEU A1181 4329 4994 6049 737 -757 -1133 C ATOM 2972 C LEU A1181 54.104 7.429 -12.431 1.00 49.81 C ANISOU 2972 C LEU A1181 5425 6253 7249 782 -767 -1198 C ATOM 2973 O LEU A1181 54.550 7.351 -11.286 1.00 50.51 O ANISOU 2973 O LEU A1181 5485 6387 7321 660 -612 -1111 O ATOM 2974 CB LEU A1181 55.744 5.771 -13.325 1.00 28.50 C ANISOU 2974 CB LEU A1181 3009 3377 4443 654 -626 -851 C ATOM 2975 CG LEU A1181 56.086 4.406 -13.921 1.00 32.54 C ANISOU 2975 CG LEU A1181 3599 3827 4936 571 -563 -773 C ATOM 2976 CD1 LEU A1181 57.596 4.227 -13.993 1.00 22.56 C ANISOU 2976 CD1 LEU A1181 2534 2471 3568 564 -484 -518 C ATOM 2977 CD2 LEU A1181 55.457 3.295 -13.098 1.00 24.82 C ANISOU 2977 CD2 LEU A1181 2476 2915 4041 366 -416 -849 C ATOM 2978 N SER A1182 53.434 8.489 -12.877 1.00 43.16 N ANISOU 2978 N SER A1182 4553 5417 6428 978 -966 -1360 N ATOM 2979 CA SER A1182 53.246 9.696 -12.071 1.00 42.36 C ANISOU 2979 CA SER A1182 4393 5361 6342 1064 -1020 -1443 C ATOM 2980 C SER A1182 52.547 9.430 -10.735 1.00 43.65 C ANISOU 2980 C SER A1182 4296 5721 6566 931 -873 -1595 C ATOM 2981 O SER A1182 53.069 9.770 -9.667 1.00 45.78 O ANISOU 2981 O SER A1182 4570 6022 6802 872 -767 -1515 O ATOM 2982 CB SER A1182 52.452 10.736 -12.867 1.00 47.31 C ANISOU 2982 CB SER A1182 5031 5958 6986 1321 -1285 -1632 C ATOM 2983 OG SER A1182 53.103 11.058 -14.084 1.00 50.45 O ANISOU 2983 OG SER A1182 5705 6168 7296 1450 -1408 -1472 O ATOM 2984 N LYS A1183 51.362 8.830 -10.810 1.00 44.95 N ANISOU 2984 N LYS A1183 5594 7242 4242 19 539 8 N ATOM 2985 CA LYS A1183 50.563 8.504 -9.632 1.00 43.85 C ANISOU 2985 CA LYS A1183 5341 7150 4169 172 568 -132 C ATOM 2986 C LYS A1183 51.369 7.681 -8.627 1.00 48.97 C ANISOU 2986 C LYS A1183 5851 7815 4942 44 722 -83 C ATOM 2987 O LYS A1183 51.302 7.909 -7.416 1.00 45.63 O ANISOU 2987 O LYS A1183 5454 7331 4552 96 689 -108 O ATOM 2988 CB LYS A1183 49.295 7.752 -10.055 1.00 39.15 C ANISOU 2988 CB LYS A1183 4561 6742 3574 315 647 -322 C ATOM 2989 CG LYS A1183 48.590 6.981 -8.946 1.00 49.89 C ANISOU 2989 CG LYS A1183 5736 8215 5005 383 761 -474 C ATOM 2990 CD LYS A1183 47.862 7.901 -7.980 1.00 67.47 C ANISOU 2990 CD LYS A1183 8063 10390 7181 564 601 -582 C ATOM 2991 CE LYS A1183 47.028 7.100 -6.989 1.00 69.07 C ANISOU 2991 CE LYS A1183 8069 10748 7425 610 728 -763 C ATOM 2992 NZ LYS A1183 46.404 7.964 -5.952 1.00 64.78 N ANISOU 2992 NZ LYS A1183 7600 10176 6835 773 581 -878 N ATOM 2993 N PHE A1184 52.147 6.738 -9.149 1.00 44.39 N ANISOU 2993 N PHE A1184 5131 7313 4421 -115 877 -22 N ATOM 2994 CA PHE A1184 52.993 5.879 -8.332 1.00 40.06 C ANISOU 2994 CA PHE A1184 4463 6778 3979 -222 1008 17 C ATOM 2995 C PHE A1184 54.018 6.698 -7.541 1.00 35.35 C ANISOU 2995 C PHE A1184 4010 6038 3384 -303 915 137 C ATOM 2996 O PHE A1184 54.138 6.561 -6.315 1.00 34.39 O ANISOU 2996 O PHE A1184 3876 5870 3322 -276 928 124 O ATOM 2997 CB PHE A1184 53.699 4.854 -9.224 1.00 34.87 C ANISOU 2997 CB PHE A1184 3662 6209 3377 -351 1139 50 C ATOM 2998 CG PHE A1184 53.972 3.540 -8.551 1.00 42.45 C ANISOU 2998 CG PHE A1184 4569 7009 4550 -331 1175 12 C ATOM 2999 CD1 PHE A1184 54.013 3.445 -7.171 1.00 42.65 C ANISOU 2999 CD1 PHE A1184 4613 6981 4613 -301 1183 1 C ATOM 3000 CD2 PHE A1184 54.189 2.397 -9.305 1.00 50.90 C ANISOU 3000 CD2 PHE A1184 5600 7992 5748 -335 1195 -2 C ATOM 3001 CE1 PHE A1184 54.265 2.238 -6.555 1.00 46.01 C ANISOU 3001 CE1 PHE A1184 5029 7273 5181 -286 1215 -17 C ATOM 3002 CE2 PHE A1184 54.443 1.184 -8.694 1.00 51.21 C ANISOU 3002 CE2 PHE A1184 5633 7903 5920 -306 1222 -16 C ATOM 3003 CZ PHE A1184 54.481 1.104 -7.316 1.00 50.46 C ANISOU 3003 CZ PHE A1184 5567 7762 5844 -285 1233 -20 C ATOM 3004 N ARG A1185 54.745 7.555 -8.255 1.00 32.11 N ANISOU 3004 N ARG A1185 3743 5562 2896 -418 824 251 N ATOM 3005 CA ARG A1185 55.777 8.395 -7.656 1.00 29.16 C ANISOU 3005 CA ARG A1185 3513 5063 2501 -533 739 364 C ATOM 3006 C ARG A1185 55.193 9.327 -6.602 1.00 30.04 C ANISOU 3006 C ARG A1185 3789 5033 2591 -392 593 341 C ATOM 3007 O ARG A1185 55.795 9.539 -5.543 1.00 43.92 O ANISOU 3007 O ARG A1185 5576 6719 4392 -427 576 381 O ATOM 3008 CB ARG A1185 56.500 9.206 -8.736 1.00 29.95 C ANISOU 3008 CB ARG A1185 3769 5126 2483 -709 665 475 C ATOM 3009 CG ARG A1185 57.180 8.349 -9.791 1.00 29.75 C ANISOU 3009 CG ARG A1185 3571 5264 2469 -866 806 489 C ATOM 3010 CD ARG A1185 58.120 9.158 -10.668 1.00 31.13 C ANISOU 3010 CD ARG A1185 3895 5420 2514 -1101 750 601 C ATOM 3011 NE ARG A1185 59.142 8.308 -11.279 1.00 36.98 N ANISOU 3011 NE ARG A1185 4423 6344 3283 -1281 897 600 N ATOM 3012 CZ ARG A1185 59.091 7.838 -12.521 1.00 50.06 C ANISOU 3012 CZ ARG A1185 5991 8119 4909 -1339 961 579 C ATOM 3013 NH1 ARG A1185 58.072 8.145 -13.311 1.00 70.45 N ANISOU 3013 NH1 ARG A1185 8683 10672 7411 -1252 904 573 N ATOM 3014 NH2 ARG A1185 60.070 7.069 -12.976 1.00 45.79 N ANISOU 3014 NH2 ARG A1185 5287 7606 4506 -1374 993 511 N ATOM 3015 N GLU A1186 54.015 9.873 -6.889 1.00 34.74 N ANISOU 3015 N GLU A1186 4484 5599 3116 -219 480 261 N ATOM 3016 CA GLU A1186 53.358 10.768 -5.945 1.00 43.94 C ANISOU 3016 CA GLU A1186 5796 6649 4251 -54 324 206 C ATOM 3017 C GLU A1186 52.939 10.009 -4.686 1.00 36.84 C ANISOU 3017 C GLU A1186 4721 5822 3456 33 426 102 C ATOM 3018 O GLU A1186 53.080 10.516 -3.566 1.00 44.90 O ANISOU 3018 O GLU A1186 5817 6750 4494 70 356 110 O ATOM 3019 CB GLU A1186 52.151 11.447 -6.593 1.00 54.04 C ANISOU 3019 CB GLU A1186 7202 7910 5422 143 168 106 C ATOM 3020 CG GLU A1186 51.733 12.740 -5.903 1.00 73.21 C ANISOU 3020 CG GLU A1186 9871 10171 7773 298 -62 79 C ATOM 3021 CD GLU A1186 52.846 13.776 -5.874 1.00 79.84 C ANISOU 3021 CD GLU A1186 10982 10808 8547 133 -184 258 C ATOM 3022 OE1 GLU A1186 53.633 13.839 -6.844 1.00 86.74 O ANISOU 3022 OE1 GLU A1186 11932 11661 9365 -67 -157 383 O ATOM 3023 OE2 GLU A1186 52.936 14.526 -4.879 1.00 77.09 O ANISOU 3023 OE2 GLU A1186 10768 10332 8193 188 -302 267 O ATOM 3024 N ASN A1187 52.437 8.789 -4.876 1.00 28.35 N ANISOU 3024 N ASN A1187 3425 4909 2438 50 591 6 N ATOM 3025 CA ASN A1187 52.098 7.918 -3.754 1.00 27.45 C ANISOU 3025 CA ASN A1187 3162 4865 2403 83 710 -85 C ATOM 3026 C ASN A1187 53.308 7.648 -2.868 1.00 37.51 C ANISOU 3026 C ASN A1187 4434 6064 3753 -46 763 26 C ATOM 3027 O ASN A1187 53.204 7.666 -1.640 1.00 43.00 O ANISOU 3027 O ASN A1187 5137 6721 4480 -5 757 -7 O ATOM 3028 CB ASN A1187 51.520 6.591 -4.247 1.00 26.81 C ANISOU 3028 CB ASN A1187 2877 4954 2354 72 887 -186 C ATOM 3029 CG ASN A1187 50.141 6.742 -4.854 1.00 52.33 C ANISOU 3029 CG ASN A1187 6070 8298 5513 223 849 -347 C ATOM 3030 OD1 ASN A1187 49.732 5.941 -5.693 1.00 63.53 O ANISOU 3030 OD1 ASN A1187 7359 9847 6932 206 958 -409 O ATOM 3031 ND2 ASN A1187 49.418 7.776 -4.437 1.00 56.25 N ANISOU 3031 ND2 ASN A1187 6675 8755 5942 383 685 -430 N ATOM 3032 N CYS A1188 54.453 7.399 -3.500 1.00 34.96 N ANISOU 3032 N CYS A1188 4093 5738 3453 -199 812 142 N ATOM 3033 CA CYS A1188 55.695 7.188 -2.761 1.00 30.01 C ANISOU 3033 CA CYS A1188 3454 5060 2886 -311 846 230 C ATOM 3034 C CYS A1188 56.091 8.424 -1.959 1.00 35.81 C ANISOU 3034 C CYS A1188 4366 5649 3591 -310 698 297 C ATOM 3035 O CYS A1188 56.429 8.322 -0.775 1.00 38.04 O ANISOU 3035 O CYS A1188 4645 5884 3925 -301 704 301 O ATOM 3036 CB CYS A1188 56.826 6.803 -3.711 1.00 35.52 C ANISOU 3036 CB CYS A1188 4083 5821 3591 -471 910 308 C ATOM 3037 SG CYS A1188 56.571 5.221 -4.528 1.00 36.39 S ANISOU 3037 SG CYS A1188 3981 6094 3752 -477 1087 231 S ATOM 3038 N LYS A1189 56.045 9.588 -2.604 1.00 27.86 N ANISOU 3038 N LYS A1189 3533 4561 2490 -321 558 350 N ATOM 3039 CA LYS A1189 56.361 10.842 -1.923 1.00 30.53 C ANISOU 3039 CA LYS A1189 4076 4741 2781 -322 399 413 C ATOM 3040 C LYS A1189 55.492 11.041 -0.683 1.00 34.79 C ANISOU 3040 C LYS A1189 4631 5239 3347 -144 343 317 C ATOM 3041 O LYS A1189 56.000 11.273 0.424 1.00 41.45 O ANISOU 3041 O LYS A1189 5507 6013 4230 -161 320 348 O ATOM 3042 CB LYS A1189 56.190 12.033 -2.869 1.00 30.06 C ANISOU 3042 CB LYS A1189 4250 4580 2591 -336 236 466 C ATOM 3043 CG LYS A1189 57.175 12.069 -4.028 1.00 49.14 C ANISOU 3043 CG LYS A1189 6693 7026 4949 -560 274 573 C ATOM 3044 CD LYS A1189 57.169 13.433 -4.709 1.00 59.81 C ANISOU 3044 CD LYS A1189 8358 8223 6146 -613 86 651 C ATOM 3045 CE LYS A1189 58.045 13.446 -5.953 1.00 71.26 C ANISOU 3045 CE LYS A1189 9839 9725 7510 -863 135 745 C ATOM 3046 NZ LYS A1189 57.500 12.573 -7.031 1.00 74.90 N ANISOU 3046 NZ LYS A1189 10140 10335 7984 -821 238 687 N ATOM 3047 N LYS A1190 54.181 10.931 -0.872 1.00 28.56 N ANISOU 3047 N LYS A1190 3806 4516 2532 23 326 185 N ATOM 3048 CA LYS A1190 53.237 11.179 0.211 1.00 28.66 C ANISOU 3048 CA LYS A1190 3819 4527 2544 192 267 58 C ATOM 3049 C LYS A1190 53.335 10.133 1.326 1.00 39.17 C ANISOU 3049 C LYS A1190 4987 5930 3966 159 421 17 C ATOM 3050 O LYS A1190 53.135 10.449 2.504 1.00 55.39 O ANISOU 3050 O LYS A1190 7072 7943 6029 223 374 -26 O ATOM 3051 CB LYS A1190 51.815 11.246 -0.344 1.00 29.29 C ANISOU 3051 CB LYS A1190 3864 4707 2558 371 220 -107 C ATOM 3052 CG LYS A1190 51.631 12.379 -1.343 1.00 36.88 C ANISOU 3052 CG LYS A1190 5037 5565 3409 442 26 -77 C ATOM 3053 CD LYS A1190 50.179 12.803 -1.471 1.00 63.51 C ANISOU 3053 CD LYS A1190 8420 9007 6702 692 -98 -276 C ATOM 3054 CE LYS A1190 50.060 14.091 -2.276 1.00 76.74 C ANISOU 3054 CE LYS A1190 10380 10525 8251 790 -343 -240 C ATOM 3055 NZ LYS A1190 48.661 14.600 -2.330 1.00 82.70 N ANISOU 3055 NZ LYS A1190 11158 11345 8919 1080 -505 -462 N ATOM 3056 N ARG A1191 53.659 8.896 0.961 1.00 32.24 N ANISOU 3056 N ARG A1191 3958 5150 3144 58 594 29 N ATOM 3057 CA ARG A1191 53.873 7.848 1.955 1.00 30.26 C ANISOU 3057 CA ARG A1191 3602 4934 2962 12 728 6 C ATOM 3058 C ARG A1191 55.114 8.136 2.801 1.00 31.50 C ANISOU 3058 C ARG A1191 3829 4974 3164 -66 691 124 C ATOM 3059 O ARG A1191 55.082 8.006 4.028 1.00 32.23 O ANISOU 3059 O ARG A1191 3930 5034 3282 -41 699 97 O ATOM 3060 CB ARG A1191 53.997 6.480 1.282 1.00 29.91 C ANISOU 3060 CB ARG A1191 3415 4996 2955 -68 896 -6 C ATOM 3061 CG ARG A1191 54.474 5.369 2.210 1.00 35.48 C ANISOU 3061 CG ARG A1191 4067 5695 3718 -130 1011 -2 C ATOM 3062 CD ARG A1191 53.562 5.208 3.415 1.00 42.99 C ANISOU 3062 CD ARG A1191 5026 6662 4646 -75 1033 -112 C ATOM 3063 NE ARG A1191 54.118 4.277 4.392 1.00 54.33 N ANISOU 3063 NE ARG A1191 6471 8053 6120 -140 1114 -88 N ATOM 3064 CZ ARG A1191 53.653 4.125 5.628 1.00 53.03 C ANISOU 3064 CZ ARG A1191 6345 7874 5932 -132 1131 -151 C ATOM 3065 NH1 ARG A1191 52.622 4.849 6.043 1.00 50.21 N ANISOU 3065 NH1 ARG A1191 5989 7569 5518 -57 1078 -257 N ATOM 3066 NH2 ARG A1191 54.221 3.254 6.451 1.00 47.89 N ANISOU 3066 NH2 ARG A1191 5735 7160 5301 -193 1192 -119 N ATOM 3067 N ALA A1192 56.203 8.526 2.143 1.00 25.90 N ANISOU 3067 N ALA A1192 3166 4218 2456 -171 654 243 N ATOM 3068 CA ALA A1192 57.433 8.870 2.853 1.00 34.35 C ANISOU 3068 CA ALA A1192 4290 5204 3557 -256 615 339 C ATOM 3069 C ALA A1192 57.203 10.029 3.823 1.00 41.06 C ANISOU 3069 C ALA A1192 5287 5934 4379 -184 473 343 C ATOM 3070 O ALA A1192 57.580 9.958 5.002 1.00 42.34 O ANISOU 3070 O ALA A1192 5453 6051 4582 -177 473 349 O ATOM 3071 CB ALA A1192 58.534 9.215 1.869 1.00 31.56 C ANISOU 3071 CB ALA A1192 3957 4857 3179 -404 597 439 C ATOM 3072 N MET A1193 56.572 11.090 3.322 1.00 37.26 N ANISOU 3072 N MET A1193 4938 5397 3821 -118 340 333 N ATOM 3073 CA MET A1193 56.270 12.257 4.147 1.00 32.84 C ANISOU 3073 CA MET A1193 4537 4716 3223 -25 179 321 C ATOM 3074 C MET A1193 55.375 11.894 5.335 1.00 40.15 C ANISOU 3074 C MET A1193 5387 5689 4178 108 207 195 C ATOM 3075 O MET A1193 55.585 12.374 6.455 1.00 43.15 O ANISOU 3075 O MET A1193 5829 5993 4573 136 143 202 O ATOM 3076 CB MET A1193 55.622 13.350 3.296 1.00 39.32 C ANISOU 3076 CB MET A1193 5532 5467 3941 55 15 308 C ATOM 3077 CG MET A1193 56.575 13.940 2.261 1.00 72.37 C ANISOU 3077 CG MET A1193 9856 9576 8065 -114 -38 447 C ATOM 3078 SD MET A1193 55.815 15.096 1.103 1.00 89.77 S ANISOU 3078 SD MET A1193 12309 11676 10122 -28 -237 440 S ATOM 3079 CE MET A1193 57.242 15.584 0.134 1.00 84.87 C ANISOU 3079 CE MET A1193 11840 10982 9426 -324 -245 622 C ATOM 3080 N SER A1194 54.390 11.034 5.090 1.00 35.92 N ANISOU 3080 N SER A1194 4715 5290 3642 172 310 74 N ATOM 3081 CA SER A1194 53.515 10.556 6.159 1.00 30.38 C ANISOU 3081 CA SER A1194 3929 4669 2947 252 367 -62 C ATOM 3082 C SER A1194 54.296 9.798 7.236 1.00 33.44 C ANISOU 3082 C SER A1194 4276 5029 3400 156 468 -7 C ATOM 3083 O SER A1194 54.086 10.004 8.434 1.00 33.85 O ANISOU 3083 O SER A1194 4351 5058 3451 199 440 -53 O ATOM 3084 CB SER A1194 52.418 9.660 5.585 1.00 28.79 C ANISOU 3084 CB SER A1194 3583 4638 2718 287 483 -202 C ATOM 3085 OG SER A1194 51.586 9.154 6.613 1.00 43.12 O ANISOU 3085 OG SER A1194 5315 6552 4515 319 555 -345 O ATOM 3086 N PHE A1195 55.197 8.924 6.797 1.00 36.01 N ANISOU 3086 N PHE A1195 4545 5361 3776 39 575 82 N ATOM 3087 CA PHE A1195 56.022 8.134 7.707 1.00 27.28 C ANISOU 3087 CA PHE A1195 3417 4222 2725 -31 652 129 C ATOM 3088 C PHE A1195 56.902 9.026 8.583 1.00 33.24 C ANISOU 3088 C PHE A1195 4272 4857 3499 -38 541 211 C ATOM 3089 O PHE A1195 56.977 8.844 9.807 1.00 39.49 O ANISOU 3089 O PHE A1195 5084 5613 4307 -22 548 194 O ATOM 3090 CB PHE A1195 56.884 7.154 6.913 1.00 24.62 C ANISOU 3090 CB PHE A1195 3004 3920 2429 -125 751 191 C ATOM 3091 CG PHE A1195 57.425 6.024 7.730 1.00 34.56 C ANISOU 3091 CG PHE A1195 4242 5164 3727 -160 838 193 C ATOM 3092 CD1 PHE A1195 56.631 4.926 8.024 1.00 37.65 C ANISOU 3092 CD1 PHE A1195 4604 5605 4097 -161 950 107 C ATOM 3093 CD2 PHE A1195 58.729 6.050 8.195 1.00 40.88 C ANISOU 3093 CD2 PHE A1195 5065 5900 4569 -195 800 272 C ATOM 3094 CE1 PHE A1195 57.127 3.875 8.775 1.00 44.05 C ANISOU 3094 CE1 PHE A1195 5445 6370 4922 -192 1010 114 C ATOM 3095 CE2 PHE A1195 59.233 5.004 8.947 1.00 43.78 C ANISOU 3095 CE2 PHE A1195 5436 6240 4960 -198 854 265 C ATOM 3096 CZ PHE A1195 58.430 3.914 9.238 1.00 43.87 C ANISOU 3096 CZ PHE A1195 5455 6269 4944 -194 953 193 C ATOM 3097 N SER A1196 57.561 9.994 7.950 1.00 31.88 N ANISOU 3097 N SER A1196 4175 4623 3315 -77 440 298 N ATOM 3098 CA SER A1196 58.385 10.960 8.675 1.00 35.98 C ANISOU 3098 CA SER A1196 4801 5030 3838 -102 328 373 C ATOM 3099 C SER A1196 57.559 11.733 9.701 1.00 36.62 C ANISOU 3099 C SER A1196 4965 5055 3893 17 228 305 C ATOM 3100 O SER A1196 57.984 11.936 10.851 1.00 47.88 O ANISOU 3100 O SER A1196 6427 6422 5344 22 197 321 O ATOM 3101 CB SER A1196 59.045 11.925 7.696 1.00 37.78 C ANISOU 3101 CB SER A1196 5126 5205 4023 -192 236 464 C ATOM 3102 OG SER A1196 59.766 11.209 6.711 1.00 50.97 O ANISOU 3102 OG SER A1196 6698 6961 5708 -308 333 505 O ATOM 3103 N LYS A 294 56.375 12.157 9.268 1.00 31.87 N ANISOU 3103 N LYS A 294 4387 4486 3236 125 172 213 N ATOM 3104 CA LYS A 294 55.415 12.818 10.143 1.00 32.19 C ANISOU 3104 CA LYS A 294 4474 4518 3239 266 75 101 C ATOM 3105 C LYS A 294 55.158 11.974 11.393 1.00 35.83 C ANISOU 3105 C LYS A 294 4843 5044 3729 266 182 31 C ATOM 3106 O LYS A 294 55.220 12.471 12.529 1.00 37.91 O ANISOU 3106 O LYS A 294 5157 5252 3993 305 116 16 O ATOM 3107 CB LYS A 294 54.105 13.070 9.394 1.00 30.21 C ANISOU 3107 CB LYS A 294 4207 4351 2920 395 25 -32 C ATOM 3108 CG LYS A 294 53.319 14.265 9.893 1.00 45.56 C ANISOU 3108 CG LYS A 294 6256 6252 4801 567 -162 -137 C ATOM 3109 CD LYS A 294 54.050 15.555 9.566 1.00 69.55 C ANISOU 3109 CD LYS A 294 9518 9099 7810 560 -347 -14 C ATOM 3110 CE LYS A 294 53.319 16.767 10.116 1.00 75.73 C ANISOU 3110 CE LYS A 294 10436 9812 8526 751 -559 -121 C ATOM 3111 NZ LYS A 294 54.023 18.031 9.766 1.00 76.50 N ANISOU 3111 NZ LYS A 294 10799 9695 8575 725 -750 5 N ATOM 3112 N GLN A 295 54.886 10.690 11.169 1.00 31.68 N ANISOU 3112 N GLN A 295 4197 4625 3215 210 345 -10 N ATOM 3113 CA GLN A 295 54.618 9.755 12.258 1.00 30.32 C ANISOU 3113 CA GLN A 295 3972 4504 3043 177 458 -73 C ATOM 3114 C GLN A 295 55.802 9.657 13.216 1.00 35.85 C ANISOU 3114 C GLN A 295 4734 5092 3796 118 449 37 C ATOM 3115 O GLN A 295 55.622 9.615 14.440 1.00 48.51 O ANISOU 3115 O GLN A 295 6363 6684 5385 131 450 -6 O ATOM 3116 CB GLN A 295 54.280 8.371 11.704 1.00 39.82 C ANISOU 3116 CB GLN A 295 5080 5810 4240 101 626 -114 C ATOM 3117 CG GLN A 295 53.976 7.335 12.776 1.00 58.28 C ANISOU 3117 CG GLN A 295 7410 8185 6550 35 744 -175 C ATOM 3118 CD GLN A 295 53.828 5.934 12.212 1.00 72.94 C ANISOU 3118 CD GLN A 295 9218 10103 8395 -58 899 -192 C ATOM 3119 OE1 GLN A 295 54.068 5.701 11.027 1.00 80.52 O ANISOU 3119 OE1 GLN A 295 10129 11081 9384 -67 923 -151 O ATOM 3120 NE2 GLN A 295 53.433 4.992 13.062 1.00 70.46 N ANISOU 3120 NE2 GLN A 295 8931 9814 8026 -140 1003 -254 N ATOM 3121 N ILE A 296 57.011 9.623 12.659 1.00 27.71 N ANISOU 3121 N ILE A 296 3718 3996 2816 54 440 163 N ATOM 3122 CA ILE A 296 58.214 9.582 13.488 1.00 30.79 C ANISOU 3122 CA ILE A 296 4149 4299 3250 11 418 249 C ATOM 3123 C ILE A 296 58.297 10.807 14.401 1.00 41.24 C ANISOU 3123 C ILE A 296 5564 5539 4566 63 284 259 C ATOM 3124 O ILE A 296 58.546 10.683 15.610 1.00 47.43 O ANISOU 3124 O ILE A 296 6377 6284 5361 72 280 256 O ATOM 3125 CB ILE A 296 59.487 9.500 12.634 1.00 36.57 C ANISOU 3125 CB ILE A 296 4857 5018 4022 -68 418 350 C ATOM 3126 CG1 ILE A 296 59.463 8.239 11.769 1.00 44.87 C ANISOU 3126 CG1 ILE A 296 5814 6150 5082 -107 543 332 C ATOM 3127 CG2 ILE A 296 60.725 9.514 13.520 1.00 33.87 C ANISOU 3127 CG2 ILE A 296 4539 4614 3717 -97 384 409 C ATOM 3128 CD1 ILE A 296 60.622 8.143 10.800 1.00 41.53 C ANISOU 3128 CD1 ILE A 296 5338 5756 4686 -184 547 401 C ATOM 3129 N ARG A 297 58.073 11.985 13.826 1.00 26.03 N ANISOU 3129 N ARG A 297 3701 3577 2613 100 166 269 N ATOM 3130 CA ARG A 297 58.099 13.216 14.613 1.00 33.48 C ANISOU 3130 CA ARG A 297 4754 4426 3541 158 20 273 C ATOM 3131 C ARG A 297 57.051 13.203 15.736 1.00 43.60 C ANISOU 3131 C ARG A 297 6020 5753 4795 259 15 146 C ATOM 3132 O ARG A 297 57.339 13.592 16.881 1.00 47.54 O ANISOU 3132 O ARG A 297 6565 6193 5304 278 -38 151 O ATOM 3133 CB ARG A 297 57.895 14.426 13.698 1.00 41.87 C ANISOU 3133 CB ARG A 297 5929 5425 4555 189 -121 293 C ATOM 3134 CG ARG A 297 59.120 14.764 12.850 1.00 40.16 C ANISOU 3134 CG ARG A 297 5769 5147 4342 48 -143 427 C ATOM 3135 CD ARG A 297 58.806 15.827 11.807 1.00 48.24 C ANISOU 3135 CD ARG A 297 6940 6099 5291 58 -275 449 C ATOM 3136 NE ARG A 297 58.560 15.246 10.490 1.00 58.76 N ANISOU 3136 NE ARG A 297 8206 7514 6605 19 -197 450 N ATOM 3137 CZ ARG A 297 57.752 15.775 9.576 1.00 56.96 C ANISOU 3137 CZ ARG A 297 8065 7269 6308 91 -283 413 C ATOM 3138 NH1 ARG A 297 57.097 16.899 9.836 1.00 57.88 N ANISOU 3138 NH1 ARG A 297 8345 7285 6361 222 -462 364 N ATOM 3139 NH2 ARG A 297 57.592 15.176 8.404 1.00 61.37 N ANISOU 3139 NH2 ARG A 297 8551 7912 6855 48 -200 416 N ATOM 3140 N ALA A 298 55.845 12.740 15.411 1.00 36.01 N ANISOU 3140 N ALA A 298 4981 4912 3790 311 76 20 N ATOM 3141 CA ALA A 298 54.779 12.623 16.409 1.00 39.46 C ANISOU 3141 CA ALA A 298 5373 5443 4178 378 94 -133 C ATOM 3142 C ALA A 298 55.180 11.714 17.576 1.00 43.73 C ANISOU 3142 C ALA A 298 5901 5981 4734 293 202 -113 C ATOM 3143 O ALA A 298 55.028 12.078 18.762 1.00 38.39 O ANISOU 3143 O ALA A 298 5254 5294 4039 325 158 -160 O ATOM 3144 CB ALA A 298 53.507 12.108 15.758 1.00 32.66 C ANISOU 3144 CB ALA A 298 4405 4747 3256 413 170 -284 C ATOM 3145 N ARG A 299 55.688 10.533 17.231 1.00 31.82 N ANISOU 3145 N ARG A 299 4362 4477 3251 191 332 -48 N ATOM 3146 CA ARG A 299 56.162 9.581 18.229 1.00 25.80 C ANISOU 3146 CA ARG A 299 3630 3682 2491 117 418 -19 C ATOM 3147 C ARG A 299 57.238 10.207 19.107 1.00 28.10 C ANISOU 3147 C ARG A 299 3999 3849 2829 134 319 75 C ATOM 3148 O ARG A 299 57.286 9.958 20.315 1.00 35.28 O ANISOU 3148 O ARG A 299 4953 4734 3717 121 332 58 O ATOM 3149 CB ARG A 299 56.690 8.314 17.554 1.00 25.37 C ANISOU 3149 CB ARG A 299 3557 3624 2458 35 533 41 C ATOM 3150 CG ARG A 299 55.606 7.292 17.255 1.00 25.52 C ANISOU 3150 CG ARG A 299 3529 3759 2408 -23 669 -66 C ATOM 3151 CD ARG A 299 56.003 6.343 16.136 1.00 37.96 C ANISOU 3151 CD ARG A 299 5072 5339 4011 -73 751 -15 C ATOM 3152 NE ARG A 299 55.739 4.952 16.490 1.00 58.04 N ANISOU 3152 NE ARG A 299 7664 7892 6498 -165 878 -50 N ATOM 3153 CZ ARG A 299 54.535 4.387 16.472 1.00 81.71 C ANISOU 3153 CZ ARG A 299 10634 11005 9406 -234 985 -173 C ATOM 3154 NH1 ARG A 299 53.468 5.093 16.118 1.00 84.37 N ANISOU 3154 NH1 ARG A 299 10868 11479 9708 -194 975 -289 N ATOM 3155 NH2 ARG A 299 54.395 3.113 16.815 1.00 87.90 N ANISOU 3155 NH2 ARG A 299 11506 11770 10124 -346 1094 -191 N ATOM 3156 N ARG A 300 58.088 11.033 18.503 1.00 25.70 N ANISOU 3156 N ARG A 300 3716 3473 2577 148 223 169 N ATOM 3157 CA ARG A 300 59.087 11.769 19.271 1.00 25.80 C ANISOU 3157 CA ARG A 300 3795 3382 2625 154 124 245 C ATOM 3158 C ARG A 300 58.446 12.716 20.286 1.00 35.72 C ANISOU 3158 C ARG A 300 5100 4622 3851 232 28 175 C ATOM 3159 O ARG A 300 58.878 12.777 21.442 1.00 37.05 O ANISOU 3159 O ARG A 300 5308 4740 4027 235 4 190 O ATOM 3160 CB ARG A 300 60.008 12.551 18.340 1.00 25.95 C ANISOU 3160 CB ARG A 300 3834 3348 2677 117 45 341 C ATOM 3161 CG ARG A 300 61.013 11.680 17.621 1.00 38.20 C ANISOU 3161 CG ARG A 300 5326 4925 4265 36 124 407 C ATOM 3162 CD ARG A 300 61.782 12.477 16.594 1.00 46.83 C ANISOU 3162 CD ARG A 300 6431 6001 5363 -36 61 480 C ATOM 3163 NE ARG A 300 62.747 11.651 15.878 1.00 48.61 N ANISOU 3163 NE ARG A 300 6569 6288 5615 -113 136 516 N ATOM 3164 CZ ARG A 300 63.470 12.078 14.850 1.00 53.80 C ANISOU 3164 CZ ARG A 300 7208 6973 6262 -212 117 566 C ATOM 3165 NH1 ARG A 300 63.331 13.324 14.415 1.00 55.36 N ANISOU 3165 NH1 ARG A 300 7504 7113 6418 -254 20 603 N ATOM 3166 NH2 ARG A 300 64.327 11.261 14.255 1.00 62.42 N ANISOU 3166 NH2 ARG A 300 8194 8150 7373 -272 187 570 N ATOM 3167 N LYS A 301 57.418 13.450 19.859 1.00 26.72 N ANISOU 3167 N LYS A 301 3956 3526 2669 310 -37 87 N ATOM 3168 CA LYS A 301 56.717 14.358 20.771 1.00 34.77 C ANISOU 3168 CA LYS A 301 5010 4551 3651 410 -143 -12 C ATOM 3169 C LYS A 301 56.117 13.623 21.974 1.00 38.61 C ANISOU 3169 C LYS A 301 5449 5126 4094 393 -50 -111 C ATOM 3170 O LYS A 301 56.363 13.997 23.133 1.00 47.07 O ANISOU 3170 O LYS A 301 6564 6154 5167 411 -102 -114 O ATOM 3171 CB LYS A 301 55.613 15.120 20.037 1.00 28.06 C ANISOU 3171 CB LYS A 301 4155 3759 2748 525 -236 -127 C ATOM 3172 CG LYS A 301 56.117 16.101 18.999 1.00 31.28 C ANISOU 3172 CG LYS A 301 4670 4048 3168 546 -368 -34 C ATOM 3173 CD LYS A 301 54.958 16.804 18.311 1.00 44.19 C ANISOU 3173 CD LYS A 301 6324 5730 4735 691 -481 -164 C ATOM 3174 CE LYS A 301 55.407 17.474 17.024 1.00 53.28 C ANISOU 3174 CE LYS A 301 7600 6767 5876 676 -579 -61 C ATOM 3175 NZ LYS A 301 55.934 16.475 16.052 1.00 59.27 N ANISOU 3175 NZ LYS A 301 8282 7568 6670 537 -426 34 N ATOM 3176 N THR A 302 55.334 12.579 21.701 1.00 29.01 N ANISOU 3176 N THR A 302 4156 4037 2831 341 88 -195 N ATOM 3177 CA THR A 302 54.702 11.825 22.786 1.00 31.13 C ANISOU 3177 CA THR A 302 4401 4398 3027 280 191 -297 C ATOM 3178 C THR A 302 55.729 11.185 23.712 1.00 31.34 C ANISOU 3178 C THR A 302 4516 4314 3079 199 231 -182 C ATOM 3179 O THR A 302 55.586 11.213 24.942 1.00 31.76 O ANISOU 3179 O THR A 302 4605 4373 3089 185 228 -226 O ATOM 3180 CB THR A 302 53.772 10.722 22.257 1.00 33.18 C ANISOU 3180 CB THR A 302 4585 4806 3216 196 346 -398 C ATOM 3181 OG1 THR A 302 54.393 10.063 21.147 1.00 67.10 O ANISOU 3181 OG1 THR A 302 8884 9045 7567 149 404 -284 O ATOM 3182 CG2 THR A 302 52.452 11.317 21.813 1.00 32.31 C ANISOU 3182 CG2 THR A 302 4367 4867 3042 286 310 -587 C ATOM 3183 N ALA A 303 56.772 10.615 23.122 1.00 26.58 N ANISOU 3183 N ALA A 303 3944 3616 2539 157 260 -47 N ATOM 3184 CA ALA A 303 57.799 9.969 23.923 1.00 29.99 C ANISOU 3184 CA ALA A 303 4460 3945 2989 112 278 45 C ATOM 3185 C ALA A 303 58.519 10.990 24.824 1.00 30.44 C ANISOU 3185 C ALA A 303 4563 3914 3088 173 151 92 C ATOM 3186 O ALA A 303 58.785 10.704 25.995 1.00 30.25 O ANISOU 3186 O ALA A 303 4608 3849 3038 157 153 97 O ATOM 3187 CB ALA A 303 58.781 9.227 23.026 1.00 25.95 C ANISOU 3187 CB ALA A 303 3949 3377 2533 83 314 147 C ATOM 3188 N ARG A 304 58.801 12.184 24.299 1.00 26.45 N ANISOU 3188 N ARG A 304 4040 3377 2635 235 36 124 N ATOM 3189 CA ARG A 304 59.394 13.254 25.111 1.00 26.66 C ANISOU 3189 CA ARG A 304 4117 3321 2691 285 -91 159 C ATOM 3190 C ARG A 304 58.481 13.661 26.272 1.00 30.20 C ANISOU 3190 C ARG A 304 4576 3818 3082 332 -121 46 C ATOM 3191 O ARG A 304 58.944 13.826 27.410 1.00 44.99 O ANISOU 3191 O ARG A 304 6498 5639 4957 337 -158 64 O ATOM 3192 CB ARG A 304 59.715 14.480 24.249 1.00 34.64 C ANISOU 3192 CB ARG A 304 5144 4279 3740 319 -212 205 C ATOM 3193 CG ARG A 304 60.376 15.629 25.008 1.00 39.00 C ANISOU 3193 CG ARG A 304 5768 4735 4316 351 -347 245 C ATOM 3194 CD ARG A 304 60.931 16.669 24.049 1.00 56.20 C ANISOU 3194 CD ARG A 304 8002 6837 6513 331 -453 317 C ATOM 3195 NE ARG A 304 59.890 17.217 23.185 1.00 74.09 N ANISOU 3195 NE ARG A 304 10289 9125 8737 395 -508 253 N ATOM 3196 CZ ARG A 304 59.335 18.412 23.350 1.00 83.02 C ANISOU 3196 CZ ARG A 304 11508 10201 9833 491 -659 197 C ATOM 3197 NH1 ARG A 304 59.727 19.196 24.345 1.00 85.93 N ANISOU 3197 NH1 ARG A 304 11949 10491 10210 519 -760 206 N ATOM 3198 NH2 ARG A 304 58.392 18.827 22.514 1.00 85.31 N ANISOU 3198 NH2 ARG A 304 11822 10515 10077 573 -721 124 N ATOM 3199 N MET A 305 57.191 13.824 25.983 1.00 22.69 N ANISOU 3199 N MET A 305 3536 2339 2747 -161 569 44 N ATOM 3200 CA MET A 305 56.215 14.123 27.032 1.00 21.72 C ANISOU 3200 CA MET A 305 3311 2224 2716 -139 409 -46 C ATOM 3201 C MET A 305 56.268 13.084 28.151 1.00 32.81 C ANISOU 3201 C MET A 305 4549 3718 4198 -94 470 -92 C ATOM 3202 O MET A 305 56.390 13.424 29.335 1.00 30.24 O ANISOU 3202 O MET A 305 4083 3437 3969 -104 430 -108 O ATOM 3203 CB MET A 305 54.803 14.185 26.451 1.00 33.85 C ANISOU 3203 CB MET A 305 4970 3686 4204 -106 253 -119 C ATOM 3204 CG MET A 305 53.730 14.495 27.483 1.00 35.59 C ANISOU 3204 CG MET A 305 5085 3899 4537 -72 109 -204 C ATOM 3205 SD MET A 305 52.061 14.482 26.802 1.00 46.11 S ANISOU 3205 SD MET A 305 6520 5153 5845 -30 -77 -271 S ATOM 3206 CE MET A 305 51.899 12.758 26.352 1.00 37.91 C ANISOU 3206 CE MET A 305 5516 4157 4729 -5 15 -322 C ATOM 3207 N LEU A 306 56.190 11.815 27.763 1.00 34.08 N ANISOU 3207 N LEU A 306 4744 3899 4306 -48 573 -113 N ATOM 3208 CA LEU A 306 56.222 10.712 28.721 1.00 36.09 C ANISOU 3208 CA LEU A 306 4859 4228 4624 5 651 -150 C ATOM 3209 C LEU A 306 57.497 10.702 29.562 1.00 33.81 C ANISOU 3209 C LEU A 306 4405 4030 4410 -10 757 -65 C ATOM 3210 O LEU A 306 57.450 10.470 30.775 1.00 35.53 O ANISOU 3210 O LEU A 306 4479 4310 4708 12 735 -94 O ATOM 3211 CB LEU A 306 56.071 9.380 27.988 1.00 35.88 C ANISOU 3211 CB LEU A 306 4927 4190 4517 47 773 -173 C ATOM 3212 CG LEU A 306 54.739 9.236 27.255 1.00 30.97 C ANISOU 3212 CG LEU A 306 4453 3491 3825 51 645 -265 C ATOM 3213 CD1 LEU A 306 54.729 7.991 26.382 1.00 26.72 C ANISOU 3213 CD1 LEU A 306 4048 2926 3179 67 775 -284 C ATOM 3214 CD2 LEU A 306 53.588 9.224 28.252 1.00 19.18 C ANISOU 3214 CD2 LEU A 306 2849 2003 2435 83 507 -363 C ATOM 3215 N MET A 307 58.634 10.954 28.918 1.00 34.95 N ANISOU 3215 N MET A 307 4568 4181 4529 -49 872 46 N ATOM 3216 CA MET A 307 59.904 11.018 29.634 1.00 32.56 C ANISOU 3216 CA MET A 307 4091 3967 4312 -75 958 146 C ATOM 3217 C MET A 307 59.890 12.137 30.665 1.00 23.96 C ANISOU 3217 C MET A 307 2904 2901 3299 -139 802 131 C ATOM 3218 O MET A 307 60.386 11.970 31.781 1.00 26.84 O ANISOU 3218 O MET A 307 3107 3353 3739 -146 798 154 O ATOM 3219 CB MET A 307 61.068 11.218 28.665 1.00 28.33 C ANISOU 3219 CB MET A 307 3596 3417 3753 -112 1110 274 C ATOM 3220 CG MET A 307 61.342 10.026 27.777 1.00 28.55 C ANISOU 3220 CG MET A 307 3712 3424 3712 -48 1314 307 C ATOM 3221 SD MET A 307 62.600 10.388 26.546 1.00 40.17 S ANISOU 3221 SD MET A 307 5265 4848 5149 -90 1509 454 S ATOM 3222 CE MET A 307 62.427 8.960 25.478 1.00 41.40 C ANISOU 3222 CE MET A 307 5610 4939 5180 -8 1720 437 C ATOM 3223 N VAL A 308 59.316 13.275 30.287 1.00 22.80 N ANISOU 3223 N VAL A 308 2869 2670 3126 -187 673 94 N ATOM 3224 CA VAL A 308 59.217 14.402 31.206 1.00 28.78 C ANISOU 3224 CA VAL A 308 3569 3421 3944 -252 535 69 C ATOM 3225 C VAL A 308 58.334 14.052 32.405 1.00 25.30 C ANISOU 3225 C VAL A 308 3062 3004 3548 -204 449 -36 C ATOM 3226 O VAL A 308 58.665 14.385 33.548 1.00 28.66 O ANISOU 3226 O VAL A 308 3383 3478 4028 -244 401 -39 O ATOM 3227 CB VAL A 308 58.670 15.657 30.499 1.00 28.68 C ANISOU 3227 CB VAL A 308 3707 3293 3896 -295 430 52 C ATOM 3228 CG1 VAL A 308 58.280 16.724 31.514 1.00 25.92 C ANISOU 3228 CG1 VAL A 308 3328 2913 3609 -344 293 -3 C ATOM 3229 CG2 VAL A 308 59.707 16.199 29.529 1.00 22.40 C ANISOU 3229 CG2 VAL A 308 2968 2474 3071 -362 520 165 C ATOM 3230 N VAL A 309 57.227 13.361 32.148 1.00 23.82 N ANISOU 3230 N VAL A 309 2938 2779 3332 -123 433 -119 N ATOM 3231 CA VAL A 309 56.354 12.930 33.237 1.00 23.16 C ANISOU 3231 CA VAL A 309 2792 2710 3299 -69 379 -215 C ATOM 3232 C VAL A 309 57.111 12.004 34.184 1.00 21.01 C ANISOU 3232 C VAL A 309 2376 2549 3059 -47 474 -182 C ATOM 3233 O VAL A 309 57.035 12.153 35.405 1.00 24.60 O ANISOU 3233 O VAL A 309 2754 3037 3558 -53 423 -215 O ATOM 3234 CB VAL A 309 55.092 12.220 32.717 1.00 26.09 C ANISOU 3234 CB VAL A 309 3240 3026 3648 6 358 -300 C ATOM 3235 CG1 VAL A 309 54.275 11.672 33.877 1.00 16.82 C ANISOU 3235 CG1 VAL A 309 1986 1866 2540 64 336 -390 C ATOM 3236 CG2 VAL A 309 54.253 13.176 31.889 1.00 31.02 C ANISOU 3236 CG2 VAL A 309 3991 3545 4250 -10 235 -325 C ATOM 3237 N LEU A 310 57.857 11.063 33.612 1.00 37.08 N ANISOU 3237 N LEU A 310 4385 4635 5067 -18 617 -109 N ATOM 3238 CA LEU A 310 58.667 10.142 34.402 1.00 29.10 C ANISOU 3238 CA LEU A 310 3231 3731 4094 16 720 -50 C ATOM 3239 C LEU A 310 59.669 10.883 35.283 1.00 35.52 C ANISOU 3239 C LEU A 310 3922 4618 4957 -64 667 25 C ATOM 3240 O LEU A 310 59.828 10.568 36.466 1.00 33.37 O ANISOU 3240 O LEU A 310 3545 4417 4718 -53 643 23 O ATOM 3241 CB LEU A 310 59.406 9.167 33.489 1.00 24.12 C ANISOU 3241 CB LEU A 310 2605 3123 3435 58 903 36 C ATOM 3242 CG LEU A 310 60.274 8.143 34.218 1.00 24.84 C ANISOU 3242 CG LEU A 310 2540 3320 3577 111 1028 118 C ATOM 3243 CD1 LEU A 310 59.422 7.336 35.182 1.00 19.17 C ANISOU 3243 CD1 LEU A 310 1793 2618 2874 186 1009 26 C ATOM 3244 CD2 LEU A 310 60.984 7.233 33.230 1.00 27.12 C ANISOU 3244 CD2 LEU A 310 2851 3607 3845 161 1237 207 C ATOM 3245 N LEU A 311 60.341 11.871 34.698 1.00 26.17 N ANISOU 3245 N LEU A 311 2759 3412 3772 -153 645 92 N ATOM 3246 CA LEU A 311 61.320 12.674 35.424 1.00 27.45 C ANISOU 3246 CA LEU A 311 2811 3635 3983 -256 582 165 C ATOM 3247 C LEU A 311 60.683 13.439 36.581 1.00 34.03 C ANISOU 3247 C LEU A 311 3662 4446 4822 -302 424 69 C ATOM 3248 O LEU A 311 61.233 13.486 37.686 1.00 28.91 O ANISOU 3248 O LEU A 311 2909 3877 4200 -349 373 95 O ATOM 3249 CB LEU A 311 62.013 13.653 34.477 1.00 31.10 C ANISOU 3249 CB LEU A 311 3317 4052 4446 -348 594 242 C ATOM 3250 CG LEU A 311 62.902 14.704 35.144 1.00 30.39 C ANISOU 3250 CG LEU A 311 3137 4001 4410 -484 505 301 C ATOM 3251 CD1 LEU A 311 64.061 14.044 35.870 1.00 29.87 C ANISOU 3251 CD1 LEU A 311 2863 4075 4410 -497 552 414 C ATOM 3252 CD2 LEU A 311 63.405 15.708 34.120 1.00 35.31 C ANISOU 3252 CD2 LEU A 311 3830 4552 5034 -570 526 363 C ATOM 3253 N VAL A 312 59.524 14.038 36.321 1.00 25.28 N ANISOU 3253 N VAL A 312 2693 3225 3688 -289 349 -37 N ATOM 3254 CA VAL A 312 58.827 14.821 37.335 1.00 25.29 C ANISOU 3254 CA VAL A 312 2737 3175 3698 -323 226 -132 C ATOM 3255 C VAL A 312 58.338 13.920 38.467 1.00 30.66 C ANISOU 3255 C VAL A 312 3362 3904 4385 -248 234 -193 C ATOM 3256 O VAL A 312 58.338 14.312 39.633 1.00 29.74 O ANISOU 3256 O VAL A 312 3234 3799 4269 -293 163 -229 O ATOM 3257 CB VAL A 312 57.645 15.593 36.726 1.00 18.86 C ANISOU 3257 CB VAL A 312 2071 2221 2874 -303 162 -215 C ATOM 3258 CG1 VAL A 312 56.815 16.261 37.811 1.00 25.45 C ANISOU 3258 CG1 VAL A 312 2952 2987 3730 -312 71 -315 C ATOM 3259 CG2 VAL A 312 58.156 16.623 35.738 1.00 19.74 C ANISOU 3259 CG2 VAL A 312 2252 2275 2972 -384 147 -150 C ATOM 3260 N PHE A 313 57.936 12.705 38.114 1.00 32.51 N ANISOU 3260 N PHE A 313 3578 4158 4615 -140 328 -205 N ATOM 3261 CA PHE A 313 57.532 11.709 39.098 1.00 29.58 C ANISOU 3261 CA PHE A 313 3153 3833 4253 -61 364 -250 C ATOM 3262 C PHE A 313 58.712 11.323 39.992 1.00 30.92 C ANISOU 3262 C PHE A 313 3191 4131 4426 -92 381 -157 C ATOM 3263 O PHE A 313 58.612 11.346 41.225 1.00 29.88 O ANISOU 3263 O PHE A 313 3041 4028 4286 -101 328 -191 O ATOM 3264 CB PHE A 313 56.963 10.474 38.392 1.00 20.92 C ANISOU 3264 CB PHE A 313 2070 2726 3153 48 474 -273 C ATOM 3265 CG PHE A 313 56.536 9.380 39.325 1.00 26.89 C ANISOU 3265 CG PHE A 313 2776 3519 3924 135 533 -316 C ATOM 3266 CD1 PHE A 313 57.430 8.394 39.717 1.00 35.97 C ANISOU 3266 CD1 PHE A 313 3819 4774 5073 173 631 -229 C ATOM 3267 CD2 PHE A 313 55.238 9.330 39.803 1.00 29.59 C ANISOU 3267 CD2 PHE A 313 3172 3782 4288 184 500 -435 C ATOM 3268 CE1 PHE A 313 57.039 7.386 40.576 1.00 32.87 C ANISOU 3268 CE1 PHE A 313 3392 4409 4691 257 693 -263 C ATOM 3269 CE2 PHE A 313 54.839 8.321 40.658 1.00 36.78 C ANISOU 3269 CE2 PHE A 313 4044 4717 5214 263 570 -472 C ATOM 3270 CZ PHE A 313 55.740 7.351 41.047 1.00 37.01 C ANISOU 3270 CZ PHE A 313 3983 4850 5229 299 665 -388 C ATOM 3271 N ALA A 314 59.826 10.968 39.355 1.00 24.69 N ANISOU 3271 N ALA A 314 2315 3417 3650 -105 459 -33 N ATOM 3272 CA ALA A 314 61.042 10.578 40.060 1.00 25.75 C ANISOU 3272 CA ALA A 314 2294 3681 3807 -131 475 87 C ATOM 3273 C ALA A 314 61.486 11.663 41.032 1.00 20.36 C ANISOU 3273 C ALA A 314 1591 3026 3118 -261 321 91 C ATOM 3274 O ALA A 314 61.799 11.386 42.198 1.00 34.19 O ANISOU 3274 O ALA A 314 3274 4857 4859 -272 270 111 O ATOM 3275 CB ALA A 314 62.153 10.271 39.063 1.00 19.79 C ANISOU 3275 CB ALA A 314 1452 2977 3089 -135 590 228 C ATOM 3276 N ILE A 315 61.502 12.900 40.546 1.00 20.19 N ANISOU 3276 N ILE A 315 1646 2931 3096 -364 248 71 N ATOM 3277 CA ILE A 315 61.862 14.040 41.376 1.00 27.84 C ANISOU 3277 CA ILE A 315 2629 3898 4052 -506 104 59 C ATOM 3278 C ILE A 315 60.889 14.207 42.541 1.00 25.20 C ANISOU 3278 C ILE A 315 2396 3510 3668 -491 29 -71 C ATOM 3279 O ILE A 315 61.305 14.351 43.688 1.00 24.68 O ANISOU 3279 O ILE A 315 2302 3504 3572 -560 -57 -63 O ATOM 3280 CB ILE A 315 61.904 15.338 40.553 1.00 28.02 C ANISOU 3280 CB ILE A 315 2742 3821 4083 -608 62 50 C ATOM 3281 CG1 ILE A 315 63.077 15.298 39.571 1.00 29.46 C ANISOU 3281 CG1 ILE A 315 2817 4060 4316 -650 138 194 C ATOM 3282 CG2 ILE A 315 62.015 16.548 41.469 1.00 22.41 C ANISOU 3282 CG2 ILE A 315 2093 3073 3349 -753 -81 2 C ATOM 3283 CD1 ILE A 315 63.124 16.478 38.622 1.00 29.86 C ANISOU 3283 CD1 ILE A 315 2968 4006 4372 -735 123 195 C ATOM 3284 N CYS A 316 59.595 14.169 42.244 1.00 24.34 N ANISOU 3284 N CYS A 316 2406 3288 3553 -402 63 -184 N ATOM 3285 CA CYS A 316 58.568 14.375 43.261 1.00 29.97 C ANISOU 3285 CA CYS A 316 3225 3926 4238 -376 20 -308 C ATOM 3286 C CYS A 316 58.573 13.311 44.356 1.00 30.37 C ANISOU 3286 C CYS A 316 3217 4060 4261 -308 51 -308 C ATOM 3287 O CYS A 316 58.158 13.584 45.483 1.00 30.90 O ANISOU 3287 O CYS A 316 3362 4093 4284 -328 2 -381 O ATOM 3288 CB CYS A 316 57.182 14.428 42.613 1.00 34.94 C ANISOU 3288 CB CYS A 316 3957 4424 4896 -281 62 -408 C ATOM 3289 SG CYS A 316 56.746 16.035 41.918 1.00 38.60 S ANISOU 3289 SG CYS A 316 4553 4738 5375 -359 -12 -451 S ATOM 3290 N TYR A 317 59.035 12.105 44.035 1.00 33.95 N ANISOU 3290 N TYR A 317 3551 4613 4735 -225 143 -225 N ATOM 3291 CA TYR A 317 59.009 11.023 45.018 1.00 25.76 C ANISOU 3291 CA TYR A 317 2463 3649 3675 -145 187 -216 C ATOM 3292 C TYR A 317 60.370 10.719 45.645 1.00 29.09 C ANISOU 3292 C TYR A 317 2748 4224 4082 -200 143 -79 C ATOM 3293 O TYR A 317 60.452 9.938 46.595 1.00 26.13 O ANISOU 3293 O TYR A 317 2337 3916 3675 -146 156 -57 O ATOM 3294 CB TYR A 317 58.434 9.751 44.391 1.00 24.54 C ANISOU 3294 CB TYR A 317 2281 3487 3557 4 335 -226 C ATOM 3295 CG TYR A 317 56.923 9.717 44.408 1.00 26.06 C ANISOU 3295 CG TYR A 317 2590 3550 3762 77 366 -369 C ATOM 3296 CD1 TYR A 317 56.184 10.283 43.376 1.00 32.16 C ANISOU 3296 CD1 TYR A 317 3436 4218 4568 75 356 -430 C ATOM 3297 CD2 TYR A 317 56.235 9.135 45.466 1.00 20.31 C ANISOU 3297 CD2 TYR A 317 1895 2804 3019 148 403 -436 C ATOM 3298 CE1 TYR A 317 54.801 10.264 43.394 1.00 38.82 C ANISOU 3298 CE1 TYR A 317 4359 4947 5445 141 374 -546 C ATOM 3299 CE2 TYR A 317 54.852 9.110 45.491 1.00 26.18 C ANISOU 3299 CE2 TYR A 317 2724 3425 3798 213 440 -558 C ATOM 3300 CZ TYR A 317 54.140 9.676 44.452 1.00 40.01 C ANISOU 3300 CZ TYR A 317 4524 5080 5598 209 421 -610 C ATOM 3301 OH TYR A 317 52.764 9.655 44.471 1.00 45.63 O ANISOU 3301 OH TYR A 317 5295 5675 6367 275 448 -717 O ATOM 3302 N LEU A 318 61.432 11.334 45.132 1.00 20.53 N ANISOU 3302 N LEU A 318 1582 3194 3027 -308 89 22 N ATOM 3303 CA LEU A 318 62.762 11.115 45.705 1.00 25.88 C ANISOU 3303 CA LEU A 318 2101 4022 3712 -372 29 168 C ATOM 3304 C LEU A 318 62.889 11.535 47.189 1.00 33.34 C ANISOU 3304 C LEU A 318 3092 5003 4573 -464 -123 141 C ATOM 3305 O LEU A 318 63.351 10.735 48.004 1.00 34.99 O ANISOU 3305 O LEU A 318 3214 5323 4760 -424 -137 218 O ATOM 3306 CB LEU A 318 63.832 11.830 44.868 1.00 27.45 C ANISOU 3306 CB LEU A 318 2201 4255 3973 -487 0 277 C ATOM 3307 CG LEU A 318 65.272 11.659 45.360 1.00 33.07 C ANISOU 3307 CG LEU A 318 2714 5127 4725 -564 -69 449 C ATOM 3308 CD1 LEU A 318 65.725 10.209 45.233 1.00 31.96 C ANISOU 3308 CD1 LEU A 318 2417 5088 4638 -414 70 574 C ATOM 3309 CD2 LEU A 318 66.220 12.590 44.621 1.00 32.00 C ANISOU 3309 CD2 LEU A 318 2499 5002 4660 -704 -109 536 C ATOM 3310 N PRO A 319 62.483 12.774 47.550 1.00 29.53 N ANISOU 3310 N PRO A 319 2759 4422 4037 -586 -234 33 N ATOM 3311 CA PRO A 319 62.672 13.189 48.949 1.00 27.99 C ANISOU 3311 CA PRO A 319 2635 4255 3743 -691 -377 6 C ATOM 3312 C PRO A 319 61.989 12.294 49.987 1.00 28.25 C ANISOU 3312 C PRO A 319 2737 4292 3703 -575 -335 -48 C ATOM 3313 O PRO A 319 62.635 11.904 50.960 1.00 34.26 O ANISOU 3313 O PRO A 319 3447 5165 4403 -606 -418 27 O ATOM 3314 CB PRO A 319 62.057 14.591 48.979 1.00 24.37 C ANISOU 3314 CB PRO A 319 2370 3643 3247 -805 -443 -128 C ATOM 3315 CG PRO A 319 62.202 15.083 47.596 1.00 24.00 C ANISOU 3315 CG PRO A 319 2278 3550 3291 -820 -393 -99 C ATOM 3316 CD PRO A 319 61.940 13.882 46.742 1.00 25.36 C ANISOU 3316 CD PRO A 319 2351 3756 3530 -644 -238 -55 C ATOM 3317 N ILE A 320 60.713 11.980 49.788 1.00 27.55 N ANISOU 3317 N ILE A 320 2760 4084 3625 -447 -212 -168 N ATOM 3318 CA ILE A 320 59.982 11.146 50.740 1.00 23.82 C ANISOU 3318 CA ILE A 320 2361 3595 3094 -334 -147 -225 C ATOM 3319 C ILE A 320 60.566 9.732 50.787 1.00 21.85 C ANISOU 3319 C ILE A 320 1948 3484 2871 -219 -72 -96 C ATOM 3320 O ILE A 320 60.532 9.071 51.827 1.00 31.40 O ANISOU 3320 O ILE A 320 3181 4738 4010 -169 -71 -81 O ATOM 3321 CB ILE A 320 58.469 11.086 50.402 1.00 29.54 C ANISOU 3321 CB ILE A 320 3210 4157 3856 -221 -20 -372 C ATOM 3322 CG1 ILE A 320 57.687 10.423 51.539 1.00 30.62 C ANISOU 3322 CG1 ILE A 320 3448 4255 3931 -128 47 -442 C ATOM 3323 CG2 ILE A 320 58.227 10.368 49.083 1.00 19.30 C ANISOU 3323 CG2 ILE A 320 1808 2859 2665 -109 105 -343 C ATOM 3324 CD1 ILE A 320 57.839 11.124 52.875 1.00 40.93 C ANISOU 3324 CD1 ILE A 320 4903 5544 5107 -239 -66 -483 C ATOM 3325 N SER A 321 61.121 9.285 49.664 1.00 21.52 N ANISOU 3325 N SER A 321 1751 3500 2926 -177 0 3 N ATOM 3326 CA SER A 321 61.756 7.977 49.588 1.00 29.32 C ANISOU 3326 CA SER A 321 2578 4608 3955 -64 93 139 C ATOM 3327 C SER A 321 63.003 7.944 50.453 1.00 37.47 C ANISOU 3327 C SER A 321 3492 5796 4951 -143 -42 287 C ATOM 3328 O SER A 321 63.148 7.080 51.317 1.00 43.67 O ANISOU 3328 O SER A 321 4248 6654 5693 -68 -30 346 O ATOM 3329 CB SER A 321 62.113 7.631 48.143 1.00 28.02 C ANISOU 3329 CB SER A 321 2297 4451 3896 -15 211 211 C ATOM 3330 OG SER A 321 60.965 7.651 47.319 1.00 33.08 O ANISOU 3330 OG SER A 321 3050 4955 4562 49 311 80 O ATOM 3331 N ILE A 322 63.900 8.897 50.214 1.00 38.60 N ANISOU 3331 N ILE A 322 3565 5988 5116 -300 -174 352 N ATOM 3332 CA ILE A 322 65.145 8.982 50.967 1.00 35.86 C ANISOU 3332 CA ILE A 322 3082 5794 4749 -404 -333 502 C ATOM 3333 C ILE A 322 64.872 9.172 52.455 1.00 48.46 C ANISOU 3333 C ILE A 322 4822 7395 6194 -461 -471 440 C ATOM 3334 O ILE A 322 65.536 8.566 53.296 1.00 55.82 O ANISOU 3334 O ILE A 322 5667 8457 7087 -449 -546 561 O ATOM 3335 CB ILE A 322 66.032 10.134 50.463 1.00 33.04 C ANISOU 3335 CB ILE A 322 2647 5463 4444 -590 -459 557 C ATOM 3336 CG1 ILE A 322 66.278 10.000 48.959 1.00 37.37 C ANISOU 3336 CG1 ILE A 322 3082 5989 5128 -534 -308 615 C ATOM 3337 CG2 ILE A 322 67.348 10.165 51.222 1.00 38.88 C ANISOU 3337 CG2 ILE A 322 3217 6373 5183 -704 -636 727 C ATOM 3338 CD1 ILE A 322 66.801 8.643 48.539 1.00 36.42 C ANISOU 3338 CD1 ILE A 322 2776 5963 5099 -372 -150 767 C ATOM 3339 N LEU A 323 63.887 10.006 52.774 1.00 41.20 N ANISOU 3339 N LEU A 323 4133 6329 5191 -518 -496 258 N ATOM 3340 CA LEU A 323 63.522 10.252 54.165 1.00 37.49 C ANISOU 3340 CA LEU A 323 3848 5833 4563 -574 -600 179 C ATOM 3341 C LEU A 323 63.008 8.980 54.830 1.00 38.20 C ANISOU 3341 C LEU A 323 3965 5941 4608 -397 -485 187 C ATOM 3342 O LEU A 323 63.429 8.635 55.939 1.00 46.87 O ANISOU 3342 O LEU A 323 5082 7128 5600 -416 -584 252 O ATOM 3343 CB LEU A 323 62.471 11.361 54.263 1.00 26.94 C ANISOU 3343 CB LEU A 323 2759 4308 3168 -643 -598 -19 C ATOM 3344 CG LEU A 323 62.984 12.795 54.126 1.00 29.28 C ANISOU 3344 CG LEU A 323 3104 4573 3448 -859 -754 -44 C ATOM 3345 CD1 LEU A 323 61.836 13.781 54.241 1.00 31.73 C ANISOU 3345 CD1 LEU A 323 3670 4679 3709 -893 -714 -236 C ATOM 3346 CD2 LEU A 323 64.053 13.088 55.171 1.00 30.37 C ANISOU 3346 CD2 LEU A 323 3224 4836 3478 -1030 -973 44 C ATOM 3347 N ASN A 324 62.104 8.282 54.148 1.00 30.44 N ANISOU 3347 N ASN A 324 2989 4872 3704 -231 -281 123 N ATOM 3348 CA ASN A 324 61.560 7.038 54.680 1.00 27.93 C ANISOU 3348 CA ASN A 324 2696 4555 3362 -59 -145 125 C ATOM 3349 C ASN A 324 62.639 5.983 54.879 1.00 31.86 C ANISOU 3349 C ASN A 324 2994 5226 3883 9 -152 327 C ATOM 3350 O ASN A 324 62.631 5.269 55.873 1.00 37.62 O ANISOU 3350 O ASN A 324 3764 6002 4529 77 -150 369 O ATOM 3351 CB ASN A 324 60.463 6.488 53.769 1.00 23.32 C ANISOU 3351 CB ASN A 324 2132 3851 2878 87 68 28 C ATOM 3352 CG ASN A 324 59.095 7.055 54.093 1.00 30.65 C ANISOU 3352 CG ASN A 324 3278 4602 3767 90 116 -166 C ATOM 3353 OD1 ASN A 324 58.856 7.542 55.199 1.00 36.52 O ANISOU 3353 OD1 ASN A 324 4182 5304 4391 28 42 -229 O ATOM 3354 ND2 ASN A 324 58.185 6.988 53.128 1.00 38.20 N ANISOU 3354 ND2 ASN A 324 4243 5448 4824 164 243 -256 N ATOM 3355 N VAL A 325 63.568 5.889 53.935 1.00 33.79 N ANISOU 3355 N VAL A 325 3029 5563 4248 -3 -149 460 N ATOM 3356 CA VAL A 325 64.646 4.911 54.038 1.00 35.40 C ANISOU 3356 CA VAL A 325 3019 5928 4504 71 -140 672 C ATOM 3357 C VAL A 325 65.599 5.254 55.186 1.00 43.57 C ANISOU 3357 C VAL A 325 4013 7099 5443 -54 -378 787 C ATOM 3358 O VAL A 325 65.994 4.380 55.956 1.00 45.14 O ANISOU 3358 O VAL A 325 4152 7398 5602 28 -391 909 O ATOM 3359 CB VAL A 325 65.431 4.805 52.719 1.00 34.87 C ANISOU 3359 CB VAL A 325 2740 5910 4597 83 -63 791 C ATOM 3360 CG1 VAL A 325 66.672 3.948 52.900 1.00 35.18 C ANISOU 3360 CG1 VAL A 325 2540 6119 4707 144 -69 1032 C ATOM 3361 CG2 VAL A 325 64.542 4.233 51.626 1.00 28.49 C ANISOU 3361 CG2 VAL A 325 1979 4980 3866 220 173 696 C ATOM 3362 N LEU A 326 65.956 6.529 55.307 1.00 42.72 N ANISOU 3362 N LEU A 326 3947 6992 5293 -258 -570 749 N ATOM 3363 CA LEU A 326 66.829 6.977 56.390 1.00 32.32 C ANISOU 3363 CA LEU A 326 2614 5797 3871 -413 -825 840 C ATOM 3364 C LEU A 326 66.207 6.733 57.760 1.00 32.77 C ANISOU 3364 C LEU A 326 2895 5822 3736 -391 -874 763 C ATOM 3365 O LEU A 326 66.882 6.283 58.686 1.00 45.21 O ANISOU 3365 O LEU A 326 4418 7529 5232 -400 -1006 898 O ATOM 3366 CB LEU A 326 67.159 8.463 56.239 1.00 41.89 C ANISOU 3366 CB LEU A 326 3873 6978 5063 -650 -1004 776 C ATOM 3367 CG LEU A 326 68.166 8.846 55.155 1.00 43.41 C ANISOU 3367 CG LEU A 326 3821 7244 5428 -728 -1026 903 C ATOM 3368 CD1 LEU A 326 68.345 10.351 55.116 1.00 34.50 C ANISOU 3368 CD1 LEU A 326 2787 6060 4264 -968 -1193 815 C ATOM 3369 CD2 LEU A 326 69.496 8.155 55.400 1.00 50.03 C ANISOU 3369 CD2 LEU A 326 4376 8288 6345 -718 -1119 1158 C ATOM 3370 N LYS A 327 64.918 7.031 57.886 1.00 33.39 N ANISOU 3370 N LYS A 327 3223 5723 3742 -358 -764 554 N ATOM 3371 CA LYS A 327 64.226 6.893 59.163 1.00 38.46 C ANISOU 3371 CA LYS A 327 4111 6303 4200 -340 -780 462 C ATOM 3372 C LYS A 327 63.935 5.436 59.527 1.00 41.64 C ANISOU 3372 C LYS A 327 4483 6736 4601 -123 -619 532 C ATOM 3373 O LYS A 327 64.253 4.985 60.629 1.00 39.39 O ANISOU 3373 O LYS A 327 4252 6530 4185 -113 -710 612 O ATOM 3374 CB LYS A 327 62.917 7.687 59.146 1.00 35.00 C ANISOU 3374 CB LYS A 327 3935 5650 3713 -363 -687 224 C ATOM 3375 CG LYS A 327 62.063 7.489 60.392 1.00 45.30 C ANISOU 3375 CG LYS A 327 5509 6860 4844 -319 -644 118 C ATOM 3376 CD LYS A 327 60.672 8.080 60.226 1.00 52.12 C ANISOU 3376 CD LYS A 327 6589 7501 5714 -294 -491 -99 C ATOM 3377 CE LYS A 327 59.791 7.753 61.423 1.00 57.23 C ANISOU 3377 CE LYS A 327 7491 8043 6210 -224 -401 -194 C ATOM 3378 NZ LYS A 327 58.410 8.290 61.270 1.00 61.63 N ANISOU 3378 NZ LYS A 327 8236 8378 6802 -185 -232 -391 N ATOM 3379 N ARG A 328 63.333 4.708 58.592 1.00 42.83 N ANISOU 3379 N ARG A 328 4560 6820 4894 43 -383 502 N ATOM 3380 CA ARG A 328 62.799 3.373 58.856 1.00 35.62 C ANISOU 3380 CA ARG A 328 3659 5887 3987 250 -187 525 C ATOM 3381 C ARG A 328 63.814 2.245 58.676 1.00 39.13 C ANISOU 3381 C ARG A 328 3858 6493 4518 363 -156 754 C ATOM 3382 O ARG A 328 63.675 1.183 59.282 1.00 50.78 O ANISOU 3382 O ARG A 328 5352 7988 5953 506 -59 818 O ATOM 3383 CB ARG A 328 61.592 3.107 57.952 1.00 31.39 C ANISOU 3383 CB ARG A 328 3176 5190 3561 364 52 373 C ATOM 3384 CG ARG A 328 60.397 4.010 58.211 1.00 34.17 C ANISOU 3384 CG ARG A 328 3771 5364 3849 302 70 155 C ATOM 3385 CD ARG A 328 59.753 3.688 59.546 1.00 47.39 C ANISOU 3385 CD ARG A 328 5659 6975 5372 350 107 93 C ATOM 3386 NE ARG A 328 58.507 4.419 59.748 1.00 56.11 N ANISOU 3386 NE ARG A 328 6987 7889 6444 323 179 -111 N ATOM 3387 CZ ARG A 328 57.739 4.295 60.826 1.00 59.68 C ANISOU 3387 CZ ARG A 328 7659 8240 6777 362 250 -198 C ATOM 3388 NH1 ARG A 328 58.092 3.467 61.799 1.00 60.74 N ANISOU 3388 NH1 ARG A 328 7831 8451 6796 426 245 -101 N ATOM 3389 NH2 ARG A 328 56.619 4.998 60.931 1.00 62.98 N ANISOU 3389 NH2 ARG A 328 8261 8476 7194 344 333 -374 N ATOM 3390 N VAL A 329 64.823 2.460 57.839 1.00 36.49 N ANISOU 3390 N VAL A 329 3294 6263 4309 308 -220 884 N ATOM 3391 CA VAL A 329 65.808 1.414 57.584 1.00 44.20 C ANISOU 3391 CA VAL A 329 4020 7380 5393 426 -166 1113 C ATOM 3392 C VAL A 329 67.102 1.644 58.364 1.00 49.64 C ANISOU 3392 C VAL A 329 4571 8256 6035 318 -424 1310 C ATOM 3393 O VAL A 329 67.670 0.706 58.925 1.00 51.36 O ANISOU 3393 O VAL A 329 4681 8586 6248 426 -426 1489 O ATOM 3394 CB VAL A 329 66.137 1.300 56.081 1.00 39.44 C ANISOU 3394 CB VAL A 329 3230 6770 4985 465 -23 1158 C ATOM 3395 CG1 VAL A 329 67.123 0.172 55.835 1.00 32.59 C ANISOU 3395 CG1 VAL A 329 2116 6029 4238 604 71 1399 C ATOM 3396 CG2 VAL A 329 64.865 1.085 55.278 1.00 38.18 C ANISOU 3396 CG2 VAL A 329 3208 6433 4866 556 203 967 C ATOM 3397 N PHE A 330 67.562 2.890 58.409 1.00 46.60 N ANISOU 3397 N PHE A 330 4187 7902 5615 101 -647 1283 N ATOM 3398 CA PHE A 330 68.827 3.201 59.068 1.00 47.05 C ANISOU 3398 CA PHE A 330 4094 8140 5642 -33 -918 1470 C ATOM 3399 C PHE A 330 68.633 3.891 60.417 1.00 47.85 C ANISOU 3399 C PHE A 330 4435 8239 5507 -188 -1153 1385 C ATOM 3400 O PHE A 330 69.599 4.314 61.051 1.00 51.04 O ANISOU 3400 O PHE A 330 4758 8783 5853 -341 -1421 1512 O ATOM 3401 CB PHE A 330 69.697 4.060 58.152 1.00 42.80 C ANISOU 3401 CB PHE A 330 3355 7658 5249 -183 -1013 1535 C ATOM 3402 CG PHE A 330 70.058 3.383 56.864 1.00 53.79 C ANISOU 3402 CG PHE A 330 4511 9063 6864 -40 -789 1645 C ATOM 3403 CD1 PHE A 330 71.036 2.402 56.834 1.00 63.67 C ANISOU 3403 CD1 PHE A 330 5567 10400 8224 74 -725 1861 C ATOM 3404 CD2 PHE A 330 69.412 3.715 55.686 1.00 57.29 C ANISOU 3404 CD2 PHE A 330 5011 9366 7391 -22 -609 1501 C ATOM 3405 CE1 PHE A 330 71.369 1.769 55.651 1.00 57.88 C ANISOU 3405 CE1 PHE A 330 4775 9563 7654 191 -469 1894 C ATOM 3406 CE2 PHE A 330 69.741 3.086 54.500 1.00 60.69 C ANISOU 3406 CE2 PHE A 330 5305 9762 7994 100 -387 1575 C ATOM 3407 CZ PHE A 330 70.721 2.112 54.483 1.00 61.06 C ANISOU 3407 CZ PHE A 330 5256 9829 8116 200 -307 1744 C ATOM 3408 N GLY A 331 67.381 3.998 60.848 1.00 48.69 N ANISOU 3408 N GLY A 331 4840 8181 5479 -152 -1049 1174 N ATOM 3409 CA GLY A 331 67.063 4.484 62.178 1.00 52.18 C ANISOU 3409 CA GLY A 331 5555 8592 5678 -264 -1214 1084 C ATOM 3410 C GLY A 331 67.548 5.881 62.518 1.00 49.21 C ANISOU 3410 C GLY A 331 5260 8233 5203 -541 -1488 1033 C ATOM 3411 O GLY A 331 67.733 6.207 63.690 1.00 58.61 O ANISOU 3411 O GLY A 331 6622 9459 6188 -663 -1691 1031 O ATOM 3412 N MET A 332 67.753 6.712 61.503 1.00 47.70 N ANISOU 3412 N MET A 332 4964 8012 5150 -647 -1494 990 N ATOM 3413 CA MET A 332 68.140 8.096 61.743 1.00 57.73 C ANISOU 3413 CA MET A 332 6326 9271 6338 -916 -1729 923 C ATOM 3414 C MET A 332 66.955 8.883 62.294 1.00 73.31 C ANISOU 3414 C MET A 332 8681 11039 8136 -981 -1686 667 C ATOM 3415 O MET A 332 65.854 8.344 62.430 1.00 82.48 O ANISOU 3415 O MET A 332 10003 12074 9262 -813 -1472 554 O ATOM 3416 CB MET A 332 68.669 8.745 60.463 1.00 58.11 C ANISOU 3416 CB MET A 332 6160 9330 6590 -1000 -1720 953 C ATOM 3417 CG MET A 332 69.920 8.077 59.916 1.00 70.01 C ANISOU 3417 CG MET A 332 7285 11031 8283 -952 -1756 1214 C ATOM 3418 SD MET A 332 70.769 9.071 58.675 1.00 84.42 S ANISOU 3418 SD MET A 332 8883 12881 10312 -1118 -1809 1265 S ATOM 3419 CE MET A 332 72.110 7.973 58.220 1.00 86.84 C ANISOU 3419 CE MET A 332 8825 13332 10837 -972 -1732 1548 C ATOM 3420 N PHE A 333 67.192 10.153 62.614 1.00 70.83 N ANISOU 3420 N PHE A 333 8507 10686 7721 -1227 -1880 583 N ATOM 3421 CA PHE A 333 66.177 11.026 63.206 1.00 66.39 C ANISOU 3421 CA PHE A 333 8319 9920 6985 -1311 -1849 350 C ATOM 3422 C PHE A 333 65.669 10.450 64.525 1.00 68.70 C ANISOU 3422 C PHE A 333 8863 10184 7054 -1243 -1842 315 C ATOM 3423 O PHE A 333 64.512 10.643 64.894 1.00 78.58 O ANISOU 3423 O PHE A 333 10400 11246 8210 -1187 -1682 132 O ATOM 3424 CB PHE A 333 65.005 11.245 62.243 1.00 58.00 C ANISOU 3424 CB PHE A 333 7322 8663 6051 -1188 -1578 183 C ATOM 3425 CG PHE A 333 65.422 11.468 60.815 1.00 61.50 C ANISOU 3425 CG PHE A 333 7501 9140 6727 -1186 -1529 242 C ATOM 3426 CD1 PHE A 333 66.478 12.313 60.505 1.00 55.68 C ANISOU 3426 CD1 PHE A 333 6631 8489 6036 -1396 -1729 319 C ATOM 3427 CD2 PHE A 333 64.761 10.822 59.782 1.00 60.08 C ANISOU 3427 CD2 PHE A 333 7213 8902 6715 -981 -1280 221 C ATOM 3428 CE1 PHE A 333 66.863 12.511 59.191 1.00 47.53 C ANISOU 3428 CE1 PHE A 333 5369 7477 5212 -1389 -1665 377 C ATOM 3429 CE2 PHE A 333 65.140 11.016 58.467 1.00 56.98 C ANISOU 3429 CE2 PHE A 333 6605 8531 6514 -979 -1229 275 C ATOM 3430 CZ PHE A 333 66.192 11.862 58.170 1.00 53.49 C ANISOU 3430 CZ PHE A 333 6038 8169 6116 -1178 -1412 354 C ATOM 3431 N ALA A 334 66.542 9.735 65.228 1.00 63.89 N ANISOU 3431 N ALA A 334 8143 9762 6370 -1243 -2010 500 N ATOM 3432 CA ALA A 334 66.203 9.179 66.530 1.00 70.35 C ANISOU 3432 CA ALA A 334 9202 10570 6956 -1190 -2030 493 C ATOM 3433 C ALA A 334 66.437 10.215 67.622 1.00 78.66 C ANISOU 3433 C ALA A 334 10552 11591 7744 -1453 -2283 411 C ATOM 3434 O ALA A 334 66.135 9.980 68.793 1.00 74.33 O ANISOU 3434 O ALA A 334 10276 11009 6957 -1452 -2320 378 O ATOM 3435 CB ALA A 334 67.015 7.922 66.801 1.00 72.50 C ANISOU 3435 CB ALA A 334 9234 11053 7260 -1061 -2096 740 C ATOM 3436 N HIS A 335 66.978 11.363 67.225 1.00 85.24 N ANISOU 3436 N HIS A 335 11346 12425 8616 -1683 -2449 377 N ATOM 3437 CA HIS A 335 67.265 12.452 68.151 1.00 81.05 C ANISOU 3437 CA HIS A 335 11070 11809 7915 -1905 -2618 280 C ATOM 3438 C HIS A 335 66.449 13.694 67.807 1.00 73.77 C ANISOU 3438 C HIS A 335 10386 10651 6994 -2003 -2496 48 C ATOM 3439 O HIS A 335 66.882 14.819 68.052 1.00 68.40 O ANISOU 3439 O HIS A 335 9791 9895 6303 -2181 -2592 -12 O ATOM 3440 CB HIS A 335 68.758 12.785 68.140 1.00 80.33 C ANISOU 3440 CB HIS A 335 10712 11866 7943 -2042 -2844 441 C ATOM 3441 N ASP A 338 67.048 18.090 67.533 1.00 76.89 N ANISOU 3441 N ASP A 338 11108 10632 7475 -2561 -2597 -270 N ATOM 3442 CA ASP A 338 66.335 18.895 66.546 1.00 82.46 C ANISOU 3442 CA ASP A 338 11853 11170 8308 -2548 -2422 -398 C ATOM 3443 C ASP A 338 65.327 18.053 65.755 1.00 84.83 C ANISOU 3443 C ASP A 338 12095 11445 8690 -2343 -2224 -437 C ATOM 3444 O ASP A 338 65.704 17.239 64.910 1.00 85.48 O ANISOU 3444 O ASP A 338 11873 11689 8915 -2263 -2242 -309 O ATOM 3445 CB ASP A 338 67.331 19.567 65.597 1.00 86.42 C ANISOU 3445 CB ASP A 338 12090 11743 9001 -2666 -2516 -310 C ATOM 3446 CG ASP A 338 66.750 20.790 64.904 1.00 93.92 C ANISOU 3446 CG ASP A 338 13165 12489 10031 -2711 -2376 -451 C ATOM 3447 OD1 ASP A 338 65.567 20.759 64.499 1.00 97.09 O ANISOU 3447 OD1 ASP A 338 13690 12745 10455 -2582 -2172 -572 O ATOM 3448 OD2 ASP A 338 67.487 21.789 64.761 1.00 95.70 O ANISOU 3448 OD2 ASP A 338 13361 12700 10302 -2872 -2467 -436 O ATOM 3449 N ARG A 339 64.043 18.264 66.031 1.00 77.44 N ANISOU 3449 N ARG A 339 11450 10299 7675 -2257 -2022 -610 N ATOM 3450 CA ARG A 339 62.976 17.494 65.397 1.00 69.42 C ANISOU 3450 CA ARG A 339 10424 9230 6721 -2064 -1818 -671 C ATOM 3451 C ARG A 339 62.181 18.326 64.395 1.00 68.17 C ANISOU 3451 C ARG A 339 10299 8884 6719 -2031 -1638 -797 C ATOM 3452 O ARG A 339 61.662 17.800 63.408 1.00 64.19 O ANISOU 3452 O ARG A 339 9637 8378 6373 -1880 -1496 -796 O ATOM 3453 CB ARG A 339 62.033 16.932 66.461 1.00 68.49 C ANISOU 3453 CB ARG A 339 10595 9006 6421 -1943 -1682 -761 C ATOM 3454 CG ARG A 339 61.637 17.954 67.519 1.00 84.33 C ANISOU 3454 CG ARG A 339 12935 10812 8294 -2023 -1630 -883 C ATOM 3455 CD ARG A 339 60.389 17.529 68.271 1.00 88.76 C ANISOU 3455 CD ARG A 339 13767 11205 8753 -1861 -1396 -995 C ATOM 3456 NE ARG A 339 59.234 17.443 67.384 1.00 91.70 N ANISOU 3456 NE ARG A 339 14118 11432 9290 -1690 -1138 -1094 N ATOM 3457 CZ ARG A 339 57.999 17.167 67.791 1.00 93.38 C ANISOU 3457 CZ ARG A 339 14509 11471 9500 -1518 -879 -1191 C ATOM 3458 NH1 ARG A 339 57.755 16.953 69.076 1.00 95.24 N ANISOU 3458 NH1 ARG A 339 14975 11651 9561 -1499 -838 -1206 N ATOM 3459 NH2 ARG A 339 57.008 17.108 66.912 1.00 91.30 N ANISOU 3459 NH2 ARG A 339 14174 11088 9429 -1359 -658 -1261 N ATOM 3460 N GLU A 340 62.089 19.625 64.661 1.00 74.19 N ANISOU 3460 N GLU A 340 11239 9484 7466 -2137 -1618 -884 N ATOM 3461 CA GLU A 340 61.289 20.531 63.844 1.00 66.51 C ANISOU 3461 CA GLU A 340 10323 8316 6632 -2095 -1441 -994 C ATOM 3462 C GLU A 340 61.783 20.582 62.401 1.00 56.74 C ANISOU 3462 C GLU A 340 8792 7171 5598 -2110 -1481 -919 C ATOM 3463 O GLU A 340 60.986 20.712 61.474 1.00 63.27 O ANISOU 3463 O GLU A 340 9592 7886 6561 -2004 -1320 -983 O ATOM 3464 CB GLU A 340 61.285 21.936 64.456 1.00 71.52 C ANISOU 3464 CB GLU A 340 11186 8790 7197 -2222 -1437 -1069 C ATOM 3465 CG GLU A 340 62.659 22.571 64.617 1.00 83.50 C ANISOU 3465 CG GLU A 340 12615 10427 8685 -2439 -1672 -977 C ATOM 3466 CD GLU A 340 62.592 23.953 65.240 1.00 95.11 C ANISOU 3466 CD GLU A 340 14340 11728 10070 -2569 -1655 -1062 C ATOM 3467 OE1 GLU A 340 61.536 24.298 65.813 1.00 96.81 O ANISOU 3467 OE1 GLU A 340 14817 11752 10215 -2492 -1478 -1176 O ATOM 3468 OE2 GLU A 340 63.593 24.695 65.155 1.00101.06 O ANISOU 3468 OE2 GLU A 340 15028 12537 10834 -2746 -1810 -1009 O ATOM 3469 N THR A 341 63.094 20.465 62.215 1.00 42.55 N ANISOU 3469 N THR A 341 6126 5808 4234 -2632 -744 -333 N ATOM 3470 CA THR A 341 63.685 20.458 60.880 1.00 47.80 C ANISOU 3470 CA THR A 341 6633 6498 5029 -2591 -743 -280 C ATOM 3471 C THR A 341 63.297 19.196 60.116 1.00 44.22 C ANISOU 3471 C THR A 341 6007 6114 4682 -2452 -732 -233 C ATOM 3472 O THR A 341 62.880 19.261 58.956 1.00 45.88 O ANISOU 3472 O THR A 341 6172 6280 4979 -2377 -667 -244 O ATOM 3473 CB THR A 341 65.221 20.569 60.948 1.00 47.88 C ANISOU 3473 CB THR A 341 6528 6608 5056 -2684 -844 -196 C ATOM 3474 OG1 THR A 341 65.585 21.897 61.342 1.00 56.88 O ANISOU 3474 OG1 THR A 341 7833 7667 6112 -2824 -845 -238 O ATOM 3475 CG2 THR A 341 65.845 20.262 59.598 1.00 34.56 C ANISOU 3475 CG2 THR A 341 4644 4985 3502 -2623 -840 -130 C ATOM 3476 N VAL A 342 63.432 18.051 60.780 1.00 40.23 N ANISOU 3476 N VAL A 342 5423 5705 4157 -2422 -799 -178 N ATOM 3477 CA VAL A 342 63.064 16.766 60.196 1.00 36.57 C ANISOU 3477 CA VAL A 342 4826 5298 3771 -2298 -801 -128 C ATOM 3478 C VAL A 342 61.581 16.748 59.835 1.00 44.82 C ANISOU 3478 C VAL A 342 5948 6263 4820 -2234 -696 -201 C ATOM 3479 O VAL A 342 61.192 16.315 58.742 1.00 55.18 O ANISOU 3479 O VAL A 342 7169 7569 6228 -2141 -657 -186 O ATOM 3480 CB VAL A 342 63.372 15.604 61.160 1.00 36.40 C ANISOU 3480 CB VAL A 342 4764 5369 3696 -2291 -894 -63 C ATOM 3481 CG1 VAL A 342 63.066 14.268 60.502 1.00 35.38 C ANISOU 3481 CG1 VAL A 342 4520 5284 3640 -2168 -906 -5 C ATOM 3482 CG2 VAL A 342 64.822 15.661 61.610 1.00 42.24 C ANISOU 3482 CG2 VAL A 342 5426 6202 4423 -2358 -1005 4 C ATOM 3483 N TYR A 343 60.761 17.242 60.758 1.00 36.25 N ANISOU 3483 N TYR A 343 5029 5121 3621 -2287 -648 -284 N ATOM 3484 CA TYR A 343 59.319 17.291 60.557 1.00 37.20 C ANISOU 3484 CA TYR A 343 5220 5186 3728 -2221 -537 -362 C ATOM 3485 C TYR A 343 58.958 18.218 59.400 1.00 38.75 C ANISOU 3485 C TYR A 343 5435 5282 4005 -2138 -442 -406 C ATOM 3486 O TYR A 343 58.029 17.942 58.641 1.00 40.36 O ANISOU 3486 O TYR A 343 5589 5465 4279 -1990 -356 -411 O ATOM 3487 CB TYR A 343 58.613 17.742 61.837 1.00 34.19 C ANISOU 3487 CB TYR A 343 5021 4773 3196 -2274 -488 -444 C ATOM 3488 CG TYR A 343 57.122 17.500 61.810 1.00 50.85 C ANISOU 3488 CG TYR A 343 7151 6871 5300 -2137 -353 -487 C ATOM 3489 CD1 TYR A 343 56.593 16.274 62.191 1.00 55.85 C ANISOU 3489 CD1 TYR A 343 7714 7588 5918 -2105 -355 -438 C ATOM 3490 CD2 TYR A 343 56.244 18.493 61.392 1.00 60.76 C ANISOU 3490 CD2 TYR A 343 8492 8037 6558 -2041 -226 -571 C ATOM 3491 CE1 TYR A 343 55.230 16.043 62.162 1.00 60.05 C ANISOU 3491 CE1 TYR A 343 8241 8134 6443 -2002 -232 -469 C ATOM 3492 CE2 TYR A 343 54.879 18.272 61.361 1.00 60.93 C ANISOU 3492 CE2 TYR A 343 8498 8079 6575 -1910 -104 -604 C ATOM 3493 CZ TYR A 343 54.378 17.046 61.746 1.00 63.25 C ANISOU 3493 CZ TYR A 343 8699 8475 6857 -1902 -107 -552 C ATOM 3494 OH TYR A 343 53.021 16.820 61.714 1.00 68.16 O ANISOU 3494 OH TYR A 343 9285 9141 7472 -1794 13 -578 O ATOM 3495 N ALA A 344 59.701 19.314 59.269 1.00 29.84 N ANISOU 3495 N ALA A 344 4386 4092 2860 -2244 -466 -434 N ATOM 3496 CA ALA A 344 59.491 20.255 58.175 1.00 32.05 C ANISOU 3496 CA ALA A 344 4711 4263 3204 -2182 -387 -468 C ATOM 3497 C ALA A 344 59.833 19.612 56.829 1.00 38.36 C ANISOU 3497 C ALA A 344 5321 5107 4148 -2090 -395 -387 C ATOM 3498 O ALA A 344 59.089 19.761 55.851 1.00 38.87 O ANISOU 3498 O ALA A 344 5378 5109 4282 -1949 -309 -402 O ATOM 3499 CB ALA A 344 60.318 21.512 58.389 1.00 31.03 C ANISOU 3499 CB ALA A 344 4725 4055 3010 -2348 -422 -504 C ATOM 3500 N TRP A 345 60.957 18.897 56.788 1.00 33.09 N ANISOU 3500 N TRP A 345 4505 4551 3518 -2159 -499 -300 N ATOM 3501 CA TRP A 345 61.349 18.149 55.597 1.00 34.08 C ANISOU 3501 CA TRP A 345 4453 4730 3765 -2060 -506 -219 C ATOM 3502 C TRP A 345 60.273 17.144 55.203 1.00 36.77 C ANISOU 3502 C TRP A 345 4745 5073 4155 -1885 -454 -208 C ATOM 3503 O TRP A 345 59.954 16.988 54.019 1.00 36.83 O ANISOU 3503 O TRP A 345 4696 5047 4249 -1765 -402 -190 O ATOM 3504 CB TRP A 345 62.679 17.425 55.821 1.00 36.52 C ANISOU 3504 CB TRP A 345 4611 5172 4092 -2097 -614 -123 C ATOM 3505 CG TRP A 345 63.876 18.249 55.470 1.00 45.45 C ANISOU 3505 CG TRP A 345 5707 6322 5241 -2178 -634 -92 C ATOM 3506 CD1 TRP A 345 64.739 18.857 56.337 1.00 45.75 C ANISOU 3506 CD1 TRP A 345 5785 6391 5207 -2299 -691 -86 C ATOM 3507 CD2 TRP A 345 64.344 18.562 54.152 1.00 43.90 C ANISOU 3507 CD2 TRP A 345 5429 6121 5131 -2158 -596 -60 C ATOM 3508 NE1 TRP A 345 65.715 19.526 55.639 1.00 47.73 N ANISOU 3508 NE1 TRP A 345 5977 6663 5496 -2361 -692 -51 N ATOM 3509 CE2 TRP A 345 65.495 19.361 54.297 1.00 49.28 C ANISOU 3509 CE2 TRP A 345 6099 6838 5788 -2276 -629 -34 C ATOM 3510 CE3 TRP A 345 63.900 18.243 52.865 1.00 36.94 C ANISOU 3510 CE3 TRP A 345 4487 5211 4339 -2061 -536 -47 C ATOM 3511 CZ2 TRP A 345 66.208 19.847 53.201 1.00 47.81 C ANISOU 3511 CZ2 TRP A 345 5840 6664 5661 -2301 -597 4 C ATOM 3512 CZ3 TRP A 345 64.610 18.725 51.780 1.00 44.04 C ANISOU 3512 CZ3 TRP A 345 5322 6115 5295 -2080 -504 -10 C ATOM 3513 CH2 TRP A 345 65.750 19.519 51.955 1.00 46.07 C ANISOU 3513 CH2 TRP A 345 5567 6412 5525 -2200 -530 15 C ATOM 3514 N PHE A 346 59.707 16.472 56.202 1.00 26.14 N ANISOU 3514 N PHE A 346 3426 3764 2741 -1886 -470 -217 N ATOM 3515 CA PHE A 346 58.648 15.501 55.952 1.00 27.44 C ANISOU 3515 CA PHE A 346 3553 3939 2935 -1758 -427 -204 C ATOM 3516 C PHE A 346 57.375 16.150 55.412 1.00 24.77 C ANISOU 3516 C PHE A 346 3277 3520 2615 -1657 -307 -274 C ATOM 3517 O PHE A 346 56.783 15.649 54.455 1.00 31.92 O ANISOU 3517 O PHE A 346 4115 4418 3595 -1539 -273 -252 O ATOM 3518 CB PHE A 346 58.333 14.712 57.224 1.00 28.77 C ANISOU 3518 CB PHE A 346 3755 4167 3009 -1808 -465 -196 C ATOM 3519 CG PHE A 346 59.063 13.404 57.316 1.00 33.24 C ANISOU 3519 CG PHE A 346 4227 4812 3591 -1802 -570 -100 C ATOM 3520 CD1 PHE A 346 58.554 12.270 56.702 1.00 27.45 C ANISOU 3520 CD1 PHE A 346 3437 4084 2909 -1695 -564 -51 C ATOM 3521 CD2 PHE A 346 60.260 13.308 58.008 1.00 35.10 C ANISOU 3521 CD2 PHE A 346 4440 5114 3781 -1901 -682 -58 C ATOM 3522 CE1 PHE A 346 59.223 11.062 56.778 1.00 24.65 C ANISOU 3522 CE1 PHE A 346 3029 3781 2557 -1671 -660 36 C ATOM 3523 CE2 PHE A 346 60.935 12.104 58.088 1.00 33.34 C ANISOU 3523 CE2 PHE A 346 4136 4964 3567 -1866 -781 33 C ATOM 3524 CZ PHE A 346 60.415 10.979 57.472 1.00 26.16 C ANISOU 3524 CZ PHE A 346 3194 4041 2706 -1743 -766 78 C ATOM 3525 N THR A 347 56.953 17.258 56.019 1.00 25.60 N ANISOU 3525 N THR A 347 3518 3564 2643 -1694 -249 -358 N ATOM 3526 CA THR A 347 55.747 17.951 55.566 1.00 32.84 C ANISOU 3526 CA THR A 347 4496 4412 3568 -1574 -136 -427 C ATOM 3527 C THR A 347 55.920 18.415 54.126 1.00 24.92 C ANISOU 3527 C THR A 347 3464 3340 2665 -1493 -114 -412 C ATOM 3528 O THR A 347 55.013 18.265 53.290 1.00 37.96 O ANISOU 3528 O THR A 347 5073 4979 4373 -1356 -59 -415 O ATOM 3529 CB THR A 347 55.403 19.164 56.456 1.00 35.11 C ANISOU 3529 CB THR A 347 4967 4629 3745 -1612 -77 -523 C ATOM 3530 OG1 THR A 347 56.531 20.042 56.536 1.00 51.60 O ANISOU 3530 OG1 THR A 347 7148 6651 5806 -1741 -130 -533 O ATOM 3531 CG2 THR A 347 55.022 18.710 57.856 1.00 27.44 C ANISOU 3531 CG2 THR A 347 4036 3727 2662 -1673 -76 -544 C ATOM 3532 N PHE A 348 57.098 18.959 53.836 1.00 25.27 N ANISOU 3532 N PHE A 348 3527 3350 2723 -1587 -162 -391 N ATOM 3533 CA PHE A 348 57.401 19.393 52.480 1.00 26.69 C ANISOU 3533 CA PHE A 348 3686 3467 2986 -1531 -141 -368 C ATOM 3534 C PHE A 348 57.339 18.230 51.505 1.00 27.39 C ANISOU 3534 C PHE A 348 3621 3617 3171 -1428 -159 -295 C ATOM 3535 O PHE A 348 56.755 18.349 50.429 1.00 31.09 O ANISOU 3535 O PHE A 348 4083 4035 3697 -1308 -110 -297 O ATOM 3536 CB PHE A 348 58.777 20.047 52.401 1.00 25.63 C ANISOU 3536 CB PHE A 348 3575 3319 2846 -1683 -193 -343 C ATOM 3537 CG PHE A 348 59.221 20.326 50.997 1.00 33.09 C ANISOU 3537 CG PHE A 348 4479 4222 3873 -1641 -171 -303 C ATOM 3538 CD1 PHE A 348 58.678 21.383 50.285 1.00 35.54 C ANISOU 3538 CD1 PHE A 348 4923 4398 4182 -1578 -97 -350 C ATOM 3539 CD2 PHE A 348 60.168 19.523 50.381 1.00 35.85 C ANISOU 3539 CD2 PHE A 348 4666 4666 4290 -1652 -220 -215 C ATOM 3540 CE1 PHE A 348 59.077 21.642 48.989 1.00 40.90 C ANISOU 3540 CE1 PHE A 348 5580 5034 4924 -1545 -74 -310 C ATOM 3541 CE2 PHE A 348 60.572 19.777 49.083 1.00 43.35 C ANISOU 3541 CE2 PHE A 348 5585 5584 5304 -1612 -187 -177 C ATOM 3542 CZ PHE A 348 60.025 20.839 48.386 1.00 39.71 C ANISOU 3542 CZ PHE A 348 5264 4985 4839 -1568 -115 -224 C ATOM 3543 N SER A 349 57.948 17.110 51.885 1.00 29.36 N ANISOU 3543 N SER A 349 3763 3965 3428 -1470 -234 -231 N ATOM 3544 CA SER A 349 57.984 15.929 51.026 1.00 29.55 C ANISOU 3544 CA SER A 349 3670 4033 3525 -1373 -259 -161 C ATOM 3545 C SER A 349 56.582 15.411 50.723 1.00 30.57 C ANISOU 3545 C SER A 349 3798 4148 3667 -1258 -213 -181 C ATOM 3546 O SER A 349 56.272 15.058 49.579 1.00 38.65 O ANISOU 3546 O SER A 349 4781 5148 4755 -1156 -197 -155 O ATOM 3547 CB SER A 349 58.827 14.831 51.669 1.00 31.01 C ANISOU 3547 CB SER A 349 3772 4317 3694 -1426 -351 -93 C ATOM 3548 OG SER A 349 60.166 15.267 51.825 1.00 28.27 O ANISOU 3548 OG SER A 349 3388 4012 3342 -1527 -402 -64 O ATOM 3549 N HIS A 350 55.738 15.373 51.750 1.00 22.17 N ANISOU 3549 N HIS A 350 2777 3109 2537 -1283 -191 -224 N ATOM 3550 CA HIS A 350 54.341 14.990 51.574 1.00 27.63 C ANISOU 3550 CA HIS A 350 3452 3816 3232 -1196 -140 -245 C ATOM 3551 C HIS A 350 53.662 15.903 50.555 1.00 30.29 C ANISOU 3551 C HIS A 350 3815 4082 3612 -1083 -71 -287 C ATOM 3552 O HIS A 350 53.067 15.429 49.567 1.00 31.34 O ANISOU 3552 O HIS A 350 3892 4216 3801 -989 -67 -263 O ATOM 3553 CB HIS A 350 53.595 15.035 52.912 1.00 27.86 C ANISOU 3553 CB HIS A 350 3524 3893 3167 -1248 -106 -291 C ATOM 3554 CG HIS A 350 54.103 14.053 53.921 1.00 33.13 C ANISOU 3554 CG HIS A 350 4180 4627 3780 -1352 -177 -246 C ATOM 3555 ND1 HIS A 350 53.792 14.132 55.262 1.00 41.53 N ANISOU 3555 ND1 HIS A 350 5305 5732 4742 -1431 -160 -280 N ATOM 3556 CD2 HIS A 350 54.902 12.967 53.785 1.00 25.79 C ANISOU 3556 CD2 HIS A 350 3199 3726 2875 -1377 -266 -167 C ATOM 3557 CE1 HIS A 350 54.377 13.140 55.907 1.00 33.21 C ANISOU 3557 CE1 HIS A 350 4240 4727 3652 -1510 -242 -221 C ATOM 3558 NE2 HIS A 350 55.056 12.418 55.036 1.00 33.73 N ANISOU 3558 NE2 HIS A 350 4237 4785 3794 -1471 -309 -151 N ATOM 3559 N TRP A 351 53.775 17.212 50.785 1.00 30.96 N ANISOU 3559 N TRP A 351 4003 4097 3662 -1094 -25 -347 N ATOM 3560 CA TRP A 351 53.179 18.184 49.871 1.00 30.48 C ANISOU 3560 CA TRP A 351 3999 3952 3629 -977 37 -387 C ATOM 3561 C TRP A 351 53.664 18.001 48.437 1.00 30.27 C ANISOU 3561 C TRP A 351 3930 3884 3685 -924 12 -333 C ATOM 3562 O TRP A 351 52.894 18.159 47.497 1.00 29.93 O ANISOU 3562 O TRP A 351 3882 3810 3679 -802 40 -339 O ATOM 3563 CB TRP A 351 53.473 19.619 50.313 1.00 33.28 C ANISOU 3563 CB TRP A 351 4513 4208 3922 -1013 77 -454 C ATOM 3564 CG TRP A 351 53.037 20.618 49.283 1.00 30.13 C ANISOU 3564 CG TRP A 351 4199 3701 3548 -891 129 -483 C ATOM 3565 CD1 TRP A 351 51.802 21.187 49.164 1.00 36.21 C ANISOU 3565 CD1 TRP A 351 5015 4447 4297 -739 197 -538 C ATOM 3566 CD2 TRP A 351 53.825 21.143 48.207 1.00 28.14 C ANISOU 3566 CD2 TRP A 351 3995 3358 3340 -901 116 -453 C ATOM 3567 NE1 TRP A 351 51.776 22.042 48.089 1.00 31.30 N ANISOU 3567 NE1 TRP A 351 4483 3710 3701 -647 218 -544 N ATOM 3568 CE2 TRP A 351 53.005 22.031 47.482 1.00 26.68 C ANISOU 3568 CE2 TRP A 351 3906 3077 3153 -754 173 -492 C ATOM 3569 CE3 TRP A 351 55.144 20.951 47.787 1.00 32.18 C ANISOU 3569 CE3 TRP A 351 4471 3870 3886 -1015 67 -392 C ATOM 3570 CZ2 TRP A 351 53.461 22.726 46.366 1.00 34.42 C ANISOU 3570 CZ2 TRP A 351 4972 3946 4161 -732 179 -473 C ATOM 3571 CZ3 TRP A 351 55.595 21.640 46.676 1.00 35.94 C ANISOU 3571 CZ3 TRP A 351 5013 4251 4391 -999 84 -373 C ATOM 3572 CH2 TRP A 351 54.757 22.517 45.980 1.00 37.28 C ANISOU 3572 CH2 TRP A 351 5302 4310 4554 -865 138 -413 C ATOM 3573 N LEU A 352 54.945 17.681 48.279 1.00 32.80 N ANISOU 3573 N LEU A 352 4220 4214 4030 -1012 -41 -279 N ATOM 3574 CA LEU A 352 55.555 17.512 46.962 1.00 25.72 C ANISOU 3574 CA LEU A 352 3286 3286 3200 -968 -54 -226 C ATOM 3575 C LEU A 352 54.967 16.298 46.246 1.00 30.67 C ANISOU 3575 C LEU A 352 3826 3955 3872 -873 -78 -183 C ATOM 3576 O LEU A 352 54.610 16.352 45.050 1.00 29.22 O ANISOU 3576 O LEU A 352 3649 3725 3730 -774 -61 -171 O ATOM 3577 CB LEU A 352 57.071 17.373 47.111 1.00 21.35 C ANISOU 3577 CB LEU A 352 2691 2770 2652 -1083 -100 -174 C ATOM 3578 CG LEU A 352 57.945 17.289 45.863 1.00 29.14 C ANISOU 3578 CG LEU A 352 3633 3744 3694 -1056 -99 -115 C ATOM 3579 CD1 LEU A 352 57.847 18.564 45.045 1.00 28.93 C ANISOU 3579 CD1 LEU A 352 3715 3606 3670 -1038 -39 -145 C ATOM 3580 CD2 LEU A 352 59.383 17.021 46.270 1.00 29.20 C ANISOU 3580 CD2 LEU A 352 3558 3837 3699 -1170 -148 -62 C ATOM 3581 N VAL A 353 54.866 15.205 46.999 1.00 23.09 N ANISOU 3581 N VAL A 353 2806 3075 2894 -912 -122 -158 N ATOM 3582 CA VAL A 353 54.225 13.991 46.515 1.00 22.68 C ANISOU 3582 CA VAL A 353 2699 3055 2863 -851 -153 -121 C ATOM 3583 C VAL A 353 52.827 14.303 45.997 1.00 26.16 C ANISOU 3583 C VAL A 353 3145 3482 3313 -761 -113 -159 C ATOM 3584 O VAL A 353 52.454 13.870 44.908 1.00 32.49 O ANISOU 3584 O VAL A 353 3930 4263 4151 -684 -129 -134 O ATOM 3585 CB VAL A 353 54.146 12.916 47.616 1.00 25.04 C ANISOU 3585 CB VAL A 353 2967 3428 3118 -925 -201 -98 C ATOM 3586 CG1 VAL A 353 53.192 11.802 47.215 1.00 19.43 C ANISOU 3586 CG1 VAL A 353 2230 2740 2413 -887 -226 -71 C ATOM 3587 CG2 VAL A 353 55.527 12.365 47.905 1.00 24.65 C ANISOU 3587 CG2 VAL A 353 2896 3403 3066 -977 -260 -42 C ATOM 3588 N TYR A 354 52.059 15.076 46.758 1.00 25.01 N ANISOU 3588 N TYR A 354 3024 3352 3128 -762 -63 -221 N ATOM 3589 CA TYR A 354 50.723 15.433 46.286 1.00 27.00 C ANISOU 3589 CA TYR A 354 3259 3614 3386 -656 -23 -255 C ATOM 3590 C TYR A 354 50.777 16.403 45.105 1.00 30.93 C ANISOU 3590 C TYR A 354 3819 4015 3919 -551 1 -268 C ATOM 3591 O TYR A 354 49.865 16.438 44.274 1.00 33.25 O ANISOU 3591 O TYR A 354 4087 4312 4235 -446 3 -270 O ATOM 3592 CB TYR A 354 49.889 16.024 47.424 1.00 21.21 C ANISOU 3592 CB TYR A 354 2535 2933 2592 -658 38 -318 C ATOM 3593 CG TYR A 354 49.529 15.001 48.476 1.00 27.15 C ANISOU 3593 CG TYR A 354 3222 3793 3300 -752 22 -301 C ATOM 3594 CD1 TYR A 354 48.757 13.892 48.157 1.00 24.50 C ANISOU 3594 CD1 TYR A 354 2796 3534 2978 -758 -12 -260 C ATOM 3595 CD2 TYR A 354 49.967 15.137 49.784 1.00 25.20 C ANISOU 3595 CD2 TYR A 354 3021 3566 2987 -850 35 -324 C ATOM 3596 CE1 TYR A 354 48.431 12.951 49.112 1.00 34.53 C ANISOU 3596 CE1 TYR A 354 4027 4894 4199 -862 -25 -239 C ATOM 3597 CE2 TYR A 354 49.645 14.202 50.746 1.00 29.15 C ANISOU 3597 CE2 TYR A 354 3480 4159 3437 -941 22 -304 C ATOM 3598 CZ TYR A 354 48.877 13.111 50.406 1.00 37.00 C ANISOU 3598 CZ TYR A 354 4389 5224 4446 -948 -5 -260 C ATOM 3599 OH TYR A 354 48.557 12.177 51.366 1.00 32.76 O ANISOU 3599 OH TYR A 354 3830 4771 3848 -1056 -17 -234 O ATOM 3600 N ALA A 355 51.857 17.172 45.025 1.00 32.45 N ANISOU 3600 N ALA A 355 4093 4126 4111 -591 14 -271 N ATOM 3601 CA ALA A 355 52.014 18.169 43.975 1.00 25.59 C ANISOU 3601 CA ALA A 355 3312 3150 3261 -515 42 -280 C ATOM 3602 C ALA A 355 52.201 17.500 42.621 1.00 28.47 C ANISOU 3602 C ALA A 355 3642 3499 3677 -459 6 -222 C ATOM 3603 O ALA A 355 51.806 18.051 41.591 1.00 29.67 O ANISOU 3603 O ALA A 355 3847 3584 3842 -358 21 -225 O ATOM 3604 CB ALA A 355 53.185 19.090 44.281 1.00 21.10 C ANISOU 3604 CB ALA A 355 2841 2507 2670 -612 61 -290 C ATOM 3605 N ASN A 356 52.809 16.315 42.626 1.00 24.24 N ANISOU 3605 N ASN A 356 3034 3017 3159 -517 -41 -169 N ATOM 3606 CA ASN A 356 52.962 15.533 41.393 1.00 28.10 C ANISOU 3606 CA ASN A 356 3505 3489 3682 -457 -74 -117 C ATOM 3607 C ASN A 356 51.649 15.379 40.604 1.00 34.11 C ANISOU 3607 C ASN A 356 4261 4250 4451 -352 -90 -126 C ATOM 3608 O ASN A 356 51.601 15.565 39.367 1.00 46.71 O ANISOU 3608 O ASN A 356 5903 5783 6061 -270 -94 -109 O ATOM 3609 CB ASN A 356 53.531 14.152 41.728 1.00 30.34 C ANISOU 3609 CB ASN A 356 3727 3834 3967 -514 -127 -67 C ATOM 3610 CG ASN A 356 53.802 13.319 40.493 1.00 35.55 C ANISOU 3610 CG ASN A 356 4398 4464 4647 -446 -157 -16 C ATOM 3611 OD1 ASN A 356 54.878 13.400 39.903 1.00 46.44 O ANISOU 3611 OD1 ASN A 356 5792 5815 6039 -435 -139 17 O ATOM 3612 ND2 ASN A 356 52.825 12.511 40.095 1.00 24.25 N ANISOU 3612 ND2 ASN A 356 2961 3043 3211 -407 -200 -10 N ATOM 3613 N SER A 357 50.589 15.049 41.341 1.00 28.28 N ANISOU 3613 N SER A 357 3459 3592 3695 -360 -101 -151 N ATOM 3614 CA SER A 357 49.256 14.849 40.780 1.00 40.18 C ANISOU 3614 CA SER A 357 4923 5140 5205 -280 -125 -157 C ATOM 3615 C SER A 357 48.739 16.081 40.044 1.00 41.85 C ANISOU 3615 C SER A 357 5189 5291 5420 -153 -92 -189 C ATOM 3616 O SER A 357 47.980 15.965 39.082 1.00 42.10 O ANISOU 3616 O SER A 357 5208 5327 5460 -67 -128 -177 O ATOM 3617 CB SER A 357 48.271 14.466 41.886 1.00 44.13 C ANISOU 3617 CB SER A 357 5329 5760 5678 -328 -122 -180 C ATOM 3618 OG SER A 357 48.666 13.268 42.531 1.00 52.54 O ANISOU 3618 OG SER A 357 6363 6870 6729 -446 -161 -144 O ATOM 3619 N ALA A 358 49.138 17.259 40.509 1.00 37.26 N ANISOU 3619 N ALA A 358 4686 4649 4823 -143 -31 -229 N ATOM 3620 CA ALA A 358 48.757 18.497 39.845 1.00 40.22 C ANISOU 3620 CA ALA A 358 5156 4938 5189 -17 2 -258 C ATOM 3621 C ALA A 358 49.733 18.807 38.719 1.00 33.47 C ANISOU 3621 C ALA A 358 4407 3964 4348 -13 0 -221 C ATOM 3622 O ALA A 358 49.403 19.526 37.776 1.00 41.12 O ANISOU 3622 O ALA A 358 5461 4854 5310 96 4 -223 O ATOM 3623 CB ALA A 358 48.704 19.647 40.840 1.00 32.53 C ANISOU 3623 CB ALA A 358 4258 3929 4175 -8 68 -320 C ATOM 3624 N ALA A 359 50.937 18.254 38.822 1.00 29.65 N ANISOU 3624 N ALA A 359 3915 3476 3876 -128 -4 -185 N ATOM 3625 CA ALA A 359 51.972 18.488 37.824 1.00 28.05 C ANISOU 3625 CA ALA A 359 3791 3186 3681 -138 9 -145 C ATOM 3626 C ALA A 359 51.648 17.813 36.497 1.00 32.38 C ANISOU 3626 C ALA A 359 4339 3722 4241 -53 -32 -105 C ATOM 3627 O ALA A 359 51.854 18.406 35.440 1.00 33.45 O ANISOU 3627 O ALA A 359 4574 3768 4367 5 -14 -89 O ATOM 3628 CB ALA A 359 53.322 18.012 38.334 1.00 22.21 C ANISOU 3628 CB ALA A 359 3010 2480 2950 -270 16 -113 C ATOM 3629 N ASN A 360 51.149 16.580 36.540 1.00 26.11 N ANISOU 3629 N ASN A 360 3453 3009 3458 -56 -89 -87 N ATOM 3630 CA ASN A 360 50.915 15.852 35.282 1.00 23.00 C ANISOU 3630 CA ASN A 360 3082 2594 3062 7 -138 -50 C ATOM 3631 C ASN A 360 50.027 16.567 34.228 1.00 30.20 C ANISOU 3631 C ASN A 360 4063 3451 3959 132 -155 -59 C ATOM 3632 O ASN A 360 50.440 16.700 33.066 1.00 31.65 O ANISOU 3632 O ASN A 360 4342 3555 4129 180 -151 -30 O ATOM 3633 CB ASN A 360 50.336 14.465 35.578 1.00 23.14 C ANISOU 3633 CB ASN A 360 3014 2698 3080 -31 -208 -35 C ATOM 3634 CG ASN A 360 51.354 13.532 36.187 1.00 24.96 C ANISOU 3634 CG ASN A 360 3216 2954 3313 -121 -208 -7 C ATOM 3635 OD1 ASN A 360 52.555 13.689 35.975 1.00 31.04 O ANISOU 3635 OD1 ASN A 360 4021 3685 4088 -133 -168 16 O ATOM 3636 ND2 ASN A 360 50.882 12.552 36.949 1.00 46.18 N ANISOU 3636 ND2 ASN A 360 5838 5715 5993 -184 -255 -4 N ATOM 3637 N PRO A 361 48.818 17.033 34.612 1.00 27.37 N ANISOU 3637 N PRO A 361 3659 3142 3598 194 -171 -96 N ATOM 3638 CA PRO A 361 47.957 17.626 33.575 1.00 24.19 C ANISOU 3638 CA PRO A 361 3312 2700 3178 330 -203 -97 C ATOM 3639 C PRO A 361 48.531 18.874 32.883 1.00 29.86 C ANISOU 3639 C PRO A 361 4194 3277 3875 395 -150 -97 C ATOM 3640 O PRO A 361 48.321 19.042 31.676 1.00 34.05 O ANISOU 3640 O PRO A 361 4810 3744 4383 481 -182 -72 O ATOM 3641 CB PRO A 361 46.679 17.984 34.345 1.00 23.69 C ANISOU 3641 CB PRO A 361 3147 2738 3115 392 -212 -139 C ATOM 3642 CG PRO A 361 46.684 17.086 35.534 1.00 21.03 C ANISOU 3642 CG PRO A 361 2685 2514 2793 267 -210 -146 C ATOM 3643 CD PRO A 361 48.127 16.972 35.914 1.00 27.51 C ANISOU 3643 CD PRO A 361 3566 3266 3620 158 -164 -134 C ATOM 3644 N ILE A 362 49.240 19.731 33.616 1.00 23.82 N ANISOU 3644 N ILE A 362 3488 2457 3106 343 -76 -121 N ATOM 3645 CA ILE A 362 49.828 20.917 32.992 1.00 37.54 C ANISOU 3645 CA ILE A 362 5402 4050 4813 373 -25 -115 C ATOM 3646 C ILE A 362 50.999 20.519 32.086 1.00 31.29 C ANISOU 3646 C ILE A 362 4664 3206 4017 304 -6 -60 C ATOM 3647 O ILE A 362 51.277 21.184 31.078 1.00 38.32 O ANISOU 3647 O ILE A 362 5698 3988 4873 348 16 -36 O ATOM 3648 CB ILE A 362 50.285 21.959 34.045 1.00 40.78 C ANISOU 3648 CB ILE A 362 5882 4407 5208 310 43 -157 C ATOM 3649 CG1 ILE A 362 49.098 22.544 34.805 1.00 51.32 C ANISOU 3649 CG1 ILE A 362 7141 5794 6563 134 71 -147 C ATOM 3650 CG2 ILE A 362 51.078 23.075 33.379 1.00 42.50 C ANISOU 3650 CG2 ILE A 362 6056 4677 5417 403 39 -215 C ATOM 3651 CD1 ILE A 362 49.499 23.360 36.012 1.00 60.69 C ANISOU 3651 CD1 ILE A 362 8384 6948 7727 54 119 -193 C ATOM 3652 N ILE A 363 51.667 19.422 32.437 1.00 20.69 N ANISOU 3652 N ILE A 363 3213 1946 2702 206 -11 -38 N ATOM 3653 CA ILE A 363 52.681 18.836 31.571 1.00 20.41 C ANISOU 3653 CA ILE A 363 3203 1891 2660 171 9 15 C ATOM 3654 C ILE A 363 52.039 18.439 30.252 1.00 35.06 C ANISOU 3654 C ILE A 363 5121 3712 4489 283 -43 38 C ATOM 3655 O ILE A 363 52.563 18.754 29.184 1.00 28.36 O ANISOU 3655 O ILE A 363 4388 2783 3606 310 -10 71 O ATOM 3656 CB ILE A 363 53.350 17.601 32.205 1.00 23.82 C ANISOU 3656 CB ILE A 363 3508 2422 3120 86 -1 33 C ATOM 3657 CG1 ILE A 363 54.216 18.008 33.397 1.00 25.92 C ANISOU 3657 CG1 ILE A 363 3721 2724 3403 -37 46 22 C ATOM 3658 CG2 ILE A 363 54.193 16.860 31.175 1.00 19.61 C ANISOU 3658 CG2 ILE A 363 3004 1876 2571 101 15 86 C ATOM 3659 CD1 ILE A 363 54.822 16.830 34.129 1.00 25.53 C ANISOU 3659 CD1 ILE A 363 3548 2776 3376 -106 26 41 C ATOM 3660 N TYR A 364 50.897 17.756 30.330 1.00 32.67 N ANISOU 3660 N TYR A 364 4744 3474 4194 335 -127 22 N ATOM 3661 CA TYR A 364 50.148 17.396 29.124 1.00 25.34 C ANISOU 3661 CA TYR A 364 3874 2522 3233 431 -198 41 C ATOM 3662 C TYR A 364 49.740 18.635 28.339 1.00 26.48 C ANISOU 3662 C TYR A 364 4151 2569 3342 538 -192 39 C ATOM 3663 O TYR A 364 49.678 18.614 27.107 1.00 27.43 O ANISOU 3663 O TYR A 364 4381 2623 3416 604 -219 69 O ATOM 3664 CB TYR A 364 48.894 16.593 29.465 1.00 26.80 C ANISOU 3664 CB TYR A 364 3941 2813 3431 444 -296 25 C ATOM 3665 CG TYR A 364 49.142 15.340 30.263 1.00 31.64 C ANISOU 3665 CG TYR A 364 4446 3510 4066 337 -314 29 C ATOM 3666 CD1 TYR A 364 50.373 14.697 30.232 1.00 31.16 C ANISOU 3666 CD1 TYR A 364 4414 3423 4005 277 -272 56 C ATOM 3667 CD2 TYR A 364 48.138 14.799 31.051 1.00 21.72 C ANISOU 3667 CD2 TYR A 364 3061 2365 2825 301 -373 9 C ATOM 3668 CE1 TYR A 364 50.592 13.549 30.971 1.00 25.44 C ANISOU 3668 CE1 TYR A 364 3611 2762 3291 197 -296 63 C ATOM 3669 CE2 TYR A 364 48.347 13.663 31.791 1.00 19.59 C ANISOU 3669 CE2 TYR A 364 2721 2158 2566 197 -393 17 C ATOM 3670 CZ TYR A 364 49.571 13.037 31.746 1.00 22.30 C ANISOU 3670 CZ TYR A 364 3113 2454 2904 151 -359 44 C ATOM 3671 OH TYR A 364 49.769 11.897 32.486 1.00 27.38 O ANISOU 3671 OH TYR A 364 3706 3148 3549 64 -386 55 O ATOM 3672 N ASN A 365 49.446 19.711 29.058 1.00 21.98 N ANISOU 3672 N ASN A 365 3590 1979 2780 562 -158 4 N ATOM 3673 CA ASN A 365 49.043 20.947 28.409 1.00 28.19 C ANISOU 3673 CA ASN A 365 4528 2657 3525 678 -153 1 C ATOM 3674 C ASN A 365 50.176 21.544 27.582 1.00 29.18 C ANISOU 3674 C ASN A 365 4828 2649 3609 639 -81 39 C ATOM 3675 O ASN A 365 49.968 21.959 26.442 1.00 35.21 O ANISOU 3675 O ASN A 365 5734 3323 4320 728 -101 65 O ATOM 3676 CB ASN A 365 48.558 21.962 29.442 1.00 25.92 C ANISOU 3676 CB ASN A 365 4238 2364 3245 718 -123 -49 C ATOM 3677 CG ASN A 365 48.079 23.249 28.807 1.00 34.96 C ANISOU 3677 CG ASN A 365 5563 3382 4337 864 -123 -53 C ATOM 3678 OD1 ASN A 365 46.942 23.342 28.343 1.00 37.66 O ANISOU 3678 OD1 ASN A 365 5890 3757 4665 1017 -198 -56 O ATOM 3679 ND2 ASN A 365 48.948 24.253 28.780 1.00 52.01 N ANISOU 3679 ND2 ASN A 365 7900 5400 6463 813 -45 -50 N ATOM 3680 N PHE A 366 51.378 21.574 28.148 1.00 32.34 N ANISOU 3680 N PHE A 366 5214 3048 4026 499 1 45 N ATOM 3681 CA PHE A 366 52.500 22.210 27.458 1.00 38.93 C ANISOU 3681 CA PHE A 366 6194 3779 4820 436 83 85 C ATOM 3682 C PHE A 366 53.208 21.296 26.456 1.00 36.61 C ANISOU 3682 C PHE A 366 5899 3506 4507 417 99 137 C ATOM 3683 O PHE A 366 53.862 21.779 25.532 1.00 36.26 O ANISOU 3683 O PHE A 366 5991 3376 4409 405 158 177 O ATOM 3684 CB PHE A 366 53.517 22.739 28.473 1.00 33.27 C ANISOU 3684 CB PHE A 366 5456 3064 4120 281 162 75 C ATOM 3685 CG PHE A 366 53.021 23.913 29.268 1.00 36.24 C ANISOU 3685 CG PHE A 366 5918 3368 4484 296 168 26 C ATOM 3686 CD1 PHE A 366 52.700 25.105 28.639 1.00 48.74 C ANISOU 3686 CD1 PHE A 366 7717 4797 6005 374 179 27 C ATOM 3687 CD2 PHE A 366 52.881 23.828 30.643 1.00 40.43 C ANISOU 3687 CD2 PHE A 366 6336 3973 5052 240 164 -21 C ATOM 3688 CE1 PHE A 366 52.241 26.189 29.364 1.00 50.16 C ANISOU 3688 CE1 PHE A 366 8005 4893 6161 410 187 -21 C ATOM 3689 CE2 PHE A 366 52.425 24.909 31.375 1.00 40.91 C ANISOU 3689 CE2 PHE A 366 6498 3958 5087 268 177 -72 C ATOM 3690 CZ PHE A 366 52.104 26.090 30.734 1.00 51.47 C ANISOU 3690 CZ PHE A 366 8058 5137 6363 359 189 -73 C ATOM 3691 N LEU A 367 53.074 19.985 26.623 1.00 36.40 N ANISOU 3691 N LEU A 367 5734 3583 4512 418 52 137 N ATOM 3692 CA LEU A 367 53.822 19.047 25.792 1.00 26.08 C ANISOU 3692 CA LEU A 367 4435 2294 3181 411 76 180 C ATOM 3693 C LEU A 367 52.941 18.177 24.896 1.00 29.59 C ANISOU 3693 C LEU A 367 4915 2737 3592 514 -18 184 C ATOM 3694 O LEU A 367 53.437 17.276 24.220 1.00 29.25 O ANISOU 3694 O LEU A 367 4896 2700 3517 525 -8 212 O ATOM 3695 CB LEU A 367 54.698 18.157 26.672 1.00 25.75 C ANISOU 3695 CB LEU A 367 4238 2360 3185 316 108 184 C ATOM 3696 CG LEU A 367 55.883 18.872 27.322 1.00 30.25 C ANISOU 3696 CG LEU A 367 4773 2947 3773 192 205 197 C ATOM 3697 CD1 LEU A 367 56.632 17.939 28.259 1.00 34.83 C ANISOU 3697 CD1 LEU A 367 5185 3650 4399 118 214 202 C ATOM 3698 CD2 LEU A 367 56.816 19.421 26.256 1.00 27.71 C ANISOU 3698 CD2 LEU A 367 4566 2565 3396 172 298 247 C ATOM 3699 N SER A 368 51.639 18.444 24.888 1.00 33.67 N ANISOU 3699 N SER A 368 5436 3248 4108 593 -112 158 N ATOM 3700 CA SER A 368 50.729 17.735 23.992 1.00 35.00 C ANISOU 3700 CA SER A 368 5642 3419 4236 676 -219 165 C ATOM 3701 C SER A 368 49.709 18.681 23.376 1.00 33.10 C ANISOU 3701 C SER A 368 5499 3120 3958 791 -282 161 C ATOM 3702 O SER A 368 48.913 19.296 24.084 1.00 33.90 O ANISOU 3702 O SER A 368 5532 3256 4094 830 -312 130 O ATOM 3703 CB SER A 368 50.010 16.605 24.728 1.00 44.92 C ANISOU 3703 CB SER A 368 6744 4791 5534 641 -307 142 C ATOM 3704 OG SER A 368 48.980 16.057 23.924 1.00 40.52 O ANISOU 3704 OG SER A 368 6219 4243 4934 702 -427 147 O ATOM 3705 N GLY A 369 49.738 18.786 22.051 1.00 34.06 N ANISOU 3705 N GLY A 369 5785 3154 4003 857 -299 194 N ATOM 3706 CA GLY A 369 48.842 19.667 21.327 1.00 24.99 C ANISOU 3706 CA GLY A 369 4752 1939 2803 981 -367 200 C ATOM 3707 C GLY A 369 47.376 19.309 21.482 1.00 38.68 C ANISOU 3707 C GLY A 369 6369 3773 4554 1055 -513 179 C ATOM 3708 O GLY A 369 46.533 20.188 21.674 1.00 43.61 O ANISOU 3708 O GLY A 369 6984 4403 5184 1157 -554 164 O ATOM 3709 N LYS A 370 47.067 18.019 21.405 1.00 24.91 N ANISOU 3709 N LYS A 370 4538 2114 2813 1003 -591 179 N ATOM 3710 CA LYS A 370 45.682 17.570 21.488 1.00 36.57 C ANISOU 3710 CA LYS A 370 5891 3707 4298 1040 -737 166 C ATOM 3711 C LYS A 370 45.088 17.843 22.869 1.00 34.05 C ANISOU 3711 C LYS A 370 5369 3509 4061 1028 -728 129 C ATOM 3712 O LYS A 370 43.988 18.404 22.988 1.00 52.65 O ANISOU 3712 O LYS A 370 7649 5934 6422 1129 -797 118 O ATOM 3713 CB LYS A 370 45.584 16.084 21.141 1.00 38.82 C ANISOU 3713 CB LYS A 370 6155 4039 4556 952 -818 176 C ATOM 3714 CG LYS A 370 45.902 15.776 19.686 1.00 46.04 C ANISOU 3714 CG LYS A 370 7282 4843 5369 987 -851 208 C ATOM 3715 CD LYS A 370 45.418 14.390 19.288 1.00 55.63 C ANISOU 3715 CD LYS A 370 8496 6102 6538 917 -974 211 C ATOM 3716 CE LYS A 370 45.609 14.144 17.800 1.00 52.91 C ANISOU 3716 CE LYS A 370 8384 5645 6076 965 -1018 238 C ATOM 3717 NZ LYS A 370 45.023 12.842 17.367 1.00 57.18 N ANISOU 3717 NZ LYS A 370 8955 6215 6555 891 -1158 238 N ATOM 3718 N PHE A 371 45.823 17.458 23.908 1.00 24.20 N ANISOU 3718 N PHE A 371 4034 2291 2869 914 -640 110 N ATOM 3719 CA PHE A 371 45.404 17.729 25.280 1.00 28.55 C ANISOU 3719 CA PHE A 371 4415 2946 3487 892 -612 73 C ATOM 3720 C PHE A 371 45.210 19.224 25.507 1.00 30.09 C ANISOU 3720 C PHE A 371 4666 3084 3683 1009 -559 54 C ATOM 3721 O PHE A 371 44.243 19.641 26.142 1.00 32.52 O ANISOU 3721 O PHE A 371 4858 3483 4013 1084 -587 26 O ATOM 3722 CB PHE A 371 46.420 17.178 26.282 1.00 32.18 C ANISOU 3722 CB PHE A 371 4814 3421 3993 754 -522 62 C ATOM 3723 CG PHE A 371 46.182 15.745 26.666 1.00 34.93 C ANISOU 3723 CG PHE A 371 5047 3870 4355 647 -584 65 C ATOM 3724 CD1 PHE A 371 45.100 15.399 27.461 1.00 30.02 C ANISOU 3724 CD1 PHE A 371 4253 3391 3762 618 -646 45 C ATOM 3725 CD2 PHE A 371 47.049 14.746 26.247 1.00 27.87 C ANISOU 3725 CD2 PHE A 371 4227 2926 3438 576 -575 89 C ATOM 3726 CE1 PHE A 371 44.877 14.081 27.822 1.00 27.51 C ANISOU 3726 CE1 PHE A 371 3852 3153 3445 499 -705 53 C ATOM 3727 CE2 PHE A 371 46.833 13.426 26.606 1.00 24.16 C ANISOU 3727 CE2 PHE A 371 3689 2524 2968 480 -637 93 C ATOM 3728 CZ PHE A 371 45.744 13.094 27.395 1.00 30.94 C ANISOU 3728 CZ PHE A 371 4389 3513 3852 429 -705 77 C ATOM 3729 N ARG A 372 46.131 20.024 24.978 1.00 35.32 N ANISOU 3729 N ARG A 372 5514 3593 4311 1027 -480 69 N ATOM 3730 CA ARG A 372 46.052 21.473 25.117 1.00 34.34 C ANISOU 3730 CA ARG A 372 5502 3376 4170 1128 -429 54 C ATOM 3731 C ARG A 372 44.799 22.017 24.447 1.00 39.91 C ANISOU 3731 C ARG A 372 6237 4091 4836 1314 -531 60 C ATOM 3732 O ARG A 372 44.143 22.911 24.981 1.00 46.70 O ANISOU 3732 O ARG A 372 7083 4961 5700 1433 -525 31 O ATOM 3733 CB ARG A 372 47.295 22.144 24.529 1.00 25.65 C ANISOU 3733 CB ARG A 372 4612 2108 3027 1082 -333 82 C ATOM 3734 CG ARG A 372 47.266 23.660 24.607 1.00 26.72 C ANISOU 3734 CG ARG A 372 4913 2112 3127 1169 -284 70 C ATOM 3735 CD ARG A 372 48.616 24.273 24.272 1.00 43.66 C ANISOU 3735 CD ARG A 372 7244 4111 5235 1063 -173 98 C ATOM 3736 NE ARG A 372 49.068 23.936 22.925 1.00 51.58 N ANISOU 3736 NE ARG A 372 8367 5052 6178 1058 -179 152 N ATOM 3737 CZ ARG A 372 49.994 23.022 22.654 1.00 53.86 C ANISOU 3737 CZ ARG A 372 8610 5381 6475 940 -134 179 C ATOM 3738 NH1 ARG A 372 50.572 22.348 23.639 1.00 54.49 N ANISOU 3738 NH1 ARG A 372 8521 5560 6622 817 -90 159 N ATOM 3739 NH2 ARG A 372 50.342 22.781 21.397 1.00 47.00 N ANISOU 3739 NH2 ARG A 372 7870 4450 5537 957 -131 224 N ATOM 3740 N GLU A 373 44.466 21.471 23.281 1.00 38.80 N ANISOU 3740 N GLU A 373 6142 3951 4649 1349 -627 97 N ATOM 3741 CA GLU A 373 43.287 21.920 22.548 1.00 38.25 C ANISOU 3741 CA GLU A 373 6095 3905 4535 1526 -744 111 C ATOM 3742 C GLU A 373 42.000 21.558 23.287 1.00 36.41 C ANISOU 3742 C GLU A 373 5607 3879 4349 1575 -828 86 C ATOM 3743 O GLU A 373 41.053 22.348 23.325 1.00 41.28 O ANISOU 3743 O GLU A 373 6192 4539 4953 1750 -873 78 O ATOM 3744 CB GLU A 373 43.268 21.329 21.137 1.00 42.48 C ANISOU 3744 CB GLU A 373 6742 4398 4999 1528 -837 157 C ATOM 3745 CG GLU A 373 42.051 21.733 20.317 1.00 57.35 C ANISOU 3745 CG GLU A 373 8646 6318 6829 1706 -980 178 C ATOM 3746 CD GLU A 373 41.884 23.238 20.223 1.00 82.24 C ANISOU 3746 CD GLU A 373 11949 9354 9946 1887 -947 179 C ATOM 3747 OE1 GLU A 373 42.869 23.927 19.883 1.00 89.17 O ANISOU 3747 OE1 GLU A 373 13055 10044 10782 1867 -846 193 O ATOM 3748 OE2 GLU A 373 40.767 23.732 20.493 1.00 87.04 O ANISOU 3748 OE2 GLU A 373 12451 10058 10561 2050 -1019 167 O ATOM 3749 N GLU A 374 41.960 20.369 23.878 1.00 38.14 N ANISOU 3749 N GLU A 374 5647 4230 4616 1424 -845 76 N ATOM 3750 CA GLU A 374 40.765 19.967 24.613 1.00 41.66 C ANISOU 3750 CA GLU A 374 5840 4890 5101 1438 -913 58 C ATOM 3751 C GLU A 374 40.617 20.758 25.915 1.00 43.24 C ANISOU 3751 C GLU A 374 5950 5134 5346 1495 -812 11 C ATOM 3752 O GLU A 374 39.502 21.129 26.298 1.00 54.79 O ANISOU 3752 O GLU A 374 7264 6736 6816 1622 -850 -3 O ATOM 3753 CB GLU A 374 40.783 18.463 24.890 1.00 44.67 C ANISOU 3753 CB GLU A 374 6085 5381 5506 1243 -959 65 C ATOM 3754 CG GLU A 374 40.735 17.611 23.627 1.00 61.92 C ANISOU 3754 CG GLU A 374 8361 7535 7632 1194 -1076 105 C ATOM 3755 CD GLU A 374 39.636 18.040 22.664 1.00 78.95 C ANISOU 3755 CD GLU A 374 10518 9743 9737 1344 -1214 131 C ATOM 3756 OE1 GLU A 374 38.520 18.362 23.128 1.00 86.11 O ANISOU 3756 OE1 GLU A 374 11233 10817 10668 1432 -1266 122 O ATOM 3757 OE2 GLU A 374 39.891 18.057 21.439 1.00 78.19 O ANISOU 3757 OE2 GLU A 374 10611 9528 9571 1381 -1269 161 O ATOM 3758 N PHE A 375 41.737 21.026 26.583 1.00 34.12 N ANISOU 3758 N PHE A 375 4885 3866 4212 1404 -684 -11 N ATOM 3759 CA PHE A 375 41.736 21.893 27.760 1.00 28.27 C ANISOU 3759 CA PHE A 375 4120 3125 3494 1453 -583 -59 C ATOM 3760 C PHE A 375 41.233 23.277 27.372 1.00 33.19 C ANISOU 3760 C PHE A 375 4879 3658 4071 1682 -584 -67 C ATOM 3761 O PHE A 375 40.516 23.930 28.129 1.00 33.52 O ANISOU 3761 O PHE A 375 4849 3769 4117 1812 -555 -104 O ATOM 3762 CB PHE A 375 43.136 22.003 28.375 1.00 32.03 C ANISOU 3762 CB PHE A 375 4704 3478 3988 1303 -463 -75 C ATOM 3763 CG PHE A 375 43.669 20.710 28.926 1.00 47.13 C ANISOU 3763 CG PHE A 375 6489 5475 5943 1103 -455 -70 C ATOM 3764 CD1 PHE A 375 42.815 19.672 29.262 1.00 42.25 C ANISOU 3764 CD1 PHE A 375 5665 5039 5350 1053 -528 -68 C ATOM 3765 CD2 PHE A 375 45.032 20.535 29.109 1.00 51.30 C ANISOU 3765 CD2 PHE A 375 7106 5906 6481 963 -377 -63 C ATOM 3766 CE1 PHE A 375 43.310 18.484 29.767 1.00 39.83 C ANISOU 3766 CE1 PHE A 375 5276 4788 5070 875 -525 -60 C ATOM 3767 CE2 PHE A 375 45.532 19.350 29.614 1.00 42.18 C ANISOU 3767 CE2 PHE A 375 5846 4823 5357 805 -375 -55 C ATOM 3768 CZ PHE A 375 44.671 18.324 29.944 1.00 42.64 C ANISOU 3768 CZ PHE A 375 5732 5036 5435 764 -449 -54 C ATOM 3769 N LYS A 376 41.622 23.710 26.178 1.00 35.01 N ANISOU 3769 N LYS A 376 5322 3731 4249 1737 -612 -30 N ATOM 3770 CA LYS A 376 41.204 24.992 25.633 1.00 40.60 C ANISOU 3770 CA LYS A 376 6206 4322 4897 1957 -626 -26 C ATOM 3771 C LYS A 376 39.692 25.025 25.439 1.00 46.44 C ANISOU 3771 C LYS A 376 6780 5236 5630 2157 -741 -21 C ATOM 3772 O LYS A 376 39.028 25.985 25.830 1.00 51.45 O ANISOU 3772 O LYS A 376 7427 5877 6246 2359 -724 -48 O ATOM 3773 CB LYS A 376 41.924 25.255 24.308 1.00 49.42 C ANISOU 3773 CB LYS A 376 7578 5249 5949 1947 -642 23 C ATOM 3774 CG LYS A 376 41.822 26.676 23.795 1.00 59.63 C ANISOU 3774 CG LYS A 376 9129 6361 7168 2137 -631 31 C ATOM 3775 CD LYS A 376 43.088 27.058 23.052 1.00 64.29 C ANISOU 3775 CD LYS A 376 9978 6746 7704 2006 -557 64 C ATOM 3776 CE LYS A 376 44.307 26.913 23.956 1.00 69.70 C ANISOU 3776 CE LYS A 376 10675 7375 8434 1805 -429 40 C ATOM 3777 NZ LYS A 376 45.581 27.281 23.271 1.00 72.11 N ANISOU 3777 NZ LYS A 376 11201 7511 8687 1666 -348 78 N ATOM 3778 N ALA A 377 39.153 23.967 24.840 1.00 51.60 N ANISOU 3778 N ALA A 377 7280 6034 6292 2100 -860 13 N ATOM 3779 CA ALA A 377 37.714 23.862 24.620 1.00 52.03 C ANISOU 3779 CA ALA A 377 7136 6293 6341 2255 -986 27 C ATOM 3780 C ALA A 377 36.951 23.828 25.942 1.00 54.38 C ANISOU 3780 C ALA A 377 7173 6797 6691 2290 -939 -17 C ATOM 3781 O ALA A 377 35.835 24.340 26.039 1.00 63.74 O ANISOU 3781 O ALA A 377 8231 8121 7865 2500 -985 -20 O ATOM 3782 CB ALA A 377 37.395 22.625 23.792 1.00 42.86 C ANISOU 3782 CB ALA A 377 5869 5242 5173 2129 -1125 71 C ATOM 3783 N ALA A 378 37.563 23.228 26.959 1.00 43.61 N ANISOU 3783 N ALA A 378 5731 5459 5378 2091 -844 -47 N ATOM 3784 CA ALA A 378 36.927 23.103 28.267 1.00 44.19 C ANISOU 3784 CA ALA A 378 5570 5727 5493 2092 -785 -88 C ATOM 3785 C ALA A 378 36.699 24.456 28.941 1.00 49.04 C ANISOU 3785 C ALA A 378 6264 6283 6084 2314 -687 -136 C ATOM 3786 O ALA A 378 35.597 24.748 29.404 1.00 61.56 O ANISOU 3786 O ALA A 378 7668 8054 7670 2484 -693 -152 O ATOM 3787 CB ALA A 378 37.761 22.206 29.169 1.00 46.27 C ANISOU 3787 CB ALA A 378 5781 5997 5802 1830 -707 -107 C ATOM 3788 N PHE A 379 37.744 25.277 28.991 1.00 52.41 N ANISOU 3788 N PHE A 379 6971 6457 6486 2311 -595 -157 N ATOM 3789 CA PHE A 379 37.697 26.544 29.719 1.00 57.73 C ANISOU 3789 CA PHE A 379 7778 7031 7125 2486 -492 -210 C ATOM 3790 C PHE A 379 37.069 27.691 28.931 1.00 65.26 C ANISOU 3790 C PHE A 379 8891 7893 8013 2788 -541 -197 C ATOM 3791 O PHE A 379 37.145 28.845 29.351 1.00 71.26 O ANISOU 3791 O PHE A 379 9843 8508 8725 2946 -462 -238 O ATOM 3792 CB PHE A 379 39.106 26.954 30.157 1.00 49.19 C ANISOU 3792 CB PHE A 379 6941 5715 6035 2325 -380 -236 C ATOM 3793 CG PHE A 379 39.544 26.336 31.452 1.00 56.01 C ANISOU 3793 CG PHE A 379 7670 6665 6944 2125 -294 -275 C ATOM 3794 CD1 PHE A 379 39.012 26.771 32.655 1.00 63.61 C ANISOU 3794 CD1 PHE A 379 8556 7715 7898 2218 -214 -334 C ATOM 3795 CD2 PHE A 379 40.496 25.330 31.470 1.00 45.98 C ANISOU 3795 CD2 PHE A 379 6365 5388 5715 1859 -293 -252 C ATOM 3796 CE1 PHE A 379 39.413 26.209 33.852 1.00 60.64 C ANISOU 3796 CE1 PHE A 379 8072 7415 7552 2032 -140 -368 C ATOM 3797 CE2 PHE A 379 40.903 24.764 32.664 1.00 48.37 C ANISOU 3797 CE2 PHE A 379 6558 5768 6053 1686 -224 -283 C ATOM 3798 CZ PHE A 379 40.361 25.204 33.856 1.00 54.33 C ANISOU 3798 CZ PHE A 379 7240 6607 6797 1764 -150 -340 C ATOM 3799 N SER A 380 36.452 27.382 27.796 1.00 69.79 N ANISOU 3799 N SER A 380 9403 8540 8574 2870 -678 -141 N ATOM 3800 CA SER A 380 35.823 28.415 26.980 1.00 77.75 C ANISOU 3800 CA SER A 380 10547 9481 9512 3091 -727 -121 C ATOM 3801 C SER A 380 34.389 28.693 27.425 1.00 89.66 C ANISOU 3801 C SER A 380 11813 11235 11020 3291 -744 -135 C ATOM 3802 O SER A 380 33.459 27.980 27.046 1.00 89.41 O ANISOU 3802 O SER A 380 11518 11441 11012 3315 -857 -99 O ATOM 3803 CB SER A 380 35.850 28.020 25.503 1.00 76.72 C ANISOU 3803 CB SER A 380 10482 9314 9354 3043 -856 -53 C ATOM 3804 OG SER A 380 37.175 28.037 25.002 1.00 76.29 O ANISOU 3804 OG SER A 380 10694 9015 9280 2877 -814 -38 O ATOM 3805 N CYS A 381 34.221 29.736 28.232 1.00 94.89 N ANISOU 3805 N CYS A 381 12568 11839 11646 3419 -632 -186 N ATOM 3806 CA CYS A 381 32.907 30.128 28.728 1.00 91.36 C ANISOU 3806 CA CYS A 381 11916 11609 11187 3623 -623 -202 C ATOM 3807 C CYS A 381 32.396 31.365 27.998 1.00 95.11 C ANISOU 3807 C CYS A 381 12585 11977 11577 3824 -649 -187 C ATOM 3808 O CYS A 381 33.041 32.413 28.012 1.00 99.38 O ANISOU 3808 O CYS A 381 13448 12263 12050 3848 -579 -209 O ATOM 3809 CB CYS A 381 32.955 30.390 30.235 1.00 91.03 C ANISOU 3809 CB CYS A 381 11830 11603 11153 3646 -476 -273 C ATOM 3810 SG CYS A 381 33.460 28.967 31.231 1.00 91.72 S ANISOU 3810 SG CYS A 381 11670 11847 11331 3428 -436 -299 S TER 3811 CYS A 381 HETATM 3812 C1 SUV A2001 51.065 6.873 55.061 1.00 28.86 C HETATM 3813 N1 SUV A2001 51.928 5.873 54.855 1.00 29.78 N HETATM 3814 O1 SUV A2001 50.274 7.311 54.118 1.00 31.92 O HETATM 3815 CL1 SUV A2001 47.586 11.394 57.073 1.00 41.55 CL HETATM 3816 N2 SUV A2001 50.868 7.553 56.183 1.00 34.08 N HETATM 3817 O2 SUV A2001 55.542 8.030 54.017 1.00 34.54 O HETATM 3818 C3 SUV A2001 49.914 8.446 55.906 1.00 34.98 C HETATM 3819 N3 SUV A2001 54.068 6.441 53.433 1.00 36.48 N HETATM 3820 C4 SUV A2001 49.332 9.378 56.660 1.00 21.58 C HETATM 3821 N4 SUV A2001 54.727 8.096 50.464 1.00 40.50 N HETATM 3822 C5 SUV A2001 48.345 10.192 56.121 1.00 22.65 C HETATM 3823 N5 SUV A2001 54.437 7.845 49.303 1.00 45.50 N HETATM 3824 C6 SUV A2001 47.973 10.028 54.796 1.00 30.72 C HETATM 3825 N6 SUV A2001 55.807 7.587 50.753 1.00 38.01 N HETATM 3826 C7 SUV A2001 48.611 9.044 54.061 1.00 28.58 C HETATM 3827 C8 SUV A2001 49.552 8.289 54.626 1.00 32.15 C HETATM 3828 C11 SUV A2001 51.895 5.284 53.512 1.00 27.27 C HETATM 3829 C12 SUV A2001 52.842 6.111 52.661 1.00 31.25 C HETATM 3830 C14 SUV A2001 54.848 5.528 54.313 1.00 29.80 C HETATM 3831 C15 SUV A2001 53.978 4.624 55.193 1.00 21.84 C HETATM 3832 C16 SUV A2001 52.881 5.438 55.890 1.00 20.33 C HETATM 3833 C17 SUV A2001 54.550 7.695 53.369 1.00 37.43 C HETATM 3834 C19 SUV A2001 53.863 8.668 52.642 1.00 35.50 C HETATM 3835 C20 SUV A2001 53.959 8.848 51.254 1.00 36.96 C HETATM 3836 C21 SUV A2001 53.213 9.857 50.648 1.00 23.40 C HETATM 3837 C22 SUV A2001 52.386 10.692 51.393 1.00 13.97 C HETATM 3838 C23 SUV A2001 52.297 10.514 52.766 1.00 21.68 C HETATM 3839 C24 SUV A2001 53.034 9.511 53.379 1.00 28.54 C HETATM 3840 C27 SUV A2001 55.382 7.090 48.757 1.00 32.50 C HETATM 3841 C28 SUV A2001 56.281 6.922 49.707 1.00 34.66 C HETATM 3842 C29 SUV A2001 51.476 11.336 53.529 1.00 31.10 C HETATM 3843 C30 SUV A2001 55.815 4.670 53.495 1.00 23.16 C HETATM 3844 C1 OLA A2002 57.305 21.848 32.533 1.00 62.33 C HETATM 3845 O1 OLA A2002 56.801 21.949 31.381 1.00 62.63 O1- HETATM 3846 O2 OLA A2002 58.437 21.335 32.739 1.00 64.65 O HETATM 3847 C2 OLA A2002 56.491 22.381 33.767 1.00 49.19 C HETATM 3848 C3 OLA A2002 56.313 21.385 34.916 1.00 44.33 C HETATM 3849 C4 OLA A2002 55.286 21.753 36.007 1.00 34.96 C HETATM 3850 C5 OLA A2002 55.837 22.587 37.158 1.00 34.83 C HETATM 3851 C6 OLA A2002 54.819 22.881 38.240 1.00 27.64 C HETATM 3852 O HOH A4001 52.671 18.070 54.208 1.00 28.11 O HETATM 3853 O HOH A4002 47.791 12.018 34.054 1.00 37.41 O HETATM 3854 O HOH A4003 58.583 13.753 48.186 1.00 22.37 O HETATM 3855 O HOH A4004 52.581 14.807 23.372 1.00 25.65 O HETATM 3856 O HOH A4005 62.961 8.826 -14.095 1.00 31.74 O HETATM 3857 O HOH A4006 56.355 16.352 23.578 1.00 37.48 O HETATM 3858 O HOH A4007 39.051 -1.168 58.273 1.00 37.56 O HETATM 3859 O HOH A4008 38.759 -1.440 60.992 1.00 36.60 O HETATM 3860 O HOH A4009 75.414 -5.861 -0.115 1.00 47.06 O HETATM 3861 O HOH A4010 41.337 9.690 66.264 1.00 30.89 O HETATM 3862 O HOH A4011 53.073 2.333 -15.117 1.00 34.19 O HETATM 3863 O HOH A4012 69.086 0.246 -2.923 1.00 44.45 O HETATM 3864 O HOH A4013 55.701 8.795 -15.802 1.00 35.96 O HETATM 3865 O HOH A4014 58.200 11.931 60.967 1.00 28.73 O HETATM 3866 O HOH A4015 61.285 4.144 -18.820 1.00 31.46 O HETATM 3867 O HOH A4016 61.750 15.497 15.456 1.00 40.87 O HETATM 3868 O HOH A4017 32.736 25.831 27.616 1.00 53.73 O HETATM 3869 O HOH A4018 60.631 1.434 -20.166 1.00 38.41 O HETATM 3870 O HOH A4019 49.235 15.523 21.123 1.00 35.86 O HETATM 3871 O HOH A4020 69.741 -3.163 0.475 1.00 35.43 O HETATM 3872 O HOH A4021 57.036 5.873 57.481 1.00 39.03 O HETATM 3873 O HOH A4022 50.958 3.048 66.204 1.00 44.68 O HETATM 3874 O HOH A4023 40.491 0.993 29.520 1.00 47.15 O HETATM 3875 O HOH A4024 73.577 13.436 -11.583 1.00 46.38 O HETATM 3876 O HOH A4025 55.853 9.838 56.024 1.00 27.64 O HETATM 3877 O HOH A4026 68.859 -9.715 -23.335 1.00 56.04 O HETATM 3878 O HOH A4027 49.032 10.530 24.606 1.00 44.07 O HETATM 3879 O HOH A4028 55.937 6.016 31.359 1.00 25.57 O CONECT 619 1189 CONECT 1189 619 CONECT 3812 3813 3814 3816 CONECT 3813 3812 3828 3832 CONECT 3814 3812 3827 CONECT 3815 3822 CONECT 3816 3812 3818 CONECT 3817 3833 CONECT 3818 3816 3820 3827 CONECT 3819 3829 3830 3833 CONECT 3820 3818 3822 CONECT 3821 3823 3825 3835 CONECT 3822 3815 3820 3824 CONECT 3823 3821 3840 CONECT 3824 3822 3826 CONECT 3825 3821 3841 CONECT 3826 3824 3827 CONECT 3827 3814 3818 3826 CONECT 3828 3813 3829 CONECT 3829 3819 3828 CONECT 3830 3819 3831 3843 CONECT 3831 3830 3832 CONECT 3832 3813 3831 CONECT 3833 3817 3819 3834 CONECT 3834 3833 3835 3839 CONECT 3835 3821 3834 3836 CONECT 3836 3835 3837 CONECT 3837 3836 3838 CONECT 3838 3837 3839 3842 CONECT 3839 3834 3838 CONECT 3840 3823 3841 CONECT 3841 3825 3840 CONECT 3842 3838 CONECT 3843 3830 CONECT 3844 3845 3846 3847 CONECT 3845 3844 CONECT 3846 3844 CONECT 3847 3844 3848 CONECT 3848 3847 3849 CONECT 3849 3848 3850 CONECT 3850 3849 3851 CONECT 3851 3850 MASTER 638 0 2 21 8 0 3 6 3878 1 42 43 END